wanglab/gogpt-training-data huggingface dataset:
Protein: Excision repair cross-complementing rodent repair deficiency complementation group 8 isoform 3 (A0A0S2Z3P2)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MLGFLSARQTGLEDPLRLRRAESTRRDHPDVHRYSVETVQWYPHDTGMFTSSSFDKTLKVWDTNTLQTADVFNFEETVYSHHMSPVSTKHCLVAGFWY
Protein: Mitogen-activated protein kinase kinase kinase kinase 1 (EC 2.7.11.1) (Hematopoietic progenitor kinase) (MAPK/ERK kinase kinase kinase 1) (MEK kinase kinase 1) (MEKKK 1) (Q92918)
Organism: Homo sapiens (Human)
Function: Serine/threonine-protein kinase, which may play a role in the response to environmental stress. Appears to act upstream of the JUN N-terminal pathway. May play a role in hematopoietic lineage decisions and growth regulation. Able to autophosphorylate. Together with CLNK, it enhances CD3-triggered activation of T-cells and subsequent IL2 production (By similarity).
Interaction partners:
- GRB2-related adapter protein 2
- Mitogen-activated protein kinase kinase kinase 11
- Growth factor receptor-bound protein 2
- Drebrin-like protein
- Lymphocyte cytosolic protein 2
- C-Jun-amino-terminal kinase-interacting protein 1
- C-Jun-amino-terminal kinase-interacting protein 2
- Adapter molecule crk
- Crk-like protein
- SH2/SH3 adapter protein NCK1
Sequence:
MDVVDPDIFNRDPRDHYDLLQRLGGGTYGEVFKARDKVSGDLVALKMVKMEPDDDVSTLQKEILILKTCRHANIVAYHGSYLWLQKLWICMEFCGAGSLQDIYQVTGSLSELQISYVCREVLQGLAYLHSQKKIHRDIKGANILINDAGEVRLADFGISAQIGATLARRLSFIGTPYWMAPEVAAVALKGGYNELCDIWSLGITAIELAELQPPLFDVHPLRVLFLMTKSGYQPPRLKEKGKWSAAFHNFIKVTLTKSPKKRPSATKMLSHQLVSQPGLNRGLILDLLDKLKNPGKGPSIGDIEDEEPELPPAIPRRIRSTHRSSSLGIPDADCCRRHMEFRKLRGMETRPPANTARLQPPRDLRSSSPRKQLSESSDDDYDDVDIPTPAEDTPPPLPPKPKFRSPSDEGPGSMGDDGQLSPGVLVRCASGPPPNSPRPGPPPSTSSPHLTAHSEPSLWNPPSRELDKPPLLPPKKEKMKRKGCALLVKLFNGCPLRIHSTAAWTHPSTKDQHLLLGAEEGIFILNRNDQEATLEMLFPSRTTWVYSINNVLMSLSGKTPHLYSHSILGLLERKETRAGNPIAHISPHRLLARKNMVSTKIQDTKGCRACCVAEGASSGGPFLCGALETSVVLLQWYQPMNKFLLVRQVLFPLPTPLSVFALLTGPGSELPAVCIGVSPGRPGKSVLFHTVRFGALSCWLGEMSTEHRGPVQVTQVEEDMVMVLMDGSVKLVTPEGSPVRGLRTPEIPMTEAVEAVAMVGGQLQAFWKHGVQVWALGSDQLLQELRDPTLTFRLLGSPRLECSGTISPHCNLLLPGSSNSPASASRVAGITGL
Protein: Tubulin beta-3 chain (Beta-3-tubulin) (P08841)
Organism: Drosophila melanogaster (Fruit fly)
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:
- Tubulin alpha-2 chain
- Tubulin alpha-4 chain
- Tubulin alpha-1 chain
- AT04270p
- Tubulin alpha-3 chain
- Serine/threonine-protein kinase CG17528
- non-specific serine/threonine protein kinase
- Echinoderm microtubule-associated protein-like CG42247
- Protein mini spindles
- Dynein heavy chain, cytoplasmic
Sequence:
MREIVNLQAGQCGNQIGAKFWEIISEEHGIDSNGIYVGDSDLQLERVSVYYNEASAVTRSSGGKYVPRAILLDLEPGTMESVRSGPYGQLFRPDNFVYGQSGAGNNWAKGHYTEGAELVDNVLDVVRKECENCDCLQGFQLTHSLGGGTGSGMGTLLISKIREEYPDRIMNTYSVVPSPKVSDTVVEPYNATLSIHQLVENTDETYCIDNEALYDICFRTLKVSNPSYGDLNHLVSLTMSGVTTCLRFPGQLNADLRKLAVNMVPFPRLHFFMPGFAPLTSRGSQQYRALTVPELTQQMFDAKNMMAACDPRHGRYLTVAAVFRGRMSMKEVDEQMLAVQNKNSSYFVEWIPNNVKTAVCDIPPKGLKMSSTFIGNTTAIQELFKRISEQFSAMFRRKAFLHWYTGEGMDEMEFTEAESNMNDLVSEYQQYQEATADDEFDPEVNQEEVEGDCI
Protein: AP-1-like transcription factor yap1 (BZIP domain-containing transcription factor yap1) (Q4WMH0)
Organism: Aspergillus fumigatus (strain ATCC MYA-4609 / CBS 101355 / FGSC A1100 / Af293) (Neosartorya fumigata)
Function: Transcription activator involved in oxidative stress response and redox homeostasis. Regulates the transcription of genes encoding antioxidant enzymes and components of the cellular thiol-reducing pathways, including thioredoxin peroxidase (aspF3), cytochrome peroxidase, and the protein AFUA_3G00730, which appears to belong to the glutathione S-transferase family. Proteins of the protein degradation pathway are also regulated by yap1, as well the p-nitroreductase family protein AFUA_5G09910. May be involved in antifungal resistance to voriconazole.
Subcellular location: Nucleus {ECO:0000269|PubMed:17921349}. Cytoplasm {ECO:0000269|PubMed:17921349}. Note=The nuclear localization is oxidative stress-dependent and oxidized yap1 is found predominantly in the nucleus, while reduced yap1 is continuously exported to the cytoplasm. {ECO:0000269|PubMed:17921349}.
Interaction partners:
- Basic leucine zipper
- very-long-chain enoyl-CoA reductase
- Exportin KapK
- Transcription factor
Sequence:
MADYNTLYQQGLYLSPDQQDLLLAALSSNNPTQKQQTVTHNSEANQNLNHTPGHASSGSFSVSPPSGLDGSVNQSTTFGYEDSPYLDLNPDFDLDFLGNESLIGDLPPSLPSTEDYEPGDKRKDIDGQVNDKEDSGKKRRESDEKAAKKPGRKPLTSEPTSKRKAQNRAAQRAFRERKEKHLKDLEAKVEELQKASDNANQENGLLRAQVERLQLELKEYRKRLSWVTSTSGLSPVNAIPGAYSKGMYGLNNNEFMFDFPKFGDLPGSHLFTNTQTSKSNQNKAKDNPTATPRSEAQVPGVLNRNDLKISSPNGLSNGPSPAKSTPSGQTPNSQTSTRPGSGTLNGAVDNNGAARGYQVNSSYSASTKQATHDTPSSDSPSSSSDSHQSQLLSSNGTSPEPSLHSPAVKATESSTPHACTYTTINGEESFCAQLSMACGNINNPIPAVRQNSESASNTPSHANSSDKALGLDFFAQQNGGQFDPVLFGDWREPQDAILSQDFGTFFDDAFPLPDLGSPSHNFSEATKQPAAPKKDLIAEIDSKLDEDEEVVPGEDKSQMLTCNKIWDRLQSMEKFRNGEIDVDNLCSELRTKARCSEGGVVVNQKDVEDIMGRVK
Protein: Ammonium transporter AmtB-like domain-containing protein (Q22947)
Organism: Caenorhabditis elegans
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
Interaction partners:
- Probable Na
Sequence:
MRSPLHQNQLTLILGLFQVVFLVIFALYGSYDASALPSETKNVEEAARMTNLYPLFQDTHVMIFIGFGFLMTFLKRYGFSAVSINMLLAVFTIQWGIIVRGMASAHHGFKFTISLEQLLTADFAAAVILISMGAMLGKLSPSQYVIMAFFETPVALIVEHICVHNLQINDVGGSIIVHAFGAYFGLACAKGFGKKEQRGHTNEGSTYHTDIFAMIGAIFLWIYWPSFNAAVAATDDARQRAVANTFLSLCACTMTTFLVSQAVDKHKRFDMVHIANSTLAGGVAIGTTANVVLEPYHAMIIGVIAGAVSVIGYKYITPFLSEKLGIHDTCGVNNLHGMPGLIAGFASIAFLFIYDETRYPAQYDKIYPGMARGEDRTRMFDEKTQALNQLMAIGLVFLASTVSGYLTGLLLKLKIWDQVRDDEYYADGDYFETPGDYDFTSRIVTSVKQIEVAEYNPLSQKEV
Protein: Dolichyl-phosphate-mannose--protein mannosyltransferase (EC 2.4.1.109) (Q4WWN0)
Organism: Aspergillus fumigatus (strain ATCC MYA-4609 / CBS 101355 / FGSC A1100 / Af293) (Neosartorya fumigata)
Subcellular location: Endoplasmic reticulum membrane {ECO:0000256|ARBA:ARBA00004477, ECO:0000256|RuleBase:RU367007}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004477, ECO:0000256|RuleBase:RU367007}.
Interaction partners:
- Dolichyl-phosphate-mannose--protein mannosyltransferase
- Dolichyl-phosphate-mannose--protein mannosyltransferase
Sequence:
MSQKSKETLQVKPLPRKGRSPSRSPRPKDRKKVPADTSSYGSEGVKDNNIFHLPSSDYKVLVLVTLVALVVRLFRIYQPSSVVFDEVHFGGFASKYIKGRFFMDVHPPLAKLLITLAGWLAGFDGNFDFKDIGKDYLEPGVPYVAMRLLPAVLGVLTVPLMFLTLKASGCRTITAVLGAGVVIFENGLITQSRLILLDSPLVFFTALTALAFTSFTNQQELGPSHAFRGPWWFWLAATGLSLGATLSVKWVGLFTVAWVGSLTVLQLWVLWGDAQNVTPRLWFKHFFARVFCLIIVPLGIYCGMFAIHFLCLVNPGDGDGFMSSEFQATLNSKGMQDVPADVVFGSRVSIRHLNTQGGYLHSHAHMYPTGSKQQQITLYPHKDENNVFILENQTQPLGPFGQVEGPYAWDNITTEYIQDGAVVRLYHAMTHRRLHSHDERPPVTDVDWQFEVSAYGYEGFPGDANDLFRVEIVKSKSDGEEAKKRLRTIESKFRLVHVMTGCVLFSHKVKLPEWGFDQQEVTCARGGTLPNSLWYIESNHHPMLPEDAEKVNYRNPGFFGKFWELQKVMWTTNAGLTESHAWDSRPPSWPTLLRGINFWGRDHRQIYLLGNPFIWWSSTAAIVVYIVFKGIAVIRWQRSCGDYRNVNFKRFDYEVGTSVLGWAFHYFPFYLMARQLFLHHYFPALYFALMALCQEFDFIANRFKSFGLSSRPIIGKGLVAVFLALSIFTFTLYSPLVYGNPWTQDACKKVKLVSTWDFDCNTFYTDLGQYVTQFLNANPIASSTPSAQVNPVPELPVQNSPVKEPPVAPPQQHHQEVHKEAQEASVTSQAQQPRGTMARVEYRDQHGNVLDEALVASLAREGKVSFETRHETRTRLEHAHEVEMIDGRIAPPHPDVEGQNPETVKDQEHQAAGDSPASAAVGERSVKEPSSPEPKPASEAKEATQN
Protein: Cyclin-dependent kinase D-2 (CDKD;2) (EC 2.7.11.22) (EC 2.7.11.23) (CDK-activating kinase 4-At) (CAK4-At) (Q9C9M7)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Forms a stable complex with cyclin CYCH1-1 that phosphorylates human CDK2 and the C-terminal domain (CTD) of the large subunit of RNA polymerase II.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:15486101}. Nucleus {ECO:0000269|PubMed:15486101}.
Interaction partners:
- Cyclin-H1-1
- General transcription and DNA repair factor IIH subunit TFB4
- General transcription and DNA repair factor IIH subunit TFB2
- Pentatricopeptide repeat-containing protein At4g30825
- General transcription and DNA repair factor IIH helicase subunit XPD
- General transcription factor IIH subunit 2
- General transcription and DNA repair factor IIH subunit TFB1-1
- General transcription and DNA repair factor IIH subunit TFB1-3
- General transcription and DNA repair factor IIH helicase/translocase subunit XPB2
- General transcription and DNA repair factor IIH helicase/translocase subunit XPB1
Sequence:
MSKSGDNQPVDRYLRRQILGEGTYGVVYKATDTKTGKTVAVKKIRLGNQKEGVNFTALREIKLLKELNHPHIVELIDAFPHDGSLHLVFEYMQTDLEAVIRDRNIFLSPGDIKSYMLMTLKGLAYCHKKWVLHRDMKPNNLLIGENGLLKLADFGLARLFGSPNRRFTHQVFATWYRAPELLFGSRQYGAGVDVWAAGCIFAELLLRRPFLPGSTEIDQLGKIFQAFGTPVPSQWSDMIYLPDYMEFSYTPAPPLRTIFPMASDDALDLLAKMFIYDPRQRITIQQALDHRYFSSSPSPTEPGKLQIPASKGDALEPKASEQNQHGNSPAVLSPPGKMRRVMGPEGFT
Protein: Probable conserved membrane protein (P96409)
Organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Interaction partners:
- Probable conserved transmembrane protein
- Possible lipoprotein LprC
- Alpha-
- Uncharacterized protein Rv0479c
- Membrane protein Rv1476
- Possible protease
- Carboxylesterase/lipase Culp6
- Probable integral membrane acyltransferase
- Protein Rv3035
- Uncharacterized methyltransferase Rv0224c
Sequence:
MLRFAACGAIGLGAALLIAALLLSTYTTSRIAEIPLDIDATLISDGTGTALDSASLATEHIVVNQDVPLVSQQQVTVESPANADVVTLQVGSSLRRTDKQKDSGLLLAIVDTVTLNRKTAMAVSDDTHTGGAVQKPRGLNDENPPTAIPLRHDGLSYRFPFHTEKKTYPYFDPIAQKAFDANYEGEEDVNGLTTYRFTQNVGYTPEGKLVAPLKYPSLYAGDEDGKVTTSAAMWGLPGDPNEQITMTRYYAAQRTFWVDPVSGTIVKETERANHYFARDPLKPEVTFADYQVTSTEETVESQVNAARDERDRLALWSRVLPITFTAAGLVALVGGGLFASFSLRTEGALMAASGDRDDHDYRRGGFEEPVPGAEAETEKLPTQRPDFPREPSGSDPPRLGSAQPPPPPDAGHPDPGPPERR
Protein: Isovaleryl-CoA dehydrogenase, mitochondrial (IVD) (EC 1.3.8.4) (Q9SWG0)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Involved in degradation of the branched-chain amino acids, phytol and lysine for the supply of carbon and electrons to the ETF/ETFQO complex during dark-induced sugar starvation.
Subcellular location: Mitochondrion {ECO:0000269|PubMed:10380813, ECO:0000269|PubMed:14671022}.
Interaction partners:
- Methylcrotonoyl-CoA carboxylase beta chain, mitochondrial
- Methylcrotonoyl-CoA carboxylase subunit alpha, mitochondrial
- Lipoamide acyltransferase component of branched-chain alpha-keto acid dehydrogenase complex, mitochondrial
- Electron transfer flavoprotein subunit beta, mitochondrial
- Probable enoyl-CoA hydratase 1, peroxisomal
- Electron transfer flavoprotein subunit alpha, mitochondrial
- Electron transfer flavoprotein-ubiquinone oxidoreductase, mitochondrial
- Probable enoyl-CoA hydratase 2, mitochondrial
- Probable acyl-CoA dehydrogenase IBR3
- Hydroxymethylglutaryl-CoA lyase, mitochondrial
Sequence:
MQRFFSARSILGYAVKTRRRSFSSRSSSLLFDDTQLQFKESVSKFAQDNIAPHAERIDKTNSFPKDVNLWKLMGEFNLHGITAPEEYGGLGLGYLYHCIAMEEISRASGSVALSYGAHSNLCINQLVRNGTAAQKEKYLPKLISGEHVGALAMSEPNAGSDVVGMKCKAEKVDGGYILNGNKMWCTNGPSAETLVVYAKTDTKAGSKGITAFIIEKGMTGFSTAQKLDKLGMRGSDTCELVFENCFVPEENILDKEGKGVYVLMSGLDLERLVLAAGPLGIMQACLDNVLPYIRQREQFGRPVGEFQFIQGKVADMYTALQSSRSYVYSVARDCDNGKVDPKDCAGTILCAAERATQVALQAIQCLGGNGYINEYATGRLLRDAKLYEIGAGTSEIRRIVIGRELFKEE
Protein: GM13131p (Homeobox protein SIX4) (Myotonix) (RT01027p) (Six4, isoform A) (Six4, isoform B) (Q9Y1P6)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123, ECO:0000256|PROSITE-ProRule:PRU00108, ECO:0000256|RuleBase:RU000682}.
Interaction partners:
- Protein phosphatase eya
- Paired box pox-meso protein
- Dachshund, isoform B
- Shaven, isoform A
Sequence:
MFDKNLDGNNLSVSIGGDLDSTSSGGTSSDHSAVHQDNLSSPMAYGSLFLPNAGYRGNLSCKTVLQLDKFAPYEGVEKDHLLERRFQDITNDYDKSPPPTASTTPTHYPSLNSIIFENGSSGNLGDLNGNTKTDLCAGLQRSGGGLGGNAGSGGHLISNLTAAHNMSAVSSFPIDAKMLQFSTDQIQCMCEALQQKGDIEKLTTFLCSLPPSEFFKTNESVLRARAMVAYNLGQFHELYNLLETHCFSIKYHVDLQNLWFKAHYKEAEKVRGRPLGAVDKYRLRKKYPLPKTIWDGEETVYCFKEKSRNALKDCYLTNRYPTPDEKKTLAKKTGLTLTQVSNWFKNRRQRDRTPQQRPDIMSVLPVGQLDGNGFPRMFNAPSYYPETIFNGQ
Protein: RNA polymerase sigma-B factor (General stress protein 84) (GSP84) (Sigma-37) (P06574)
Organism: Bacillus subtilis (strain 168)
Function: Sigma factors are initiation factors that promote the attachment of RNA polymerase (RNAP) to specific initiation sites and are then released. Sigma B is not essential for sporulation; rather it is required for maximal expression of ctc and csbA which are transcribed in the early stationary phase under conditions inimical to sporulation. May play a role in the ability of the bacterium to adapt to various stresses but is not essential for its survival under these conditions. Positively regulates expression of its own operon. The second most abundant sigma factor, it associates with RNAP core under all growth phases.
Interaction partners:
- Phosphoserine phosphatase RsbX
- Serine-protein kinase RsbW
- Anti-sigma-B factor antagonist
- Phosphoserine phosphatase RsbU
- Serine/threonine-protein kinase RsbT
- RsbT co-antagonist protein RsbRA
- General stress protein Ctc
- RsbT antagonist protein RsbS
- RNA polymerase sigma-H factor
- Anti-sigma F factor
Sequence:
MTQPSKTTKLTKDEVDRLISDYQTKQDEQAQETLVRVYTNLVDMLAKKYSKGKSFHEDLRQVGMIGLLGAIKRYDPVVGKSFEAFAIPTIIGEIKRFLRDKTWSVHVPRRIKELGPRIKMAVDQLTTETQRSPKVEEIAEFLDVSEEEVLETMEMGKSYQALSVDHSIEADSDGSTVTILDIVGSQEDGYERVNQQLMLQSVLHVLSDREKQIIDLTYIQNKSQKETGDILGISQMHVSRLQRKAVKKLREALIEDPSMELM
Protein: Low affinity glucose transporter MstE (Q5B0S0)
Organism: Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) (Aspergillus nidulans)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
Interaction partners:
- Major facilitator superfamily
Sequence:
MGVDIKGLFKPKAEQQEHSQATTPSRTDSIAEKDNGIIDDSPVKYLTWRSFILGIVVSMGGFIFGYSTGQISGFTTMADFKKRFAERQANGEYVFSNVRNGLIVGLLCIGTMIGALVAAPIADRIGRKLSMSFWSIIHIVGIIIQIATDSNWVQIAMGRWVAGLGVGALSSVVPMYQSEAAPRQVRGAMISAFQLFVAFGIFISYIINYGTESIQSTASWRITMGIGFAWPLILGLGALFLPESPRYAYRLGRIDEARKVMAKLYGVEVNHRVVVQEMKDMKDKLEEERAAGVAPWHEVVTGPRMLYRTLLGIALQSLQQLSGANFIFYYGNSIFTSTGLNNSYVTQIILGAVNFGMTLPGLYIVEHFGRRASLMVGGAWMAICFYIWASVGNSVLDLDNPQNTPKAGAAMIVFTCFFIAGFATTWGPIVWSICSEMYPNRSRATSIGIATCANWTWNFLISFFTPFISGSIHFAYGYVFASCCVVGVLIVFFFVNETQGRTLEEVDTMYVLHVVPWKSASWVPDESIVRDLHPGSDANKTEGLGQAEHGEESRPEPVEIRE
Protein: ADP/ATP translocase (ADP,ATP carrier protein) (A0A0S2Z3H3)
Organism: Homo sapiens (Human)
Subcellular location: Membrane {ECO:0000256|RuleBase:RU368008}; Multi-pass membrane protein {ECO:0000256|RuleBase:RU368008}. Mitochondrion inner membrane {ECO:0000256|ARBA:ARBA00004448}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004448}.
Interaction partners:
Sequence:
MGDHAWSFLKDFLAGGVAAAVSKTAVAPIERVKLLLQVQHASKQISAEKQYKGIIDCVVRIPKEQGFLSFWRGNLANVIRYFPTQALNFAFKDKYKQLFLGGVDRHKQFWRYFAGNLASGGAAGATSLCFVYPLDFARTRLAADVGKGAAQREFHGLGDCIIKIFKSDGLRGLYQGFNVSVQGIIIYRAAYFGVYDTAKGMLPDPKNVHIFVSWMIAQSVTAVAGLVSYPFDTVRRRMMMQSGRKGADIMYTGTVDCWRKIAKDEGAKAFFKGAWSNVLRGMGGAFVLVLYDEIKKYV
Protein: Guanine nucleotide exchange factor subunit RGP1 (Reduced growth phenotype protein 1) (Rgp1p) (P16664)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: The RIC1-RGP1 complex acts as a guanine nucleotide exchange factor (GEF), which activates YPT6 by exchanging bound GDP for free GTP. It is thereby required for efficient fusion of endosome-derived vesicles with the Golgi. The RIC1-RGP1 participates in the recycling of SNC1, presumably by mediating fusion of endosomal vesicles with the Golgi compartment.
Subcellular location: Golgi apparatus {ECO:0000269|PubMed:10990452, ECO:0000269|PubMed:11689439}.
Interaction partners:
- Guanine nucleotide exchange factor subunit RIC1
- GTP-binding protein YPT6
- Translation initiation factor eIF2B subunit delta
- Translation initiation factor eIF2B subunit gamma
- Translation initiation factor eIF2B subunit epsilon
- Translation initiation factor eIF2B subunit beta
- Protein SLM4
- GTP-binding protein GTR2
- GTP-binding protein GTR1
- Protein MEH1
Sequence:
MRAHRIDTFLIRENIKLEIIHESNSYFGGEHISIAFRFKHLGSQHELFNYKEKLLTVDKAVEEKLEQQAKVQDDGEGTMENQTWSLKSLLGAFKRTGEPEESVDVDNMKMLNESKMLREKIQKQMYFHQPVTLISGYVQISGVFQYDSEVISESKFKQDEVKMVGLDIVPGHTTNSVLALEDGEHFKGKRNLTNYLNSDYTNVTNGLLFSESGSRGRTGTYNERTLMISNDTSIKTLPLLLIPQTLLFSEISLEPGEVRTFYFKSTKLPKDICPSYSSSKVASINYTLEVGADVLSDDNIEKFSNRVPITIAPYISSNAEQYTSRLDKPAIILKTGNIKELKPRLFTRKVSTASAVSFGRRKSSIIDIDSPLEDNEFVKRVKKNFIELVESNQNVSRDIDELIDLQMGVQFGKDEDSSDPEPNDSHFSNEMVTSAESSLRSDAVTKRRKSYSVRDNISNLEQKMWNDCSLVKSDENSNLLPQLINLQNAYQINRNNETMAKVSLSAPFYKTTDDINLVIELDPITTPLLKVTSLTVSLESFEIINPKYKTEGKGIGSKPKGNSVYEKHFICFDECKSVSVKLLPPRSPTNQITGQFKTDVFQHKWMIGLKFVIIAKTESITLDQFYEDKKGILFHSKENLEGEEFTCYVPIPILCTSEDFMGW
Protein: NADH-cytochrome b5 reductase 3 (B5R) (Cytochrome b5 reductase) (EC 1.6.2.2) (Diaphorase-1) (P07514)
Organism: Bos taurus (Bovine)
Function: Catalyzes the reduction of two molecules of cytochrome b5 using NADH as the electron donor.
Subcellular location: Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:P20070}; Lipid-anchor {ECO:0000250|UniProtKB:P20070}; Cytoplasmic side {ECO:0000250|UniProtKB:P20070}. Mitochondrion outer membrane {ECO:0000250|UniProtKB:P20070}; Lipid-anchor {ECO:0000250|UniProtKB:P20070}; Cytoplasmic side {ECO:0000250|UniProtKB:P20070}.
Interaction partners:
- Cytochrome b5
- Cytochrome b5
- Sulfite oxidase, mitochondrial
- Dihydroorotate dehydrogenase
- Dihydropyrimidine dehydrogenase [NADP
- Cytidine monophosphate-N-acetylneuraminic acid hydroxylase
- Uridine 5'-monophosphate synthase
- NADPH--cytochrome P450 reductase
- NADPH:adrenodoxin oxidoreductase, mitochondrial
Sequence:
MGAQLSTLGHVVLSPVWFLYSLIMKLFQRSTPAITLENPDIKYPLRLIDKEVISHDTRRFRFALPSPEHILGLPVGQHIYLSARIDGNLVIRPYTPVSSDDDKGFVDLVIKVYFKDTHPKFPAGGKMSQYLESMKIGDTIEFRGPNGLLVYQGKGKFAIRPDKKSDPVIKTVKSVGMIAGGTGITPMLQVIRAIMKDPDDHTVCHLLFANQTEKDILLRPELEELRNEHSARFKLWYTVDKAPEAWDYSQGFVNEEMIRDHLPPPEEEPLVLMCGPPPMIQYACLPNLDRVGHPKERCFAF
Protein: Programmed cell death 1 ligand 2 (PD-1 ligand 2) (PD-L2) (PDCD1 ligand 2) (Programmed death ligand 2) (Butyrophilin B7-DC) (B7-DC) (CD antigen CD273) (Q9WUL5)
Organism: Mus musculus (Mouse)
Function: Involved in the costimulatory signal essential for T-cell proliferation and IFNG production in a PDCD1-independent manner. Interaction with PDCD1 inhibits T-cell proliferation by blocking cell cycle progression and cytokine production.
Subcellular location: Cell membrane {ECO:0000250|UniProtKB:Q9BQ51}; Single-pass type I membrane protein {ECO:0000250|UniProtKB:Q9BQ51, ECO:0000305|PubMed:18641123}.
Interaction partners:
- Programmed cell death protein 1
- Cytotoxic T-lymphocyte protein 4
- Programmed cell death 1 ligand 1
- T-lymphocyte activation antigen CD80
- Repulsive guidance molecule B
- Inducible T-cell costimulator
- T-cell surface glycoprotein CD4
- Hepatitis A virus cellular receptor 2 homolog
- T-lymphocyte activation antigen CD86
- Tyrosine-protein phosphatase non-receptor type 11
Sequence:
MLLLLPILNLSLQLHPVAALFTVTAPKEVYTVDVGSSVSLECDFDRRECTELEGIRASLQKVENDTSLQSERATLLEEQLPLGKALFHIPSVQVRDSGQYRCLVICGAAWDYKYLTVKVKASYMRIDTRILEVPGTGEVQLTCQARGYPLAEVSWQNVSVPANTSHIRTPEGLYQVTSVLRLKPQPSRNFSCMFWNAHMKELTSAIIDPLSRMEPKVPRTWPLHVFIPACTIALIFLAIVIIQRKRI
Protein: Coiled-coil-helix-coiled-coil-helix domain containing 10 (Nur77 downstream protein 2) (Q7TNL9)
Organism: Mus musculus (Mouse)
Interaction partners:
- TAR DNA-binding protein 43
- MICOS complex subunit Mic19
- MICOS complex subunit Mic25
- MICOS complex subunit MIC13
- MICOS complex subunit Mic26
- MICOS complex subunit Mic27
- DnaJ homolog subfamily C member 11
- MICOS complex subunit Mic60
- MICOS complex subunit Mic10
- Matrin-3
Sequence:
MPRGSRSAAARPVSRPAPPPAHPPPSAAAPAPAAPGQPGLMAQMASTAAGVAVGSAVGHVMGSALTSAFSGGNSEPAQPAVQQAPARPASHPLQMGPCSYEIKQFLDCSTTQSDLTLCEGFSEALKQCKYNHGLSSLP
Protein: TBC1 domain family member 24 (Q3UUG6)
Organism: Mus musculus (Mouse)
Function: May act as a GTPase-activating protein for Rab family protein(s). Involved in neuronal projections development, probably through a negative modulation of ARF6 function. Involved in the regulation of synaptic vesicle trafficking (By similarity).
Subcellular location: Cell membrane {ECO:0000250|UniProtKB:Q9ULP9}; Peripheral membrane protein {ECO:0000250|UniProtKB:Q9ULP9}. Cytoplasm {ECO:0000250|UniProtKB:Q9ULP9}. Cytoplasmic vesicle membrane {ECO:0000250|UniProtKB:Q9VIH7}. Presynapse {ECO:0000250|UniProtKB:Q9ULP9}. Note=Mainly cytoplasmic with partial expression at the plasma membrane (By similarity). Associates with certain types of membrane phosphoinositides, preferentially those phosphorylated at the D5 position of the inositol ring such as phosphatidylinositol 4,5-bisphosphate (PIP2) and phosphatidylinositol 3,4,5-trisphosphate (PIP3) (By similarity). {ECO:0000250|UniProtKB:Q9ULP9, ECO:0000250|UniProtKB:Q9VIH7}.
Interaction partners:
- Ras-related protein Rab-35
- ADP-ribosylation factor 6
- Cell division cycle protein 16 homolog
Sequence:
MDPPGYNCFVDKDKMDASIQDLGPKELNCTELQELKQLARQGYWAQSHTLRGKVYQRLIRDIPCRTVTPDASVYSDIVGKIVGKHSSSSLPLPEFVDNTQVPTYCLNTRGEGAVRKILLCIANQFPDISFCPALPAVVALLLHYSIDEAECFEKACRILSCNDPTKKLIDQSFLAFESSCMTFGDLVNKYCQAAHKLMVAVSEDVLQVYSDWQRWLFGELPLNYFARVFDVFLVEGYKVLYRVALAILKFFHKVRAGQPLESDNVKQDIRMFVKDIAKTVSPEKLLEKAFAIRLFSRKEIQLLQMANEKALRQKGITVKQKSVSLSKRQFVHLAVHAENFHSEIVSVKEMRDIWSWIPERFALCQPLLLFSSLQHGYSLSRFYFQCEGHEPTLLLIKTTQKEVCGAYLSTDWSERTKFGGKLGFFGTGECFVFRLQPEVQRYEWVVIKHPELTKATSLKSSEAAGSSSLISHCSSDPADRLSPFLAARHFNLPSKTESMFMAGGNDCLIIGGGGGQALYVDGDLNRGRTGHCDTFNNQPLCSENFLIAAVEAWGFQDPDTE
Protein: Metal-binding protein SmbP (Q82S91)
Organism: Nitrosomonas europaea (strain ATCC 19718 / CIP 103999 / KCTC 2705 / NBRC 14298)
Function: Is capable of binding multiple equivalents of a variety of divalent and trivalent metals, including Cu(2+) and Fe(3+) but also Mn(2+), Ni(2+), Mg(2+) and Zn(2+). Is able to bind up to six Cu(2+) atoms. It is proposed to be a metal scavenging protein that has a role in cellular copper management in N.europaea.
Subcellular location: Periplasm {ECO:0000269|PubMed:15366930}.
Interaction partners:
- Ammonia monooxygenase alpha subunit
- Ammonia monooxygenase subunit C
- Ammonia monooxygenase beta subunit
- Outer membrane protein beta-barrel domain-containing protein
- Ammonia monooxygenase subunit C2
- Exosortase-associated protein, TIGR04073 family
- Exosortase-associated protein, TIGR04073 family
- Ammonia monooxygenase 3 subunit C
- Lipoprotein
- Porin
Sequence:
MKTTLIKVIAASVTALFLSMQVYASGHTAHVDEAVKHAEEAVAHGKEGHTDQLLEHAKESLTHAKAASEAGGNTHVGHGIKHLEDAIKHGEEGHVGVATKHAQEAIEHLRASEHKSH
Protein: Trans-O-hydroxybenzylidenepyruvate hydratase-aldolase (THBPA hydratase-aldolase) (EC 4.1.2.45) (2'-hydroxybenzalpyruvate aldolase) (Q51947)
Organism: Pseudomonas putida (Arthrobacter siderocapsulatus)
Function: Involved in the naphthalene upper catabolic pathway. Catalyzes the transformation of trans-O-hydroxybenzylidenepyruvate (THBPA) to salicylaldehyde and pyruvate. The reaction is reversible. Can also use substrate which carry trans-alpha,beta-unsaturated keto acid side chain and adjacent hydroxyl group such as trans-4-(3-hydroxy-2-thianaphthenyl)-2-oxo-but-3-enoate, trans-4-(3-hydroxy-2-benzofuranyl)-2-oxobut-3-enoate, and trans-4-(3-hydroxy-2-thienyl)-2-oxobut-3-enoate.
Interaction partners:
Sequence:
MLNKVIKTTRLTAEDINGAWTIMPTPSTPDASDWRSTNTVDLDETARIVEELIAAGVNGILSMGTFGECATLTWEEKRDYVSTVVETIRGRVPYFCGTTALNTREVIRQTRELIDIGANGTMLGVPMWVKMDLPTAVQFYRDVAGAVPEAAIAIYANPEAFKFDFPRPFWAEMSKIPQVVTAKYLGIGMLDLDLKLAPNIRFLPHEDDYYAAARINPERITAFWSSGAMCGPATAIMLRDEVERAKSTGDWIKAKAISDDMRAADSTLFPRGDFSEFSKYNIGLEKARMDAAGWLKAGPCRPPYNLVPEDYLVGAQKSGKAWAALHAKYSK