sequence
stringlengths 13
8.92k
| annotation
listlengths 2
214
| description
stringlengths 61
12.1k
| labels
int64 0
0
|
|---|---|---|---|
MELITNELLYKTYKQKPVGVEEPVYDQAGDPLFGERGAVHPQSTLKLPHKRGERDVPTNLASLPKRGDCRSGNSRGPVSGIYLKPGPLFYQDYKGPVYHRAPLELFEEGSMCETTKRIGRVTGSDGKLYHIYVCIDGCIIIKSATRSYQRVFRWVHNRLDCPLWVTTCSDTKEEGATKKKTQKPDRLERGKMKIVPKESEKDSKTKPPDATIVVEGVKYQVRKKGKTKSKNTQDGLYHNKNKPQESRKKLEKALLAWAIIAIVLFQVTMGENITQWNLQDNGTEGIQRAMFQRGVNRSLHGIWPEKICTGVPSHLATDIELKTIHGMMDASEKTNYTCCRLQRHEWNKHGWCNWYNIEPWILVMNRTQANLTEGQPPRECAVTCRYDRASDLNVVTQARDSPTPLTGCKKGKNFSFAGILMRGPCNFEIAASDVLFKEHERISMFQDTTLYLVDGLTNSLEGARQGTAKLTTWLGKQLGILGKKLENKSKTWFGAYAASPYCDVDRKIGYIWYTKNCTPACLPKNTKIVGPGKFGTNAEDGKILHEMGGHLSEVLLLSLVVLSDFAPETASVMYLILHFSIPQSHVDVMDCDKTQLNLTVELTTAEVIPGSVWNLGKYVCIRPNWWPYETTVVLAFEEVSQVVKLVLRALRDLTRIWNAATTTAFLVCLVKIVRGQMVQGILWLLLITGVQGHLDCKPEFSYAIAKDERIGQLGAEGLTTTWKEYSPGMKLEDTMVIAWCEDGKLMYLQRCTRETRYLAILHTRALPTSVVFKKLFDGRKQEDVVEMNDNFEFGLCPCDAKPIVRGKFNTTLLNGPAFQMVCPIGWTGTVSCTSFNMDTLATTVVRTYRRSKPFPHRQGCITQKNLGEDLHNCILGGNWTCVPGDQLLYKGGSIESCKWCGYQFKESEGLPHYPIGKCKLENETGYRLVDSTSCNREGVAIVPQGTLKCKIGKTTVQVIAMDTKLGPMPCRPYEIISSEGPVEKTACTFNYTKTLKNKYFEPRDSYFQQYMLKGEYQYWFDLEVTDHHRDYFAESILVVVVALLGGRYVLWLLVTYMVLSEQKALGIQYGSGEVVMMGNLLTHNNIEVVTYFLLLYLLLREESVKKWVLLLYHILVVHPIKSVIVILLMIGDVVKADSGGQEYLGKIDLCFTTVVLIVIGLIIARRDPTIVPLVTIMAALRVTELTHQPGVDIAVAVMTITLLMVSYVTDYFRYKKWLQCILSLVSAVFLIRSLIYLGRIEMPEVTIPNWRPLTLILLYLISTTIVTRWKVDVAGLLLQCVPILLLVTTLWADFLTLILILPTYELVKLYYLKTVRTDTERSWLGGIDYTRVDSIYDVDESGEGVYLFPSRQKAQGNFSILLPLIKATLISCVSSKWQLIYMSYLTLDFMYYMHRKVIEEISGGTNIISRLVAALIELNWSMEEEESKGLKKFYLLSGRLRNLIIKHKVRNETVASWYGEEEVYGMPKIMTIIKASTLSKSRHCIICTVCEGREWKGGTCPKCGRHGKPITCGMSLADFEERHYKRIFIREGNFEGMCSRCQGKHRRFEMDREPKSARYCAECNRLHPAEEGDFWAESSMLGLKITYFALMDGKVYDITEWAGCQRVGISPDTHRVPCHISFGSRMPFRQEYNGFVQYTARGQLFLRNLPVLATKVKMLMVGNLGEEIGNLEHLGWILRGPAVCKKITEHEKCHINILDKLTAFFGIMPRGTTPRAPVRFPTSLLKVRRGLETAWAYTHQGGISSVDHVTAGKDLLVCDSMGRTRVVCQSNNRLTDETEYGVKTDSGCPDGARCYVLNPEAVNISGSKGAVVHLQKTGGEFTCVTASGTPAFFDLKNLKGWSGLPIFEASSGRVVGRVKVGKNEESKPTKIMSGIQTVSKNRADLTEMVKKITSMNRGDFKQITLATGAGKTTELPKAVIEEIGRHKRVLVLIPLRAAAESVYQYMRLKHPSISFNLRIGDMKEGDMATGITYASYGYFCQMPQPKLRAAMVEYSYIFLDEYHCATPEQLAIIGKIHRFSESIRVVAMTATPAGSVTTTGQKHPIEEFIAPEVMKGEDLGSQFLDIAGLKIPVDEMKGNMLVFVPTRNMAVEVAKKLKAKGYNSGYYYSGEDPANLRVVTSQSPYVIVATNAIESGVTLPDLDTVIDTGLKCEKRVRVSSKIPFIVTGLKRMAVTVGEQAQRRGRVGRVKPGRYYRSQETATGSKDYHYDLLQAQRYGIEDGINVTKSFREMNYDWSLYEEDSLLITQLEILNNLLISEDLPAAVKNIMARTDHPEPIQLAYNSYEVQVPVLFPKIRNGEVTDTYENYSFLNARKLGEDVPVYIYATEDEDLAVDLLGLDWPDPGNQQVVETGKALKQVTGLSSAENALLVALFGYVGYQALSKRHVPMITDIYTIEDQRLEDTTHLQYAPNAIKTDGTETELKELASGDVEKIMGAISDYAAGGLEFVKSQAEKIKTAPLFKENAEAAKGYVQKFIDSLIENKEEIIRYGLWGTHTALYKSIAARLGHETAFATLVLKWLAFGGESVSDHVKQAAVDLVVYYVMNKPSFPGDSETQQEGRRFVASLFISALATYTYKTWNYHNLSKVVEPALAYLPYATSALKMFTPTRLESVVILSTTIYKTYLSIRKGKSDGLLGTGISAAMEILSQNPVSVGISVMLGVGAIAAHNAIESSEQKRTLLMKVFVKNFLDQAATDELVKENPEKIIMALFEAVQTIGNPLRLIYHLYGVYYKGWEAKELSERTAGRNLFTLIMFEAFELLGMDSQGKIRNLSGNYILDLIYGLHKQINRGLKKMVLGWAPAPFSCDWTPSDERIRLPTDNYLRVETRCPCGYEMKAFKNVGGKLTKVEESGPFLCRNRPGRGPVNYRVTKYYDDNLREIKPVAKLEGQVEHYYKGVTAKIDYSKGKMLLATDKWEVEHGVITRLAKRYTGVGFNGAYLGDEPNHRALVERDCATITKNTVQFLKMKKGCAFTYDLTISNLTRLIELVHRNNLEEKEIPTATVTTWLAYTFVNEDVGTIKPVLGERVIPDPVVDINLQPEVQVDTSEVGITIIGRETLMTTGVTPVLEKVEPDASDNQNSVKIGLDEGNYPGPGIQTHTLTEEIHNRDARPFIMILGSRNSISNRAKTARNINLYTGNDPREIRDLMAAGRMLVVALRDVDPELSEMVDFKGTFLDREALEALSLGQPKPKQVTKEAVRNLIEQKKDVEIPNWFASDDPVFLEVALKNDKYYLVGDVGELKDQAKALGATDQTRIIKEVGSRTYAMKLSSWFLKASNKQMSLTPLFEELLLRCPPATKSNKGHMASAYQLAQGNWEPLGCGVHLGTIPARRVKIHPYEAYLKLKDFIEEEEKKPRVKDTVIREHNKWILKKIRFQGNLNTKKMLNPGKLSEQLDREGRKRNIYNHQIGTIMSSAGIRLEKLPIVRAQTDTKTFHEAIRDKIDKSENRQNPELHNKLLEIFHTIAQPTLKHTYGEVTWEQLEAGVNRKGAAGFLEKKNIGEVLDSEKHLVEQLVRDLKAGRKIKYYETAIPKNEKRDVSDDWQAGDLVVEKRPRVIQYPEAKTRLAITKVMYNWVKQQPVVIPGYEGKTPLFNIFDKVRKEWDSFNEPVAVSFDTKAWDTQVTSKDLQLIGEIQKYYYKKEWHKFIDTITDHMTEVPVITADGEVYIRNGQRGSGQPDTSAGNSMLNVLTMMYGFCESTGVPYKSFNRVARIHVCGDDGFLITEKGLGLKFANKGMQILHEAGKPQKITEGEKMKVAYRFEDIEFCSHTPVPVRWSDNTSSHMAGRDTAVILSKMATRLDSSGERGTTAYEKAVAFSFLLMYSWNPLVRRICLLVLSQQPETDPSKHATYYYKGDPIGAYKDVIGRNLSELKRTGFEKLANLNLSLSTLGVWTKHTSKRIIQDCVAIGKEEGNWLVKPDRLISSKTGHLYIPDKGFTLQGKHYEQLQLRTETNPVMGVGTERYKLGPIVNLLLRRLKILLMTAVGVSS
|
[
3730,
4587,
4666,
5058,
5174,
5943,
8200,
10917,
10922,
10930,
12938,
13919,
13935,
13963,
13984,
14664,
19487,
25325,
25809,
26294,
26300,
26481,
27616,
27904,
27925,
27926,
28055,
28223,
28227,
29033,
29034,
29906,
30398,
31393,
31535,
32073,
33696,
34236,
35921,
36173,
37314,
37738,
41973,
43377,
45651,
47717,
53820,
54100,
58239,
59810,
61269,
61542,
61645,
64186,
69276,
69277,
69278,
69442,
69818,
69990,
75231,
77967,
87103,
87110,
87121,
87316,
87411,
87413,
87481,
87482,
87491,
87522,
87539,
87577,
87580,
87586,
87595,
87601,
87625,
87637,
87653,
87674,
87676,
87741,
87760,
87850,
87855,
87856,
87965,
88003,
88008,
88049,
88134,
88153,
88159,
88161,
88162,
88192,
88194,
88211,
88212,
88220,
88237,
88241,
88242
] |
The following text describes a protein:
Function:
[N-terminal protease]: Leader cysteine autoprotease that cleaves itself from the nascent polyprotein during translation of the viral mRNA. Once released, plays a role in the inhibition of host innate immune response by interacting with host IRF3 and inducing its proteasomal degradation; [Capsid protein C]: Packages viral RNA to form a viral nucleocapsid and thereby protects viral RNA. Also plays a role in transcription regulation. Protects the incoming virus against IFN-induced effectors; [E(rns) glycoprotein]: Initial binding to target cell probably involves interaction of E(rns) with glycosaminoglycans. Also possesses intrinsic ribonuclease (RNase) activity that can inhibit the production of type I interferon and assist in the development of persistent infections (By similarity); [Envelope glycoprotein E1]: E1 and/or E2 are probably responsible of cell attachment with CD46 and subsequent fusion after internalization of the virion by endocytosis; [Envelope glycoprotein E2]: E1 and/or E2 are probably responsible of cell attachment with CD46 and subsequent fusion after internalization of the virion by endocytosis (Probable). Probably functions as a coeffector of fusion providing structural integrity to the fusion complex and possibly controlling exposure of the fusion motif in E1; [Viroporin p7]: Plays an essential role in the virus replication cycle by acting as a viroporin (By similarity). Forms ion conductive pores, which alters the cell permeability allowing the transport of ions and other small molecules (By similarity). Forms a leader sequence to properly orient NS2 in the membrane; [Non-structural protein 2-3]: Uncleaved NS2-3 is required for production of infectious virus; [Cysteine protease NS2]: Plays a role in the regulation of viral RNA replication; [Serine protease NS3]: Multifunctional protein that contains an N-terminal protease and a C-terminal helicase, playing essential roles in viral polyprotein processing and viral genome replication. The chymotrypsin-like serine protease activity utilizes NS4A as an essential cofactor and catalyzes the cleavage of the polyprotein leading to the release of NS4A, NS4B, NS5A, and NS5B. Interacts with NS5B to enhance RNA-dependent RNA polymerase activity; [Non-structural protein 4A]: Acts as a cofactor for the NS3 protease activity; [Non-structural protein 4B]: Induces a specific membrane alteration that serves as a scaffold for the virus replication complex (By similarity). Plays a role in the inhibition of host innate immune response by inhibiting RIGI/IFIH1-mediated IFN-beta production; [RNA-directed RNA polymerase]: Replicates the viral (+) and (-) genome. Initiates the primer-independent RNA replication via a de novo mechanism requiring GTP.
Miscellaneous:
MISCELLANEOUS: BVDV is divided in two types: cytopathic and non-cytopathic. Both types of viruses can be found in animals suffering from mucosal disease, as a cytopathic BVDV can develop from a non-cytopathic virus within the infected animal by deletions, mutations or insertions. Both types express uncleaved NS2-3, but cytopathic strains also express NS3. The cytopathic NADL strain contains an insertion (Jiv 90) that potentiate the partial cleavage of NS2-3. Removal of this insertion in the NADL Jiv 90(-) strain results in a non-cytopathic strain in which NS2-3 remains uncleaved.
Subcellular Localization:
[Capsid protein C]: Virion; [E(rns) glycoprotein]: Host membrane; Peripheral membrane protein. Virion membrane; Peripheral membrane protein. Note=The C-terminus membrane anchor of Erns represents an amphipathic helix embedded in plane into the membrane; [Envelope glycoprotein E1]: Host endoplasmic reticulum membrane; Single-pass type I membrane protein. Virion membrane; Single-pass type I membrane protein. Note=The C-terminal transmembrane domain acts as a signal sequence and forms a hairpin structure before cleavage by host signal peptidase. This explains that E1 and E2 are mostly lumenal. After cleavage, the C-terminus transmembrane sequence acts as ER membrane anchor; [Envelope glycoprotein E2]: Host endoplasmic reticulum membrane; Single-pass type I membrane protein. Virion membrane; Single-pass type I membrane protein. Note=The C-terminal transmembrane domain acts as a signal sequence and forms a hairpin structure before cleavage by host signal peptidase. This explains that E1 and E2 are mostly lumenal. After cleavage, the C-terminus transmembrane sequence acts as ER membrane anchor; [Cysteine protease NS2]: Host membrane; Multi-pass membrane protein; [Serine protease NS3]: Host cytoplasm; [Non-structural protein 4B]: Host cytoplasm; [Non-structural protein 5A]: Host membrane; Peripheral membrane protein. Note=The N-terminus membrane anchor represents an amphipathic helix embedded in plane into the membrane.
Domain:
[Envelope glycoprotein E1]: The transmembrane domain is responsible for ER localization; [Envelope glycoprotein E2]: The transmembrane domain is responsible for ER localization.
| 0
|
MTCLGLSRPSKRVADEAGNFSPLGQACGCRALRFLKGKVSVLLATALPANVAFLCCRGSQAKPRRRSRSGWRSEQPWMPFVPKWTLPTGLNVSIECKRVSGLEPATVDWAFDLTKTNMQTMYEQSEWGWKDREKREEMTDDRAWYLIAWENSSVPVAFSHFRFDVECGDEVLYCYEVQLESKVRRKGLGKFLIQILQLMANSTQMKKVMLTVFKHNHGAYQFFREALQFEIDDSSPSMSGCCGEDCSYEILSRRTKFGDSQHSHADHGFLIPLTQGDQKEPPVFIPCKVSSVYIVSFQSLDAWHQLVKGCLVPYPAHPSLCRPCPEGFLRRSGLGWERHCLRPAVTLVGVEPIHFQNICLSPLPPGLGFEKHSRHGWAGWLTPVISALWEAEAGRVT
|
[
2605,
24917,
24978,
29733,
32329,
35846,
36091,
49230,
67196,
87125,
87367,
87735,
87821,
87857,
88008,
88153
] |
The following text describes a protein:
Function:
N-alpha-acetyltransferase that specifically mediates the acetylation of the N-terminal residues of histones H4 and H2A. In contrast to other N-alpha-acetyltransferase, has a very specific selectivity for histones H4 and H2A N-terminus and specifically recognizes the 'Ser-Gly-Arg-Gly sequence'. Acts as a negative regulator of apoptosis. May play a role in hepatic lipid metabolism.
Subcellular Localization:
Cytoplasm. Nucleus.
| 0
|
MPSLPQEGVIQGPSPLDLNTELPYQSTMKRKVRKKKKKGTITANVAGTKFEIVRLVIDEMGFMKTPDEDETSNLIWCDSAVQQEKISELQNYQRINHFPGMGEICRKDFLARNMTKMIKSRPLDYTFVPRTWIFPAEYTQFQNYVKELKKKRKQKTFIVKPANGAMGHGISLIRNGDKLPSQDHLIVQEYIEKPFLMEGYKFDLRIYILVTSCDPLKIFLYHDGLVRMGTEKYIPPNESNLTQLYMHLTNYSVNKHNEHFERDETENKGSKRSIKWFTEFLQANQHDVAKFWSDISELVVKTLIVAEPHVLHAYRMCRPGQPPGSESVCFEVLGFDILLDRKLKPWLLEINRAPSFGTDQKIDYDVKRGVLLNALKLLNIRTSDKRRNLAKQKAEAQRRLYGQNSIKRLLPGSSDWEQQRHQLERRKEELKERLAQVRKQISREEHENRHMGNYRRIYPPEDKALLEKYENLLAVAFQTFLSGRAASFQRELNNPLKRMKEEDILDLLEQCEIDDEKLMGKTTKTRGPKPLCSMPESTEIMKRPKYCSSDSSYDSSSSSSESDENEKEEYQNKKREKQVTYNLKPSNHYKLIQQPSSIRRSVSCPRSISAQSPSSGDTRPFSAQQMISVSRPTSASRSHSLNRASSYMRHLPHSNDACSTNSQVSESLRQLKTKEQEDDLTSQTLFVLKDMKIRFPGKSDAESELLIEDIIDNWKYHKTKVASYWLIKLDSVKQRKVLDIVKTSIRTVLPRIWKVPDVEEVNLYRIFNRVFNRLLWSRGQGLWNCFCDSGSSWESIFNKSPEVVTPLQLQCCQRLVELCKQCLLVVYKYATDKRGSLSGIGPDWGNSRYLLPGSTQFFLRTPTYNLKYNSPGMTRSNVLFTSRYGHL
|
[
6409,
6686,
8828,
10809,
11620,
25040,
25069,
25495,
26070,
26218,
29033,
30063,
32115,
32536,
33240,
34356,
39520,
87016,
87103,
87110,
87139,
87278,
87311,
87367,
87371,
87402,
87407,
87722,
87747,
87767,
87782,
87829,
87855,
87976,
88008
] |
The following text describes a protein:
Function:
Polyglutamylase which modifies tubulin, generating polyglutamate side chains of variable lengths on the gamma-carboxyl group of specific glutamate residues within the C-terminal tail of tubulin. Mediates both ATP-dependent initiation and elongation steps of the polyglutamylation reaction. Preferentially modifies the beta-tubulin tail over an alpha-tail. Competes with monoglycylase TTLL3 for modification site on beta-tubulin substrate, thereby creating an anticorrelation between glycylation and glutamylation reactions (By similarity). Required for neurite growth; responsible for the strong increase in tubulin polyglutamylation during postnatal neuronal maturation (By similarity).
Subcellular Localization:
Cell projection, cilium. Cytoplasm, cytoskeleton, cilium basal body. Cell projection, dendrite. Perikaryon. Note=In cells with primary cilia, found in both cilia and basal bodies. In neuronal cells, found in dendrites and perikaryon.
Domain:
The enzyme uses its core to engage the disordered anionic tails of alpha- and beta-tubulin and the flexible c-MTBD (cationic microtubule binding domain) region to bind the microtubule and position itself for beta-tail modification. The c-MTBD region is positively charged and becomes ordered when bound to microtubules: it interacts with a negatively charged patch on alpha-tubulin. The presence of positive charges in the c-MTBD region is essential for proper binding.
| 0
|
MPSNPNRSIYDFYNITDIIGEGTFSTVTLANHIEKIEDKYAIKIISKEVLDNERRTYVDWEISILSKCQHPNIIKFYEHYESDEDICLVLEWIPNGDLFDRIVKKGVFNEEEARLTMKSLLSAVEYLHDKSVVHRDIKPENILFSDSYGGIKLGDFGLAKFYEESIGLELACGTLAYSAPEITNNQVYRKSVDMWSCGCILYFILFGRPPFYSDDESEMFELITKGQWEFPSKTQHKYSDQVKDLIKLLLENDPNKRLTVKQSLAHKWIQSIDERSFSSVIKQSPLITSQQQQQQSPSSLLSSSSSSTASSPSLKPLSPLVAIIEQQEYNYNHQQLQNHNILHSSNSHSRHHHASSANSTTVDQQQEEDNNHHYHRHNSNNNINNNNDNNDNNNSNSNNSNNNINNFINNNNNNNNNNSNFFDDDDEIDINQNEMDDIDDEQQQPTNSLRSSSKPIAIKKSQIRTSLNGNIDIKRGVLTPL
|
[
3613,
8175,
8663,
24978,
28524,
28531,
29033,
36535,
42974,
45290,
50333,
59889,
87110,
87694,
87855,
88008,
88052,
88153
] |
The following text describes a protein:
Function:
May phosphorylate a specific serine in the N-terminus of a myosin light chain.
| 0
|
MGKAEESGRKETQQSISMQVMNLPRDLLQRFMSSSNHFSQNGETEEEEQEEEIELSLGLSLNGRFGVDPKAKKLTRSSSIPDFINNTNESSSSPSYLFPMACGSLVRTCSLPVETEEEWRKRKEIQSLRRLAAKRKRSEKQKNLKALKDKNREGLGEENCDEDKKEEGWVNGGRGPLMAASQGSIGSQGSGSSGISELDSQPPQGTYKCQGSRSPTSVQSTTQTEQKPNIINPGKISTQKSEKLAGITAKNQHNQPGVDEKRLRASLKNIMEDMPCVSTTGDGPNGKRIEGFLYRYRKGEEVRIVCVCHGSFLSPAEFVKHAGGGDVEHPLKHIVVSPSFIF
|
[
8663,
9429,
15387,
24917,
46376,
60221,
61078,
61080,
87857,
88008
] |
The following text describes a protein:
Function:
Acts as a negative regulator of abscisic acid (ABA) response.
Subcellular Localization:
Nucleus.
| 0
|
MVEMLPTVVALVLAVSVVAKDNTTCDGPCGLRFRQNPQAGIRIVGGQTSSPGAWPWMVSLQIFTSHNSRRYHACGGSLLNSHWVLTAAHCFDNKKKVYDWRLVFGAHEIEYGRNKPVKEPQQERYVQKIVIHEKYNAVTEGNDIALLKVTPPVTCGDFVGPGCLPHFKSGPPRIPHTCYVTGWGYIKDNAPRPSPVLMEARVDLIDLDLCNSTQWYNGRVTSTNVCAGYPEGKIDTCQGDSGGPLMCRDSVDSPFVIVGITSWGVGCARAKRPGVYTATWDYLDWIASKIGPTALHLIQPATPHPPTTQQPVISFHPPSIHPPWYFQHLSPRPPHLRPPRPLLHQPSSVHTSSAPVIPLLSLLTPVQPVSFTLAAYHTRHHTTLSFARRLQHLIEALKMRTYPIKYPSRYSGPVNYQHRFSTFEPLSNKPSEPLLHS
|
[
4573,
7176,
8200,
8682,
8781,
8782,
8783,
8784,
11624,
16171,
24841,
25022,
25807,
26205,
28105,
28227,
29039,
29144,
29147,
32076,
36986,
37036,
43583,
46236,
50917,
61632,
69992,
87413,
87522,
87601,
87965,
88008,
88049,
88058,
88264
] |
The following text describes a protein:
Function:
Acrosin is the major protease of mammalian spermatozoa. It is a serine protease of trypsin-like cleavage specificity, it is synthesized in a zymogen form, proacrosin and stored in the acrosome.
| 0
|
MQLYLVLLLISYLLTPIGASILGRCTVAKMLYDGGLNYFEGYSLENWVCLAYFESKFNPSAVYEDPQDGSTGFGLFQIRDNEWCGHGKNLCSVSCTALLNPNLKDTIQCAKKIVKGKHGMGAWPIWSKNCQLSDVLDRWLDGCDL
|
[
8781,
9332,
24841,
24907,
26074,
27944,
36747,
37535,
52289,
55152,
87278,
87311,
87369,
87413,
87461,
87468,
88008,
88038,
88058
] |
The following text describes a protein:
Function:
May be involved in fertilization. Has no detectable bacteriolytic in vitro. Has no lysozyme activity in vitro (By similarity).
Subcellular Localization:
Secreted. Cytoplasmic vesicle, secretory vesicle, acrosome. Cell projection, cilium, flagellum. Note=Found in the principal piece of sperm tail.
| 0
|
MTKQAEETQKPIIFAPETYQYDKFTLNEKQLTDDPIDLFTKWFNEAKEDPRETLPEAITFSSAELPSGRVSSRILLFKELDHRGFTIYSNWGTSRKAHDIATNPNAAIVFFWKDLQRQVRVEGITEHVNRETSERYFKTRPRGSKIGAWASRQSDVIKNREELDELTQKNTERFKDAEDIPCPDYWGGLRIVPLEIEFWQGRPSRLHDRFVYRRKTENDPWKVVRLAP
|
[
1783,
9110,
9313,
24987,
28563,
29679,
36483,
45707,
46284,
52100,
52242,
87005,
87103,
87456,
87470,
87684,
87785,
87873,
87987,
88008,
88180
] |
The following text describes a protein:
Function:
Catalyzes the oxidation of either pyridoxine 5'-phosphate (PNP) or pyridoxamine 5'-phosphate (PMP) into pyridoxal 5'-phosphate (PLP).
Subcellular Localization:
Mitochondrion intermembrane space.
| 0
|
MECVKQLCRNHLRLDNLTDPVRSVLTKGTTAEKVQLAACCLGVVCSIICLALGIAAAAVGVSCGGFALGLGIIAILLGIVLFATSALDVLENHGLVGCPFKLPCKSSPANEPAVQFFKGKNGSADQVILVTQ
|
[
24878,
25884,
27248,
63047,
87586,
87760,
88038,
88159,
88161,
88240
] |
The following text describes a protein:
Function:
Inclusion membrane protein probably involved in early modification events of the chlamydial inclusion.
Subcellular Localization:
Secreted. Host vacuole, host pathogen-containing vacuole, host pathogen-containing vacuole membrane; Multi-pass membrane protein. Note=Secreted, probably by a type III secretion system (Probable). Localized in the inclusion membrane. Inclusion membrane staining is punctate.
| 0
|
MSGQGEDDSDISEEFSGEENEGWDEDISDEDDVIDEEEEEEEEETNQMEEAGRNIQQLAKRVLEDEETTDQPPTKSVRTGKPDLYRPPTNEEMNQLKETENLFQSSLFRMQIEELVSEVTPKNKKSPALDKVLHSLNEIVMKLPKTDSKELTDQSWLPSNVKVPIQQSPYQVKGHFHFAPPTSMKVVGSYLLGFCTKPGMNVDVLLEIPKECLQAKDYLNHRYHRKRALYLACLAASLDKQDLFTSVMFTFFHQDCNKPVILLKPSGKAGKHYTIRLHACPPEGFFKPSRFHPDKNNIRSDWYMGKGRDQDSEPPTPHYNSSILVDMTMAEHLHHLFSLSADFPAMREGLVLLKVWLHQRELDTGSGCFSGFLMSMLLSYLLSAHKLSKVMSSYQIMKNVLQYLANSDWSTQGISLASCVTAEDVPTLSDFHQAHQVVFVDPTGHLNMCADMSTATYARVCHEARQAVAILEDKSLDGFQLLFMQTVPFAHKFDHIFHITRVPRLRLVCEHMSLQDAVMDHCGNYLMAALPSILQLLNKALGNRVSLIGVRGHDFGQWSIGDAPPSLKDIGRLTFGLLLNTEFSTSVLDKGPPADQPQAAEFCEFWGDKSQLRRFQDGTICEAVVWQGSNIAERRLVCCQVIQHILNRHANIPQSIIKYFGGHLDSLLSRPNLQGGTAAQSTDTHDKLHKSQPQGKKAKKSKNAPKEQLLDPNQNSTSHPGTGDEENVTVMRVYNDLCRILRGLQDLPLNITSIQGTSPVFRYAEVFPPRPAHMKKTKDKTVVQGHIQVPVSGQPCPPFVPALKVICHMEGSGKWPEDADAIRRVKAAFHIKLGELLHKQHGLVTSAATGHVDIAMGGFVFQLVIAYHREVNILKLEKTAEGLLRERDNEASRHLERETVMLPKLTSALHGLQQLYSSFSGCLRLAKRWVSAQLLHRHVPDVMVDLLVAHVFLHPQPLTPPGSPAVGFLRFLHLLSTHDWKMNPLIVNFNRELKAADLQEISNQFTSCRSQLPIMFIATPNNKLTSHWTKAKPTVQVLQRLISLSQEALKMLEVQILTASDGTDFKQVFRPPLDIYDVIIHLNPWNVPRRSEGVDYLKLKGCRDVPTDGGMGQGSKEILPVVEFDPVQMYLEELEDTYGDMALFFHDPCGGLYITALWKPAAFTAKPFKVTTLNGRAPDLDQSGEDLMMIPNVAAILEDFHSLGKGLVILVDVKKERPVVR
|
[
8109,
8137,
24957,
25726,
25779,
25922,
27925,
40606,
63018,
63231,
63232,
63233,
63234,
63235,
87306,
87857,
88001,
88008
] |
The following text describes a protein:
Function:
Part of the small subunit (SSU) processome, first precursor of the small eukaryotic ribosomal subunit. During the assembly of the SSU processome in the nucleolus, many ribosome biogenesis factors, an RNA chaperone and ribosomal proteins associate with the nascent pre-rRNA and work in concert to generate RNA folding, modifications, rearrangements and cleavage as well as targeted degradation of pre-ribosomal RNA by the RNA exosome.
Subcellular Localization:
Chromosome. Nucleus, nucleolus.
| 0
|
MTSEVIEDEKQFYSKAKTYWKQIPPTVDGMLGGYGHISNIDLNSSRKFLQRFLREGPNKTGTSCALDCGAGIGRITKRLLLPLFRVVDMVDVTEDFLAKAKTYLGEEGKRVRNYFCCGLQDFSPEPGSYDVIWIQWVIGHLTDQHLAEFLRRCKRGLRPNGIIVIKDNMAQEGVILDDVDSSVCRDLEVVRRIIRTAGLSLLAEERQENLPDEIYHVYSFALR
|
[
2213,
8596,
8603,
10797,
10798,
10799,
13411,
13412,
24917,
24926,
25040,
29169,
32000,
34422,
43232,
59229,
87115,
87777,
87857,
88008,
88026,
88153
] |
The following text describes a protein:
Function:
Distributive alpha-N-methyltransferase that methylates the N-terminus of target proteins containing the N-terminal motif [Ala/Gly/Pro/Ser]-Pro-Lys when the initiator Met is cleaved. Specifically catalyzes mono-, di- or tri-methylation of the exposed alpha-amino group of the Ala, Gly or Ser residue in the [Ala/Gly/Ser]-Pro-Lys motif and mono- or di-methylation of Pro in the Pro-Pro-Lys motif. Some of the substrates may be primed by NTMT2-mediated monomethylation. Catalyzes the trimethylation of the N-terminal Gly in CENPA (after removal of Met-1) (By similarity). Responsible for the N-terminal methylation of KLHL31, MYL2, MYL3, RB1, RCC1, RPL23A and SET. Required during mitosis for normal bipolar spindle formation and chromosome segregation via its action on RCC1.
Subcellular Localization:
Nucleus. Note=Predominantly nuclear.
| 0
|
MSVKSAAMRDAADSEEFEDMSEDYEEASDASYEYEEGSDDDACHMDAAHGDAGPSSSAGPGWSVLNQDAIVKLQAEAVADVVAILGVKSSVAKTVLMYFRWDKEALMSKVAERDPESVLKQAGVAITDAGSAGPNGQQGGPIMCRVCFTDTEQAETTSMDCGHAFCNDCWRQHFKTQIGEGQARTIRCMAPKCGVVCDEEKVCSLLKSDPAASSSTAAGSGSAGPSGSAGASGSAGTSGSGREPNEALDKYKHSMALSYVEDNARVNFCPSVPWCGHAVQVDGDPFVEPECSCGKVFCFKCLKDPHTPCTCKMWDEWDEKIHGDSETRNWFMANTKPCPKCSKPVEKNGGCNLVMCKCGQAFCWLCGAATGTQHTWQKIEGHSCGRWKDELDRKIDNAARSHKRYMHYFERYKLHMDSYSKEGVKRSDLLKRIGEMVETGIEARDYTWLVRALDQLKVARGVLSNSYAFAYFFFGGEMYKDDFSDEDNKRNQDLFEEHQQRLEGEVERLSGLVEECSESLTIDSDARVRVINSTVSIESRILKFFDMIEVDLYGKLQSCSAQIAVYRPKRNLVA
|
[
2746,
8202,
10753,
24729,
24978,
29166,
31138,
34103,
37468,
38301,
46929,
51583,
60177,
70370,
72000,
74773,
87767,
88008,
88009,
88153,
88181,
88261,
88263
] |
The following text describes a protein:
Function:
Might act as an E3 ubiquitin-protein ligase, or as part of E3 complex, which accepts ubiquitin from specific E2 ubiquitin-conjugating enzymes and then transfers it to substrates.
| 0
|
MEELSWTNVHSQDIQIEAESFWRAIDIWWLKPQVINRRISASVEQHKISGLSESTAAGSLAELSRVTPAVRLHEQWLFSLLNDLKHLTSQEENTTSISFEKCIDHHVSLLEESKNETMSNNQVSKCESGSVGEEKVTEQVAEIVTDNHTGEMENEESLLLDKSKMCVICIRKLLPRRASDAVVHEVGIFDHERNEATFTLLECGSKEAKFPSYKFSFQCSRISLHVDDNYKSAPYSSSIPSIEWLGNTLAPKLTKWASEIVGSGQVVVVKPLVPMDRYTELYREMKQKYGTEFVKIWPENTDPQKFVYEDVAIATYLILLFEEERKETGDDKKQSYVDLGCGNGLLVHILNSEGYPGKGIDLRRRKIWSLYGPETHLEESTIIASMETSFKDTDWLIGNHSDELTPWIPVMAARSSYKTRYFVLPCCFHDFDSKFGQRVGGETQYRTYLNFVREAGEMCGFEVEEDKMRIPSTKKICHVGRRKTYAAEEHPQVLARMEEYVACRCRKSACHKRKSHLIDSVRDSESSRICPVSSLETGIGADSAESTACDCKDTECTHKRELTSSDSSSTEGQCLGGEGDTDKNLAPNFKPRAVEERVKNCSRVERSLKDRITLEVAWAILEDGGVRRTSKDGDEVQGGGGVQDDTGRSSKMPKLWRRGGSIGLGDAAKLFDGPTLKNLKSECGGLKTLLKNYNPVFEIIKSKVSLKDWSQLPSSDATDPVSSSGSSSRTASRQSEKKDRERQQLYKTKLCWFHEHHPDSCPRMAEACPFAHGQVELRSRPTFGKAPVI
|
[
2180,
11739,
24978,
29166,
30158,
35613,
36409,
45777,
87367,
87767,
87777,
88008,
88026,
88153,
88261,
88263,
88278
] |
The following text describes a protein:
Function:
Adenosyl-L-methionine (AdoMet)-dependent tRNA (uracil-O(2)-)-methyltransferase.
Subcellular Localization:
Cytoplasm.
| 0
|
MHCRAHTVSAMPPSSPLVKLPLLPRGLLSYLPASILPSSGRESTITPTTSSPSTPPQPAPPSPKKMSSSPGQQQQAGSGGGKADSAELARVFELFDKNGDGRITREELEESLGKLGMSVPGDELASMIARIDANGDGCVDVEEFGELYRAIMAGDGGRAGGEGAGAGEEGAGGEDADEDMREAFRVFDANGDGYITVDELGAVLSSLGLKQGRTAEECRRMIGRVDRDGDGRVDFHEFRQMMRAGGLATLG
|
[
26225,
29025,
37640,
46081,
51011,
87244,
87767,
88008,
88009
] |
The following text describes a protein:
Function:
Potential calcium sensor.
| 0
|
MAGITGVMNMKLAARPSSGRHSRGCRPAVVPSAGKQMLLVRRHPPGSASWPTRATGGGGGGVPAGATAADSSGQAKEEEEEDRASRNTSSFEPSIWGDFFLTYSSPLATSSAQKARMVHRAEQLKKQVAKLIAASGACSLYHRIHLVDALERLCLDYLFEDEINDMVTQIHNVDVSGCDLQTVAMWFYLLRNHGYRVSSDVVFAKFRDEQGGFAANNPRDLLNLYNAACLRTHGETILDEAASFTSKCLKSLAPYTYMEASLASEIKRALEIPLPRSVRIYGAKSRIAEYGNQTEANELVLELAKLNYNLVQLQHQEELKIITRWWNDLELQTRLSFARDRVVECYFWMVGVYFEPSYSRARVILSKVLAIVSLLDDTYDVYGTSQECELFTKCIESWDPAATGGRLPGNMKFIFAKILDTCQSFEDELAPDEKYRMHYLKTFIIDLVRAYNEEVKWREQGYVPATVEEHLQVSARSGGCHLLSCTSFVGMGDVADQEAFEWVRGVPKIVKALCIILRLSDDLKSYEREKMSSHVASTMESCMKEHQVPLEVARVKIQETIDETWKDFNEEWLNLNTNSHLPRELLERIFNLTRTMVYIYQQDDAYTNCHVIKDTINSLFVEPVSIT
|
[
5620,
5635,
5637,
5638,
5675,
5686,
9350,
10642,
10645,
25225,
27681,
29710,
33596,
33597,
35032,
37526,
40676,
43535,
43545,
62779,
64688,
71056,
75803,
87016,
87017,
87139,
87296,
87321,
87741,
87747,
87752,
87767,
87930,
88008,
88154
] |
The following text describes a protein:
Function:
Component of the volatile terpenes biosynthesis pathways. Mediates the synthesis of a blend of monoterpenes. Converts mainly geranyl diphosphate to alpha-terpineol. Also triggers the biosynthesis of minor monoterpenes including limonene, gamma-terpinene, beta-myrcene, terpinolene and 4-terpineol.
Subcellular Localization:
Plastid, chloroplast.
Domain:
The Asp-Asp-Xaa-Xaa-Asp/Glu (DDXXD/E) motif is important for the catalytic activity, presumably through binding to Mg(2+).
| 0
|
MKSRKVKSVRPGRGRILGLTDVTPSTSLPPLVEGQVRSFLQVTVSKILWTVPKPPPSVLVRLRWWGETANGTVFRPRDSSQTEQKGAKTTTRYAVRCGPKQFTSYLTDMGMLVFEVMTKLDHFPIGRAQISGIAQLSLAHPVSGFFTIVSPTSEKLGELQVSVQLEPLPETYDSSSSAPNTDISFDHASESYGKALTGHPTTMNDPPQPIILSLASADKRESESSSRVTTPRGRDHLYFQENADPGKDSYRGTQDHVTVGWSNVTEGVQSIKPIYSEGTTAGKDALTVNSGPATKDLLSALLDQGSKLRDAMVVSALKSSPDLDHNPDIKLPLALNNYSLSQARATSEIPSPTLMRNLLNSRHSPQTRDILLQPADSFIPDMEAPSDAKAIELLLGSSVLSPGHYWDGTGSPPESISGSDFYNESELNDPLYDQSLLEKLFYKAPKSDSSASDFMSDDENTRSQNKKNKIALDRGRHRDNSPSEYKEDAKQTKGNDSLRDSKTSEKSTSRCEGISLSMDQAALLGQIHVAHVVVESLRVPLDGTAVTPSKTNSRGRPPRPVRPAKQTFFVEFQFPVLSKSRSGEVNSATEITRLVSSKVVNGSIKFQQRFTFPVLFSGQMIKHWWNTDLTFRIFLRKGTQNKPGPVGSATLPLRDVLQSPGLSVTCSLPVSCTAEDSHTAAGPLKISVALAGDNKNIHDISEKTLEPENQAPVLPAVTSKAELENSASYTDLRPVAEKSSPLRQSLPPHIGNGGPKVSFSQNPQQTAEEDGLLLHIVLMVPEGKGLVAAGGDSSGICNSYLNCKLFSAQEATRSSVVWGSTQPQYNFSQVAPLTLNARLLERMKNNVMIIEIWNRVASPGQDQLLGLAKLPLHQFYMSFSDPKITRLLLQAQYPVVAVDSYVPIIDVFSGCDRGKLKVLLAIGSGDQVVALQRLKNEEGTSQTAMPRPAHFLDPPLSSSQMGRPQEGMTDHIFEIHVENVKGLTPLQSTVWGEADCFVQYYFPAHGPDSHTAIDLPEIAMTLKPVRTATTLCVPDPVFNDRQSHTIVAQSDTPVQRLLLGAYSMQGLSGGGGVPFEIWCRYYYPNVRDQMVAKGVLPLSRLCAMVTMQHREDVGIQAFSLPLIPRSEKSAELPPQPSGLLNVNVTYRRSMRNPVGMLATRMASISVQIHRASGLQAAARLVAQQDASFQYSADVGVNAYVTIHPAFLPDVELRNTRTVARTFCPEFDHHYEFPCNMVIQRNNGEACSLAEVLYFSEIVLSIHHQNVASVGSTRPQPVRDYHLGMVRIPCRQLITKRSGVSGWYPVTVPEDSKLPTDSTILHSVVGGLELSVHFAHHSDRDRVLEVARGLGWNEYNEDFQEAIATEADEWHKREDLVNLSVNIPKIWLPLHCLLLAGHKHIHKSTYCYLRYKFYDREAVCSPLRRPRLSEDGQQATIMFELSENRELIKHQPLVWYLREERMEIQVWRSYGKDTNGPRPQDTDRLIGCAYVDLKALSENTSRTLAVSGVYPLFKRNVSSLWGAAVRVHLALSSAYHPSNSSRRLSCAGERSQSEGEEWAPTSGDSFEEKQDDSAKNDKPEAKTEVPLLDAKEQPVGEVDLKNTFAASIVVERAMHLSLKGTPLTERAAATPTCCVSYPVAGCSEPVTTPVIANTDSPLWNFQHQARLHKELLLDPQQRLVFKVWHKTDVERVVGFASVDLSPLLSGFQSICGWYNIVDFVGQCQGQVKVSITPLEGVAHLKTKVTSQRSSSYQSRPAFCSSFSYNPSQSEVPAFIPHIPTLHHQLSDRENSGPLFPFLRHEEHMENVRRFHESLQQAERNAHTVEGLDSLSQSSRSSLLSALRKNLGELDEIQKYFNQKLYRSISNAETSRCASVQIPQVQPPNSEPAEEDSDAKMLLQKSSFLVSQVSNLITGLQGIPKFAPAFSSTEQRLDVQGQTSVQHQQVDNMEPMAPERSEAYEREGQRSDTPPFSPLGSLNVSGEKLMEFIGTDMDEKERHLFAEKHQEEQDKHIIHGSSDEEYEEDVIEPRTLNEITTMTDRTSPWSSILSERDSDSMDHPQDQPVNPLAAENNRVITDFFSSFHQNDPSSVLSSARSTDSEVLAEGSRVRKISSSSGSEAETVGVQLSVDPAEQGALGEAESEAESQEMDGDPEANRTEEEQQDPVTVFSALSSGSDESEHITYGASEPDCSPPQDEPETDYPCSEPLEGNMHHIDEEEQPAGSESPQVPPSNLLSDPVIVPNFFLPPQHLEASMRHLSLSAVREGRSDTPGIPFRRSKRQKPRLAPADLPKEETNRIARIFAAQFPGPPTPP
|
[
18103,
18977,
23543,
24978,
25027,
25108,
25920,
35959,
63695,
65368,
87278,
87311,
87312,
87367,
87371,
88008,
88009
] |
The following text describes a protein:
Function:
Component of the centrioles that acts as a positive regulator of centriole elongation. Promotes assembly of centriolar distal appendage, a structure at the distal end of the mother centriole that acts as an anchor of the cilium. Required for primary cilium formation (By similarity).
Subcellular Localization:
Cytoplasm, cytoskeleton, cilium basal body. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome, centriole. Note=Localizes to centriolar satellites. Also localizes to the distal ends of the mother and daughter centrioles (By similarity).
| 0
|
MIAPRLSMPAIVNAQSLVAKLRQLNCEKNYCHPNNLPGFTASAFYKESSSPLDQLVQTARLCHWLLSQLGISVQGVSEFDDPIAISTDLLVACKDIVNVANIPPHRIRMGYGDDLTALVLGIADACLAKLQPNIVSWKSLGSENANAGVERDNDDDDAPILDDLIVDDALIGTMTAKKGTFTTAAGLATGSLTTDSGCIAPGLISEADWEQELMAVDSQLGGKQLGGVYAGQDWRKDVVSMSLLAKALSKETGSCAQSISGLVTDFGKQLERISTREQHLNSQVGQYSAKLGDANRTHAGVTEELAELSQSISALTGELSTINEKLRALKVELQVESARASDTSNIHIVKTAFSSLSGEIRQLDLRITLAQQRLFSIAPPEPNTVRI
|
[
13491,
14057,
17404,
23543,
25018,
25028,
25108,
25109,
25564,
26070,
26954,
26989,
27615,
52063,
87278,
87311,
87312,
87367,
87371,
87468,
88008
] |
The following text describes a protein:
Function:
Component of the intraflagellar transport complex B (IFT-B) involved in flagellar assembly (Probable).
Subcellular Localization:
Cell projection, cilium, flagellum. Cytoplasm, cytoskeleton, flagellum axoneme. Cytoplasm, cytoskeleton, flagellum basal body. Note=Localizes to the cytoplasmic and membrane-bound portions of each of the eight axonemes, localizing particularly at the flagellar pores and at the distal flagellar tips. Localizes to the basal bodies.
| 0
|
MASIKYNIPKDGKLGFRLAESEPKFNWRNNPRIADCRRLVTNSIQVHLVQNASMNFAPEIPALAAYLENQLFKDALSENDYMDREKLLIRVQNLINLRWTSAQHEPMHATTSLPTYVSAPTLGMKSNLINKPLCDQYTIADTGCMLDRAPKLLADVPRSSIYGSQKCMLEANLWQPELVPPNNHFSGMGFSNAESGDSGITYSGLQYDSEASFESHRYKYQDSTKGEANFDIFNDMNSPSVHTSAMARENLKFEVSSVSDGLYMRQPVLGSLQLKQQLSCLESHSDGRFGENESLGSLPVQNRNLYALPGTTSTSSNTQQLPAVLLVNYIIYNLSRGRLKVPLLEFLHSRNCEGGICKCEEHKWFLSHYDDCGSANCNICGPAVKECSARGINIVQPGLRKQRIGVDRLTHSNDCGKRVCVNTSEDLMNPAKSRKLDSSPRSDSPCDVSVLTEEPFSPSGPLNFAQPSVSQMMATIANPGANVEITTSHTNDALRISEVDNSHLDDVLGSGDATLPSEGVSAVVQQKDERVSSHIYDAARLSQEGNGTLKDTWRSNSDDVTKFSDDPSADDFCQKKIEPAVNELKVEVPDSRCELPSDYVPTFCDDKSIAPNVDFTPGRDPEEIQPRINQEGFPPIPGSWTGMKSEKQKVDGISLIDFFTPEEIKQHISGLRQKDDQGIIKELVGNGASCSVSENFCQLCALPQLAFSPMPLYCSSCAGRIKKNATYYSTNDKTCDPFFFCTTCYNKCHREFTFYGLSFSKPNLETLKNDSLTVESWVQCDRCEGWQHQICALFNDKKDLGGKSEYLCPRCYLEDLEFGVHMSLPRSSSLDASNLPQTLLSDHLEQRLFESLKEERKNRAKAAGKNPEEVPHPADLAVRVVSSVNKRVKVKQQFLDIFPEKSYPAEFPYRSKVILLFQRIEGVDVCLFAMYVQEFGSSCSQPNQRCVYISYLDSVKYFRPDTKTVKGEALRTFVYHEILVGYLDYCKKRGFVTCYIWACPPVKGEDYILYCHPETQKTPRPDKLRQWYQSMLKKATEEKIVVNFSNLYEKFIAPTEEYNTKVTAARLPYFDGDYWSTVVEGMIKKIDKKSRGNPQEQLKGFTKRRLKAMGHTNPSADDAKDILLMQELEQSISSAKEDFIIVYLQFVCTHCHEIISGIRWFCNQCKNFQLCGRCHDVAKQSGPADTHMSSAGQRHALSQEVVNDVPVDTEDNDAIMDNCFLENRHALLSFCQGNHYQFDSLRRAKHSSMMILYHLHHPNGSNAGTSCGLCLKDIISADPRWMCEICPEFNVCSSCYEKRGAFCHNHTLMHHPSTAIRKTEVKMEELVKQLLDVLLHASRCQTTTNHPCSYPNCVILRRLFSHAHACSIRVAGGCRHCKKTWFILLMHSRKCKDSSCGIPRCMELKNHARRIELESASRCLPSVSVIN
|
[
2673,
15427,
24715,
24917,
24936,
27922,
28307,
29166,
31126,
36103,
36296,
37576,
45292,
46929,
47005,
52278,
60193,
63699,
69834,
87123,
87125,
87302,
87767,
87857,
88008,
88148,
88150,
88153,
88261,
88263
] |
The following text describes a protein:
Function:
Acetyltransferase enzyme. Acetylates histones, giving a specific tag for transcriptional activation.
Subcellular Localization:
Nucleus.
| 0
|
MAMLSTASVSGSVDLPRGTMKVDSSASPEVVSDLPPSSPKGSPDRHDPSTSSPSPSRGGDNQSEVISKSEEYRQLFRLPADEILVQDFNCACQESILMQGHMYLFIHYICFYSNIFGYETKKIIPFAEISCVKRAKTAGIFPNAIEILAGGKKYFFASFLSRDEAFKLIHDGWLEYGSAVKSEGEILVTEPQVSDGVVKRARSSMDLANELDIPVRDETLHLSSSSSLPVISQNGVPPSSVQRHAEPDVDVVAANTFNWKPEDTDAPKLSSDFTKVAEAKFSIPVEEFFRLFFSDGAVSFVESFHKNCGDKEFRCTSWQPHEKLGHTRNVSFQHPIKIYFGAKFGGCQESQKFRMYRNSHLVIETSQEISDVPYADYFTVEGVWDLKRDCRDSVEGCILDVYVNVAFSKRTVWKGKIVQSTLEECREAYAHWIRMAHELLKQKKLENQEGNKLIEDGEPLAAREERVSECDEEGKVEMVGEGVVKKSLKEAWVNLTSFVKRQSGTRQVIVLAFAVILLMQVTIVVLLKKGGGGQVEYHERYDEYSVNGETLGWLEKRMHFLREEMMMVEDRLQRMRQDHAALKAQFHHLERLLRRNKQ
|
[
9358,
9420,
9441,
9515,
14335,
14481,
24878,
25008,
25225,
25325,
39372,
46082,
60823,
87170,
87296,
87326,
87441,
87522,
87604,
87760,
87925,
87930,
88008,
88154,
88159,
88161
] |
The following text describes a protein:
Function:
Involved in ethylene- and salicylic acid-dependent cell death control associated with cells in the vicinity of vascular bundles.
Subcellular Localization:
Membrane; Single-pass membrane protein. Plastid, chloroplast.
| 0
|
MTSRDQLVQQVLRDLQEAVESEGLEGLIGAALEAKQVLSSFTLPICQKGGPGAQVLEVDSVALSLYPEDAPRNMLPLVCKGEGSLLFEATSLLLWGHTGLSLELRARTVVEMLLHRHYYLQGMIDSKVMLQAVRYSLCSEESPEMTNLSFATLEAIFDADVKATCFPTSFSNVWHLYALASILECNIYSIYPMRNIKIRPYFNRVIMPRCSTHVTSMLHIMWAGQPLTSHLFRHQYFAPVVGLEEVEADCTASLNPVPPNLGPLLPPAKTLELLNREPGLSYSHLCDRISITKSTFYRWRRQTQEHRQKVATRFSAKHFLQDSFHRGGFVPLQQFLQRFPEISRSTYYAWKHELLGSGANSALGPATPSREALAVPEVERPPGKKAAEEVGCSSLAAAMLSPPSMILMQRAKSFLEYCISLNKLVPYRCFKCRFPGISRSTYYNWRRKALRRTPSFKLSQAAFETAESLQPTDVGKETPFSLKREAGEEETGKAGSGAPLTSRGLISPKMPLSRWQRRLRRAARKQVLNGHLPFCRFRLRYPSLLPSTFWVWKSLSRRSPGMQIPSLSQRRQKPQGRQKPEGRQKPEEQQKPEGRQKPEGRQKPVEPQAMEADQNVPAMVVPPAETLPVATSPEDVPGGPSREGNIIQEAAMTQSQPHSGSLPSQTLAEAPGGSDGQVLVMDMLTTTRFKAQAKLFLQKRFQSKTFPSYKEFQALFPLTARSTYYMWKRALYEGLTLIDG
|
[
8103,
24917,
27904,
66283,
73242,
87384,
87402,
87857,
88008,
88148,
88150
] |
The following text describes a protein:
Function:
Acts as a transcription factor that regulates development of thoracic vertebrae.
Subcellular Localization:
Nucleus.
| 0
|
MAPSSPSPAAPTRVSGRKRAAKAEEIHQNKEEEEEVAAASSAKRSRKAASSGKKPKSPPKQAKPGRKKKGDAEMKEPVEDDVCAEEPDEEELAMGEEEAEEQAMQEEVVAVAAGSPGKKRVGRRNAAAAAGDHEPEFIGSPVAADEARSNWPKRYGRSTAAKKPDEEEELKARCHYRSAKVDNVVYCLGDDVYVKAGENEADYIGRITEFFEGTDQCHYFTCRWFFRAEDTVINSLVSISVDGHKHDPRRVFLSEEKNDNVLDCIISKVKIVHVDPNMDPKAKAQLIESCDLYYDMSYSVAYSTFANISSENGQSGSDTASGISSDDVDLETSSSMPTRTATLLDLYSGCGGMSTGLCLGAALSGLKLETRWAVDFNSFACQSLKYNHPQTEVRNEKADEFLALLKEWAVLCKKYVQDVDSNLASSEDQADEDSPLDKDEFVVEKLVGICYGGSDRENGIYFKVQWEGYGPEEDTWEPIDNLSDCPQKIREFVQEGHKRKILPLPGDVDVICGGPPCQGISGFNRYRNRDEPLKDEKNKQMVTFMDIVAYLKPKYVLMENVVDILKFADGYLGKYALSCLVAMKYQARLGMMVAGCYGLPQFRMRVFLWGALSSMVLPKYPLPTYDVVVRGGAPNAFSQCMVAYDETQKPSLKKALLLGDAISDLPKVQNHQPNDVMEYGGSPKTEFQRYIRLSRKDMLDWSFGEGAGPDEGKLLDHQPLRLNNDDYERVQQIPVKKGANFRDLKGVRVGANNIVEWDPEIERVKLSSGKPLVPDYAMSFIKGKSLKPFGRLWWDETVPTVVTRAEPHNQVIIHPTQARVLTIRENARLQGFPDYYRLFGPIKEKYIQVGNAVAVPVARALGYCLGQAYLGESEGSDPLYQLPPSFTSVGGRTAGQARASPVGTPAGEVVEQ
|
[
2339,
12244,
14787,
24917,
27904,
27908,
28004,
36732,
36794,
37213,
49245,
50919,
55524,
59229,
69840,
76045,
87103,
87302,
87384,
87777,
87857,
88008,
88026,
88148,
88150,
88153
] |
The following text describes a protein:
Function:
Involved in the CpXpG methylation and in gene silencing.
Subcellular Localization:
Nucleus.
| 0
|
MEGRPPKSPTRRRLPQSPTRGRALGSPSTCGRAPGSPSTCGGGRSPGSPSTRGMAGCRPPHRRAAGRRAPHRRVAAAGCRDPHRRAAGRPAGRLYCCSCDFFLTLNLAVWDLCRCSCFASVW
|
[
8482,
29024,
29166,
70925,
87767,
87768,
88008
] |
The following text describes a protein:
Function:
Metallothioneins have a high content of cysteine residues that bind various heavy metals.
| 0
|
MDTESQYSGYSYKSGHSRSSRKHRDRRDRHRSKSRDGSRGDKSVTIQAPGEPLLDNESTRGDERDDNWGETTTVVTGTSEHSISHDDLTRIAKDMEDSVPLDCSRHLGVAAGAILALLSFLTPLAFLLLPPLLWREELEPCGTACEGLFISVAFKLLILLLGSWALFFRRPKASLPRVFVLRALLMVLVFLLVISYWLFYGVRILDARERSYQGVVQFAVSLVDALLFVHYLAVVLLELRQLQPQFTLKVVRSTDGASRFYNVGHLSIQRVAVWILEKYYHDFPVYNPALLNLPKSVLAKKVSGFKVYSLGEENSTNNSTGQSRAVIAAAARRRDNSHNEYYYEEAEHERRVRKRRARLVVAVEEAFTHIKRLQEEEQKNPREVMDPREAAQAIFASMARAMQKYLRTTKQQPYHTMESILQHLEFCITHDMTPKAFLERYLAAGPTIQYHKERWLAKQWTLVSEEPVTNGLKDGIVFLLKRQDFSLVVSTKKVPFFKLSEEFVDPKSHKFVMRLQSETSV
|
[
6964,
7039,
7086,
7090,
7669,
7670,
8727,
9561,
10365,
11524,
11614,
12507,
12568,
13137,
13408,
13521,
13763,
13812,
13813,
14049,
15080,
15089,
15969,
15971,
16172,
17237,
17238,
17279,
17306,
17308,
17577,
17578,
17579,
17868,
19710,
19711,
19761,
19763,
23543,
23671,
24844,
25079,
25094,
25336,
25337,
25339,
25474,
26501,
26774,
26826,
27066,
27093,
44024,
87276,
87402,
87760,
88008,
88159,
88161
] |
The following text describes a protein:
Function:
Involved in the control of early morphogenesis and patterning of both axial midline structures and the development of neural plate. Plays a role in the regulation of planar cell polarity, particularly in the orientation of stereociliary bundles in the cochlea. Required for polarization and movement of myocardializing cells in the outflow tract and seems to act via RHOA signaling to regulate this process. Required for cell surface localization of FZD3 and FZD6 in the inner ear.
Subcellular Localization:
Cell membrane; Multi-pass membrane protein.
| 0
|
MGCCGCSRGCGSGCGGCGSSCGGCGSGCGGCGSGRGGCGSGCGGCSSSCGGCGSRCYVPVCCCKPVCSWVPACSCTSCGSCGGSKGGCGSCGGSKGGCGSCGGSKGGCGSCGCSQSSCCKPCCCSSGCGSSCCQSSCCKPCCCQSSCCVPVCCQSSCCKPCCCQSNCCVPVCCQCKI
|
[
25040,
25075,
87692,
87976,
88008,
88009
] |
The following text describes a protein:
Function:
In the hair cortex, hair keratin intermediate filaments are embedded in an interfilamentous matrix, consisting of hair keratin-associated protein (KRTAP), which are essential for the formation of a rigid and resistant hair shaft through their extensive disulfide bond cross-linking with abundant cysteine residues of hair keratins. The matrix proteins include the high-sulfur and high-glycine-tyrosine keratins.
| 0
|
MSVSLLQPYFFMSKTKSYAQILIGSRLFLTAMAIHLSLRVAPPDLQQGGNSRISYVHVPAARMSIVIYIATAINSSLFPLTKHPLFLRSSGTGTEIGAFSTLFTLVTGGFRGRPMWGTFRVWDARLTSVFILFLIYLGALRFQKLPVEPAPISIRAGPIDIPIIKSPVNWWNTSHQPGSISRSGTSIHVPMPIPILSNFANFPFSTRILFVLETRLPIPSFPESPLTEEIEAREGIPLKT
|
[
10765,
24979,
25079,
25709,
29895,
30838,
38044,
38849,
71286,
87362,
87760,
87785,
88159,
88161
] |
The following text describes a protein:
Function:
May be involved in the export of heme to the mitochondrion for the biogenesis of c-type cytochromes.
Subcellular Localization:
Membrane; Multi-pass membrane protein. Mitochondrion membrane.
| 0
|
MLLDEDPATLIRHTIGNFNIVPDKSAVARINESLSTLQQARDLRIREAESALKKLSRNLNTLNNNHLETVSAHSPTAHASEIATLDTQKFRIAKAASDLEIESERLSSQLADLQARLQELEQQGMEGGENVKRGQVDDEISLKLKVYRGLGIDIERDRESGEYSKAIIRNGKKGDVHVVNMDNKFSKFFYANYFWQTL
|
[
8603,
16787,
24917,
25028,
25618,
47070,
65590,
87272,
87273,
87284,
87306,
87326,
87695,
87790,
87857,
88008
] |
The following text describes a protein:
Function:
Acts as a component of the essential kinetochore-associated NDC80 complex, which is required for chromosome segregation and spindle checkpoint activity.
Subcellular Localization:
Cytoplasm, cytoskeleton, microtubule organizing center. Nucleus. Chromosome, centromere, kinetochore.
| 0
|
MDPNCSCPTGGSCSCAGSCTCKACRCTSCKKSCCSCCPAGCARCAQGCICKGASDKCSCCA
|
[
8486,
9789,
15413,
18797,
18801,
18813,
24917,
24978,
29166,
32536,
35957,
50723,
50873,
55353,
87115,
87767,
87768,
87914,
88008
] |
The following text describes a protein:
Function:
Metallothioneins have a high content of cysteine residues that bind various heavy metals; these proteins are transcriptionally regulated by both heavy metals and glucocorticoids.
Domain:
Class I metallothioneins contain 2 metal-binding domains: four divalent ions are chelated within cluster A of the alpha domain and are coordinated via cysteinyl thiolate bridges to 11 cysteine ligands. Cluster B, the corresponding region within the beta domain, can ligate three divalent ions to 9 cysteines.
| 0
|
MMSSNLIMELSTMIPTHSEMLQNHSDQPSGNSTSHNSTNDAFDEFVRCLTLFTCICGVIGNGIVLWLLSFHIKRTPFSFYVLSLAASDFTYLFLEVIWVINYLLYRPMFQNIVNLLTNMGLHVTFTVGLGLLASISSQRCLSILFPIWYRNHHPKRGPMVVCGILWLMSLLLNPPKVYYCVVRMEELPPSGCDLMSKLSGTLMLSMLILMTLSSLILFIRVLWSAKRYKPKKLVILILLTVSVFLLCAVPHGINHSVFNWRAMYNHTFHEISYFLSCVNSSANPLIYFFIGSLKHQRLKEPLRVVLQRALRDDSDLTEDRGTSSRTDTTLDAPS
|
[
8678,
25079,
28715,
36171,
50338,
57581,
87276,
87484,
87522,
87760,
88006,
88008,
88152,
88159,
88161
] |
The following text describes a protein:
Function:
Orphan receptor. May bind to a neuropeptide and may regulate nociceptor function and/or development, including the sensation or modulation of pain.
Subcellular Localization:
Cell membrane; Multi-pass membrane protein.
| 0
|
MRIFVLEDDFSQQTRIETTIEKLLKEHHITLSSFEVFGKPDQLLAEVHEKGAHQLFFLDIEIRNEEMKGLEVARKIREQDPYALIVFVTTHSEFMPLSFRYQVSALDYIDKALSAEEFESRIETALLYANSQDSKSLAEDCFYFKSKFAQFQYPFKEVYYLETSPRPHRVILYTKTDRLEFTASLEEVFKQEPRLLQCHRSFLINPANVVHLDKKEKLLFFPNGGSCLIARYKVREVSEAINNLH
|
[
8101,
25040,
25809,
27655,
27731,
37430,
42319,
45288,
72939,
87123,
87367,
87914,
88008,
88174
] |
The following text describes a protein:
Function:
Required for high-level post-exponential phase expression of a series of secreted proteins.
| 0
|
MFAAIASGNPLQLSVEVPNSNGLQHTIVLSRTKPKLYSHITLFILPNVTFPQDYIATVYFKLSPQEEFKLFGYLSSEKPSAIFKVQIPSSKKDAGDTSDGLGEIDMDVDDGSGAADPFTDTNGSSSNNISELIIGISIEPREQGMMKLEEWKASMNAEAQKNNSLILSRPNLGIIRNITTAGQLAQVYPSLTQELAAKIVQHAYNYLSGFLDAQGNVPIKRFDTWWDKFRNRLANDGTFLDEVTKN
|
[
7892,
8286,
9126,
24917,
24978,
25040,
34098,
43162,
60231,
74231,
87367,
87728,
87731,
87857,
87909,
87911,
88008
] |
The following text describes a protein:
Function:
Involved in phospholipid biosynthesis.
Miscellaneous:
MISCELLANEOUS: Present with 1910 molecules/cell in log phase SD medium.
Subcellular Localization:
Cytoplasm. Nucleus.
| 0
|
MFGNLKKKLSSAIQEGLVISENLQQQYRQRVSSGNSGSSQASGITTPISPLGLNESLSSSRSSSLSLSAPFQLTDGVPSHLNVAAGCSLLAKYEDDWQQIHGANEKNAEKAAQIANQISGIQDQASHQHRIMSELNSSLAGIPTLIAQLQNSSQVLNSLEEMGKQLEIELEKLEDLREECELQEFILEQQFQLSRHKQKKLNELEQYRQQIAQKHQSKIKDQEQTLLKLQRERQAVFDDAFREDMEEYKQRGQLTKIQTTSNKLALEEVVLEANEVETKDALEQFLNG
|
[
8976,
8978,
9013,
9069,
9075,
13794,
15441,
15937,
15990,
16503,
17073,
21254,
25136,
25578,
27007,
42352,
87326,
88008
] |
The following text describes a protein:
Function:
Component of the biogenesis of lysosome-related organelles complex-1 (BLOC-1) involved in pigment granule biogenesis and membrane trafficking in synapses. In response to high synaptic activity at neuromuscular junctions, stabilizes Pldn protein levels and, together with Pldn, plays a role in promoting efficient synaptic vesicle recycling and re-formation through early endosomes.
| 0
|
MLGDTALKLVHDSRRTAALDLLPAYQEELVRGVCREIRQLDASINKTQDEPGYDPQDRVAHCNLLVQHLAMRRDKRCLLAYQFTRARRMNEAAWKQTEEPNLNGNEQEYMKAYEDLIVDIKGPYTDIDLTGSLEPPNDVFIDVRVLQSVGEVQTEYGVFNLEKDSQFFVRRSDVQTLLLQGYLKEI
|
[
22297,
22300,
24803,
40415,
53214,
63993,
87381,
87857,
88008
] |
The following text describes a protein:
Function:
The GINS complex plays an essential role in the initiation of DNA replication.
Subcellular Localization:
Nucleus.
| 0
|
MDTAERAYEKFQNQMIAFDNLKIEMNELAVDLDQQLSDKQSLILQQEQDHKQKVNDLTNQEYKLKLQAKSLKEKENATRDKLNLAMRSLEQQKSKVEDLVKKKQSLVDTKQDLESQIKQLETAIDQGTRELNKSNDNMSLQMNKNLVELNKYEIYTGLKIEVQSNELMCFKFFNLDPNDYDREFAITLNIGGSTYSIENTSPKLSDETVEQIQGKLNQGRQLSKFLKEVRTLFKDFVQY
|
[
8603,
16787,
24917,
25618,
47072,
71364,
87272,
87273,
87284,
87306,
87326,
87695,
87790,
87857,
88008
] |
The following text describes a protein:
Function:
Acts as a component of the essential kinetochore-associated NDC80 complex, which is required for chromosome segregation and spindle checkpoint activity.
Subcellular Localization:
Nucleus. Chromosome, centromere, kinetochore. Note=Associated with kinetochores.
| 0
|
MSEGDAYEDFMMSEDEEMHYAEMEEDSDEMGVYEEETSQGAEEEVPLDPSSSIVEGRYYRAKGLKENSKFREAIEALEGVATSSEPLWAFRALKQIAKCWNFKGAQASEGYQDGVRTALVRLLEHGLRWRQKLGAAYVERSLISTLRMLVPANSQNFVFDEAHEICLPTIEFHLRLLDAVAPLPGDFKDLCTLHMQLRLENLIWRERLRGADCTAILSEAPAPQLTAETLLLLLQCHICRFLRLCQPPAQQFAELVSELQDRAERSLALAQQPHAMVLLAFAQCMRGMQQQPQPHSALRTHFSACLQGLEEIGSNSSFFRDLNLCGFVLADALAYSAGRCSHRVDPFALEQIRILRETPIVHNLQLLYESYVALDLPSFARALDLLAPFRSALAPLFARLCALARERKLWDAIAPLHSCIALADIQRLLCIGSSSLSRDSLLTLMMQGVMASSARVPFRLDLTRDYVYFGDEPRVQLRAPAARPGLRHCAHDLGLTSACARPFQGSSALQLMDCLSEHRNRAASAAADPADAVCRARQPLAAYRTLAALILDE
|
[
6713,
24978,
25142,
36533,
76526,
87367,
87857,
88008,
88062
] |
The following text describes a protein:
Function:
Component of the COP9 signalosome (CSN) complex that acts as an regulator of the ubiquitin (Ubl) conjugation pathway by mediating the deneddylation of the cullin subunit of SCF-type E3 ubiquitin-protein ligase complexes. The CSN complex is involved in the regulation of the mating pheromone response (By similarity).
Subcellular Localization:
Cytoplasm. Nucleus.
| 0
|
MQPQIILITGASSGFGKITAQMLSEQGHIVYGTSRKPSENIGKVRMLVVDVTNSISVRQAVEQIISEQGRMDVLINNAGMGIGGALELATEEEVSMQMNTNFFGVVNMCKAVLPYMRKARRGKIINISSIGGVMGIPYQGFYSASKFAVEGYSEALALEVHPFHIKVCLVQPGDFNTGFTDNRNISELTGQNEDYADSFLRSLKIIEKEERNGCHPRKLGAAICKIVARKNPPFRTKVGPLVQVLFAKSKSWLPDNMMQYALRIFYAIR
|
[
7,
8333,
11615,
25325,
32918,
34296,
37894,
52988,
64058,
77563,
87731,
87823,
87855,
87873,
88008,
88070
] |
The following text describes a protein:
Function:
Catalyzes the reduction of 3'-oxosphinganine (3-ketodihydrosphingosine/KDS) to sphinganine (dihydrosphingosine/DHS), the second step of de novo sphingolipid biosynthesis.
| 0
|
MKNLSETEAEVTMQENVVHESLPQIPVATSVSCCFVLAVLYVGSLYIWSTKHNRDHPTTVKRRFASVSMVMLAAPFFVYFFSSPELLSRVPFPKLLGLRLEGLWQAVVIPYSLTVLLFLGPIFVNMQNESVRSYFDLDYWRGSFGSIIWVRNHVIAPLSEEFVFRACMMPLILQSFSPLVAVFITPLFFGVAHLHHIAERLSLGVELSTALLIGLFQFIYTTLFGFYSAFLFARTGHVMAPILVHAFCNHMGLPDLQDLWQQDLWRRVVAIILYLAGFVGWMFLVPLATDPSIYDNTLYWNA
|
[
4840,
18999,
25014,
28225,
38927,
67032,
87432,
87601,
87760,
87965,
88008,
88159,
88161
] |
The following text describes a protein:
Function:
Protease involved in the processing of a variety of prenylated proteins containing the C-terminal CAAX motif, where C is a cysteine modified with an isoprenoid lipid, A is an aliphatic amino acid and X is any C-terminal amino acid. Proteolytically removes the C-terminal three residues of farnesylated and geranylated proteins, leaving the prenylated cysteine as the new C-terminus. Is able to process K-Ras, N-Ras, H-Ras, RAP1B and G-gamma-1.
Subcellular Localization:
Endoplasmic reticulum membrane; Multi-pass membrane protein.
| 0
|
MLSRSRIALSASYALLNASKRSVGKIVQPSIVILNNRCISQSPRLAKENAVQTTSNRTLKELIEEKTGTSGPYVLGGGILAYLLSKEMLVLHTETLIALSIFGVSYGIIRKVGKPTAEFLDQQGDEILDTLNEGRNMQMERLQEAIEAEKGIERMFDSRNEIFEVMKENNAMKLELEYRKRQQHVYEEVKKRLDYQVEVEQTKRRQEKEHIVGWLEQEVVKSISAQQEKDFLSQCFVDLKAISSSNRL
|
[
10591,
24983,
26421,
29777,
43324,
47569,
87238,
87598,
87676,
87760,
87785,
87786,
88008,
88162
] |
The following text describes a protein:
Function:
Subunit b, of the mitochondrial membrane ATP synthase complex (F(1)F(0) ATP synthase or Complex V) that produces ATP from ADP in the presence of a proton gradient across the membrane which is generated by electron transport complexes of the respiratory chain. ATP synthase complex consist of a soluble F(1) head domain - the catalytic core - and a membrane F(1) domain - the membrane proton channel. These two domains are linked by a central stalk rotating inside the F(1) region and a stationary peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation. In vivo, can only synthesize ATP although its ATP hydrolase activity can be activated artificially in vitro. Part of the complex F(0) domain. Part of the complex F(0) domain and the peripheric stalk, which acts as a stator to hold the catalytic alpha(3)beta(3) subcomplex and subunit a/ATP6 static relative to the rotary elements.
Subcellular Localization:
Mitochondrion. Mitochondrion inner membrane.
| 0
|
MFKDHQSLIPNEIRDLLDLSSVGKSSPGALLTGCSAGGLSTILRCDDFKSLFPLSTKVKCMRDAGFFLDTVDISGGRTLRRMYSGVVNTQCFFPQNIISQVMTPLYILNSAFDSWQIGNSLAPPSADSSGSWHDCSFMFRCNAAQKKVLEGFRISMLNALETFLTTRKNGVLITSGGKQAPFLQRLDQRGLLDLETDWMGLIELTCLPPAGIVATQRAPWLIWSLWTAPKDWQNAQCQDEPKKPSQRKIEDVPHYDTVLQTDAAWTETTGTAGLGWAIKTARETQRFSSSTTFVISPLMAESLAMREAIKKSKELGIRRLRCE
|
[
3922,
18986,
24878,
25223,
33957,
40072,
87280,
87281,
87601,
88008,
88038
] |
The following text describes a protein:
Function:
Hydrolyzes acetyl esters in homogalacturonan regions of pectin. In type I primary cell wall, galacturonic acid residues of pectin can be acetylated at the O-2 and O-3 positions. Decreasing the degree of acetylation of pectin gels in vitro alters their physical properties.
Subcellular Localization:
Secreted, cell wall.
| 0
|
MWEQRRQKVVFSLTILVRYRLKQSMAKKISKNSRAARQSDALEPEVKDLSELPRAEKTDLTNILIRTAAKNEALLEAKISKKANKSKRGKKLNKKALEDKLANSISSMDRDRLVKALNFTNRLDGKIAKSISRAKYIQNTRKAGWDSTNETIKKELAFLNGGLSVQAKSASEGNAEKEDEEIPEVFDSLAEDNTVQKTPTNRFGVLPDDVEE
|
[
6658,
24917,
24974,
24978,
25526,
54707,
78925,
87103,
87367,
87857,
87914,
88008,
88023,
88162
] |
The following text describes a protein:
Function:
Pre-ribosomal factor involved in 60S ribosomal protein subunit export from the nucleus.
Miscellaneous:
MISCELLANEOUS: Present with 2840 molecules/cell in log phase SD medium.
Subcellular Localization:
Nucleus, nucleolus. Nucleus. Cytoplasm. Note=Shuttles between the nucleus and the cytoplasm and is re-imported by the KAP123 karyopherin.
| 0
|
MTDNAIPGPLDPEELQIQYAKSFLLQTDNSGLSLYEHLSALLSRILSERPPNALEVFESLSAELHWSRLKQGSDVLRAPREESHTCRKAEVQRALFSRGDGEGEESEAEGEMTESPLPNLLDLAHLLQQGGVNLGRDEAVRISLALKRLTDTHPLQVCHFWGKILGSGGSYLVAEVQFREGEDDEAEEGGEEEEKGEVEDDVEEEENEEAEDLPPKSTYRPPPVIPKEENGTGANKHVYYVCSEAGAEWVRLPPVTPAQISAARKIRHLFTGNLDAPVITYPPFPGTEINLLRAQIARISAGTHVSPLGYYQFGEEEGEEEEEGAVRDTYEENPDFEGIPVSELVESLSNWVHHVQHILPQGRCVWVNTSVKSEEEEDEEEAEEEEKEEENEPEPEVGPPLLTPLSEDAEIGQTPPWTAFLSTHLIPHYALAVLRSNLWPGAYTVSSAKKFENIYIGWGLKYMPEGYSPPAPPAPQAEYPSGPEITESTDPTVEEEQALKAAKEEAEAAAEEMEEEEDEEEEEEDD
|
[
17404,
17421,
24836,
25668,
41726,
87278,
87311,
87367,
87371,
87468,
88008
] |
The following text describes a protein:
Function:
Functions as part of radial spoke complexes in the axoneme of sperm flagella that play an important part in motility. The triple radial spokes (RS1, RS2 and RS3) are required to modulate beating of the sperm flagellum.
Subcellular Localization:
Cytoplasm, cytoskeleton, flagellum axoneme.
| 0
|
MESGDSGLAAQGFLGWGADEEVAQELETEEESEGEGEETAAESEEEPDARLSDEDEEGKTKQECIVSDPSFSMVAVQREDSGITWETNSSRSSTPWASGESQTSGICSLEGSALTSPPGSVSFIMDEVKRTRKRTQKSKRGSPSLRRKGSKKRNSLESQDVLTNQEDGPSISESPVLNIENEKSSIGTYDKTRRKKTASNTPPITGAIYKEHKPLVLKPVYIGTVQYKIKMFNSVKEELIPLQFYGTLPKGYVIKEIHYRRGKDSSISLEPDLSNGGSNIVPQRKLAQSPEEDKVRELAPPWRGALSKGSRTSLFSHEEQKKTYADSNLNVPSSTEHAFPSSARNDTADQEENLSLPQMMPQQPADESKTHRMEPPSIPATMVLERAKEELEQNAQGKESSEDDASVLTGSADDVQQEGLVSVNHSMPWEAEKESLETGPPRPAPAIQEKFEPDMEGLEPISTEKTEQASEYVTSSEPIVHREEEHAPEPIVHREEEHAPEPIVHREEEHAPEPESIVHREEEHAPESIVHREEEHAPEPVPIVHREEEHAPEPESIVHREEEHAPEPIVHRDKGHALEPIVHREEEHAPEPIVHRDEGHAPEPIVHREEEHVPEPESIVRKGEEHAPEPIVHREEEQVPEPESIVHREEEHAPEPIVHREEEQVPEPESIVHREEEHAPEPMVLREEHAPEPIVRREEEHAPEPIVHREEEHAPEPMVHRKAQQLERGVETSTPITDITEPEDSSLEEEIIELDYPESPLASKETSPSPLSPEVEHRKEPILPTQMTFTPERITLSEEEREENESVSTDSAFVSEYSVLQDLNHTPEKLEVEAVSVSDVKSSNEPAVFSEDDEERESYSPAMTSVSEQSLSPSTTEKTSAIQSPLFSTVSPVLSGDEASENVCHSPESESAAEYSVPAHAQELLLKTGDHKLPLKSQRVSEPIIQAEDEKEDIGLLPPAALSQAVLSEDESLGSGSFASDSKLPFKPSVSQNATRESPQKTIDDMPQFKPRGLSDPATLLEEEKEAIGVGLSSSNEVSAVECALPPQTTELLSESHAPPPWAISSEQVVQSEEGSRDQQRGSFSSTPELGHTSLLLKGASSPTGLSEQGQEEDNIGPLSPDSAFASEFSFSPYPTQELEKRELGRDSPLCLTSPSEQTVLSEEDTEEADLFSPDSASQVSIPPYRIAETEQNKVEPDELLPTRSAPDYPYFSEADEEEAGSSVVTLVPEHSEPSQEREESSPCRPVFEDLSLPPSADKTGQAETMSDVPTISTSVSEYLILARQAKTQASLEPEAEDLVPPPTSGWEKRDAKSSLPAVTIAASSSALSSVVKEETTSVLPTSQPSVSPESTCVLKPEQEPTAPLTLTSADEQMALPRVGREKAVLDSQEATAHKSQDQTPEPRLPNVPGSGMKYSVLSDLGDEPKADVKLNLAPTVTSELEQRMLSKNEPEVAKPHSPPEETSISGPKVLSAVKTEVKQESKITRELPAASSGRERGAEHSPPVPPALPALTEETGKDTEASSSATTVPVTKLDSNSTKLGRDEVLTDPSLASPVEHPGLKGIGKSELGSGLPLPSMSASEVLRPEPKLPVNSGVEVEREDNEPPPLQVSPTSKPTVPNDKHEEITRSPDSENLVSDDLAPTLLAFRHEMNRQAEETSSPVPGSFLSGEQELIKLPPEPEKHKQLSEVPTAGSELIDSRDRDRSLGIEPVKPIGTEPGPSILEKGPAELQRRGKEQEENRKLPVPASAPLETASFDLPIEQKEPKRTLHEGQAVEVPDESSSSADKPELGVKQLAEKKENLEQPKPFVTTERASVTGSKVKESLISPKDNIWMLEKPDGLVNQHEDRKPGTGQLESSESTDLMSEKLGAASLDTDHTSETRNQETSKAPVSGEKLSQEPRRVQSKAVDDSEEGRKLASGNVEVLTQSKSVPAVKAKATPQPPETPEVTQKPSEKSLVTEQGLPAEKGKKGISSFKSWMSSLLFGSSIPDSKVSDNEDLETRPGPSVEKAVPAIEPKGTVPAEVNIAEKPAVHSLPEVTVKLAEEPKGVSVKSSISQDLKEKLTFLSNEDVLKQPKSNSENYGQKELPGFSEGMGESLATSVGDKHPGIHPCSPMGEKVGMEEAQNMAPLHITESQRRQKPEVSPPSMWNISARKEEPSSDHKETWLSSSDVVDRMPQKPKSAQSAFTRMNSEEPASMILPVESKGSLSDLGEDRLRQEMPKPTSLEHCEEEVERPTEEKDGWETRSFSLAGKRGLAEKQEIMAPLELRENEAVGELQRMPESRPFKLEESKAAERLEQRISPTEKLMEKPSKTLALDRREKEVQEWVFSEGEKQEYPPAAMPVPGASAVSLDKAQPHLLAKPTPVVEKPEHIVTEVYPEIRERKAAETQPHPQEEGKTLVEKTKVSRVESPHGEETDGHSLTQEGNLELEKSGESRVDLKEERRRFVMPELPLGASVAAEDGSVQPRPLSKDAARASDMTDETKHLGTPPTQPSAVEPQTLVLGTSVEHAVKKQETWSDRPTVHTFQTSKDDTEEMLKQSVLISKHHLEAVEDVHRNEPPSSAASNYAQFMLSASEISADGVPPMGGTAQEPEGTSVKDEEFSVTSKPAGLSEDQKSAFSIISEGCEILNIHAPAFIPSVDQEESEQMQDKLQYLEEKASFKSISVHDEKKAAASHKTQKSKLEVPDRKITSLKENKTKETHKTKEEIATDSGMGDFTPIQPTVSGEEDYFEKYTLIDYNLSPGSGKQKSTVEESSEEATKTLTSFPESSAEQALDHEYNLVKLDESFYGPEKDDSKLSHAEMQKSLAIQKPDDRNAPKGISRDVDSRSPGMPLFDVEEGVLSKRQIFPTTPKAVNPELLEEPPALSFFYKDLYEGACGEKNEGETASEGDSVDSETSFPRRHSDTDDGPGMYFEKYILKDDILHDESVTQEDQGQGLEEKPVGEEDSQQLRVAEREIRRKPETSFWEKNLEEQHKVVGREGEPTGHMETLDEAAMQQKAPITEQVRAVTQKMSYAVPFQDTRCVLESEPSSQGNEAGNASPDVNLNVPVQVSFPEEESAAGATYAPEVLQERLVPSVSREERLHNTPVQDEYDFVGSLNQEAASQAILPEEPGSESSPKEVLSQGSESFEHIREQELTSEGEPRMSASQEVWDRTEDQSARESVTAKTQKEPKKTQAESYCYTCKSLVSEMDKALDIHKDHEVSALDTAISAVKVQLGEFLENLQEKSLRIEAFVSEIESFFNTIEEKCSKNEKRLEMQNEEMMKRVLAQYDEKAQSFEEVKKKKMEFLHDQMVHFLQSMDTAKDTLETIVREAEELDETVFLASFEEINERLLSAMESTASLENMPAAFSLFEHYDDSSARSDQMLKQVAVPQPPRLEPQEPSSATSTTIAVYWSVNKEDVVDSFQVYCVEEPQDDQEINELVEEYRLTVKESCCIFEDLEPDRCYQVWVMAVNFTGCSLPSERAIFRTAPSTPVIHVEDCTVCWNTATVRWRPANPEATETYTLEYCRQHSPEGEGLRSFSGIKGHQLKVNLPPNDNYFFYVRATNASGTSEQSEAALISTRGTRFLLLRETAHPALQISANGTVISFSERRRLTEIPSVLGEELPACGQHYWETTVADSPAYRLGICTSSAVRAGALGQGETSWYMHCSEPQRYTFFYSGIVSEVHATERPARVGILLDYTNQRLLFINAESGQLLFIVRHRFNEGVHPAFALEKPGRCTLHLGLEPPDSVRHK
|
[
10293,
18661,
24917,
25353,
25645,
26199,
26465,
28676,
32073,
37495,
39106,
39177,
47128,
47529,
63892,
69826,
76272,
87326,
87367,
87857,
87914,
88008,
88009,
88035
] |
The following text describes a protein:
Function:
May serve as an anchoring protein that mediates the subcellular compartmentation of protein kinase A (PKA) via binding to PRKAR2A. May attenuate calcineurin ability to induce slow-fiber gene program in muscle and may negatively modulate skeletal muscle regeneration. Plays a role in the assembly of ryanodine receptor (RYR2) clusters in striated muscle.
Subcellular Localization:
Nucleus. Cytoplasm. Cytoplasm, perinuclear region. Cytoplasm, myofibril, sarcomere, M line. Sarcoplasmic reticulum. Note=Found predominantly at the periphery of the nucleus but also throughout the cell. Localized in lysosomes. In skeletal muscles, localizes along myofiber periphery, at costameres. Predominantly flanks Z-disks (By similarity). Occasionally present at the M-band level. In the mdx mouse model for Duchenne muscular dystrophy, exhibits a discontinuous localization at the myofiber periphery with extensive regions devoid of CMYA5. This highly irregular pattern is associated with an increased cytoplasmic localization, particularly in discrete foci within myofibers. Colocalized with RYR2 in the sarcoplasmic reticulum (By similarity).
Domain:
Amphipathic helix regions act as an anchoring domain for PKA, and appear to be responsible of the interaction between myospryn and PRKAR2A.
| 0
|
MNILSAIIVFENLHEVKRLFHWGPIIALTVIGVCSSMAILDSIIWYWPLDTTGGSINFIMLINWTVLILYNYFNAMFVGPGYIPLEWKPEKQQDIMYLQFCRLCQGYKAPRSHHCRKCNRCVMKMDHHCPWINNCCGHLNHAYFTSFLLLAPLGCIHAALIFIMTMYTQLYDRISFGWSSVKIDMSAARHIHHPIMPFSIAAFAATLFALGLALGTTIAVGMLFFIQMKVILRNRTSIEAWIEEKAKDRIQYYQTGEDFIFPYDLGSRWENFKQVFTWSGAPMGDGIEWPVHEKCDQYTLTIEQLKQKHDKRQRSVEYRVVEEYNGACCPLGKGLNTFFRTPCTEEPRIKLTKGETIFATRGTKWWMYGDKVLNEEQAKAGVRIRGWFPRRCVEKCLYDSANNSTSEEKKEQ
|
[
2459,
2570,
8290,
25008,
25014,
25018,
30754,
35392,
37269,
87125,
87432,
87735,
87760,
87882,
88008,
88031,
88153,
88159,
88161
] |
The following text describes a protein:
Function:
Endoplasmic reticulum palmitoyl acyltransferase that probably catalyzes the addition of palmitate onto various protein substrates and is involved in a variety of cellular processes (By similarity). Could also function as a stearoyltransferase (By similarity).
Subcellular Localization:
Endoplasmic reticulum membrane; Multi-pass membrane protein.
Domain:
The DHHC domain is required for palmitoyltransferase activity; The C-terminal di-lysine motif confers endoplasmic reticulum localization.
| 0
|
MSRENNCTTADLAWGIPSITQAWGLWALFGVVTMLLLISLAALLSQWTRGRRRTQEEQGPPSGRSVEEVPLYGNLHYLQTGRLSEESRSEEQDPSSGGLARGAEEATCYTSLQLRPAQGRIPSSGTPIKYCEVVLDSEPKPQASGPEPELYASVCAQTRRARASFPDQAYANSQPAPS
|
[
7262,
8663,
14453,
16534,
25079,
30810,
61701,
87126,
87276,
87413,
87522,
87616,
87760,
87914,
88008,
88061,
88159,
88161
] |
The following text describes a protein:
Function:
Negatively regulates T-cell antigen receptor (TCR)-mediated signaling. Involved in positive selection of T-cells.
Subcellular Localization:
Cell membrane; Single-pass type III membrane protein.
| 0
|
MSPLPLRDPSHQANAGPRLVEPSCGPGVSLSNRTLCHPSWPMYDNWGRSPTTSERPEEEQVVSKDTGVPVRNYEDVFLLDPLLPCGQRVPLILTKPPQQAMDSRKLLLPPPIMSPSVHPSSSQACSSTWLSEAEMIALAGLLQMSQGEQTPNCVASSLPSTSCPDPVSVSEDPGPSGDQSCSGTDT
|
[
15387,
24917,
24978,
59323,
87103,
87367,
87857,
88008,
88010,
88148,
88150
] |
The following text describes a protein:
Function:
Involved in the transcriptional repression mediated by the mSIN3A but not the N-CoR corepressor complex.
Subcellular Localization:
Nucleus. Cytoplasm. Note=Shuttles between the nucleus and the cytoplasm.
| 0
|
MKIGSGEKLLFIGDSITDCGRARPEGEGSFGALGTGYVAYVVGLLQAVYPELGIRVVNKGISGNTVRDLKARWEEDVIAQKPDWVSIMIGINDVWRQYDLPFMKEKHVYLDEYEATLRSLVLETKPLVKGIILMTPFYIEGNEQDPMRRTMDQYGRVVKQIAEETNSLFVDTQAAFNEVLKTLYPAALAWDRVHPSVAGHMILARAFLREIGFEWVRSR
|
[
3987,
15166,
24978,
28482,
32497,
47565,
64260,
77185,
87103,
87258,
87367,
87601,
87937,
88048
] |
The following text describes a protein:
Function:
Acetylxylan esterase involved in the degradation of xylan, a major structural heterogeneous polysaccharide found in plant biomass representing the second most abundant polysaccharide in the biosphere, after cellulose. Cleaves acetyl side groups from the xylose backbone units of the hemicellulolytic polymer xylan and xylo-oligosaccharides. Hydrolyzes about 20%-30% of the available acetyl groups on fully acetylated birch wood xylan. Completely deacetylates xylobiose peracetate (fully acetylated), and is active on both the alpha- and beta-forms of the sugar. Also hydrolyzes fully acetylated methyl-beta-D-xylopyranoside and methyl-beta-D-glucopyranoside, and the synthetic substrates 2-naphthyl acetate, 4-nitrophenyl acetate, 4-methylumbelliferyl acetate, and phenyl acetate.
Subcellular Localization:
Cytoplasm.
| 0
|
MINQRLFEIDEWKIKTNTFNKEHTRLLESLTSLANGYMGVRGNFEEGYSGDSHQGTYIAGVWFPDKTRVGWWKNGYPEYFGKVINAMNFMGIGLYVDGEKIDLHQNPIELFEVELNMKEGILRRSAVVRIQDKTVRIRSERFLSLAVKELCAIHYEAECLTGDAVITLVPYLDGNVANEDSNYQEQFWQEEAKGADSHSGHLAAKTIENPFGTPRFTVLAAMANETEGFVHESFKTTEMYVENRYSYQTKASLKKFVIVTTSRDFREEELLSKAKELLADVVENGYEDAKRRHTDRWKERWAKADIEIKGDEELQQGIRYNIFQLFSTYYGGDARLNIGPKGFTGEKYGGAAYWDTEAYAVPMYLATAEPEVTKNLLLYRYHQLEAAKRNAAKLGMKGALYPMVTFTGDECHNEWEITFEEIHRNGAICYAIYNYINYTGDRNYMEEYGIDVLVAVSRFWADRVHFSKRKNKYMIHGVTGPNEYENNVNNNWYTNVIAAWTLEYTLQSLESISAEKRRHLDVQEVELEVWREIIQHMYYPFSEELQIFVQHDTFLDKDLQTVDELDPAERPLYQNWSWDKILRSNFIKQADVLQGIYLFNDRFTMEEKRRNFEFYEPMTVHESSLSPSVHAILAAELKLEKKALELYKRTARLDLDNYNHDTEEGLHITSMTGSWLAIVHGFAGMRTANETLSFAPFLPKEWDEYSFNINYRNRLINVTVDEKRVIFELVKGEPLHMNVYEEPVVLQGRCERRTPNE
|
[
3052,
6647,
7854,
28423,
30908,
33300,
40287,
40288,
40289,
43533,
45294,
46278,
49976,
64735,
87258,
87525,
88008,
88153
] |
The following text describes a protein:
Function:
Catalyzes the phosphorolysis of maltose, leading to the formation of glucose and glucose 1-P.
| 0
|
MYGIFASFRRGSQLENITLHARDLSSKISPSIARILKDAKRTNNGRKHPKISTLQLARTKRKFIQQGKEWPQEPLPPLNLKPYRKGHKWEEAKAARKVTIAENMAKMPQMIAEYREQVRERREKYRNRKDAAKKDPNQPEYVQYLLAKGVRLADIAVKLGTQNKKAKI
|
[
24917,
24979,
25047,
27616,
51151,
68002,
69741,
87272,
87326,
87785,
87857,
88008,
88020,
88022
] |
The following text describes a protein:
Function:
Acts as a negative regulator of G1 to S cell cycle phase progression by inhibiting cyclin-dependent kinases. Inhibitory effects are additive with GADD45 proteins but also occur in the absence of GADD45 proteins. Acts as a repressor of the orphan nuclear receptor NR4A1 by inhibiting AB domain-mediated transcriptional activity. May be involved in the hormone-mediated regulation of NR4A1 transcriptional activity. May play a role in mitochondrial protein synthesis.
Subcellular Localization:
Mitochondrion. Nucleus.
| 0
|
MIDLFAIVNKGGIVLWKKTNSLVNLKCLQVLFHEAFLSEQRTVNNTVTFDRYTMQYQEATQYSIVFVVVFQDLKCMAYSQSLLNSAHNIFLNLFKEKLEDRQVPNEAEVEKLFAPIFNRKSAQLENETDTKSLPVEANNDNSARKKNEYEMKKKGAQSKQTNAPKKGKKQLRKWDDQITEEEQAALNYSSQASSASQTVDNSQLSSIVGNNNKFQKTGSGDVIISDLEMDPNQTISNKSASSAFSLFSNLIGGKYLKEEDLSPILKQMQEHLTKKNVANSIALELCESVKASLINKKVGSFDTVKNTVNKAFRDRLTQILTPSTSLDLLHSIRSVRKNENRPYTISLIGVNGVGKSTTLAKIAYWLLSNNFRILVAACDTFRSGAIEQLGVHVKNLQSLKGSSIELFAQGYGKDSSFVVKNAVEYAKQNSFDVILIDTAGRRHNDQRLMGSLEKFTKATKLDKIFQVAEALVGTDSLAQAKHFQASLYHRPLDGFIISKVDTVGQLVGVMVGMVYAVRVPIIFVGIGQTYSDLRTLSVDWVVDQLMK
|
[
8292,
8490,
15025,
24917,
25010,
25014,
25040,
28025,
28801,
29034,
30398,
36688,
38873,
42078,
45293,
47559,
58239,
63994,
69095,
87432,
87491,
87760,
87855,
88006,
88008
] |
The following text describes a protein:
Function:
Component of the SRP (signal recognition particle) receptor (SR). Ensures, in conjunction with the signal recognition particle, the correct targeting of the nascent secretory proteins to the endoplasmic reticulum membrane system. GTP hydrolysis may enhance the fidelity of and provide unidirectionality to the targeting reaction (By similarity).
Subcellular Localization:
Endoplasmic reticulum membrane; Peripheral membrane protein; Cytoplasmic side. Note=Thought to be anchored in the membrane through an interaction with SR-beta, which contains a bona fide transmembrane domain.
Domain:
The NG domain, also named G domain, is a special guanosine triphosphatase (GTPase) domain, which forms a guanosine 5'-triphosphate (GTP)-dependent complex with a homologous NG domain in the signal recognition particle (SRP) complex subunit SRP54 (By similarity). The two NG domains undergo cooperative rearrangements upon their assembly, which culminate in the reciprocal activation of the GTPase activity of one another (By similarity). GTPase induced rearrangement of SR drives SRP-mediated cotranslational protein translocation into the ER (By similarity).
| 0
|
MNTRQLLSVGIDIGTTTTQVIFSRLELVNRAAVSQVPRYEFIKREISWQSPVFFTPVDKQGGLKEAELKTLILEQYHAAGIEPESVDSGAIIITGESAKTRNARPAVMALSQSLGDFVVASAGPHLESVIAGHGAGAQTLSEQRLCRVLNIDIGGGTANYALFDAGKISGTACLNVGGRLLETDSHGRVVYAHKPGQMIVDECFGAGTDARSLTGAQLVQVTRRMAELIVEVIDGTLSPLAQALMQTGLLPAGVTPEIITLSGGVGECYRHQPADPFCFADIGPLLATALHDHPRLREMNVQFPAQTVRATVIGAGAHTLSLSGSTIWLEGVQLPLRNLPVAIPIDETDLVGAWQQALIQLDLDPKTDAYVLALPASLPVRYAAVLTVINALVDFVARFPNPHPLLVVAGQDFGKALGMLLRPQLQQLPLAVIDEVIVRAGDYIDIGTPLFGGSVVPVTVKSLAFPS
|
[
11607,
15621,
25655,
43883,
69819,
76351,
87203,
87285,
87411,
88008
] |
The following text describes a protein:
Function:
Reactivates suicidally inhibited ethanolamine ammonia-lyase (EAL), cyanocobalamin-inactivated EAL and O(2)-inactivated EAL; requires Mg(2+), ATP and adenosylcobalamin. Reactivation probably occurs by the ATP-dependent exchange of cobalamin.
Subcellular Localization:
Bacterial microcompartment.
| 0
|
MKDSAILNQLKVVLPPHIMEIIYFRYNQIDTYLKPYNLPIKTDVLLLALFTLIFIIIISKLFGSSGNKTRSVGGRTSNDKKVKRGVNIAILGLSNAGKTALLLNLTNVDKKISTHTSITTNNGVYITENKKKLPIIDVPGNGKAKASLPKILSNSACIIYVIDGTTFIDNSTQEAQYLYDILTNESVYQKKIPVLVFNNKMDLDSTIDTEQVKNILERELDDLRRTRGATPIVLGQEEDKKDIYLGIEGTPFQFDHLPNDVQFSNGSASPSNGELKEIDDIKNFIQTTTL
|
[
15025,
25010,
29034,
40315,
51630,
55834,
58239,
87432,
87491,
87760,
87855,
88006,
88008,
88159,
88161
] |
The following text describes a protein:
Function:
Component of the signal recognition particle (SRP) complex receptor (SR) (By similarity). Ensures, in conjunction with the SRP complex, the correct targeting of the nascent secretory proteins to the endoplasmic reticulum membrane system (By similarity). May mediate the membrane association of SR (By similarity).
Subcellular Localization:
Endoplasmic reticulum membrane; Single-pass membrane protein.
| 0
|
METTARVHQPKAGSSSSRHRSSRARRSATPQRLEQLEQSEARGIDDVSSQQSPDQEMAMADGTSKNRTTAPSRTVRRPDTPEHSGASSTTTNASGSVTGMTVPDSGALSRVSQTPRSNSPAIVTTELVAEQAPPVASEEPAAGPPADKLQKGILGYMDRQLKVQSLSDSQKSPAQRSTRSSTRSSNLDKSPRRKRSKSESRRRRERKILAAGEMEVRQANETLMRYLKQCSDFNDASLSGDLEIPEPLEDRRVHRKTKSQRERKQHQPQQPDHRSGGRTHADDLMSYHGEIYNPFTPVVSPTTEAAATRIDKMYIQTASGYRPVDNTYSYHKSRALIGGDPESNSHTISTSVHLSCAVQRVWHLLSTVCHGLLGGLAFAHLLLICTTKPYDWVDASIHHYSAFAEVYANTFYCLAIVCMVSIFDRMDIAYGGDTNISFRSIFIIMIYVMTIILSLSAGTMDERLYVTASLNVTVWEEELETNKVLSVWNALSIARSVGAIFGWLIVGFLPNQDNLYDQLLEMEKYQLQ
|
[
17404,
25325,
26048,
59561,
87278,
87311,
87312,
87760,
88008,
88159,
88161
] |
The following text describes a protein:
Function:
Component of the transition zone in primary cilia. Required for ciliogenesis.
Subcellular Localization:
Cell projection, cilium. Membrane; Multi-pass membrane protein.
| 0
|
MESDPPPTSPSRAQPGRSQLNATSSAAGNEDPQRQGPTPGDHATPPPGRAEPEKNETVKDVTELSLEELLEKAKAGDPKAQTEAGKYYLKLAEDADEELNNSNAIDWLILAAKQGRREAVKLLRRCLADRRGITTENEQEVKKLSSETDLERAVRKAALVMYWKLNPKKKKQVAVSELLENVGQVNEQDGEKQPGPIPKSIQKQRRMLERLVSSEAKSYFALDDFVEITKKYAKGIIPSQLFVQDDDDDELAGKTPEDLPLRLKVVKFPLHAIMEIKEYLIEMASKAGMHWLSTIVPTHHINALLFFFVISNLTVEFFAFFIPLVIFYLSFVSMVICTLKVFQDSKAWENFRTLTDLLLRFEPNLDVEQAEVNFGWNHLEPYVYFLLSVAFVIFSFPVASKECIPCSELAVVSLFFTATSYMSLSTCAEPFTRRALLTEVAAGALSLLPHVPLSLGPLALLGQTFWTVPVGSLVVLNVSVPCLLFVYLFYLLFRMARLRNFQGTYCYLVPYLVCFMWCELSVVILRESSGLGLVRATVGYFLFLFALPVLAVGLALMGAVQLAKWFASLELAKMVATAGLCAVPLLARRWTRASLSPAGVVRSLSRSSVVKLILVWLTAVVAFCWFYVYRSEGMKVYNSTLSWQQYGFLCGPRAWKETNMARTQILCSHLEGHRVTWTGRFKYVRVTDIDNSAEAAINVLPFFLGDWLRCLYGEPYPACDPARDPAHNPAPREEDLCRLKALAKHRCHMKRFDRYKFEITVGMPYGAAGKTPEEDDITKDVVLRASHEFKDVLLHLRQGSVIEFSTILEGRLGSKWPVFELKAIGCLNCMAKLIPSGRHVKIEHDWRSTVHTALKFAFDFFFFPFLAVA
|
[
6673,
7018,
7641,
8554,
8966,
8970,
10779,
11875,
12027,
12340,
13808,
14280,
14681,
15414,
16511,
17053,
17185,
21982,
22746,
22949,
24412,
25014,
25473,
25480,
31139,
33735,
35433,
46079,
57555,
57556,
71602,
71651,
71653,
71654,
87115,
87369,
87432,
87522,
87760,
87914,
88008,
88159,
88161
] |
The following text describes a protein:
Function:
Participates in the regulation of cellular Ca(2+) homeostasis, at least partly, by modulating the filling state of the endoplasmic reticulum Ca(2+) store. Negatively regulates the ER stress response and positively regulates the stability of V-ATPase subunits ATP6V1A and ATP1B1 by preventing their degradation through an unknown proteasome-independent mechanism.
Subcellular Localization:
Cytoplasmic vesicle, secretory vesicle. Endoplasmic reticulum membrane; Multi-pass membrane protein.
| 0
|
MTDLNSESFSALNFWKSVEKKNISTNFQGTKVVAPSKKINSFPLLAPPAPPPPPTEQEINIGSGNSTFISSNNNNSNNNNNNNSNNNNNNNLNNSNNNNNNLNSNNNNNNNNNNNNNNGNNNNNSNFLTRQDSSTQKEWDEQNVTEAFGFWKQKAVQLQKETERYNARRNARQTIDLTNILRKSTSSDLLIKPPVESPPLTPVGQDDEGEQQQQQQQQKQSSPSTPSNDTDTETTAAAVTTTTTTTTTTTTSTTTTTTETVLQANQLEIKYGGETIAVVDDSGTTPRDYRRSRSISCEIIPKINGVITTSPQRVTTTTTTTTPSTGGVVVADEESDSSEEESDSSEEESDEYTDEESETELQVVSNATPRRSDDFTPTIVESPPLTSVNSNDNTSSGTVVAPIDLNSSTGGNTGSQQPPQPSSQQQKPDQASENTAVAASSISATTNVTSAASTTTVAPDSIINTKDVTVVSSTLTTTTSATSSTTSATTQSIPAPPSPSQQRAAQSISTSSVTPAAITKPTKDAKDKKDPAKKSIGATLTRTVTKTFIRDSKENNKVPTGTSPPVSSSTSISSSTGIKKDKVKLSKEEKDRIKKEKSAKKKKEKDEKKQQKTNKKALTKNNSSTDVKKGFVSPQQQQILDSPYRIYGVRLTQLVLSNDGDLPAILTQTITVLSNSNKLDVNSVFVGAENEPAVREIRKRSDLERIDFSIIGDPRVVAGLLILFFAELPQPLFNSKFFGDLVEINDITNPQVKLNDLKQLINSLSQLRRSLLQILVTFFTSKYINGNSVTTRAIAIQSIAQSFGPQFFRGTSSSDSDIQVGIETLKLIIDNYVFLFEKTNEPDVKYKNIDGKMIISEGSIDKLIDKATDQYYPYNEKYFSLTFFITHLFFIQPHELADKLITLYRENLDTLETKKKWKKHRRSKKASFINEAVKLWVDYCYKEMREDKELSKKILKGFPHLEAQLASRLSHRTTINDFLKLPKRVHSRTRSASFSDTLLSTGGIGSTSGGIGGGVNNCLLSAMEIAEQCTLVDYDLFTNVRLSDWVRLVQGSVDPQTAPSLSLALKRSTIWAQWAMGEILSTEDKSQRVAIINLLVDVAINCKDLANFNTAISIHTALTNHHIKRLQQTWDSVPKETLNKITQLEQSLQVWLKPDATNPFGVICQSINSACVPNFSILRTILSQIDQKIPTFSNDGSMVNVEKLRTIFGIVVEIQRLQQQRNYTMKPTKLFIQLQDINTVSMDELADLSLKCEPPVSKAKKYNAPADIVDEDWRLKITKTFNKPLATTSVGIDLPRLASSFTFNTTGHKTTPEEKSAYGNKIQDIFHVLVSLAQIESSELETDVREKFTTYIPMSTDPDSDFKRELLKFLDEVCHADNSKLVRVLKCCNQAIIAPVIIEITLNIAKGVPFMDAGGWRILISNINNSNNSVILDKIDEINEDSSNVEKEKLSSSQEQQEQQEQKQQEQQQQQQEPQPLFIRHYKKQRSRSAQSKDFFEFEWFIQLNLDADCKNILSFDLKISNLVFSTDTSPNIRDQLLESFKSYLVSQECVQYINFNENKQPVAAPVTPATTIVTTKEESTTVTSSTTTVVQESVPSTNAE
|
[
8522,
11826,
12353,
15732,
17297,
17957,
23541,
24978,
25114,
25444,
25482,
25608,
26653,
27370,
27873,
28810,
29319,
31103,
33717,
36104,
36477,
37516,
43538,
55346,
64687,
87118,
87278,
87287,
87367,
87371,
87535,
87914
] |
The following text describes a protein:
Function:
GpaB-activated, rapA-specific guanine nucleotide exchange factor, involved in the regulation of the balance between Ras and Rap signaling at the leading edge of chemotaxing cells. Spatially localized activation of Rap and Ras induces F-actin polymerization at the leading edge of chemotaxing cells through the Rac, PI3K, and TORC2 pathways. Also acts as a key regulator of actin-driven membrane protrusions during processes such as phagocytosis and cytokinesis, possibly by modulating rapA signaling pathways.
Subcellular Localization:
Cytoplasm, cell cortex. Cytoplasm, cytoskeleton. Cell projection, filopodium. Cell projection, lamellipodium. Note=During chemotaxis, localizes at the leading edge of cells, whereas in response to cAMP stimulation, rapidly and transiently translocates to the cortex. Localizes to F-actin-rich regions. During macropinocytosis, strongly localizes to crowns and remains there for a short time after the cups were enclosed. During phagocytosis of heat-killed yeast, strongly localizes to phagocytic cups with F-actin. During cytokinesis, mainly colocalizes with F-actin at filopodia or lamellipodia of daughter cells.
Domain:
The N-terminus (residues 1262 to 1601) functions to regulate both GflB-GEF activity and its localization at the leading edge of cells by binding F-actin directly.
| 0
|
MSFLCGSASTSNKPIERKIVILGDGACGKTSLLNVFTRGYFPEVYEPTVFENYIHDIFVDSKHITLSLWDTAGQEEFDRLRSLSYSDTQCIMLCFSIDSRDSLENVQNKWVGEITDHCEGVKLVLVALKCDLRNNENESNAITPNNIQQDNSVSNDNGNNINSTSNGKNLISYEEGLAMAKKIGALRYLECSAKLNKGVNEAFTEAARVALTAGPVATEVKSDSGSSCTIM
|
[
8572,
8663,
8725,
11869,
12568,
15408,
19886,
25040,
25079,
25110,
28025,
29034,
30811,
37443,
38866,
40315,
58239,
87276,
87491,
87735,
87760,
87776,
87855,
87951,
88008
] |
The following text describes a protein:
Function:
Plays an important role in cell growth. Required to keep the uninucleated state. Modulates morphogenesis during bud growth via directing organization of the actin cytoskeleton and the position of the secretory machinery for exocytosis.
Miscellaneous:
MISCELLANEOUS: Present with 5910 molecules/cell in log phase SD medium.
Subcellular Localization:
Cell membrane; Lipid-anchor; Cytoplasmic side.
| 0
|
MRKSLITLGLASVIGTSSFLIPFTSKTASAETLDEKKQKIESKQSEVASSIEAKEKELTELQENQSKIEKELKDINDKALDTSNKIEDKKEENDKTKEEIKKLKKEIKETEARIEKRNEILKKRVRSLQESGGSQGYIDVLLGSTSFGDFISRATAVSSIVDADKDLIKQQEQDKAKLEDSEADLNDKLKEVQAALAKLETMQKDLDKQLNEKDKLFDEAKASQKKTAKAISELKSEASELANQKANTEAEQARIKKEQEAAAALIKKQEEAQKASDETQTDDSQTATTESSKASSSDDSSDNSSDNSSNGSSNSSSNGSSSKKSSGSNSNSGGTVISNSGGIEGAISVGSSIVGQSPYKFGGGRTQSDINNRIFDCSSFVRWAYASAGVNLGPVGGTTTDTLVGRGQAVSASEMKRGDLVFFDTYKTNGHVGIYLGNGTFLNDNTSHGVSVDSMSNPYWKAAFKGVVRRVVQ
|
[
4484,
6692,
8200,
18986,
24878,
28216,
29145,
36001,
66234,
76856,
87103,
87280,
87281,
87601,
87965,
88008,
88038,
88058,
88134
] |
The following text describes a protein:
Function:
The C-terminal part of CwlO shows a cell wall hydrolytic DL-endopeptidase activity.
Miscellaneous:
MISCELLANEOUS: The N-terminal part of CwlO was shown to have no cell wall-binding activity.
Subcellular Localization:
Secreted. Secreted, cell wall.
| 0
|
MSLLHEKQVRVLKLFERLSVAASGEKIPADQIDARLSTVGELPNSAFFSCFLPAHLEEAKRLIEIFYSAKDFDDFVLLAEQARTFVNSTLFAFAAEVAILHRADSRGIIVPPIQEIFADRFVPADTLIRAFSVATTKPAGDESDVIIDVQETGNILDPEYKLAYYREDIGVNAHHWHWHVVYPSVYDSKFFGKKKDRTGELFYYMHQQMCARYDCERLSNGLTRMVPFHNFEEPLEGYAAHLTHIASGRHYAPRPDGLAMTDLRLVDVQDMQRWTERILEAIHLGKVIDSEGNDIILDEETGADILGSLIESNLESKNRQFYGNLHNWGHVMMAYIHDPDGRFRETPGVMTDTATSLRDPIFYRFHRFIDNVFQEYKKTLPVYSRDNLTFPDIEITESKVNAKITNVIHTFIREDELELTHCMNFGSPGSVKARYHHLDHESFSYIFNANNNGSEEKKGTVRIFLAPKYDELGNVIPLDEQRRLYIEMDKFDTDLRPGKNIIVRSSTDSTVTISSTYTFKELLHGEDLEEDRSEFCSCGWPQHLLVPKGSNKGMVFDLFVMITDAEKDKVPTSGKKLCNDALSYCGVMDEKYPDKRAMGYPFDRTITAQSHEEFITPNMKISNITVRFQD
|
[
24878,
28962,
29024,
30200,
31111,
36687,
37787,
40296,
40297,
43528,
47534,
48276,
64437,
64737,
87346,
87413,
87522,
87767,
87874,
88038,
88162
] |
The following text describes a protein:
Function:
Hemocyanins are copper-containing oxygen carriers occurring freely dissolved in the hemolymph of many mollusks and arthropods.
Subcellular Localization:
Secreted, extracellular space.
| 0
|
MGDSANTASVRFPLSADAAAEALAVAGQQRGAAHLLSNEDDVDEDDVYEESEERYNSDDDAHGGERSLPAKTAEAAASVFMKGTPRSFGPVAGAGGDLGSGAEAKGAGGSAAASLNAQRSALIAANLSRQLFKAKMPDIAASTKYQDELEEEDLDQLSAVDRDFVMNTKDLFDDVDAELLGEDFVPHEHVVGIIASEATGGEASPDEIDDNLVDYKDLEAEINADLADYIDAHHQEFNNAICDFSEMVLAVSGSDDTLAEFKKELADAIVSLESHAGELKVLRLRAAKSLFMADALEHIQEVVLAEAEVKGLLQNRHYLAAVQTLQAQARLLAGDELKGVRAVQSLRDTHNATISTLHHLIIDDLLACVFRHERLVEADAQLLQEMLDSSERDTKDTHAAAPSVQHTIYKYWKMAGVGAPGSGHPDDDEDDAGEVDRDDGLVAATHNGTTAGSTKTAGVGGLARKDRTLSAIIETLTDDPRDDQVLGNYLKFVPLCVKSLMLLGKIDHCHETFFSRATRSMERFIAHFLCLYDAWRRRTRSGASLSNDEVEAAIRGTHVRALDLACDLISFDEAVATIQARDLRAMLGALFTELEKILRNAAYLQKVVLVAHFPFVSPYVVQPDPFVPEATSRQWNVMNAPLRNEMWLHDTLTTALDHAQNSMRNAPAQSDKSSSSRSLPAAGGDSNVGDVIAKFLELFNTDAVLASLKAETEEKDVAAAAAAAATTTPVNLKTSGGVALNTDAAANDVSLFLAFDRRKPCLTLQNILDRVNSACAQTRAIFPAAEAVLRKLQLAVSAELRDAVRVKLVAEVQTLLQEWDLQALWSQLNYHIECVFHVICDAKESQDETDDAVTLLPFLRQKNLISRVQRTATIMLDADKQGDDTTTLDRLLSTYASGGLLRMVEETGTVSFSLVGAVKKAQADMRKAREGQASQFDVMQCDKAKLIAFTDSGLGGGGVGGAGAPLVLLHASMLRRWFVFTAMNALTCYECAARFYSRSCDRVPEFRLLSEEECVVGFFKRFLRATYIPTLHAFHSQQLQLLLMSIGDSGGTSAAGATPSASPLPEDAGSTTSRGGKAPTAMKALSGAWPTVVVDEVQHPILACVQYVGQVLAKVSDVRRILPESLTEEVEQNTSEALIIELVVFLKRQVQWLGRGTLAHRLLDKPFEDAFSGMPNRRWAALADEENILDAHRYIDQDLYRYYQLNSDERTSGHEYNRSTVSVLEAMRVLETSSAASPGDGGGAGAAEAELDQHIGRMEPRDICVRDDSTLVAFALLCTSAEWLCDVLLRYLWPRRRRARNYTDCCVPGYCFAHEMRVSDAASFVLVDGDYTMQRKIRLSGHLVRLCSLAQVALFHLSVEARFLAFLFLPQLRDVSYDVVAVSSAADMFVQAYARRVHNFYAILRQHLHAKKIKYTCLTAGKPASELILMELAHLRDKAISQAGLMRLRTDLLVMQTTLQLVLPADSDVREAVSRFFLRPVLFLRHIFNKDVVNEIVSSLDYLNFSTKEVEVLIRLVFRQVSGSNDDTLAVQQIRFFYQKLKTIRNLRCAGNRTGGGSSVVSEPSLLPDGRGSSADAIGGGGLPSFVPLSTNAAAVAAAALDDGDDYHSGAFSYDDGGSDASDLQPPPLPLSSATRGCQSAAGGLAASPSMSAPPESVPAPTSASAAAAPVSARLTTSSEEDEEDDEGEEDEETPEASTTLRPDRQPQQRPIPRGADRTRSSISAVAPAGAEATALGSRPTRRVDPTSLPDTPCLPSSKSATAAKPALARPVVPPLAMAPFRGAPSKAPAPAAKAGAVKVEASSEEDEDDEEYEYEEETSEYEEEEEEEEEVEEEEEEEEEVEAAPVQASTDKRPPHPRPHPAGSPTNGTAAAIRRPSASSAFAPK
|
[
8290,
8491,
8496,
8504,
10368,
19972,
24727,
24978,
42048,
66989,
87448,
87974,
88008,
88162
] |
The following text describes a protein:
Function:
Component of the exocyst complex involved in the docking of exocytic vesicles with fusion sites on the plasma membrane.
| 0
|
MALRFSVLRLASYLGRKKDLYQILEVESSATHDEIKRAFVRLTARLHPDTRGVDKESERLQWSNRSLTEQFMEVKEAYDILRKPEKRKEYDEERRLAQGLDGHLVEATSARFEKNTVINLQRDRNEMYTGPGKKRDDSASGHFRNPEEEYEKERQKNRSLYLIGALFLSIVLTNIGYVHYLRSSDNRKVL
|
[
13808,
25008,
25325,
33731,
33820,
37291,
64599,
77600,
87285,
87760,
88008,
88159,
88161
] |
The following text describes a protein:
Function:
Co-chaperone for Hsp70 protein HSPA5/BiP that acts as a key repressor of the ERN1/IRE1-mediated unfolded protein response (UPR). J domain-containing co-chaperones stimulate the ATPase activity of Hsp70 proteins and are required for efficient substrate recognition by Hsp70 proteins. In the unstressed endoplasmic reticulum, interacts with the luminal region of ERN1/IRE1 and selectively recruits HSPA5/BiP: HSPA5/BiP disrupts the dimerization of the active ERN1/IRE1 luminal region, thereby inactivating ERN1/IRE1. Also involved in endoplasmic reticulum-associated degradation (ERAD) of misfolded proteins. Required for survival of B-cell progenitors and normal antibody production.
| 0
|
MFTYVSKFFTNPDRNREDILESLDRENSFLDQKLMEEKMDQQLKANPNEINGVLSNKIAELTHGLSEMDVSKESSCTARKGVITSLDGDRGVIDKDVLFETKVAEDIILDLHVGCVVEYLTFTTGEAMRVVKVKSILEHSWEDTSQKEIEKAVDNLKNEKPTFFNTETRSVLGLISQRLASSIDVETEYGQLTVELDNIEMNFIPTNGDRVRLECNIQLDDGFVDKQGEILEVTKLFPTRIQEGEKCIVERVYVHMVVLGPETYILKTDLPTGTDLHLGDIVLADLIECQYSKFTRRAIKITPLEKNFGATKLTQQSSMGSSGSGKAVTVTGVNRFITAELWQKESVSLKLTNNLNRTLRLESITVCNDSESQLSVVSPLESKEISSGSEITVTFEIHTQFLGEAIEKYVLNFDLLKVRRVFTVIVCKTKEEVAEAEKRMIAAEALMAPGRNSQERSRFYANQVWCNKVDVIPGQQIVTKRRFVALRLGCFEVPKELRQICLTSERRQEMIKAIEQHYSFLTEPLSIKTYMHRFRLLLHLEEIECFVNFRNYDRDRAHFLRDGEFLTLQIENLAERRPSLVIGDTLRVINPWSDPDSQTTKSYEGIIHKVLFDRILLKFHSSFQEKYNGEDYRLEFYFSRYSFRKQHHAISKIVGVMGEDFLFPSKVTKRENPQLDVYMKDDDMYLYDSKLEWYNQSLNSIQKRAVFNILRGEAENIPYVLFGPPGSGKTMTLIETLLQLVRNLPGARILVGTPSNSSADLVTKRLIDSKALLQGDFIRLVSYNQVEKDLIPPEIMSYCATSDVGAVGSCEDKMMVTESGLKLRCQAKFIGTHRITISTCTTLGNFLQLGFPAGHFTHVLFDEAGQCTEPETMVPIVMLTKKRSQVVLSGDPRQLQSIVTSRIASKMGFSISFLERLLERSPYRKDLQRFPESSGYNPLVLTKLLYNYRALPSIMSIYSRLFYDDELIPVLSEKDSRESRLLSKLRCVFESEKDIPQAHGTFFYGIIGENRQNNDSPSWFNPQEVREVFLMTIALYRANVTADQIGIITPYQKQVKMLRSMFIGTDVVMPKIGSVEEFQGQERDIILISTVRSSEEILRMDARFSLGFVRCSKRLNVAVSRARAMMIIFGNPHLLAVDECWRQLILFCVKNNAYFGCDLPQMVINQKDEVPVCLETFVPSLNTTDDLN
|
[
5174,
6682,
6779,
8752,
8776,
8978,
11891,
13236,
15859,
16123,
18675,
21043,
21052,
23982,
24978,
25040,
25494,
25495,
25625,
25776,
26197,
26207,
26663,
27925,
27926,
29033,
30398,
31341,
31706,
58239,
68695,
68697,
73159,
74878,
74879,
87110,
87367,
87402,
87539,
87601,
87855,
88004,
88008
] |
The following text describes a protein:
Function:
Probable RNA helicase required for axial polarization of the oocyte during early and mid oogenesis. Plays a central role in RNA interference (RNAi) process, a process that mediates mRNA destruction of translational repression. Required for the assembly of the RISC complex, a complex required for target RNA destruction or repression. May be required in the RISC assembly to unwind miRNAs, in the production of single-stranded miRNA from the double-stranded miRNA, a key step in RISC formation. Required both for the translational control of oskar (osk) mRNA and cytoskeletal polarization in the oocyte. Required for somatic primary piRNA biogenesis. Involved in repression of long interspersed nuclear elements (LINEs) including HeT-A, I-element and TART LINEs.
Subcellular Localization:
Cytoplasm. Note=Component of Yb bodies, an electron dense structure containing Yb protein found in somatic cells of ovary and testis.
| 0
|
MAFPRSSSISFFTFLLFSVLINTAISSRVSSFIKLPTSVDESVSSSLESYCASWRLAVETDNAGKWKVVPSQCVSSLETYYDKGQFDKDYSVVAGYAYAYAKTITLKGDGKDAWVFDIDETLLSNLEYYKAHGYGSEPYNSLAFNEWVLQGTAPGFAASLKLFNRLKKLGFALILLTGRDEVQRSVTEQNLLDAGYSGWEYLLLRGHQDQGKAAAQYKSEQRSRMVKEGYRLHGNTGDQWSDLQGFSVADRSFKVPNPMYYIA
|
[
28075,
32459,
40575,
44447,
48075,
55054,
64168,
87522,
88008,
88058,
88084
] |
The following text describes a protein:
Function:
May function as somatic storage protein during early seedling development.
| 0
|
MAFLYENEGTTRTLLHQVLEMHPLSSPISTNNRSRSCTESLFASSDTTLRKRKKTAPVQPKDTGGTDQHFVEHYDLLEKGTPRILLKKILQTASEDSVLVPVLMNSQEPVPVELQEESKWNSLELQLPEPEPSASLAPELLIHSRRKRCLRVSEFEQEVDQGLAVSSDLTGEKRASANKSSMSRSFNLTLATVIPPESVERPGLARRPQIRKKVDMEAFEHGLKDIPLTLLSDRCSNHSTTPVDGARSFQSSPYSLRFRKSLTKDQQPRATTYQANQRKKGPRRAIKSWPKSPLQNQPPSANSMSIRRQARPWTGRPSQNSYLSAYSVLATSNISREAVAKSDVVYQGEEEEERLMVDQAEESEEDTETPQRAVVSELSMKTPEFLQAKRHRSFSQPASLAPPNIVLLPSKLTQAKCAPKRCATGPRQPRDPDKASLDHYCKVFSYYAKMPVEKSASKTLVKCLDQYFRTLCDDLETFAHHAGRKTVLLDDLELLMRRQGLVTDEVSLYVLVERHLPLEYRRLLIPCAASGNSVFPAGAHKAKERDRKEKQRYWSWLPRSEQAPFPPMWIWMEKISQKRTL
|
[
6695,
8603,
16787,
16815,
24783,
24917,
27904,
32577,
43635,
58861,
61138,
63277,
87272,
87273,
87284,
87306,
87384,
87695,
87790,
87857,
88008
] |
The following text describes a protein:
Function:
Component of the CENPA-NAC (nucleosome-associated) complex, a complex that plays a central role in assembly of kinetochore proteins, mitotic progression and chromosome segregation. The CENPA-NAC complex recruits the CENPA-CAD (nucleosome distal) complex and may be involved in incorporation of newly synthesized CENPA into centromeres. Part of a nucleosome-associated complex that binds specifically to histone H3-containing nucleosomes at the centromere, as opposed to nucleosomes containing CENPA. Component of the heterotetrameric CENP-T-W-S-X complex that binds and supercoils DNA, and plays an important role in kinetochore assembly. CENPT has a fundamental role in kinetochore assembly and function. It is one of the inner kinetochore proteins, with most further proteins binding downstream. Required for normal chromosome organization and normal progress through mitosis.
Subcellular Localization:
Chromosome, centromere, kinetochore. Nucleus.
| 0
|
MATAPAPADAKAEAAKMDLLEDDDEFEEFEIDQEWDDKEEGNEAVQQWEDDWDDDDVNDDFSLQLRKELEGASAQKS
|
[
6796,
8135,
14543,
24780,
24917,
25160,
42626,
87857,
87967,
88008
] |
The following text describes a protein:
Function:
Component of the 26S proteasome, a multiprotein complex involved in the ATP-dependent degradation of ubiquitinated proteins.
Subcellular Localization:
Nucleus.
| 0
|
MSTDQRDRLLEGVGWKARGDRIPEFPNPRPFFPRLKHSIKLIPLFVRVALHTFVEWWNGREAFIDIFNVFRHFTYTGVPLGGIGSGSIGTDFRGGFNRFSIIPGIKEQTETQKCNQFIASVHSKKTFELIYQSILSCAEFPATVLPKWDSTIPAEDVRYRGLFPRAWQEFRLGTSGITVVVEHLSPVIPEDYSDSSLPLANFDFHVFNDSPEEVEVSITMSFRNGTGNKKWNDESLCQSHKVQKDTMVVRTLSHTVKGMPVTYAIGTEEKNGAKVTTCLFDPNGTGGRLWSDLEAYGHLSSYDHLPPKPKELGIAVCSSFFVPPDGSHTTQFSLAWYMPQVHFGTAERFYNRRYCRFFNGPDADEVGASICRHGLQNIETWQEAIRKWQDPIINDEKLPEWYRSAIFNELYYIVDGSTVWFEYDPEWRTDEILISEETEKQFKQYGRFGYMESWEYFMINTYDVHFYSSWAILKNWPQIEMSMQMDFADQVDRVDYGTATSLADGDTMTIKSYDRIPHDMGHPSNPHLPSIQEHHRLSVADPWIHTNAYILHDTGHWKDLNLKFVISCYRDWKMIAEGEEDSQEILEFFLGKCTKIVDGALENWDKDKDGMIENDGFADQTYDVWKMTGTSAYCGSLWIAALTSYIQMLKRAGIPTKDYEEKLLMAYEAYTTKLWNGKFFKFDELPDNSKIVMADQLCGFWALTAMDEPIQVSEGKIQSALETIFKYNVEMYDGGKCGAVNGFLASERVDGSSIQSEEVWAGITYSLSAMMIEKAPIYLQGMDEMAFKTSEGLFHSIWNRFPLQYQTPEAITADGMYRALGYMRPLSIWAIQHALDKKKNRK
|
[
4386,
7854,
8346,
25325,
28264,
29225,
41700,
43533,
46278,
48169,
56102,
78215,
87523,
87601,
87731,
87760,
88008
] |
The following text describes a protein:
Function:
Non-lysosomal glucosylceramidase that catalyzes the hydrolysis of glucosylceramide (GlcCer) to free glucose and ceramide.
| 0
|
MWRLLLALLLVSSVCCESELFRDDLRTPETMAYINGLMQRRHQMQQEAQQHIQAIPPAVPLQSPGLVNGLGNQNDPALNRISGTSVKPSNLPAAYSNGYVDLATSDRIANSVLNFANILGQHLANGKTQIYSPLSIVHSLALLLLGAKGRSYEELSTVFDIPDTSRLHEQFGLMLQDLQQPTREAISAGRPLTDWRASSAMRSNRRAQRPGAHEVHLANGLFTQTGYTLNPDYRRVIVEVYASDLQIQDFEGSPATARYNINAYVAQHTKNHIENIIASDIPQTTRMILANALYFKAFWETDFIESATRPDNFYPNGEGTEPVMRVQMMATGGAYPYHEDHELGCKIIGLPYRGNLSTMYIIQPFKSSVRELMALQKRLTADKIESMISRMYRRAALVAFPKMHLTESVNLKTVMQRMGLGGIFSAVQNDLSLIATNEATRTNALGGNSLQNLEAQRRAGTGGARSDLVVDDIVHKVDFTVNEQGTEAAASSVTYLKKSGPDVLFRGDTPFMVLVRHDPTKLVLFYGLINEPPAAA
|
[
7331,
9350,
13131,
14219,
15373,
24907,
28679,
36120,
55539,
63958,
69165,
69169,
87402,
87522,
87616,
87758,
87966,
88008,
88038,
88051,
88058
] |
The following text describes a protein:
Function:
Serine protease inhibitor which is required for pupal viability and plays an essential role in regulating the melanization reaction. Inhibits spontaneous melanization and appears to be involved in the melanization immune response to physical wounding in larvae and adults. Acts by negatively regulating the Hayan-phenoloxidase (PPO1) cascade in the hemolymph and possibly the trachea. May function by controlling the initial release of the activated form of PPO1, phenoloxidase (PO) and thus maintains PO availability for processes such as wound response and pigmentation.
Subcellular Localization:
Secreted.
| 0
|
MSPCGRARRHTSRGAMAVLAWKFPRTRLPVGASALCVVVLCWLYVFPVYRLPDEKEIVQGVLQQGTAWRRNRTAAGIFRKQMEDCCDPAHLFAMTKMNAPMGKSLWYDGEFLYSFTIDNSTYSLFPQATPFQLPLKKCAVVGNGGILKKSGCGRQIDEADFVMRCNLPPLSSEYTKDVGSKSHLVTANPSIIRQRFQNLLWSRKTFVDHMKVYNHSYIYMPAFSMKTGTEPSLRVYYTLSDVGANQTVLFANPNFLRSIGKFWKSRGIHAKRLSTGLFLVSAALGLCEEVAIYGFWPFSVNMHEQPISHHYYDNVLPFSGFHAMPEEFLQLWYLHKIGALRMQLDPCEDNSLQPTS
|
[
3128,
8188,
8192,
8332,
9280,
24724,
27950,
37336,
46189,
66060,
76598,
87413,
87522,
87525,
87528,
87728,
87731,
87760,
88008,
88061,
88070,
88153,
88159,
88161
] |
The following text describes a protein:
Function:
Catalyzes the addition of sialic acid in alpha 2,8-linkage to the sialic acid moiety of the ganglioside GM3 to form ganglioside GD3; gangliosides are a subfamily of complex glycosphingolipds that contain one or more residues of sialic acid (By similarity). Can catalyze the addition of a second alpha-2,8- sialic acid to GD3 to form GT3 (By similarity). Can use GM1b, GD1a and GT1b as acceptor substrates to synthesize GD1c, GT1a and GQ1b respectively (By similarity).
Subcellular Localization:
Golgi apparatus membrane; Single-pass type II membrane protein.
| 0
|
MQCSWKAVILLALVSIAIQYTAIRTFTAKPFHICPVPNPLNCGLGQDVESFDRMCDEYPYFNYNSSRKTHILILATTRSGSSFVGQLFNQHSDVFYLFEPLYHVQTTLIPHLSPSRYAVERRVMLGASRDLLRSLYNCDLYFLESYIKPQPANHTTDKLFRRGASKALCSMPVCDAFSPNDGNIEEGDCVRKCASLNLTLATESCRERRHVAIKTVRIPEVNDLKALIEDPRLNLKVIQLVRDPRGILSSRIETFRDTYRLWRIWRATGRKPYNLDLTQLTTVCDDFLNSVSTGLSRPPWLRGRYMLVRYEDLARNPLQKTKEVYEFLGLSLEKGVVDWIHNNTRGNNDVSAKHKYGTLRDSAANAESWRLKLSHDIVDYTQTVCQHILDELGYKAVNSPEELKNMSISLIEDKTFIPFL
|
[
3861,
7854,
7905,
14165,
24724,
27793,
32392,
36659,
49474,
58239,
76789,
87258,
87522,
87528,
87760,
88008,
88061,
88153,
88159,
88161
] |
The following text describes a protein:
Function:
Sulfotransferase that utilizes 3'-phospho-5'-adenylyl sulfate (PAPS) as sulfonate donor to catalyze the transfer of sulfate to position 6 of galactose (Gal) residues of keratan.
Subcellular Localization:
Golgi apparatus membrane; Single-pass type II membrane protein.
| 0
|
MQYQHPSSSALGLSVPLFAPTPLQHPTPFYIDDILGRNSASNGTPALPTPTLPSPNSSFTSLVATYRTPIYEPTPIHPAFTHPGAALAASYGASTYASPLYPFSRPVSDYTHALIRHDSLGKPLLWSPFIQRPLHKRKGGQVRFSNDQTIELEKKFETQKYLSPPERKRLAKMLQLSERQVKTWFQNRRAKWRRLKQENPQGNKKDETESLENICEESQERCLSAEQKSRESSLDDPTSSPTSQGNLDSEVSDDSDQEVDIEGDKGYYNCAH
|
[
6673,
6911,
7053,
8103,
8912,
9561,
10615,
11620,
11630,
13215,
15387,
24917,
27733,
27735,
32185,
37071,
43624,
50806,
52772,
76654,
87384,
87402,
87566,
87857,
88008,
88010,
88148,
88150,
88256
] |
The following text describes a protein:
Function:
Recognizes the DNA sequence 5'-ATTAA-3'. Transcriptional repressor. Regulates the differentiation of both endothelial and blood cells (By similarity). Probably plays a role in the proliferation of vascular endothelial cells during blood vessel development. Establishes anterior identity at two levels; acts early to enhance canonical wnt-signaling by repressing expression of tle4, and acts later to inhibit nodal-signaling by directly targeting nodal/nr1 and nodal2/nr2. May play a role in liver development. Induces heart development.
Subcellular Localization:
Nucleus.
| 0
|
MFAMYNSYNEAEKTVFVGNLDSSVREEILFELFLQAGPLTKVTIAKDKDGRQRSYGFVCYKHREAVPYAIALLNGICLYGRPIKLQYRLGSSHNAEAHAVFPVLENGPGKPSQESYRTVCCQKASVFPSSAVSTCLSQENLCWQNPMFCSPIQPYSMDAQIAQQQSYLPDAFSQQSRMTSLSWFVQSCPASSSFVQWTHAQQDQQDQLSEFLSYSWVREGQVVDTWDTDQKERRTKKTQDGKQEFRKHKSKHKI
|
[
6728,
8126,
9086,
11620,
24917,
25367,
27929,
29164,
36354,
46581,
62588,
63774,
77935,
87402,
87407,
87857,
88001,
88008,
88273,
88274
] |
The following text describes a protein:
Function:
Tissue-specific splicing factor with potential implication in the regulation of alternative splicing during neuron and germ cell differentiation. Antagonizes SRSF1-mediated BCL-X splicing. May affect the choice of alternative 5' splice sites by binding to specific sequences in exons and antagonizing the SR protein SRSF1.
Subcellular Localization:
Nucleus speckle. Nucleus, nucleoplasm.
| 0
|
MAVSWIVFDLWLLTVFLGQIGGHSLFSCEPITLRMCQDLPYNTTFMPNLLNHYDQQTAALAMEPFHPMVNLDCSRDFRPFLCALYAPICMEYGRVTLPCRRLCQRAYSECSKLMEMFGVPWPEDMECSRFPDCDEPYPRLVDLNLVGDPTEGAPVAVQRDYGFWCPRELKIDPDLGYSFLHVRDCSPPCPNMYFRREELSFARYFIGLISIICLSATLFTFLTFLIDVTRFRYPERPIIFYAVCYMMVSLIFFIGFLLEDRVACNASSPAQYKASTVTQGSHNKACTMLFMVLYFFTMAGSVWWVILTITWFLAAVPKWGSEAIEKKALLFHASAWGIPGTLTIILLAMNKIEGDNISGVCFVGLYDVDALRYFVLAPLCLYVVVGVSLLLAGIISLNRVRIEIPLEKENQDKLVKFMIRIGVFSILYLVPLLVVIGCYFYEQAYRGIWETTWIQERCREYHIPCPYQVTQMSRPDLILFLMKYLMALIVGIPSIFWVGSKKTCFEWASFFHGRRKKEIVNESRQVLQEPDFAQSLLRDPNTPIIRKSRGTSTQGTSTHASSTQLAMVDDQRSKAGSVHSKVSSYHGSLHRSRDGRYTPCSYRGMEERLPHGSMSRLTDHSRHSSSHRLNEQSRHSSIRDLSNNPMTHITHGTSMNRVIEEDGTSA
|
[
6964,
7039,
7086,
7161,
9297,
11856,
12692,
13763,
13812,
13813,
14235,
15448,
16921,
17278,
17279,
18121,
19048,
20212,
21282,
24978,
25079,
25278,
25337,
25339,
25494,
25495,
25772,
26197,
26409,
26472,
27093,
28715,
30491,
30893,
32078,
36384,
48909,
50814,
52539,
64525,
68783,
87276,
87402,
87413,
87484,
87522,
87760,
87829,
88006,
88008,
88058,
88152,
88159,
88161,
88180,
88256
] |
The following text describes a protein:
Function:
Receptor for Wnt proteins. Most of frizzled receptors are coupled to the beta-catenin canonical signaling pathway, which leads to the activation of disheveled proteins, inhibition of GSK-3 kinase, nuclear accumulation of beta-catenin and activation of Wnt target genes. A second signaling pathway involving PKC and calcium fluxes has been seen for some family members, but it is not yet clear if it represents a distinct pathway or if it can be integrated in the canonical pathway, as PKC seems to be required for Wnt-mediated inactivation of GSK-3 kinase. Both pathways seem to involve interactions with G-proteins. Activation by Wnt5A stimulates PKC activity via a G-protein-dependent mechanism. Involved in transduction and intercellular transmission of polarity information during tissue morphogenesis and/or in differentiated tissues. Plays a role in controlling early axon growth and guidance processes necessary for the formation of a subset of central and peripheral major fiber tracts. Required for the development of major fiber tracts in the central nervous system, including: the anterior commissure, the corpus callosum, the thalamocortical, corticothalamic and nigrostriatal tracts, the corticospinal tract, the fasciculus retroflexus, the mammillothalamic tract, the medial lemniscus, and ascending fiber tracts from the spinal cord to the brain. In the peripheral nervous system, controls axon growth in distinct populations of cranial and spinal motor neurons, including the facial branchimotor nerve, the hypoglossal nerve, the phrenic nerve, and motor nerves innervating dorsal limbs. Involved in the migration of cranial neural crest cells. May also be implicated in the transmission of sensory information from the trunk and limbs to the brain. Controls commissural sensory axons guidance after midline crossing along the anterior-posterior axis in the developing spinal cord in a Wnt-dependent signaling pathway. Together with FZD6, is involved in the neural tube closure and plays a role in the regulation of the establishment of planar cell polarity (PCP), particularly in the orientation of asymmetric bundles of stereocilia on the apical faces of a subset of auditory and vestibular sensory cells located in the inner ear. Promotes neurogenesis by maintaining sympathetic neuroblasts within the cell cycle in a beta-catenin-dependent manner.
Subcellular Localization:
Membrane; Multi-pass membrane protein. Cell membrane; Multi-pass membrane protein. Cell surface. Apical cell membrane; Multi-pass membrane protein. Note=Colocalizes with FZD6 at the apical face of the cell.
Domain:
Lys-Thr-X-X-X-Trp motif interacts with the PDZ domain of Dvl (Disheveled) family members and is involved in the activation of the Wnt/beta-catenin signaling pathway; The FZ domain is involved in binding with Wnt ligands.
| 0
|
GTVFFDQDSPDSPVKVTGEVTGLQKHGFHIHEFGDNTNMSADGSSYLQVSGSKLTQEGQASMEVKGNAGARVAXGVVGIAK
|
[
8435,
8959,
15949,
24878,
28880,
29024,
37130,
50940,
55824,
64179,
87411,
87567,
88038
] |
The following text describes a protein:
Function:
Final heterodimeric neurohormone released at the end of the molting cycle, involved in the sclerotization (tanning) of the insect cuticle, melanization and wing spreading.
Subcellular Localization:
Secreted.
| 0
|
MREIVTLQFGERSNYLGTHFWNTQESYFTYPPEAESPVNHDILFRPGIAPDGSDTFTPRALIYDLKGAFGSMRKINALYEPEDDRSILDQPGVWPSKPIVQRTQPIPPSTYQEHLDNGLDPPALNISSVRYWSDYSRVFYHPKSIAQLSEFDVNDTLMPFEKWEVGKGLFEKLEREVDLVDRDLRPFVEECDGIQGLQIFTGVDDAWGGWASGWIERLRDEYGKMSIWTWGLGDQGANAAVGRERRLQQMVNASQSLQTLGEQSSVYIPISNSPTKTPSYLSLDATSLWHVGALQAIGLESMTISSRLRTSVGGRGNLQDLEDTINSTGKRRIGKFEMSIADPEVLSENYSKEMAQAEKTGSMTSRRTSEDDEELSSFDIDVFTRDYRAVSRSGKKEHVFGRAEVSRGDWNLTDDNEARDPHNRFNQGPTLQRYTAPILFPLLDSYPTSIFDVGSGLGTKLAVHAGLTTSTAVAGQIRAVEQIVKRLVGIEEREALCNGLQVLAEEYDEGWDSGTDSDDDG
|
[
8565,
24978,
24979,
47570,
52123,
59369,
64271,
75612,
87785
] |
The following text describes a protein:
Function:
Involved in the partitioning of the mitochondrial organelle and mitochondrial DNA (mtDNA) inheritance.
Subcellular Localization:
Mitochondrion.
| 0
|
MVNEPLDSQSTTTVTAQPIISIGKPSDDHDTQTSALSDTATIVALILRLIFGHTPWLVYRFLSYTVTATITLDLWSVLGLLSLISLVVYLLIRYRLLNTYTHLKTPAPIAPRAPFDLQPDATLDDDTDLNKGYPDEFMNAFLSSIKVFGYLDKPVFHELARHLQTRKLKTGEILFDEDSEDRDFYVVVDGCVQIYLKGNSNALARHSLGSNNFEDRSDSDDPEDEFSGHHLLNEVKAGETVSSLFTILSLFTEDFELSTLMQPHSAATNLNESHGTSFSSKHSGFPQAQSPAFSTQLDSDESAWLRFNHLQQDSSIDSTPTPETAHPDAKPPHGLDGSEDHKHFTHPTSGNHIPKRKHRSVHPGIITRASSPTTLAVIPAQAFRKLTEKFPNAAAHIVQVILTRFQRVTFLTLYRYLGLSKELLKIERQVNQFSGYGLPTDLFPPEILHDLRLRTIRKRRGINNTFVTNEVDSSNGNEVDRRMSEMPGSRGTYNVNDDTASLTISMGLTHSQQRNHRRAHRNVVEINEYNNTADSSENDTAGPAKPPRKPNAKSSYRPTRLNDEADGPIKEAVFKCIAQLIGMRPYSGPPGHSNLAPMTDRLYYSRSRTSWKPTSSTVFSIGSARASHPKTPDETTSPSNSTGNFSIDSSDQVEIDIMYFEHGQTLVKEGERGAGLYFVLDGVLEASMSTSNSQLFPIRTGDASQNSNPSSRGKSRRNLFLIHPGGLAGYLAALTGQTSFVTIKAKTDAHVGFMSKQVLDKYVERFPDILLCLAKRLVNQLSPLVLHIDVALEWGQVNAGQVLCRQGEPSTSIYIVLTGRLRAIVERSRNGIESLDILGEYGQLESVGEMEVLMDAPRTATIHAIRDTEVAIMPKTLFNALAIGHPEITISIARIIAARSTQSFLGKMGPGQQPSFNMRGSPDSGNNNVNLKTVAILPVTSIVPVFEFADHIRDALQLIGASVAFLNTASVMRELGKHAFTRLGRLKLMSWLSEQEESHRLVLYVADGGVSSPWTQRCVRQADCILLVGLGDEDPGIGEFERLLIGMKTTARKELVLLHNQRACIPGSTAQWLKNRVWVHAHHHVQMNLNTPKLLNKTTQKQLTLINLKSHFQRVYTSMYPMNSTGKKSSAPNIYSGVRSDFARLARRLLSKSIGLVLGGGGARGFAHIGVIRAFEEAGIPVDMIGGTSMGSFVGGCYARENDHVSVYGRAKMLGGRLGSTWRSLIDLTYPITAIFTGKSFCHEFNRGIWKVFSDTQIEDCWISYFAVTTNLNWSRMEVHQTGYMWRYIRASMSLSGYLPPLCDHGSMLLDGGYINNLPADIMHSLGAHTIIAVDVSLADDTSPVSYGDSVSGWWMLLSKLNPFPQSYSFRPPEIADIQSRLTYISSVKQLEDAKRIDGCLYIHPPVAAYTAMDFKKFKEIVEVGYKFGQTVVQEWHNNGTLQRQLGVTLADSVERKLRGGRRASI
|
[
3972,
10604,
15681,
25008,
25014,
28482,
36430,
37129,
38123,
48241,
49123,
51166,
51167,
75956,
87432,
87601,
87729,
87731,
87760,
88008,
88159,
88161
] |
The following text describes a protein:
Function:
Intracellular phospholipase B that catalyzes the double deacylation of phosphatidylcholine (PC) to glycerophosphocholine (GroPCho). Plays an important role in membrane lipid homeostasis.
Subcellular Localization:
Endoplasmic reticulum membrane. Membrane.
| 0
|
MGRASKDKRDIYYRKAKEEGYRARSAYKLLQLHEEFGILRREEIRTGVVDLCAAPGSWSQVLSNHLCGSQPGSAAEACEGDEAINSEASQRPRIVAVDLQEMMPIDGVQLLQGDITSEWTAREIIRLLNGDSSSVPECSDATALSTAGAINDFNNGRGNNVSEEGKSSQQRSDCGVGLMNERNNASECVDGDNNNNNSNNNDDRNGGDAGASTRPVAGRKADLVVCDGAPDVTGMHELDEYLQHHLLLAALNITTFVLRRGGTFVTKMFRGPNTPFLVAKAEVFFRQVTIAKPKSSRNASMEAFMVCQNYDPPASYQPSFERPLTQTTSCFTPAAPALHLAAVDAQRMSSDNVNNGELHHSGVTDIVDEAYAVESVIVPFLACGDLTGYDADMCYDRGESDVVLPPVQPPLQAPYIAISEAVKERTKRQRVG
|
[
2173,
7203,
7224,
11739,
24978,
29123,
35189,
38310,
48903,
58980,
59229,
75737,
87367,
87777,
88008,
88026,
88153,
88278
] |
The following text describes a protein:
Function:
Methylates the 2'-O-ribose of nucleotides at positions 32 and 34 of the tRNA anticodon loop of substrate tRNAs.
Subcellular Localization:
Cytoplasm.
| 0
|
MLRSLSVFVLLAVACCHAEEVKSKSKICANVFCGAGRECAITEKGEPTCLCIEECKPHKRPVCGSNGRTYRNHCELHRDACLTGLKIQVAHDGHCEEKKTEKSAASPIVCYLADRNELRNRVIEWLQTEVVPDGWFSKGSNFSEILHRYFKTYDDGDSQMDSAEFLKFIQHNETAVNISSYMDEENNRLLRSLCVDALIELSDENADWKLSFNEFLNCFKPGFNPTQKKCALEDETFEDGAETQVECNRCVCACGNWVCTAMTCDGQNKKTAPLEDTDLTGQEEMTEEEWTRRVEELNKHQETVEKSKKSSTKEK
|
[
11620,
11749,
24878,
29025,
29141,
37640,
37895,
38901,
46081,
48833,
63842,
76308,
87413,
87522,
87552,
87914,
88008,
88009,
88038,
88058
] |
The following text describes a protein:
Function:
Secreted glycoprotein that is involved in various physiological processes, such as angiogenesis, regulation of the immune response, cell proliferation and differentiation. Plays a role in the development of the central nervous system, skeletal system, lungs, and ureter. Promotes endothelial cell survival, migration and differentiation into network structures in an AKT-dependent manner. Also promotes survival of cardiac myocytes. Initiates various signaling cascades by activating different receptors on the cell surface such as DIP2A, TLR4 or BMP receptors.
Subcellular Localization:
Secreted.
| 0
|
MGLIAIACGLIVALGALGASIGIAMVGSKYLESSARQPELIGPLQTKLFLIAGLIDAAFLIGVAIALLFAFVNPFAGA
|
[
10591,
25079,
25848,
26421,
29172,
30332,
32555,
36311,
37916,
40973,
52797,
63722,
66141,
87109,
87238,
87274,
87276,
87598,
87601,
87676,
87733,
87760,
88008,
88159,
88161,
88162
] |
The following text describes a protein:
Function:
F(1)F(0) ATP synthase produces ATP from ADP in the presence of a proton or sodium gradient. F-type ATPases consist of two structural domains, F(1) containing the extramembraneous catalytic core and F(0) containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation; Key component of the F(0) channel; it plays a direct role in translocation across the membrane. A homomeric c-ring of between 10-14 subunits forms the central stalk rotor element with the F(1) delta and epsilon subunits.
Subcellular Localization:
Cell inner membrane; Multi-pass membrane protein. Cell membrane; Multi-pass membrane protein.
| 0
|
MMKIYLMGSDQRIVRCARVSFAKDSYVDEKRDKRLIRYLFKHRHASPFEHNIIAFEWKKEKWIELLSKLENPTVQVYYSNGFVFLNLRNAINVWELLPDAVKERIKEAFPTTYGVIQRRGEIEDEELYSLPYTKDKAYVKEKIETSSGWIGLVDKLELETDMDFYTFVVECPLFVARQWMRHRFGSYNEVSKRYVGKEFLEFYLPKYIRKQAEKNKQASVDEPISESEVFIKKIENLISKSVKLYEEIIEKGGAKELARGVLPQFMKTRFYWTVPRISLDNFITLRTHEGAQKEIREFAEAIKEMVGYRGTDKKNVI
|
[
2113,
8034,
8037,
12244,
28618,
33679,
33700,
34296,
38921,
63876,
87004,
87455,
87470,
87777,
87823,
87853,
88008,
88153
] |
The following text describes a protein:
Function:
Catalyzes the reductive methylation of 2'-deoxyuridine-5'-monophosphate (dUMP) to 2'-deoxythymidine-5'-monophosphate (dTMP) while utilizing 5,10-methylenetetrahydrofolate (mTHF) as the methyl donor, and NADPH and FADH(2) as the reductant.
| 0
|
MTPALTALLCLGLSLGPRTRVQAGPFPKPTLWAEPGSVISWGSPVTIWCQGSQEAQEYRLHKEGSPEPLDRNNPLEPKNKARFSIPSMTEHHAGRYRCHYYSSAGWSEPSDPLEMVMTGAYSKPTLSALPSPVVASGGNMTLRCGSQKGYHHFVLMKEGEHQLPRTLDSQQLHSRGFQALFPVGPVTPSHRWRFTCYYYYTNTPWVWSHPSDPLEILPSGVSRKPSLLTLQGPVLAPGQSLTLQCGSDVGYNRFVLYKEGERDFLQRPGQQPQAGLSQANFTLGPVSPSNGGQYRCYGAHNLSSEWSAPSDPLNILMAGQIYDTVSLSAQPGPTVASGENVTLLCQSWWQFDTFLLTKEGAAHPPLRLRSMYGAHKYQAEFPMSPVTSAHAGTYRCYGSYSSNPHLLSHPSEPLELVVSGHSGGSSLPPTGPPSTPGLGRYLEVLIGVSVAFVLLLFLLLFLLLRRQRHSKHRTSDQRKTDFQRPAGAAETEPKDRGLLRRSSPAADVQEENLYAAVKDTQSEDRVELDSQSPHDEDPQAVTYAPVKHSSPRREMASPPSSLSGEFLDTKDRQVEEDRQMDTEAAASEASQDVTYAQLHSLTLRRKATEPPPSQEGEPPAEPSIYATLAIH
|
[
7262,
7520,
8531,
8664,
10947,
15260,
25079,
25516,
28688,
31311,
31958,
38877,
38878,
41979,
46981,
47529,
63951,
76067,
87126,
87139,
87276,
87413,
87522,
87616,
87618,
87760,
87914,
87976,
88006,
88008,
88009,
88058,
88159,
88161
] |
The following text describes a protein:
Function:
May act as receptor for class I MHC antigens. Becomes activated upon coligation of LILRB3 and immune receptors, such as FCGR2B and the B-cell receptor. Down-regulates antigen-induced B-cell activation by recruiting phosphatases to its immunoreceptor tyrosine-based inhibitor motifs (ITIM).
Miscellaneous:
MISCELLANEOUS: Belongs to the leukocyte receptor cluster (LRC) present on 19q13.4.
Subcellular Localization:
Cell membrane; Single-pass type I membrane protein.
Domain:
Contains 3 copies of a cytoplasmic motif that is referred to as the immunoreceptor tyrosine-based inhibitor motif (ITIM). This motif is involved in modulation of cellular responses. The phosphorylated ITIM motif can bind the SH2 domain of several SH2-containing phosphatases, including PTPN6/SHP-1, resulting in the dephosphorylation of the downstream protein kinases SYK and BTK.
| 0
|
MAEAALEGTEPVDLSKHPSGIIPTLQNIVSTVNLDCKLDLKAIALQARNAEYNPKRFAAVIMRIREPKTTALIFASGKMVCTGAKSEQQSKLAARKYARIIQKLGFPAKFKDFKIQNIVGSCDVKFPIRLEGLAYSHGAFSSYEPELFPGLIYRMKQPKIVLLIFVSGKIVLTGAKVREETYTAFENIYPVLTEFRKVQQ
|
[
8098,
24917,
27904,
30147,
36617,
46245,
59839,
61957,
87384,
87857,
88008,
88148
] |
The following text describes a protein:
Function:
General transcription factor that functions at the core of the DNA-binding multiprotein factor TFIID. Binding of TFIID to the TATA box is the initial transcriptional step of the pre-initiation complex (PIC), playing a role in the activation of eukaryotic genes transcribed by RNA polymerase II.
Subcellular Localization:
Nucleus.
| 0
|
MTEEPTKENLGGPKSPTPVTMEKSPKSEVVVTTVPLVSEVQLTAATGGAELSCYRCIIPFAVVVFITGIVVTAVAYSFNSHGSVISILGLVLLSSGLFLLASSALCWKVRQRNKKVKRRESQTALVVNQRSLFA
|
[
6890,
6911,
6947,
7707,
7708,
8706,
11748,
15202,
16521,
17039,
17054,
17790,
19082,
24646,
25008,
25079,
26218,
26465,
61284,
87276,
87367,
87402,
87407,
87432,
87760,
87914,
88008,
88159,
88161
] |
The following text describes a protein:
Function:
Plays a role during embryonic arterial endothelium differentiation and vascular morphogenesis through the ACVRL1 receptor-dependent signaling pathway upon stimulation by bone morphogenetic proteins, such as GDF2/BMP9 and BMP10. Involved in the regulation of nociception, acting as a modulator of the interaction between TRPA1 and TRPV1, two molecular sensors and mediators of pain signals in dorsal root ganglia (DRG) neurons. Mechanistically, it weakens their interaction, thereby releasing the inhibition of TRPA1 by TRPV1 and increasing the single-channel open probability of the TRPA1-TRPV1 complex.
Subcellular Localization:
Cell membrane; Multi-pass membrane protein. Membrane; Multi-pass membrane protein. Perikaryon. Cytoplasm, perinuclear region. Endoplasmic reticulum. Note=Colocalized with HSPA5 in the endoplasmic reticulum (ER). Enriched in ER microsome. Colocalized with BMP4 in neural cell bodies and neural fibers of the enteric nervous system (By similarity).
| 0
|
MEKYNAIKIVKGSGGFGGPLTVKPEEGKDTLLYITGGGAEPEIVEKIVNLTGCKAVNGFKTSVPEEQIFLVIIDCGGTLRCGIYPQKRIPTINVMPVGKSGPLAKFITEDIYVSAVGLNQISLADSSAEPIKSTKVPEEGKREFKYSADKKVSQSLAENSKSSIVQKIGMGAGKVVNTLYQAGRDAVQSMITTILPFMAFVAMLIGIIQGSGFGNWFAKILVPLAGNGIGLMILGFICSIPLLSALLGPGAVIAQIVGTLIGVEIGKGTIPPSLALPALFAINTQCACDFIPVGLGLAEAEPETVEVGVPSVLYSRFMIGVPRVAVAWVASIGLYQ
|
[
3489,
9291,
25079,
29579,
30159,
34600,
39846,
45731,
45746,
87276,
87694,
87760,
87914,
87915,
88087,
88153,
88159,
88161,
88162
] |
The following text describes a protein:
Function:
The phosphoenolpyruvate-dependent sugar phosphotransferase system (sugar PTS), a major carbohydrate active transport system, catalyzes the phosphorylation of incoming sugar substrates concomitantly with their translocation across the cell membrane. The enzyme II complex composed of SrlA, SrlB and SrlE is involved in glucitol/sorbitol transport.
Subcellular Localization:
Cell membrane; Multi-pass membrane protein.
Domain:
The EIIB domain is phosphorylated by phospho-EIIA on a cysteinyl or histidyl residue, depending on the transported sugar. Then, it transfers the phosphoryl group to the sugar substrate concomitantly with the sugar uptake processed by the EIIC domain.
| 0
|
MVMEKPSPLLVGREFVRQYYTLLNKAPEYLHRFYGRNSSYVHGGVDASGKPQEAVYGQNDIHHKVLSLNFSECHTKIRHVDAHATLSDGVVVQVMGLLSNSGQPERKFMQTFVLAPEGSVPNKFYVHNDMFRYEDEVFGDSEPELDEESEDEVEEEQEDRQPSPEPVQENANSAYYDAHPVTNGIEEPLEESSHEPEPEPESETKTEELKPQVEEKHLEELEEKSATPPPAEPASLPQEPPKAFSWASVTSKNLPPSGTVSSSGIPPHVKAPVSQPRVDAKPEVQSQPPRVREQRPRERPGFPPRGPRPGRGDMEQNDSDNRRIIRYPDSHQLFVGNLPHDIDENELKEFFMSFGNVVELRINTKGVGGKLPNFGFVVFDDSEPVQRILIAKPIMFRGEVRLNVEEKKTRAARERETRGGGDDRRDIRRNDRGPGGPRGIVGGGMMRDRDGRGPPPRGGMTQKLGSGRGTGQMEGRFTGQRR
|
[
8725,
12862,
15044,
16634,
16763,
25040,
25296,
27925,
35466,
36354,
37663,
46581,
50988,
61424,
62503,
63774,
66860,
87139,
87367,
87616,
87662,
87684,
87776,
87914,
88001,
88008,
88162,
88180,
88275
] |
The following text describes a protein:
Function:
Scaffold protein that plays an essential role in cytoplasmic stress granule formation which acts as a platform for antiviral signaling. Plays an essential role in stress granule formation. Stress granules are membraneless compartments that store mRNAs and proteins, such as stalled translation pre-initiation complexes, in response to stress (By similarity). Promotes formation of stress granules phase-separated membraneless compartment by undergoing liquid-liquid phase separation (LLPS) upon unfolded RNA-binding: functions as a molecular switch that triggers RNA-dependent LLPS in response to a rise in intracellular free RNA concentrations (By similarity).
Subcellular Localization:
Cytoplasm. Cytoplasm, Stress granule.
Domain:
Can mediate both protein-protein and protein-RNA interactions via the NTF2 domain and RNA-binding domain RRM; protein-protein and protein-RNA interactions are essential for undergoing liquid-liquid phase separation (LLPS); The acidic disordered region acts as a negative regulator of phase separation; The NTF2 domain mediates interaction with CAPRIN1 and USP10 regulators, thereby regulating assembly of stress granules.
| 0
|
MCLLRLPVTLLVLCVALNELKATSIASDTGHQVGKRKCNTATCATQRLTNFLVRSSHNLGAALLPTDVGSNTYGKRNAPQISDRELLHYLPL
|
[
10955,
11698,
15141,
15260,
15320,
16523,
20256,
21079,
24907,
26197,
28880,
32073,
33211,
36303,
37350,
51100,
53185,
53186,
87142,
87150,
87317,
87413,
87567,
88008,
88038,
88058
] |
The following text describes a protein:
Function:
Amylin/IAPP is a glucoregulatory peptide hormone that plays an important role in the regulation of energy homeostasis (By similarity). Selectively inhibits insulin-stimulated glucose utilization and glycogen deposition in muscle, while not affecting adipocyte glucose metabolism. IAPP function is mediated by the CALCR-RAMPs (AMYRs) receptor complexes. Amylin can also bind CALCR receptor in the absence of RAMPs, although it is more selective for AMYRs (By similarity).
Subcellular Localization:
Secreted.
Domain:
The mature protein is largely unstructured in the absence of a cognate ligand.
| 0
|
MFQWYQRSLIQRPLLTQSLTTACLFAVGDSLAQQAVEKRGIAQHDVARTGRMAFYGGGNVQPFPYKLPLLTVVAVFGPLATKWFQVLQRRINLPSAQRTVVGRVAADQLLFAPTMIGVFLSSMSVLEGGSLSEKLERSYWPALKANWTVWPFLQLVNFALVPLQFRVLTVNVLNIGWNCFLSLSNNVGSQDVPLVA
|
[
24978,
24979,
24983,
42103,
87760,
87785,
87786,
88008,
88159,
88161
] |
The following text describes a protein:
Function:
May be involved in cellular response to stress. Required to maintain mitochondrial DNA (mtDNA) integrity and stability (By similarity).
Subcellular Localization:
Mitochondrion inner membrane; Multi-pass membrane protein.
| 0
|
MLFKKDRKQETAYFSDSNGQQKNRIQLTNKHADVKKQLKMVRLGDAELYVLEQLQPLIQENIVNIVDAFYKNLDHESSLMDIINDHSSVDRLKQTLKRHIQEMFAGVIDDEFIEKRNRIASIHLRIGLLPKWYMGAFQELLLSMIDIYEASITNQQELLKAIKATTKILNLEQQLVLEAFQSEYNQTRDEQEEKKNLLHQKIQETSGSIANLFSETSRSVQELVDKSEGISQASKAGTVTSSTVEEKSIGGKKELEVQQKQMNKIDTSLVQIEKEMVKLDEIAQQIEKIFGIVTGIAEQTNLLSLNASIESARAGEHGKGFAVVANEVRKLSEDTKKTVSTVSELVNNTNTQINIVSKHIKDVNELVSESKEKMTQINRLFDEIVHSMKISKEQSGKIDVDLQAFLGGLQEVSRAVSHVAASVDSLVILTEE
|
[
8522,
8663,
9322,
25325,
30786,
30838,
32536,
39288,
43619,
46244,
66736,
70674,
87103,
87541,
87678,
87767,
88008,
88152
] |
The following text describes a protein:
Function:
Heme-containing signal transducer responsible for aerotaxis, the migratory response toward or away from oxygen.
| 0
|
MAVTEAVKEAIWMIGMVQELGIEQKNVNVYCDNQSAIHLTKHQVFHERSKHIDVRLNFVRNTVSKGRIKVEKVHTDDNAADMLTKSLPVSKFKYCMDLVSCYILYTLNPDVSGASTLFNDIFGAFGIGNNPETVPCCSWENSSPATSNCLYHTVTKFLESLIDNTHNCLHLRLLDKHCPSDPRTEMQVRFLELGSRKPSTCYCRKEDVESFVWAICRRIVPPKLLGEHSNWRILRTNIFKFIRLRKFEKFSLKECFHNLKISKFPLLHDNIHNGCSVLGITDIARHVILGCWIFWFFKCLVSPLFQANFYVIESEFERNEVLYYRKSTWRKLIREAECMKNDTFRPLNVSAVRKILKNRSHGFSRVRLLPKKTGFRMLANLQASSKLRLNSTSSKFQSDGSVNKVLNDVQVVLRGSLTKEREKFGSSVFDYNDVYRKLVPFLSRLKKRWSKMPRVFIVVSDVSKAFDSVNHDKLLSVMEDVLSDDEYALEKFTQVFCTKKALKVHHTLALADQDFVTVSSGKIKSIPPPKSLDGVLVNKALDRTIRKADINTTLKEHIKRNVVRQSDKKFYLQNVGIPQGSVLCTFLCSLYYGHMERNVVYPFIEKARETNGASSSAGGKNGKQKFACGCEYILLRFIDDFLFISTSEKQASMYFSRVDRGFHDYNCYMNKDKYGLNFKMKNGQECRSSSRPYVGRDGVSFLRWSGVLVNCSTLEIQADYTRYLDFHLSSTLTVSRQGKVGEQLKSKLRAHMSNKCHPLFYDSNVNSPDVVRLNIYQIFLLCAIKFVCHLSNLSILPKFTPQFITNAIVASVRCTSKFIEKKMYSFSGVDIAFRPKYEVKRAEVLFLGLYAYNRVLEKKQTRYKNLIPFLRTKLKACGEIAHMSSELKYAIHDEHSSVFWRIKY
|
[
3731,
8564,
24761,
24785,
27924,
32009,
32536,
34243,
36329,
38838,
53887,
74934,
87306,
87747,
87767,
87856,
87857,
88002,
88008,
88125,
88153
] |
The following text describes a protein:
Function:
Telomerase is a ribonucleoprotein enzyme essential for the replication of chromosome termini in most eukaryotes. It elongates telomeres. It is a reverse transcriptase that adds simple sequence repeats to chromosome ends by copying a template sequence within the RNA component of the enzyme.
Subcellular Localization:
Nucleus. Chromosome, telomere.
| 0
|
MAASSGSPQLATEDHLRKGEAVSGLHAVVAGSVSGLVARSVTAPMDTVKIRRQLQLASEHKYHGILHTFRTVAREEGVRALWKGNVPASAMYVLYGSLQFGTYAWLNTAAASAGLPPQAHSLAVGALAGLVSSLLTYPLDLLRTRLVANRSAHFFSLRRQARVIWDTEGPAGFFRGGAWAIAATTLTTGLIFGIYETCTIAADTYGLPWLAAAASPTAGLVSKAAVFPLDTVRRRLQIVDAKHIPFFTRDPGAYSALRGTRFLGLAVHMVRAEGIASLYKGLTMALCKSTPTTVITLWVYQRCLRLLEPTRAPQLPA
|
[
11877,
23866,
24983,
29897,
34579,
37655,
50913,
55191,
87760,
87785,
87786,
88008,
88009,
88159,
88161,
88162
] |
The following text describes a protein:
Function:
Mitochondrial transporter that mediates uptake of thiamine pyrophosphate (ThPP) into mitochondria.
Subcellular Localization:
Mitochondrion inner membrane; Multi-pass membrane protein.
| 0
|
MAAAPQAPGRGSVRKTRPLPVKTSLNNPYSICWGVLDREDMHFILQTLEDRIQSLGLQKIEDRKRKKKQPPLKKQSGDTSSIDVDTGEDLKKEKPKGDAQASGWTPVDVRKQLAIGINEVTRALERNELLLALACKSAKPAIVTSHLVQLSVSRGVPACQVPRLSERLAPVLGLKCVLALGFKRNTTAFGEELRAILPRVPRLNVAWLQDALEDPRENLQTESLESQDEEILDTSFEDLSKPKRKLAEGQQPVVLQPLKIKKLIPNPNKIRKPPKSKRTASK
|
[
6939,
8109,
24734,
24838,
24927,
24974,
25523,
28407,
31374,
39242,
59230,
69635,
87115,
87857,
87914,
88008,
88276,
88278
] |
The following text describes a protein:
Function:
Component of ribonuclease P, a ribonucleoprotein complex that generates mature tRNA molecules by cleaving their 5'-ends. Also a component of the MRP ribonuclease complex, which cleaves pre-rRNA sequences.
Subcellular Localization:
Nucleus, nucleolus.
| 0
|
MLPSQEASKLYHDNYVRNSRAIGVLWAIFTICFAIINVVVFIQPYWVGDSVNTPKPGYFGLFHYCVGSGLAGRELACRGSFTDFSTIPSGAFQAAAFFVLLSMVLTLGCITCFALFFFCNTATVYKICAWMQLLAALCLVLGCMIFPDGWDAETIRDMCGEKTGKYSLGDCSVRWAYILAIIGILNALILSFLAFVLGNRQNDLLHEELKTESKGGRCATRFCRHREDIRPSTRSRTSSRGRRPGRSLPVLPLICRRWPRSAPGRTARTGAVPAARRAHVHTDTAIPRTPPAPHLRRRRGRMPQTRFV
|
[
8970,
20094,
20588,
23629,
25079,
25495,
26414,
26492,
27095,
27136,
33702,
51919,
87276,
87278,
87760,
87943,
88008,
88097,
88159,
88161
] |
The following text describes a protein:
Function:
Plays a role in the regulation of inhibitory synapse formation and function by being involved in maintening gamma-aminobutyric acid receptors (GABAARs) clustering and their associated scaffold proteins at inhibitory synaptic sites. Acts in concert with NLGN2 to recruit or stabilize GABAARs.
Subcellular Localization:
Cell projection, dendrite. Postsynaptic cell membrane; Multi-pass membrane protein.
| 0
|
MAASEENSALFPIFILTIMALPLVPYTVMKLCRAASRKTKVIHCQCADCSRSGKYRKSIFKRISNFSTCSNLTLVLLWIIMIFLVYYIKNMSGEIQVFEPYSILGLEPGASDAEIRKAYRRLSILYHPDKNPDPAAHKHFVEYIVKAYQALTDPISRENYEKYGHPDGRQGFQMGIALPQFLLDIDGASGGILLLWIVGVCILLPLVIAVIYLSRSSKYTGNYVMHQTLSTYYYLMKPSLAPSKVMDVFTKAAEYVEIPVRRTDDEPLQKLFMSVRSELNLDLKNIKQEQAKFWKQHPAIVKTELLIQAQLTRESAALSPALLGDFRRMLELAPRLLEELLKMAVVPRTAQGHGWLRPAIGVVELSQCIIQAVPLSARKTTGGSSEGIASFLQLPHFSEAVIKKIARKKVRTFQELRDMTVEDRAELLTQAAGFSSAEVQDVEMVLEMMPSLTVEVTCETEGEEGIQEADIVTVQAWITLKRGSGLIGALPHAPNFPFHKEENFWFLLADGVSNNVWFSQKVSFMDEAAAITTASKTIQEAMEVSGASVKETSEAVKRAVEKVRGGSRLVMGKFPAPTEGNYNLTCYCLCDSWIGCDKKTNLKVKILKRTRAGTRSGHVSEEGLLVEDGVEEEEENEEEYDDYESEYSEDEEDEKDTKKKGPAANGTVNQKGSSSEGSGTDEE
|
[
8292,
8295,
25596,
29185,
37291,
39369,
48276,
63695,
64599,
87285,
87432,
87522,
87760,
87974,
88008,
88159,
88161,
88162
] |
The following text describes a protein:
Function:
Required for integral membrane and secreted preprotein translocation across the endoplasmic reticulum membrane.
Subcellular Localization:
Endoplasmic reticulum membrane; Multi-pass membrane protein.
| 0
|
MNLVQDKVTIITGGTRGIGFAAAKIFIDNGAKVSIFGETQEEVDTALAQLKELYPEEEVLGFAPDLTSRDAVMAAVGQVAQKYGRLDVMINNAGITSNNVFSRVSEEEFKHIMDINVTGVFNGAWCAYQCMKDAKKGVIINTASVTGIFGSLSGVGYPASKASVIGLTHGLGREIIRKNIRVVGVAPGVVNTDMTNGNPPEIMEGYLKALPMKRMLEPEEIANVYLFLASDLASGITATTVSVDGAYRP
|
[
266,
8364,
9035,
11768,
16776,
22499,
24978,
30232,
31277,
31443,
31466,
34297,
37894,
52988,
64058,
75914,
87103,
87731,
87822,
87873,
88078
] |
The following text describes a protein:
Function:
Involved in the multi-step bile acid 7alpha-dehydroxylation pathway that transforms primary bile acids to secondary bile acids in the human gut. Catalyzes the oxidation of C3-hydroxyl group of CoA conjugated bile acids generating a C3-oxo bile acid intermediate. Can use choloyl-CoA, chenodeoxycholoyl-CoA, deoxycholoyl-CoA, and lithocholoyl-CoA as substrates with similar efficiency. Highly prefers NAD over NADP as cosubstrate. Also catalyzes the reverse reactions; in vitro, the preferred direction of reaction depends on the pH. Has very little activity with unconjugated (non-CoA) bile acid substrates.
Miscellaneous:
MISCELLANEOUS: There are three genes for BaiA proteins: baiA1 is identical to baiA3 and encodes a polypeptide sharing 92% identity with baiA2 gene product; MISCELLANEOUS: Reaction mechanism seems to proceed via a nicotinamide-OH(-) adduct, which is proposed to be involved in proton relay instead of hydride transfer.
| 0
|
MHFKLLLLAALVLLFSTATHASVGGYICPNDRKKLLTVLVKALINVEGDFSTPYYGIKGFKALNEQVAAVLVKDNCAHIKKYYKADCTPEENFQGLSAWNLLGCSGKLHTDATITNLRTVLESDKSTTSDIRYAAETLKLLGAAIPNGAKVAQLIQAKLKEDDSLQSLGHALHAAALLGTSGNFIQDRIEEVVVQADEVDGKLLQWEGGLTTTSLLITGLLRFPGAKPLNAQQAEKLATYLLTRRTVQTPKGALALLEATTSLASSDISPVSITIAGPAQVTLDKPELKVHISDILGRALKAPPTPVVAQSATRITDDVVVLSKQPLSPGGTPVEFVLPLRLEPGQYRIALTAGSHSTTLTVRVLGPVTLEWLQIGLGDADGSAAPRLTKLTHPSKLPSPLRADSSHHLVAKFAISRVVHQAFLRLYSGKKEIIFVAEPDNSKLYKISVNLASELAHSGTFEMELILGDSVMSNPIRWVIGTIEVSLSTPEPEKKSLRGPKPEIKHLFRQPEKRPAEVVSMLFTGLTVSPLLLLFVLWWKVGVNFGGFTTLSVPFHVGFGGILYLFFLFWWKLDMFTTCAWLIPIGGFTFLAGHKLLSHVAKHKKA
|
[
8189,
25147,
43429,
87432,
87760,
88008,
88058,
88159,
88161
] |
The following text describes a protein:
Function:
Subunit of the oligosaccharyl transferase (OST) complex that catalyzes the initial transfer of a defined glycan (Glc(3)Man(9)GlcNAc(2) in eukaryotes) from the lipid carrier dolichol-pyrophosphate to an asparagine residue within an Asn-X-Ser/Thr consensus motif in nascent polypeptide chains, the first step in protein N-glycosylation. N-glycosylation occurs cotranslationally and the complex associates with the Sec61 complex at the channel-forming translocon complex that mediates protein translocation across the endoplasmic reticulum (ER). All subunits are required for a maximal enzyme activity.
Subcellular Localization:
Endoplasmic reticulum membrane; Multi-pass membrane protein.
| 0
|
MDSPSLLEVLQVQQVEKLISPSLRFILAYFTHRYPRFLLRAYNSFDGIYLLVKLLLEKSQLKKWNATSVERRFQLKRVIAVRDSSIIAEEFPQESESATSLNGIDVLKKLFLTYCIPYLLEKCESLTTVKENHTAVSILSLQARDKQKGALSVFYSKIKILLVRLKKILHFVFRLIRKSNTYLQWLYYLLYALGKTPYTNLADHILRQRVIYNVENIHSRKLISTREKSSLLTSIADHSMEGFLIIIQLIDWWQSNNYESHLKKGEVAFTELAPPKLPFEINVSTTDICKICGEKIKNPAVLSTGFVFCYPCIQVWLQRHPFKCPVTNLELSRKGESFWRLMI
|
[
8203,
10748,
10752,
25005,
27507,
28656,
29166,
34103,
41762,
46929,
50276,
87760,
87767,
87894,
87974,
88008,
88159,
88161,
88162,
88181,
88261,
88263
] |
The following text describes a protein:
Function:
Component of a retrotranslocation channel required for peroxisome organization by mediating export of the PEX5 receptor from peroxisomes to the cytosol, thereby promoting PEX5 recycling. The retrotranslocation channel is composed of PEX2, PEX10 and PEX12; each subunit contributing transmembrane segments that coassemble into an open channel that specifically allows the passage of PEX5 through the peroxisomal membrane. PEX12 also regulates PEX5 recycling by activating the E3 ubiquitin-protein ligase activity of PEX10. When PEX5 recycling is compromised, PEX12 stimulates PEX10-mediated polyubiquitination of PEX5, leading to its subsequent degradation.
Subcellular Localization:
Peroxisome membrane; Multi-pass membrane protein.
Domain:
The three subunits of the retrotranslocation channel (PEX2, PEX10 and PEX12) coassemble in the membrane into a channel with an open 10 Angstrom pore. The RING-type zinc-fingers that catalyze PEX5 receptor ubiquitination are positioned above the pore on the cytosolic side of the complex; The RING-type zinc-finger is degenerated and only coordinates one zinc ions, preventing E3 ubiquitin-protein ligase activity.
| 0
|
MTPAEIAPKDRLIVALDLPSVDAAEAMIARLGDSVTFYKIGYRLAYAGGLPLVARLADKGKKVFLDLKLHDIGNTVAQGVESITRLGATFLTVHAYPQTMKGAVEGRGGSNLKILAVTVLTSYNEDDLHAAGFRLGVAELVEARAQQAQVLGIDGLVSSPEEVGALRKIVGHQMSLVTPGIRPAGSASGDQKRIMTPGRAITAGADYLVVGRPVVEAAEPKAIADAIQAEIGQALGA
|
[
5272,
8013,
14816,
25040,
28455,
37403,
45333,
47531,
48258,
50896,
73549,
87388,
87741,
87988,
88008
] |
The following text describes a protein:
Function:
Catalyzes the decarboxylation of orotidine 5'-monophosphate (OMP) to uridine 5'-monophosphate (UMP).
| 0
|
MHLPMEEGREKSSTQQDSEITAQDERIDPNATILSHSVLSLLVPKVEYVQGSVKEITKTQNVLAKSVEQENEKFRQIGYIHDLSNTFIRCRRCRFKLVNIRREMLNLSDRMNKLKKRAARLKSIREKQQLKQAQEEAERQAYQASLLAKPAKHLTNQN
|
[
25473,
25578,
50155,
58758,
87326,
87367,
88008
] |
The following text describes a protein:
Function:
Component of the biogenesis of lysosome-related organelles complex-1 (BLOC-1) involved in pigment granule biogenesis.
Subcellular Localization:
Cytoplasm.
| 0
|
MSLADELLADLEEAGDEGDEPGLYPGAEGADGADSDGEGGAEGPGGLADIPEEMEVDYSGTESVTSIAKLRHSKSFAEIMEKISQYIGNQRKTSEVSGPVEADPEYRLIVDANNLTVEIDNELSECPACSLPPTTLSTKGCPLFAVLCALELGNNLDKCKNNETLQQILTNATIMVVSVTASTTQGVLLGDEELLRLEEACDMALELNQSKHSIYEYVESRMSFIAPNLSIIVGASTAAKIMGIAGGLTNLSKMPACNLMLLGAQRRSLSGFSSTSLLPHTGYIYHSDIVQSLPPDLRRKAARLVSAKCTLASRVDSFHESSDGKVGYDLKEEIERKFDKWQEPPPVKQVKPLPAPLDGQRKKRGGRRYRKMKERLGLTEIRKHANRMTFAEIEDDAYQEDLGFSLGQLGKSGSGRVRQAQVNEATKARISKSLQRTLQKQSMVYGGRSTVRDRSSGTSSSVAFTPLQGLEIVNPQAAEKKVAEANQKYFSNMAEFLKVKREAKETYTE
|
[
6687,
6728,
6736,
17250,
24951,
26439,
26705,
26949,
38162,
51755,
58101,
63852,
69218,
87857,
88008,
88020
] |
The following text describes a protein:
Function:
Involved in pre-mRNA splicing as component of the spliceosome. Required for the assembly of the U4/U5/U6 tri-snRNP complex, one of the building blocks of the spliceosome.
Subcellular Localization:
Nucleus.
| 0
|
MSGDDDWWTSSNEALLVSLVTPSDTGVKTLDTFHPEYTNNIFGEKEQIFGYKGLRINLQYNASDMLPNLKVSYKKKYQPTADEEALDINEVLSEFLPEIAFQKQSDFETRLKSIPDNWTPPGTLVTSFTNKDGEYEVYSGKITDPAVKQLLNRIQILVPFFVDGGTPIDMEDPDVDRWTIYFLYNKRPLLNQPDKFSYHFAGYSTLYRYYAFQPPAESESKTPTDTPTFSVDGDFDLDTLPCRTRISQFIIIPPFQQKGLGSRLYSIIYQQYLKHEPTIELTVEDPNEAFDDMRDLADLAFLSKQPEFQALKIDTSVEIPEEGKAPSNIVDQAAWEACRKKFKIVPRQFARVLEMYLMSQLPESVRPGLGAPEDEDYEEQSGRSKSKGHEKALPKPTPEDEHTYRLWMMLVKRRLYVHNRDALGQLELKERREELAKVFAGVEFDYARLLIKAEEQGKLAQADGETAGDQVPATPSAANGKRKLDEVEQAEGTAAASSKKAKVESGHA
|
[
2673,
8065,
12059,
24785,
24917,
24978,
29733,
32042,
47303,
49230,
50281,
52007,
64820,
87125,
87302,
87367,
87374,
87380,
87857,
88008,
88153
] |
The following text describes a protein:
Function:
Catalytic component of the histone acetylase B (HAT-B) complex. Acetylates 'Lys-12' of histone H4 which is required for telomeric silencing. Has intrinsic substrate specificity that modifies lysine in recognition sequence GXGKXG. Involved in DNA double-strand break repair.
Subcellular Localization:
Cytoplasm. Nucleus.
| 0
|
MDTFKRWLNKPKADDKSLLARFFHADRSLTAVASELDSFDGRAEPDRCTRLVSRLRQNQDKVLAITNLIMEELLGEDRDPRAFRAKFPEEVLQENLAGQLWFGAECLAAGSSIMNRETESKEMRPLAQAVTKSLGNVRVLLRDQCLKNNVPNSKTLHLDLNDSTTEQLYESLKIFDRLFAEFELSYVSAMVQVKSRHEYEMQQWIGVLFSETLQRALKIGLLDQEMVDAFDPGLMFSIPRLAIVAGLVVYAKGPLNMDMPGDQLSEMFRPFRTILIKIRDLLRNLNNQELYQLEKLLCTNEDINTKVPLGSSSIEAPSPEHSSHPTTSSSQNNNNSSNNNHSSSSTNTTSTTTTTAGTTNTHRTVERLVDQRNNNHNSNSNSSTNPTVEAATLRSPSMLSLSATSTPTASPAPSPTPSHSIASTSSAATSSTNPPADWSDGDDEDEDDDDIDVDEEDIESSDDGTDEEQLLKDIVSADCASGYLIPNTNLGNLLQPQEVPLTDNFVASEDDEYGTAEQQGHQGLEEDEPSTSAAMLAATRTLQRLRLPSSDNEPLAEPTTIKASEEHMQQPSGRHRDSHSHRHHQRHHHHHHHRHPHQHQHRQPHPHRTTRSGRKRCSLEAADPERIQPDREQNLASGDTSAASSLSDDVSLAMRNTTARLKFKSTENLLHRLFVCIAGVADQLQTNFASDLRQILRSVFLMNMSTAQEEIDIPEKTKESELFEFRASENDVIQESAGSNQSIYSAEEVNPELDNVFSAGGGNQATGQRHSAGASMQRNNTIDLASQPGEGSPSGATTATSRSHVTRSRSLGDQEAASSATSSTAQLRQLEQQQQQQQLQIQLQRQRNNSVGSNTPSSASSTSSSSEQNSPVSARSGSRRRLQSNNETQMPSSATSTSATLSPPAWIPDGKAPRCMACQTPFTAFRRRHHCRNCGGVFCGVCSNASAPLPKYGLTKAVRVCRDCYVREVRSGMGVQGVQSVQSVQASAS
|
[
14048,
25696,
29166,
36191,
45292,
46929,
50341,
69910,
76772,
87767,
87914,
88008,
88261,
88263
] |
The following text describes a protein:
Function:
Negative regulator of epidermal growth factor receptor (EGFR) signaling.
| 0
|
MSKEKLPFVVTAGQMRSAEEAAVVRGTTWAALMEQAGAGVADAVLRYAAPLANRQVLVLVGPGNNGGDALVAARHLADAGALVTLYVWRRSGVDANLQACRERAIPELSAATDGDGSLLAQALRKAVLVLDGLLGTGARPPTADLATIIQAVNAERTQRSDLRVVAIDLPSGVGADDGQVPTVAIRADLTVATGLIKRGLLLWPGRGYAGEIVVAPIGLSSLDGVLTMSELLTASQARTLLPPRPADAHKGVFGKVLVVAGSINYPGAAVLACAGAQRSGAGLVTLATGRTVLSLATLPPEVTLLPVAEGDWGAIGPAAVDDLAEHLPGYQALLLGPGLGQAEATRKLVLRLFGLDHTRSRARVGFVAVGEPLTNQPQQTVALPPTVIDADGLNILATAADWFERLPPEHCVLTPHPGEMRRLLGVSELPADRVATAAEAAQRWRQTVVLKGATTVIAAPDGRTLMYDGANPALATAGSGDVLAGVIAGLIAQGCLPFAAAALGVYLHGAAGARARMAFGDAGVVAGDLLPLLPSVMQELRTG
|
[
5481,
6053,
15698,
20693,
25325,
29033,
30159,
32536,
33991,
33992,
36459,
39602,
50795,
59222,
59915,
64395,
87012,
87016,
87110,
87683,
87694,
87741,
87760,
87767,
87814,
87822,
87823,
87855,
87945,
88008,
88153,
88159,
88161
] |
The following text describes a protein:
Function:
Bifunctional enzyme that catalyzes the epimerization of the S- and R-forms of NAD(P)HX and the dehydration of the S-form of NAD(P)HX at the expense of ADP, which is converted to AMP. This allows the repair of both epimers of NAD(P)HX, a damaged form of NAD(P)H that is a result of enzymatic or heat-dependent hydration; Catalyzes the dehydration of the S-form of NAD(P)HX at the expense of ADP, which is converted to AMP. Together with NAD(P)HX epimerase, which catalyzes the epimerization of the S- and R-forms, the enzyme allows the repair of both epimers of NAD(P)HX, a damaged form of NAD(P)H that is a result of enzymatic or heat-dependent hydration; Catalyzes the epimerization of the S- and R-forms of NAD(P)HX, a damaged form of NAD(P)H that is a result of enzymatic or heat-dependent hydration. This is a prerequisite for the S-specific NAD(P)H-hydrate dehydratase to allow the repair of both epimers of NAD(P)HX.
| 0
|
MAKSSLGQDSDSTAAVAVLKRAVELDAESRYQQALVCYQEGIDMLLQVLKGTKESSKRSTLRTKISGYMDRAENIKKYLDQEKEDGKYHKQIKIEENATGFSYESLFREYLQETVTEVWIEDPYIRQTHQLYNFLRFCEMLIKKPCKVRTIHLLTSGDEGFGNTQQSSGLEEIKQSLRSHGVVLEINYSSSIHDREIRFNNGWMIKIGRGLDYFKKPQGRFSLGYCDLDLRPCHETTVDIFHNKHTKKI
|
[
6697,
18246,
25325,
25506,
25697,
30814,
31754,
32073,
42175,
61110,
63953,
65631,
71541,
78465,
87272,
87273,
87434,
87760,
88008,
88162
] |
The following text describes a protein:
Function:
Required for efficient abscission at the end of cytokinesis, together with components of the ESCRT complexes. Seems not to be involved in endosomal transport (By similarity).
Subcellular Localization:
Late endosome membrane; Peripheral membrane protein; Cytoplasmic side. Midbody. Membrane; Peripheral membrane protein; Cytoplasmic side. Note=During cytokinesis, recruited to the midbody via interaction with CHMP1A. Interacts with membranes enriched in phosphoinositides (By similarity).
Domain:
The C-terminal domain interacts with lipid membranes containing acidic phosphoinositides and is required for location at the midbody; The MIT domain interacts with the MIT-interacting motifs of several components of the ESCRT-III complex.
| 0
|
MALNAPSGSCSSKVLLHPLVIMQMSEHYSRTKVQQGPTVKKVFGAILGRQNGRQVEAINSFVLKMETEEMAEPVTFSTEHLLQRADQYLEVFPELQVIGLYCAGEDDNLTPEEKPLLSKLTNAVRNSEKAGQIDATLFLKLNSITAGTTRKLPLFAFEADVTDQEKHKPIEWILVSEESERVGVNHIAKLSTKHGKDGKSVGKKHAEAQDAAMSMLQNRVDLIVAYLEKVQDGTLQPNFEILKEANLLAQKLKTIDRYAAEFTDSFEKEEKTMTVFSLMPRLTTLLGNMQNVWNKLSAQRADLLADDGFHGKSTSRWAHPVRFKSQHLGRPQQADDDDYFDDEDLENDMSGPRRKIHAADSPAGSRRRRVPPRAMNFLGRNSGMQAATDEMELSGQEENMGSNYIPDVPRPSATAHNESDESSQAS
|
[
16123,
17352,
23703,
24917,
24978,
25142,
29148,
36397,
56492,
65177,
87367,
87402,
87407,
87857,
87863,
88008,
88062
] |
The following text describes a protein:
Function:
Component of the COP9 signalosome complex (CSN), a complex involved in various cellular and developmental processes. The CSN complex is an essential regulator of the ubiquitin (Ubl) conjugation pathway by mediating the deneddylation of the cullin subunits of the SCF-type E3 ligase complexes, leading to decrease the Ubl ligase activity of SCF. The CSN complex plays an essential role in embryogenesis and oogenesis and is required to regulate microtubule stability in the early embryo. Mediates mei-3/katanin targeting for degradation at the meiosis to mitosis transition via deneddylation of cul-3.
Miscellaneous:
MISCELLANEOUS: Although strongly related to metalloprotease proteins, it lacks the JAMM motif that probably constitutes the catalytic center. Its function as protease is therefore unsure.
Subcellular Localization:
Cytoplasm. Nucleus.
| 0
|
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