wanglab/gogpt-training-data huggingface dataset:
Protein: SD04152p (Q7YU77)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MCERNNNKQVTSSNKIPSSFNAKLELDSSKDDTIHSTSLNKKLVKIKKFKLDDMKEMVGGCCVCSDERGWPENPLVYCDGQNCTVAVHQACYGIVTVPTGPWYCRKCESQERTSRVRCELCPSRDGALKKTDNSGWAHVVCALYIPEVRFGNVTTMEPIILSLIPQERYSKTCYICQEIGKPNRANVGACMQCNKSNCKQQFHVTCAQSLGLLCEEAGNYLDNVKYCGYCQHHYSKLKKGGNVKTIPPYKPIQHDTSSDSCSSPEKEIDSTMNSATTSATIIKITSSSGSAGGSSNVLNASSSAGISAGSSSGSGVSSSAKQRKSNASSKSSSSSSSSSSSSTGGAPNPSSSSVHSGSASNMTGGGSVLPGSSNIGNISNSLNNNLPGGSSSTSSAGNVPGGSGGIISASSGGATQSTSSQSSTAPGTTKSSASSSSSSSNSYKEKHSKSLSKSTSSKDKDGKDSSTNSANNNFTNSSASSTSSNSSSTREKSSSKLSKNKDSNQVPSATSSLSTTSSINTQPSSSTATAGSGGTGTHVSSSAASGLNSAPSTTNEHSNHAHTLSTNGTGAGSAAGKLQSVSNLSNSSSGFGSDLRSVSTSSSSTVNDSTGGFGSNSNSERENLSGAGSSASNMPGTIAPGTGGVSSSAATNLSTNKGGSSSSTANSLTSTSTSSGSSSNSSSKKRKADSAKSTSSISTSGSALEDNNSLISRYDIKDVQVALTPLTDFEKEIEKSSKRQRTELSPPTHQTSATAEVNAPLASSTSASIAVTASATAASAPPATGTTTLGSSISGNAGSTSSGNSSGVSATGGAQSAVGSGGYPKTESSKSSGTASAGSGSGSSSNTSSTKHGSNIKDISSSSNQQASTASSSSAPSLYVSVPLSTANVPGINLPTSSTSSSTTSESHSASSRSSGAQSQHQQQLSNALVGPPMGGSAGAFHGGTTSAGSSSVIQQQSGKSSPALGTLVSGNSGGSIISASGFPLPSGNLTATTTESGNLKISYEKQTTRVQQLQEQEAPPARRSRTLDLSTASASSSSPSAVPATTSPLVVLSNQLPLNSVAASSSTGGLKFTYESQTQMDVPMMPVSAIKDSPPSSPGSEIGSAMHSATTAPGSLTGASTAATAQPGNVRKRGRKAKDATIAAAAAAAAAAAALSNSQQDLKDVRILQNGASNTPGNPAGSTPTPPATPASSNAVSSASSIITHTAAHMLGNQINPNSSVAQKLSEQLHMEVQDHSIYTPDSMNSQYAGVPFPGKQRNSTAVPSNATPAQNPLQSMFSGGGMNGNMPIPQSLEQLLERQWEQGSQFLMEQAQHFDIASLLNCLHQLQSENLRLEEHVTSLIARRDHLLAVNARLQIPLSTIASNTKAEAHGK
Protein: Large envelope protein (L glycoprotein) (L-HBsAg) (LHB) (Large S protein) (Large surface protein) (Major surface antigen) (P03139)
Organism: Hepatitis B virus genotype D subtype adw (isolate United Kingdom/adyw/1979) (HBV-D)
Function: The large envelope protein exists in two topological conformations, one which is termed 'external' or Le-HBsAg and the other 'internal' or Li-HBsAg. In its external conformation the protein attaches the virus to cell receptors and thereby initiating infection. This interaction determines the species specificity and liver tropism. This attachment induces virion internalization predominantly through caveolin-mediated endocytosis. The large envelope protein also assures fusion between virion membrane and endosomal membrane. In its internal conformation the protein plays a role in virion morphogenesis and mediates the contact with the nucleocapsid like a matrix protein.
Subcellular location: Virion membrane {ECO:0000255|HAMAP-Rule:MF_04075}.
Interaction partners:
Sequence:
MGQNLSTSNPLGFFPDHQLDPAFRANTNNPDWDFNPNKDTWPDANKVGAGAFGLGFTPPHGGLLGWSPQAQGIMQTLPANPPPASTNRQSGRQPTPLSPPLRTTHPQAMHWNSTTFHQTLQDPRVRGLYFPAGGSSSGTVNPVPTTTSPISSIFSRIGDPALNMENITSGFLGPLLVLQAGFFLLTRILTIPQSLDSWWTSLNFLGGTTVCLGQNSQSPISNHSPTSCPPTCPGYRWMCLRRFIIFLFILLLCLIFLLVLLDYQGMLPVCPLIPGSSTTSTGSCRTCTTPAQGISMYPSCCCTKPSDGNCTCIPIPSSWAFGKFLWEWASARFSWLSLLVPFVQWFVGLSPIVWLSVIWMMWYWGPSLYSILSPFLPLLPIFFCLWAYI
Protein: X11Lbeta, isoform A (Q9W2S5)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
- Peripheral plasma membrane protein CASK
- Protein ROP
- Syntaxin-1A
- FI17352p1
Sequence:
MVSTTLTTLAAGQTTSSSNHHHHHHHSHQQQQQQQQQDQSQQQPHQQLPYQQRGYYALNGSLELDCDTSNTNSSSSSNNIGYQQHQQQQQQQQQPPLILSQALLSPSPPLNDQISLLFPKCRPKQQQQQQQQQQQQQQQQQQQLQPAQQHQQHVHPTDVNSSCNSNRSSSPTTAGAVGEPLASVSVSPPPPKATPTSSTPSYYKSVNIITQSPPPHSASSHSSESLSSVTPRISTNPFLCAPLTPPTPPHHHHHHHHQQQHQQKQQQPKQQHQTQQQEQQEEDTTGESVVEHSRSGAAGEVLEYPASFYYHTVGDSRRGPGSYTEMPRKRSSALPASNRQQQLHNGNGSQNPFIKENYWEAPPTRASLLLHSPTEYSEEPQQQQQIQQQQQQQQQQQQQQQQQQQQHLHASARRAYHQQREQVYGINQRPQQQQQQNILRVGRSPVNRSFPQQHQQQQQQQQQQQQQQQQQQQPHQQIPTARSNPCADGLTPLASHYLYGSKSSLDQHPGDWEPREQRKLRLREEREREREREREREREREREHLLLEQQQQLQLQEVQVARDNHLSHLAGQQQQQQQRKRHVYGEERERERDRERDMDRDHRLVNGNADPNESWQHLRVTTETLAEEGGKHGKPADKAQHQMHNTNQSQNSDVNVYREHQLDAWKLERSYTLAVESRHGIIEYEGSPRRIGVTTTSNLGATGAAAASAAADESEPPAAAEGAAAATATSQPQQQVPMATVPPLSSTATSLQKTAARAALAALAQSHPHSSHNILSTLLPHSPNPVNPGQMHAAQQSIQNYPVRPGFPQRIISPPSRDPRSSSPPLQQQQYQQQQQQQLQHQQQHFASLMSSHSNNNSNTNKQPLSSDNNAEDTSNDVSEIGTISDLTTPEAVGLSIGIAAGEMASRASTPPQTAQAPPTAVAGSTANGTGSGNGTATGNATAAGSGLGPLSLHTKSSTFDYLYEFSETRKVLEEFFKCPSTDEQPIMENGSDVDSIDIQYEFHSNFERDEEDLAEEEEAEDDEEVDDDADEENDEAEDEDEPLEQDRDQNYRAQAPPQSGHIDSERLVYSGYGQQPQLQAQLTAQPMSGARRHYSGSPLMRDFDFFLDSTSRSSGERDADQDGLNHNQLLSTSSGHGGGVGVSGGLGVGPGGGHNYRYSPETTDYDSNCGDLDSLSGEMNGGVSTSCSNYAKFYASAMPVLEDGLSSGHTSDTENNNNNQKNLQQSTVNQGGQCPTSLSGSTSIGGSGGISMLMDMKRISTNHSLNSMNNQTTTASTTTDSNGGVGGVGHHLVATLVASPNNEQAKSQCQTQLQSHPPKTLSLDQSPSNHSKVFKNIDPELDSLYSIGVFHRPDTVQMTPPPPAPAPHRKPNNNGCSSGVVNTNGSLAGGSNDVDLLQPSSKHTPLAAAISSTLQRSSPTSTITGNGIGNGSGKTRSAGSNCSSSANGGMPPPIPERTNLVSAVQRSPSPGPNSPVWLSRHLDGGAGKDLLESGSDNHSKNHSADEEDVDTDLETDRLLGHQRLDDQGYYDENKSWDRKPRSLLSKISPKQQIPSTKTRNGYNALLSSTPELPPPIPPKGQSGLGLGLTLGAGNGGKLLDLVGGMVQRSLSRSSSEHSEKSLSKMPISGGDLCAGGVDVVASTVAATSATVVASTPALGSPGNGGGSERSAAEMANPGGAVKLSEQEIGTINGGSVMPLGSGSGTGSGAGSGAGSGTGTNAAVVANSNANNNVGGGGGGGNNSSGSGAGSNSNSGEKKVKKSKSKEGGAVLIEGVLFRAKYLGSTQLVCEGQPTKSTRMMQAEEAVSRIKALAPDGDVQPSTEVDLFISTEKIMVLNTDLKEIMMDHALRTISYIADIGDLVVLMARRRFVPQDIDDAPKPNRTPKMICHVFESDEAQFIAQSIGQAFQVAYMEFLKANGIEDHRFVKEMDYQEVLNSQEIFGDELEIFAKKELQKEVVVPKAKGEILGVVIVESGWGSMLPTVVIANLMSSGAAARCGQLNIGDQLIAINGLSLVGLPLSTCQTYIKNTKNQTVVKFTVVPCAPVVEVKIKRPETKYQLGFSVQNGVICSLLRGGIAERGGVRVGHRIIEINNQSVVAVPHEKIVNLLATSVGEILMKTMPTSMFRLLTGQENPIYI
Protein: Probable serine/threonine-protein kinase PBL10 (EC 2.7.11.1) (PBS1-like protein 10) (Protein kinase 1B) (P46573)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Possible bi-functional kinase. In vitro, it exhibits serine/threonine activity. In vivo, can phosphorylate tyrosine residues of limited substrates (By similarity). May be involved in plant defense signaling (By similarity). Required for full light-induced stomatal opening.
Subcellular location: Cell membrane {ECO:0000250|UniProtKB:O48814}; Lipid-anchor {ECO:0000250|UniProtKB:O48814}.
Interaction partners:
- Pectate lyase
- IQ domain-containing protein IQM3
- THO complex subunit 4D
Sequence:
MGICLSAQIKAVSPGASPKYMSSEANDSLGSKSSSVSIRTNPRTEGEILQSPNLKSFTFAELKAATRNFRPDSVLGEGGFGSVFKGWIDEQTLTASKPGTGVVIAVKKLNQDGWQGHQEWLAEVNYLGQFSHPNLVKLIGYCLEDEHRLLVYEFMPRGSLENHLFRRGSYFQPLSWTLRLKVALGAAKGLAFLHNAETSVIYRDFKTSNILLDSEYNAKLSDFGLAKDGPTGDKSHVSTRIMGTYGYAAPEYLATGHLTTKSDVYSYGVVLLEVLSGRRAVDKNRPPGEQKLVEWARPLLANKRKLFRVIDNRLQDQYSMEEACKVATLALRCLTFEIKLRPNMNEVVSHLEHIQTLNEAGGRNIDMVQRRMRRRSDSVAINQKPNAGFARQTAVGVIATAYPRPSDSPLFV
Protein: Rho GTPase-activating protein 19 (Rho-type GTPase-activating protein 19) (Q14CB8)
Organism: Homo sapiens (Human)
Function: GTPase activator for the Rho-type GTPases by converting them to an inactive GDP-bound state.
Subcellular location: Nucleus {ECO:0000269|PubMed:17454002}.
Interaction partners:
- Transforming protein RhoA
Sequence:
MATEAQSEGEVPARESGRSDAICSFVICNDSSLRGQPIIFNPDFFVEKLRHEKPEIFTELVVSNITRLIDLPGTELAQLMGEVDLKLPGGAGPASGFFRSLMSLKRKEKGVIFGSPLTEEGIAQIYQLIEYLHKNLRVEGLFRVPGNSVRQQILRDALNNGTDIDLESGEFHSNDVATLLKMFLGELPEPLLTHKHFNAHLKIADLMQFDDKGNKTNIPDKDRQIEALQLLFLILPPPNRNLLKLLLDLLYQTAKKQDKNKMSAYNLALMFAPHVLWPKNVTANDLQENITKLNSGMAFMIKHSQKLFKAPAYIRECARLHYLGSRTQASKDDLDLIASCHTKSFQLAKSQKRNRVDSCPHQEETQHHTEEALRELFQHVHDMPESAKKKQLIRQFNKQSLTQTPGREPSTSQVQKRARSRSFSGLIKRKVLGNQMMSEKKKKNPTPESVAIGELKGTSKENRNLLFSGSPAVTMTPTRLKWSEGKKEGKKGFL
Protein: SH3-containing GRB2-like protein 3-interacting protein 1 (Endophilin-3-interacting protein) (P0DJJ3)
Organism: Rattus norvegicus (Rat)
Function: May function in clathrin-mediated endocytosis. Has both a membrane binding/tubulating activity and the ability to recruit proteins essential to the formation of functional clathrin-coated pits. Has a preference for membranes enriched in phosphatidylserine and phosphoinositides and is required for the endocytosis of the transferrin receptor. May also bind tubulin. May play a role in the regulation of energy homeostasis.
Subcellular location: Membrane, clathrin-coated pit {ECO:0000250|UniProtKB:Q9BQI5}; Peripheral membrane protein {ECO:0000250|UniProtKB:Q9BQI5}; Cytoplasmic side {ECO:0000250|UniProtKB:Q9BQI5}.
Interaction partners:
- Epidermal growth factor receptor pathway substrate 15
- Synaptojanin-1
- Epidermal growth factor receptor substrate 15-like 1
- Disabled homolog 2
- Intersectin 2
- WD repeat domain 31
- AP2-associated protein kinase 1
- AP-2 complex subunit alpha
- AP-2 complex subunit beta
- Adaptin ear-binding coat-associated protein 1
Sequence:
MMEGLKKRTRKAFGIRKKEKDTDSTGSPDRDGMQPSPHEPPYHSKAECAREGGKKASKKSNGAPNGFYAEIDWERYNSPELDEEGYSIRPEEPGSTKGKHFYSSSESEEEEESHKKFNIKIKPLQSKDVLKNAATVDELKASIGNIALSPSPVRKSPRRSPGAIKRNLSSEEVARPRRSTPTPELTSKKPLDDTLALAPLFGPPLESAFDEQKTEVLLDQPEIWGSGQPINPSMESPKLARPFPTGTPPPLPPKAVPATPPRTGSPLTVATGNDQAATEAKIEKLPSISDLDSIFGPVLSPKSVAVNTEEKWVHFSDASPEHVTPELTPREKVVTPPAASDIPADSPAPGPPGPPGSAGPPGPPGPRHVPSPLNLEEVQKKVAEQTFIKDDYLETLSSPKECGLGQRATPPPPPPPTYRTVVSSPGPGSGSGTGTASGASSPARPATPLVPCSSTTPPPPPPRPPSRPKLPPGKPGVGDVSRPFSPPIHSSSPPPIAPLARAESTSSISSTNSLSAATTPTVENEQPSLVWFDRGKFYLTFEGSSRGPSPLTMGAQDTLPVAAAFTETVNAYFKGADPSKCIVKITGEMVLSFPAGITRHFANNPSPAALTFRVINSSRLEHVLPNPQLLCCDNTQNDANTKEFWVNMPNLMTHLKKVSEQKPQATYYNVDMLKYQVSAQGIQSTPLNLAVNWRCEPGSTDLRIDYKYNTDAMTTAVALNNVQFLVPIDGGVTKLQAVLPPAVWNAEQQRILWKIPDISQKSENGGVGSLLARFQLSEGPSKPSPLVVQFTSEGSTLSGCDIELVGAGYRFSLIKKRFAAGKYLADN
Protein: Medium-chain fatty acid ethyl ester synthase/esterase 1 (Alcohol O-acetyltransferase) (EC 2.3.1.84, EC 3.1.1.-) (Ethyl ester biosynthesis protein 1) (Q02891)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Displays enzymatic activity both for medium-chain fatty acid (MCFA) ethyl ester synthesis and hydrolysis (esterase activity). MCFA are toxic for yeast and this enzyme could thus be involved in their detoxification by esterification.
Interaction partners:
- Alcohol O-acetyltransferase 1
- Isoamyl acetate-hydrolyzing esterase
- Ethanol acetyltransferase 1
- Branched-chain-amino-acid aminotransferase, cytosolic
Sequence:
MFRSGYYPTVTPSHWGYNGTVKHVLGEKGTKSLAFRDSKRQIPLHEFVTKHVPTLKDGANFRLNSLLFTGYLQTLYLSAGDFSKKFQVFYGREIIKFSDGGVCTADWVMPEWEQTYSLNAEKASFNEKQFSNDEKATHPKGWPRLHPRTRYLSSEELEKCHSKGYSYPLVVVLHGLAGGSHEPLIRALSEDLSKVGDGKFQVVVLNARGCSRSKVTTRRIFTALHTGDVREFLNHQKALFPQRKIYAVGTSFGAAMLTNYLGEEGDNCPLNAAVALSNPWDFVHTWDKLAHDWWSNHIFSRTLTQFLTRTVKVNMNELQVPENFEVSHKPTVEKPVFYTYTRENLEKAEKFTDILEFDNLFTAPSMGLPDGLTYYRKASSINRLPNIKIPTLIINATDDPVTGENVIPYKQARENPCVLLCETDLGGHLAYLDNESNSWLTKQAAEFLGSFDELVL
Protein: (-)-alpha-terpineol synthase, chloroplastic (EC 4.2.3.111) (Q84KL4)
Organism: Pinus taeda (Loblolly pine)
Function: Involved in defensive oleoresin formation in conifers in response to insect attack or other injury. Involved in monoterpene (C10) olefins biosynthesis. Produces 57.3% alpha-terpineol (15.1% (+)/84.9% (-)), 27.6% limonene (25.2% (+)/74.8% (-)), 8% terpinolene, 4.7% beta-pinene (14.8% (+)/85.2% (-)), 1.3% alpha-pinene (100% (+)) and 1.1% myrcene.
Subcellular location: Plastid, chloroplast {ECO:0000305}.
Interaction partners:
Sequence:
MDLISVLPSASKSCVCLHKPLSSSTHKLKPFCKTIRILVMPRRWEFARPSMSLSTVASEDDIQRRTGGYLSNLWNDDVIQFLSTPYGELAYRERAERLIDEVRDIFSSMSLEDGEFSDLIQRLWMVDNVERLGIDRHFKNEIKSALDYVYSYWSEKGIGCGTKSIITNLNSTALGFRTLRLHGYPVSADVLKHFRNQIGQFVSCPSETEEDIRIMVNLYRASLIAFPVAFPGEKVMEEAESFSEKYLKETLQKIPDCSLSREIGDVLEHGWHTNLPRLEARNYIDVFGQDTKNMEPNRKTEKLLELAKLEFNIFQSIQKTELESLLRWWNDSGSPQITFTRHRHVEYYTLASCIAFEPQHSGFRLGFAKACHILTVLDDMYDLFGTVDELKLFTAAIKRWDPSATDCLPQYMKGIYMMVYNTVNEMSAEAQKAQGRDTLNYARQAWEDCLDSHMQEAKWIATGFLPTFEEYLENGKVSSAHRVSALQPMLTMDIPFPPHILKEVDFPSNLNDLACAMLRLRGDTRCYQADRARGEETSCISCYMKDNPGATEEDALNHLNVMISGVIKELNWELLKPNSSVPISSKKINFDITRAFHYGYKYRDGYSVSSVETKSLVMRTLLEPVPL
Protein: Sll1306 protein (P73597)
Organism: Synechocystis sp. (strain ATCC 27184 / PCC 6803 / Kazusa)
Interaction partners:
- Putative carboxypeptidase slr1534
- GDP-mannose 4,6-dehydratase
- Sll1305 protein
- PilJ protein
- Pyruvate kinase 2
- Sll1785 protein
- Probable ketose 3-epimerase
Sequence:
MQRRDLFKYGLATGAGAIASYALMGNKPLLAQQSSNRGGKFWPDNIRLPISLSLMFETGSQPAKGAPTPFGNFTPPPDYYDMPTITWYRYGYTEGVPRILDLLDKYKIKITSHMSGRTVEMYPDRAKEIVQRGHEAAAHGWDWDNEFNMTAPQERDFIQRNVDIILKVTGQRAVGYNAPGLRGSVNILTVLNELGFVYHIDDVSRDEPFIVNLNNGKSIMVVPYAVYLNDIRAYEARFFSSGQYLTELKNSFDRLYEEAAYRRRMMAVTMHDRLQRPEHVYVFEDFLKYVMAKPGVAFMKKIDIANFALNDPNTIREDIQNVYPNVPNFVPSATS
Protein: Conserved hypothetical alanine rich protein (O33329)
Organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Interaction partners:
Sequence:
MSTFRECRSMFDAAVKSYQSGDLANARAAFGRLTVENPDMSDGWLGLLACGDHHLDTLAGAHQHSEALYSETRRVGLTDGELSAVVMAPMYLGLRVWSRATIGLAYASALIIADRHDEAAATLDDPVITEDTGAAQYRQFVMATLFHKTRSWSNLLKVTEISPPSGATDVRDEVADAVAALASTAAASLGQFQFALELAEQVSTTNPRVTADVTLTRAWCLRELGDDDAARVALSATTTGDAPRTNTTAEQAGSPQPKFRHPYDDGRDLLVARRRPPAGDGWRKAVTKMTFGRVNPEPSAKREQTDELIQRICAPLADVHKLAFVSAKGGVGKTTMTVLVGNAVARLRGDRVMAVDVDADLGDLSARFSERGGPQTNIEHFVSSQHTKRYADVRVHTVMNKDRLEMLGAQNDPRSTYKFGPEDYGAAMQILETHCNVILLDCGTPVNGPLFSNILNDVTGLVVVASEDVRGVEGALVTLDWLGAHGFGRLLQHTVVVLNAIQKTRSLVDCGAAENQFRKRVPDFFRIPYDPHLATGLAVDFSSLKRRTRNAVLDLAGGLAQHYPASRVRPRGEDSWKTWIETMRQVG
Protein: Snake venom vascular endothelial growth factor toxin (svVEGF) (PM-VEGF) (TM-VEGF) (VEGF-F) (Q330K6)
Organism: Protobothrops mucrosquamatus (Taiwan habu) (Trimeresurus mucrosquamatus)
Function: Snake venom VEGFs may contribute to venom dispersion and prey subjugation by inducing vascular permeability and hypotension. This protein activates the vascular endothelial growth factor receptor-1 (VEGFR-1/FLT1), and consequently promotes the proliferation and tissue factor production of endothelial cells, the neovascularization in the chicken chorioallantoic membrane, and increases vascular permeability. Also stimulates tissue-factor production and human monocyte chemotaxis.
Subcellular location: Secreted {ECO:0000269|PubMed:15711751}.
Interaction partners:
Sequence:
MAVYLLAVAILFCIQGWPSGTVQGEVMPFMEVYDRSACQTREMLVPILKEYPNEVSHLFKPSCVPVLRCGGCCSDESLTCTATGKRSVGREVMRVDPHKGTSKIEVMQFKEHTACECRPRSPGDVNDGRNPKEGEPRARFPFV
Protein: NADH-ubiquinone oxidoreductase chain 1 (EC 7.1.1.2) (Q8HCR7)
Organism: Oryza sativa subsp. japonica (Rice)
Subcellular location: Cell membrane {ECO:0000256|RuleBase:RU000471}; Multi-pass membrane protein {ECO:0000256|RuleBase:RU000471}. Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
Interaction partners:
- NADH dehydrogenase iron-sulfur protein 3
- NADH dehydrogenase flavoprotein 1, mitochondrial
- NADH-ubiquinone oxidoreductase chain 3
- NADH-ubiquinone oxidoreductase chain 5
- NADH dehydrogenase iron-sulfur protein 3
- NADH-ubiquinone oxidoreductase chain 4
- NADH-ubiquinone oxidoreductase 75 kDa subunit, mitochondrial, putative, expressed
- NADH dehydrogenase iron-sulfur protein 2
- Os05g0509200 protein
- NADH-ubiquinone oxidoreductase 23 kDa subunit, mitochondrial, putative, expressed
Sequence:
MYIAVPAEILCLILPLLLGVAFLVLAERKVMAFVQRRKGPDVVGSFGLLQPLADGLKLILKEPISPSSANFFLFRMAPVATFMLSLVAWAVVPFDYGMVLSDLNIGLLYLFAISSLGVYGIIIAGWSSNSKYAFLGALRSAAQMVSYEVSIGLILITVLICVGSCNLSEIVMAQKQIWFGIPLFPVLVMFFISCLAETNRAPFDLPEAEAELVAGYNVEYSSMGFALFFLGEYANMILMSGLCTLLFLGGWLPILDLPIFKKIPCSIWFSIKVLFFLFLYIWVRAAFPRYRYDQLMGLGWKVFLPLSLAWVVSVSGVLVTFRWLP
Protein: Acyl-coenzyme A thioesterase 13 (EC 3.1.2.2) (Novel protein similar to vertebratethioesterase superfamily member 2 (THEM2)) (Q1LWU4)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Interaction partners:
Sequence:
MASLTLNAVKQIFRAMADSPGFDRVLSKVSVVEVLSAAPGKVVCEMKVEEQHTNRGGTLHGGMTATLVDMISTMAIMYSERGAPGVSVDMNITYMNAAKIGEDILITAQVLKQGRTLAFATVDLTNKANGKLIAQGRHTKHLGS
Protein: Small ribosomal subunit protein uS8c (30S ribosomal protein S8, chloroplastic) (Q6END8)
Organism: Oryza nivara (Indian wild rice) (Oryza sativa f. spontanea)
Function: One of the primary rRNA binding proteins, it binds directly to 16S rRNA central domain where it helps coordinate assembly of the platform of the 30S subunit.
Subcellular location: Plastid, chloroplast.
Interaction partners:
- Small ribosomal subunit protein uS11c
- 40S ribosomal protein S16
- Small ribosomal subunit protein uS12c
- Uncharacterized protein
- Large ribosomal subunit protein uL14c
- Small ribosomal subunit protein uS7cz/uS7cy
- Small ribosomal subunit protein eS21
- Small ribosomal subunit protein uS2c
- Small ribosomal subunit protein uS2c
- Small ribosomal subunit protein eS31 domain-containing protein
Sequence:
MGKDTIADLLTSIRNADMNKKGTVRVVSTNITENIVKILLREGFIESVRKHQESNRYFLVSTLRHQKRKTRKGIYRTRTFLKRISRPGLRIYANYQGIPKVLGGMGIAILSTSRGIMTDREARLNRIGGEVLCYIW
Protein: Deoxynogalonate monooxygenase (EC 1.13.12.22) (12-deoxy-nogalonic acid oxygenase) (Cofactor-independent monooxygenase SnoaB) (O54259)
Organism: Streptomyces nogalater
Function: Involved in the biosynthesis of the anthracycline (aromatic polyketide) antibiotic nogalamycin. Catalyzes the oxygenation of 12-deoxy-nogalonic acid at position 12 to yield nogalonic acid.
Interaction partners:
Sequence:
MPTRVNDGVDADEVTFVNRFTVHGGPAEFESVFARTAAFFARQPGFVRHTLLRERDKDNSYVNIAVWTDHDAFRRALAQPGFLPHATALRALSTSEHGLFTARQTLPEGGDTTGSGHR
Protein: Galactosylgalactosylxylosylprotein 3-beta-glucuronosyltransferase 1 (EC 2.4.1.135) (Beta-1,3-glucuronyltransferase 1) (Glucuronosyltransferase P) (GlcAT-P) (UDP-GlcUA:glycoprotein beta-1,3-glucuronyltransferase) (GlcUAT-P) (Q9P2W7)
Organism: Homo sapiens (Human)
Function: Involved in the biosynthesis of L2/HNK-1 carbohydrate epitope on glycoproteins. Can also play a role in glycosaminoglycan biosynthesis. Substrates include asialo-orosomucoid (ASOR), asialo-fetuin, and asialo-neural cell adhesion molecule. Requires sphingomyelin for activity: stearoyl-sphingomyelin was the most effective, followed by palmitoyl-sphingomyelin and lignoceroyl-sphingomyelin. Activity was demonstrated only for sphingomyelin with a saturated fatty acid and not for that with an unsaturated fatty acid, regardless of the length of the acyl group.
Subcellular location: [Isoform 1]: Golgi apparatus membrane {ECO:0000250|UniProtKB:O35789}; Single-pass type II membrane protein {ECO:0000250|UniProtKB:O35789}. Secreted {ECO:0000250|UniProtKB:O35789}.; SUBCELLULAR LOCATION: [Isoform 2]: Golgi apparatus membrane {ECO:0000250|UniProtKB:O35789}; Single-pass type II membrane protein {ECO:0000250|UniProtKB:O35789}. Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:O35789}. Secreted {ECO:0000250|UniProtKB:O35789}.
Interaction partners:
- Carbohydrate sulfotransferase 10
- Neural cell adhesion molecule 1
- Beta-1,4-galactosyltransferase 1
- Beta-1,4-galactosyltransferase 2
- Beta-1,4-galactosyltransferase 3
- Galactosylgalactosylxylosylprotein 3-beta-glucuronosyltransferase 2
- T-cell-specific surface glycoprotein CD28
- CD27 antigen
- T-cell surface glycoprotein CD8 alpha chain
- C-X-C chemokine receptor type 5
Sequence:
MPKRRDILAIVLIVLPWTLLITVWHQSTLAPLLAVHKDEGSDPRRETPPGADPREYCTSDRDIVEVVRTEYVYTRPPPWSDTLPTIHVVTPTYSRPVQKAELTRMANTLLHVPNLHWLVVEDAPRRTPLTARLLRDTGLNYTHLHVETPRNYKLRGDARDPRIPRGTMQRNLALRWLRETFPRNSSQPGVVYFADDDNTYSLELFEEMRSTRRVSVWPVAFVGGLRYEAPRVNGAGKVVGWKTVFDPHRPFAIDMAGFAVNLRLILQRSQAYFKLRGVKGGYQESSLLRELVTLNDLEPKAANCTKILVWHTRTEKPVLVNEGKKGFTDPSVEI
Protein: Formin-binding protein 1 (Formin-binding protein 17) (Q80TY0)
Organism: Mus musculus (Mouse)
Function: Required to coordinate membrane tubulation with reorganization of the actin cytoskeleton during the late stage of clathrin-mediated endocytosis. Binds to lipids such as phosphatidylinositol 4,5-bisphosphate and phosphatidylserine and promotes membrane invagination and the formation of tubules. Also enhances actin polymerization via the recruitment of WASL/N-WASP, which in turn activates the Arp2/3 complex. Actin polymerization may promote the fission of membrane tubules to form endocytic vesicles. May act as a link between RND2 signaling and regulation of the actin cytoskeleton. May be required for the lysosomal retention of FASLG/FASL (By similarity).
Subcellular location: Cytoplasm {ECO:0000250}. Cytoplasm, cytoskeleton {ECO:0000250}. Cytoplasm, cell cortex {ECO:0000250}. Lysosome {ECO:0000250}. Cytoplasmic vesicle {ECO:0000250}. Cell membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}; Cytoplasmic side {ECO:0000250}. Membrane, clathrin-coated pit {ECO:0000250}. Note=Enriched in cortical regions coincident with F-actin. Also localizes to endocytic vesicles and lysosomes. {ECO:0000250}.
Interaction partners:
- Cell division control protein 42 homolog
- Actin nucleation-promoting factor WASL
- Actin nucleation-promoting factor WAS
- F-BAR domain only protein 1
- F-BAR domain only protein 2
- Intersectin-2
- Intersectin-1
- tRNA-splicing endonuclease subunit Sen2
Sequence:
MSWGTELWDQFDNLEKHTQWGIDILEKYIKFVKERTEIELSYAKQLRNLSKKYQPKKNSKEEEEYKYTACKAFLSTLNEMNDYAGQHEVISENMTSQITVDLMRYVQELKQERKSNFHDGRKAQQHIETCWKQLESSKRRFERDCKEADRAQQYFEKMDADINVTKADVEKARQQAQIRQQMAEDSKADYSLILQRFNQEQWEYYHTHIPNIFQKIQEMEERRIVRIGESMKTYAEVDRQVIPIIGKCLDGIVKAAESIDQKNDSQLVVEAYKSGFEPPGDIEFEDYTQPMKRTVSDNSLSSSKEGKPELRFGGKSRGKLWPFIKKNKLMSLLTSPHQPPPPPPASASPSAVPNGPQSPKQPKEPLSHRFNEFMTSKPKIHCFRSLKRGLSLKLGVTPEDFSNFPPEQRRKKLQQKVDDLNREIQKETDQRDAITKMKDVYLKNPQMGDPASLDQKLTEVTQNIEKLRLEAQKFEAWLAEVEGRLPARSEQARRQSGLYDGQTHQTVTNCAQDRESPDGSYTEEQSQESEHKVLAPDFDDEFDDEEPLPAIGTCKALYTFEGQNEGTISVVEGETLSVIEEDKGDGWTRIRRNEDEEGYVPTSYVEVYLDKNAKGS
Protein: Hemocyanin subunit 2 (P83177)
Organism: Carcinus maenas (Common shore crab) (Green crab)
Function: Hemocyanins are copper-containing oxygen carriers occurring freely dissolved in the hemolymph of many mollusks and arthropods.
Subcellular location: Secreted, extracellular space.
Interaction partners:
Sequence:
TCLAHKQQAVNRLLYRIYSPIXXXF
Protein: Protein DEHYDRATION-INDUCED 19 homolog 6 (AtDi19-6) (Q6NM26)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Subcellular location: Nucleus {ECO:0000269|PubMed:16786289}.
Interaction partners:
Sequence:
MDSDSWSDRLASASRRYQLDFLSRSDNFLGFEEIEGEDDFREEYACPFCSDYFDIVSLCCHIDEDHPMDAKNGVCPICAVKVSSDMIAHITLQHANMFKVTRKRKSRRGGAQSMLSILKREFPDGNFQSLFEGTSRAVSSSSASIAADPLLSSFISPMADDFFISESSLCADTSSAKKTLNQSLPERNVEKQSLSAEDHREKLKQSEFVQGILSSMILEDGL
Protein: Rhoptry-associated protein 1 (Q8ILZ1)
Organism: Plasmodium falciparum (isolate 3D7)
Interaction partners:
Sequence:
MSFYLGSLVIIFHVLFRNVADGINVNGDNNYGKTIINNDFNFDDYNYWTPINKKEFLNSYEDKFSSESFLENKSSVDDGNINLTDTSTSNKSSKKGHGRSRVRSASAAAILEEDDSKDDMEFKASPSVVKTSTPSGTQTSGLKSSSPSSTKSSSPSNVKSASPHGESNSSEESTTKSSKRSASVAGIVGADEEAPPAPKNTLTPLEELYPTNVNLFNYKYSLNNMEENINILKNEGDLVAQKEEFEYDENMEKAKQDKKKALEKIGKESDEEPFMFSENKFLENQVKERNVAGSFSRFFSKLNPFKKDEVIEKTEVSKKTFSGIGFNLTEKEAKVLGVGVTYQEYPETMLYNCPNNSNLFDTIESLQGRVIDIKKRESMISTTFEQQKECLKNMGVLDLELNDTQCKFGTCIGSFGEHHLRLYEFENDLLKFHPNIDYLTLADGYKLQKNDIYELSHVNFCLLNPKTLEEFLKKKEIKDLMGGDDLIKYKENFDNFMSISITCHIESLIYDDIEASQDIAAVLKIAKSKLHVITSGLSYKARKLVYKIYSEIQKNPDELYEKLTWIYDNIYMIKRYYTAYALEGVCSYLEHDKSQMYTELHIYNKIVDSVRYYSSCFKNVIVYNAIISGIHEKIKHFLKLVPRHNFLLDYHFNSIFEKEIKPAKKYSTSHIYFDPTVASYAYYNLDRRTMVTIINDYFEAKKKELTVIVSRMKTDMLSLQNEESKIPNDKSANSKLATRLMKKFKAEIRDFFKEMRIQYAKLINIRYRSHLKKNYFAFKRLD
Protein: Probable holocytochrome-c-type synthase (EC 4.4.1.17) (Cytochrome c-type heme lyase) (CCHL) (P53703)
Organism: Caenorhabditis elegans
Function: Probable lyase that catalyzes the covalent linking of the heme group to the cytochrome C apoprotein to produce the mature functional cytochrome.
Subcellular location: Mitochondrion inner membrane {ECO:0000250|UniProtKB:P53701}.
Interaction partners:
- Protoheme IX farnesyltransferase, mitochondrial
- FErroChelatase-Like
- EOG090X04TT
- Cytochrome c domain-containing protein
- NADH dehydrogenase 1 alpha subcomplex subunit 6
- NADH dehydrogenase 1 alpha subcomplex subunit 9, mitochondrial
- Probable NADH dehydrogenase flavoprotein 2, mitochondrial
- Uncharacterized protein F52C9.3
- Sidoreflexin
- TPR_REGION domain-containing protein
Sequence:
MGSSQSTPKVQDANADAERIRKAQHSMAAAGGGSQCPLTPEQRAAASGENCGAGGACPVGADKASINPLNNELEHPNQKPAPDQPFALPTKREKSTIPKAGTETETWTYPSPQMFWNAMLKKGWRWQDDSLSKSDMENIISIHNANNEEAWREVLKWENLLHPECAEPKLKSFKGDAKNLSPRARFRNLFLGYDLPFDRHDWIVDRCGTKQVQYVIDYYDGGAVDPSSKLFTILDVRPAVNDIGNIWDRMVVAYWRFKFETLGFTPSLPIPPTEGHNVNH