wanglab/gogpt-training-data huggingface dataset:
Protein: Splicing factor YJU2 (Coiled-coil domain-containing protein 94) (Q9BW85)
Organism: Homo sapiens (Human)
Function: Part of the spliceosome which catalyzes two sequential transesterification reactions, first the excision of the non-coding intron from pre-mRNA and then the ligation of the coding exons to form the mature mRNA. Plays a role in stabilizing the structure of the spliceosome catalytic core and docking of the branch helix into the active site, producing 5'-exon and lariat intron-3'-intermediates (By similarity). May protect cells from TP53-dependent apoptosis upon dsDNA break damage through association with PRP19-CD5L complex.
Subcellular location: Nucleus {ECO:0000255|HAMAP-Rule:MF_03226, ECO:0000269|PubMed:29301961}.
Interaction partners:
- U5 small nuclear ribonucleoprotein 200 kDa helicase
- Pre-mRNA-splicing factor CWC22 homolog
- Pre-mRNA-processing-splicing factor 8
- Pre-mRNA-splicing factor SYF1
- Cell division cycle 5-like protein
- Pleiotropic regulator 1
- Pre-mRNA-splicing factor CWC25 homolog
- Pre-mRNA-processing factor 19
- Pre-mRNA-splicing factor ISY1 homolog
- Pre-mRNA-splicing factor ISY1 homolog
Sequence:
MSERKVLNKYYPPDFDPSKIPKLKLPKDRQYVVRLMAPFNMRCKTCGEYIYKGKKFNARKETVQNEVYLGLPIFRFYIKCTRCLAEITFKTDPENTDYTMEHGATRNFQAEKLLEEEEKRVQKEREDEELNNPMKVLENRTKDSKLEMEVLENLQELKDLNQRQAHVDFEAMLRQHRLSEEERRRQQQEEDEQETAALLEEARKRRLLEDSDSEDEAAPSPLQPALRPNPTAILDEAPKPKRKVEVWEQSVGSLGSRPPLSRLVVVKKAKADPDCSNGQPQAAPTPGAPQNRKEANPTPLTPGASSLSQLGAYLDSDDSNGSN
Protein: MITF (Mitf, isoform B) (RE45331p) (Q6WSQ9)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
MTESGIDLGFDMEFDLNINLLNDNDNMDFLPNVTENMEFYELKSSSRCIRHNEIPTFKTATPTSRTQLKLQLQREQQQQMMIQQQTLDTAMDPKMHLLFGSGQGLMESEFIDSGSTSACGSGSSSLEQMSQLVQMDNLIDSSSGAKLKVPLQSIGVDVPPQVLQVSTVLENPTRYHVIQKQKNQVRQYLSESFKPSMWGSHTSEIKLANNSASTGNLQNSSLQKGICDPLERTNRFGCDSAVSAKRIMPSDDAMPISPFGGSFVRCDDINPIEPTVLRPNSHGAGEPENAHRTAQLGLSKANSSLSSTRSSSGIVNSIRISSTSSSLQSTSAPISPSVSSVATSVSELPSFDSDPDDIFDDILQNDSFNFDKNFNSELSIKQEPQNLTDAEMNALAKDRQKKDNHNMIERRRRFNINDRIKELGTLLPKGSDAFYEVVRDIRPNKGTILKSSVDYIKCLKHEVTRLRQNELRQRQVELQNRKLMSRIKELEMQAKSHGILLSENHLTSLSAPTQPYLKSFSLSPTASRSRRSLFDQPVEKKIQVIDGADGNMGMNQVDEFMEDCKYAVQGGDPMLSSHSHMQSAPQSPSSKTLNSGSFEPKNFSEADESLFRGKSSLASDDCCGINCSTSCYIQHQLTSREGHPNHSHHTGIREIHSLSDSAQNSEFSRLEHCDDPLLSSSHRSLGTVDEDQHNSVDMSAVMVHDSLSSLVDDNNSETMVLASDTLDIEL
Protein: E3 ubiquitin-protein ligase UHRF (EC 2.3.2.27) (RING-type E3 ubiquitin transferase UHRF) (Ubiquitin-like PHD and RING finger domain-containing protein) (Ubiquitin-like-containing PHD and RING finger domains protein) (A0A087WVR3)
Organism: Homo sapiens (Human)
Subcellular location: Nucleus {ECO:0000256|PROSITE-ProRule:PRU00358, ECO:0000256|RuleBase:RU369101}.
Interaction partners:
Sequence:
MGVFAVPPLSADTMWIQVRTMDGRQTHTVDSLSRLTKVEELRRKIQELFHVEPGLQRLFYRGKQMEDGHTLFDYEVRLNDTIQLLVRQSLVLPHSTKERDSELSDTDSGCCLGQSESDKSSTHGEAAAETDSRPADEDMWDETELGLYKVNEYVDARDTNMGAWFEAQVVRVTRKAPSRDEPCSSTSRPALEEDVIYHVKYDDYPENGVVQMNSRDVRARARTIIKWQDLEVGQVVMLNYNPDNPKERGFWYDAEISRKRETRTARELYANVVLGDDSLNDCRIIFVDEVFKIERPGEGSPMVDNPMRRKSGPSCKHCKDDVNRLCRVCACHLCGGRQDPDKQLMCDECDMAFHIYCLDPPLSSVPSEDEWYCPECRNDASEVVLAGERLRESKKKAKMASATSSSQRDWGKGMACVGRTKECTIVPSNHYGPIPGIPVGTMWRFRVQVSESGVHRPHVAGIHGRSNDGAYSLVLAGGYEDDVDHGNFFTYTGSGGRDLSGNKRTAEQSCDQKLTNTNRALALNCFAPINDQEGAEAKDWRSGKPVRVVRNVKGGKNSKYAPAEGNRYDGIYKVVKYWPEKGKSGFLVWRYLLRRDDDEPGPWTKEGKDRIKKLGLTMQYPEGYLEALANREREKENSKREEEEQQEGGFASPRTGKGKWKRKSAGGGPSRAGSPRRTSKKTKVEPYSLTAQQSSLIREDKSNAKLWNEVLASLKDRPASGSPFQLFLSKVEETFQCICCQELVFRPITTVCQHNVCKDCLDRSFRAQVFSCPACRYDLGRSYAMQVNQPLQTVLNQLFPGYGNGR
Protein: Vacuolar protein sorting-associated protein 55 (Q9UUH1)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Involved in protein transport from endosomes to the vacuole.
Subcellular location: Endosome membrane {ECO:0000269|PubMed:16823372}; Multi-pass membrane protein {ECO:0000269|PubMed:16823372}. Golgi apparatus membrane {ECO:0000269|PubMed:16823372}; Multi-pass membrane protein {ECO:0000269|PubMed:16823372}.
Interaction partners:
- UPF0220 protein C8D2.02c
- Protein bem46
- UDP-galactose transporter homolog 1
- Vacuolar protein sorting/targeting protein 10
- V-type proton ATPase subunit a
Sequence:
MSDLRKIIGLSSVLAVGFMLVILSCALFKNWYPLLIVIPFILAPLPNLLTKKYSTSHDFLQEEDRNLLDFGRFTFGATICTGFALPIVFVNVGLIGTAAATMSCVGGSIIFLVITLYSQAFVQHEEEF
Protein: Expressed protein (Transmembrane protein, putative (DUF1068)) (O80895)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
- Uncharacterized protein At3g06530
- rRNA biogenesis protein RRP5
- Nucleolar-like protein
- Protein SLOW WALKER 1
- KRR1 small subunit processome component
- Nucleolar protein
- F18K10.11 protein
- Putative WD-repeat membrane protein
- Probable U3 small nucleolar RNA-associated protein 11
- Protein NUCLEOLAR COMPLEX ASSOCIATED 4
Sequence:
MAKHTAALKVGLALLALSMIGYILGPPLYWHLTEALAVSATSCSACVCDCSSLPLLTIPTGLSNGSFTDCAKRDPEVNEDTEKNYAELLTEELKQREAASMEKHKRVDTGLLEAKKITSSYQKEADKCNSGMETCEEAREKAEKALVEQKKLTSMWEQRARQKGYKDGATKSTVKSKSGTEVA
Protein: Catalase isozyme 1 (EC 1.11.1.6) (P18122)
Organism: Zea mays (Maize)
Function: Occurs in almost all aerobically respiring organisms and serves to protect cells from the toxic effects of hydrogen peroxide.
Subcellular location: Peroxisome.
Interaction partners:
- Peroxisome biogenesis protein 5
- Peroxisome biogenesis protein 5
- Trehalase
- 1-Cys peroxiredoxin PER1
- Acyl-coenzyme A oxidase
- Acyl-coenzyme A oxidase
- 2-Cys peroxiredoxin BAS1, chloroplastic
- 2-Cys peroxiredoxin BAS1, chloroplastic
- Peroxiredoxin
Sequence:
MDPYKHRPSSGSNSSFWTTNSGAPVWNNNSALTVGQRGPILLEDYHLIEKLAQFDRERIPERVVHARGASAKGFFEVTHDVSHLTCADFLRAPGVQTPVIVRFSTVVHERGSPETLRDPRGFAVKFYTREGNFDLVGNNMPVFFIRDGMKFPDMVHAFKPNPKTNLQENWRIVDFFSHHPESLHMFTFLFDDVGIPLNYRHMEGFGVNTYSLINRDGKPHLVKFHWKPTCGVKCLLDNEAVTVGGTCHSHATKDLYDSIAAGNYPEWKLYIQTIDLDHEDKFDFDPLDVTKTWPEDIIPLQPVGRMVLNKNVDNFFAENEQIAFCPAISVPAIHYSDDKLLQTRIFSYADTQRHRLGPNYLMLPVNAPKCAHHNNHHDGFMNFMHRDEEVNYFPSRFDPARHAEKVPIPPRVLTRCREKCIIQKENNFKQAGERYRSFDPARQDRFIQRWVDALTHPRVTHEHRTIWISYWSQCDAALGQKLPSRLNLKPSM
Protein: C2H2-type domain-containing protein (Q9N360)
Organism: Caenorhabditis elegans
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
- H/ACA ribonucleoprotein complex non-core subunit NAF1
- Gustatory receptor
- Major facilitator superfamily
- ADP-ribosylation factor-related protein 1
- Major facilitator superfamily
- Major facilitator superfamily
- Cytochrome P450
- Nuclear transcription factor Y subunit nfyb-1
Sequence:
MTLDYHQPTTTNTTLPDDIHMKDPEEEEFEEYEDELLEEEEEFDEELEELENSDSASSLVSAGSPHGSSSSNGSHGSSPPLQVQSPSQGSGSSGSPTGQPEKRHICTVCGKGFSYFSILESHKRSHTGEKPYNCHFCQKTFAQKATLQVHERTHTGERPYKCRYCEKTFAQYGTKTVHEKSAHLGIRNYKCPKCDKLLSSPSALYTHKKTHGDKTFRCDFCPKTFALKNYLKLHVKQVHEQNERKHVCVYCNKGFAYAGSLQVHVRTHTGERPYVCKFCPKAFASQGNLQSHERTHTGERPYSCQFCQRTFIQKSQLTAHESTHLTQKHSVNPDSTTADILPVAGSVTDHQMVGNYECTFCNKKYPYASSLYIHMRKHTEKSAYSCDGCGKPYSQKISLNIHQDQCEAFKNRLKTTDSQFSHNCDGCGKSFVQRIALQIHVDSCEPHKNLARLKLSQQQNQNQNSDSESDTEMKICPLPNPPLTLAPTHQQIPPPVNIYAQQPPPNPLGSILGNTSLTPQTLNFGLPSLSSASFSSLNAHAPFTPVELPNSADFGPLTASKPHAVPFHPSEMCLSAFRKVPESSSISGLGSLSTSILSTQLLLQLQHTPDFNYLLNQNLLSSLAGLSGLSATLGPQLQATTPTSANQQPFLMAAPSAVQPLV
Protein: Mitochondrial inner membrane i-AAA protease supercomplex subunit YME1 (EC 3.4.24.-) (Protein OSD1) (Tat-binding homolog 11) (Yeast mitochondrial escape protein 1) (P32795)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Catalytic subunit of the mitochondrial inner membrane i-AAA protease supercomplex required for mitochondrial inner membrane protein turnover. The protease is probably ATP-dependent. Important to maintain the integrity of the mitochondrial compartment. Required both for the degradation of unassembled subunit 2 of cytochrome c oxidase (COX2) and for efficient assembly of mitochondrial respiratory chain. Binds unfolded substrates in an ATPase-independent manner; binding of folded COX2, a physiological substrate, requires an active ATPase but when COX2 is destabilized an active ATPase is no longer necessary.
Subcellular location: Mitochondrion inner membrane {ECO:0000269|PubMed:14562095, ECO:0000269|PubMed:8355690, ECO:0000269|PubMed:8688560}; Peripheral membrane protein {ECO:0000269|PubMed:14562095, ECO:0000269|PubMed:8355690, ECO:0000269|PubMed:8688560}; Matrix side {ECO:0000269|PubMed:14562095, ECO:0000269|PubMed:8355690, ECO:0000269|PubMed:8688560}. Note=Although this protein does not have any predicted transmembrane helices it behaves like an integral membrane protein.
Interaction partners:
- Mitochondrial escape protein 2
- Mitochondrial inner membrane i-AAA protease supercomplex subunit MGR1
- Autophagy-related protein 32
- Mitochondrial inner membrane i-AAA protease supercomplex subunit MGR3
- Mitochondrial metalloendopeptidase OMA1
- Prohibitin-2
- Prohibitin-1
- Lon protease homolog, mitochondrial
- Mitochondrial import inner membrane translocase subunit TIM10
- Mitochondrial import inner membrane translocase subunit TIM9
Sequence:
MNVSKILVSPTVTTNVLRIFAPRLPQIGASLLVQKKWALRSKKFYRFYSEKNSGEMPPKKEADSSGKASNKSTISSIDNSQPPPPSNTNDKTKQANVAVSHAMLATREQEANKDLTSPDAQAAFYKLLLQSNYPQYVVSRFETPGIASSPECMELYMEALQRIGRHSEADAVRQNLLTASSAGAVNPSLASSSSNQSGYHGNFPSMYSPLYGSRKEPLHVVVSESTFTVVSRWVKWLLVFGILTYSFSEGFKYITENTTLLKSSEVADKSVDVAKTNVKFDDVCGCDEARAELEEIVDFLKDPTKYESLGGKLPKGVLLTGPPGTGKTLLARATAGEAGVDFFFMSGSEFDEVYVGVGAKRIRDLFAQARSRAPAIIFIDELDAIGGKRNPKDQAYAKQTLNQLLVELDGFSQTSGIIIIGATNFPEALDKALTRPGRFDKVVNVDLPDVRGRADILKHHMKKITLADNVDPTIIARGTPGLSGAELANLVNQAAVYACQKNAVSVDMSHFEWAKDKILMGAERKTMVLTDAARKATAFHEAGHAIMAKYTNGATPLYKATILPRGRALGITFQLPEMDKVDITKRECQARLDVCMGGKIAEELIYGKDNTTSGCGSDLQSATGTARAMVTQYGMSDDVGPVNLSENWESWSNKIRDIADNEVIELLKDSEERARRLLTKKNVELHRLAQGLIEYETLDAHEIEQVCKGEKLDKLKTSTNTVVEGPDSDERKDIGDDKPKIPTMLNA
Protein: Catenin (cadherin-associated protein), delta 2b (Catenin delta-2b isoform 2) (B0V2S9)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Subcellular location: Cell junction {ECO:0000256|ARBA:ARBA00004282}.
Interaction partners:
- Transcription factor 7-like 2
- Catenin
- Lymphoid enhancer-binding factor 1
- Transcription factor 7-like 1-A
- Transcription factor 7.
Sequence:
MPVPDQPSGTENSSMLSPVLNASNGDGSETETTSAILASVKEQELQFERLTRELEAERQIVATQLERCKLGSETGSMSSISSADEKFRWNNQDGQKDIEEELTTGLELVDSCIRSLQESGILDSQEFTAGERPGILSQSALQLNNQEGTFPYPVSYHSNQTLALGDLSASQPPRSGQVGGALHSYNQVTSNRVAQLAARETAARAHSRDSYAQSHGSAFHMPDDQPTVPVNYSCATLPAQRVSSPFSMQALGSPSKLQRLGSASDMPSYATLARVSSPKQSPSRLAKSYSTSSPINMAAGGGSSSSPLHMAGAGNVSNSSPLHQLSAAVGSYATLSPTKRMLHTTDQYKISHDLYANATLQRPGSLAGSRGSYSSQHSHLGSELRPLQSPEHHIDPIYEDRVYQKAPLRNFNQAQDPMNQFCDQVLNFLLCPYSPVIAPSSPGVDSIPLQRTGSQNATGTFPRAGYATGPGASTADYANPYRTLQFCPSTDSPYSKSGPALPPEATLVRSPSVDSIQKDPREFGWRDPELPEVIQMLQHQFPSVQSNAAAYLQHLCFGDNKIKSEIRRQGGIQLLVDLLDHRMTDVHRSACGALRNLVYGKANDDNKIALKNCGGIPALVRLLRKTTDVEIRELLTGVLWNLSSCDALKMPIIQDALAVLTNTVIIPHSGWDTSPLQDDRKLHLHSSQVLRNATGCLRNVSSAGEEARRRMRECEGLTDALLYVIQTALGTSEIDSKTIENCVCILRNLSYRLAAETSQGQQMGSEELDGVLCTDASGKDAESSGCWGKKKKKKKSHDQWDGVGPFPDSSDPPKGLQMLWHPSIVKPYLTLLSECSNPDTLEGAAGALQNLAAGSWKVGPTLKPWSVYIRAAVRKEKGLPILVELLRIDNDRVVCAVATALRNMALDVRNKELIGKYAMRDLVHRLPGGNNNNSTGTGGSSKSMSDDTITAICCALHEVITKNMENTKALRDAGGIEKLIGIARSKGDKHTPKVVKAASQVLNSMWQYRDLRSLYKKDGYSQYHFVGSSSTIERDRQRPYSSSRTPSISPVRTSPNNRSASAPTSPREMMSLKERKTDYESTGSNSTYHGNKGEHTSRKDAMAAQISSGTSTLFRGAYMSPADDIKHNQVSAQGNPPEAYPPFQTPPGANFEEPYYEDQAHKRPPPAADGTMHLGLKSTGNYVDFYSASRPYSELNYETSHYPASPDSWV
Protein: DNA polymerase alpha subunit B (B0S687)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123, ECO:0000256|PIRNR:PIRNR018300}.
Interaction partners:
- DNA primase large subunit
- DNA primase
- DNA polymerase
- DNA polymerase epsilon catalytic subunit
- DNA polymerase.
- DNA replication licensing factor MCM4
- REV3-like, DNA directed polymerase zeta catalytic subunit.
- Proliferating cell nuclear antigen
- Polymerase
- Replication factor C
Sequence:
MASVTAEDIKSELDTFNIAFNNDTIDKMLEQCFCHRLTGEEIVFEWFAFSSTRKQLPLTLENLDQFEQEVLNKKKKPKSTSKGSQINKTRDINSIQELIRAEEEEENMLDSYSTPAKGSQKRALTTPEHPQSKRGVARLASPSLMLSPASFSPSATPSQKYGMRGGRGEVVSTFGAVQGPRWMGKGQTAVSVEMLDGGENSLISSYKYMFQRLRDVRDVLTGKIEELGEELRTNFNIEEFAPVSLPVQDSITVLGQVCCDSNGKLNAQSVLLEAGQEQGGRQVPVDLSELKEFSLFPGQVVVMEGMNPSGEKLVATKLYEGIPLPFYCPSEVKQEMDEVCEPVMVMIACGPYTPSESLTYDPLLDLITIINKDRPDVCILFGPFVDSKHEQIEKNQVTETFETIFKRCMDSIVEGTKGTACKLVFVPSQRDVHHHYIYPQPPFNLTISKEDTARVTLAPDPCTLLIGNVTFGLTSTDILFHMGAEEISSGTGTERFSRIMKHMLTQRSYYPLYPPAEEVNMDYDKFQQFSQMSLTPDILVAPSELRYFIKDVIGCVCVNPGRLTKGQIGGTYGRLLIQPNPALVEGKRVSPCIAGQVVKI
Protein: Aspartyl/asparaginyl beta-hydroxylase (EC 1.14.11.16) (Aspartate beta-hydroxylase) (ASP beta-hydroxylase) (Peptide-aspartate beta-dioxygenase) (Q12797)
Organism: Homo sapiens (Human)
Function: Specifically hydroxylates an Asp or Asn residue in certain epidermal growth factor-like (EGF) domains of a number of proteins.
Subcellular location: [Isoform 1]: Endoplasmic reticulum membrane; Single-pass type II membrane protein {ECO:0000250|UniProtKB:Q28056}.; SUBCELLULAR LOCATION: [Isoform 4]: Sarcoplasmic reticulum membrane; Single-pass type II membrane protein {ECO:0000305|PubMed:15485681}.; SUBCELLULAR LOCATION: [Isoform 8]: Endoplasmic reticulum membrane; Single-pass type II membrane protein {ECO:0000269|PubMed:22586105}.
Interaction partners:
- Triadin
- Calsequestrin-1
- Ryanodine receptor 2
- Calsequestrin-2
- Ryanodine receptor 1
- Peptidyl-prolyl cis-trans isomerase FKBP1B
- Coagulation factor X
- Ryanodine receptor 3
- Junctophilin-1
- Calmodulin-1
Sequence:
MAQRKNAKSSGNSSSSGSGSGSTSAGSSSPGARRETKHGGHKNGRKGGLSGTSFFTWFMVIALLGVWTSVAVVWFDLVDYEEVLGKLGIYDADGDGDFDVDDAKVLLGLKERSTSEPAVPPEEAEPHTEPEEQVPVEAEPQNIEDEAKEQIQSLLHEMVHAEHVEGEDLQQEDGPTGEPQQEDDEFLMATDVDDRFETLEPEVSHEETEHSYHVEETVSQDCNQDMEEMMSEQENPDSSEPVVEDERLHHDTDDVTYQVYEEQAVYEPLENEGIEITEVTAPPEDNPVEDSQVIVEEVSIFPVEEQQEVPPETNRKTDDPEQKAKVKKKKPKLLNKFDKTIKAELDAAEKLRKRGKIEEAVNAFKELVRKYPQSPRARYGKAQCEDDLAEKRRSNEVLRGAIETYQEVASLPDVPADLLKLSLKRRSDRQQFLGHMRGSLLTLQRLVQLFPNDTSLKNDLGVGYLLIGDNDNAKKVYEEVLSVTPNDGFAKVHYGFILKAQNKIAESIPYLKEGIESGDPGTDDGRFYFHLGDAMQRVGNKEAYKWYELGHKRGHFASVWQRSLYNVNGLKAQPWWTPKETGYTELVKSLERNWKLIRDEGLAVMDKAKGLFLPEDENLREKGDWSQFTLWQQGRRNENACKGAPKTCTLLEKFPETTGCRRGQIKYSIMHPGTHVWPHTGPTNCRLRMHLGLVIPKEGCKIRCANETKTWEEGKVLIFDDSFEHEVWQDASSFRLIFIVDVWHPELTPQQRRSLPAI
Protein: Complement C1q tumor necrosis factor-related protein 6 (Q6IR41)
Organism: Mus musculus (Mouse)
Subcellular location: Secreted {ECO:0000305}.
Interaction partners:
Sequence:
MRVIMGIASLGFLWAVFLLPLVFGVPTEETTFGESVASHLPKGCRRCCDPEDLMSSDDTVQAPVSPYVLPEVRPYINITILKGDKGDRGPTGTPGKPGKNGTRGDRGSQGVKGDKGQAGSPGSSCQTHYSAFSVGRKTGLHSSENFLSLLFDRVFVNTDGHFDMATGSFVAPLRGLYFFSLNVHSWNYKETYVHIVHNEQAVVILYAQPSERSIMQSQSVMLPLVPGDRVWVRLFKRERENGIYSDDVDTYITFSGHLIKAEDN
Protein: (-)-beta-pinene synthase 1, chloroplastic (EC 4.2.3.120) ((-)-alpha-pinene synthase (-)betapin1, chloroplastic) (EC 4.2.3.119) (Terpene synthase (-)betapin1) (PcTPS-(-)betapin1) (R9QMQ9)
Organism: Pinus contorta (Shore pine) (Lodgepole pine)
Function: Monoterpene synthase (TPS) involved in the biosynthesis of monoterpene natural products included in conifer oleoresin secretions and volatile emissions; these compounds contribute to biotic and abiotic stress defense against herbivores and pathogens. Catalyzes the conversion of (2E)-geranyl diphosphate (GPP) to (-)-beta-pinene and, to a lower extent, to (-)-alpha-pinene.
Subcellular location: Plastid, chloroplast {ECO:0000255}.
Interaction partners:
Sequence:
MDLISVLPSTSKSCVCLHKPLSSSTHKLKPFCRTIRILGMPRPRKSVLMASSMSMSVNTLVSDDDIQRRTGGYHSNLWNDDVIQFLSTPYGELAYRERGERLIDEVREIFSSMSLEDGEFSDLIQRLWMVDNVERLGIDRHFKNEIKSALDYVYSYWSEKGIGCGTKSIITNLNSTALGFRTLRLHGYPVSADVLKHFRNQIGQFVSCPSETEEDIRSIVNLYRASLIAFPGEKVMEEAERFSEKYLKETLQKIPDCSLSREIGDVLEHGWHTNLPRLEARNYIDVFGQDTKNMESNRKTEKLLELAKLEFNIFQSIQKTELESLLRWWNDSGSPQITFTRHRHVEYYTLASCIAFEPQHSGFRLGFAKACHIITVLDDMYDLFGTVDELKLFTAAIKRWDPSATDCLPQYMKGIYMMVYNTVNEMSAEAQKAQGRDTLNYARQAWEVYLDSYMQEAKWIATGYLPTFEEYLENGKVSSGHRVSALQPMLTMDIPFPPHILKEVDFPSNLNDLACAILRLRGDTRCYQEDRARGEETSCISCYMKDNPGATEEDALNHLNVMISGVIKGLNWELLKPDSGVPISSKKINFDITRAFHYGYKYRDGYSVSSVETKSLVMRTLLEPVPL
Protein: Chloride anion exchanger (Down-regulated in adenoma) (Protein DRA) (Solute carrier family 26 member 3) (P40879)
Organism: Homo sapiens (Human)
Function: Mediates chloride-bicarbonate exchange with a chloride bicarbonate stoichiometry of 2:1 in the intestinal epithelia. Plays a role in the chloride and bicarbonate homeostasis during sperm epididymal maturation and capacitation (By similarity).
Subcellular location: Apical cell membrane {ECO:0000269|PubMed:22159084}; Multi-pass membrane protein {ECO:0000255}. Membrane {ECO:0000250|UniProtKB:Q9WVC8}; Multi-pass membrane protein {ECO:0000255}. Cell membrane {ECO:0000269|PubMed:19321737, ECO:0000269|PubMed:22627094}; Multi-pass membrane protein {ECO:0000255}. Note=Localized in sperm membranes. Midpiece of sperm tail. Colocalizes with CFTR at the midpiece of sperm tail (By similarity). {ECO:0000250|UniProtKB:Q9WVC8}.
Interaction partners:
- Na
- Calmodulin-1
- Na
- Sodium/hydrogen exchanger 3
- Calmodulin-1
- Cystic fibrosis transmembrane conductance regulator
- Na
- Myelin basic protein
- Solute carrier family 13 member 1
- HLA class II histocompatibility antigen DQ alpha chain
Sequence:
MIEPFGNQYIVARPVYSTNAFEENHKKTGRHHKTFLDHLKVCCSCSPQKAKRIVLSLFPIASWLPAYRLKEWLLSDIVSGISTGIVAVLQGLAFALLVDIPPVYGLYASFFPAIIYLFFGTSRHISVGPFPILSMMVGLAVSGAVSKAVPDRNATTLGLPNNSNNSSLLDDERVRVAAAASVTVLSGIIQLAFGILRIGFVVIYLSESLISGFTTAAAVHVLVSQLKFIFQLTVPSHTDPVSIFKVLYSVFSQIEKTNIADLVTALIVLLVVSIVKEINQRFKDKLPVPIPIEFIMTVIAAGVSYGCDFKNRFKVAVVGDMNPGFQPPITPDVETFQNTVGDCFGIAMVAFAVAFSVASVYSLKYDYPLDGNQELIALGLGNIVCGVFRGFAGSTALSRSAVQESTGGKTQIAGLIGAIIVLIVVLAIGFLLAPLQKSVLAALALGNLKGMLMQFAEIGRLWRKDKYDCLIWIMTFIFTIVLGLGLGLAASVAFQLLTIVFRTQFPKCSTLANIGRTNIYKNKKDYYDMYEPEGVKIFRCPSPIYFANIGFFRRKLIDAVGFSPLRILRKRNKALRKIRKLQKQGLLQVTPKGFICTVDTIKDSDEELDNNQIEVLDQPINTTDLPFHIDWNDDLPLNIEVPKISLHSLILDFSAVSFLDVSSVRGLKSILQEFIRIKVDVYIVGTDDDFIEKLNRYEFFDGEVKSSIFFLTIHDAVLHILMKKDYSTSKFNPSQEKDGKIDFTINTNGGLRNRVYEVPVETKF
Protein: High mobility group protein 20A (HMG box-containing protein 20A) (HMG domain-containing protein 1) (HMG domain-containing protein HMGX1) (Q9NP66)
Organism: Homo sapiens (Human)
Function: Plays a role in neuronal differentiation as chromatin-associated protein. Acts as inhibitor of HMG20B. Overcomes the repressive effects of the neuronal silencer REST and induces the activation of neuronal-specific genes. Involved in the recruitment of the histone methyltransferase KMT2A/MLL1 and consequent increased methylation of histone H3 lysine 4 (By similarity).
Subcellular location: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00267}.
Interaction partners:
- Genetic suppressor element 1
- REST corepressor 1
- SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily E member 1-related
- REST corepressor 3
- Histone deacetylase 2
- PHD finger protein 21A
- PHD finger protein 14
- Lysine-specific histone demethylase 1A FAD-dependent demethylase 1A)
- Histone deacetylase 1
- Zinc finger protein SNAI1
Sequence:
MENLMTSSTLPPLFADEDGSKESNDLATTGLNHPEVPYSSGATSSTNNPEFVEDLSQGQLLQSESSNAAEGNEQRHEDEQRSKRGGWSKGRKRKKPLRDSNAPKSPLTGYVRFMNERREQLRAKRPEVPFPEITRMLGNEWSKLPPEEKQRYLDEADRDKERYMKELEQYQKTEAYKVFSRKTQDRQKGKSHRQDAARQATHDHEKETEVKERSVFDIPIFTEEFLNHSKAREAELRQLRKSNMEFEERNAALQKHVESMRTAVEKLEVDVIQERSRNTVLQQHLETLRQVLTSSFASMPLPGSGETPTVDTIDSYMNRLHSIILANPQDNENFIATVREVVNRLDR
Protein: Gibberellin 2-beta-dioxygenase 4 (EC 1.14.11.13) (GA 2-oxidase 4) (Gibberellin 2-beta-hydroxylase 4) (Gibberellin 2-oxidase 4) (Q9C7Z1)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Catalyzes the 2-beta-hydroxylation of several biologically active gibberellins, leading to the homeostatic regulation of their endogenous level. Catabolism of gibberellins (GAs) plays a central role in plant development. Converts GA9/GA20 to GA51/GA29 and GA4/GA1 to GA34/GA8.
Interaction partners:
- Gibberellin 3-beta-dioxygenase 4
- Gibberellin 3-beta-dioxygenase 2
- Gibberellin 3-beta-dioxygenase 1
- Ent-kaur-16-ene synthase, chloroplastic
- Gibberellin 20 oxidase 4
- Gibberellin 20 oxidase 1
- Gibberellin 20 oxidase 3
- Gibberellin 20 oxidase 2
- Gibberellin 3-beta-dioxygenase 3
- Gibberellin receptor GID1B
Sequence:
MVKGSQKIVAVDQDIPIIDMSQERSQVSMQIVKACESLGFFKVINHGVDQTTISRMEQESINFFAKPAHEKKSVRPVNQPFRYGFRDIGLNGDSGEVEYLLFHTNDPAFRSQLSFSSAVNCYIEAVKQLAREILDLTAEGLHVPPHSFSRLISSVDSDSVLRVNHYPPSDQFFGEANLSDQSVSLTRVGFGEHTDPQILTVLRSNGVGGLQVSNSDGMWVSVSPDPSAFCVNVGDLLQVMTNGRFISVRHRALTYGEESRLSTAYFAGPPLQAKIGPLSAMVMTMNQPRLYQTFTWGEYKKRAYSLRLEDSRLDMFRTCKD
Protein: Equilibrative nucleoside transporter 3 (rENT3) (Solute carrier family 29 member 3) (Q80WK7)
Organism: Rattus norvegicus (Rat)
Function: Mediates both influx and efflux of nucleosides across the membrane (equilibrative transporter). Mediates transport of adenine, adenosine and uridine (By similarity).
Subcellular location: Lysosome membrane {ECO:0000250|UniProtKB:Q9BZD2}; Multi-pass membrane protein {ECO:0000305}. Late endosome membrane {ECO:0000250|UniProtKB:Q9BZD2}; Multi-pass membrane protein {ECO:0000305}. Mitochondrion membrane {ECO:0000250|UniProtKB:Q9BZD2}; Multi-pass membrane protein {ECO:0000305}. Cell membrane {ECO:0000250|UniProtKB:Q9BZD2}; Multi-pass membrane protein {ECO:0000305}.
Interaction partners:
- Equilibrative nucleoside transporter 2
- Equilibrative nucleoside transporter 1
- Solute carrier family 28 member 3
- Sodium/nucleoside cotransporter 1
- Sodium/nucleoside cotransporter 2
Sequence:
MAFASEDIAYHSSNAVYRVPSNRHEADQEALLGKPLDYPAPGLQRPEDRFNGAYIIFFCLGIGGLLPWNFFVTAKEYWAFKLRNCSSPASGKDPEDADILNYFESYLAVASTVPSLLFLVANFLLVNRIRVHVRVLASLSVSLAIFVVMAVLVRVDTSSWTRGFFSIAMACMAIISSSSTIFNSSVYGLTGSFPMRNAQALISGGAMGGTVSAVASLVDLAASSDVRDSALAFFLTAAVFLGLCVGLYLLLPQLEYARYYMRPVVPIHVFSSEDSPPRDAPSTSSVAPASRAVHTPPLGPILKKTAGLGFCAVFLYFITALIFPAISTNIQPMHKGTGSPWTSKFYVPLTVFLLFNFADLCGRQVTAWIQVPGPRSKLLPILAVSRVCLVPLFLLCNYQPRSHLTLVLFQSDIYPILFTCLLGLSNGYLSTLVLMYGPKIVPRELAEATSVVMLFYMSLGLMLGSACAALLEHFI