wanglab/gogpt-training-data huggingface dataset:
Protein: 60 kDa heat shock protein, mitochondrial (EC 5.6.1.7) (60 kDa chaperonin) (Chaperonin 60) (CPN60) (Heat shock protein 60) (HSP-60) (Hsp60) (Heat shock protein family D member 1) (HuCHA60) (Mitochondrial matrix protein P1) (P60 lymphocyte protein) (P10809)
Organism: Homo sapiens (Human)
Function: Chaperonin implicated in mitochondrial protein import and macromolecular assembly. Together with Hsp10, facilitates the correct folding of imported proteins. May also prevent misfolding and promote the refolding and proper assembly of unfolded polypeptides generated under stress conditions in the mitochondrial matrix. The functional units of these chaperonins consist of heptameric rings of the large subunit Hsp60, which function as a back-to-back double ring. In a cyclic reaction, Hsp60 ring complexes bind one unfolded substrate protein per ring, followed by the binding of ATP and association with 2 heptameric rings of the co-chaperonin Hsp10. This leads to sequestration of the substrate protein in the inner cavity of Hsp60 where, for a certain period of time, it can fold undisturbed by other cell components. Synchronous hydrolysis of ATP in all Hsp60 subunits results in the dissociation of the chaperonin rings and the release of ADP and the folded substrate protein (Probable).
Subcellular location: Mitochondrion matrix.
Interaction partners:
- 10 kDa heat shock protein, mitochondrial
- Stress-70 protein, mitochondrial
- Toll-like receptor 4
- GrpE protein homolog 1, mitochondrial
- Toll-like receptor 2
- Heat shock protein HSP 90-beta
- Heat shock protein HSP 90-alpha
- T-complex protein 1 subunit alpha
- Heat shock cognate 71 kDa protein
- Mitochondrial disaggregase
Sequence:
MLRLPTVFRQMRPVSRVLAPHLTRAYAKDVKFGADARALMLQGVDLLADAVAVTMGPKGRTVIIEQSWGSPKVTKDGVTVAKSIDLKDKYKNIGAKLVQDVANNTNEEAGDGTTTATVLARSIAKEGFEKISKGANPVEIRRGVMLAVDAVIAELKKQSKPVTTPEEIAQVATISANGDKEIGNIISDAMKKVGRKGVITVKDGKTLNDELEIIEGMKFDRGYISPYFINTSKGQKCEFQDAYVLLSEKKISSIQSIVPALEIANAHRKPLVIIAEDVDGEALSTLVLNRLKVGLQVVAVKAPGFGDNRKNQLKDMAIATGGAVFGEEGLTLNLEDVQPHDLGKVGEVIVTKDDAMLLKGKGDKAQIEKRIQEIIEQLDVTTSEYEKEKLNERLAKLSDGVAVLKVGGTSDVEVNEKKDRVTDALNATRAAVEEGIVLGGGCALLRCIPALDSLTPANEDQKIGIEIIKRTLKIPAMTIAKNAGVEGSLIVEKIMQSSSEVGYDAMAGDFVNMVEKGIIDPTKVVRTALLDAAGVASLLTTAEVVVTEIPKEEKDPGMGAMGGMGGGMGGGMF
Protein: Probable type I inositol 1,4,5-trisphosphate 5-phosphatase (5PTase) (EC 3.1.3.56) (Q17848)
Organism: Caenorhabditis elegans
Interaction partners:
- Inositol-trisphosphate 3-kinase homolog
- 1-phosphatidylinositol 4,5-bisphosphate phosphodiesterase gamma plc-3
- Inositol polyphosphate 5-phosphatase
- 1-phosphatidylinositol 4,5-bisphosphate phosphodiesterase beta egl-8
- Kinase
- Inositol polyphosphate-related phosphatase domain-containing protein
- Phosphoinositide phospholipase C
- 1-phosphatidylinositol 4,5-bisphosphate phosphodiesterase epsilon-1
- Rho-GAP domain-containing protein
- Inositol 1,4,5-trisphosphate receptor itr-1
Sequence:
MVQYLLITANVGSLFEPDARLHTSWIKTVADQVESVDPSFFVIHLQETGGKKFTECSQQVPIIINRLSTALPKFDLLRAYVDIDYEAIEYTALGALCFIKRSLWSNVSQFNFHTKKYEQLTSPKEVVTHGLENYPYVVKHKFPKDFWPSIKWGRKGYMQTRWKIENKVFDFVNAHLFHDESNLALIHENPQLYSQNRKRALDFVLAELSSKENGCTPLLFVFGDLNFRLDSRSFLNRLTERTAQHPVADQEQMGSLADGLQASAANLQVITHPSENLRRTVSAIEFRRESDSDDSQNSCVLRIEKKKFDYFNHKKLLDDWRSYRDDDKETENFQSMFEMHINFPPTYPWSEDPENSETLMKTRAPAWCDRVLMNKNAYSLVEEGEPQYRSFGMETCTGDHKPVMLTFNI
Protein: BRISC complex subunit Abraxas 2 (Abraxas brother protein 1) (Protein FAM175B) (Q15018)
Organism: Homo sapiens (Human)
Function: Component of the BRISC complex, a multiprotein complex that specifically cleaves 'Lys-63'-linked polyubiquitin, leaving the last ubiquitin chain attached to its substrates. May act as a central scaffold protein that assembles the various components of the BRISC complex and retains them in the cytoplasm. Plays a role in regulating the onset of apoptosis via its role in modulating 'Lys-63'-linked ubiquitination of target proteins (By similarity). Required for normal mitotic spindle assembly and microtubule attachment to kinetochores via its role in deubiquitinating NUMA1. Plays a role in interferon signaling via its role in the deubiquitination of the interferon receptor IFNAR1; deubiquitination increases IFNAR1 activities by enhancing its stability and cell surface expression. Down-regulates the response to bacterial lipopolysaccharide (LPS) via its role in IFNAR1 deubiquitination. Required for normal induction of p53/TP53 in response to DNA damage. Independent of the BRISC complex, promotes interaction between USP7 and p53/TP53, and thereby promotes deubiquitination of p53/TP53, preventing its degradation and resulting in increased p53/TP53-mediated transcription regulation and p53/TP53-dependent apoptosis in response to DNA damage.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:20656690, ECO:0000269|PubMed:21195082, ECO:0000269|PubMed:21282113, ECO:0000269|PubMed:22974638, ECO:0000269|PubMed:24075985, ECO:0000269|PubMed:25283148}. Nucleus {ECO:0000269|PubMed:21282113, ECO:0000269|PubMed:22974638, ECO:0000269|PubMed:24075985, ECO:0000269|PubMed:25283148}. Cytoplasm, cytoskeleton, spindle pole {ECO:0000269|PubMed:26195665}. Cytoplasm, cytoskeleton {ECO:0000269|PubMed:26195665}. Note=A minor proportion is detected in the nucleus (PubMed:21282113, PubMed:22974638). Translocates into the nucleus in response to DNA damage (PubMed:25283148). Directly binds to microtubules and is detected at the minus end of K-fibers (PubMed:26195665). Co-localizes with NUMA1 at mitotic spindle poles (PubMed:26195665). {ECO:0000269|PubMed:21282113, ECO:0000269|PubMed:22974638, ECO:0000269|PubMed:25283148, ECO:0000269|PubMed:26195665}.
Interaction partners:
- Serine hydroxymethyltransferase, mitochondrial
- Lys-63-specific deubiquitinase BRCC36
- BRISC and BRCA1-A complex member 2
- BRISC and BRCA1-A complex member 1
- BRCA1-A complex subunit RAP80
- Ubiquitin carboxyl-terminal hydrolase 7
- Breast cancer type 1 susceptibility protein
- Cellular tumor antigen p53
- 26S proteasome non-ATPase regulatory subunit 14
- THAP domain-containing protein 5
Sequence:
MAASISGYTFSAVCFHSANSNADHEGFLLGEVRQEETFSISDSQISNTEFLQVIEIHNHQPCSKLFSFYDYASKVNEESLDRILKDRRKKVIGWYRFRRNTQQQMSYREQVLHKQLTRILGVPDLVFLLFSFISTANNSTHALEYVLFRPNRRYNQRISLAIPNLGNTSQQEYKVSSVPNTSQSYAKVIKEHGTDFFDKDGVMKDIRAIYQVYNALQEKVQAVCADVEKSERVVESCQAEVNKLRRQITQRKNEKEQERRLQQAVLSRQMPSESLDPAFSPRMPSSGFAAEGRSTLGDAEASDPPPPYSDFHPNNQESTLSHSRMERSVFMPRPQAVGSSNYASTSAGLKYPGSGADLPPPQRAAGDSGEDSDDSDYENLIDPTEPSNSEYSHSKDSRPMAHPDEDPRNTQTSQI
Protein: Epididymis luminal protein 60 (Epididymis secretory sperm binding protein) (V9HWB7)
Organism: Homo sapiens (Human)
Subcellular location: Cytoplasm {ECO:0000256|RuleBase:RU361275}.
Interaction partners:
Sequence:
MSNPFAHLAEPLDPVQPGKKFFNLNKLEDSRYGRLPFSIRVLLEAAIRNCDEFLVKKQDIENILHWNVTQHKNIEVPFKPARVILQDFTGVPAVVDFAAMRDAVKKLGGDPEKINPVCPADLVIDHSIQVDFNRRADSLQKNQDLEFERNRERFEFLKWGSQAFHNMRIIPPGSGIIHQVNLEYLARVVFDQDGYYYPDSLVGTDSHTTMIDGLGILGWGVGGIEAEAVMLGQPISMVLPQVIGYRLMGKPHPLVTSTDIVLTITKHLRQVGVVGKFVEFFGPGVAQLSIADRATIANMCPEYGATAAFFPVDEVSITYLVQTGRDEEKLKYIKKYLQAVGMFRDFNDPSQDPDFTQVVELDLKTVVPCCSGPKRPQDKVAVSDMKKDFESCLGAKQGFKGFQVAPEHHNDHKTFIYDNTEFTLAHGSVVIAAITSCTNTSNPSVMLGAGLLAKKAVDAGLNVMPYIKTSLSPGSGVVTYYLQESGVMPYLSQLGFDVVGYGCMTCIGNSGPLPEPVVEAITQGDLVAVGVLSGNRNFEGRVHPNTRANYLASPPLVIAYAIAGTIRIDFEKEPLGVNAKGQQVFLKDIWPTRDEIQAVERQYVIPGMFKEVYQKIETVNESWNALATPSDKLFFWNSKSTYIKSPPFFENLTLDLQPPKSIVDAYVLLNLGDSVTTDHISPAGNIARNSPAARYLTNRGLTPREFNSYGSRRGNDAVMARGTFANIRLLNRFLNKQAPQTIHLPSGEILDVFDAAERYQQAGLPLIVLAGKEYGAGSSRDWAAKGPFLLGIKAVLAESYERIHRSNLVGMGVIPLEYLPGENADALGLTGQERYTIIIPENLKPQMKVQVKLDTGKTFQAVMRFDTDVELTYFLNGGILNYMIRKMAK
Protein: Pleckstrin homology like domain family B member 2 (E9PDY7)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MEEHSYIQKELDLQNGSLEEDSVVHSVENDSQNMMESLSPKKYSSSLRFKANGDYSGSYLTLSQPVPAKRSPSPLGTSVRSSPSLAKIQGSKQFSYDGTDKNIPMKPPTPLLNTTSSLSGYPLGRADFDHYTGRDSERALRLSEKPPYSKYSSRHKSHDNVYSLGGLEGRKASGSLLAMWNGSSLSDAGPPPISRSGAASMPSSPKQARKMSIQDSLALQPKLTRHKELASENINLRTRKYSSSSLSHMGAYSRSLPRLYRATENQLTPLSLPPRNSLGNSKRTKLGEKDLPHSVIDNDNYLNFSSLSSGALPYKTSASEGNPYVSSTLSVPASPRVARKMLLASTSSCASDDFDQASYVGTNPSHSLLAGESDRVFATRRNFSCGSVEFDEADLESLRQASGTPQPALRERKSSISSISGRDDLMDYHRRQREERLREQEMERLVIFISTVIDLTVSLTSIYRAALEMDSRICGNIGYSCSLATAAIFLFSPAILLLPISLLIGLFGYLEGLQELMLI
Protein: Transmembrane protein 143 (Q96AN5)
Organism: Homo sapiens (Human)
Subcellular location: Membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}.
Interaction partners:
Sequence:
MTVELWLRLRGKGLAMLHVTRGVWGSRVRVWPLLPALLGPPRALSSLAAKMGEYRKMWNPREPRDWAQQYRERFIPFSKEQLLRLLIQEFHSSPAEKAALEAFSAHVDFCTLFHYHQILARLQALYDPINPDRETLDQPSLTDPQRLSNEQEVLRALEPLLAQANFSPLSEDTLAYALVVHHPQDEVQVTVNLDQYVYIHFWALGQRVGQMPLKSSVGSRRGFFTKLPPAERRYFKRVVLAARTKRGHLVLKSFKDTPLEGLEQLLPELKVRTPTLQRALLNLMLVVSGVAIFVNVGMVVLTDLKVATSLLLLLFAIFMGLRASKMFGQRRSAQALELAHMLYYRSTSNNSELLSALALRAQDEHTKEALLAHSFLARRPGGTQGSPEETSRWLRSEVENWLLAKSGCEVTFNGTRALAHLQALTPSMGLYPPPGFPKLDPVAPITSEPPQATPSSNIS
Protein: Sll1632 protein (P73457)
Organism: Synechocystis sp. (strain ATCC 27184 / PCC 6803 / Kazusa)
Interaction partners:
- Penicillin-binding protein
- Sll0446 protein
- Cyanophycin synthetase
- UDP-N-acetylglucosamine--N-acetylmuramyl-
- Probable peptidoglycan glycosyltransferase FtsW
- UDP-N-acetylmuramoylalanine--D-glutamate ligase
- Protein translocase subunit SecE
- UDP-N-acetylmuramate--L-alanine ligase
- Protein translocase subunit SecY
- Slr0243 protein
Sequence:
MTDLVVSDSLKNRREQLMWQRRWKRLRSCWQFVCVCGLTGGMVWVMSWPEWSIRSDRQVEFLGNKLVSRETLYEDLDLEYPQAVWQLSTQALGDELAKNPALLRVEVTRQLFPAQVNVAVQERQPVAIAVADQGPGYLDGEGNYIPASLYSQAVRKTLPQTPQFLGYGPQYRSFWQTHQILIQQSPVNIRIINGNNPSNISLTTDLGLVFIGSDLSRFGQQVQVLEKMQNLPSRVPKERLLFIDLTNPDSPSIQLRPQPPKEKAAVNKP
Protein: Dihydrofolate reductase (EC 1.5.1.3) (Q5A5E0)
Organism: Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast)
Interaction partners:
- Thymidylate synthase
- Dihydrofolate synthetase
- methionyl-tRNA formyltransferase
- Bifunctional phosphoribosylaminoimidazolecarboxamide formyltransferase/IMP cyclohydrolase
- Phosphoribosylglycinamide formyltransferase
- Folylpolyglutamate synthase
- C-1-tetrahydrofolate synthase, cytoplasmic
- Mis12p
- Serine hydroxymethyltransferase, cytosolic
- Serine hydroxymethyltransferase
Sequence:
MSKPNVAIIVAALKPALGIGYKGKMPWRLRKEIRYFKDVTTRTTKPNTRNAVIMGRKTWESIPQKFRPLPDRLNIILSRSYENEIIDDNIIHASSIESSLNLVSDVERVFIIGGAEIYNELINNSLVSHLLITEIEHPSPESIEMDTFLKFPLESWTKQPKSELQKFVGDTVLEDDIKEGDFTYNYTLWTRK
Protein: NADH-ubiquinone oxidoreductase chain 3 (EC 7.1.1.2) (Q37035)
Organism: Oryza sativa subsp. japonica (Rice)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004370}. Mitochondrion membrane {ECO:0000256|RuleBase:RU003640}; Multi-pass membrane protein {ECO:0000256|RuleBase:RU003640}.
Interaction partners:
Sequence:
MDNIFFGVYNARNGYESATVLQGIRIDLAINGYESAFLSEFAPICIYLVISPLVSLIPLGVPFPFASNSSTYPEKLSAYECGFDPSGDARSRFDIRFYPVPILFIIPDLEVTFFFPWAVPPNKIDLFGSWSMMAFLLILTIGFLYEWKRGASDRE
Protein: Putative L-ribulose-5-phosphate 3-epimerase SgbU (EC 5.1.3.22) (L-xylulose-5-phosphate 3-epimerase) (P37679)
Organism: Escherichia coli (strain K12)
Function: Catalyzes the isomerization of L-xylulose-5-phosphate to L-ribulose-5-phosphate (Potential). May be involved in the utilization of 2,3-diketo-L-gulonate.
Interaction partners:
- 3-keto-L-gulonate-6-phosphate decarboxylase SgbH
- L-xylulose/3-keto-L-gulonate kinase
- L-ribulose-5-phosphate 4-epimerase SgbE
- 3-keto-L-gulonate-6-phosphate decarboxylase UlaD
- L-ribulose-5-phosphate 4-epimerase UlaF
- L-ribulose-5-phosphate 4-epimerase AraD
- 2,3-diketo-L-gulonate-binding periplasmic protein YiaO
- L-ribulose-5-phosphate 3-epimerase UlaE
- 2,3-diketo-L-gulonate TRAP transporter large permease protein YiaN
- Ribulokinase
Sequence:
MRNHQLGIYEKALAKDLSWPERLVLAKSCGFDFVEMSVDETDERLSRLDWSAAQRTSLVAAMIETGVGIPSMCLSAHRRFPFGSRDEAVRERAREIMSKAIRLARDLGIRTIQLAGYDVYYEDHDEGTRQRFAEGLAWAVEQAAASQVMLAVEIMDTAFMNSISKWKKWDEMLASPWFTVYPDVGNLSAWGNDVPAELKLGIDRIAAIHLKDTQPVTGQSPGQFRDVPFGEGCVDFVGIFKTLHKLNYRGSFLIEMWTEKAKEPVLEIIQARRWIEARMQEAGFIC
Protein: Bruno 3, isoform G (M9MRT4)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MVHIIELVGQPKVEFAQQVTMNRALQLKPAENESRSEHLDRKLFVGMLSKQQTEDDVRQIFHPFGTIEECTILRGPDGASKGCAFVKFGSQQEAQSAITNLHGSQTMPGASSSLVVKYADTEKERQIRRMQQMAGHMNLLNPFVFNQFSPYGAYAQLPSPPELQQQQQAALMAAAATAPGSAAAYMNPMAALATQIPHGLNGTGQPPSLPSPTMPNFNMGANTPNGQPGGAAAAAAAAAAADGVFTNGIPQTAFPGHPLHLTIPPQGLPNGDAATLQHAFPGLPPFPGVDFLMFPGCSISGPEGCNLFIYHLPQEFGDAELMQMFLPFGNVISSKVFIDRATNQSKCFGFVSFDNPASAQAAIQAMNGFQIGMKRLKVQLKRPKDASRPY
Protein: 4-hydroxybenzoate polyprenyltransferase, mitochondrial (4-HB polyprenyltransferase) (EC 2.5.1.39) (4-hydroxybenzoate decaprenyltransferase) (Para-hydroxybenzoate--polyprenyltransferase) (PHB:PPT) (PHB:polyprenyltransferase) (p-hydroxybenzoate polyprenyl diphosphate transferase) (Q10252)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Catalyzes the prenylation of para-hydroxybenzoate (PHB) with an all-trans polyprenyl group. Mediates the second step in the final reaction sequence of coenzyme Q (CoQ) biosynthesis, which is the condensation of the polyisoprenoid side chain with PHB, generating the first membrane-bound Q intermediate.
Subcellular location: Mitochondrion {ECO:0000269|PubMed:24911838}. Mitochondrion inner membrane {ECO:0000255|HAMAP-Rule:MF_03189, ECO:0000269|PubMed:11092853}; Multi-pass membrane protein {ECO:0000255|HAMAP-Rule:MF_03189}; Matrix side {ECO:0000255|HAMAP-Rule:MF_03189}.
Interaction partners:
- Ubiquinone biosynthesis O-methyltransferase, mitochondrial
- Ubiquinone biosynthesis monooxygenase COQ6, mitochondrial
- Ubiquinone biosynthesis protein coq4, mitochondrial
- Ubiquinone biosynthesis protein coq9
- 2-methoxy-6-polyprenyl-1,4-benzoquinol methylase, mitochondrial
- Atypical kinase COQ8, mitochondrial
- 5-demethoxyubiquinone hydroxylase, mitochondrial
- Decaprenyl-diphosphate synthase subunit 1
- Ubiquinone biosynthesis protein coq11
- Isopentenyl-diphosphate delta-isomerase
Sequence:
MIIKPIASPARYFLRTPSWSAVAIFQAVKIKPLQLRTNSSNSVTPNLISPSKKSWKDLFSKRWQYYAEISRAGSPTGTYLLYSPCTWSILMAAYAYDSSLVNVTKMLALFGVGSFLMRSAGCVINDLWDRELDAKVERSKSRPLASGKLSVRQAISLLSVQLTASLGILLQLNPYTIKLGVASLVPVCIYPAMKRITYYPQVVLGLTFGYGAVMGWPALAGEACMNWSVVAPLYLSTISWIVLYDTIYAHQDKRDDVKANIYSTALRFGDNTKPVLCGLAALQIATLATAGIMNGQGPVFYTLGVAGAAYRLSSMIYKVDLDDPKDCFRWFKRNSNTGYLVAAAIALDWLAKSFIYDS
Protein: Validamycin A dioxygenase (EC 1.14.11.52) (Alpha-ketoglutarate/Fe(II)-dependent dioxygenase VldW) (Validamycin B synthase) (Q15JG7)
Organism: Streptomyces hygroscopicus subsp. limoneus
Function: Involved in the biosynthesis of validamycin B, a component of the antifungal and antibiotic validamycin complex used as a crop protectant. Catalyzes the regioselective hydroxylation of validamycin A (4-O-beta-D-glucopyranosyl-validoxylamine A) at the C-6 position to yield validamycin B. To a lesser extent, also able to convert validoxylamine A to its hydroxylated derivative.
Interaction partners:
Sequence:
MTGSVPIVDLEAWRAADEENRASLAEIIDGALHTVGTFLLAGHGVPAELTARMRTAGRSFFDLPWEKKEPHAVQRPHDNGWRGLVKHRTDTIEGTGGAPDLHEAFHMGPTHRTGDDAFDALYYPANKWPAELPELRETALAYTAHMTRVAGAVMEMLAGVLGLEPAFFTSRCEHATWTQSVNWYPSLDTVGQTAEGQMRVGPHTDFGTITLLDRQQGVSGLEVWSEEDGWFAPPFVEGTLLVNLGDLMHQWTDGRWRSLRHRVLAPSASAPQEELVSLVYFFDADPEAELVPLAAPVGGGAGMPTVNVGETILKKNIQMLTDLKGHGLFQGELSLSRPGSADSPGSSPADDHPSRPGRHPAQGPQ
Protein: Tail fiber assembly helper protein (Gene product 57) (gp57) (P04532)
Organism: Enterobacteria phage T4 (Bacteriophage T4)
Function: Chaperone essential for folding and oligomerization of both long and short tail fibers. Required for the assembly of gp34, gp36 and gp37 (components of the long tail fiber) and p12 (the subunit of the short tail fiber). Together with gp38, participates in the formation of the distal part of the long fibers.
Interaction partners:
Sequence:
MSEQTVEQKLSAEIVTLKSRILDTQDQAARLMEESKILQGTLAEIARAVGITGDTIKVEEIVEAVKNLTAESADEAKDEE
Protein: Protein kinase superfamily protein (F4KI00)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
- TOM1-like protein 9
- Protein DETOXIFICATION 51
- TOM1-like protein 5
- Transcription factor MYB36
- TOM1-like protein 3
- TOM1-like protein 6
Sequence:
MAVEEMEKKIKGSQETELHKNDLSIEDPSPRCVLEIPVMSSDSDNSSSCSSCSPDKSSSPLSTTPPNVSSFHQWNKMIESIKKKSIRRFSVIPLLASYELTRKKKQPKLSPCSENDFDCDQILVAKPSWRNFTFDELVAATDNFNPENMIGKGGHAEVYKGVLPDGETVAIKKLTRHAKEVEERVSDFLSELGIIAHVNHPNAARLRGFSCDRGLHFVLEYSSHGSLASLLFGSEECLDWKKRYKVAMGIADGLSYLHNDCPRRIIHRDIKASNILLSQDYEAQISDFGLAKWLPEHWPHHIVFPIEGTFGYLAPEYFMHGIVDEKTDVFAFGVLLLEIITGRRAVDTDSRQSIVMWAKPLLEKNNMEEIVDPQLGNDFDETEMKRVMQTASMCIHHVSTMRPDMNRLVQLLRGDDQLAEQKPGGARTVSLDDCDLDHTSSSYLNDLTRHRQLLME
Protein: Mitogen-activated protein kinase 16 (AtMPK16) (MAP kinase 16) (EC 2.7.11.24) (Q8W4J2)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
- Protein-tyrosine-phosphatase PTP1
- Protein phosphatase 2C and cyclic nucleotide-binding/kinase domain-containing protein
Sequence:
MQPDHRKKSSVEVDFFTEYGEGSRYRIEEVIGKGSYGVVCSAYDTHTGEKVAIKKINDIFEHVSDATRILREIKLLRLLRHPDIVEIKHILLPPSRREFRDIYVVFELMESDLHQVIKANDDLTPEHYQFFLYQLLRGLKYIHTANVFHRDLKPKNILANADCKLKICDFGLARVAFNDTPTAIFWTDYVATRWYRAPELCGSFFSKYTPAIDIWSIGCIFAELLTGKPLFPGKNVVHQLDLMTDMLGTPSAEAIGRVRNEKARRYLSSMRKKKPIPFSHKFPHTDPLALRLLEKMLSFEPKDRPTAEEALADVYFKGLAKVEREPSAQPVTKLEFEFERRRITKEDVRELIYRESLEYHPKMLKEYLDGSEPTNFMYPSAVEHFKKQFAYLEEHYKNGTSHNPPERQQHASLPRACVLYSDNNHPVAQQSSAEVTDGLSKCSIRDERPRGADRNAQMPMSRIPINVPQTIQGAAVARPGKVVGSVLRYNNCGAATGVEALEQQQRRMVRNPAAASQYPKRTQPCKSNRGDEDCATAAEGPSRLKPNTQYIPQKVSAAQDTAMSRWY
Protein: Initiator protein NS1 (NS1) (EC 3.1.21.-) (EC 3.6.4.12) (Non-structural protein 1) (Non-structural protein NS1) (P24030)
Organism: Aleutian mink disease parvovirus (strain G) (ADV)
Function: Multifunctional protein which displays endonuclease and helicase activities required for initiating and directing viral DNA replication. Also plays a role in viral packaging and transactivation of several promoters. Binds site-specifically to 2-3 approximate tandem copies within the origins of replication (Ori), unwinds this hairpin region and nicks one DNA strand thereby initiating the rolling circle replication (RCR).
Subcellular location: Host nucleus {ECO:0000269|PubMed:12692232}.
Interaction partners:
Sequence:
MAQAQIDEQRRLQDLYVQLKKEINDGEGVAWLFQQKTYTDKDNKPTKATPPLRTTSSDLRLAFDSIEENLTASNEHLTNNEINFCKLTLGKTLLLIDKHVKSHRWDSNKVNLIWQIEKGKTQQFHIHCCLGYFDKNEDPKDVQKSLGWFMKRLNKDLAVIYSNHHCDIQDIKDPEDRAKNLKVWIEDGPTKPYKYFNKQTKQDYNKPVHLRDYTFIYLFNKDKINTDSMDGYFAAGNGGIVDNLTNKERKTLRKMYLDEQSSDIMDANIDWEDGQDAPKVTDQTDSATTKTGTSLIWKSCATKVTSKKEVANPVQQPSKKLYSAQSTLDALFNVGCFTPEDMIIKQSDKYLELSLEPNGPQKINTLLHMNQVKTSTMITAFDCIIKFNEEEDDKPLLATIKDMGLNEQYLKKVLCTILTKQGGKRGCIWFYGPGGTGKTLLASLICKATVNYGMVTTSNPNFPWTDCGNRNIIWAEECGNFGNWVEDFKAITGGGDVKVDTKNKQPQSIKGCVIVTSNTNITKVTVGCVETNAHAEPLKQRMIKIRCMKTINPKTKITPGMLKRWLNTWDRQPIQLSHEMPELYLGKCRW
Protein: Large ribosomal subunit protein eL43 (60S ribosomal protein L37a) (Q9VMU4)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
- Large ribosomal subunit protein eL8
- Large ribosomal subunit protein eL21
- Large ribosomal subunit protein uL6
- Small ribosomal subunit protein uS17
- Large ribosomal subunit protein uL11
- Large ribosomal subunit protein uL13
- Small ribosomal subunit protein uS15
- Small ribosomal subunit protein uS11A
- 40S ribosomal protein S27
- Small ribosomal subunit protein uS14
Sequence:
MAKRTKKVGIVGKYGTRYGASLRKMVKKMEITQHSKYTCSFCGKDSMKRAVVGIWSCKRCKRTVAGGAWVYSTTAAASVRSAVRRLRETKEQ
Protein: AT14762p (Q8T977)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MEGNRSLVVLGLILILIELTTPTSTPAPTPQPAGAEEAPGNSTAEASKSSTASKCKSTEILSENGCVDRENFLNKIVMRSWRDEGFEKAKARAGLVDCVECRDGELRTAFGCSKPLYPPHVDVNRVPVHHSRLNGERIVHDKGIYTLYHHVEDVEQKPIRKPRVVGPPITGNKRPRKYVFLPGRSIGKGHTCRANEVLGRRNRCIHRKRLAGQRQNQTIENEQSQ
Protein: Protocadherin 18a (Protocadherin-18a isoform X1) (F1QRP2)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004167}; Single-pass membrane protein {ECO:0000256|ARBA:ARBA00004167}.
Interaction partners:
Sequence:
METSKGTVLCATLLKLALLVTLAGYTTAATLKYQVYEEQKVGTVIARLREDVADVLSKLPSSIPLRFRAMQRGSASLLSVRDQDGEISIRTKIDREKLCEKNLNCTIEFDVLTLPTEHLQLFHIEVEILDINDNAPQFARPVIPIEISETAAVGTRIPLDSATDPDVGENSLNTYSLTPSDFFKIDILTRTDGAKYAELVVLKELDREVRASYELQLTASDRGVPPKFGTTLLKISIADSNDNNPVFEKPSYVINLLENSPLGSLLIDLNATDPDEGANGKIIYSFSSHVSPKILETFKINSDNGHLTLMRKVDFESTNSYDIDVQAQDMGPNSMPAHCKVIIKVVDVNDNKPDISVNLMSTGNEEIAYISETAPVDTFVALVSVNDLDSGLNGEVECRLYGQGHFRLQKSYEKNYMILTNVTLDREKRSEFSLTVIAEDKGSPSLSTIKNFIVEVQDENDNAPSFAKSRYEISKAENNSPGAYLSSVKASDPDLGPNGQVSYSILESMVHGSSISTYVTIDPSNGDIYALRTFDREDVSQISFLVQARDSGNPPLRSNVTVVLTVLDENDNRPVIMMPQLWNHTADVPVSKYAEIGDVVTVVRAMDHDAGANGDLSCSVVGGNEAGYFNMDPKTCEIRTNVSIQEVPRDHVELTILVQDHGTPTLSARALLRLSLYENIENLMNPHLTGGRNGDGPLDVSMIIIISLGAICAVLLLIMVAFALRCSREKKDTRSYNCRVAESTYQQHPKKPSRQIHKGDITLMPTVNGTLPIRAHHRSPTSSPGPERAHMGSRQSQHSRQSLNSLVTISSNHIPENFALELTHATPPVEQVSQLLSILHQGQYQPRPSFRGNKYSRSYRYALQDMDKFSLKDSGRGDSDAGDSDCEMGRDSPIDRLLGDGFGDLFHSDGHHRLHPAVMRLCTEECRVLGHSDQCWMPSQASSDYRANMFIPGEESRPQVLEEDQQSVDSAKKSFSTFGKDNEEECGGSLLSEMNNVFQRLLPTSYADVRELDESTSQPASSIGMEIRKGFLPGKASSTGSAYPQGVAVWAANTHFQNPGGAVTSGHATTNHAASQAHLKWLPAMEEIPENYEEDDLESVLSQRQGKRNDTRHEVVDASELVAEINKLLQDVRQS
Protein: Dihydromonacolin L-[lovastatin nonaketide synthase] thioesterase (EC 3.1.2.31) (Esterase lovG) (Lovastatin biosynthesis cluster protein G) (Q9Y7C9)
Organism: Aspergillus terreus
Function: Esterase; part of the gene cluster that mediates the biosynthesis of lovastatin (also known as mevinolin, mevacor or monacolin K), a hypolipidemic inhibitor of (3S)-hydroxymethylglutaryl-coenzyme A (HMG-CoA) reductase (HMGR). The first step in the biosynthesis of lovastatin is the production of dihydromonacolin L acid by the lovastatin nonaketide synthase lovB and the trans-acting enoyl reductase lovC via condensation of one acetyl-CoA unit and 8 malonyl-CoA units. Dihydromonacolin L acid is released from lovB by the thioesterase lovG. Next, dihydromonacolin L acid is oxidized by the dihydromonacolin L monooxygenase lovA twice to form monacolin J acid. The 2-methylbutyrate moiety of lovastatin is synthesized by the lovastatin diketide synthase lovF via condensation of one acetyl-CoA unit and one malonyl-CoA unit. Finally, the covalent attachment of this moiety to monacolin J acid is catalyzed by the transesterase lovD to yield lovastatin. LovD has broad substrate specificity and can also convert monacolin J to simvastatin using alpha-dimethylbutanoyl-S-methyl-3-mercaptopropionate (DMB-S-MMP) as the thioester acyl donor, and can also catalyze the reverse reaction and function as hydrolase in vitro. LovD has much higher activity with LovF-bound 2-methylbutanoate than with free diketide substrates.
Interaction partners:
Sequence:
MRYQASPALVKAPRALLCIHGAGCSPAIFRVQLSKLRAALRENFEFVYVTAPFPSSAGPGILPVFADLGPYYSWFESSSDNNHNGPSVSERLAAVHDPIRRTIVDWQTQHPHIPIVGAIGFSEGALVTTLLLWQQQMGHLPWLPRMSVALLICPWYQDEASQYMRNEVMKNHDDDNDSKDTEWQEELVIRIPTLHLQGRDDFALAGSKMLVARHFSPREAQVLEFAGQHQFPNRPRDVLEVINRFRKLCVTAQTLE
Protein: Tubulin beta-2 chain (Beta-tubulin class-II) (P32882)
Organism: Gallus gallus (Chicken)
Function: Tubulin is the major constituent of microtubules, a cylinder consisting of laterally associated linear protofilaments composed of alpha- and beta-tubulin heterodimers. Microtubules grow by the addition of GTP-tubulin dimers to the microtubule end, where a stabilizing cap forms. Below the cap, tubulin dimers are in GDP-bound state, owing to GTPase activity of alpha-tubulin.
Subcellular location: Cytoplasm, cytoskeleton.
Interaction partners:
- Gap junction alpha-1 protein
- Tubulin alpha chain
- Tubulin alpha chain
- Tubulin alpha-2 chain
- Tubulin alpha-5 chain
- Tubulin alpha chain
- Tubulin alpha chain
- Tubulin alpha chain
- Tubulin alpha chain
- Tubulin alpha chain
Sequence:
MREIVHIQAGQCGNQIGAKFWEVISDEHGIDPTGSYHGDSDLQLERINVYYNEATGNKYVPRAILVDLEPGTMDSVRSGPFGQIFRPDNFVFGQSGAGNNWAKGHYTEGAELVDSVLDVVRKESESCDCLQGFQLTHSLGGGTGSGMGTLLISKIREEYPDRIMNTFSVMPSPKVSDTVVEPYNATLSVHQLVENTDETYCIDNEALYDICFRTLKLTTPTYGDLNHLVSATMSGVTTCLRFPGQLNADLRKLAVNMVPFPRLHFFMPGFAPLTSRGSQQYRALTVPELTQQMFDSKNMMAACDPRHGRYLTVAAIFRGRMSMKEVDEQMLNVQNKNSSYFVEWIPNNVKTAVCDIPPRGLKMSATFIGNSTAIQELFKRISEQFTAMFRRKAFLHWYTGEGMDEMEFTEAESNMNDLVSEYQQYQDATADEQGEFEEEGEEDEA