wanglab/gogpt-training-data huggingface dataset:
Protein: Popeye domain-containing protein 1-A (Popeye protein 1-A) (Xpop-1-A) (Blood vessel epicardial substance-A) (Xbves-A) (Q8JH92)
Organism: Xenopus laevis (African clawed frog)
Function: Cell adhesion molecule involved in the establishment and/or maintenance of cell integrity. Plays a role in vamp3-mediated vesicular transport and recycling of different receptor molecules. May be involved in the formation and regulation of the tight junction (TJ) paracellular permeability barrier in epithelial cells. May induce primordial adhesive contact and aggregation of epithelial cells in a Ca(2+)-independent manner. May be involved in epithelial movement during corneal sheet formation and regeneration. May play a role in the regulation of cell shape and movement by modulating the Rho-GTPase activity. May also be involved in striated muscle regeneration and in the regulation of cell spreading.
Subcellular location: Lateral cell membrane {ECO:0000250}. Cell junction, tight junction {ECO:0000250}. Membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}. Note=Detected at points of cell-cell contact in confluent epithelial sheets. Colocalizes with components of the adherens and tight junctions.
Interaction partners:
Sequence:
MTTESIFITTLPMDFNSQFDNITIGLNDNETLCENWREIHHLVFHLANTCFAAGLVIPSTLNLHMLFLRGMLCLGCTFFIIWAVLFRCALDIMIWNATFLSINFMHFVYLVYKKRPIKIKKELKGIYHRMFEPLHVSPELFNRLTGQFCEIKTLAKGQTYAVEDKTSVDDRLSILLKGIMKVSYRGHFLHTISANAYIDSPEFRSTEMNRGETFQVTITADDNCVFLCWSRERLTYFLESEPFLYEIFKYLIGKDITTKLYSLNDPTLGKKRKLDTQPSLCSQLSVMEMRNSLASTNDNEDGLQNFLRGTSTTSSQRNKQQEFYNAYGVGPLSHAVFC
Protein: Chorion protein b at 7F, isoform A (Q9W3E8)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
- Chorion protein c at 7F
- Chorion protein a at 7F, isoform A
- Chorion protein S36
- Chorion protein S38
- Vitelline membrane protein Vm32E
- Heparanase
- Chorion protein S19
- AT11423p
- Chorion protein S16
- Uncharacterized protein
Sequence:
MRYSMAMIPILGLLLVALIHAAPVEVVYTGESCACPTQLGYQLNVPNTPKPKKYVGGEYGYRVEKPVQTKAKITYSFDFTVEQPRTPAPPKNNPAKLYAKVDRITVNKADCQAKNKSTCGCSSCSGQKPRYVASPVRSPNAIRRRRDVRQPGSLLRRRLMRQQKIQERPPRFVKLYHKDLTPAQEKHQLKLFGLFPVESPESVAAAPKTKRKTKKTQPSWMGLGRRLKKRDIKGEFDLLEQERSQIDLTAPEIIQFMPETLNPDFRPGQCHVGCGAMTASAPPPEEPMPKEEQVPQTTQPVQTEPPEQLNSIPAKRAAYGYYPLQIPSPLGRREDYKFVDDSQLRSLLSTTSVPDPQEYSSTPLQFAGDLESVTRRSYGVPLTSLGGGYPVEHVSDSQLDSIISGIVYNHPAYDHYSTEGSLVDPEPIQKQQTTDFLKKLIDGRLGGWGFDQGSETEHSLHNDYSTQPAKTYGYNSQTQNGYSIDTYNAPPITDYLRAWF
Protein: Pre-B-cell leukemia transcription factor 2 (Homeobox protein PBX2) (O35984)
Organism: Mus musculus (Mouse)
Function: Transcriptional activator that binds the sequence 5'-ATCAATCAA-3'. Activates transcription of PF4 in complex with MEIS1 (By similarity).
Subcellular location: Nucleus {ECO:0000305}.
Interaction partners:
- Homeobox protein PKNOX1
- Homeobox protein Meis2
- Homeobox protein Hox-B7
- Homeobox protein Meis1
- Homeobox protein Hox-A10
- Homeobox protein Hox-A9
- Homeobox protein Hox-C9
- Homeobox protein Hox-B5
- Pre-B-cell leukemia transcription factor 1
Sequence:
MDERLLGPPPPGGGRGGLGLVGAEPGGPGEPPGGGDPGGGSGGVPGGRGKQDIGDILQQIMTITDQSLDEAQAKKHALNCHRMKPALFSVLCEIKEKTGLSIRSSQEEEPVDPQLMRLDNMLLAEGVAGPEKGGGSAAAAAAAAASGGGVSPDNSIEHSDYRSKLAQIRHIYHSELEKYEQACNEFTTHVMNLLREQSRTRPVAPKEMERMVSIIHRKFSAIQMQLKQSTCEAVMILRSRFLDARRKRRNFSKQATEVLNEYFYSHLSNPYPSEEAKEELAKKCGITVSQVSNWFGNKRIRYKKNIGKFQEEANIYAVKTAVSVAQGGHSRTSSPTPPSSAGSGGSFNLSGSGDMFLGMPGLNGDSYPASQVESLRHSMGPGSYGDNIGGGQIYSPREIRANGGWQEAVTPSSVTSPTEGPGSVHSDTSN
Protein: Leukocyte immunoglobulin-like receptor subfamily A member 1 (CD85 antigen-like family member I) (Leukocyte immunoglobulin-like receptor 6) (LIR-6) (CD antigen CD85i) (O75019)
Organism: Homo sapiens (Human)
Function: May act as receptor for class I MHC antigens.
Subcellular location: Membrane; Single-pass type I membrane protein.
Interaction partners:
- Tyrosine-protein kinase SYK
- Tyrosine-protein phosphatase non-receptor type 6
- HLA class I histocompatibility antigen, C alpha chain
- CMRF35-like molecule 6
- TYRO protein tyrosine kinase-binding protein
- HLA class I histocompatibility antigen, A alpha chain
- Myeloid cell nuclear differentiation antigen
- High affinity immunoglobulin epsilon receptor subunit gamma
- HLA class I histocompatibility antigen, alpha chain F
Sequence:
MTPIVTVLICLRLSLGPRTHVQAGTLPKPTLWAEPGSVITQGSPVTLWCQGILETQEYRLYREKKTAPWITRIPQEIVKKGQFPIPSITWEHTGRYRCFYGSHTAGWSEPSDPLELVVTGAYIKPTLSALPSPVVTSGGNVTLHCVSQVAFGSFILCKEGEDEHPQCLNSQPRTHGWSRAIFSVGPVSPSRRWSYRCYAYDSNSPHVWSLPSDLLELLVLGVSKKPSLSVQPGPIVAPGESLTLQCVSDVSYDRFVLYKEGERDFLQLPGPQPQAGLSQANFTLGPVSRSYGGQYRCSGAYNLSSEWSAPSDPLDILIAGQFRGRPFISVHPGPTVASGENVTLLCQSWGPFHTFLLTKAGAADAPLRLRSIHEYPKYQAEFPMSPVTSAHSGTYRCYGSLSSNPYLLSHPSDSLELMVSGAAETLSPPQNKSDSKAGAANTLSPSQNKTASHPQDYTVENLIRMGIAGLVLVVLGILLFEAQHSQRSL
Protein: Probable aquaporin PIP1-4 (Plasma membrane intrinsic protein 1-4) (AtPIP1;4) (Transmembrane protein C) (TMP-C) (Q39196)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Aquaporins facilitate the transport of water and small neutral solutes across cell membranes.
Subcellular location: Cell membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}.
Interaction partners:
- PAMP-induced secreted peptide 1
- Novel plant SNARE 12
- Probable aquaporin SIP2-1
Sequence:
MEGKEEDVRVGANKFPERQPIGTSAQSTDKDYKEPPPAPLFEPGELSSWSFYRAGIAEFIATFLFLYITVLTVMGVKRAPNMCASVGIQGIAWAFGGMIFALVYCTAGISGGHINPAVTFGLFLARKLSLTRAVFYMIMQCLGAICGAGVVKGFQPTPYQTLGGGANTVAHGYTKGSGLGAEIIGTFVLVYTVFSATDAKRSARDSHVPILAPLPIGFAVFLVHLATIPITGTGINPARSLGAAIIYNKDHSWDDHWIFWVGPFIGAALAALYHQIVIRAIPFKSKS
Protein: Polynucleotide kinase 3'-phosphatase (M0R000)
Organism: Homo sapiens (Human)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
MGEVEAPGRLWLESPPGGAPPIFLPSDGQALVLGRGPLTQVTDRKCSRTQVELVADPETRTVAVKQLGVNPSTTGTQELKPGLEGSLGVGDTLYLVNGLHPLTLRWEETRTPESQPDTPPGTPLVSQDEKRDAELPKKRMRKSNPGWENLEKLLVFTAAGVKPQGKVAGFDLDGTL
Protein: P2X receptor C (P2XC) (Q553Y0)
Organism: Dictyostelium discoideum (Social amoeba)
Function: P2X receptors are ligand-gated ion channels that play a role in intracellular calcium signaling. ATP does not evoke inward currents in p2xC. Not essential for osmoregulation.
Subcellular location: Contractile vacuole membrane {ECO:0000269|PubMed:19833731}. Note=Ligand binding domain within the lumen of the vacuole.
Interaction partners:
Sequence:
MLDWDSILAYNTIKVVRIRDRRLGILHLIFMIAIISYVVIYSAIIKKGYLSIEEPVGSIRTSLWSPNQFNGNESYCKNNAKPYPYEKLDCVYYDDALALYPIGDDVGFTASTRIEISDQKANCSLMNPSCKFKTFNYSNVYLADIESFTVLIDHTMYAPSSQIQFNGGDLSGYVLDQNGNEIQLNESVNVIGVEGKPDVLEISKLLEFAGVNLDDPSLTNSSNPIRYDGCVLFVFIEYSNTFSYDLNKIKYVYSIKLVDDTIYNIPEVVILDDVNSRLYYKRHAIRLIFIQTGVIGSFNFQSLLLTLVSGLGLLTVSTLIVDQLAIRFLPQRKSYSSLKFQTTESFKMKKKIVNDDGEDKLYHNIEAL
Protein: Anion exchange protein (Q45EK3)
Organism: Caenorhabditis elegans
Subcellular location: Cell membrane {ECO:0000256|ARBA:ARBA00004651}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004651}.
Interaction partners:
Sequence:
MSNGSPGRHSNKAFSIGSDDGENENVFVEETSTPPKTPLGTLLTNCTEQSPLILPMPTRPRLEDSPVAEHDHHIVVDVFTVNNDDGTWKQASRFARYEEDCEGFDNHLGRPHVPCIPMGTYDALKMVTAKSILFPKVQYESLDEFVNFLETKIVDPDVPKLGEKIAKLINDRIAEIEKMRPLHQRNSSSTQSLDASNPQTISTVGIFPRSLLSAPNNLGSLAHHPMRRLPTSHSGLRFGSSFLPQQPVVSQLEPVIWDEDNEISMLVAGEIPHVNVCRFIAIRFVETTAMEKIFPNMTNVRHLFFLIGPALENVTYLDLGRALASVVSNPPATTTFDQLKSPDSITKAIERFLAGTVVIAPGRIDNKNLVRSDLIRKLVNMQGEKTETKIVHPKDVDVERNATKKAEEAEDKPFRLFSGVTSDLRNRAKHYFSDYRDGFNISIFTVVFYMFCVTVVPTLTFGAIMGAGTSGLLAVKECLVSQALSGLIWSVLSCQPLLVMSPTGPFLVFEKALFKFTDQNDMDFLEVRFYTGIFLFFISIVGAATNCAHLIHYVTIYTEDIFCALISLIFFSEVVEFIHLQEEHNSIENLKYYIENAANCTVTEVKDCALSRPNTFLLQLIMVVVSIAIFHYLRQVSRSTFFGRTFRNLCKNFGGIFAVIAVSIAYRILFQNVGVAVVDIPVAVGQSRPFDGIFVIPSAPPTASTLTIALISSILLFVLIFVETEIPEQMALREGRKLKKGGGLHWDLIVVGFCTLVSSVLGLPWMCPAAVQSLAHITSLTEYKKSAPGVPSRISHVIEQRVSGMVTYLLLGTFAILGHFLAIPAATIFGVFFYLGVRNLEGSKMILRLKLCFLPSKYRGSHKFLEILVAFSSHSLLYPTPYL
Protein: Predicted gene 14744 (B1AVU4)
Organism: Mus musculus (Mouse)
Subcellular location: Secreted {ECO:0000256|ARBA:ARBA00004613}.
Interaction partners:
Sequence:
MVKFLLIALALGVSCAHHESLDISPSEVNGDWRTLYIAADKVEKVKMNGDLRAYFEHMECNDDCGTLKIKFHVQMNGKCQTHTVVGEKQEDGRYTTDYSGRNYFEVVMKEDGALFFHNVNVDESGQETNVILVAGKGETLSKAQKQELGKLVKEYNIPKENIQHLAPTDTCNQ
Protein: Small ribosomal subunit protein uS17m (28S ribosomal protein S17, mitochondrial) (MRP-S17) (S17mt) (Q9CQE3)
Organism: Mus musculus (Mouse)
Subcellular location: Mitochondrion {ECO:0000250|UniProtKB:P82916}.
Interaction partners:
- Small ribosomal subunit protein uS14m
- Small ribosomal subunit protein uS15m
- Small ribosomal subunit protein uS7m
- Small ribosomal subunit protein mS25
- Small ribosomal subunit protein uS12m
- Small ribosomal subunit protein mS26
- Small ribosomal subunit protein uS5m
- Small ribosomal subunit protein uS3m
- Small ribosomal subunit protein mS33
- Small ribosomal subunit protein mS37
Sequence:
MSIVRSSVHAKWVVGKVIGTAMIKTAKVRATRLVLDPYLLKYFNKRKTYFAHDALQQCSVGDIVLLRALPVPRSKHVKHELAEIIFKVGRVIDPVTGKPCAGTAYLESPLSEPREELKVS
Protein: Receptor-associated protein of the synapse (A0A0G2K9X2)
Organism: Rattus norvegicus (Rat)
Interaction partners:
- Muscle, skeletal receptor tyrosine protein kinase
- Docking protein 7
- Acetylcholine receptor subunit delta
- Agrin
- Acetylcholine receptor subunit beta
- Acetylcholine receptor subunit epsilon
- Acetylcholine receptor subunit alpha
- Neuronal acetylcholine receptor subunit alpha-2
- Dystroglycan 1
Sequence:
MGQDQTKQQIEKGLQLYQSNQTEKALQVWMKVLEKGSDLVGRFRVLGCLVTAHSEMGRYKEMLKFAVVQIDTARELEDADFLLESYLNLARSNEKLCEFHKTISYCKTCLGLPGTRAGAQLGGQVSLSMGNAFLGLSLFQKALESFEKALRYAHNNDDTMLECRVCCSLGSFYAQVKDYEKALFFPCKAAELVNDYGKGWSLKYRAMSQYHMAVAYRLLGHLGSAMECCEESMKIALQHGDRPLQALCLLCFADIHRSRGDLETAFPRYDSAMSIMTEIGNRLGQVHVLLGVAKCWIARKVLDKALDAIEKAQDLAEEVGNKLSQLKLHCLSEGICRSKGLQRELRAHVVRFHECVEETELYCGLCGESIGEKNSRLQALPCSHIFHLRCLQNNGTRSCPNCRRSSMKPGFV
Protein: Chemosensory protein B 53b (A1ZAG6)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MSQQLFRIWQLLVLMAFIPHSIEVSYEFTMEDERITSDCQNEPPKTLNIDGLFDMSNIDFEMAEDGVQLSGYKTVVWDIQPTDRVELQGSVQYFDRGTWQPTTLNMLVKDFCHVLFDKKQVWYDAYSKHITNSAQINNTCFRVKGSVIEFETYTIGLEFGSGIPLHRGRYAIRLKFRAFDKNGKVRPNEICFEIKGQFSKKSLG
Protein: Rac family small GTPase 2 (Ras-related C3 botulinum toxin substrate 2) (Q6IQN5)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Interaction partners:
Sequence:
MQAIKCVVVGDGAVGKTCLLISYTTNAFPGEYIPTVFDNYSANVMVDSKPVNLGLWDTAGQEDYDRLRPLSYPQTDVFLICFSLVSPASFENVRAKWYPEVRHHCPSTPIILVGTKLDLRDEKETIEKLKEKKLAPITYPQGLALAKEIDAVKYLECSALTQRGLKTVFDEAIRAVLCPQPTKVKKKGCVML
Protein: Cone-rod homeobox protein (O54751)
Organism: Mus musculus (Mouse)
Function: Transcription factor that binds and transactivates the sequence 5'-TAATC[CA]-3' which is found upstream of several photoreceptor-specific genes, including the opsin genes. Acts synergistically with other transcription factors, such as NRL, RORB and RAX, to regulate photoreceptor cell-specific gene transcription. Essential for the maintenance of mammalian photoreceptors.
Subcellular location: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00108, ECO:0000269|PubMed:16574740}.
Interaction partners:
- Photoreceptor-specific nuclear receptor
- Rhodopsin
- Recoverin
- Medium-wave-sensitive opsin 1
- Short-wave-sensitive opsin 1
- Rod outer segment membrane protein 1
- Aryl-hydrocarbon-interacting protein-like 1
- Ataxin-7
- Neurogenic differentiation factor 1
- Arrestin-C
Sequence:
MMAYMNPGPHYSVNALALSGPNVDLMHQAVPYSSAPRKQRRERTTFTRSQLEELEALFAKTQYPDVYAREEVALKINLPESRVQVWFKNRRAKCRQQRQQQKQQQQPPGAQTKARPAKRKAGTSPRPSTDVCTDPLGISDSYSPSLPGPSGSPTTAVATVSIWSPASEAPLPEAQRAGLVASGPSLTSAPYAMTYAPASAFCSSPSAYASPSSYFSGLDPYLSPMVPQLGGPALSPLSGPSVGPSLAQSPTSLSGQSYSTYSPVDSLEFKDPTGTWKFTYNPMDPLDYKDQSAWKFQIL
Protein: MKKS centrosomal shuttling protein (F1QCQ8)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Interaction partners:
- T-complex protein 1 subunit epsilon
- T-complex protein 1 subunit eta
- T-complex protein 1 subunit theta
- T-complex protein 1 subunit gamma.
- Chaperonin-containing TCP1, subunit 6A
- Chaperonin-containing TCP1, subunit 2
- Chaperonin-containing TCP1, subunit 2
- Protein FAM161A
- T-complex protein 1 subunit delta
- 10 kDa heat shock protein, mitochondrial
Sequence:
MSRISKKKPALCTDEPLSNSTICQKITLLRNILSTAYGPTGRLKQIHNNVGGHVLTTSTSTALLKRLEMSEPLLKLISTALQHHTTRYSDSGLFMGIFTLTLIENTKKYGLRTSTAIKVYKHLVEQCNVYLKGDSCGCKVPVEFSSCDSLVALAHSMITSKPACMLDSRETQQISSLITQAFLYSIPCNSSGTACFGRTVTIGIEGQSVNHSSVFPGLLLDVPEMLLPGDLERLGDGPFKVVLFGVSLSGDISEVGDVALEVHRGLNPERDLLQQLLKIGEQVVKDKVSLFACQKVVHPVLQHYLREHEVVVIERLGLALMEPFAKITGARAVASLFSLVPMEAYGLVAGLCFQDCGSKKLLQLLSSKHAAISTMVLCHRNETMLEELKMTCQRAEHVLRLTLREPYALLGGGCTETQLATHITHMNQSTAPTTAAALGISHSEFLMAVESFRSSLLAVALSLEHDGQDCLIDLTYGHRWVMDISSQTEVKHTCGCGLLEDRSNLEKTHLNTACQTFSPVFLENNDTQPKVLDSFSAKLNALNVAVEMASLVLDVKYIIKDVN
Protein: tRNA (uracil-5-)-methyltransferase homolog A (EC 2.1.1.35) (mRNA (uracil-5-)-methyltransferase TRMT2A) (EC 2.1.1.-) (Q8IZ69)
Organism: Homo sapiens (Human)
Function: S-adenosyl-L-methionine-dependent methyltransferase that catalyzes the formation of 5-methyl-uridine in tRNAs and some mRNAs. Mainly catalyzes the methylation of uridine at position 54 (m5U54) in cytosolic tRNAs. Also able to mediate the formation of 5-methyl-uridine in some mRNAs.
Subcellular location: Cytoplasm, cytosol {ECO:0000305|PubMed:31361898}.
Interaction partners:
- Ran-specific GTPase-activating protein
- Transducin beta-like protein 3
- Ribosome biogenesis protein BOP1
- tRNA
- 2-oxoglutarate and iron-dependent oxygenase domain-containing protein 2
Sequence:
MSENLDNEGPKPMESCGQESSSALSCPTVSVPPAAPAALEEVEKEGAGAATGPGPQPGLYSYIRDDLFTSEIFKLELQNVPRHASFSDVRRFLGRFGLQPHKTKLFGQPPCAFVTFRSAAERDKALRVLHGALWKGRPLSVRLARPKADPMARRRRQEGESEPPVTRVADVVTPLWTVPYAEQLERKQLECEQVLQKLAKEIGSTNRALLPWLLEQRHKHNKACCPLEGVRPSPQQTEYRNKCEFLVGVGVDGEDNTVGCRLGKYKGGTCAVAAPFDTVHIPEATKQVVKAFQEFIRSTPYSAYDPETYTGHWKQLTVRTSRRHQAMAIAYFHPQKLSPEELAELKTSLAQHFTAGPGRASGVTCLYFVEEGQRKTPSQEGLPLEHVAGDRCIHEDLLGLTFRISPHAFFQVNTPAAEVLYTVIQDWAQLDAGSMVLDVCCGTGTIGLALARKVKRVIGVELCPEAVEDARVNAQDNELSNVEFHCGRAEDLVPTLVSRLASQHLVAILDPPRAGLHSKVILAIRRAKNLRRLLYVSCNPRAAMGNFVDLCRAPSNRVKGIPFRPVKAVAVDLFPQTPHCEMLILFERVEHPNGTGVLGPHSPPAQPTPGPPDNTLQETGTFPSS
Protein: Lysine-specific histone demethylase (EC 1.14.99.66) (R4GMQ1)
Organism: Homo sapiens (Human)
Subcellular location: Nucleus {ECO:0000256|PIRNR:PIRNR038051}.
Interaction partners:
Sequence:
MLSGKKAAAAAAAAAAAATGTEAGPGTAGGSENGSEVAAQPAGLSGPAEVGPGAVGERTPRKKEPPRASPPGGLAEPPGSAGPQAGPTVVPGSATPMETGIAETPEGRRTSRRKRAKVEYREMDESLANLSEDEYYSEEERNAKAEKEKKLPPPPPQAPPEEENESEPEEPSGVEGAAFQSRLPHDRMTSQEAACFPDIISGPQQTQKVFLFIRNRTLQLWLDNPKIQLTFEATLQQLEAPYNSDTVLVHRVHSYLERHGLINFGIYKRIKPLPTKKTGKVIIIGSGVSGLAAARQLQSFGMDVTLLEARDRVGGRVATFRKGNYVADLGAMVVTGLGGNPMAVVSKQVNMELAKIKQKCPLYEANGQAVPKEKDEMVEQEFNRLLEATSYLSHQLDFNVLNNKPVSLGQALEVVIQLQEKHVKDEQIEHWKKIVKTQEELKELLNKMVNLKEKIKELHQQYKEASEVKPPRDITAEFLVKSKHRDLTALCKEYDELAETQGKLEEKLQELEANPPSPLFFCSDVYLSSRDRQILDWHFANLEFANATPLSTLSLKHWDQDDDFEFTGSHLTVRNGYSCVPVALAEGLDIKLNTAVRQVRYTASGCEVIAVNTRSTSQTFIYKCDAVLCTLPLGVLKQQPPAVQFVPPLPEWKTSAVQRMGFGNLNKVVLCFDRVFWDPSVNLFGHVGSTTASRGELFLFWNLYKAPILLALVAGEAAGIMENISDDVIVGRCLAILKGIFGSSAVPQPKETVVSRWRADPWARGSYSYVAAGSSGNDYDLMAQPITPGPSIPGAPQPIPRLFFAGEHTIRNYPATVHGALLSGLREAGRIADQFLGAMYTLPRQATPGVPAQQSPSM
Protein: NADH dehydrogenase [ubiquinone] 1 subunit C1, mitochondrial (Complex I-KFYI) (CI-KFYI) (NADH-ubiquinone oxidoreductase KFYI subunit) (Q02376)
Organism: Bos taurus (Bovine)
Function: Accessory subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I), that is believed not to be involved in catalysis. Complex I functions in the transfer of electrons from NADH to the respiratory chain. The immediate electron acceptor for the enzyme is believed to be ubiquinone.
Subcellular location: Mitochondrion inner membrane {ECO:0000305|PubMed:10852722, ECO:0000305|PubMed:18721790}; Single-pass membrane protein; Matrix side.
Interaction partners:
- Acyl carrier protein, mitochondrial
- NADH dehydrogenase 1 beta subcomplex subunit 3
- NADH dehydrogenase 1 subunit C2
- NADH dehydrogenase 1 beta subcomplex subunit 6
- NADH dehydrogenase 1 beta subcomplex subunit 5, mitochondrial
- NADH dehydrogenase 1 alpha subcomplex subunit 5
- NADH dehydrogenase 1 alpha subcomplex subunit 12
- NADH dehydrogenase 1 alpha subcomplex subunit 8
- NADH dehydrogenase 1 alpha subcomplex subunit 10, mitochondrial
- NADH dehydrogenase 1 beta subcomplex subunit 1
Sequence:
MAPSALLRPFWKLLAPARFPSVSSSRSKFYIQEPPHGSPNWLKVGLTLGTSVFLWIYLIKQHNEDVLEYKRRNGLE
Protein: VP17 (C8CHL5)
Organism: Thermus virus P23-77
Interaction partners:
Sequence:
MGVFDRIRGALGRGLDVFRGDLPQVQPPAPQPAPAPAITPAAVQVGGWGFAWIDNEDFSPTGLAWRSGEYFALAQMKTPETAHFRIAAQERRLRIYLRGQKVVNGRNLSDPDSRTVNLPFLMQTPQGAPTLPSTYHPDVAVWAKVGSTWQPCVITAINYSTGDVTFTEPAGVTASDGIEIYYVHGDGQFRLRVARDAGGVDDSAATVFNQSFSTMHSVDQNNVETMIAWPQQVELVPGTRLVLEVFTTQVPMVWNERSGHYIQIAAMGRRIEVLDKGGLQRLAELEARGGL
Protein: Peptidyl-prolyl cis-trans isomerase cyp3 (PPIase cyp3) (EC 5.2.1.8) (Rotamase cyp3) (O74729)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides (By similarity).
Subcellular location: Cytoplasm, cytoskeleton, microtubule organizing center, spindle pole body {ECO:0000269|PubMed:16134115}.
Interaction partners:
- Uncharacterized WD repeat-containing protein C227.12
- U4/U5/U6 small nuclear ribonucleoprotein prp3
- 13 kDa ribonucleoprotein-associated protein
- Pre-mRNA-processing factor 31
- Peptidyl-prolyl cis-trans isomerase
- Ran-specific GTPase-activating protein 1
- Uncharacterized protein C18H10.07
- Small nuclear ribonucleoprotein F
- LSM complex subunit lsm4
- LSM complex subunit lsm7
Sequence:
MSTEPVVFMDIAIDGRLLGRIKIRLFSSIVPKTAENFRQFCTGETLGVNQKPIGYKNSTFHRIIQGFMIQGGDFVSGDGTGSATIFNSRTFPDENFTLKHDRPGLLSMANAGKDSNGCQFFITTVPCDFLDGKHVVFGEVIEGYDIVKEIESTPVGANSRPKSNVAIVECGEM
Protein: GH06338p (Q7YTY9)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MRRARPRQDNVKPKERKASGAVHPRSLHPCPECEKKFTRNFQLKLHMTAVHGMGEMRYQCEECRKNFASRHSLRYHVKSVHSTERPFGCQHCDRRFILRTQLLSHLRTHTGEAKPRIFECQRCSKSWPTKSDLRTHMRSHNPNMERPFKCDRCSKAFFTRGHLNSHLLVHTGEKPFACEYCDKCYQSVGNLNNHMVRLHADIIEAQLEAEGIES
Protein: NAD(P)H-hydrate epimerase (EC 5.1.99.6) (Apolipoprotein A-I-binding protein) (AI-BP) (NAD(P)HX epimerase) (B0BNM1)
Organism: Rattus norvegicus (Rat)
Function: 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. Accelerates cholesterol efflux from endothelial cells to high-density lipoprotein (HDL) and thereby regulates angiogenesis (By similarity).
Subcellular location: Mitochondrion {ECO:0000255|HAMAP-Rule:MF_03159}. Secreted {ECO:0000255|HAMAP-Rule:MF_03159}. Note=In sperm, secretion gradually increases during capacitation. {ECO:0000255|HAMAP-Rule:MF_03159}.
Interaction partners:
- ATP-dependent
- Probable ATP-dependent RNA helicase DDX6
- Uridine diphosphate glucose pyrophosphatase NUDT14
- 5'-
- 5'-
- Pyridoxine-5'-phosphate oxidase
- Large ribosomal subunit protein bL28m
- Mitochondrial ribosomal protein S23
- Exosome complex component RRP41
- Transmembrane protein 160
Sequence:
MSGLRTLLGLGLLVAGSRLPRIASRQSVCRAGPIWWGTQHRSSETMASAAVKYLSQEEAQAVDEELFNEYQFSVDQLMELAGLSCATAIAKAYPPTSMSKSPPTVLVICGPGNNGGDGLVCARHLKLFGYQPTIYYPKRPNKPLFTGLVTQCQKMDIPFLGEMPPEPMMVDELYELVVDAIFGFSFKGDVREPFHSILSVLSGLTVPIASIDIPSGWDVEKGNPSGIQPDLLISLTAPKKSATQFTGRYHYLGGRFVPPALEKKYQLNLPAYPDTECVYRLQ
Protein: Immunoglobulin kappa variable 2-29 (A2NJV5)
Organism: Homo sapiens (Human)
Function: V region of the variable domain of immunoglobulin light chains that participates in the antigen recognition. Immunoglobulins, also known as antibodies, are membrane-bound or secreted glycoproteins produced by B lymphocytes. In the recognition phase of humoral immunity, the membrane-bound immunoglobulins serve as receptors which, upon binding of a specific antigen, trigger the clonal expansion and differentiation of B lymphocytes into immunoglobulins-secreting plasma cells. Secreted immunoglobulins mediate the effector phase of humoral immunity, which results in the elimination of bound antigens. The antigen binding site is formed by the variable domain of one heavy chain, together with that of its associated light chain. Thus, each immunoglobulin has two antigen binding sites with remarkable affinity for a particular antigen. The variable domains are assembled by a process called V-(D)-J rearrangement and can then be subjected to somatic hypermutations which, after exposure to antigen and selection, allow affinity maturation for a particular antigen.
Subcellular location: Secreted {ECO:0000303|PubMed:20176268, ECO:0000303|PubMed:22158414}. Cell membrane {ECO:0000303|PubMed:20176268, ECO:0000303|PubMed:22158414}.
Interaction partners:
Sequence:
MRLPAQLLGLLMLWIPGSSADIVMTQTPLSLSVTPGQPASISCKSSQSLLHSDGKTYLYWYLQKPGQSPQLLIYEVSSRFSGVPDRFSGSGSGTDFTLKISRVEAEDVGVYYCMQGIHLP
Protein: Rap guanine nucleotide exchange factor 2 (Cyclic nucleotide ras GEF) (Neural RAP guanine nucleotide exchange protein) (PDZ domain-containing guanine nucleotide exchange factor 1) (RA-GEF-1) (Ras/Rap1-associating GEF-1) (A0A2R8Y661)
Organism: Homo sapiens (Human)
Subcellular location: Cell junction {ECO:0000256|ARBA:ARBA00004282}. Cell membrane {ECO:0000256|ARBA:ARBA00004236}. Cytoplasm, perinuclear region {ECO:0000256|ARBA:ARBA00004556}. Late endosome {ECO:0000256|ARBA:ARBA00004603}.
Interaction partners:
Sequence:
MIEYGLSVDYMDENEEYFQRQASHRQSRRRFRKINQKGERQTIIDTVDPYPMGKPPLPRGYHTLPADFTKLHLTDSLHPQVTHVSSSHSGCSITSDSGSSSLSDIYQATESEAGDMDLSGLPETAVDSEDDDDEEDIERASDPLMSRDIVRDCLEKDPIDRTDDDIEQLLEFMHQLPAFANMTMSVRRELCAVMVFAVVERAGTIVLNDGEELDSWSVILNGSVEVTYPDGKAEILCMGNSFGVSPTMDKEYMKGVMRTKVDDCQFVCIAQQDYCRILNQVEKNMQKVEEEGEIVMVKEHRELDRTGTRKGHIVIKGTSERLTMHLVEEHSVVDPTFIEDFLLTYRTFLSSPMEVGKKLLEWFNDPSLRDKVTRVVLLWVNNHFNDFEGDPAMTRFLEEFENNLEREKMGGHLRLLNIACAAKAKRRLMTLTKPSREAPLPFILLGGSEKGFGIFVDSVDSGSKATEAGLKRGDQILEVNGQNFENIQLSKAMEILRNNTHLSITVKTNLFVFKELLTRLSEEKRNGAPHLPKIGDIKKASRYSIPDLAVDVEQVIGLEKVNKKSKANTVGGRNKLKKILDKTRISILPQKPYNDIGIGQSQDDSIVGLRQTKHIPTALPVSGTLSSSNPDLLQSHHRILDFSATPDLPDQVLRVFKADQQSRYIMISKDTTAKEVVIQAIREFAVTATPDQYSLCEVSVTPEGVIKQRRLPDQLSKLADRIQLSGRYYLKNNMETETLCSDEDAQELLRESQISLLQLSTVEVATQLSMRNFELFRNIEPTEYIDDLFKLRSKTSCANLKRFEEVINQETFWVASEILRETNQLKRMKIIKHFIKIALHCRECKNFNSMFAIISGLNLAPVARLRTTWEKLPNKYEKLFQDLQDLFDPSRNMAKYRNVLNSQNLQPPIIPLFPVIKKDLTFLHEGNDSKVDGLVNFEKLRMIAKEIRHVGRMASVNMDPALMFRTRSLSQGSTNATVLDVAQTGGHKKRVRRSSFLNAKKLYEDAQMARKVKQYLSNLELEMDEESLQTLSLQCEPATNTLPKNPGDKKPVKSETSPVAPRAGSQQKAQSLPQPQQQPPPAHKINQGLQVPAVSLYPSRKKVPVKDLPPFGINSPQALKKILSLSEEGSLERHKKQAEDTISNASSQLSSPPTSPQSSPRKGGSGNQLRSFGSGQLDLTSSSSSLGSYTLAPSGTVDNFSDSGHSEISSRSSIVSNSSFDSVPVSLHDERRQRHSVSIVETNLGMGRMERRTMIEPDQYSLGSYAPMSEGRGLYATATVISSPSTEELSQDQGDRASLDAADSGRGSWTSCSSGSHDNIQTIQHQRSWETLPFGHTHFDYSGDPAGLWASSSHMDQIMFSDHSTKYNRQNQSRESLEQAQSRASWASSTGYWGEDSEGDTGTIKRRGGKDVSIEAESSSLTSVTTEETKPVPMPAHIAVASSTTKGLIARKEGRYREPPPTPPGYIGIPITDFPEGHSHPARKPPDYNVALQRSRMVARSSDTAGPSSVQQPHGHPTSSRPVNKPQWHKPNESDPRLAPYQSQGFSTEEDEDEQVSAV