wanglab/gogpt-training-data huggingface dataset:
Protein: NADH-quinone oxidoreductase subunit J (EC 7.1.1.-) (P95172)
Organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Subcellular location: Cell membrane {ECO:0000256|RuleBase:RU004429}; Multi-pass membrane protein {ECO:0000256|RuleBase:RU004429}.
Interaction partners:
- NADH-quinone oxidoreductase subunit F
- NADH-quinone oxidoreductase subunit D
- NADH-quinone oxidoreductase subunit A
- Uncharacterized response regulatory protein Rv3143
- NADH-quinone oxidoreductase subunit M
- NADH-quinone oxidoreductase subunit L
- NADH-quinone oxidoreductase subunit I
- NADH-quinone oxidoreductase subunit B
- NADH-quinone oxidoreductase subunit E
- NADH-quinone oxidoreductase subunit H
Sequence:
MTAVLASDVIVRTSTGEAVMFWVLSALALLGAVGVVLAVNAVYSAMFLAMTMIILAVFYMAQDALFLGVVQVVVYTGAVMMLFLFVLMLIGVDSAESLKETLRGQRVAAVLTGVGFGVLLISTIGQVATRGFAGLTVANANGNVEGLAALIFSRYLWAFELTSALLITAAVGAMVLAHRERFERRKTQRELSQERFRPGGHPTPLPNPGVYARHNAVDVAALLPDGSYSELSVPRMLRTRGADGLQTPSPGAVSGSLEGGAS
Protein: U3 small nucleolar RNA-associated protein 6 (U3 snoRNA-associated protein 6) (U three protein 6) (Q02354)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Component of the SSU processome, a pre-ribosomal particle required for the maturation of the 18S rRNA from the 35S pre-rRNA precursor.
Subcellular location: Nucleus, nucleolus {ECO:0000269|PubMed:12068309, ECO:0000269|PubMed:12150911}.
Interaction partners:
- Ribosomal RNA small subunit methyltransferase NEP1
- rRNA 2'-O-methyltransferase fibrillarin
- U3 small nucleolar RNA-associated protein 5
- Nucleolar complex protein 14
- Something about silencing protein 10
- U3 small nucleolar RNA-associated protein 9
- U3 small nucleolar ribonucleoprotein protein IMP4
- rRNA biogenesis protein RRP36
- U3 small nucleolar RNA-associated protein 12
- U3 small nucleolar RNA-associated protein 7
Sequence:
MSKTRYYLEQCIPEMDDLVEKGLFTKNEVSLIMKKRTDFEHRLNSRGSSINDYIKYINYESNVNKLRAKRCKRILQVKKTNSLSDWSIQQRIGFIYQRGTNKFPQDLKFWAMYLNYMKARGNQTSYKKIHNIYNQLLKLHPTNVDIWISCAKYEYEVHANFKSCRNIFQNGLRFNPDVPKLWYEYVKFELNFITKLINRRKVMGLINEREQELDMQNEQKNNQAPDEEKSHLQVPSTGDSMKDKLNELPEADISVLGNAETNPALRGDIALTIFDVCMKTLGKHYINKHKGYYAISDSKMNIELNKETLNYLFSESLRYIKLFDEFLDLERDYLINHVLQFWKNDMYDLSLRKDLPELYLKTVMIDITLNIRYMPVEKLDIDQLQLSVKKYFAYISKLDSASVKSLKNEYRSYLQDNYLKKMNAEDDPRYKILDLIISKL
Protein: 27 kDa antibacterial protein (P81925)
Organism: Cyprinus carpio (Common carp)
Function: Has antibacterial activity. It inhibits fish bacterial pathogens, A.hydrophila and M.luteus, and also E.coli, P.fluorescens and S.aureus. Forms large ion channels responsible for disrupting the cellular envelope of bacteria leading to cell lysis.
Interaction partners:
Sequence:
GIGGKPVQTAFVDNDGIYD
Protein: Collagen alpha-1(III) chain (P04258)
Organism: Bos taurus (Bovine)
Function: Collagen type III occurs in most soft connective tissues along with type I collagen. Involved in regulation of cortical development. Is the major ligand of ADGRG1 in the developing brain and binding to ADGRG1 inhibits neuronal migration and activates the RhoA pathway by coupling ADGRG1 to GNA13 and possibly GNA12 (By similarity).
Subcellular location: Secreted, extracellular space, extracellular matrix {ECO:0000250}.
Interaction partners:
Sequence:
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
Protein: Flagellin B (Flagellin N) (Q07911)
Organism: Helicobacter pylori (strain ATCC 700392 / 26695) (Campylobacter pylori)
Function: Flagellin is the subunit protein which polymerizes to form the filaments of bacterial flagella. Important for motility and virulence.
Subcellular location: Secreted. Bacterial flagellum.
Interaction partners:
- Flagellar secretion chaperone FliS
- Flagellar hook-associated protein 2
- Flagellar motor switch protein FliN
- Flagellar hook-associated protein 1
- Flagellin A
- 6-hydroxymethylpterin diphosphokinase MptE-like domain-containing protein
- Flagellar motor switch protein FliG
- Flagellar hook protein FlgE
- Flagellar motor switch protein FliM
- Flagellar basal body rod protein FlgB
Sequence:
MSFRINTNIAALTSHAVGVQNNRDLSSSLEKLSSGLRINKAADDSSGMAIADSLRSQSANLGQAIRNANDAIGMVQTADKAMDEQIKILDTIKTKAVQAAQDGQTLESRRALQSDIQRLLEELDNIANTTSFNGQQMLSGSFSNKEFQIGAYSNATVKASIGSTSSDKIGHVRMETSSFSGAGMLASAAAQNLTEVGLNFKQVNGVNDYKIETVRISTSAGTGIGALSEIINRFSNTLGVRASYNVMATGGTPVQSGTVRELTINGVEIGTVNDVHKNDADGRLTNAINSVKDRTGVEASLDIQGRINLHSIDGRAISVHAASASGQVFGGGNFAGISGTQHAVIGRLTLTRTDARDIIVSGVNFSHVGFHSAQGVAEYTVNLRAVRGIFDANVASAAGANANGAQAETNSQGIGAGVTSLKGAMIVMDMADSARTQLDKIRSDMGSVQMELVTTINNISVTQVNVKAAESQIRDVDFAEESANFSKYNILAQSGSFAMAQANAVQQNVLRLLQ
Protein: WD repeat-containing protein 26 (A0A0H5BJW1)
Organism: Xenopus laevis (African clawed frog)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
MQANGAAGEEPAGSGSLSAHNGESSEPAHSNGLLSNNNNNGLSSSSSAPAEQPGVKKKKRLSQADEDVIRLIGQHLHGLGLNQTVELLMQESGCRLEHPSATKFRNHVMEGEWDKAENDLNELKSLVHSPHAVVACRPSSGGSGSEHSSVSCPTTDVIRRMKFLLLQQKYLEYLEDGKVLEALQVLRCELTPLKYNTERIHVLSGYLMCSHADDLRAKAEWEGKGTASRSKLLDKLQTYLPPSVMLPPRRLQTLLRQAVELQRDRCLYHNTKLDNNLDSVSLLIDHVCSRKQFPCFTQQVLTEHCNEVWFCKFSNDGTKLATGSKDTTVIIWQVDPDTHQLKLLKTLEGHAYGVSYLAWSPDDNYLIACGPDDCSELWLWNVQTGELRTKMSQSHEDSLTSVAWNPDGKRFVTGGQRGQFYQCDLDGNLLDSWEGVRVQCLWCLSDGKTVLASDTHQRIRGYNFEDLTDRNIVQEDHPIMSFTISRNGRLALLNVATQGVHLWDLQDRVLVRKYQGVTQGFYTIHSCFGGHNEDFIASGSEDHKVYVWHKKSELPIAELTGHTRTVNCVSWNPQIPSLMASASDDGTVRIWGPAPYVDNQEFEEECSSMDS
Protein: Cornichon protein (Q381F1)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
Sequence:
MGILQHQADVWHALRYPSKHSWGERKRAYLFVFAYCLAAIALFASVMHFIGAWIACGLLQVIMLIFAMLFALNIADCRDKCLNVLECERAINPVMEVYIGLRFIQFLHATFLLTNIPMGVSILVALLYSLWRMWCGTYFVDATSLWREVGRLERDSYIHICIEIALIVIYLIAIVFAMVDKYS
Protein: Ras GTPase-activating protein 3 (GAP1(IP4BP)) (Ins P4-binding protein) (Q14644)
Organism: Homo sapiens (Human)
Function: Inhibitory regulator of the Ras-cyclic AMP pathway. Binds inositol tetrakisphosphate (IP4) with high affinity. Might be a specific IP4 receptor.
Subcellular location: Cell membrane.
Interaction partners:
- Ras-related protein R-Ras
- GTPase NRas
- GTPase HRas
- Ras-related protein Rap-1A
- GTPase KRas
- Ras-related protein M-Ras
- Ras GTPase-activating protein 1
Sequence:
MAVEDEGLRVFQSVKIKIGEAKNLPSYPGPSKMRDCYCTVNLDQEEVFRTKIVEKSLCPFYGEDFYCEIPRSFRHLSFYIFDRDVFRRDSIIGKVAIQKEDLQKYHNRDTWFQLQHVDADSEVQGKVHLELRLSEVITDTGVVCHKLATRIVECQGLPIVNGQCDPYATVTLAGPFRSEAKKTKVKRKTNNPQFDEVFYFEVTRPCSYSKKSHFDFEEEDVDKLEIRVDLWNASNLKFGDEFLGELRIPLKVLRQSSSYEAWYFLQPRDNGSKSLKPDDLGSLRLNVVYTEDHVFSSDYYSPLRDLLLKSADVEPVSASAAHILGEVCREKQEAAVPLVRLFLHYGRVVPFISAIASAEVKRTQDPNTIFRGNSLASKCIDETMKLAGMHYLHVTLKPAIEEICQSHKPCEIDPVKLKDGENLENNMENLRQYVDRVFHAITESGVSCPTVMCDIFFSLREAAAKRFQDDPDVRYTAVSSFIFLRFFAPAILSPNLFQLTPHHTDPQTSRTLTLISKTVQTLGSLSKSKSASFKESYMATFYEFFNEQKYADAVKNFLDLISSSGRRDPKSVEQPIVLKEGFMIKRAQGRKRFGMKNFKKRWFRLTNHEFTYHKSKGDQPLYSIPIENILAVEKLEEESFKMKNMFQVIQPERALYIQANNCVEAKDWIDILTKVSQCNQKRLTVYHPSAYLSGHWLCCRAPSDSAPGCSPCTGGLPANIQLDIDGDRETERIYSLFNLYMSKLEKMQEACGSKSVYDGPEQEEYSTFVIDDPQETYKTLKQVIAGVGALEQEHAQYKRDKFKKTKYGSQEHPIGDKSFQNYIRQQSETSTHSI
Protein: Cytosolic carboxypeptidase 4 (EC 3.4.17.-) (EC 3.4.17.24) (ATP/GTP-binding protein-like 1) (Protein deglutamylase CCP4) (Q09M05)
Organism: Mus musculus (Mouse)
Function: Metallocarboxypeptidase that mediates deglutamylation of tubulin and non-tubulin target proteins. Catalyzes the removal of polyglutamate side chains present on the gamma-carboxyl group of glutamate residues within the C-terminal tail of tubulin protein. Specifically cleaves tubulin long-side-chains, while it is not able to remove the branching point glutamate. Also catalyzes the removal of polyglutamate residues from the carboxy-terminus of non-tubulin proteins such as MYLK.
Subcellular location: Cytoplasm, cytosol {ECO:0000250|UniProtKB:Q96MI9}.
Interaction partners:
- Lipoxygenase homology domain-containing protein 1
- Solute carrier family 4 member 11
- KN motif and ankyrin repeat domain-containing protein 4
Sequence:
MAEQEGSGLQMLLHTLQNSSDKASTLSILQVLGDLLSVGTDRRIYYMISKGGSEALLQTLVDTARSSSPDWDILLPLFRLLAKVGLRDKKFGQKALELEALDVTLILARKNLSHSQNLLHCLWVLRVFASSVTTGAMLGINGAMELLFKVLSPYTRKHTRTIRAATEVLAALLKSSKHLRRAVNRGYVNSLLRLHQDWHSRDVTNTYVTIRHGLLLCLRHIVALRSGREAFLAAQGMETLFSSAQTCLENKNMELVISAVIQILRQCYPASRLPLVTASSAYTFPAPGSTSSELPLNLTEEDFDDDGDEEMDKDSDVEAVKEDDDLETDLSKLSSKPGLDLPEEELAQYDAMCPELSCSFEELEPKCGDDLNNKDTLHANHHHIPSVASLRQHCFNREHSSWRQEREDTVHSSILHMVKTGKSGVPSSSKQRSATNVNQSLQQNGLEIDSSGHDTSDIQAPLEQAAWDMEAISCPRITASFPNSTKPEESIGAAEKLLHTHAKHIPFHDPHLYIANAMRTRSAVGFKTMAFPDLWGHCPPPAAQPMLDRKLGVQRIKILEDIRRLLHPSDVINKVVFSLDEPRPLQGSISNCLMFHSKFESGNLRKAIQVREFEYDLLVNADVNSSQHQQWFYFKVSGMRAAVPYHFNIINCEKPNSQFNYGMQPTLYSVKEALLGRPAWIRTGSDICYYKNHYRQNAATMDGALGKRYYTLTFAVTFPHNEDACYLAYHYPYTYSTLMTHLEILERSIDHREIYFRHDVLCQTLGGNPCPLVTITAFPESNSTEHLEQFRCRPYQVITARVHPGESNASWVMKGTLEFLVSSDPVAKLLRENFVFKIIPMLNPDGVINGNHRCSLRGEDLNRQWLSPQAHLQPTIYHAKGLLHYLSSTGRGPVVFCDFHGHSQKKNVFLYGCSMKETLWQAGCTVGESALLEDVSYRTLPKILDKLAPAFTMNSCSFLVEKSRASTARVVVWREMGVSRSYTMESSYCGCNQGPYQGLQFGTGELEEMGAMYCLGLLILELKSVNCSHKLLARASSLLNADVLEHYLQRCSSSSSNSSNRTSEVDDEPYCMEEIDYSADSSSDAEQNFTELDRQIQECALNKDEEEEEKEEGTGWRRRSVT
Protein: Citrate synthase (Q388Q5)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
- Aconitate hydratase
- Acetyl-coenzyme A synthetase
- Malate dehydrogenase
- Succinate--CoA ligase subunit beta, mitochondrial
- malate dehydrogenase
- malate dehydrogenase
- Malate dehydrogenase
- Dihydrolipoamide acetyltransferase component of pyruvate dehydrogenase complex
- Dihydrolipoamide acetyltransferase, putative
- hydroxymethylglutaryl-CoA lyase
Sequence:
MCMRARYSSGIVRGAMLRGFSSSPSLFCAAAGGSPIFDELKLSILKKHQSDAPRIKQLIAKHGGDKLSESTVSSMYGGMRGVTGFVYEPSYLDKEVGIRFRGLTISECCEKLPKSWRGGSSPLPEGMLWLLVTGTIPNERQVKEMHEELHRRADERAISAAVKTIASLPDNSHPMTQFGAGLMALQTYSKFATAYSQGKANKTNYWEYALDDSLDLIARSSHVAAIVYNRLATGKAQLANPSDPNLDWAANFTNMLGYKDESFWDCMRLYLCLHADHEGGNVSAHATVLVASALSDPYLSLVAGLAGLAGPLHGLANQEVLTYLFEMRDKCKAAGVDLHDRKRLAAELEKLTWDVLNAKRVVPGYGHAVLGMTDPRYTCFREYCKNNFPNDELFILVDAIYEIMPGILKKHGKVRNPFPNVDAQSGVLLQHYGMKEQLFYTVLFGLSRQLGVLTGIVWDRLQGRPIERPKTMTSESLLTKYNIA
Protein: ATP-dependent RNA helicase (EC 3.6.4.13) (Q57WU5)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
- rRNA biogenesis protein, putative
- Nucleolar complex protein 2
- RNA helicase
- Ribosome biogenesis protein BOP1 homolog
- ATP-dependent RNA helicase
- Nop14-like protein
- Pescadillo homolog
- ATP-dependent DEAD/H RNA helicase, putative
- U3 small nucleolar RNA-associated protein 18
- ATP-dependent RNA helicase
Sequence:
MSLAGSERAHLCVHGLTENDEQDALRHLLSATGSSQLTDISDEVVVKGAAKRKNQAATQCANSSESIKDKKTQRSSEVQQQKPDGGTVGRVKKSSDVPVKRTASKVVPVPKEVEAESVAFQADSVSHEAESLPPIAELVHKKLIRPLTEVLCINSLTRIQKLSWMPMVDKTRDVLVRSETGSGKTLAYALPLLHQLLCDCDTRPLKRDVGSVIIVLCPVRELVVQVSDVLTILTRCALFLTVGGIHGGENRHKEKARLRKGITILATTPGRLLDHLKATSSFRVEELQTIVLDEADRLLDMGFEKTIREVMDLLVAKKRDAHQTGGGDAQSSFKRVLVSATITAAVERLSHFALRDNIVRVGETEDTFSIPSSLRQHYVLVPTKHRLATLISFLRSQLDAGAQRLIVFVSTADSAEFHYYLLSRLKSPFRGKTNSGRSAGAPQKNSNRYSLKKRIGEANRHIHEGRDEDVVTFDDDSDDEDPTEVSELSEKNAVLDVNIFKLHGNMSQVDRASVFHAFKHMDSSVQPSKKGILFCTDVAARGLDMPNVDWIVHYDPPTDAPCYIHRIGRTARIGNTGDSMLFLMPHEEGYASYLSNFLAKETKLGSMAKGANAESGIIEERKYESFLFYLTKLDPKANHMWAQSTATLERAICRLVMKRHSNEENVNDESTGRTDDITRLALFAYQSYIRAYAGHSRELKRLFFNSDALHLGHVAQNFGIDKRPSEVRSQLQGLIKEDRKVARETTSVVLDDGSERPRKVLRTEVPHDDRYRSTVVQKQRKVTRDWYENKKKLEGPTYKHQQFTEFDA
Protein: WD repeat-containing protein 26 (CUL4- and DDB1-associated WDR protein 2) (Myocardial ischemic preconditioning up-regulated protein 2) (Q9H7D7)
Organism: Homo sapiens (Human)
Function: G-beta-like protein involved in cell signal transduction. Acts as a negative regulator in MAPK signaling pathway. Functions as a scaffolding protein to promote G beta:gamma-mediated PLCB2 plasma membrane translocation and subsequent activation in leukocytes. Core component of the CTLH E3 ubiquitin-protein ligase complex that selectively accepts ubiquitin from UBE2H and mediates ubiquitination and subsequent proteasomal degradation of the transcription factor HBP1. Acts as a negative regulator of the canonical Wnt signaling pathway through preventing ubiquitination of beta-catenin CTNNB1 by the beta-catenin destruction complex, thus negatively regulating CTNNB1 degradation. Serves as a scaffold to coordinate PI3K/AKT pathway-driven cell growth and migration. Protects cells from oxidative stress-induced apoptosis via the down-regulation of AP-1 transcriptional activity as well as by inhibiting cytochrome c release from mitochondria. Protects also cells by promoting hypoxia-mediated autophagy and mitophagy (By similarity).
Subcellular location: Cytoplasm {ECO:0000269|PubMed:15378603}. Nucleus {ECO:0000269|PubMed:29911972}. Mitochondrion {ECO:0000250|UniProtKB:F1LTR1}.
Interaction partners:
- Glucose-induced degradation protein 8 homolog
- E3 ubiquitin-protein transferase RMND5A
- Ran-binding protein 9
- Armadillo repeat-containing protein 8
- Ran-binding protein 10
- E3 ubiquitin-protein transferase RMND5B
- Glucose-induced degradation protein 4 homolog
- E3 ubiquitin-protein transferase MAEA
- Muskelin
- Homeobox protein goosecoid
Sequence:
MQANGAGGGGGGGGGGGGGGGGGGGQGQTPELACLSAQNGESSPSSSSSAGDLAHANGLLPSAPSAASNNSNSLNVNNGVPGGAAAASSATVAAASATTAASSSLATPELGSSLKKKKRLSQSDEDVIRLIGQHLNGLGLNQTVDLLMQESGCRLEHPSATKFRNHVMEGDWDKAENDLNELKPLVHSPHAIVVRGALEISQTLLGIIVRMKFLLLQQKYLEYLEDGKVLEALQVLRCELTPLKYNTERIHVLSGYLMCSHAEDLRAKAEWEGKGTASRSKLLDKLQTYLPPSVMLPPRRLQTLLRQAVELQRDRCLYHNTKLDNNLDSVSLLIDHVCSRRQFPCYTQQILTEHCNEVWFCKFSNDGTKLATGSKDTTVIIWQVDPDTHLLKLLKTLEGHAYGVSYIAWSPDDNYLVACGPDDCSELWLWNVQTGELRTKMSQSHEDSLTSVAWNPDGKRFVTGGQRGQFYQCDLDGNLLDSWEGVRVQCLWCLSDGKTVLASDTHQRIRGYNFEDLTDRNIVQEDHPIMSFTISKNGRLALLNVATQGVHLWDLQDRVLVRKYQGVTQGFYTIHSCFGGHNEDFIASGSEDHKVYIWHKRSELPIAELTGHTRTVNCVSWNPQIPSMMASASDDGTVRIWGPAPFIDHQNIEEECSSMDS
Protein: CD70 antigen (CD27 ligand) (CD27-L) (Tumor necrosis factor ligand superfamily member 7) (CD antigen CD70) (P32970)
Organism: Homo sapiens (Human)
Function: Cytokine which is the ligand for CD27. The CD70-CD27 pathway plays an important role in the generation and maintenance of T cell immunity, in particular during antiviral responses. Upon CD27 binding, induces the proliferation of costimulated T-cells and enhances the generation of cytolytic T-cells.
Subcellular location: Cell membrane {ECO:0000269|PubMed:11920585, ECO:0000269|PubMed:28011863, ECO:0000269|PubMed:28011864, ECO:0000269|PubMed:8120384, ECO:0000269|PubMed:8387892}; Single-pass type II membrane protein {ECO:0000255}.
Interaction partners:
- CD27 antigen
- Tumor necrosis factor receptor superfamily member 4
- Tumor necrosis factor receptor superfamily member 9
- T-cell-specific surface glycoprotein CD28
- CD40 ligand
- Tumor necrosis factor ligand superfamily member 9
- Inducible T-cell costimulator
- Tumor necrosis factor receptor superfamily member 8
- Tumor necrosis factor receptor superfamily member 5
- Tumor necrosis factor ligand superfamily member 4
Sequence:
MPEEGSGCSVRRRPYGCVLRAALVPLVAGLVICLVVCIQRFAQAQQQLPLESLGWDVAELQLNHTGPQQDPRLYWQGGPALGRSFLHGPELDKGQLRIHRDGIYMVHIQVTLAICSSTTASRHHPTTLAVGICSPASRSISLLRLSFHQGCTIASQRLTPLARGDTLCTNLTGTLLPSRNTDETFFGVQWVRP
Protein: Rubisco accumulation factor 1.2, chloroplastic (Q9SR19)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Required for assembly or stability of RuBisCO. Acts at a postchaperonin step to fold and/or assemble the large subunit (rbcL) into RuBisCO. RAF1 brackets an rbcL dimer (rbcL(2)), leading to rbcL(8)-RAF1(4) complex formation. In the next step, RBCS displaces RAF1, thus resulting in holoenzyme formation.
Subcellular location: Plastid, chloroplast {ECO:0000305}.
Interaction partners:
- Protein BUNDLE SHEATH DEFECTIVE 2, chloroplastic
- 20 kDa chaperonin, chloroplastic
Sequence:
MFSLKSLISSPFTQSTTHGLFTNPITRPVNPLPRTVSFTVTASMIPKRSSANMIPKNPPARQQLYQPFRPPSSPIPTQFRSLDSAGKIEILAGRMALWFEYAPLISSLYTDGFTPPTIEELTGISSIEQNRLIVGAQVRDSILQSIHEPELISAFDTGGAELLYEIRLLSTTQRVAAATFIIDRNIDSKGAQDLARAIKDYPNRRGDVGWLDFDYNLPGDCLSFLYYRQSRENKNPSDQRTSMLLQALGVAESEKAKNRLNTELYGDKEAEKEKEKKKKEEEVKAIRIPVVRLKFGEVAEATSVVVLPVCKAEEGEKKILEAPMEIIAGGDFKVVEAEKGWKRWVVLPSWNPVAAIGKGGVAVSFRDDRKVLPWDGKEEPLLVVADRVRNVVEADDGYYLVVAENGLKLEKGSDLKAREVKESLGMVVLVVRPPREDDDDWQTSHQNWD
Protein: 2,7-dihydroxy-5-methyl-1-naphthoate 7-O-methyltransferase (EC 2.1.1.303) (Neocarzinostatin O-methyltransferase) (Neocarzinostatin biosynthesis protein B1) (Q84HC8)
Organism: Streptomyces carzinostaticus
Function: S-adenosyl-L-methionine-dependent O-methyltransferase that catalyzes regiospecific methylation at the 7-hydroxy group of 2,7-dihydroxy-5-methyl-1-naphthoate in the biosynthesis of the naphthoate moiety of the neocarzinostatin chromophore. Also recognizes other dihydroxynaphthoate as substrates and catalyzes their regiospecific O-methylation. The carboxylate and its ortho-hydroxy groups of the substrate appear to be crucial for NcsB1 substrate recognition and binding, and O-methylation takes place only at the free hydroxy group of these dihydroxynaphthoic acids.
Interaction partners:
Sequence:
MGKRAAHIGLRALADLATPMAVRVAATLRVADHIAAGHRTAAEIASAAGAHADSLDRLLRHLVAVGLFTRDGQGVYGLTEFGEQLRDDHAAGKRKWLDMNSAVGRGDLGFVELAHSIRTGQPAYPVRYGTSFWEDLGSDPVLSASFDTLMSHHLELDYTGIAAKYDWAALGHVVDVGGGSGGLLSALLTAHEDLSGTVLDLQGPASAAHRRFLDTGLSGRAQVVVGSFFDPLPAGAGGYVLSAVLHDWDDLSAVAILRRCAEAAGSGGVVLVIEAVAGDEHAGTGMDLRMLTYFGGKERSLAELGELAAQAGLAVRAAHPISYVSIVEMTAL
Protein: Hsc70-interacting protein (Hip) (Protein FAM10A1) (Protein ST13 homolog) (Q99L47)
Organism: Mus musculus (Mouse)
Function: One HIP oligomer binds the ATPase domains of at least two HSC70 molecules dependent on activation of the HSC70 ATPase by HSP40. Stabilizes the ADP state of HSC70 that has a high affinity for substrate protein. Through its own chaperone activity, it may contribute to the interaction of HSC70 with various target proteins (By similarity).
Subcellular location: Cytoplasm {ECO:0000250}.
Interaction partners:
- Heat shock cognate 71 kDa protein
- Heat shock 70 kDa protein 1B
- Heat shock protein HSP 90-alpha
- Heat shock protein HSP 90-beta
- DnaJ homolog subfamily B member 1
- BAG family molecular chaperone regulator 1
- Prostaglandin E synthase 3
- Heat shock 70 kDa protein 4
- BAG family molecular chaperone regulator 3
- Glycogen synthase kinase-3 beta
Sequence:
MDPRKVSELRAFVKMCRQDPSVLHTEEMRFLREWVESMGGKVPPATHKAKSEENTKEEKRDKTTEENIKTEELSSEESDLEIDNEGVIEPDTDAPQEMGDENAEITEEMMDEANEKKGAAIEALNDGELQKAIDLFTDAIKLNPRLAILYAKRASVFVKLQKPNAAIRDCDRAIEINPDSAQPYKWRGKAHRLLGHWEEAAHDLALACKLDYDEDASAMLREVQPRAQKIAEHRRKYERKREEREIKERIERVKKAREEHERAQREEEARRQSGSQYGSFPGGFPGGMPGNFPGGMPGMGGAMPGMAGMAGMPGLNEILSDPEVLAAMQDPEVMVAFQDVAQNPSNMSKYQSNPKVMNLISKLSAKFGGQS
Protein: Dynein, axonemal, intermediate chain 2, isoform B (Q9VTM3)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Cytoplasm, cytoskeleton, cilium axoneme {ECO:0000256|ARBA:ARBA00004430}.
Interaction partners:
Sequence:
MEYIFKKERRSFGARVHFEDKDEVVFTENSNPELVKSYILKNPVDRVTQYAGQTSLSVANTERATYKSTGITHNEGGWPKDINMHDPEQTVRYKRKIEKDENYITQVMNLTKPMEHYIHQNNAVNIYENYFENLDPAPLPEPCKSRTVNVYRDPNPIKVPVKHLSWSPDGGIKMAVSHCDMRFQGDKSNQKCNSYIWEVENPNEPFLTLEPKVPCVCLEYNQKDPTSLVSGMYNGQVAAWDTRHGKLPVMISEREVCHRDPVNSVLWNNSKSGTEFFSGGSDGQVLWWDTRKLTEPLDRLLMDPVKSDDQDLSRSYGISVLEYETTIPTRFMAGTEMGMLFSCNRKGKTPTEKIQIRMMCHLGPVYAITRNPAFVKNFLTVGDWCARIWSEDCRESSIIWTKSSSSMLTDGAWSYTKVSQFFITRMDGVLDTWDLLQQQNEPVLTVKVCDEPLYCVRTNENGKFVSCGSQLGATFLVEVSDNMVMSAKNDKPLLTAMFERENRREKILEAKSRESKLKVKANHGQDQGDTMMVNGKINMAPFEAACEQAASEYFAAVEQERQRRLPGGKRRGCGGG
Protein: PRA1 family protein B5 (AtPRA1.B5) (Q9M012)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: May be involved in both secretory and endocytic intracellular trafficking in the endosomal/prevacuolar compartments.
Subcellular location: Endosome membrane {ECO:0000269|PubMed:18583532}; Multi-pass membrane protein {ECO:0000269|PubMed:18583532}.
Interaction partners:
- PRA1 family protein A3
- PRA1 family protein H
- PRA1 family protein A1
- PRA1 family protein A2
- PRA1 family protein C
Sequence:
MVSTNPPVLPISTTATDTTNQPPIVTAVVESQPPVVRAFVNGVTETVCGGLSRSRPWSELLDRSAFTKPDSLSEAGTRFRKNSSYFRVNYVCIVALILGFSLLAHPFSLILLLCLAASWLFLYLFRPSDRPLILFGRSFSEYETLGGLILSTIAVIFFTSVGSVLISALMIGIATICVHGAFRAPDDLFLDEQDHAASGFLSFIGVPAIPSVAPSASSAASPV
Protein: Probable WRKY transcription factor 50 (WRKY DNA-binding protein 50) (Q8VWQ5)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Transcription factor. Interacts specifically with the W box (5'-(T)TGAC[CT]-3'), a frequently occurring elicitor-responsive cis-acting element (By similarity).
Subcellular location: Nucleus {ECO:0000305}.
Interaction partners:
- At5g12930
- F22K20.6 protein
Sequence:
MNDADTNLGSSFSDDTHSVFEFPELDLSDEWMDDDLVSAVSGMNQSYGYQTSDVAGALFSGSSSCFSHPESPSTKTYVAATATASADNQNKKEKKKIKGRVAFKTRSEVEVLDDGFKWRKYGKKMVKNSPHPRNYYKCSVDGCPVKKRVERDRDDPSFVITTYEGSHNHSSMN
Protein: Core-capsid bridging protein (Core protein V) (P24938)
Organism: Human adenovirus C serotype 5 (HAdV-5) (Human adenovirus 5)
Function: Associates loosely with the viral DNA to form an outer shell around the nucleoprotein-DNA complex and links it with the capsid by binding the endosome lysis protein. Dissociates from the viral genome during entry. Might be involved in nuclear capsid assembly of the viral particles through its association with NPM1/nucleophosmin.
Subcellular location: Virion {ECO:0000255|HAMAP-Rule:MF_04053, ECO:0000269|PubMed:25071205}. Host nucleus, host nucleolus {ECO:0000255|HAMAP-Rule:MF_04053}. Note=Located inside the capsid (core). Present in 157 copies per virion. Localizes in the nucleoli during infection, then translocates from the nucleoli to the nucleoplasm as the infection progresses and is finally incorporated into the viral particles. {ECO:0000255|HAMAP-Rule:MF_04053, ECO:0000269|PubMed:25071205}.
Interaction partners:
Sequence:
MSKRKIKEEMLQVIAPEIYGPPKKEEQDYKPRKLKRVKKKKKDDDDELDDEVELLHATAPRRRVQWKGRRVKRVLRPGTTVVFTPGERSTRTYKRVYDEVYGDEDLLEQANERLGEFAYGKRHKDMLALPLDEGNPTPSLKPVTLQQVLPALAPSEEKRGLKRESGDLAPTVQLMVPKRQRLEDVLEKMTVEPGLEPEVRVRPIKQVAPGLGVQTVDVQIPTTSSTSIATATEGMETQTSPVASAVADAAVQAVAAAASKTSTEVQTDPWMFRVSAPRRPRGSRKYGAASALLPEYALHPSIAPTPGYRGYTYRPRRRATTRRRTTTGTRRRRRRRQPVLAPISVRRVAREGGRTLVLPTARYHPSIV
Protein: Coiled-coil domain-containing protein 32 (Q9BV29)
Organism: Homo sapiens (Human)
Function: Has a role in ciliogenesis (By similarity). Required for proper cephalic and left/right axis development.
Subcellular location: Membrane, coated pit {ECO:0000269|PubMed:33859415}; Peripheral membrane protein {ECO:0000305|PubMed:33859415}; Cytoplasmic side {ECO:0000305|PubMed:33859415}.
Interaction partners:
- AP-2 complex subunit sigma
- Alpha- and gamma-adaptin-binding protein p34
- Chromobox protein homolog 3
Sequence:
MKMFESADSTATRSGQDLWAEICSCLPNPEQEDGANNAFSDSFVDSCPEGEGQREVADFAVQPAVKPWAPLQDSEVYLASLEKKLRRIKGLNQEVTSKDMLRTLAQAKKECWDRFLQEKLASEFFVDGLDSDESTLEHFKRWLQPDKVAVSTEEVQYLIPPESQVEKPVAEDEPAAGDKPAAAEQ