wanglab/gogpt-training-data huggingface dataset:
Protein: Outer envelope protein 64, mitochondrial (Mitochondrial outer membrane protein 64) (mtOM64) (Translocon at the outer membrane of chloroplasts 64-V) (AtTOC64-V) (F4KCL7)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Chaperone receptor mediating Hsp90-dependent protein targeting to mitochondria.
Subcellular location: Mitochondrion outer membrane {ECO:0000305}; Single-pass membrane protein {ECO:0000305}.
Interaction partners:
- Glutamyl-tRNA
- Mitochondrial import receptor subunit TOM40-1
- Heat shock 70 kDa protein 4
- Aspartate--tRNA ligase, chloroplastic/mitochondrial
- Protein TOC75-3, chloroplastic
- Outer envelope protein 61
- Glutamate--tRNA ligase, chloroplastic/mitochondrial
- Translocase of chloroplast 34, chloroplastic
- Mitochondrial outer membrane import complex protein METAXIN
- Tetratricopeptide repeat
Sequence:
MSNTLSLIQSNASNPKVWVVIGVTVAGIVILAETRKRRIRALREEDFGAFLDRFELLPFPPPPPPAAKQSLSGLTFSISDAFDVKDYITGFGCPQWKKTHEAAEKTAVVVTTLLKNGATCVGKTIMDELGFGIIGENKHYGTPINPLMPDNVPGGCSSGSAVSVGAELVDFSLGIDTTGGVRVPAAFCGILGFRPSQGTVSSVGVLPNSQSLETVGWFASDPSVLCQVGHALLNLSAVTHRRQRSLIFADDLFELSDIPKQKSVQVVRKAIENLSGYKTPKHVNVGQYVASNVPSLAEFCEQSGKSQNSASTLRALSSVMLAIQRHEFKTNHEEWWQTCKSFLGPRFSNDVVTALKSKNESIKSLYRVKNEMRATIQSLLKEDGILVIPTVADPPPRLNTKRNKSLNEFLDRTYALSCIASMSGCCQVTIPLGEHGDRPISVSLLTYYGGDKFLLDTTLDVYASLQDQAKLASNLAPVSDTNGNMEASEVMKEKGNAAYKGKQWNKAVNFYTEAIKLNGANATYYCNRAAAFLELCCFQQAEQDCTKAMLIDKKNVKAYLRRGTARESLVRYKEAAADFRHALVLEPQNKTAKVAEKRLRKHI
Protein: Tyrosine-protein phosphatase non-receptor type 12 (EC 3.1.3.48) (A0A8I5ZN71)
Organism: Rattus norvegicus (Rat)
Subcellular location: Cytoplasm {ECO:0000256|PIRNR:PIRNR000932}.
Interaction partners:
Sequence:
MEQVEILRRFIQRVQAMKSPDHNGEDNFARDFMRLRRLSTKYRTEKIYPTATGEKEENVKKNRYKDILPFDHSRVKLTLKTPSQDSDYINANFIKGVYGPRAYVATQGPLANTVIDFWRMIWEYNVVIIVMACREFEMGRKKCERYWPLYGEDPITFAPFKISCVICTYILLLTECLFFMKESRRLYQFHYVNWPDHDVPSSFDSILDMISLMRKYQEHEDVPICIHCSAGCGRTGAICAIDYTWNLLKAGKIPEEFNVFNLIQEMRTQRHSAVQTKEQYELVHRAIAQLFEKQLQLYEIHGAQKITDGNEISTGNMVSSIDSEKQDSPPPKPPRTRSCLVEGDAKEEILQPPEPHPVPPILTPSPPSAFPTVTTVWQDSDRYHPKPVLHMASPEQPPTDLNRNYDKSADLMGRSESAVEHTDKKLEQNLSFEIKKVPLQEGPKSFDGNTLLNRGHAIKIKSASSSVVDKSSKPQELSSGDLKVHDVSQNSCADCSASHLDNAPESSEESQNSHTPPRPDCLPLDKKGHVTWSLHGPENATPVSDSPDNHSQTLKTVSSTPNSTAEEESHDLTEHHNSSPLPRAPLSFTNPLHSDDSDSDEGNSDGAVTKNKTSISTASATVSPASSTESACTRRVLPMSIARQEMAGRRHSGAEKDADVSEESPPPLPERTPESFVLADMPIRSDWHELPSQECSEHRESEGLITSGNDKHDAGVSHTAACSPTFSDKKEEITESLTEVTDIGFGNRCGKPKGPRDPPSEWT
Protein: Succinate--CoA ligase [ADP-forming] subunit beta (EC 6.2.1.5) (Succinyl-CoA synthetase subunit beta) (SCS-beta) (P53593)
Organism: Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1)
Function: Succinyl-CoA synthetase functions in the citric acid cycle (TCA), coupling the hydrolysis of succinyl-CoA to the synthesis of either ATP or GTP and thus represents the only step of substrate-level phosphorylation in the TCA. The beta subunit provides nucleotide specificity of the enzyme and binds the substrate succinate, while the binding sites for coenzyme A and phosphate are found in the alpha subunit. Can also generate UTP or CTP, although it preferentially synthesizes ATP and/or GTP.
Interaction partners:
- Succinate--CoA ligase subunit alpha
- 2-oxoglutarate dehydrogenase E1 component
- Dihydrolipoyllysine-residue succinyltransferase component of 2-oxoglutarate dehydrogenase complex
- Succinate dehydrogenase cytochrome b556 subunit
- Succinate dehydrogenase flavoprotein subunit
- Succinate dehydrogenase iron-sulfur subunit
- Succinate dehydrogenase hydrophobic membrane anchor subunit
- Citrate synthase
- Citrate synthase
- NADH-quinone oxidoreductase subunit C/D
Sequence:
MNLHEYQGKQLFAEYGLPVSKGFAVDTPEEAAEACDKIGGSEWVVKAQVHAGGRGKAGGVKLVKSKEDAKAFAQQWLGKNLVTYQTDANGQPVSKILVESCTDIDKELYLGAVVDRSSRRIVFMASTEGGVDIEKVAHDTPEKILKATIDPLVGAQPYQGRELAFQLGLKGDQIKQFTHIFVGLAKLFQDYDLALLEVNPLVIKKDGNLHCLDAKINIDSNALYRQPKLRAMHDPSQDDAREAHAQKWELNYVALEGNIGCMVNGAGLAMGTMDIVNLHGGKPANFLDVGGGATKERVTEAFKIILSDSNVKAVLVNIFGGIVRCDMIAEGIIGAVKEVGVKVPVVVRLEGNNAELGAKVLAESGLNIIAATSLTDAAQQVVKAAEGK
Protein: Cyclin-dependent kinase 2 (EC 2.7.11.22) (CDC2 homolog Eg1 protein kinase) (Cell division protein kinase 2) (P23437)
Organism: Xenopus laevis (African clawed frog)
Function: Involved in the control of the cell cycle. Interacts with cyclins A, B, D, or E. Activity of CDK2 is maximal during S phase and G2.
Interaction partners:
Sequence:
MENFQKVEKIGEGTYGVVYKARNRETGEIVALKKIRLDTETEGVPSTAIREISLLKELNHPNIVKLLDVIHTENKLYLVFEFLNQDLKKFMDGSNISGISLALVKSYLFQLLQGLAFCHSHRVLHRDLKPQNLLINSDGAIKLADFGLARAFGVPVRTFTHEVVTLWYRAPEILLGCKFYSTAVDIWSLGCIFAEMITRRALFPGDSEIDQLFRIFRTLGTPDEVSWPGVTTMPDYKSTFPKWIRQDFSKVVPPLDEDGRDLLAQMLQYDSNKRISAKVALTHPFFRDVSRPTPHLI
Protein: B3 domain-containing protein At3g11580 (Protein AUXIN RESPONSE FACTOR 32) (Q8RYD3)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Subcellular location: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00326}.
Interaction partners:
- Protein DA1-related 7
- Protein DA1-related 5
Sequence:
MSVNHYHNTLSLHHHHQNDVAIAQRESLFEKSLTPSDVGKLNRLVIPKQHAEKYFPLNNNNNNGGSGDDVATTEKGMLLSFEDESGKCWKFRYSYWNSSQSYVLTKGWSRYVKDKHLDAGDVVFFQRHRFDLHRLFIGWRRRGEASSSPAVSVVSQEALVNTTAYWSGLTTPYRQVHASTTYPNIHQEYSHYGAVVDHAQSIPPVVAGSSRTVRLFGVNLECHGDAVEPPPRPDVYNDQHIYYYSTPHPMNISFAGEALEQVGDGRG
Protein: Heterogeneous nuclear rnp K-like protein 2 (KH domain-containing protein 1) (P38199)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: RNA-binding protein involved in the correct localization of transcripts in the cell. RNA localization is a widespread mechanism for achieving localized protein synthesis. Required for the asymmetric localization to the daughter cell nucleus of the ASH1 transcript, coding for a specific repressor of transcription. Overexpression inhibits translation of the ASH1 transcript. Involved in the stability of transcripts such as the MTL1 mRNA. Involved in structural and functional organization of telomeric chromatin and regulates silencing at the HMR locus.
Subcellular location: Cytoplasm. Cytoplasm, P-body. Nucleus. Chromosome, telomere.
Interaction partners:
- SWI5-dependent HO expression protein 2
- 60S ribosomal subunit assembly/export protein LOC1
- SWI5-dependent HO expression protein 3
- Pumilio homology domain family member 6
- Protein SCP160
- Transcriptional regulatory protein ASH1
- Myosin-4
- Eukaryotic initiation factor 4F subunit p150
- Nuclear and cytoplasmic polyadenylated RNA-binding protein PUB1
- CCR4-Not complex 3'-5'-exoribonuclease subunit Ccr4
Sequence:
MSQFFEAATPVAIPTNNTNGGSSDAGSAATGGAPVVGTTAQPTINHRLLLSLKEAAKIIGTKGSTISRIRAANAVKIGISEKVPGCSDRILSCAGNVINVANAIGDIVDVLNKRNPENEDAAEGEAEEHYYFHFLNHILPAPSKDEIRDLQQLEDIGYVRLIVANSHISSIIGKAGATIKSLINKHGVKIVASKDFLPASDERIIEIQGFPGSITNVLIEISEIILSDVDVRFSTERSYFPHLKKSSGEPTSPSTSSNTRIELKIPELYVGAIIGRGMNRIKNLKTFTKTNIVVERKDDDDKDENFRKFIITSKFPKNVKLAESMLLKNLNTEIEKRENYKRKLEAAEGDATVVTERSDSASFLEEKEEPQENHDNKEEQS
Protein: NADH dehydrogenase subunit 4L (Q2F967)
Organism: Oryza sativa subsp. indica (Rice)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
Interaction partners:
Sequence:
MDPIKYFTFSMIISILGIRGILLNRRNILIMSMPIESMLLAVNLNFLVFSVSLDDMMGQSFASLVPTVAAAESAIGLAIFVITFRVRGTIAVEFINCIQG
Protein: Capsid decoration protein (Auxiliary protein D) (Gene product D) (gpD) (Major capsid protein D) (P03712)
Organism: Escherichia phage lambda (Bacteriophage lambda)
Function: Stabilizes the expansion of the capsid head shell after genome packaging. The packaging of viral genome in the procapsid triggers a dramatic reconfiguration of the capsid shell, expanding from roughly 50nm to 60nm while the capsid thickness decreases. 415 capsid decoration protein molecules cooperatively bind the expanded capsid, thereby stabilizing the mature capsid shell.
Subcellular location: Virion. Host cytoplasm.
Interaction partners:
Sequence:
MTSKETFTHYQPQGNSDPAHTATAPGGLSAKAPAMTPLMLDTSSRKLVAWDGTTDGAAVGILAVAADQTSTTLTFYKSGTFRYEDVLWPEAASDETKKRTAFAGTAISIV
Protein: Cytochrome P450 monooxygenase paxP (EC 1.-.-.-) (Paxilline synthesis protein P) (Q9C449)
Organism: Penicillium paxilli
Function: Cytochrome P450 monooxygenase; part of the ATM2 gene cluster that mediates the biosynthesis of paxilline, a mycotoxin that acts as an inhibitor of mammalian maxi-K channels. PaxG, the geranylgeranyl diphosphate (GGPP) synthase is proposed to catalyze the first step in paxilline biosynthesis. Condensation of indole-3-glycerol phosphate with GGPP by paxC then forms 3-geranylgeranylindole (3-GGI), followed by epoxidation and cyclization of this intermediate (by paxM and paxB) to form paspaline. Paspaline is subsequently converted to 13-desoxypaxilline by paxP, the latter being then converted to paxilline by paxQ. Finally paxilline can be mono- and di-prenylated by paxD. PaxP can also utilized beta-paxitriol and alpha-PC-M6 as substrates converting them to paxilline.
Subcellular location: Membrane {ECO:0000255}; Single-pass membrane protein {ECO:0000255}.
Interaction partners:
Sequence:
MDLSDFHISTPLRYFHEEASLLWKLGVFAVLVYFLLPKPTYKTNVKVPTVKYMGPWMPEILSRIFFNSHAPTVIYKGYEKFKTSAFKVVKPDGDLVVLSTRYAEELRQMPSTTLNALEATFTDHVGGYTTILTDSHLHTETIQKKLTPAIGRLIPRMISELDHAFEVEFPTCDDQFASINPYTVFLRLVARVGARIFIGDELCREEKWLQASIDYTKNIFLTIALMRPMPGFLHPIVGRILPSSRSLKDQLSYIQQDLLGPVIKERRRLEASSDSEYKKPDDFLQWMMDLAQNENESHPDNLSHRLLGITSMAVVHTSAMSMTHILYDLLTMPDLIEPLRDEIRNEIKDWNKATQADLSRLIIMDSFLKESQRLNPPGDLSFHRVVKKDLTLSDGLFLPKGTHICMAAGPISKDPDVVSDPDTFDAFRFVKQRTATSGFVSTGPNNMHFGLGRYACPGRFFAAFVIKLILSRFLMDYDFKFETEHKERPKNLLIGDKIVPNVATPILIKRRATKA
Protein: Protein Atg16l2 (APG16-like 2) (Autophagy-related protein 16-2) (Q6KAU8)
Organism: Mus musculus (Mouse)
Function: May play a role in regulating epithelial homeostasis in an ATG16L1-dependent manner.
Subcellular location: Cytoplasm, cytosol {ECO:0000269|PubMed:22082872}. Note=Also localizes to discrete punctae along the ciliary axoneme. {ECO:0000269|PubMed:24089209}.
Interaction partners:
- Autophagy protein 5
- Ubiquitin-like protein ATG12
- Ubiquitin-like-conjugating enzyme ATG3
- WD repeat domain phosphoinositide-interacting protein 1
- WD repeat domain phosphoinositide-interacting protein 2
- RB1-inducible coiled-coil protein 1
- Ras-related protein Rab-33B
- Autophagy-related protein 16-1
- Serine/threonine-protein kinase ULK2
- Autophagy-related protein 9B
Sequence:
MAGPGAPCDPCAPAAVWKRHIVRQLRHRDRTQKALFLELVPAYNHLLEKAELLAKFSEKLKSEPKDAISTRHEDWREEVSGTGPDQVSSPASLRVKWQQEKKGLQLVCGEMAYQVVKKSAALDTLQSQLEERQDRLEALQACVVQLQEARAQQSRQLEERQAENAAQREAYETLLQQAVHQEAALRRLQEEARDLLEQLVQRKARAAAERNLRNERRERANQALVSQELKKAAKRTVSISEIPNTLEDGTKEETVALAPAALPEFSESETCEKWKRPFRSASATSLTLSRCVDVVKGLLDFKKRRGHSVGGAPEQRYQSIPVCVSAQIPSQAQDVLDAHLSEVNAVCFGPNSSLLATGGADRLIHLWNVVGGRLEANQTLEGAGGSITSVDFDPSGSQVLAATYNQAAQLWKVGETQSKETLSGHKDKVTAAKFKLTRHQAVTGSRDRTVKEWDLGRAYCSRTINVLSYCNDVVCGDHIIISGHNDQKIRFWDSRGPHCIQVIPVQGRVTSLHLSYDQLHLLSCSRDNTLKVIDLRISNIRQVFRADGFKCSSDWTKAVFSPDRSYALAGSSNGDLYIWDVNTGKLETSLQGPHCTAVNAVAWCFSGNHVVSVDQGRKVVLWH
Protein: Putative phospholipase B-like 2 (EC 3.1.1.-) (66.3 kDa protein) (76 kDa protein) (p76) (LAMA-like protein 2) (Lamina ancestor homolog 2) (Phospholipase B domain-containing protein 2) [Cleaved into: Putative phospholipase B-like 2 28 kDa form; Putative phospholipase B-like 2 40 kDa form; Putative phospholipase B-like 2 15 kDa form] (Q3TCN2)
Organism: Mus musculus (Mouse)
Function: Putative phospholipase.
Subcellular location: Lysosome lumen {ECO:0000269|PubMed:17007843, ECO:0000269|PubMed:17105447}.
Interaction partners:
Sequence:
MAAPVDGSSGGWAARALRRALALTSLTTLALLASLTGLLLSGPAGALPTLGPGWQRQNPDPPVSRTRSLLLDAASGQLRLEDGFHPDAVAWANLTNAIRETGWAYLDLSTNGRYNDSLQAYAAGVVEASVSEELIYMHWMNTVVNYCGPFEYEVGYCEKLKNFLEANLEWMQREMELNPDSPYWHQVRLTLLQLKGLEDSYEGRLTFPTGRFTIKPLGFLLLQISGDLEDLEPALNKTNTKPSLGSGSCSALIKLLPGGHDLLVAHNTWNSYQNMLRIIKKYRLQFREGPQEEYPLVAGNNLVFSSYPGTIFSGDDFYILGSGLVTLETTIGNKNPALWKYVQPQGCVLEWIRNVVANRLALDGATWADVFKRFNSGTYNNQWMIVDYKAFLPNGPSPGSRVLTILEQIPGMVVVADKTAELYKTTYWASYNIPYFETVFNASGLQALVAQYGDWFSYTKNPRAKIFQRDQSLVEDMDAMVRLMRYNDFLHDPLSLCEACNPKPNAENAISARSDLNPANGSYPFQALHQRAHGGIDVKVTSFTLAKYMSMLAASGPTWDQCPPFQWSKSPFHSMLHMGQPDLWMFSPIRVPWD
Protein: Phosphoribosyl 1,2-cyclic phosphate phosphodiesterase (EC 3.1.4.55) (Phosphoribosyl cyclic phosphodiesterase) (P16692)
Organism: Escherichia coli (strain K12)
Function: Catalyzes the hydrolysis of the cyclic ribose-phosphate to form alpha-D-ribose 1,5-bisphosphate.
Interaction partners:
- Alpha-D-ribose 1-methylphosphonate 5-phosphate C-P lyase
- Alpha-D-ribose 1-methylphosphonate 5-triphosphate diphosphatase
- Ribose 1,5-bisphosphate phosphokinase PhnN
- Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL
- Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnH
- Putative phosphonates utilization ATP-binding protein PhnK
- Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnG
- Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnI
- Aminoalkylphosphonate N-acetyltransferase
- Probable transcriptional regulator PhnF
Sequence:
MSLTLTLTGTGGAQGVPAWGCECAACARARRSPQYRRQPCSGVVKFNDAITLIDAGLHDLADRWSPGSFQQFLLTHYHMDHVQGLFPLRWGVGDPIPVYGPPDEQGCDDLFKHPGLLDFSHTVEPFVVFDLQGLQVTPLPLNHSKLTFGYLLETAHSRVAWLSDTAGLPEKTLKFLRNNQPQVMVMDCSHPPRADAPRNHCDLNTVLALNQVIRSPRVILTHISHQFDAWLMENALPSGFEVGFDGMEIGVA
Protein: Probable ATP-dependent RNA helicase DDX28 (EC 3.6.4.13) (Mitochondrial DEAD box protein 28) (Q9CWT6)
Organism: Mus musculus (Mouse)
Function: Plays an essential role in facilitating the proper assembly of the mitochondrial large ribosomal subunit and its helicase activity is essential for this function. May be involved in RNA processing or transport. Has RNA and Mg(2+)-dependent ATPase activity (By similarity).
Subcellular location: Nucleus {ECO:0000250|UniProtKB:Q9NUL7}. Mitochondrion {ECO:0000250|UniProtKB:Q9NUL7}. Mitochondrion matrix, mitochondrion nucleoid {ECO:0000250|UniProtKB:Q9NUL7}. Mitochondrion matrix {ECO:0000250|UniProtKB:Q9NUL7}. Note=Transported between these two compartments. Nuclear localization depends on active RNA polymerase II transcription. Localizes to mitochondrial RNA granules found in close proximity to the mitochondrial nucleoids (By similarity). {ECO:0000250|UniProtKB:Q9NUL7}.
Interaction partners:
- rRNA methyltransferase 3, mitochondrial
- Mitochondrial assembly of ribosomal large subunit protein 1
- Neuroguidin
- Something about silencing protein 10
- GTP-binding protein 10
- ESF1 homolog
- Pseudouridylate synthase RPUSD4, mitochondrial
- Transcription termination factor 3, mitochondrial
- Mitochondrial ribosome-associated GTPase 1
- Large ribosomal subunit protein uL4m
Sequence:
MALAGPSRLLALAVRLLLEPRRNLVVRGSDQSLPVVRVPRALQRRQEQRQSGRGSLQRPVLVRPGPLLVSARRPELNQPARLTLGRWERAPLASRGWKHRRSRQDHFSIERVQQEAPALRNLSSRGSFVDLGLEPRVLLALQEAVPEVVQPTSVQSKTIPPLLRGRHLLCAAETGSGKTLSYLLPLFQRLLRGSDLDSRSFTAPRGLVLVPSRELAEQVQAVAQSLGGYLGLQVIELGGGLGMSRLKLQLYRRPAADVLVATPGALWKALKSQLISLQHLNFIVLDEVDTLLDESFLELVDYILEKSPIAESPAELEDPFNPKAQLVLVGATFPEGLNQLLSKVTSPDSLTTITSSKLHCLMPHVRQTFMRLKGADKVTELVQILKQQDKASKTEPSGTVLVFCNSASTVNWLGYILDDHKIQHLRLQGQMPASMRAGIFQSFQKGSQNILVCTDIASRGLDSVHVEVVINYDFPPTLQDYIHRAGRVGRVGSEVPGSVISFVTHPWDVSLVQKIELAARRRRSLPGLASSVGDPLPQKA
Protein: Polycomb group protein ASXL1 (Additional sex combs-like protein 1) (P59598)
Organism: Mus musculus (Mouse)
Function: Probable Polycomb group (PcG) protein involved in transcriptional regulation mediated by ligand-bound retinoic acid receptors (RARs) and peroxisome proliferator-activated receptor gamma (PPARG). Acts as a coactivator of RARA and RXRA through association with NCOA1. Acts as a corepressor for PPARG and suppresses its adipocyte differentiation-inducing activity. Non-catalytic component of the PR-DUB complex, a complex that specifically mediates deubiquitination of histone H2A monoubiquitinated at 'Lys-119' (H2AK119ub1) (By similarity). Acts as a sensor of N(6)-methyladenosine methylation on DNA (m6A): recognizes and binds m6A DNA, leading to its ubiquitination and degradation by TRIP12, thereby inactivating the PR-DUB complex and regulating Polycomb silencing (By similarity).
Subcellular location: Nucleus {ECO:0000305}.
Interaction partners:
- Ubiquitin carboxyl-terminal hydrolase BAP1
- Histone-lysine N-methyltransferase EZH2
- Polycomb protein Suz12
- Forkhead box protein K1
- UDP-N-acetylglucosamine--peptide N-acetylglucosaminyltransferase 110 kDa subunit
- Host cell factor 1
- Methylcytosine dioxygenase TET2
- Lysine-specific histone demethylase 1B
- Transcriptional repressor protein YY1
- Forkhead box protein K2
Sequence:
MKDKQKRKKERTWAEAARLVLENYSDAPMTPKQILQVIEAEGLKEMRSGTSPLACLNAMLHSNSRGGEGLFYKLPGRISLFTLKKDAVQWSRNAATVDGDEPEDSADVESCGSNEASTVSGENDVSLDETSSNASCSTESQSRPLSNPRDSHRASSQANKQKKRTGVMLPRVVLTPLKVNGAHVEPASGFSGRHADGESGSPSSSSSGSLALGNSAIRGQAEVTRDPAPLLRGFRKPATGQMKRNRGEEVDFETPGSILVNTNLRALINSRTFHALPLHFQQQLLLLLPEVDRQVGTDGLLRLSGSALNNEFFTHAAQSWRERLADGEFTHEMQVRLRQEMEKEKKVEQWKEKFFEDYYGQKLGLTKEESLQQKEVQEEAKVKSGLCVSGESVRPQRGPNTRQRDGHFKKRSRPDLRTRSRRNIYKKQEPEQAGVAKDASAAPDVSLSKDTKTDLAGVNSTPGPDVSSATSGQEGPKCPSEPVASQIQAERDNLACASASPDRIPTLPQDTVDQETKDQKRKSFEQEASASFPEKKPRLEDRQSFRNTIESVHTEKPQPTKEEPKVPPIRIQLSRIKPPWVAKGRPTYQICPRIVPITESSCRGWTGARTLADIKARALQARGARGYHCNRETATTAIGGGGGPGGGGSGAIDEGGGRDSSSGDGSEACGHPEPRGAPSTSGESASDLQRTQLLPPCPLNGEHTPAEAAMPRARREDSASLRKEESCLLKRVPGVLTSGLEDASQPPIAPTGDQPCQALPPLSSQTPVAEMLTEQPKLLLDDRTECESSREDQGPTIPSESSSGRFPLGDLLGGGSDQAFDNMKEPVSMTPTFISELSLANYLQDRPDDDGLGLGATGLLIRESSRQEALTEAFASGSPTSWVPILSNYEVIKTSDPESRENIPCPEPQDEKEWERAVPLIAATESVPQPESCISHWTPPPAAVGSTGSDSEQVDLERLEMNGISEAPSPHSESTDTASDSEGHLSEDSSEVDASEVTVVKGSLGGDEKQDWDPSASLSKVNNDLSVLTRTGGVAASQSWVSRVCSVPHKIPDSLLLSSTECQPRSVCPLRPGSSVEVTNPLVMHLLHGNLPLEKVLPPGHRSSRLESSQLPLREQSQDRGTLQGTGENNRLAARINPGSAQTLKESILAQSYGASAGLVRAMASKAPAMSQKIAKMVTSLDSQHPETELTPSSGNLEEIDSKEHLSSFLCEEQKEGHSLSQGSDPGAAPGQCLGDHTTSKVPCFSSTNVSLSFGSEQTDGTLSDQNNAGGHEKKLFGPGNTVTTLQCPRSEEQTPLPAEVPPVFPSRKIEPSKNSVSGGVQTTRENRMPKPPPVSADSIKTEQTFLRDPIKADAENRKAAGYSSLELVGHLQGMPFVVDLPFWKLPREPGKGFSQPLEPSSIPSQLNIKQALYGKLSKLQLSPTSFNYSSSSATFPKGLAGGVVQLSHKASFGTGHTASLSLQMFADSSAVESISLQCACSLKAMIMCQGCGAFCHDDCIGPSKLCVLCLVVR
Protein: Salivary gland-derived secreted factor (A0A0B4LH27)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
- Uncharacterized protein, isoform A
Sequence:
MSARRHSGIILVLCCINLSYSYRIIESNEVPKTCPALNKDIIFEEPHLNNNQREFYDVREIPRRLHFNSNKKEIQSENWLLRIIRIKTINDGPRHKVTEIKEDKHMDGFAKRLFNILKKTLKMHEPSYKHNNDQKDLFVLKKNHFPPEHHIVKREPVHYNYM
Protein: TIL domain-containing protein (A1ZAJ3)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
- Seminal fluid protein 84E
- GEO11741p1
- Aquarius
Sequence:
MMAWPKVYFVVQLIGILFQKHVLMAEDSAEDQITWPDDIAEPTLESELTWPNELPVTVTNGMTFRTARTLDHFDALRDDDEFMENPHKKVFDEFDSLEHRYHIVHPIGEEIALKRNPLPEEKYIKQPFKFGCCHNSTYVGCAGVCPETCEYRSKYCVPLCGPPCRCKRGYVYNIPHSACTLRSDCPKGIVQSKNGIYRVFL
Protein: AT09608p (Q7JUS1)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MSLFAFLKSRTAFWLSFTGTTTGLAFFVKDLMQGGQFTKETNETGKVFIVTGANTGIGKETVREIAKRGGTVYMACRNLKKCEEAREEIVLETKNKYVYCRQCDLASQESIRHFVAAFKREQEHLHVLINNAGVMRCPRSLTSDGIELQLGVNHMGHFLLTNLLLDLLKKSSPSRIVNVSSLAHTRGEINTGDLNSDKSYDEGKAYSQSKLANVLFTRELAKRLEGTNVTANALHPGVVDTEIIRHMGFFNNFFAGLFVKPLFWPFVKTPRNGAQTSLYVALDPELEKVTGQYFSDCKLKEMAPAATDTQTAKWLWAVSEKWTKPTMIKIQ
Protein: SH3 domain-binding protein 5 (SH3BP-5) (Vascular endothelial cell-specific protein 18) (Q91Y80)
Organism: Rattus norvegicus (Rat)
Function: Functions as guanine nucleotide exchange factor (GEF) with specificity for RAB11A and RAB25. Inhibits the auto- and transphosphorylation activity of BTK. Plays a negative regulatory role in BTK-related cytoplasmic signaling in B-cells. May be involved in BCR-induced apoptotic cell death.
Subcellular location: Cytoplasmic vesicle membrane {ECO:0000250|UniProtKB:O60239}; Peripheral membrane protein {ECO:0000250|UniProtKB:O60239}. Mitochondrion {ECO:0000269|PubMed:15158451}. Note=Colocalizes with RAB11A on cytoplasmic vesicle membranes. {ECO:0000250|UniProtKB:O60239}.
Interaction partners:
- Ras-related protein Rab-11A
- Ras-related protein Rab-11B
Sequence:
MDTALKRSRSEEPVELPPPAREAEEKEEEEERMEQGLEEEEEVDPRIQGELEKLNQSTDDINRRETELEDARQKFRSVLVEATVKLDELAKKIGKAVEDSKPYWEARRVARQAQLEAQKATQDFQRATEVLRAAKETISLAEQRLLEDDKRQFDSAWQEMLNHATQRVMEAEQTKTRSELVHKETAARYNAAMGRMRQLEKKLKRAINKSKPYFELKAKYYVQLEQLKKTVDDLQAKLALAKGEYKAALKSLERISDEIHERRRSNAMGPRGCGVGAEGSITSVENLPASKPEPDAISVASEAFEDDNCGNLVSEDDSETQSVSSFSSGPTSPSEMPDQFPAVARPGSLDLPSPVSLSEFGMMFPILGPRSECSGASSPECEVERGDRAEGAENKMSDKANNNRVLSSTSAGGGRSRSQSSTSLEGQALETRMKQLSLQCSKGREGIIADIKTVQIG
Protein: Progonadoliberin [Cleaved into: Gonadoliberin (Gonadotropin-releasing hormone) (GnRH) (Luliberin) (Luteinizing hormone-releasing hormone) (LH-RH); GnRH-associated peptide (GnRH-associated peptide)] (A0A068PF27)
Organism: Coturnix japonica (Japanese quail) (Coturnix coturnix japonica)
Subcellular location: Secreted {ECO:0000256|ARBA:ARBA00004613, ECO:0000256|RuleBase:RU000635}.
Interaction partners:
Sequence:
LAQHWSYGLQPGGKRNAENLVESFQEIANEMENLREVKEAECP
Protein: Palmitoyltransferase ZDHHC3 (EC 2.3.1.225) (Acyltransferase ZDHHC3) (EC 2.3.1.-) (GABA-A receptor-associated membrane protein 1) (Golgi-specific DHHC zinc finger protein) (Zinc finger DHHC domain-containing protein 3) (DHHC-3) (Q8R173)
Organism: Mus musculus (Mouse)
Function: Golgi-localized palmitoyltransferase that catalyzes the addition of palmitate onto various protein substrates. Has no stringent fatty acid selectivity and in addition to palmitate can also transfer onto target proteins myristate from tetradecanoyl-CoA and stearate from octadecanoyl-CoA (Probable). Plays an important role in G protein-coupled receptor signaling pathways involving GNAQ and potentially other heterotrimeric G proteins by regulating their dynamic association with the plasma membrane. Palmitoylates ITGA6 and ITGB4, thereby regulating the alpha-6/beta-4 integrin localization, expression and function in cell adhesion to laminin (By similarity). Plays a role in the TRAIL-activated apoptotic signaling pathway most probably through the palmitoylation and localization to the plasma membrane of TNFRSF10A (By similarity). In the brain, by palmitoylating the gamma subunit GABRG2 of GABA(A) receptors and regulating their postsynaptic accumulation, plays a role in synaptic GABAergic inhibitory function and GABAergic innervation. Palmitoylates the neuronal protein GAP43 which is also involved in the formation of GABAergic synapses. Palmitoylates NCDN thereby regulating its association with endosome membranes. Probably palmitoylates PRCD and is involved in its proper localization within the photoreceptor. Could mediate the palmitoylation of NCAM1 and regulate neurite outgrowth. Could palmitoylate DNAJC5 and regulate its localization to Golgi membranes. Also constitutively palmitoylates DLG4. May also palmitoylate SNAP25. Could palmitoylate the glutamate receptors GRIA1 and GRIA2 but this has not been confirmed in vivo. Could also palmitoylate the D(2) dopamine receptor DRD2 (By similarity).
Subcellular location: Golgi apparatus membrane {ECO:0000269|PubMed:12163046, ECO:0000269|PubMed:15229235, ECO:0000269|PubMed:16129400, ECO:0000269|PubMed:18596047}; Multi-pass membrane protein {ECO:0000255}. Note=Localizes to the Golgi cis cisterna. {ECO:0000269|PubMed:27875292}.
Interaction partners:
Sequence:
MMLIPTHHFRDIERKPEYLQPEKCAPPPFPGPAGAMWFIRDGCGIACAIVTWFLVLYAEFVVLFVMLVPSRDYAYSIINGIVFNLLAFLALASHCRAMLTDPGAVPKGNATKEFIESLQLKPGQVVYKCPKCCSIKPDRAHHCSVCKRCIRKMDHHCPWVNNCVGENNQKYFVLFTMYIALISLHALIMVGFHFLHCFEEDWTKCSSFSPPTTVILLILLCFEALLFLIFTSVMFGTQVHSICTDETGIEQLKKEERRWAKKTKWMNMKAVFGHPFSLGWASPFATPDQGKADPYQYVV
Protein: HLA class II histocompatibility antigen DP alpha chain (HLA-DPA1*01:03:01:New) (MHC class II antigen) (X5CKE2)
Organism: Homo sapiens (Human)
Subcellular location: Endosome membrane {ECO:0000256|ARBA:ARBA00004530}; Single-pass type I membrane protein {ECO:0000256|ARBA:ARBA00004530}. Lysosome membrane {ECO:0000256|ARBA:ARBA00004352}; Single-pass type I membrane protein {ECO:0000256|ARBA:ARBA00004352}.
Interaction partners:
Sequence:
MRPEDRMFHIRAVILRALSLAFLLSLRGAGAIKADHVSTYAAFVQTHRPTGEFMFEFDEDEMFYVDLDKKETVWHLEEFGQAFSFEAQGGLANIAILNNNLNTLIQRSNHTQATNDPPEVTVFPKEPVELGQPNTLICHIDKFFPPVLNVTWLCNGELVTEGVAESLFLPRTDYSFHKFHYLTFVPSAEDFYDCRVEHWGLDQPLLKHWEAQEPIQMPETTETVLCALGLVLGLVGIIVGTVLIIKSLRSGHDPRAQGTL