wanglab/gogpt-training-data huggingface dataset:
Protein: Transcription factor MYB29 (Myb-related protein 29) (AtMYB29) (Protein HIGH ALIPHATIC GLUCOSINOLATE 3) (Protein PRODUCTION OF METHIONINE-DERIVED GLUCOSINOLATE 2) (Q9FLR1)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Plays a minor rheostat role in aliphatic glucosinolates (GLSs) biosynthesis, mostly short chained. Together with MYB28/HAG1 and MYB76/HAG2, promotes aliphatic glucosinolate biosynthesis but represses indolic glucosinolate biosynthesis. Prevents insect performance (e.g. lepidopteran insect Mamestra brassicae) by promoting glucosinolates.
Subcellular location: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00625}.
Interaction partners:
- Transcription factor MYC3
- Probable inactive 2-oxoglutarate-dependent dioxygenase AOP2
- Methylthioalkylmalate synthase 1, chloroplastic
- Cytochrome P450 83A1
- Dihomomethionine N-hydroxylase
- Methylthioalkylmalate synthase 3, chloroplastic
- Tryptophan N-monooxygenase 1
- Hexahomomethionine N-hydroxylase
- Transcription factor MYC4
- Tryptophan N-monooxygenase 2
Sequence:
MSRKPCCVGEGLKKGAWTAEEDKKLISYIHEHGEGGWRDIPQKAGLKRCGKSCRLRWANYLKPDIKRGEFSYEEEQIIIMLHASRGNKWSVIARHLPKRTDNEIKNYWNTHLKKLLIDKGIDPVTHKPLAYDSNPDEQSQSGSISPKSLPPSSSKNVPEITSSDETPKYDASLSSKKRCFKRSSSTSKLLNKVAARASSMGTILGASIEGTLISSTPLSSCLNDDFSETSQFQMEEFDPFYQSSEHIIDHMKEDISINNSEYDFSQFLEQFSNNEGEEADNTGGGYNQDLLMSDVSSTSVDEDEMMQNITGWSNYLLDHSDFNYDTSQDYDDKNFI
Protein: Protein ICE2 (Inheritance of cortical ER protein 2) (P40499)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Subcellular location: Endoplasmic reticulum membrane {ECO:0000269|PubMed:14562095}; Multi-pass membrane protein {ECO:0000269|PubMed:14562095}.
Interaction partners:
- CTP-dependent diacylglycerol kinase 1
- Vesicle-associated membrane protein-associated protein SCS2
- Protein SEY1
- Acyl-coenzyme A diphosphatase SCS3
- Increased sodium tolerance protein 2
- Tricalbin-1
- Phosphatidyl-N-methylethanolamine N-methyltransferase
Sequence:
MTSLSKSFMQSGRICAACFYLLFTLLSIPISFKVGGLECGLSFTVTLFTLYFITTTLNVLARRHGGRLYIFFTNCLYYSQHFIIASLLYLFLSGFSNDELGNVLKNKYNESESFLEALKNSLNSNQINYVLYYYYYRFVVQPWQFVLTKSTPFFTLSEGFFTILAIQAVGETNRWLSNDLNSNTWIISSLLTSGGVITASLYYLYRIYVTPIWPLSIQTASLLGLVLSMVCGLGLYGIVSQKGSVIESSLFFAYIVRCIYEISPKLATTATDEILNLFKDVWQKHQRNLPTADNLLCYFHNVILKNAEVLWGSFIPRGRKKTGDFHDKLISILSFEKVSLISKPFWKFFKNFTFSVPLSINEFCQVTIKMASESVSPAIVINLCFRVLMFYSATRIIPALQRKNDKQLRKSRRIMKGLYWYSPCILIAMYTHLILQYSGELKKDLCIWGCSEKWFGVDQPEIIVDSWGFWNWCNIFCTILVYATELIGSGS
Protein: POTE ankyrin domain family member B3 (A0JP26)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MVAEVCSMPAASAVKKPFDLRSKMGKWCHHRFPCCRGSGKSNMGTSGDHDDSFMKTLRSKMGKCCHHCFPCCRGSGTSNVGTSGDHDNSFMKTLRSKMGKWCCHCFPCCRGSGKSNVGTWGDYDDSAFMEPRYHVRREDLDKLHRAAWWGKVPRKDLIVMLRDTDMNKRDKQKRTALHLASANGNSEVVQLLLDRRCQLNVLDNKKRTALIKAVQCQEDECVLMLLEHGADGNIQDEYGNTALHYAIYNEDKLMAKALLLYGADIESKNKCGLTPLLLGVHEQKQQVVKFLIKKKANLNALDRYGRTALILAVCCGSASIVNLLLEQNVDVSSQDLSGQTAREYAVSSHHHVICELLSDYKEKQMLKISSENSNPEQDLKLTSEEESQRLKVSENSQPEKMSQEPEINKDCDREVEEEIKKHGSNPVGLPENLTNGASAGNGDDGLIPQRKSRKPENQQFPDTENEEYHSDEQNDTQKQLSEEQNTGISQDEILTNKQKQIEVAEKEMNSKLSLSHKKEEDLLRENSMLREEIAMLRLELDETKHQNQLRENKILEEIESVKEKLLKAIQLNEEALTKTSI
Protein: AT24316p (Q5U0U8)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
MCSIFRNRINYRGTGGTRSGSGERERDRDRDRDRDRDRERDRDTLLAKELDADSNNNGTEPQMEAEAVPESDTERETAEERGEEQEPENSNEALDLSLISSGGRESLPGSGHVSLEALQHTKVAVAQFAATAMAGNHQSADLAMVQSTIFNVQRQHLMQLQLIQHLQSQLKRAEAAALGRHSHSDEEEEEPEPEPEPKKQPTNGLKEELELEQGPESEQDQESRREENSKTDKRGTEDRKAEPEGYQSMMCDISSSLASSIITNHDPPPAPNEPNCLEMLQRRTEEVLDSASQSLHAAQMQEEYSEYASKEAQSRGEIFKHRCKYCGKIFGSYSALQIHLRSHTGERPFVCNVCGSKFTTKGNLKVHYQRHTQIFPPMLLPPGVAPNVGHSGQGQVQGEQYPIRLPFAPPVAHVGQEQHQNQVEEPEEIRQEIPVPQAEDLSKPMVKEKEKSHSPVERVKTPKEVKTDAALPSSEKPEKEISKPVVTSSRRNGSVRKRQTSAVSPPQEDRERDLVEHLHIAKLVRRSSASRESQPAEYSLAQMERIIDKSWEDLIEIDKTSETSKLQQLVDNIENKLTDPNQCIFCQKVMSCRSSLQMHIRTHTGERPFRCKICGRAFATKGNLKAHMSIHKIKPPMRSQFKCPVCHQKFSNGIILQQHIRIHTMDDGSGGQGAPAANPGEAERLGIEDQNSNKSLGTSDTLDFSTTISDHSGQRSESSQGGDFDEFMTMDSTDDSRDNSSAATATPHPLERERDREKERERRIPNDCSDERSHSNPDLTGGRSESGEMPAMDLSSPSSNSGRIFATGLANGAAGGGSGNGGLPMLGMPMPPNLLLMAAAREEMHALGHAHAKFPLLPFGPLGFMGLHPPPNVCNLCFKMLPSLAALESHLQSEHAKEPATGHAQRPHCSDAGSPYGAKLTLNPNLFAKKPPSSSSSSSGEKLPESSNPPFPAENPPATPIKEDPDQEQLMVEEGASAGEGSGTGATSNYPQEAGDAEQSLMKMQLHAHRFPASPLDFQQALMSAGPPTSSLDPPVNNKHFCHVCRRNFSSSSALQIHMRTHTGDKPFQCNVCQKAFTTKGNLKVHMGTHMWTNPTSRRGRRMSLELPMRPGPNSGQGHPGSSAEQEFMQRRPELFFPYLPPFFNGLPPKPGELSPGAFPNIPPPPFANGGKYPYPPGLLGFPGFLAQHPYGLERRSSSKSPTPEPAQSPALREEEGSGNIWHPLSRIKVENNQNESMGGFNEQEDHAETDATGGDNDESESRDAEK
Protein: Oxygen sensor histidine kinase response regulator DosT (EC 2.7.13.3) (P9WGK1)
Organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Function: Interacts with the two-component regulatory system DevR/DevS (DosR/DosS) involved in onset of the dormancy response. Required for full induction of the DevR (DosR) regulon; required during early adaptation to anaerobiosis, to start induction of the DevR regulon. May act as a direct hypoxia/oxygen sensor. O(2) acts as a switch, with the Fe(2+)-O(2)-bound protein inactive in autophosphorylation. Autophosphorylates under anaerobic but not aerobic conditions, binding of NO or CO has no effect on autophosphorylation. Binds a number of gases; O(2), NO, CO. May be a secondary sensor for CO. Donates a phosphate group to transcriptional regulator DevR (DosR).
Subcellular location: Cytoplasm {ECO:0000305|PubMed:17600145}.
Interaction partners:
- DNA-binding transcriptional activator DevR/DosR
- Universal stress protein Rv2026c
- Probable transcriptional regulatory protein NarL
- Alpha-crystallin
- Universal stress protein Rv2028c
- Putative NAD
- Possible two component transcriptional regulatory protein
- ABC transporter ATP-binding/permease protein Rv1747
Sequence:
MTHPDRANVNPGSPPLRETLSQLRLRELLLEVQDRIEQIVEGRDRLDGLIDAILAITSGLKLDATLRAIVHTAAELVDARYGALGVRGYDHRLVEFVYEGIDEETRHLIGSLPEGRGVLGALIEEPKPIRLDDISRHPASVGFPLHHPPMRTFLGVPVRIRDEVFGNLYLTEKADGQPFSDDDEVLVQALAAAAGIAVDNARLFEESRTREAWIEATRDIGTQMLAGADPAMVFRLIAEEALTLMAGAATLVAVPLDDEAPACEVDDLVIVEVAGEISPAVKQMTVAVSGTSIGGVFHDRTPRRFDRLDLAVDGPVEPGPALVLPLRAADTVAGVLVALRSADEQPFSDKQLDMMAAFADQAALAWRLATAQRQMREVEILTDRDRIARDLHDHVIQRLFAVGLTLQGAAPRARVPAVRESIYSSIDDLQEIIQEIRSAIFDLHAGPSRATGLRHRLDKVIDQLAIPALHTTVQYTGPLSVVDTVLANHAEAVLREAVSNAVRHANATSLAINVSVEDDVRVEVVDDGVGISGDITESGLRNLRQRADDAGGEFTVENMPTGGTLLRWSAPLR
Protein: Transient receptor potential cation channel, subfamily V, member 3 (E9PU00)
Organism: Rattus norvegicus (Rat)
Subcellular location: Cell membrane {ECO:0000256|ARBA:ARBA00004651}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004651}.
Interaction partners:
- Transient receptor potential cation channel subfamily M member 8
- Transient receptor potential cation channel subfamily M member 3
- Ankyrin 1
- Transient receptor potential cation channel, subfamily C, member 5
- Ankyrin-3
- Transient receptor potential cation channel subfamily M member 4
- Ankyrin 2
- Transient receptor potential cation channel subfamily M member 7
- Calmodulin-1
- Hypoxia-inducible factor 1-alpha inhibitor
Sequence:
MNAHSKEMVPLMGKRTTAPGGNPAVLTEKRPADLTPTKKSAHFFLEIEGFEPNPTVTKTSPPIFSKPMDSNIRQCLSGNCDDMDSPQSPQDDVTETPSNPNSPSANLAKEEQRQKKKRLKKCIFAAVSEGCVRELRELLQDLQELCRRRRGLDASDFLMHKLTASDTGKTCLMKALLNINPNTKEIVRILLAFAEENDILDRFINAEYTEEAYEGQTALNIAIERRQGDITAVLIAAGADVNAHAKGVFFNPKYQHEGFYFGETPLALAACTNQPEIVQLLMENEQTDITSQDSRGNNILHALVTVAEDFKTQNDFVKRMYDMILLRSGNWELETMRNNDGLTPLQLAAKMGKAEILKYILGREIKEKPLRSLSRKFTDWAYGPVSSSLYDLTNVDTTTDNSVLEIIVYNTNIDNRHEMLTLEPLHTLLHMKWKKFAKYMFFLSFCFYFFYNITLTLVSYYRPREDEALPHPLALTHKMSWLQLLGRMFVLIWAMCISVKEGIAIFLLRPSDLQSILSDAWFHFVFFVQAVLVILSVFLYLFAYKEYLACLVLAMALGWANMLYYTRGFQSMGMYSVMIQKVILHDVLKFLFVYILFLLGFGVALASLIEKCSKDKKDCSSYGSFSDAVLELFKLTIGLGDLNIQQNSTYPILFLFLLITYVILTFVLLLNMLIALMGETVENVSKESERIWRLQRARTILEFEKMLPEWLRSRFRMGELCKVADEDFRLCLRINEVKWTEWKTHVSFLNEDPGPIRRTADSNKIQDSSRSNSKTTLYAFDELDEFPETSV
Protein: SOSS complex subunit C (INTS3- and NABP-interacting protein) (Sensor of single-strand DNA complex subunit C) (Sensor of ssDNA subunit C) (SOSS-C) (Single-stranded DNA-binding protein-interacting protein 1) (SSB-interacting protein 1) (hSSBIP1) (Q9NRY2)
Organism: Homo sapiens (Human)
Function: Component of the SOSS complex, a multiprotein complex that functions downstream of the MRN complex to promote DNA repair and G2/M checkpoint. The SOSS complex associates with single-stranded DNA at DNA lesions and influences diverse endpoints in the cellular DNA damage response including cell-cycle checkpoint activation, recombinational repair and maintenance of genomic stability. Required for efficient homologous recombination-dependent repair of double-strand breaks (DSBs) and ATM-dependent signaling pathways.
Subcellular location: Nucleus {ECO:0000269|PubMed:19605351, ECO:0000269|PubMed:19683501}. Note=Localizes to nuclear foci following DNA damage.
Interaction partners:
- Integrator complex subunit 3
- SOSS complex subunit B1
- SOSS complex subunit B2
- Single-stranded DNA-binding protein 2
- Single-stranded DNA-binding protein, mitochondrial
- DNA endonuclease RBBP8
- Retinoblastoma-binding protein 5
- Nibrin
- Integrator complex subunit 11
Sequence:
MAANSSGQGFQNKNRVAILAELDKEKRKLLMQNQSSTNHPGASIALSRPSLNKDFRDHAEQQHIAAQQKAALQHAHAHSSGYFITQDSAFGNLILPVLPRLDPE
Protein: Vacuolar ATPase assembly integral membrane protein VMA21 homolog (Q38DV0)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
Sequence:
MSGADDERPQPQGGADTLRTLQEEEHREREYIRKELYSSLLNGDNAESGDEPSTKETLRMSKEAREELNRAAFRPLKDKAAGFRLFAQNMRMPHNQRVASVFLLFSVLMLTVPILILLIGMHIVAPFADVDPGTCGGLMAVFSTIVIMTVYVVYSLREAPLASEAEAINPDKKQD
Protein: Cell wall alpha-1,3-glucan synthase mok12 (EC 2.4.1.183) (Q9UUL4)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Interaction partners:
- Phospholipid-transporting ATPase accessory subunit ivn1
- O-glycoside alpha-1,2-mannosyltransferase homolog 5
- Small ribosomal subunit protein uS15m
- Alpha-amylase mde5
- Alpha-amylase 3
- Uncharacterized glycosyl hydrolase C27E2.01
- Uncharacterized glycosyl hydrolase C11E10.09c
- Alpha-amylase 2
Sequence:
MLFFSIPTILLIFFLFIQIITAAFLTDENEPWNLNRNWTAQKILDYSAEWNSHEYFPSPSNWRALPFYTIILDKWTNGVPENDVAEDTVFESDPYEVTFRAGGDIVGLVTPRSLDYLESMGIKAVYIAGTPFQNLPWYPDGYSPLDFTLLDKHTGTLNQWHEAIMKLHERGFYVVVDFTISTLSELSYFVNSSMSFANTSAPFSTKGYKMKYKHPEYHYTDFQLSNGSSYSCNAPTFWDVTGLPINNTEDLNSISEVMCLSGDFDHYGDVEAFGNHPPWWRQLSNFASVQDRLRDWDPIVAKKLKHLGCLAVKMLDIDGIRVDKATQITADFLGDWSAYIRQCAREIGKENFFIPGEVTSGADFGSIYVGRGRQADQRPNNREIALQTGYNESKYFLRKESDSALDSVSFHYSVYRTLTLLLGLQGELFAAFDLNRHDFAAMWNQMLIQDDMINANTKKFDPRHLYGLTNQDIFRWPSIKDGRFKQLLGLFVVHLLMPGIPLIYYGEEQNLKLLDNQAANYIFGRQPITSSIGWQKHGCYQIGTTQYTDLDFGPASEACRDDWNSLDHLDPTSPTKHYIARMNEIRSYFPQVRDGWDLKLIGKWTHEGTFPGNELYGESNPTTWGLWSMIRGPLAPYQKFSDQNDYIWLIFTNENTTKTYDMDCMRQVDNKFPPYPALLGPYSSGSTVKNLLYPYEEIDLSTSTIDSPDIGNIGCIPHLTIDAYGSKIFVKKEDWIRPSLYLTKFLPGHDSRIYSATEVTSFKISLGFSEEVDCKDLFKRIGFNSRTLNSSFAPKILEDSISCGYLDQPAPQEYTNAPVTKWFFNATLDSVPNGMHELLLNEVKSTSNQTMQSKIARLIFRVGNEENPLVYPNNATFSPSLLYKASNGDLYVNHTGAGADKYRFSLNYGGTYSKWKTVSTPSEKLRKPTWNGTNLQKWDGDHLIVQYWSSIALSTAHVQHGDTLNYSRQFPNLFVQGAFNRFGYDGSMPSKMSYNLENRTWSYDLISTWPAELVLNVWGMNPDNNADQGWVYGDLDNDTIIDRVPPGSSRISNFIRFLDPPPKPYLSYKMYLNDFTRQLHYIPKGSWTVQIVAIVLLILLPPLFGIFSVALYSGAFSRVTIFNGSHNRGIKVAKQKIKSIMSRIFPFSVHLPLDNSSELLKQLPESEKRLNVLVATLEYDVPDLGIRVKIGGLGVMAQLMGQHMEFQDMVWVVPIISGVEYPFDKLCTEPKIAVKIGDDEFVVNCYSYKSGNITYVFLQSEVFYKQSSKEPYPLKMDDLASAIFYSVWNQCIAEVWKRFPLDIYHVNDYHGALAPLYLLPEVIPVAVSLHNAEFQGLWPLRTSAELECVCSIFNIEKDICTKYVQFGHVFNLLHSIISYVRKHQGGYGVVAVSDKYSKQTLSRYPIFWSLVHISGLPNPDPSDLKLLNHLTDDPVDVDFVLEAKRKLLKKQTQEWANLDVDPSAQLLVFVGRWSHQKGIDLIADLAPKLLTEHNVQLITIGPVIDLHGQFAAEKLEQIAKRFPTRVLCKPVFTAVPPFLFAGTDFALIPSRDEPFGLVAVEFGRKGVLCIGSRTGGLGHMPGWWFQMASPNTGHLLTQFENAITKALHSNGELRARLRVEALRQRFPVCIWKQKSENLLKSCIYVHEMETLKHASPTFKAYQFVVRICHYLTSKVKSINKDQVFNAFSPDVSERPPLFEVASCSNETDSVEKLTPELSVSPESDMHFKDGNSSKLEIVESKEIYASDSDISNSTSEDINKDECVSKDIEVDNFALNLQSQSYEGDSNDFGIREVPLSDANQSSQADSTSIDRYGPYSSQKVNFSKYKDFVESRPTFFQSSVTFTDADGSTRKTFSKRLENLTTSNTLKSLSVDHFIRKHERKYFNGLRKQEIDVKLKSRSDKEKSCTVSESYKQIDCDTYEATRLQKLLLHSIGGWPLYTIVLAIGQILGASSYQLTLLSGESAQSTVSMYILLSIFSFFSLFWWFLSRVVQARYILSLPFFFFGISFILVAITHFFQKTTACSVIQHIAAYVYAISSSTGSLYFAWNFGAEGGIATHHWILRACLVHGIQQIWSAILWSWGDLLSKKDLTQNVGPGIFAGGLIASFICFGLSYVTFAGLPAFYRQAPSIIPAFYRSLGKRNIVIWFFISQILINYWLAVPYGQAWRFFWNTSNTPLWSIIILLLIFFIVVWAVLLSVIKILSLNNVWFPVIFGLGLICPRWCLEFWSSSGLGINLPWAGKASALLTKSVWLLLALWDGIQGVGVGVMLLQTLARDHVAFTLMLAQVISCITIMIAKPSLPVSDRVFPNLGAWNPSEGPGPCASPCFYIALICQFVAVGGLLYHYRKSQLAL
Protein: LD13050p (M6, isoform B) (Proteolipid protein M6-2) (Q7KI49)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MPGKGNNRDRIRDPREEILLETNFEDDGGVLTRAYNGNPYNPTIQNRRRNSYRSDHSLDRYTERGGEGECCQSCMARIPYATLIATLMCLLGVGIFCFTMYRGASLTVIMVDQVFHLRLIWIEAVQMIFVIIGAGMAALGFMILFVGFLATGATRYKVYRAWRSRVGGRISCAVLMGITYLLNFVWSLILCFLVVVTFIYTMFWNMCTSVEHSQSCIDLTQFHFMFPPNTKLEDMKVCEKYEIKAFCKDGVENAEVMFILATLSTLLVLLSLVHYLMCLSANYAHIRDHEKFQELQEIQNLNELEYSATSKDRF
Protein: COP9 signalosome complex subunit 6 (E7EM64)
Organism: Homo sapiens (Human)
Subcellular location: Cytoplasm {ECO:0000256|RuleBase:RU367006}. Nucleus {ECO:0000256|RuleBase:RU367006}.
Interaction partners:
Sequence:
MAAAAAAAAATNGTGGSSGMEVDAAVPSVMACGVTGSVSVALHPLVILNISDHWIRMRSQEGRPVQVIGALIGKQEGRNIEVMNSFELLSHTVEEKIIIDKEYYYTKEEQFKQVFKELEFLGWYTTGGPPDPSDIHVHKQVCEIIESPLFLKLNPMTKHTDLPVSVFESVIDIINGEATMLFAELTYTLATEEAERIGVDHVARMTATGSGENSTVAEHLIAQHSAIKMLHSRVKLILEYVKASEAGEVPFNHEILREAYALCHCLPVLSTDKFKTDFYDQCNDVGLMAYLGTITKTCNTMNQFVNKFNVLYDRQGIGRRMRGLFF
Protein: Kinesin-like protein (Q388B7)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
- Kinesin-like protein, putative
- FG-GAP repeat protein, putative
- PTHB1 N-terminal domain-containing protein
- Bardet-Biedl syndrome 8 protein
- FG-GAP repeat protein, putative
- Dynein light chain
- Kinesin, putative
- Kinesin-like protein
- Kinesin-like protein
- Kinesin, putative
Sequence:
MSVEQPEQQISGLLEQLYHSSNVSAERETIMNLSNVVRQGGAEFLLDVVKTNLKSGVPEKQEASMTILDEVTLNCGPSFAVMLSSQKWMDRLIKLAKAGPPQVTTKIISTVIGWQKRYHTVSFAQCIKKLSQSKTTGEACKQALRQAGDDGTGSSLGYDASSPASLRSTGVTDSRKSKKCDAVLAELQSDLVSLEYSLENPKFVQDDAIARECKNHKMKCMQMLESGSYESIASDLMQLIERFSRALELYECMTGVDLGEGEAARSRALTRGKDNGGDSDDEYSKQLRARVAPKNAQQVMLQAQEATQQLVEKERHETMQLRTQLEEMRRKYEDMHNKYKDAKARNKEAVGALQEYAKRIEVLEKSGGGAAAAAAALPPPPPISEEKDKGKDKSGPALNVGPIATAMRDTVQVLRQSLREVREQYVSDIQKESAYYSSQLTSAIASIAAAAEKDRGSNSQLLVRTQELYKREMKLRKQYYNQIQELKGNIRVYCRVRPLLPREVAAGHTNIMDFPSADEIRVNDPAGRQKVYEFDEVYPPHAPQARVFEDTSPLIDSVVDGYNVCIFAYGQTGSGKTHTMGGYGEDRGINTRALQRLFEIIDERKDTDESTVTVSVLEIYCEMIRDLLVPKEKSKSTTYEVKQGGQFGTYVTNLSEVPVQCADEITKIMENANKNRSEGQTNMNEHSSRSHMVLYITVRTTNKETNMQCFGKLSLIDLAGSERLDKTGAEGQMLKEAVAINKSLSSLGDVISGLAQNSKHIPFRNSVLTYLLQDSMGGQAKVLMFVCVNPASYNASESNSSLQFASRARGVSLGQIKKNP
Protein: Aqy1p (Q5A1Z4)
Organism: Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast)
Subcellular location: Cell membrane {ECO:0000256|ARBA:ARBA00004651}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004651}.
Interaction partners:
- Glycerol-3-phosphate dehydrogenase
- Pho81p
- SUMO protease
Sequence:
MVAESSSIDNTPNDVEAQRPVYEPKYDDSVNVSPLKNHMIAFLGEFFGTFIFLWVAFVIAQIANQDPTIPDKGSDPMQLIMISFGFGFGVMMGVFMFFRVSGGNLNPAVTLTLVLAQAVPPIRGLFMMVAQMIAGMAAAGAASAMTPGPIAFTNGLGGGASKARGVFLEAFGTCILCLTVLMMAVEKSRATFMAPFVIGISLFLGHLICVYYTGAGLNPARSFGPCVAARSFPVYHWIYWVGPILGSVIAFAIWKIFKILKYETCNPGQDSDA
Protein: Uncharacterized protein YfjP (P52131)
Organism: Escherichia coli (strain K12)
Interaction partners:
- Uncharacterized protein YdfA
- UPF0380 protein YfjQ
Sequence:
MKNFEVLQPLQNSLSGLPLWVSERILQQINQLTHYEPVIGIMGKTGAGKSSLCNALFAGEVSPVSDVAACTRDPLRFRLQIGEHFMTIVDLPGVGESGVRDTEYAALYREQLPRLDLILWLIKADDRALATDEHFYRQVIGEAYRHKMLFVISQSDKAEPTSGGNILSTEQKQNISRKICLLHELFQPVHPVCAVSVRLQWGLRVMAERMIKCLPREASSPVVALLQHPFRTTVAREQARDDFGETVGAILDTVSTFPLIPAPVRTIIQAVRSSVVSVARAVWDFFF
Protein: Nuclear receptor coactivator 4 (A0A8I6A1Q3)
Organism: Rattus norvegicus (Rat)
Interaction partners:
Sequence:
MAQGTVSRMNTSLEQSGCCSSRETLLRCSDARRELELAIGGVLRAEQQMKDNLREVKAQIHSCISRHLECLRSREVWLNEQVDLIYQLKEETLQQQAQQLYWLMGQFNCLIHQLEITQNKDLANQVALCLERLGSLTLKPEDSTVLLFEADASALRQTITTFGSLKTIQIPEHLMAHPSSSSVRPFLEKRGYTQVPEQKSASSGTAVSLSEWLLVSKPAIGPQAPYVPSTNPQDWLTPKQTLENSQTSARICSDAWGNLKGLENWLLNSHQQEIPGKPSSSKCNSHCSTSSFSTEDEKVEDVEVLDQDELDLSDWLVTPQEPRDLEKPVNGRSDTSDKFKLLFQVFREPYNVNDWLVKPDSCTNCQGNQPRGVEIENLGNLKCLNDHLEAKKSLPVPGVITEGWLVQNHQDTCKVEEVCKANEPCTSFAECVCDDSCEKEAMHKWLLKKEGKDKNGMPMGPKSESEKHRESLSLWLCPSRNELTEHAKTPKTTAPARIADSFHIIRNSSLSEWLIGPTCKGGGPKEVPNMEERASKEMLKSPMATYWRPFNTADWVLPGKKVGNLSQFSSGEDKWLLRKKAQEVFLNSPLQEERNFRSDCYGLPAVCDLFACMQLKVDKDKWLYRAPLQM
Protein: 10-deoxymethynolide desosaminyltransferase (EC 2.4.1.277) (Q9ZGH7)
Organism: Streptomyces venezuelae
Function: Involved in the biosynthesis of the macrolide antibiotics methymycin, neomethymycin, narbomycin, and pikromycin. Catalyzes the attachment of dTDP-D-desosamine onto 12- and 14-membered macrolactone rings 10-deoxymethynolide and narbonolide to produce 10-deoxymethymycin (YC-17) and narbomycin. DesVII is unique among glycosyltransferases in that it requires an additional protein component, DesVIII, for its activity. DesVII can recognize and process not only cyclic substrates of different ring size, but also a variety of linear substrates albeit with reduced, but measurable activities. Both L-sugars and D-sugars are recognized as substrates and variant substitutions at C-3 and C-4 are tolerated, but deoxygenation at C-6 is required.
Interaction partners:
Sequence:
MRVLLTSFAHHTHYYGLVPLAWALLAAGHEVRVASQPALTDTITGSGLAAVPVGTDHLIHEYRVRMAGEPRPNHPAIAFDEARPEPLDWDHALGIEAILAPYFHLLANNDSMVDDLVDFARSWQPDLVLWEPTTYAGAVAAQVTGAAHARVLWGPDVMGSARRKFVALRDRQPPEHREDPTAEWLTWTLDRYGASFEEELLTGQFTIDPTPPSLRLDTGLPTVGMRYVPYNGTSVVPDWLSEPPARPRVCLTLGVSAREVLGGDGVSQGDILEALADLDIELVATLDASQRAEIRNYPKHTRFTDFVPMHALLPSCSAIIHHGGAGTYATAVINAVPQVMLAELWDAPVKARAVAEQGAGFFLPPAELTPQAVRDAVVRILDDPSVATAAHRLREETFGDPTPAGIVPELERLAAQHRRPPADARH
Protein: LexA repressor (EC 3.4.21.88) (P9WHR7)
Organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Function: Represses a number of genes involved in the response to DNA damage (SOS response), including recA and lexA. Has been shown to bind to the 14 bp palindromic sequence 5'-CGAACNNNNGTTCG-3'. In the presence of single-stranded DNA, RecA interacts with LexA causing an autocatalytic cleavage which disrupts the DNA-binding part of LexA, leading to derepression of the SOS regulon and eventually DNA repair.
Interaction partners:
- Protein RecA
- DNA polymerase IV 1
- Holliday junction branch migration complex subunit RuvA
- DNA repair protein RecN
- Crossover junction endodeoxyribonuclease RuvC
- UvrABC system protein A
- Cell wall hydrolase ChiZ
- Arginine repressor
- Error-prone DNA polymerase
- DNA polymerase IV 2
Sequence:
MNDSNDTSVAGGAAGADSRVLSADSALTERQRTILDVIRASVTSRGYPPSIREIGDAVGLTSTSSVAHQLRTLERKGYLRRDPNRPRAVNVRGADDAALPPVTEVAGSDALPEPTFVPVLGRIAAGGPILAEEAVEDVFPLPRELVGEGTLFLLKVIGDSMVEAAICDGDWVVVRQQNVADNGDIVAAMIDGEATVKTFKRAGGQVWLMPHNPAFDPIPGNDATVLGKVVTVIRKV
Protein: Dual endothelin-1/VEGF signal peptide receptor (DEspR protein) (Dual endothelin-1/VEGFsp receptor) (FBXW7 antisense RNA 1) (B0L3A2)
Organism: Homo sapiens (Human)
Function: Dual endothelin-1/angiotensin-2 receptor that is functionally coupled to a calcium-mobilizing transduction system, responding equivalently to both endothelin-1/EDN1 and angiotensin-2 peptides in a highly specific manner. Also binds the signal peptide of VEGFA. May play a role in angiogenesis with a significant role in cardiovascular and neural development (By similarity).
Subcellular location: Cell membrane {ECO:0000269|PubMed:24465725, ECO:0000269|PubMed:27301377, ECO:0000269|PubMed:33853558}; Single-pass membrane protein {ECO:0000305|PubMed:27301377}.
Interaction partners:
Sequence:
MTMFKGSNEMKSRWNWGSITCIICFTCVGSQLSMSSSKASNFSGPLQLYQRELEIFIVLTDVPNYRLIKENSHLHTTIVDQGRTV
Protein: Cytosolic neutral trehalase (EC 3.2.1.28) (Alpha,alpha-trehalase) (Alpha,alpha-trehalose glucohydrolase) (P32356)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Hydrolyzes intracellular trehalose to glucose (Probable). The disaccharide trehalose serves as a storage carbohydrate that is mobilized during nutrient stress (Probable). Regulates the level of trehalose as a protectant for cell integrity during heat stress.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:14562095}.
Interaction partners:
- Periplasmic acid trehalase ATH1
- Protein BMH1
- Trehalose-phosphatase
- Trehalose synthase complex regulatory subunit TPS3
- Probable trehalase
- Trehalose synthase complex regulatory subunit TSL1
- cAMP-dependent protein kinase type 1
- Alpha,alpha-trehalose-phosphate synthase 56 kDa subunit
- Glycogen phosphorylase
- m7GpppX diphosphatase
Sequence:
MSQVNTSQGPVAQGRQRRLSSLSEFNDPFSNAEVYYGPPTDPRKQKQAKPAKINRTRTMSVFDNVSPFKKTGFGKLQQTRRGSEDDTYSSSQGNRRFFIEDVDKTLNELLAAEDTDKNYQITIEDTGPKVLKVGTANSYGYKHINIRGTYMLSNLLQELTIAKSFGRHQIFLDEARINENPVNRLSRLINTQFWNSLTRRVDLNNVGEIAKDTKIDTPGAKNPRIYVPYDCPEQYEFYVQASQMHPSLKLEVEYLPKKITAEYVKSVNDTPGLLALAMEEHFNPSTGEKTLIGYPYAVPGGRFNELYGWDSYMMALGLLEANKTDVARGMVEHFIFEINHYGKILNANRSYYLCRSQPPFLTEMALVVFKKLGGRSNPDAVDLLKRAFQASIKEYKTVWTASPRLDPETGLSRYHPNGLGIPPETESDHFDTVLLPYASKHGVTLDEFKQLYNDGKIKEPKLDEFFLHDRGVRESGHDTTYRFEGVCAYLATIDLNSLLYKYEIDIADFIKEFCDDKYEDPLDHSITTSAMWKEMAKIRQEKITKYMWDDESGFFFDYNTKIKHRTSYESATTFWALWAGLATKEQAQKMVEKALPKLEMLGGLAACTERSRGPISISRPIRQWDYPFGWAPHQILAWEGLRSYGYLTVTNRLAYRWLFMMTKAFVDYNGIVVEKYDVTRGTDPHRVEAEYGNQGADFKGAATEGFGWVNASYILGLKYMNSHARRALGACIPPISFFSSLRPQERNLYGL
Protein: RCSD domain containing 1 (F1M4V3)
Organism: Rattus norvegicus (Rat)
Interaction partners:
Sequence:
MYMRPRTLKIAPLSKHLPHREDADNEDQERPSETNSNVDSSAQPSVAQLAGRFREQAAVAREKSPSSTSHPPKIKVKSSPLIEKLQANLAFDPAALLPGASPKSPGLKAMVSPFHSPPSTPSSPGIRSHPGEAEEVPVSFDQPPEGTHLPSYNKVRTRGSIKRRPPSRRFRRSQSDCGDLRDYRAVEPSQENGAREENGDDVFPSKSKDPGSPQPNQEAGADRVEGTLRSTEKPRRRNTCSSTEKPEELVGTLEEANAGAKAGQTPDTASQGHPEVQEPSQTCSPETENGCGSPREETAPGEHTDTGKATEGTASEERVTEEEDGLGQKSPDANIPEDEVVRGKVPQTSSGEAEGTTVPEPEAKQKEEAPLEPSGSPGADHSAGEASNEIQSENAVSTEDIPVEDTRM
Protein: Protein arginine N-methyltransferase 3 (EC 2.1.1.319) (Heterogeneous nuclear ribonucleoprotein methyltransferase-like protein 3) (O60678)
Organism: Homo sapiens (Human)
Function: Protein-arginine N-methyltransferase that catalyzes both the monomethylation and asymmetric dimethylation of the guanidino nitrogens of arginine residues in target proteins, and therefore falls into the group of type I methyltransferases (Probable). May regulate retinoic acid synthesis and signaling by inhibiting ALDH1A1 retinal dehydrogenase activity.
Subcellular location: Cytoplasm, cytosol {ECO:0000269|PubMed:39513743, ECO:0000269|PubMed:9642256}. Nucleus {ECO:0000269|PubMed:39513743}. Note=Localized to the nucleus by ZNF200. {ECO:0000269|PubMed:39513743}.
Interaction partners:
- Small ribosomal subunit protein uS5
- Programmed cell death protein 2-like
- Band 4.1-like protein 3
- Protein arginine N-methyltransferase 5
- Protein arginine N-methyltransferase 1
- Histone-arginine methyltransferase CARM1
- Heterogeneous nuclear ribonucleoprotein A1
- Histone-lysine N-methyltransferase SETD7
Sequence:
MCSLASGATGGRGAVENEEDLPELSDSGDEAAWEDEDDADLPHGKQQTPCLFCNRLFTSAEETFSHCKSEHQFNIDSMVHKHGLEFYGYIKLINFIRLKNPTVEYMNSIYNPVPWEKEEYLKPVLEDDLLLQFDVEDLYEPVSVPFSYPNGLSENTSVVEKLKHMEARALSAEAALARAREDLQKMKQFAQDFVMHTDVRTCSSSTSVIADLQEDEDGVYFSSYGHYGIHEEMLKDKIRTESYRDFIYQNPHIFKDKVVLDVGCGTGILSMFAAKAGAKKVLGVDQSEILYQAMDIIRLNKLEDTITLIKGKIEEVHLPVEKVDVIISEWMGYFLLFESMLDSVLYAKNKYLAKGGSVYPDICTISLVAVSDVNKHADRIAFWDDVYGFKMSCMKKAVIPEAVVEVLDPKTLISEPCGIKHIDCHTTSISDLEFSSDFTLKITRTSMCTAIAGYFDIYFEKNCHNRVVFSTGPQSTKTHWKQTVFLLEKPFSVKAGEALKGKVTVHKNKKDPRSLTVTLTLNNSTQTYGLQ