wanglab/gogpt-training-data huggingface dataset:
Protein: Dystroglycan 1 (Dystroglycan) (Dystrophin-associated glycoprotein 1) (Q9GT67)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Cell membrane, sarcolemma {ECO:0000256|ARBA:ARBA00004135}. Nucleus, nucleoplasm {ECO:0000256|ARBA:ARBA00004642}. Postsynaptic cell membrane {ECO:0000256|ARBA:ARBA00034100}. Secreted, extracellular space {ECO:0000256|ARBA:ARBA00004239}.
Interaction partners:
Sequence:
ATPTSSVATTTASTPESSSISSNFVSTDYMEPQPEENSPPIIKTRLQKLAVTSGKAFTFHVLPETFYDAEDQGNLRLALTDKDGHELKANSWLQFNADKRELYGLPLDDTVSRWQYRLSATDSGNASVTETVEISVQQHRAVRTINHEISVFVRINEKPGHNIDWQLKLINAVARTLDDSTNSAVVVREIRQTPHDPHSATFVYFNETLPTSECPEKELKDIIARLDANRLSDLVQPQLGIKSITGQLIGSCQKDLTQVKPTQHMTKNVPPMPRNQVDRVNASLGQLLVYKVPADTFYDANDNQLTLTLKTRDHLELSPRHWLQFDSKNEEFYGIPKSGDIGSEEYLLVAEDSGGLSAHDALVVVVSPAPKRDFGFFFKAYLSIKHERFNADLQRKFVERVAKLNGDPTTGQIQIRSITTHHDSDGTIVNFYNTTLYRKHNSCREKEVAMTRSVYLNSDLSLREAAKRALGPELNLTNFSVVPFSICHHTENIDTNQLDYIPSRPEEPTHKSSFGEDYMITFVWPIVIIVAMLVAASIIACCLHWCRQRSGKMELGDEEERKSFRAKGIPVIFQDEYEEKPEIGNKSPVILKDEKPPLLPPSYNTSNMNGDNDVDDYVPPPSVVVGGREVRGKSPATPSYRKPPPYVSP
Protein: Dipeptidyl-peptidase 5 (DPP5) (EC 3.4.14.-) (MER034615) (B2RIT0)
Organism: Porphyromonas gingivalis (strain ATCC 33277 / DSM 20709 / CIP 103683 / JCM 12257 / NCTC 11834 / 2561)
Function: Catalyzes the removal of dipeptides from the N-terminus of oligopeptides. Prefers Ala and hydrophobic residues except Pro at the P1 position, and has no preference for P2 residues. Shows high dipeptidyl peptidase activity toward the synthetic substrates Lys-Ala-, Gly-Phe-, Met-Leu-, and Ser-Tyr-methylcoumaryl-7-amide (MCA), and slowly hydrolyzes Val-Tyr-MCA. Is likely involved in amino acid metabolism and bacterial growth of asaccharolytic P.gingivalis, that utilizes amino acids from extracellular proteinaceous nutrients as energy and carbon sources.
Subcellular location: Periplasm {ECO:0000269|PubMed:24398682}.
Interaction partners:
Sequence:
MNKKIFSMMAASIIGSAAMTPSAGTNTGEHLTPELFMTLSRVSEMALSPDGKTAVYAVSFPDVKTNKATRELFTVNLDGSGRKQITDTESNEYAPAWMADGKRIAFMSNEGGSMQLWVMNADGTERRQLSNIEGGITGFLFSPDEKQVLFTKDIKFGKRTKDIYPDLDKATGRIITDLMYKHWDEWVETIPHPFIANATDGMITTGKDIMEGEPYEAPMKPWSGIEDFSWSPDGQNIAYASRKKTGMAYSLSTNSDIYIYNLTSGRTHNISEGMMGYDTYPKFSPDGKSIAWISMERDGYESDLKRLFVADLATGKRTHVNPTFDYNVDMIQWAPDSKGIYFLACKEAETNLWEITLKTGKIRQITQGQHDYADFSVRNDVMLAKRHSFELPDDLYRVNPKNGAAQAVTAENKAILDRLTPIACEKRWMKTTDGGNMLTWVVLPPDFDKNKKYPAILYCQGGPQNTVSQFWSFRWNLRLMAEQGYIVIAPNRHGVPGFGQKWNEQISGDYGGQNMRDYLTAVDEMKKEPYVDGDRIGAVGASYGGFSVYWLAGHHDKRFAAFIAHAGIFNLEMQYATTEEMWFANWDIGGPFWEKDNVVAQRTYATSPHKYVQNWDTPILMIHGELDFRILASQAMAAFDAAQLRGVPSEMLIYPDENHWVLQPQNALLFHRTFFGWLDRWLKK
Protein: Long-chain-fatty-acid--CoA ligase (EC 6.2.1.3) (Long-chain acyl-CoA synthetase) (Acyl-CoA synthetase) (P69451)
Organism: Escherichia coli (strain K12)
Function: Catalyzes the esterification, concomitant with transport, of exogenous long-chain fatty acids into metabolically active CoA thioesters for subsequent degradation or incorporation into phospholipids. Activity is the highest with fatty acid substrates of > 10 carbon atoms. Is involved in the aerobic beta-oxidative degradation of fatty acids, which allows aerobic growth of E.coli on fatty acids as a sole carbon and energy source.
Subcellular location: Cell membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}. Note=Partially membrane-associated. {ECO:0000250}.
Interaction partners:
- Acyl-coenzyme A dehydrogenase
- Fatty acid oxidation complex subunit alpha
- Long-chain fatty acid transport protein
- Fatty acid oxidation complex subunit alpha
- 3-ketoacyl-CoA thiolase FadA
- Thioesterase 1/protease 1/lysophospholipase L1
- Fatty acid metabolism regulator protein
- Malonyl CoA-acyl carrier protein transacylase
- Glycerol-3-phosphate acyltransferase
- 2,4-dienoyl-CoA reductase [
Sequence:
MKKVWLNRYPADVPTEINPDRYQSLVDMFEQSVARYADQPAFVNMGEVMTFRKLEERSRAFAAYLQQGLGLKKGDRVALMMPNLLQYPVALFGILRAGMIVVNVNPLYTPRELEHQLNDSGASAIVIVSNFAHTLEKVVDKTAVQHVILTRMGDQLSTAKGTVVNFVVKYIKRLVPKYHLPDAISFRSALHNGYRMQYVKPELVPEDLAFLQYTGGTTGVAKGAMLTHRNMLANLEQVNATYGPLLHPGKELVVTALPLYHIFALTINCLLFIELGGQNLLITNPRDIPGLVKELAKYPFTAITGVNTLFNALLNNKEFQQLDFSSLHLSAGGGMPVQQVVAERWVKLTGQYLLEGYGLTECAPLVSVNPYDIDYHSGSIGLPVPSTEAKLVDDDDNEVPPGQPGELCVKGPQVMLGYWQRPDATDEIIKNGWLHTGDIAVMDEEGFLRIVDRKKDMILVSGFNVYPNEIEDVVMQHPGVQEVAAVGVPSGSSGEAVKIFVVKKDPSLTEESLVTFCRRQLTGYKVPKLVEFRDELPKSNVGKILRRELRDEARGKVDNKA
Protein: Corrinoid adenosyltransferase MMAB (EC 2.5.1.-) (ATP:co(I)rrinoid adenosyltransferase MMAB) (Methylmalonic aciduria type B homolog) (Q58D49)
Organism: Bos taurus (Bovine)
Function: Converts cob(I)alamin to adenosylcobalamin (adenosylcob(III)alamin), a coenzyme for methylmalonyl-CoA mutase, therefore participates in the final step of the vitamin B12 conversion. Generates adenosylcobalamin (AdoCbl) and directly delivers the cofactor to MUT in a transfer that is stimulated by ATP-binding to MMAB and gated by MMAA (By similarity).
Subcellular location: Mitochondrion {ECO:0000250|UniProtKB:Q96EY8}.
Interaction partners:
- Metabolism of cobalamin associated D
- Mevalonate kinase
- Corrinoid adenosyltransferase
- Iodotyrosine deiodinase 1
- Phosphopantothenoylcysteine decarboxylase
- Lysosomal cobalamin transport escort protein LMBD1
- Coiled-coil domain-containing protein 137
- Cyanocobalamin reductase / alkylcobalamin dealkylase
Sequence:
MAVWGPGGRLGLRGCLGARKLLCPRFQSRGPQGVEDGDRPQPSSKTPKVPKIYTKTGDKGFSSTFTGERRSKDDQVFEAVGTTDELSSAIGFAMELIAEKGHPFVEELQKIQCSLQDVGSALATPRSSAREAHLKHATFEAGPILELEQWIDKYSRQLPPLTAFILPSGGKSSSALHFCRAVCRRAERRVVPLVQTGETDANVVKFLNRLSDYLFTLARYTAMKEGNPEKIYKKNDLSDRT
Protein: Proheparin-binding EGF-like growth factor [Cleaved into: Heparin-binding EGF-like growth factor (HB-EGF) (HBEGF)] (Q9W7C5)
Organism: Gallus gallus (Chicken)
Function: May be involved in macrophage-mediated cellular proliferation. It is mitogenic for fibroblasts and smooth muscle but not endothelial cells. It is able to bind EGF receptor/EGFR with higher affinity than EGF itself and is a far more potent mitogen for smooth muscle cells than EGF (By similarity). Plays an important role in the proper development of cranial nerves by inhibiting the migration of the cranial neural crest cells (NCCs) into the odd-numbered neuromeres (r3 and r5) of the hindbrain Plays a role in mediating v-Jun-induced oncogenic transformation.
Subcellular location: [Heparin-binding EGF-like growth factor]: Secreted, extracellular space {ECO:0000250}. Note=Mature HB-EGF is released into the extracellular space and probably binds to a receptor. {ECO:0000250}.; SUBCELLULAR LOCATION: [Proheparin-binding EGF-like growth factor]: Cell membrane {ECO:0000250}; Single-pass type I membrane protein {ECO:0000250}.
Interaction partners:
- Epidermal growth factor receptor
- Receptor protein-tyrosine kinase.
- Uncharacterized protein.
- Proepiregulin
- Probetacellulin
- Protein kinase domain-containing protein.
- 72 kDa type IV collagenase
- Sphingosine-1-phosphate receptor 3
- Receptor protein-tyrosine kinase.
- Epigen
Sequence:
MDGRVVLIHALLTAVCSAAVGKFGRDGPHGEALHNEVLLHEGGGVASVSATAPLLGGIVEKEGGGAASGDALSELPRVAFLSKPQGPVTPKKKGNGNKRRKGKGLGKKRDPCLRKYKDFCIHGECKYIRELGAPSCICQPGYHGERCHGLLLPVEHPPSTYDHTTALAVVAVVLSSLCLVIITALLMFRCHKRGVYDVENEEKIKLGITVNH
Protein: Translocation and assembly module subunit TamA (Autotransporter assembly factor TamA) (P0ADE4)
Organism: Escherichia coli (strain K12)
Function: Part of the translocation and assembly module (TAM) autotransporter assembly complex, which functions in translocation of autotransporters across the outer membrane. Allows substrate (Ag43, AC P39180) to initiate penetration into the outer membrane; TamB is not necessary but may regulate this activity. Has anion selective channel-forming ability, but the physiological relevance of this activity is unclear.
Subcellular location: Cell outer membrane {ECO:0000269|PubMed:16522795, ECO:0000269|PubMed:17214547, ECO:0000269|PubMed:22466966, ECO:0000269|PubMed:25341963}.
Interaction partners:
- Translocation and assembly module subunit TamB
- Gamma-glutamylcyclotransferase family protein YtfP
- Outer membrane protein assembly factor BamA
- Aldose sugar dehydrogenase YliI
Sequence:
MRYIRQLCCVSLLCLSGSAVAANVRLQVEGLSGQLEKNVRAQLSTIESDEVTPDRRFRARVDDAIREGLKALGYYQPTIEFDLRPPPKKGRQVLIAKVTPGVPVLIGGTDVVLRGGARTDKDYLKLLDTRPAIGTVLNQGDYENFKKSLTSIALRKGYFDSEFTKAQLGIALGLHKAFWDIDYNSGERYRFGHVTFEGSQIRDEYLQNLVPFKEGDEYESKDLAELNRRLSATGWFNSVVVAPQFDKARETKVLPLTGVVSPRTENTIETGVGYSTDVGPRVKATWKKPWMNSYGHSLTTSTSISAPEQTLDFSYKMPLLKNPLEQYYLVQGGFKRTDLNDTESDSTTLVASRYWDLSSGWQRAINLRWSLDHFTQGEITNTTMLFYPGVMISRTRSRGGLMPTWGDSQRYSIDYSNTAWGSDVDFSVFQAQNVWIRTLYDRHRFVTRGTLGWIETGDFDKVPPDLRFFAGGDRSIRGYKYKSIAPKYANGDLKGASKLITGSLEYQYNVTGKWWGAVFVDSGEAVSDIRRSDFKTGTGVGVRWESPVGPIKLDFAVPVADKDEHGLQFYIGLGPEL
Protein: DNA gyrase subunit B (EC 5.6.2.2) (Q5SHZ4)
Organism: Thermus thermophilus (strain ATCC 27634 / DSM 579 / HB8)
Function: A type II topoisomerase that negatively supercoils closed circular double-stranded (ds) DNA in an ATP-dependent manner. It probably also catalyzes the interconversion of other topological isomers of double-stranded DNA rings, including catenanes. Relaxes negatively supercoiled DNA in an ATP-independent manner. At comparable concentrations T.thermophilus gyrase does not introduce as many negative supercoils into DNA as the E.coli enzyme.
Subcellular location: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_01898}.
Interaction partners:
Sequence:
MSYDASAIRVLKGLEGVRHRPAMYIGGTGVEGYHHLFKEILDNAVDEALAGYATEILVRLNEDGSLTVEDNGRGIPVDLMPEEGKPAVEVIYTTLHSGGKFEQGAYKVSGGLHGVGASVVNALSEWTVVEVFREGKHHRIAFSRGEVTEPLRVVGEAPRGKTGTRVTFKPDPEIFGNLRFDPSKIRARLREVAYLVAGLKLVFQDRQHGKEEVFLDKGGVASFAKALAEGEDLLYEKPFLIRGTHGEVEVEVGFLHTQGYNAEILTYANMIPTRDGGTHLTAFKSAYSRALNQYAKKAGLNKEKGPQPTGDDLLEGLYAVVSVKLPNPQFEGQTKGKLLNPEAGTAVGQVVYERLLEILEENPRIAKAVYEKALRAAQAREAARKARELVRRQNPLESDELPGKLADCQTENPEEAELFIVEGDSAGGSAKQGRDRRFQAILPLRGKILNVEKAGLSKALKNAEVRAMVSAIGVGIGGDGEAHFDLEGLRYHKIIIMTDADVDGSHIRTLLLTFFYRYMRPLIERGHVYIAQPPLYRLQVGKKVEYLYSDEELQARLKELEGKHYEVQRFKGLGEMNPEQLWETTMNPEKRVLKRVELQDALEASELFEKLMGQEVAPRREFIEEHARYAELDI
Protein: Receptor-type tyrosine-protein phosphatase U (R-PTP-U) (EC 3.1.3.48) (Pancreatic carcinoma phosphatase 2) (PCP-2) (Protein-tyrosine phosphatase J) (PTP-J) (hPTP-J) (Protein-tyrosine phosphatase pi) (PTP pi) (Protein-tyrosine phosphatase receptor omicron) (PTP-RO) (Receptor-type protein-tyrosine phosphatase psi) (R-PTP-psi) (Q92729)
Organism: Homo sapiens (Human)
Function: Tyrosine-protein phosphatase which dephosphorylates CTNNB1. Regulates CTNNB1 function both in cell adhesion and signaling. May function in cell proliferation and migration and play a role in the maintenance of epithelial integrity. May play a role in megakaryocytopoiesis.
Subcellular location: Cell junction {ECO:0000269|PubMed:8700514}. Cell membrane {ECO:0000269|PubMed:8700514}; Single-pass type I membrane protein {ECO:0000269|PubMed:8700514}.
Interaction partners:
- Mast/stem cell growth factor receptor Kit
- Catenin beta-1
- 6-pyruvoyl tetrahydrobiopterin synthase
- Segment polarity protein dishevelled homolog DVL-1
- Meprin A subunit beta
- Cadherin-17
Sequence:
MARAQALVLALTFQLCAPETETPAAGCTFEEASDPAVPCEYSQAQYDDFQWEQVRIHPGTRAPADLPHGSYLMVNTSQHAPGQRAHVIFQSLSENDTHCVQFSYFLYSRDGHSPGTLGVYVRVNGGPLGSAVWNMTGSHGRQWHQAELAVSTFWPNEYQVLFEALISPDRRGYMGLDDILLLSYPCAKAPHFSRLGDVEVNAGQNASFQCMAAGRAAEAERFLLQRQSGALVPAAGVRHISHRRFLATFPLAAVSRAEQDLYRCVSQAPRGAGVSNFAELIVKEPPTPIAPPQLLRAGPTYLIIQLNTNSIIGDGPIVRKEIEYRMARGPWAEVHAVSLQTYKLWHLDPDTEYEISVLLTRPGDGGTGRPGPPLISRTKCAEPMRAPKGLAFAEIQARQLTLQWEPLGYNVTRCHTYTVSLCYHYTLGSSHNQTIRECVKTEQGVSRYTIKNLLPYRNVHVRLVLTNPEGRKEGKEVTFQTDEDVPSGIAAESLTFTPLEDMIFLKWEEPQEPNGLITQYEISYQSIESSDPAVNVPGPRRTISKLRNETYHVFSNLHPGTTYLFSVRARTGKGFGQAALTEITTNISAPSFDYADMPSPLGESENTITVLLRPAQGRGAPISVYQVIVEEERARRLRREPGGQDCFPVPLTFEAALARGLVHYFGAELAASSLPEAMPFTVGDNQTYRGFWNPPLEPRKAYLIYFQAASHLKGETRLNCIRIARKAACKESKRPLEVSQRSEEMGLILGICAGGLAVLILLLGAIIVIIRKGRDHYAYSYYPKPVNMTKATVNYRQEKTHMMSAVDRSFTDQSTLQEDERLGLSFMDTHGYSTRGDQRSGGVTEASSLLGGSPRRPCGRKGSPYHTGQLHPAVRVADLLQHINQMKTAEGYGFKQEYESFFEGWDATKKKDKVKGSRQEPMPAYDRHRVKLHPMLGDPNADYINANYIDGYHRSNHFIATQGPKPEMVYDFWRMVWQEHCSSIVMITKLVEVGRVKCSRYWPEDSDTYGDIKIMLVKTETLAEYVVRTFALERRGYSARHEVRQFHFTAWPEHGVPYHATGLLAFIRRVKASTPPDAGPIVIHCSAGTGRTGCYIVLDVMLDMAECEGVVDIYNCVKTLCSRRVNMIQTEEQYIFIHDAILEACLCGETTIPVSEFKATYKEMIRIDPQSNSSQLREEFQTLNSVTPPLDVEECSIALLPRNRDKNRSMDVLPPDRCLPFLISTDGDSNNYINAALTDSYTRSAAFIVTLHPLQSTTPDFWRLVYDYGCTSIVMLNQLNQSNSAWPCLQYWPEPGRQQYGLMEVEFMSGTADEDLVARVFRVQNISRLQEGHLLVRHFQFLRWSAYRDTPDSKKAFLHLLAEVDKWQAESGDGRTIVHCLNGGGRSGTFCACATVLEMIRCHNLVDVFFAAKTLRNYKPNMVETMDQYHFCYDVALEYLEGLESR
Protein: THAP domain-containing protein 11 (Q96EK4)
Organism: Homo sapiens (Human)
Function: Transcriptional repressor that plays a central role for embryogenesis and the pluripotency of embryonic stem (ES) cells. Sequence-specific DNA-binding factor that represses gene expression in pluripotent ES cells by directly binding to key genetic loci and recruiting epigenetic modifiers (By similarity).
Subcellular location: Nucleus {ECO:0000269|PubMed:37148549, ECO:0000269|PubMed:9853615}. Cytoplasm {ECO:0000269|PubMed:37148549}. Note=In oocytes, detected in the ooplasm, without evidence of its presence in the nucleus (By similarity). Found in the nucleus of undifferentiated embryonic stem cells (PubMed:18585351). Evenly distributed between nucleus and cytoplasm in skin fibroblasts (PubMed:37148549). {ECO:0000250|UniProtKB:Q9JJD0, ECO:0000269|PubMed:18585351, ECO:0000269|PubMed:37148549}.
Interaction partners:
- THAP domain-containing protein 7
- Host cell factor 1
- Peroxynitrite isomerase THAP4
- THAP domain-containing protein 1
- 52 kDa repressor of the inhibitor of the protein kinase
- THAP domain-containing protein 2
- THAP domain-containing protein 3
- Zinc finger protein 143
Sequence:
MPGFTCCVPGCYNNSHRDKALHFYTFPKDAELRRLWLKNVSRAGVSGCFSTFQPTTGHRLCSVHFQGGRKTYTVRVPTIFPLRGVNERKVARRPAGAAAARRRQQQQQQQQQQQQQQQQQQQQQQQQQQQQQSSPSASTAQTAQLQPNLVSASAAVLLTLQATVDSSQAPGSVQPAPITPTGEDVKPIDLTVQVEFAAAEGAAAAAAASELQAATAGLEAAECPMGPQLVVVGEEGFPDTGSDHSYSLSSGTTEEELLRKLNEQRDILALMEVKMKEMKGSIRHLRLTEAKLREELREKDRLLAMAVIRKKHGM
Protein: UDP-glycosyltransferase 708G2 (EC 2.4.1.360) (2-hydroxyflavanone C-glucosyltransferase) (CuCGT) (A0A224AKZ9)
Organism: Citrus unshiu (Satsuma mandarin) (Citrus nobilis var. unshiu)
Function: UDP-glucose-dependent glucosyltransferase catalyzing the C-glucosylation of 2-hydroxyflavanones (2-hydroxylnaringenin and 2-hydroxypinocembrin) and phloretin. No activity with flavanones, flavones or flavonols. Exhibits C-glucosylation activity toward 2-phenyl-2',4',6'-trihydroxyacetophenone. Can use UDP-xylose as sugar donor, but catalytic efficiency is much lower toward UDP-xylose than toward UDP-glucose.
Interaction partners:
Sequence:
MSDSGGFDSHPHVALIPSAGMGHLTPFLRLAASLVQHHCRVTLITTYPTVSLAETQHVSHFLSAYPQVTEKRFHLLPFDPNSANATDPFLLRWEAIRRSAHLLAPLLSPPLSALITDVTLISAVLPVTINLHLPNYVLFTASAKMFSLTASFPAIVASKSTSSGSVEFDDDFIEIPGLPPIPLSSVPPAVMDSKSLFATSFLENGNSFVKSNGVLINSFDALEADTLVALNGRRVVAGLPPVYAVGPLLPCEFEKRDDPSTSLILKWLDDQPEGSVVYVSFGSRLALSMEQTKELGDGLLSSGCRFLWVVKGKIVDKEDEESLKNVLGHELTEKIKDQGLVVKNWVDQDKVLSHRAVGGFVSHGGWNSLVEAARHGVPLLVWPHFGDQKINAEAVERAGLGMWVRSWGWGTELRAKGDEIGLKIKDLMANDFLREQAKRIEEEARKAIGVGGSSERTFKELIDKWKCNNNTH
Protein: Zinc finger CCCH domain-containing protein 7B (Rotavirus 'X'-associated non-structural protein) (RoXaN) (Q9UGR2)
Organism: Homo sapiens (Human)
Function: May be a specific regulator of miRNA biogenesis. Binds to microRNAs MIR7-1, MIR16-2 and MIR29A hairpins recognizing the 'ATA(A/T)' motif in the apical loop.
Subcellular location: Nucleus {ECO:0000269|PubMed:18799579}. Note=Nuclear localization seems to be depleted upon rotavirus A infection.
Interaction partners:
- SH2 domain-containing protein 3C
- G2/mitotic-specific cyclin-B3
Sequence:
MERQKRKADIEKGLQFIQSTLPLKQEEYEAFLLKLVQNLFAEGNDLFREKDYKQALVQYMEGLNVADYAASDQVALPRELLCKLHVNRAACYFTMGLYEKALEDSEKALGLDSESIRALFRKARALNELGRHKEAYECSSRCSLALPHDESVTQLGQELAQKLGLRVRKAYKRPQELETFSLLSNGTAAGVADQGTSNGLGSIDDIETDCYVDPRGSPALLPSTPTMPLFPHVLDLLAPLDSSRTLPSTDSLDDFSDGDVFGPELDTLLDSLSLVQGGLSGSGVPSELPQLIPVFPGGTPLLPPVVGGSIPVSSPLPPASFGLVMDPSKKLAASVLDALDPPGPTLDPLDLLPYSETRLDALDSFGSTRGSLDKPDSFMEETNSQDHRPPSGAQKPAPSPEPCMPNTALLIKNPLAATHEFKQACQLCYPKTGPRAGDYTYREGLEHKCKRDILLGRLRSSEDQTWKRIRPRPTKTSFVGSYYLCKDMINKQDCKYGDNCTFAYHQEEIDVWTEERKGTLNRDLLFDPLGGVKRGSLTIAKLLKEHQGIFTFLCEICFDSKPRIISKGTKDSPSVCSNLAAKHSFYNNKCLVHIVRSTSLKYSKIRQFQEHFQFDVCRHEVRYGCLREDSCHFAHSFIELKVWLLQQYSGMTHEDIVQESKKYWQQMEAHAGKASSSMGAPRTHGPSTFDLQMKFVCGQCWRNGQVVEPDKDLKYCSAKARHCWTKERRVLLVMSKAKRKWVSVRPLPSIRNFPQQYDLCIHAQNGRKCQYVGNCSFAHSPEERDMWTFMKENKILDMQQTYDMWLKKHNPGKPGEGTPISSREGEKQIQMPTDYADIMMGYHCWLCGKNSNSKKQWQQHIQSEKHKEKVFTSDSDASGWAFRFPMGEFRLCDRLQKGKACPDGDKCRCAHGQEELNEWLDRREVLKQKLAKARKDMLLCPRDDDFGKYNFLLQEDGDLAGATPEAPAAAATATTGE
Protein: DDB1- and CUL4-associated factor 17 (Q5H9S7)
Organism: Homo sapiens (Human)
Function: May function as a substrate receptor for CUL4-DDB1 E3 ubiquitin-protein ligase complex.
Subcellular location: Membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}. Nucleus, nucleolus {ECO:0000269|PubMed:19026396}. Note=According to PubMed:19026396, it is a nucleolar protein, while sequence analysis programs clearly predict 2 transmembrane regions.
Interaction partners:
- Cullin-4B
- DNA damage-binding protein 1
- DET1- and DDB1-associated protein 1
- Cullin-4A
- DDB1- and CUL4-associated factor 1
- Activating molecule in BECN1-regulated autophagy protein 1
- DDB1- and CUL4-associated factor 8
- E3 ubiquitin-protein ligase RBX1
- DDB1- and CUL4-associated factor 16
- DET1 homolog
Sequence:
MGPTRKPNVCSRLSRRALGCFSRDAGVVQRTNLGILRALVCQESTKFKNVWTTHSRSPIAYERGRIYFDNYRRCVSSVASEPRKLYEMPKCSKSEKIEDALLWECPVGDILPNSSDYKSSLIALTAHNWLLRISATTGKILEKIYLAPYCKFRYLSWDTPQEVIAVKSAQNRGSAVARQAGIQQHVLLYLAVFRVLPFSLVGILEINKKIFGNVTDATLSHGILIVMYSSGLVRLYSFQTIAEQFMQQKLDLGCACRWGGTTGTVGEAPFGIPCNIKITDMPPLLFEVSSLENAFQIGGHPWHYIVTPNKKKQKGVFHICALKDNSLAKNGIQEMDCCSLESDWIYFHPDASGRIIHVGPNQVKVLKLTEIENNSSQHQISEDFVILANRENHKNENVLTVTASGRVVKKSFNLLDDDPEQETFKIVDYEDELDLLSVVAVTQIDAEGKAHLDFHCNEYGTLLKSIPLVESWDVTYSHEVYFDRDLVLHIEQKPNRVFSCYVYQMICDTGEEEETINRSC
Protein: DnaJ homolog subfamily A member 1 (DnaJ protein homolog 2) (HSDJ) (Heat shock 40 kDa protein 4) (Heat shock protein J2) (HSJ-2) (Human DnaJ protein 2) (hDj-2) (P31689)
Organism: Homo sapiens (Human)
Function: Co-chaperone for HSPA8/Hsc70. Stimulates ATP hydrolysis, but not the folding of unfolded proteins mediated by HSPA1A (in vitro). Plays a role in protein transport into mitochondria via its role as co-chaperone. Functions as co-chaperone for HSPA1B and negatively regulates the translocation of BAX from the cytosol to mitochondria in response to cellular stress, thereby protecting cells against apoptosis. Promotes apoptosis in response to cellular stress mediated by exposure to anisomycin or UV.
Subcellular location: Membrane {ECO:0000305|PubMed:10816573}; Lipid-anchor {ECO:0000305|PubMed:10816573}. Cytoplasm {ECO:0000269|PubMed:10816573}. Microsome {ECO:0000250}. Nucleus {ECO:0000269|PubMed:10816573}. Cytoplasm, perinuclear region {ECO:0000269|PubMed:10816573}. Mitochondrion {ECO:0000250}. Note=Primarily associated with microsomes. A minor proportion is associated with mitochondria (By similarity). Primarily cytoplasmic. A minor proportion is associated with nuclei. {ECO:0000250}.
Interaction partners:
- Heat shock cognate 71 kDa protein
- Heat shock 70 kDa protein 4
- Heat shock protein HSP 90-alpha
- Heat shock 70 kDa protein 1A
- Heat shock protein HSP 90-beta
- Heat shock 70 kDa protein 1-like
- Stress-induced-phosphoprotein 1
- Heat shock protein 105 kDa
- DnaJ homolog subfamily B member 1
- DnaJ homolog subfamily A member 4
Sequence:
MVKETTYYDVLGVKPNATQEELKKAYRKLALKYHPDKNPNEGEKFKQISQAYEVLSDAKKRELYDKGGEQAIKEGGAGGGFGSPMDIFDMFFGGGGRMQRERRGKNVVHQLSVTLEDLYNGATRKLALQKNVICDKCEGRGGKKGAVECCPNCRGTGMQIRIHQIGPGMVQQIQSVCMECQGHGERISPKDRCKSCNGRKIVREKKILEVHIDKGMKDGQKITFHGEGDQEPGLEPGDIIIVLDQKDHAVFTRRGEDLFMCMDIQLVEALCGFQKPISTLDNRTIVITSHPGQIVKHGDIKCVLNEGMPIYRRPYEKGRLIIEFKVNFPENGFLSPDKLSLLEKLLPERKEVEETDEMDQVELVDFDPNQERRRHYNGEAYEDDEHHPRGGVQCQTS
Protein: non-specific serine/threonine protein kinase (EC 2.7.11.1) (Q580P8)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
Sequence:
MAEPFSTILGTDGSGGRCKYLNKGIVGLGSYGEAYVAESVEDGSLCVAKVMGLSKMSQRDKRYAQSEIKCLANCNHPNIIRYIEDHEENDRLLIVMEFADSGNLDEQIKLRGTGDARYFQEHEALFLFLQLCLALDYIHSHKMLHRDIKSANVLLTSTGLVKLGDFGFSHQYEDTVSRVVASTFCGTPYYLAPELWNNKRYNKKADVWSLGVLLYEIMGMKKPFSASNLKGLMSKVLAGTYAPLPDSFLSGFKHVVDGILVADPNDRPSVRENFQIPYINKGLKLFVQALKKNERILDSVKEVLVSQVSEILSSEVSPDAHRFLESQINYDVTHRGHVNKLGGGNGKSWKPRVLQIVRGQLILTDDEEGNNPKGLNLEQVQGACPVPHSTAKRDFVFALNTVGGKGMWFQAVSHGDMEMWVHAIQRGIGVA
Protein: Fibroblast growth factor 23 (FGF-23) (Phosphatonin) (Tumor-derived hypophosphatemia-inducing factor) [Cleaved into: Fibroblast growth factor 23 N-terminal peptide; Fibroblast growth factor 23 C-terminal peptide] (Q9GZV9)
Organism: Homo sapiens (Human)
Function: Regulator of phosphate homeostasis. Inhibits renal tubular phosphate transport by reducing SLC34A1 levels. Up-regulates EGR1 expression in the presence of KL (By similarity). Acts directly on the parathyroid to decrease PTH secretion (By similarity). Regulator of vitamin-D metabolism. Negatively regulates osteoblast differentiation and matrix mineralization.
Subcellular location: Secreted {ECO:0000269|PubMed:16638743}. Note=Secretion is dependent on O-glycosylation.
Interaction partners:
- Klotho
- Fibroblast growth factor receptor 1
- Fibroblast growth factor receptor 4
- Polypeptide N-acetylgalactosaminyltransferase 3
- Fibroblast growth factor receptor 2
- Phosphate-regulating neutral endopeptidase PHEX
- Fibroblast growth factor receptor 3
- Beta-klotho
- Parathyroid hormone
- Sodium-dependent phosphate transport protein 2C
Sequence:
MLGARLRLWVCALCSVCSMSVLRAYPNASPLLGSSWGGLIHLYTATARNSYHLQIHKNGHVDGAPHQTIYSALMIRSEDAGFVVITGVMSRRYLCMDFRGNIFGSHYFDPENCRFQHQTLENGYDVYHSPQYHFLVSLGRAKRAFLPGMNPPPYSQFLSRRNEIPLIHFNTPIPRRHTRSAEDDSERDPLNVLKPRARMTPAPASCSQELPSAEDNSPMASDPLGVVRGGRVNTHAGGTGPEGCRPFAKFI
Protein: Chromosome 11 open reading frame 54 (E9PLB3)
Organism: Homo sapiens (Human)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
MACAEFSFHVPSLEELAGVMQKGLKDNFADVQVSVVDCPDLTKEPFTFPVKGICGKTRIAEVGGVPYLLPLVNQKKVYDLNKIAKEIKLPGAFILGAGAGPFQTLGFNSEFMPVIQTESEHKPPVNGSYFAHVNPADGGCLLEKYSEKC
Protein: RAN GTPase activating protein 1 (A0A0G2K5R3)
Organism: Rattus norvegicus (Rat)
Interaction partners:
Sequence:
MGSGAFCGMDDLDPIAIYVLFEEWDPQAECYQDDQAVYRPPGEPAVVVMASEDIAKLAETLAKTQVAGGQLSFKGKGLKLNTAEDAKDVIKEIEEFDGLEALRLEGNTVGVEAARVIAKALEKKSKLKRCHWSDMFTGRLRSEIPPALISLGEGLITAGAQLVELDLSDNAFGPDGVRGFEALLKSPACFTLQELKLNNCGMGIGGGKILAAALTECHRKSSAQGKPLTLKVFVAGRNRLENDGATALAEAFGIIGTLEEVHMPQNGINHPGVTALAQAFAINPLLRVINLNDNTFTEKGGVAMAETLKTLRQVEVINFGDCLVRSKGAVAIADAVRGGLPKLKELNLSFCEIKRDAALVVAEAVADKAELEKLDLNGNALGEEGCEQLQEVLDSFNMAKVLASLSDDEGEDEDEDEEGEDDEDEEDEEEEEEEEEEEEEEEEEPQQRGSGEEPATPSRKILDPNSGEPAPVLSSPPPTDLSTFLSFPSPEKLLRLGPKVSVLIVQQTDTSDPEKVVSAFLKVASVFRDEASVKTAVLDAIDALMKKAFSSSSFNSNTFLTRLLIHMGLLKSEDKIKAIPSLHGPLMVLNHVVQQDYFPKTLAPLLLAFVTKPNGALESCSFARHSLLQTLYSI