wanglab/gogpt-training-data huggingface dataset:
Protein: Cilium assembly protein DZIP1L (DAZ-interacting zinc finger protein 1-like) (Zinc finger protein DZIP1) (Q9VC70)
Organism: Drosophila melanogaster (Fruit fly)
Function: Component of the DZIP1-Fam92-Cby complex which promotes ciliogenesis in sensory neurons and spermatocytes by acting downstream of Cep290 to initiate early ciliary membrane formation and thus transition zone (TZ) assembly. During spermatogenesis, also regulates distal elongation of the basal-body and their docking (anchoring) to the plasma membrane and as a consequence, regulates the initiation and proper elongation of axonemal microtubules. Within the complex, required to recruit or stabilize Rab8, Fam92 and Cby at the distal basal body of cilia to promote early ciliary membrane formation and initiate TZ assembly. Also acts with Fam92 to restrict cep290 localization to the proximal part of the TZ. May also be involved in recruitment or stabilization of Mks1 at the TZ.
Subcellular location: Cytoplasm, cytoskeleton, microtubule organizing center, centrosome, centriole {ECO:0000269|PubMed:31821146, ECO:0000269|PubMed:33370260}. Cytoplasm, cytoskeleton, cilium basal body {ECO:0000269|PubMed:31821146, ECO:0000269|PubMed:33370260}. Note=Localizes at the transition zone (TZ) in type I sensory neurons and spermatocytes (PubMed:31821146, PubMed:33370260). In spermatocytes, localizes along the TZ membranes (PubMed:33370260). Localizes at the centriolar distal ends of early spermatocytes and in elongating spermatids, when the TZ migrates away from the basal body, localizes at the ring centriole (PubMed:31821146, PubMed:33370260). In sensory neurons, localizes between the transition fiber and TZ core components (PubMed:33370260). {ECO:0000269|PubMed:31821146, ECO:0000269|PubMed:33370260}.
Interaction partners:
- CBY1-interacting BAR domain-containing protein homolog
- GH21622p
- FI08143p
- AT27838p
- Ccp84Ac
- carboxylesterase
Sequence:
MGFKGKYPQMVRETGFKLRQYRDGPLDWRLMGSYETERILREQNFELVDKALTHLSEAPLGTVLETHILDSGIAKYFVMSQYAIQYLMCCRTYLDECVTDLKEAHTTAQEEIATLRKSLSESNNEVVQLHKRITQIEAIREVVYPCHLCTKNFISNEALNVHIGRKHRVASPPSLTSATGKEKDRDKATDVHLINTIKMELEIKQLKERLNAAERNIKERSTGSKRVSPRQEQRHVGIQSNLAEPKEKDEDSGEARQSEASERKEQLTGLAERLSNFEEWQTQLKQSNEQFIQDINKRLEGLSHALEQSKQASASTPPLEDRVATPCLEDLERILTEKVAEIGKVSAHRLEEVVYHLEEGYKEKLGALERELKQLSVQKVQPEPVQTVPVASKIPKPVVRKEETNIDRIRKQVESEFLKQKHDDDTYSIEEAPRKGSEKPFPQLVTQVQVVEKEQPSAGSSDSNPTYTKSPREPAPNKQETKEATDVSDSLSQEETENEEERSLTEEEGTDVPTSGSEAAREDPTPKTIKPSGRIIKSPQKPLTRKDARKMVNRKLMSHGFDMKSKGISHNSLKRVNSELTEHRNKLKLQHPHFYATRNRIRKFVEKLCSAKFSERAEMLLKHKSPLKPMEVPGKGIPRSAISEKSEEDIASSQGEEQTDEQTDSSEQQTRSPSPQRLVSRDFKARLEEILVKPAATIRGASKSSLSSRPVPLPRKRVMFNTTEDGKSFNDSDDNLK
Protein: Desmethylxanthohumol 6'-O-methyltransferase (EC 2.1.1.338) (O-methyltransferase 1) (HlOMT1) (B0ZB55)
Organism: Humulus lupulus (European hop)
Function: Involved in the biosynthesis of prenylated phenolics natural products which contribute to the bitter taste of beer and display broad biological activities (Probable). Catalyzes the biosynthesis of xanthohumol. Methylates desmethylxanthohumol and xanthogalenol, but not caffeic acid, prenylflavanones, simple phenols or phenylpropanoids.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:29760092}.
Interaction partners:
Sequence:
MESLRGQEQIWQLMFSFVDSMALKCAIELRIADIIHSHGKPITLSQIASGIRSNSNSSISPNIPYLSRIMRFLVRKNIFTEHQEDNDEVISLYGLSDSSRWLLRDFKSSLAPMVLMQTHPLSMAVWHFLEDYVRNSSNTFEKAHGCNIWEFSSANPDFNKIFNNAMASIVPIYMGAVLSSYKDGLGCIKGTVVDVGGGTGGSISELMKYYPNIKGINFDLPHVIATAPALDGVTHISGDIFESIPSADAVLMKGVLHCFSDEKCVKVLRNCRKAITDKKNGKIIILEIVLDPTSNQIFDETRMVYDLLIPLFSGGKERTELEWKRLLNEAGFTSIKITKIPIIPAIIEAFLV
Protein: Transcriptional regulator CRZ2 (Calcineurin-responsive zinc finger protein 2) (Q59SN6)
Organism: Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast)
Function: Transcription factor that regulates pH-induced filamentation with RIM101. Required for yeast cell adherence to silicone substrate and biofilm formation.
Subcellular location: Nucleus {ECO:0000250}.
Interaction partners:
- Mlc2p
- Calmodulin
Sequence:
MLSTMSNLPIVAGISTTATTGTTSTATASTSTSGSVNTTATNNNNNTSASNSTSASSATANGGIGTNSGNSLQYYYTGNNTSNSVDGNKYSLPSIYFTPQDSINNTSHTYNPYTTVSGAVTPQNYQLDYSQSSTVNNNYQFTLPNQQLSSPQQQQYNRSYSNSLMPNYHYNNTTTNINTNVGSNTSPQLSNSNTPNPISPVLIPDKDNTYNNTNNVLVSSYPSMTMNQIQQQQQQYLQPSQQYQYSYNQYYMQPYYHNPQQSAPQQVQKPAQTEKLPHLSVTNIDYSSLVSYTVSPSLKRKRRTAKKSLSPSSTSSLSMMINHDSTNNGTTSTATTTRSSSTSSATSSSIGVAAADSFPCPQCNKVFQKPYNLKSHMKTHSNEKPYHCNICFKRFARSHDKKRHELLHQGVKNFKCQGYLNDGVTSWGCGKTFARSDALSRHFRTETGWLCIRPLMEEAKRLEEEEQQRQQQAQQQQQVPQQSQVSEQIGVNVGEIKFNDEYYDNSNFIKKLLQSNK
Protein: Polypeptide N-acetylgalactosaminyltransferase 14 (EC 2.4.1.41) (Polypeptide GalNAc transferase 14) (GalNAc-T14) (pp-GaNTase 14) (Protein-UDP acetylgalactosaminyltransferase 14) (UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase 14) (Q96FL9)
Organism: Homo sapiens (Human)
Function: Catalyzes the initial reaction in O-linked oligosaccharide biosynthesis, the transfer of an N-acetyl-D-galactosamine residue to a serine or threonine residue on the protein receptor. Displays activity toward mucin-derived peptide substrates such as Muc2, Muc5AC, Muc7, and Muc13 (-58). May be involved in O-glycosylation in kidney.
Subcellular location: Golgi apparatus membrane {ECO:0000250}; Single-pass type II membrane protein {ECO:0000250}.
Interaction partners:
- Mucin-13
- Mucin-7
- Mucin-5AC
- Mucin-2
Sequence:
MRRLTRRLVLPVFGVLWITVLLFFWVTKRKLEVPTGPEVQTPKPSDADWDDLWDQFDERRYLNAKKWRVGDDPYKLYAFNQRESERISSNRAIPDTRHLRCTLLVYCTDLPPTSIIITFHNEARSTLLRTIRSVLNRTPTHLIREIILVDDFSNDPDDCKQLIKLPKVKCLRNNERQGLVRSRIRGADIAQGTTLTFLDSHCEVNRDWLQPLLHRVKEDYTRVVCPVIDIINLDTFTYIESASELRGGFDWSLHFQWEQLSPEQKARRLDPTEPIRTPIIAGGLFVIDKAWFDYLGKYDMDMDIWGGENFEISFRVWMCGGSLEIVPCSRVGHVFRKKHPYVFPDGNANTYIKNTKRTAEVWMDEYKQYYYAARPFALERPFGNVESRLDLRKNLRCQSFKWYLENIYPELSIPKESSIQKGNIRQRQKCLESQRQNNQETPNLKLSPCAKVKGEDAKSQVWAFTYTQQILQEELCLSVITLFPGAPVVLVLCKNGDDRQQWTKTGSHIEHIASHLCLDTDMFGDGTENGKEIVVNPCESSLMSQHWDMVSS
Protein: ASPSCR1 tether for SLC2A4, UBX domain containing (J3QL04)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MGVFPEAATKPLLSMGWCGKSLSACGSAGAPVLEDTCRRQDFNPCEYDLKFQRSVLDLSLQWRFANLPNNAKLEMVPASRSREGPENMVRIALQLDDGSRLQDSFCSGQTLWELLSHFPQIRECLQHPGGATPVCVYTRDEVTGEAALRGTTLQSLGLTGGSATIRFVMKCYDPVGKTPGSLGSSASAGQAAASAPLPLESGELSRGDLSRPEDADTSGPCCEHTQEKQSTRAPAAAPFVPFSGGGQRLGGPPGPTRPLTSSSAKLPKSLSSPGGPSKPKKSKSGQDPQQEQEQERERDPQQEQERE
Protein: Cutinase CUT1 (EC 3.1.1.74) (CcCUT1) (B9U443)
Organism: Coprinopsis cinerea (Inky cap fungus) (Hormographiella aspergillata)
Function: Catalyzes the hydrolysis of complex carboxylic polyesters found in the cell wall of plants. Degrades cutin, a macromolecule that forms the structure of the plant cuticle. Also degrades suberin, a specialized macromolecule found in the cell wall of various plant tissues.
Interaction partners:
Sequence:
MKFTTLATLALGAVSALAAPVTELESRQLFCRDVYVFFARGTGEVGTLGTVVGPGLSAAVKLAVRDSVEFEGIDYPALVSGYLAGGDRGGARTMANKVSQTASRCPNAKIFISGYSQGAQVTHLAARQLSAADQARVTGVVTFGDPYRDDALPGGLQSRRKTYCNVGDLICAGLPTLLAPHFTYGSDTPDAARWIAARV
Protein: Wdr36 protein (Q6NSU4)
Organism: Mus musculus (Mouse)
Interaction partners:
Sequence:
PRVRGQINDMTFSPDGRWLISAAMDCSVRTWDLPSGCLIDCFLLDSAPLNVTMSPTGDFLATSHVDHLGIYLWSNISLYSVVSLRPLPPDYVPSIVMLPGTCQTQGMEDLEEKTEPSDEMIEYESPEQLSEQLVTLSLLPESRWKNLLNLDVIKKKNKPKEPPKVPQSAPFFIPTVPGLVPRFAVPEPSSDPQQSKVVNLGILAQKSNFYLKLEEGLLNNQYEAALNLLKELGPSGIETELRNLSPDDGGSVEVMRSFLSMIGMMLDRKRDFELAQAYLALFLKLHLRTLPSEPALLEELVKLSSQVEKDWTHLQSLFNQSMCVLNYIKSAFL
Protein: Phosphoribosylamine--glycine ligase (EC 6.3.4.13) (GARS) (Glycinamide ribonucleotide synthetase) (Phosphoribosylglycinamide synthetase) (P15640)
Organism: Escherichia coli (strain K12)
Function: Catalyzes the reversible conversion of phosphoribosylamine to glycinamide ribonucleotide, an enzymatic step in purine biosynthesis pathway.
Interaction partners:
- Phosphoribosylformylglycinamidine synthase
- Amidophosphoribosyltransferase
- Bifunctional purine biosynthesis protein PurH
- N5-carboxyaminoimidazole ribonucleotide mutase
- Phosphoribosylglycinamide formyltransferase
- Phosphoribosylformylglycinamidine cyclo-ligase
- N5-carboxyaminoimidazole ribonucleotide synthase
- Formate-dependent phosphoribosylglycinamide formyltransferase
- Phosphoribosylaminoimidazole-succinocarboxamide synthase
- Adenylosuccinate lyase
Sequence:
MKVLVIGNGGREHALAWKAAQSPLVETVFVAPGNAGTALEPALQNVAIGVTDIPALLDFAQNEKIDLTIVGPEAPLVKGVVDTFRAAGLKIFGPTAGAAQLEGSKAFTKDFLARHKIPTAEYQNFTEVEPALAYLREKGAPIVIKADGLAAGKGVIVAMTLEEAEAAVHDMLAGNAFGDAGHRIVIEEFLDGEEASFIVMVDGEHVLPMATSQDHKRVGDKDTGPNTGGMGAYSPAPVVTDDVHQRTMERIIWPTVKGMAAEGNTYTGFLYAGLMIDKQGNPKVIEFNCRFGDPETQPIMLRMKSDLVELCLAACESKLDEKTSEWDERASLGVVMAAGGYPGDYRTGDVIHGLPLEEVAGGKVFHAGTKLADDEQVVTNGGRVLCVTALGHTVAEAQKRAYALMTDIHWDDCFCRKDIGWRAIEREQN
Protein: SH3 and F-BAR domain-containing protein DDB_G0271676 (Q75JD4)
Organism: Dictyostelium discoideum (Social amoeba)
Interaction partners:
- GTP cyclohydrolase 1
- Vacuolar protein sorting-associated protein VTA1 homolog
Sequence:
MSAQRQFSEDLWDKFESVVKKVDNGKIFTQQLSKFLSKQQQIESAYAKSLVKLCKDKSFAPEVEMGTLRDSFQCYREQLELIGALHEEFSNRLEKLVTIGIDGYLEESRKQRKALIANGEKCTKDLKTAESNESKAKQNYEKLKRKQEEANEDLSKQPPGAKEQKARKTLESATKAADKGDNEYRESVKCLQQNQQKFYHEEMPRILDDLQRFEVERIDKSKDWLMEVITQNELVPPAVIIHNENIKKGIESIDRERDLQNYILVTMSGAQKPPEAQYEPYQSGGGFAIVNSSSNSNLNISRKSGELNGGGSIQNGASIISSPQQPQYQNIDHQTPPQPNIIIQQHQQSNNNNNTNNNSNVMTTPPPPQPQPQQQQLPQPTQLNNPPQPPISLSKNDSSNSINSNSNGEIVRALYDYNATEENEISFKANALIKVVLRDESGWWQGMVIGESDRIGVFPSNFISDSSDSSKKRVDVAGRKCKVLYDYRTDCEGELNIKEGEILTIEYEDEGWFFGSNESNVSARFPSNYVQVI
Protein: MEAB protein (C8V9H0)
Organism: Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) (Aspergillus nidulans)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
- GBLP_NEUCR Guanine nucleotide-binding protein beta subunit-like proteinGbeta like protein
- Small ribosomal subunit protein uS5
- 40S ribosomal protein S3
- 60S ribosomal protein L23
- Large ribosomal subunit protein uL18 C-terminal eukaryotes domain-containing protein
- 40S ribosomal protein S15
- Uncharacterized protein
- Large ribosomal subunit protein uL3
- Small ribosomal subunit protein eS19
- 60S ribosomal protein L31e
Sequence:
MVSMVEASILNHNDMAMDQVAPKSEPLNEGSISSAVSTPDPEGEVLTQDVAQTQKRKGGRKPIYATSEERKQRNRQAQAAFRERRTEYIRQLESTIKRNEESLQTLQQNHRTAADECLMLRYKNSLLERILLEKGIDVQAELRLKAGTPNGPGKPSPITTKAPSLQQAAISRSSAQRHPSGLAPKEPFSVPQSRDGGFGIPSPQFQATPPSHVSSPSHAKSPNYGFQGALSPAGVDPQAQRSQMLTHSRNISQTSPPMSVGQPEPTEPKSAVSASMGSRAPRLPSAYYPSPFQKHYDQLEQEYDAQADMIDDEHESSVGTSSFVPGYNPSSSVSNASHPMNPHGMNPYNHSSGEAVNGAYGNTSAMMGNYEPMLDADPFGLSASMHFQTPFSYEQNNARQ
Protein: non-specific serine/threonine protein kinase (EC 2.7.11.1) (F1R2A7)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Interaction partners:
- Mitogen-activated protein kinase
- Mitogen-activated protein kinase
- Cyclic AMP-dependent transcription factor ATF-4
- Cyclic AMP-dependent transcription factor ATF-4
- BUB1 mitotic checkpoint serine/threonine kinase
- non-specific serine/threonine protein kinase
- Motile sperm domain-containing 1.
- Zgc:171704.
- small monomeric GTPase
- small monomeric GTPase
Sequence:
MPLAQLVDPWRKMAIGSAASETEPHHVLEDSMGEDENLSCQEEVSVKEINITHLVKEGSEKADPQQFELRKVLGQGSFGKVFLVKKTTGPDAGQLYAMKVLKKATLKVRDQVRTKMERDILVEVNHPFIVKLHYAFQTEGKLYLILDFLRGGDLFTRLSKEVMFTEEDVKFYLAELALALDHLHGLGIIYRDLKPENILLDEDGHIKLTDFGLSKESIDHENKAYSFCGTVEYMAPEVVNRRGHTYSADWWSYGVLMYEMLTGTLPFQGKDRKETMTMILKAKLGMPQFLSSEAQSLLRSLFKRNPTNRLGAGPDGVEEIKRHPFYVSIDWNKLFRRESHPPFKPATGRPDDTFYFDPEFTAKTPKDSPGVPPSANANRLFRGFSFVAITSEEESQSLPSNSMSSIVQQLHRNVSQFSDAYEVKEDIGIGAYSICKRCIQKSTMMEYAVKVYDDGRTVYLVTELLKGGELLDKILRQKFFSEREACAVLHTITKTVAYLHAQGVVHRDLKPSNILYVDESGNPESIRICDFGFAKQLRAENGLLMTPCYTANFVAPEVLKKQGYDAACDIWSLGVLLYTMLTGFTPFANGPEDTPEEILARIGSGQFSLTGGFWNSVSCQAKDLVSKMLHVDPHQRLTAAQVLKHPWITHKDKLPNYQLNRQDAPHLVKGAMAATFSALNRNIPPVLEPVGCSILAQRRGVKKLTSTAL
Protein: Regulatory protein HrpB (A3P7B1)
Organism: Burkholderia pseudomallei (strain 1106a)
Interaction partners:
Sequence:
MFSTLYFAAAAALANPSSNDAYAARVLDGRFAEAVALVAARCDSQPGDAAADVRDVHAYADIQLVLGRFEEAEDTFRRAQKLLRESRDQTRVMTCRNASWQAFFQNRFGVAQAGFRRIADDRAASAAQKLESLVGTCVVMHHLGRAEDAMATLDVLDAAARGDADGRWVRLAAALRADLLLQYQIGRADALGDHVYWRSALAELPPAAFAETGAPHAACAADAPPLLRMRVAYMRETRALAAGDHAALGRIDTHVSWCAKAGLADYQRSVRLEVALAALAGQAPNVADAMIAPYREAAGRCGSHARWTLDYLYCAAKVREQQGRIRESSSLYAHYALASVRHVRSDGAALAPALAIARCGTQAAAPSDDVSARLPGKYRRAYRYLMERLDQRELSVREIAAHIDVTERALQAAFKAYLGLSPSELIRRQRMERIRGELLSDAPRAASVLEIASRWGIQHRSTLVNGYRRMFDEAPSQTFDR
Protein: LIM/homeobox protein Lhx9 (LIM homeobox protein 9) (Q90881)
Organism: Gallus gallus (Chicken)
Function: May be involved in gonadal development.
Subcellular location: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00108}.
Interaction partners:
- Empty spiracles homeobox 2.
- Uncharacterized protein.
Sequence:
MEIVGCRAEENTCPFRPPAMLFHGISGGHIQGIMEEMERRSKTESRLAKGGQMNGRETNMPPMSPEKPALCAGCGGKISDRYYLLAVDKQWHLRCLKCCECKLALESELTCFAKDGSIYCKEDYYRRFSVQRCARCHLGISASEMVMRARESVYHLSCFTCTTCNKTLTTGDHFGMKDNLVYCRAHFESLLQGEYPPQLSYTELAAKSGGLALPYFNGTGTVQKGRPRKRKSPALGVDIVNYNSGCNENEADHMDRDQQPYPPSQKTKRMATSFKHHQLRTMKSYFAINHNPDAKDLKQLAQKTGLTKRVLQVWFQNARAKFRRNLLRQENGGVDKADGTSLPAPPSADSGALTPPGTATTLTDLTNPTITVVTSVTSNLDSHEPGSPSQTTLTNLF
Protein: RNA binding motif protein 25 (E9PQU5)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MSFPPHLNRPPMGIPALPPGIPPPQFPGFPPPVPPGTPMIPVPMSIMAPAPTVLVPTVSMVGKHLGARKDHPGLKAKENDENCGPTTTVFVGNISEKASDMLIRQLLAKCGLVLSWKRVQGASGKLQAFGFCEYKEPESTLRALRLLHDLQIGEKKLLVKVDAKTKAQLDEWKAKKKASNGNARPETVTNDDEEALDEETKRRDQMIKGAIEVLIREYSSELNAPSQESDSHPRKKKKEKKED
Protein: Ankyrin 1 (A0A8I5ZJ94)
Organism: Rattus norvegicus (Rat)
Subcellular location: Cytoplasm, cytoskeleton {ECO:0000256|ARBA:ARBA00004245}. Membrane {ECO:0000256|ARBA:ARBA00004370}.
Interaction partners:
Sequence:
MAQAAKQLKKIKDIEAQALQEQKEKEESNRKRRNRSRDRKKKADAATSFLRAARSGNLDKALDHLRNGVDINTCNQNGLNGLHLASKEGHVKMVVELLHKEIILETTTKKGNTALHIAALAGQDEVVRELVNYGANVNAQSQKGFTPLYMAAQENHLEVVKFLLENGANQNVATEDGFTPLAVALQQGHENVVAHLINYGTKGKVRLPALHIAARNDDTRTAAVLLQNDPNPDVLSKTGFTPLHIAAHYENLNVAQLLLNRGASVNFTPQNGITPLHIASRRGNVIMVRLLLDRGAQIETRTKDELTPLHCAARNGHVRISEILLDHGAPIQAKTKNGLSPIHMAAQGDHLDCVRLLLQYNAEIDDITLDHLTPLHVAAHCGHHRVAKVLLDKGAKPNSRALNGFTPLHIACKKNHIRVMELLLKTGASIDAVTESGLTPLHVASFMGHLPIVKNLLQRGASPNVSNVKVETPLHMAARAGHTEVAKYLLQNKAKANAKAKDDQTPLHCAARIGHTSMVKLLLENDASPNLATTAGHTPLHTAAREGHVDTALALLEKEASQACMTKKGFTPLHVAAKYGKVRLAELLLEHDAHPNAAGKNGLTPLHVAVHHNNLDIVQLLLPRGGSPHSPAWNGYTPLHIAAKQNQIEVARSLLQYGGSANAESVQGVTPLHLAAQEGHTEMVALLLSKQANGNLGNKSGLTPLHLVAQEGHVPVADVLIKHGVTVDATTRMGYTPLHVASHYGNIKLVKFLLQHQADVNAKTKLGYSPLHQAAQQGHTDIVTLLLKNGASPNEVSSNGTTPLAIAKRLGYISVTDVLKVVTDETSVVLVSDKHRMSYPETVDEILDVSEDEGTAHISLTGDELVGSKAERRDSRDVGEEKELLDFVPKLDQVVESPAIPRIPCVTPETVVIRSEDQEQASKEYDEDSLIPSSPATETSDNISPVASPVHTGFLVSFMVDARGGSMRGSRHNGLRVVIPPRTCAAPTRITCRLVKPQKLSTPPPLAEEEGLASRIIALGPTGAQFLSPVIVEIPHFASHGRGDRELVVLRSENGSVWKEHKSRYGESYLDQILNGMDEELGSLEELEKKRVCRIITTDFPLYFVIMSRLCQDYDTIGPEGGSLRSKLVPLVQATFPENAVTKKVKLALQAQPVPDELVTKLLGNQATFSPIVTVEPRRRKFHRPIGLRIPLPPSWTDNPRDSGEGDTTSLRLLCSVIGGTDQAQWEDITGTTKLVYANECANFTTNVSARFWLSDCPRTAEAVHFATLLYKELTAVPYMAKFVIFAKMNDPREGRLRCYCMTDDKVDKTLEQHENFVEVARSRDIEVLEGMPLFAELSGNLVPVKKAAQQRSFHFQSFRENRLAIPVKVRDSSREPGGFLSFLRKPMKYEDAQHILCHLNVTMPPCTKGSGAEDRRRTLTPLTLRYSILSESRLGFTSDTDRVEMKMAVIREHLGLSWAELARELQFSVEDINRIRVENPNSLLDQSTALLTLWVDREGENAKMENLYTALRNIDRSEIVNMLEGSGRQSRNLKPDRRHGDREYSLSPSQVNGYSSLQDELLSPASLHYALPSPLCADQYWNEVAVIDAIPLAATEHDTMLEMSDMQVWSSGLTPSLVTAEDSSLECSKAEDSDAIPEWKLEGAHSEDTQGPELGSQDLVEDDTVDSDATNGLADLLGQEEGQRSEKKSQEVSGTEQDTETEVSLVSGQQRVHARITDSPSVRQVLDRSQARTVDWYKQGSAASYPQEAAQSSWQEEVTQGPQSFQRRITTIQGPEPGTLQEYEQVVVSTREHVQRGPPESDSPKAGKDPSLWASESAFSQEVQGDELQNIPGEQVTEEQFTDEQGNIVTKKIIRKVVRQVDSSGAIDTQQHEEVELRGSGLQPDLIEGRKGAQIVKRASLKRGKQ
Protein: Maleylpyruvate isomerase (MPI) (EC 5.2.1.4) (Naphthalene degradation protein L) (O86043)
Organism: Ralstonia sp
Function: Catalyzes the GSH-dependent isomerization of maleylpyruvate to fumarylpyruvate which is subsequently processed by NagK to form pyruvate and fumarate.
Interaction partners:
Sequence:
MKLYNFWRSGTSHRLRIALNLKGVPYEYLAVHLGKEEHLKDAFKALNPQQLVPALDTGAQVLIQSPAIIEWLEEQYPTPALLPADADGRQRVRALAAIVGCDIHPINNRRILEYLRKTFGADEAAINAWCGTWISAGFDAYEALLAVDPKRGRYSFGDTPTLADCYLVPQVESARRFQVDLTPYPLIRAVDAACGELDAFRRAAPAAQPDSA
Protein: Extracellular signal-regulated kinase 2 (ERK2) (EC 2.7.11.24) (Defective in aggregation protein C) (MAP kinase 2) (Q54QB1)
Organism: Dictyostelium discoideum (Social amoeba)
Function: Implicated in the relay of the cAMP chemotactic signal and cell differentiation. Important for receptor-mediated activation of adenylyl cyclase.
Interaction partners:
- Gelation factor
- Ras-like protein rasD
- 3',5'-cyclic-nucleotide phosphodiesterase regA
- Gelsolin-related protein of 125 kDa
- Cyclic AMP receptor 1
- Dual specificity mitogen-activated protein kinase kinase 1
Sequence:
MSSEDIDKHVLRKYEVLQKIGKGAYGIVWKAIDKKTKQTVALKKIFDAFQNATDAQRTFREIMFLQELHGHENIIKLLNVIKADNDRDIYLVFEHMETDLHAVIRAKILEEIHKQYTIYQLLKALKYMHSANVLHRDIKPSNLLLNSECLVKVADFGLARSITSLESIAEANPVLTEYVATRWYRAPEILLGSTKYTKGVDMWSIGCILGELLGEKAMFPGNSTMNQLDLIIEVTGRPSAEDIEAIKSPFAGTMLESLPPSNPRSLSDMYPSASVDALDLLKKLLQFNPDKRITAEEALAHPFVTQFHNPAEEPHFDRIIKISIDDGQKFPIAEYRNRLYNDIIKKKKEERKKQTNPTKPDTTAPTLST
Protein: Protein deacetylase HDAC6 (EC 3.5.1.-) (E3 ubiquitin-protein ligase HDAC6) (EC 2.3.2.-) (Tubulin-lysine deacetylase HDAC6) (EC 3.5.1.-) (A0A8I6GM68)
Organism: Rattus norvegicus (Rat)
Subcellular location: Cytoplasm {ECO:0000250|UniProtKB:Q9UBN7}. Cytoplasm, cytoskeleton {ECO:0000250|UniProtKB:Q9UBN7}. Nucleus {ECO:0000250|UniProtKB:Q9UBN7}. Perikaryon {ECO:0000250|UniProtKB:Q9Z2V5}. Cell projection, dendrite {ECO:0000250|UniProtKB:Q9Z2V5}. Cell projection, axon {ECO:0000250|UniProtKB:Q9Z2V5}. Cell projection, cilium {ECO:0000250|UniProtKB:Q9UBN7}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000250|UniProtKB:Q9UBN7}. Cytoplasm, cytoskeleton, cilium basal body {ECO:0000250|UniProtKB:Q9UBN7}. Note=Mainly cytoplasmic where it is associated with microtubules (By similarity). Can shuttle between the cytoplasm and the nucleus. Found exclusively in the cytoplasm in proliferative cells with a fraction found in the nucleus during differentiation (By similarity). May translocate to the nucleus following DNA damage (By similarity). {ECO:0000250|UniProtKB:Q9UBN7, ECO:0000250|UniProtKB:Q9Z2V5}.
Interaction partners:
Sequence:
MTSTGQDSSTRQRKSRHNPQSPLQDSSATLKRGGKKGAVPHSSPNLAEVKKKGKMKKLSQPAEEDLIVGLQGLDLNSETRVPVGTGLVFDEQLNDFHCLWDDSFPENPERLHAIKEQLILEGLLGRCVSFQARFAEKEELMLVHSLEYIDLMETTQYMNEGELRVLAGTYDSVYLHPNSYSCACLATGSVLRLVDAVMGAEIRNGMAVIRPPGHHAQRSLMDGYCMFNHLAVAARYAQKKHRIQRILIVDWDVHHGQGTQFIFDQDPSVLYFSIHRYEHGRFWPHLKASNWSTTGFGQGQGYTINVPWNQVSFCSHKLSLACFPRGSREMTDYYIAFLCLQVGMRDADYIAAFLHILLPVAFEFQPQLVLVAAGFDALHGDPKGEMSATPAGFAHLTHFLMGLAGGKLILSLEGGYNLHALAKGVSGSLHTLLGDPCPMLESPVAPCASAQTSISCTLEALEPFWEVLERSVEPQDEDEVEGDMLEDEEEEGHWEATALPMDTWPLLQNRTGLVYDERMMSHCNLWDNHHPETPQRILRIMCHLEEVGLAARCLILPARPALDSELLTCHSAEYVERLRATEKMKTRDLHREGANFESIYICPSTFACAQLATGAACRLVEAVLSGEVLNGIAIVRPPGHHAEPDAACGFCFFNSVAVAARHAQVIAGRALRILIVDWDVHHGNGTQHIFEEDPSVLYVSLHRYDRGTFFPMGDEGASSQVGRAAGTGFTVNVPWNGPRMGDADYLATWHRLVLPIAYEFNPELVLISAGFDAAQGDPLGGCQVTPEGYAHLTHLLMGLAGGRIILILEGGYNLTSISESMAACTHSLLGDPPPQLTSLRPPQSGALASISEVIQVHRKYWRSLRLMKMEDKEERSSSRLVIKKLPQSASPVSAKGMTTPKGKVLEAGMRKPTAALPTKESTLGQAKAKTAKALLAQGQSSEQAAKGTTLDLATSKDTVGGATTDQCASVAATENSANQTTSGEEASGETESFGTSPSSNASKQTTGASPLHGAAAQQSPELGLSSTLELSSEAQEVQESEEGLLGEAAGGQDMNSLMLTQGFGDFNTQDVFYAVTPLSWCPHLMAVCPIPAAGLDVSQPCKTCGSVQENWVCLTCYQVYCSRYVNAHMVCHHEASEHPLVLSCVDLSTWCYLCQAYVHHEDLQDVKNAAHQNKFGEGMPHLQ
Protein: Cytochrome bd-I ubiquinol oxidase subunit X (EC 7.1.1.7) (Cytochrome bd-I oxidase subunit X) (Cytochrome d ubiquinol oxidase subunit X) (P56100)
Organism: Escherichia coli (strain K12)
Function: Required for correct functioning of cytochrome bd-I oxidase. This protein and AppX may have some functional overlap.
Subcellular location: Cell inner membrane {ECO:0000305}; Single-pass membrane protein {ECO:0000305}. Note=In sucrose cushions fractionates with both the inner and outer membranes. {ECO:0000269|PubMed:19121005, ECO:0000269|PubMed:21778229}.
Interaction partners:
- Cytochrome bd-I ubiquinol oxidase subunit 2
- Cytochrome bd-I ubiquinol oxidase subunit 1
- Uncharacterized protein YnhF
- Putative cytochrome bd-II ubiquinol oxidase subunit AppX
- Cytochrome bd-II ubiquinol oxidase subunit 2
- Cytochrome bd-II ubiquinol oxidase subunit 1
- Multidrug efflux pump accessory protein AcrZ
- Uncharacterized protein YbgE
- Small protein MntS
- Cytochrome bo
Sequence:
MWYFAWILGTLLACSFGVITALALEHVESGKAGQEDI
Protein: RIC3 acetylcholine receptor chaperone, isoform V (A0A0B4LH23)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Endoplasmic reticulum membrane {ECO:0000256|ARBA:ARBA00004586}.
Interaction partners:
Sequence:
MPATATSKPRAPLVEEGMTPKKTALIIVTVIGCIAILWPKVFHPMMFGGVPPSQPNFKDPRAAPGGCCDVVLDREQFLNATKKDTVEPFGPHLYRKQINVYTGEISLRQERPAHLHPESIYQAMRERGRAIPATPTVPILERKTSPSNPPPRIVDGRPGPIPGMRPPMGAGALHQPQQRGSSMGFLMPLYTIGIVVFFGYTLMKIMFKKQVPNDPYGAAPPNPAFRQEVFGSQNHSQVEDLGGSKLGAATATAAAKKPAAKDTEKELYNASVSATEVASSLSASLKSHQQLKEAEQLMEIEKLRQKLESTERAMAQLVAEMNTDQYEAKLLRPYKV
Protein: F-BAR domain-containing protein (G5EF80)
Organism: Caenorhabditis elegans
Interaction partners:
- Rho-GAP domain-containing protein
- small monomeric GTPase
- Ras-like GTP-binding protein rhoA
- Cdc-42 Related Protein
- Rho-GAP domain-containing protein
- Cell division control protein 42 homolog
- Poly
- Ras-related protein Rap-1
Sequence:
MSSTSSICSSNDADFIVDTRIPASIRRDIDRFSVFINRLRSTLDLNSSVVDGESMCVNVHASLEMVSESMRDLFKYSQFKTNPIILLSLQLVQAVKDLKFDTCSVDTTPVLNIIDQLESAVLNIILNRHIVSSVHHTPSRSSTLGRWKQNNSTDSYLRQSGPLNSVSQTLQRRHSTHQTNPDPNDQSTEKVMEIDKLLISRTDGVDVAFERTKAWSTYSKDVISYVRARIQLEQDHARKVHTLVDTSRRDINKPFMPLREIFENSFDTEVEMVTHTKETTEHLKDRVVEALDARRKEHDTVRNALKVEWTKATKSLHDCEESYEKSKITLRMREEALKKARESCLRTESSPPEREASRRRRDLEKKSRAVEEAMIKKEEAERQVVSITAELRKKRRDIDKTKESVVERLRELIFQCEQTTKACTVHYFTSLAALWARLPGAFHELSNATRDYQPGTEYMAFLQTLPTRAASSSSLVRSDRSIDEGVASCDGSSSLTSLRRNAINPDDEGALPDTKRHKKTSYAGRTFDNHEISTAAQSHHIQRTVQPSKCSACDTLSILYTVQCIDCGGQWHKACFPRIQQVCGQAAKLVDRRTSIFGVPLKGLLEHQNRHIPLIIEKSIDQLQRRGLRAKGIYRTCGVKSKIEEICNAFERSSSDDEVCLDNENPMNLASVVKLYLRKLPEPLLTFELYDDFVRLGTECCSAQASGSNCEEERVEQLRQLARKLPVHNYETLKFIMLHLNRVSWFHEVNLMSTSNLSTVIAPSLIWMSPKRIDHTSAIMHTQYTNKAIEVMIRNSYHIFGMDRQADWQSFFSRYSVEEPPKEEEEEDCGNESDIEDDIEDLDEQDRSDEDDDEEIFLPPTPDILKTTRKPVEQTTSLPNPKLPVERISSGRRSNNNEPPTIVQRRTNDISRRSDMGDKRKSYTTSIVIAPRDGSPDHVDQIQIIERDVYDKGASLEQDKVESTRL
Protein: Uncharacterized protein, isoform Q (M9PC30)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MVAQWKIINENYKNLEGYKRVAWPPASEERIIREFTPQPQTQSPAPGAGGYYPQAHAPTAAAAAPPQQQYGAPSYDGQQPGAQWQQQQQQQQVPQQQYQPQSQAQAPYQPPQWNQPQQQQQQPSYQASPYQQQQQQQPSYYPQQNGGSTYAQPPYNSYSQPQLPYSQDQTDLQQQQQQQQQQYPGAYAGQDSYRGASPGIITLRKEAPVSQKPAPVYTSQPAAVSYQGGSKLRGDLKWPPPEYKEAAARENEERRQLALGPVCRPRRVNRDYTPFFAKHQLNNGYPSYKVPPGTQHIFG