wanglab/gogpt-training-data huggingface dataset:
Protein: Small ribosomal subunit protein uS12B (40S ribosomal protein S23-B) (P0CT76)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Subcellular location: Cytoplasm {ECO:0000250|UniProtKB:P0CX30}. Nucleus {ECO:0000269|PubMed:16823372}. Nucleus, nucleolus {ECO:0000269|PubMed:16823372}.
Interaction partners:
- Small ribosomal subunit protein uS10
- Small ribosomal subunit protein uS5
- Small ribosomal subunit protein uS14
- Small ribosomal subunit protein uS3
- Elongation factor 3
- Small ribosomal subunit protein eS6B
- Small ribosomal subunit protein uS15
- Small ribosomal subunit protein eS27
- Small ribosomal subunit protein uS9A
- Small ribosomal subunit protein eS7
Sequence:
MGKPAGLNAARKLRNHRREERWADAHYKKRLLGTAYKSSPFGGSSHAKGIVVEKIGVEAKQPNSAIRKCVRVQLIKNGKKVTAFVPHDGCLNFVDENDEVLLSGFGRKGKAKGDIPGVRFKVVKVAGVGLSALFHEKKEKPRA
Protein: Kinesin-related protein 7 (Kinesin family member 7) (Kinesin-1) (Q54TL0)
Organism: Dictyostelium discoideum (Social amoeba)
Function: Microtubule-associated force-producing protein that plays a role in organelle transport. Its motor activity is directed toward the microtubule's plus end. May be involved in cell motility or cell differentiation during prestalk formation.
Subcellular location: Nucleus membrane {ECO:0000269|PubMed:9693369}; Single-pass membrane protein {ECO:0000269|PubMed:9693369}. Cytoplasm, cytoskeleton {ECO:0000305|PubMed:9693369}.
Interaction partners:
- Lis-interacting protein
- Tubulin beta chain
- Kinesin-related protein 1
- Kinesin-related protein 2
- Tubulin alpha chain
Sequence:
MESPVVEGNSGEVATPTLPQPPTPVSSNIRVVCRVRPLTELEKGRNEHSIVHFFDSKSISIRANGPQFTFDRIFGYQETQSQIFEDVAEPIVNDFLDGYHGTIIAYGQTASGKTFTMVGDPDSHGIIPRVIESIFVGISKMREKDTSLSLAFCLKISALELYNEKLYDLYDASKSNLNIREHKQNGIYVEGISEIVITSIEEAYNFLNISNNNRAIASTKMSAASSRSHSVLMIELSQQNLSMESSKISKLFLVDLAGSERAHKTGAEGDRMQEAKNINLSLSALGKVINALTCGANYVPYRDSKLTRVLQDSLGGNSKTSLIINCSPSNNNEHETITTLQFGTRAKTIKNQPKINKKITYHELELFIIKLAKDLEKSRKECEEITRSKNLEINNLLIQLENNQKMVVESNQKLELLNSQISSNHSFDNTFKEIENTCENSKIIFDDLNDHINNNNNVDENNNTNNNDNNNNDNNNNNQYQEESNQYQQENNQKDGDQNNSSFDSIKVEDLRDLDDEPDIEDIILNSTLGNISDDDDDDDDHHSNNNNVDDNNNGEINNDSDGYLNRSLKDIKIPEISDLNDHNINNNNNNNNNINNDNNSNSGGLRVSTSYITSSPNLSPSKSMDVNNSPPLFSYFKTKDFPPSSDENDKFFNDLIAKGENEQQQQQQQHNDDDEDIKSTTSNATTTTITTIDMNASHPSGIDDPIEFTIIKSDKTITSTIERETIQPSSLSNSTSLLDIETVESSTLPAPPPVTTTTTLTTVTTTKLTKTTNIPSNTNDINSIDDFGFSKIEEEGSSSNRKPNDTAILSFGDDDDEENEDNENEDVIVDSDEDTHSGKNNLLNTFKNDHHRGDFGATPTKSIFNKNGNITIKEFETPQQQQQQQQQQQQQQQQQQQQQQPLILQTTSTNPTIISIKSNKEPSPSSSTTTSIKKKNFNKRRSWIIFTIILTITLVSSSLLCLYLPEYKERLVQRRGYLNKLGIYSDYPTNEKISLAQHNQISLAKELYGGNSKQYYDEMSSFNTAYNHLIEMNHLETAVSKIFGSAIDLRFSGDDVINSIECKRAIHKLKTNNYVNGDLDQQQQQHNYITKIDQLSEQSKEQNQLIENFKLDLKNKTSEIEKLEKEIKQKDNKIKEKEEKIELIESRVLNEEKGGEKVLEDQIISLRNDKNTLSTQILNLEGDKKSLGVLVIKLNSDKTEIQNEVKELKRKVQELEDAPIALIPNPFVKWVKSFYVEKKSWFVENIYKIWNWFK
Protein: Glutathione S-transferase C-terminal domain-containing protein (Q8NEC7)
Organism: Homo sapiens (Human)
Subcellular location: Cytoplasm {ECO:0000269|PubMed:24058608}.
Interaction partners:
- Integrator complex subunit 12
- Protein FAM13A
- Thrombospondin type-1 domain-containing protein 4
Sequence:
MKAIKKSLTEEEYLYLDFSHQTEGCIFPLHTSVTLFLLSYCDCKIFKICLVVTKEVSRDSSLLRDDLIQDVEIQIISRQELPPIVQNCCLPAVVERSDNFCRAGLAVVLRHIIQKSYEADPLKKELLELLGFKKTCLKACAEVSQWTRLCELTIPLAIENFLRESSDQPPTIPVEILQLEKKLSEPVRVHNDDKLRRQKLKQQKADGVGPPLTKGKAKSKVHTQETSEGLDSSSKSLELKVAFSKLTVQEEPATTNREPSHIRKAKASDLPPLEHVFAEGLYFTLADIVLLPCIHHFLVIISRKFSEKLVEFPLLASWYQRIQEVPGVKTAASKCGIQFLHLPKLLTTSTEQHPNLCEVPGVEEQSDPLFIGGPRPTMAKLMEKGIEVMFSPHPCPTWTLDWNVLPAAVSPKEGKMSSDRALRKQQQLNNLVYVVTNQAKPGDRIVDFCSGGGHVGIVLAHMLPSCQVTLIENKELSLIRAKKRSDELGLSNIWFIQANMEYFTGMFNIGVALHACGVATDMVIEHCIKTRASFVTCPCCYGFIQNTSKFNFPKSEQFKKTLSYKEHMILCRFADQTAVQLPPQRRLIGKQCMCLVDLDRARAAEECGYSVQVISMEPESCSPKNNMIVGVPI
Protein: Photoactive yellow protein (PYP) (P16113)
Organism: Halorhodospira halophila (Ectothiorhodospira halophila)
Function: Photoactive blue light protein. Probably functions as a photoreceptor for a negative phototaxis response.
Interaction partners:
Sequence:
MEHVAFGSEDIENTLAKMDDGQLDGLAFGAIQLDGDGNILQYNAAEGDITGRDPKQVIGKNFFKDVAPCTDSPEFYGKFKEGVASGNLNTMFEYTFDYQMTPTKVKVHMKKALSGDSYWVFVKRV
Protein: NYGGF5 (Q6R5J6)
Organism: Rattus norvegicus (Rat)
Subcellular location: Mitochondrion inner membrane {ECO:0000256|ARBA:ARBA00004448}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004448}.
Interaction partners:
Sequence:
MQGEAALAKLGDGAMESAPYRGMMRTALGIVQEEGFLKLWQGVTPAIYRHVVYSGGRMVTYEHLREVVFGKSEDEHYPLWKSVIGGMMAGVIGQFLANPTDLVKVQMQMEGKRRLEGKPLRFRGVHHAFAKILAEGGIRGLWAGWIPNIQRAALVNMGDLTTYDTVKHYLVLNTALEDNIATHGLSSLCSGLVASILGTPADVIKSRIMNQPRDKQGRGLLYKSSTDCVIQAVQGEGFLSLYKGFLPSWLRMTPWSMVFWLTYEKIRQLSGVSPF
Protein: CCAAT enhancer binding protein alpha (CCAAT/enhancer-binding protein alpha isoform c) (F1RNW6)
Organism: Sus scrofa (Pig)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
- Runt-related transcription factor
- Cyclin-dependent kinase 4
- Cyclin-dependent kinase 2
- Receptor-type tyrosine-protein kinase FLT3
- RUNX1 partner transcriptional co-repressor 1
- Cyclin-dependent kinase inhibitor 1
- Period circadian protein homolog 2
- Peroxisome proliferator-activated receptor gamma
- Fatty acid-binding protein, adipocyte
- CCAAT/enhancer-binding protein
Sequence:
MESADFYEAEPRPPMSSHLQSPPHAPSSAAFGFPRGAGPAQPPAPPAAPEPLGGICEHETSIDISAYIDPAAFNDEFLADLFQHSRQQEKAKAAAAPAGGGGDFDYPGAPVGPGGAVMPGGAHGPPPSYGCAAAGYLDGRLEPLYERVGAPALRPLVIKQEPREEDESKQLALAGLFPYQPPPPPPPPHSHPPPAHLAAPHLQFQIAHCGQTTMHLQPGHPTPPPTPVPSPHPAPALGAAGLPGPGGALKGLAPAHPDLRAGGGGGAGKAKKSVDKNSNEYRVRRERNNIAVRKSRDKAKQRNVETQQKVLELTSDNDRLRKRVEQLSRELDTLRGIFRQLPESSLVKAMGNCA
Protein: Cellular tumor antigen p53 (A0A087X1Q1)
Organism: Homo sapiens (Human)
Subcellular location: Cytoplasm {ECO:0000256|RuleBase:RU003304}. Nucleus {ECO:0000256|RuleBase:RU003304}. Mitochondrion matrix {ECO:0000256|ARBA:ARBA00004305}. Nucleus, PML body {ECO:0000256|ARBA:ARBA00004322}.
Interaction partners:
Sequence:
MAIYKQSQHMTEVVRRCPHHERCSDSDGLAPPQHLIRVEGNLRVEYLDDRNTFRHSVVVPYEPPEVGSDCTTIHYNYMCNSSCMGGMNRRPILTIITLEDSSGNLLGRNSFEVRVCACPGRDRRTEEENLRKKGEPHHELPPGSTKRALPNNTSSSPQPKKKPLDGEYFTLQIRGRERFEMFRELNEALELKDAQAGKEPGGSRAHSSHLKSKKGQSTSRHKKLMFKTEGPDSD
Protein: Dystrobrevin alpha (M0QZ28)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MFPDQPEKPLNLAHIVPPRPVTSMNDTLFSHSVPSSGSPFITRSMLESSNRLDEEHRLIARYAARLAAESSSSQPPQQRSAPDISFTIDANKQQRQLIAELENKNREILQEIQRLRLEHEQASQPTPEKAQQNPTLLAELRLLRQRKDELEQRMSALQESRRELMVQLEGLMKLLKTQGAGSPRSSPSHTISRPIPMPIRSASACSTPTHTPQDSLTGVGGDVQEAFAQSSRRNLRNDLLVAADSITNTMSSLVKELNSEVGSETESNVDSEFARTQFEDLVPSPTSEKAFLAQIHARKPGYIHSGATTSTMRGDMVTEDADPYVQPEDENYENDSVRQLENELQMEEYLKQKLQDEAYQVSLQG
Protein: phenylalanine--tRNA ligase (EC 6.1.1.20) (Phenylalanyl-tRNA synthetase beta subunit) (Q386S3)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Subcellular location: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
Interaction partners:
- phenylalanine--tRNA ligase
- isoleucine--tRNA ligase
- leucine--tRNA ligase
- Translation elongation factor 1-beta, putative
- Eukaryotic translation initiation factor 3 subunit L
- arginine--tRNA ligase
- Translation elongation factor 1-beta, putative
- Translation elongation factor 1-beta, putative
- GMP synthase
- tyrosine--tRNA ligase
Sequence:
MPTLAVVRDYLFDFIGKSYTEDQFEDICFQFGVELDDVTSEREMFRREQGEAVAAKGEELSDAVIYKIDTPANRYDLLCAEGMGTAMKVFLGMTPAPRFQLLNRANPLYKVTVEKSVRNVRDYIVCAVLRNVRLDKRSYRSFIDFQDKLHLGLARRRALASVGTHDLDKINQNEFLYAARPKESIRFVPLNQQERVLDCRGNGLAEFYKDDRHISKFIPLISEFSHYPVVLDGKGENILSLPPIINSDYSCISANTRNIFIECTAPDHHKASVLVNQLVCAFSTYCEKPFTVEAVRVVYDEPTPDGTKEEVTPNLDPRLVSVEQSKVEKLIGIKLNSANHMGELLERMLHHVAKVEDSTVTVEVPPTRPDVLGPTDLMEDVAVAYGYDNITHKECLTFGDVAQQPLSKLSHLIRIEMANAGYMELLTFSLCSREEGFTRLNRVDDDVAVHIANPKTMEFQICRPSLMPGILKTLNANKSHPLPLRFFECADIVLLDNEKNFPPVITPKLEYPNCGARNQRHLAALHCCSESSSFEDIHGLVEFVMAKLGVVRKVGEEVVDGDSYTLERSSDGAFFPGRCMDVFLHRSGQKVCIGGFGVVHPNTLKAYDIPFPCSYMELNVQFAQ
Protein: G protein-coupled receptor kinase (EC 2.7.11.-) (Q08CJ6)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Interaction partners:
- Arrestin, beta 2a.
- Arrb2b protein
- Beta-arrestin-1
- ARF GTPase-activating protein GIT1 isoform X2
Sequence:
MEIENIVANTVLLKAREGGGGKRNGRSKKWKEMLKLPHISQCEELRRTIERDYTSLCEKQPIGRQLFRQFCDTQPKLRRCIEFLDSVAMYQVAPDEKRRDAGLNILDTYFNNGSAAHLPEMAQDVVGECRQKLEQSPCKELFQECTRIVREYLSGAPFSAYQETMYFSRFLQWKWLERQPVTKNTFRHYRVLGKGGFGEVCACQVRATGKMYACKKLEKKRVKKRKGEAMALNEKRILEKVNSSFVVSLAYAYETKDALCLVLTIMNGGDLKFHIYNMGNSGFDEQRAIFYAAEICCGLEDLHRERIVYRDLKPENILLDDRGHIRISDLGLAVQIPEGETIRGRVGTVGYMAPEVIQNESYTFSPDWWGLGCLIYEMIQGQSPFRRRKERVKREEVDRRVCEDQEEYTEKFSEDAKDICRQLLCKDPKERLGCRGSGAAEVKLHPIFRNINFKRLEANMLDPPFCPDPRAVYCKDVLDIEQFSTVKGVNLDPTDDDFYHKFVTGSVSIPWQNEMIEMECFKEINVFEMDGALCADLDVNRPNPAPKRGFFYRLFHREASGSASPAVLRGGGA
Protein: Phloretin 2'-O-glucosyltransferase (EC 2.4.1.357) (Phloretin glucosyltransferase 1) (MdPGT1) (UDP-glucose:phloretin 2'-O-glucosyltransferase) (UDP-glycosyltransferase 88F1) (B3TKC8)
Organism: Malus domestica (Apple) (Pyrus malus)
Function: Glycosyltransferase that possesses phloretin 2'-O-glycosyltransferase activity. Converts phloretin to phlorizin (phloretin 2'-O-glucoside), a potent antioxidant. Is specific for phloretin and does not possess glycosyltransferase activity toward caffeic acid, catechin, chlorogenic acid, 2-coumaric acid, 3-coumaric acid, 4-coumaric acid, cyanidin, 3,4-dihydroxyhydrocinnamic acid, epicatechin, 3-hydroxybenzoic acid, naringenin, 3,4-dihydroxybenzoic acid, quercetin and rutin. Can glycosylate phloretin in the presence of UDP-glucose, UDP-xylose and UDP-galactose.
Interaction partners:
Sequence:
MGDVIVLYASPGMGHIVSMVELGKFIVHRYGPHKFSITILYTCGSIVDTASIPVYIRRISHSHPFISFRQFPRVTNNITRNISVPAITFDFIRQNDPHVRSALQEISKSATVRAFIIDLFCTSALPIGKEFNIPTYYFCTSGAAILAAFLYLPKIDEQTKTTESFKDLRDTVFEFPGWKSPLKATHMVQLVLDRNDPAYSDMIYFCSHLPKSNGIIVNTFEELEPPSVLQAIAGGLCVPDGPTPPVYYVGPLIEEEKELSKDADAAEKEDCLSWLDKQPSRSVLFLCFGSMGSFPAAQLKEIANGLEASGQRFLWVVKKPPVEEKSKQVHGVDDFDLKGVLPEGFLERTADRGMVVKSWAPQVVVLKKESVGGFVTHCGWNSVLEAVVAGVPMIAWPLYAEQHMNRNVLVTDMEIAIGVEQRDEEGGFVSGEEVERRVRELMESEGGRVLRERCKKLGEMASAALGETGSSTRNLVNFVSSIT
Protein: Protein SLC31A2 (Copper transporter 2) (hCTR2) (Solute carrier family 31 member 2) (O15432)
Organism: Homo sapiens (Human)
Function: Involved in low-affinity copper uptake.
Subcellular location: Membrane {ECO:0000269|PubMed:17944601}; Multi-pass membrane protein {ECO:0000255}. Cytoplasmic vesicle membrane {ECO:0000269|PubMed:17944601}; Multi-pass membrane protein {ECO:0000255}. Late endosome membrane {ECO:0000269|PubMed:17617060}; Multi-pass membrane protein {ECO:0000255}. Lysosome membrane {ECO:0000269|PubMed:17617060}; Multi-pass membrane protein {ECO:0000255}. Note=Plasma membrane localization is partial. {ECO:0000269|PubMed:17944601}.
Interaction partners:
- Copper-transporting ATPase 2
- Copper-transporting ATPase 1
- Copper transport protein ATOX1
- Cytochrome c oxidase copper chaperone
- Copper chaperone for superoxide dismutase
Sequence:
MAMHFIFSDTAVLLFDFWSVHSPAGMALSVLVLLLLAVLYEGIKVGKAKLLNQVLVNLPTSISQQTIAETDGDSAGSDSFPVGRTHHRWYLCHFGQSLIHVIQVVIGYFIMLAVMSYNTWIFLGVVLGSAVGYYLAYPLLSTA
Protein: PTS system 2-O-alpha-mannosyl-D-glycerate-specific EIIABC component (2-O-alpha-mannosyl-D-glycerate-specific phosphotransferase enzyme MngA) (Protein-Npi-phosphohistidine--2-O-alpha-mannosyl-D-glycerate phosphotransferase) [Includes: 2-O-alpha-mannosyl-D-glycerate-specific phosphotransferase enzyme IIA component (PTS system EIIA component); 2-O-alpha-mannosyl-D-glycerate-specific phosphotransferase enzyme IIB component (EC 2.7.1.195) (PTS system EIIB component); 2-O-alpha-mannosyl-D-glycerate-specific permease IIC component (PTS system EIIC component)] (P54745)
Organism: Escherichia coli (strain K12)
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. This system is involved in mannosyl-D-glycerate transport. Also involved in thermoinduction of ompC.
Subcellular location: Cell inner membrane {ECO:0000255|PROSITE-ProRule:PRU00427, ECO:0000305|PubMed:14645248}; Multi-pass membrane protein {ECO:0000255|PROSITE-ProRule:PRU00427, ECO:0000305|PubMed:14645248}.
Interaction partners:
- 1-phosphofructokinase
- ATP-dependent 6-phosphofructokinase isozyme 2
- PTS system N-acetylglucosamine-specific EIICBA component
- Phosphocarrier protein HPr
- PTS system mannitol-specific EIICBA component
- Mannosylglycerate hydrolase
- PTS system beta-glucoside-specific EIIBCA component
- Multiphosphoryl transfer protein
- Multiphosphoryl transfer protein 1
- Multiphosphoryl transfer protein 2
Sequence:
MVLFYRAHWRDYKNDQVRIMMNLTTLTHRDALCLNARFTSREEAIHALTQRLAALGKISSTEQFLEEVYRRESLGPTALGEGLAVPHGKTAAVKEAAFAVATLSEPLQWEGVDGPEAVDLVVLLAIPPNEAGTTHMQLLTALTTRLADDEIRARIQSATTPDELLSALDDKGGTQPSASFSNAPTIVCVTACPAGIAHTYMAAEYLEKAGRKLGVNVYVEKQGANGIEGRLTADQLNSATACIFAAEVAIKESERFNGIPALSVPVAEPIRHAEALIQQALTLKRSDETRTVQQDTQPVKSVKTELKQALLSGISFAVPLIVAGGTVLAVAVLLSQIFGLQDLFNEENSWLWMYRKLGGGLLGILMVPVLAAYTAYSLADKPALAPGFAAGLAANMIGSGFLGAVVGGLIAGYLMRWVKNHLRLSSKFNGFLTFYLYPVLGTLGAGSLMLFVVGEPVAWINNSLTAWLNGLSGSNALLLGAILGFMCSFDLGGPVNKAAYAFCLGAMANGVYGPYAIFASVKMVSAFTVTASTMLAPRLFKEFEIETGKSTWLLGLAGITEGAIPMAIEDPLRVIGSFVLGSMVTGAIVGAMNIGLSTPGAGIFSLFLLHDNGAGGVMAAIGWFGAALVGAAISTAILLMWRRHAVKHGNYLTDGVMP
Protein: U4/U6.U5 small nuclear ribonucleoprotein 27 kDa protein (U4/U6.U5 tri-snRNP-associated protein 3) (Q8I7W6)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
MGRSRSPASPAHRRREKERSERKKRREPRSREREAIGVAPAGGSGSGGAGRRDRERDRDRSRSRDRERERERDRARSRRSRSRSRVAGGGGGGGGGGSSGGNSSSGPSTSRRTTRNNAAATAADRPKINEADLEGKSPEEVEMLKTMGFCTFDTTKNRKVEGNDVGEVHVILKRKYRQYMNRKGGFNRPLDFVA
Protein: WASH complex subunit homolog 1 (O18195)
Organism: Caenorhabditis elegans
Function: Acts as a component of the WASH core complex that functions as a nucleation-promoting factor (NPF) at the surface of endosomes, where it recruits and activates the Arp2/3 complex to induce actin polymerization, playing a key role in the fission of tubules that serve as transport intermediates during endosome sorting (By similarity). Acts as a component of the DHIC (ddl-1-containing hsf-1 inhibitory complex) which modulates lifespan by sequestering the heat shock transcription factor hsf-1 to negatively regulate its binding to DNA and its transcriptional activity.
Interaction partners:
- WASH complex subunit homolog 3
- Heat shock factor-binding protein 1
- WASH complex subunit strumpellin
- Heat shock transcription factor hsf-1
- HEPN_LA2681 domain-containing protein
- TPR_REGION domain-containing protein
Sequence:
MYHVPLIPRDAGREETIFRINQSLQKLLRVSDEIFDRVEHRITRIHGKAEAIDRRTEVLEKKLESLQESDKVITFTLPRQLPKLPEEPPTSTSLFRINIDTEHFPGSEELPAFRRADDHVLRPCEPIDFTYELNKPDKFFLTSQVLKEYEQKGWERYKKRLLGGLRELSRSPEHIAELFYAGTSIPAFEGVSGDFSKKALDADDDGGTSRSGRTTDELAQLRLHEQLLEDTALSSTLMQEDSLDDNHPLAFRINFNEKKKKTAKMVEMPDSLPNLKGHAHDFTLRDPEIDEDRLLDILPADDQIPEASEPTEAEADAPTTFILPPPPPPMKLDPSPQPAATPVEITEIPPIISPPAPPPPPPPPPPPPPPQTPSASSSVTFSPTKSVDGGRSDLMAAIRAAGGAGNAKLSRIAEKPKRKGKFDGILESSALLGASETPRNSAPAPDGGGGGGDLMSALSKALDARRKAINGKVEAQPPAKVSSTIPAPPNFDDEEWD
Protein: Desmocollin-1 (P55849)
Organism: Mus musculus (Mouse)
Function: Component of intercellular desmosome junctions. Involved in the interaction of plaque proteins and intermediate filaments mediating cell-cell adhesion. May contribute to epidermal cell positioning (stratification) by mediating differential adhesiveness between cells that express different isoforms. Linked to the keratinization of epithelial tissues.
Subcellular location: Cell membrane {ECO:0000250|UniProtKB:Q08554}; Single-pass type I membrane protein {ECO:0000255}. Cell junction, desmosome {ECO:0000269|PubMed:11714727, ECO:0000269|PubMed:38395410}.
Interaction partners:
- Desmoglein-1-alpha
- Desmoglein-1-beta
- Corneodesmosin
- Desmoglein-1-gamma
- Junction plakoglobin
- Desmoplakin
- Desmoglein-3
- Plakophilin-1
- Desmoglein-2
- Plakophilin-3
Sequence:
MAVACAAPGSTFSKQLLFFLLVLVLFCDACQKVSLHVPSHLKAETPVGKVNLEECLKSPSLILSSDPAFRILEDGTIYTTHDLLLSSEKRGFSILLSDGQGQEQKKLEVVLSAREKKVFRKRHTKEPVHNRSKRRWAPIPCSLMENSLGPFPQHIQQIQSDAAQNYTIFYSISGPGVDKEPYNLFYIEKDTGDIYCTRSIDREQYDQFLVYGYATTADGYAPDYPLPLLFKVEDDNDNAPYFETKLTVFSVPENCRSGTSVGQVTAIDKDEPGTLHTRLKYKILQQIPDQPKHFSIHPDTGVITTTTPLLDREKCDTYKLVMEVRDMGGQPFGLFTTGTITISLEDENDNSPYFTQTSYTTEVEENRIDVEILRMVVHDQDLPNTPHSKAVYTILKGNENGNFKITTDPNTNEGVLCVVKPLNYEVSRQVTLQIGVLNEAQFTNAANAQPPTMCTTTVTVKIKDRDEGPECQPPVKVIQSKDGLPAGQELLGYKAVDPETSSGEGLRYEMVGDEDNWFEINKITGDLRTVKVLDRESKFVKNNQYNISVVATDTAGRSCTGTLVVLLEDFNDHPPQIDKEVTICQQEKDFAVLEPIDLDGPDNGPPFQFLLDNSSSKLWTLESQDGKRAILRQRHNLNYNYYSVPIQIQDRHGFSAKHVLSVRVCDCTTPTECRMAVKEERDAKPNIILGKWAILAMVLGSALLLCILFTCFCVTTTKRTVKKCFPDDVAQQNLIVSNTEGPGEEVTEANIRLPTQTANICDTSMSVGTLGGQGIKTQQSFEMVKGGHTLESHKGGVLGAAEPGRYAYTDWQTFTQPRLGEKVYLCGQAEEHKHCEDYVRPYNYEGKGSMAGSVGCCSDRQEEEGLEFLDQLEPKFRTLAKTCVKK
Protein: Aminopeptidase (EC 3.4.11.-) (B0BCY8)
Organism: Homo sapiens (Human)
Subcellular location: Cell membrane {ECO:0000256|ARBA:ARBA00004401}; Single-pass type II membrane protein {ECO:0000256|ARBA:ARBA00004401}.
Interaction partners:
Sequence:
MNFAEREGSKRYCIQTKHVAILCAVVVGVGLIVGLAVGLTRSCDSSGDGGPGTAPAPSHLPSSTASPSGPPAQDQDICPASEDESGQWKNFRLPDFVNPVHYDLHVKPLLEEDTYTGTVSISINLSAPTRYLWLHLRETRITRLPELKRPSGDQVQVRSCFEYKKQEYVVVEAEEELTPSSGDGLYLLTMEFAGWLNGSLVGFYRTTYTENGQVKSIVATDHEPTDARKSFPCFDEPNKKATYTISITHPKEYGALSNMPVAKEESVDDKWTRTTFEKSVPMSTYLVCFAVHQFDSVKRISNSGKPLTIYVQPEQKHTAEYAANITKSVFDYFEEYFAMNYSLPKLDKIAIPDFGTGAMENWGLITYRETNLLYDPKESASSNQQRVATVVAHELVHQWFGNIVTMDWWEDLWLNEGFASFFEFLGVNHAETDWQMRDQMLLEDVLPVQEDDSLMSSHPIIVTVTTPDEITSVFDGISYSKGSSILRMLEDWIKPENFQKGCQMYLEKYQFKNAKTSDFWAALEEASRLPVKEVMDTWTRQMGYPVLNVNGVKNITQKRFLLDPRANPSQPPSDLGYTWNIPVKWTEDNITSSVLFNRSEKEGITLNSSNPSGNAFLKINPDHIGFYRVNYEVATWDSIATALSLNHKTFSSADRASLIDDAFALARAQLLDYKVALNLTKYLKREENFLPWQRVISAVTYIISMFEDDKELYPMIEEYFQGQVKPIADSLGWNDAGDHVTKLLRSSVLGFACKMGDREALNNASSLFEQWLNGTVSLPVNLRLLVYRYGMQNSGNEISWNYTLEQYQKTSLAQEKEKLLYGLASVKNVTLLSRYLDLLKDTNLIKTQDVFTVIRYISYNSYGKNMAWNWIQLNWDYLVNRYTLNNRNLGRIVTIAEPFNTELQLWQMESFFAKYPQAGAGEKPREQVLETVKNNIEWLKQHRNTIREWFFNLLESG
Protein: V-type proton ATPase subunit C (V-ATPase subunit C) (Vacuolar proton pump subunit C) (P54648)
Organism: Dictyostelium discoideum (Social amoeba)
Function: Subunit of the peripheral V1 complex of vacuolar ATPase. Subunit C is necessary for the assembly of the catalytic sector of the enzyme and is likely to have a specific function in its catalytic activity. V-ATPase is responsible for acidifying a variety of intracellular compartments in eukaryotic cells (By similarity).
Interaction partners:
- V-type proton ATPase subunit B
- V-type proton ATPase subunit D
- V-type proton ATPase subunit F
- V-type proton ATPase subunit E
- V-type proton ATPase subunit H
- Vacuolar proton translocating ATPase 100 kDa subunit
- V-type proton ATPase proteolipid subunit
- V-type proton ATPase subunit G
- V-type proton ATPase subunit d
- V-ATPase proteolipid subunit C-like domain-containing protein
Sequence:
MSETQEFWLISAPNLPGADIFDQVNQKTAKENSLSENKKFNTPALRVGTLNSLITLNDELQKIDTIVESTTKKIARQLVDLVGTKPGKDKSLSINGHTIPQYLQQFAWDDAKYNLKLSLQEIVEKISSAVSKIDDDLKIKSSEYSTLSSSVASEERKASGNLQVRTLNDLITADNIVQTDYFTTAFVVIPKQSEKEFLACYETISDFVLGRSAKRVAQDNDYFLYSVILFKKFYENFKTKIIEKKWVVRDFKLEDNKPTQERSKLTEDKKNCRTSLIRWCRLNFPEAFMAWVHLKVVRVFVESVLRFGIPFNFQAILMKPQKGADKKVRDILFDQFKYLGSAHISGKNETDDSEKFYPYISVSVNWEN
Protein: Sporulation protein 23 (P33757)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Regulates expression of PIS1.
Interaction partners:
- Putative meiotic phospholipase SPO1
- Arrestin-related trafficking adapter 10
- Protein LDB19
- Uncharacterized protein YNR068C
Sequence:
MLFSSSSSSLNSEVSQVFSENISSRSTTLTESSTQSEIRQHFGNEDFSGELPKKLIQLKKLKNGGTTIKKAKEDLEYCYDSLRLYENPYVTSSVDKKCGYSIELYLDNKYKTLMFSDLQLNADYPLYYDSSLDNISTNVERERATPLQIKGKIRINIDREDQALLITSHSISLKCFTKEYACFVNSETSKNSYSDKIIKELNHTEFFESSTYPKQQLRVIHHSLNDKKILLTKGTYDYPFTFTLQANTFPASFSSFFGKTHFRIESLTTIMRIPSKPKNLLKFLKNESFTDKIILTEEIKVKRVLPSTSMLKFETFQLRSYNTASEIVVSVIGNSKLIEIGMPFQMILSITKTDSSIELQEASLAVAQRMAIPSIDLKTKKILREPYIKKSEYLLRTVESQSFDSDKTIFGFCFDDVVIPTYADGLPSWFKTFYCEPSSFYPNHAALKVTHLLLFRITYSRNELVEGLEMKKNYRITVNFPILVGDSDISTSSLLPKYEKFENISDLQDEPPLYSMVAGENSL
Protein: LIM domain binding 3 (A0A0G2JXR0)
Organism: Rattus norvegicus (Rat)
Subcellular location: Cytoplasm, myofibril, sarcomere, Z line {ECO:0000256|ARBA:ARBA00004216}.
Interaction partners:
Sequence:
MSYSVTLTGPGPWGFRLQGGKDFNMPLTISRITPGSKAAQSQLSQGDLVVAIDGVNTDTMTHLEAQNKIKSASYNLSLTLQKSKRPIPISTTAPPIQSPLPVIPHQKDPSLDTNSSLATPSPSPEARASPGTSGTLEFGDTFSSSFSQTSVCTSHMEASGPVLPLGSPVAKASSEGTQGSVSPKVLPGPSQPRLYNNPIGLYSAETLREMAQMYQMSLRGKASGAGLLGGSLPVKDLAVDSASPVYQAVIKTQSKPEDEADEWARRSSNLQSRSFRILAQMTGTEYMQDPDEEALRRSRERFETERNSPRFAKLRNWHHGLSAQILNVKS
Protein: Zinc finger C2HC domain-containing protein 1A (Q96GY0)
Organism: Homo sapiens (Human)
Interaction partners:
- Cytosolic arginine sensor for mTORC1 subunit 1
Sequence:
MEGLEENGGVVQVGELLPCKICGRTFFPVALKKHGPICQKTATKKRKTFDSSRQRAEGTDIPTVKPLKPRPEPPKKPSNWRRKHEEFIATIRAAKGLDQALKEGGKLPPPPPPSYDPDYIQCPYCQRRFNENAADRHINFCKEQAARISNKGKFSTDTKGKPTSRTQVYKPPALKKSNSPGTASSGSSRLPQPSGAGKTVVGVPSGKVSSSSSSLGNKLQTLSPSHKGIAAPHAGANVKPRNSTPPSLARNPAPGVLTNKRKTYTESYIARPDGDCASSLNGGNIKGIEGHSPGNLPKFCHECGTKYPVEWAKFCCECGIRRMIL
Protein: PH domain-containing protein (Q582W2)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
Sequence:
MDAKLVFCAHSLKLPTLSIPPALSVDNETINFRCPEPLAEAGFPVPNASFTADVMMEQPQSRSIYQRVFATAARDFEGRKNLVVFSYGVRSTPKRQLMFGSESGSGYAAKIIGDVVDVGATKGIFAISAYGVGSSEHLTDFTDENNEMGVIVESVKEGPRVRMVGRVRVTSSEDVRSVFNTVTKNYQKHFESVLRERQPTAELEALPPYMPESMILQLYRYDDEEAFSEYVEANSMTFVALGDSERPVLCGIEEETQQEYEKTQKVLASAVGIISSIRCNRLRIPFGKSKLSQLLRRAYNAEKGNPNNGYNEPTSTVFIIHAFTDAVWAEESYHCLLLSRRVSSVVGTSSIGSITRDLSVDKWRLDQDIMELRDELQIARTVYDYRPCIYDQPKPVQNIREEEQKRISAIVSKREEARERQLSLVREQAKQDADKIIKDLEARTGTTLSALEASLEAKMKENSALHADREKRIHEYEQTLEKIRKKKQEEESACEKLREEMLQLEQELSVRQNAIESKQKNLEMIKLDKSKGRDAVMRERQSIQAMRKTVLEERRRQRKQWINQIKEINAKVIDQVRMLAEERKKNGEQPTANEEAAEKAIIADVRTIEEYLPKLISLEDVPVNLEETEAIRRQFADVFAEEKKTYLARIEEEKARREKLERGLEVYRQRLLDTYQAKKKEKVHDAITKEQHLSSLVDQVITYLRNGVRMSKISSKGNIRRRFYFLSEDYKRIHSCEIDNQGAPISRKKPPVTIWLKDIKKVVIGVYTSSFTNFSSEAQLAKTRQEAVSDSGTYRQDPTQNITSANLGLHNYRSFALLLRGGKSLEVVCETDSDCEAWLVALKRLLQIKSPIERILEERMNGNTTKESPSNTHEGAVDIKWGGSLDIHNMRGFVSLSSEEATLCSENHIPPALFLRMKQEMAEKAERNTITIYDVRVSSGLDLFRSGKLYDFLCEKRVIPLPY