wanglab/gogpt-training-data huggingface dataset:
Protein: FI16807p1 (Inwardly rectifying potassium channel 1, isoform B) (A8JR87)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004141, ECO:0000256|RuleBase:RU003822}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004141, ECO:0000256|RuleBase:RU003822}.
Interaction partners:
Sequence:
MSELRRSLSRLSMIVYRATHSSEQSWREELLRYRQTRFSSRRVRKRVVFKHGECNVVQGNVAKRRRRYLQDIFTTLVDAQWRWTLLVFAASFVFSWAFFGFIWWIIAYAHNDLEYTNLKNQSPDLVANITHTVCVTQVSNMMSAFLYSVETQTTIGYGNRYVTEECPEAIFTMCIQCITGVFIQAFMVGIVFAKLSRPKKRAQTLLFSRNAVICHRDGVPCLMFRVGDMRKSHIIEAHVRAQIIRKKVTKEGEVLPFYQQELHIGADGGEDRLMFIWPTTIVHKIDRNSPLYMLSASDMLKERFEVVVMLEGVIESTGMTTQARSSYLPSEVLWGHRFVNVVSFRKETGEYEVDYTLFNNTYDVDTPLCSAKQLDELKSEYSKSAKCVNAPFADRTLSASLFQRIASAASVDHLDPASDESLDSGRLQIRSHSIPNGVLASELEPLNNNKHGASFTMGGLTITTTAPSIPNLSSINEKTNSGNSINSSNYSNNNSLSTLTGGGSAASGPGGGITIVAGSGNHGGAGGGGGGGGRHKSNPRRLSIKQDQLPIDSIC
Protein: Nuclear protein localization protein 4 homolog (Protein NPL4) (Q8TAT6)
Organism: Homo sapiens (Human)
Function: The ternary complex containing UFD1, VCP and NPLOC4 binds ubiquitinated proteins and is necessary for the export of misfolded proteins from the ER to the cytoplasm, where they are degraded by the proteasome. The NPLOC4-UFD1-VCP complex regulates spindle disassembly at the end of mitosis and is necessary for the formation of a closed nuclear envelope (By similarity). Acts as a negative regulator of type I interferon production via the complex formed with VCP and UFD1, which binds to RIGI and recruits RNF125 to promote ubiquitination and degradation of RIGI.
Subcellular location: Cytoplasm, cytosol {ECO:0000250|UniProtKB:Q9ES54}. Endoplasmic reticulum {ECO:0000250|UniProtKB:Q9ES54}. Nucleus {ECO:0000250|UniProtKB:Q9ES54}. Note=Associated with the endoplasmic reticulum and nuclear. {ECO:0000250|UniProtKB:Q9ES54}.
Interaction partners:
- FAS-associated factor 1
- FAS-associated factor 2
- Ubiquitin recognition factor in ER-associated degradation protein 1
- Transitional endoplasmic reticulum ATPase
- UBX domain-containing protein 7
- Deubiquitinating protein VCPIP1
- Polyubiquitin-C
- Tether containing UBX domain for GLUT4
- NSFL1 cofactor p47
- UBX domain-containing protein 10
Sequence:
MAESIIIRVQSPDGVKRITATKRETAATFLKKVAKEFGFQNNGFSVYINRNKTGEITASSNKSLNLLKIKHGDLLFLFPSSLAGPSSEMETSVPPGFKVFGAPNVVEDEIDQYLSKQDGKIYRSRDPQLCRHGPLGKCVHCVPLEPFDEDYLNHLEPPVKHMSFHAYIRKLTGGADKGKFVALENISCKIKSGCEGHLPWPNGICTKCQPSAITLNRQKYRHVDNIMFENHTVADRFLDFWRKTGNQHFGYLYGRYTEHKDIPLGIRAEVAAIYEPPQIGTQNSLELLEDPKAEVVDEIAAKLGLRKVGWIFTDLVSEDTRKGTVRYSRNKDTYFLSSEECITAGDFQNKHPNMCRLSPDGHFGSKFVTAVATGGPDNQVHFEGYQVSNQCMALVRDECLLPCKDAPELGYAKESSSEQYVPDVFYKDVDKFGNEITQLARPLPVEYLIIDITTTFPKDPVYTFSISQNPFPIENRDVLGETQDFHSLATYLSQNTSSVFLDTISDFHLLLFLVTNEVMPLQDSISLLLEAVRTRNEELAQTWKRSEQWATIEQLCSTVGGQLPGLHEYGAVGGSTHTATAAMWACQHCTFMNQPGTGHCEMCSLPRT
Protein: Histone H2A (P84051)
Organism: Drosophila melanogaster (Fruit fly)
Function: Core component of nucleosome. Nucleosomes wrap and compact DNA into chromatin, limiting DNA accessibility to the cellular machineries which require DNA as a template. Histones thereby play a central role in transcription regulation, DNA repair, DNA replication and chromosomal stability. DNA accessibility is regulated via a complex set of post-translational modifications of histones, also called histone code, and nucleosome remodeling.
Subcellular location: Nucleus. Chromosome.
Interaction partners:
- Histone H3.3A
- Histone H3
- Histone H4
- Histone H2B
- Regulator of chromosome condensation
- Polycomb group protein Pc
- Histone H3-like centromeric protein cid
- Histone H1
- LD21576p
- Histone acetyltransferase Tip60
Sequence:
MSGRGKGGKVKGKAKSRSNRAGLQFPVGRIHRLLRKGNYAERVGAGAPVYLAAVMEYLAAEVLELAGNAARDNKKTRIIPRHLQLAIRNDEELNKLLSGVTIAQGGVLPNIQAVLLPKKTEKKA
Protein: Spermatogenesis-associated protein 7 homolog (Q80VP2)
Organism: Mus musculus (Mouse)
Function: Involved in the maintenance of both rod and cone photoreceptor cells. Required for photoreceptor-specific localization of proximal connecting cilium (CC) proteins RPGR, AHI1, NPHP1, NPHP4, and RPGRIP1 at the distal CC, a photoreceptor-specific extension of the primary cilium transition zone. Maintenance of protein localization at the photoreceptor-specific distal CC is essential for normal microtubule stability and to prevent photoreceptor degeneration.
Subcellular location: Cytoplasm, cytoskeleton, cilium axoneme {ECO:0000269|PubMed:29899041}. Cytoplasm, cytoskeleton, cilium basal body {ECO:0000269|PubMed:29100828, ECO:0000269|PubMed:29899041}. Cytoplasm, cytoskeleton {ECO:0000250|UniProtKB:Q9P0W8}. Cell projection, cilium, photoreceptor outer segment {ECO:0000269|PubMed:25398945, ECO:0000269|PubMed:29100828, ECO:0000269|PubMed:29899041}. Note=Localizes to the microtubule network. {ECO:0000250|UniProtKB:Q9P0W8}.
Interaction partners:
- X-linked retinitis pigmentosa GTPase regulator-interacting protein 1
- X-linked retinitis pigmentosa GTPase regulator
- Aryl-hydrocarbon-interacting protein-like 1
- Retinol dehydrogenase 12
- Protein RD3
- Centrosomal protein of 290 kDa
- Nephrocystin-4
- IQ calmodulin-binding motif-containing protein 1
- Tubby-related protein 1
- Lecithin retinol acyltransferase
Sequence:
MDGSRRVRATSVLPRYSPPCLFTGHLSTKSNAFCTDSSSLRLSTLQLVKNHMAIHYNKILSAKAAVDCSIPVSVNTSIKYADQQRREKLRKELARCEKEFKLSKSAMQTNSKMNSKFFVNSLQKPSGEPQDQDVFIEEMTRYPSFSKSLIPSSEGLHLSLPESSKMLMSGTQKHASTSPSRHSGCGHGCDRRPRSAHQFQVALAKTPSGDLLEKHSDLFSNKQSPFTPRTLKTEAKSFLSQYRYYTPAKRRKDFSDQRMEAETQTELSSFNSELGTAEKTSSKDSEVNINQVPNYTRNGAEDKIAPLPSQGQNLAWDSIQDGILQQSSERASCKLSTEFSPDSKIYSDEEELLYLSFMENVTDEILKLGLFSNRFLERLFERHIKKNKHHLEEGKMRYLLHGLKVDLGCISEEDPAKQKHFRMLNQLHFQKALISRENEFVSDEETVSHHERQQYQEALDMLSAVPKDENKMFSLPGEFLIPAHKVKHSEGVIIQQVNDETDNEASPWNENNPSVSDSVIDQETSVDVIEGDSDFERAETSRELCCLSTSLSPSGPFPSINGGSNHGKELSTLRIMGMSIED
Protein: Neurexin-3-beta (E1B6S5)
Organism: Caenorhabditis elegans
Interaction partners:
Sequence:
MMMAHSIDENPNEALIESLAPSCLSLEEQQSCFIDTDDSTGFFSPVLPTVANFPTTRQTEPETTRRPLSPSKMTPSLPSPTTTTLPVFFLSQITDGDESEDEFDGSGDDLFGGDGVGITAATQPSVKRTTSISVVTKVLTTTSEPSSTHRSTVLPRPYASVKEAAEQNPDYLGASIWNQVDTLPEPMVTGPAWRTNKSLTTTATTEASSTKSNRKTTTTTTTSATTTIRIQQRPNYDIDNEVTALITSSLAPQKTRPKSTPHFTVYPVRPTTPMGDTITTTMQAATVTDFPRTPLIMCSSLAVIIAIAAVVFFVFKCRQNPPNSEHYTMAMKSQSGYTAIAPELSPPMNHDRSNDSCTQPLLAKPHINGNGYEPLKGAVIANGNGATATMMRNGNGNGVAKKKDFKEWYV
Protein: NePHronoPhthisis (Human kidney disease) homolog (Nephrocystin-4-like protein) (G5ECP0)
Organism: Caenorhabditis elegans
Interaction partners:
- Nephrocystin-1-like protein
- Protein fantom
- Transmembrane protein 231
- Transmembrane protein 237 homolog
- MecKel-Gruber Syndrome
- B9 domain-containing protein 2
- B9 domain-containing protein 1
- TMEM
- Meckelin
- CEntrosomal Protein
Sequence:
MSVNDWYSLFLANRPVEMKRNVSRGTKALCYSMFISNLTSPQLTENIRYQISAFLFDTKTSQMFGRQCRTEWIPANSNGTCVFNETLYFYSIINSRDVLLILEFVEEGSDEITPATSVGWFSTHIEKKTPVEISNTKIFDIFGGTPKLLIFDKETVLKPVGNVECTYNIFEMPPIFFQCLPEFCIVCDKDIIPGIIKDSSDEWWLSTPKEMPTIPAAIDAIVIQFKNNVPELEKQITHDIEKEWALKEGGTLKPKAIIMDRKLRIGVHNGYTYVTEPFTVDLEIISSNAGDTLRSRKKPIDFGKSSNWEEQLLFQAAGNPRLALRNLYADPRMAIIFLLEYTFHREDNQSLNQTILIGWAAWTPFSDGAFSGKEVETRVSFVGGPRPNPEGVLCYKNVLNQPDSLKPLNEKLEIFVDFKFYENGRSVHNTPTSRRAADSARVQTGRSGDNGQSARSNRKSVKIETPRSPENSNRFPALVDTGRSVSSVDELRSINEDLNRFIEEPMEIPVQDVVVAKKPVEEPLPITSVYKIPFDELKPINFPRSAHSMFARQNFTQLKDRNGSPPNTEDVTLKTIIDMKREQLDRLITSHVYFQFIAFKQLAAPDARMIKKLFFTIGFYRFPDITTESMLLTSMEKGEPTLLTRLDKNGNSDVIASPGFIAKYIIEGEESKADFLDFMASGHATIDVWDSDSLIHLGSTIVPIKNLYRRGREAVQLFIQCPVVDTSLDTSSKAGAFLYMRVANIGFPSGNTYDLSSSSSSLTTTRSNVNSGQGTVVRRLTSSIRLNEEGPHSYRIHAKPLPGNSGVGLDRFLTAQRLDIQQRHEQLFNENSLDKIRQWNDLKEGFNFSDNKEIAQKFIFEEELAAYKKLRYESKPAKLLEAVFKGITSCHQINPSFGEKVFFEFPLENYNSEPINCTIEFDDEALKPVFDAEEWKFYKTVNKVTTPSEKQMMRQTTDRIEICLQPGDVLFIPFIYDAFFFPNDAFNMYSTKVVFRRWDTKEPLAILDLHVHRRNFLLQHSVTFICETSGNWEKQLVLPPMARDRRVLSCRCSDPSVRLTVRNATLQQIVGFTTYSGETNDRKTFLLLMYSDHYQTRLMATWKITILPFFNVDVRSIVGQTTRLHLLVHRRSEHDGVPDDLLKVYTASGCMKVVDSVLTERTPTATIDFTPNFIGTKKLVVSVVNTNTLKLERGFLVYGKSEAPRITQKFVIQIPSSDEAIRKRIPIRNPYGLPKTFRITTSNSDIVKITDSLLSVPPMGKLPCEMYFVKNTHLQKNIETLLYISDAETYVQEEAYSITLAFEAS
Protein: Trophinin (E9Q160)
Organism: Mus musculus (Mouse)
Interaction partners:
Sequence:
MDRRNDHGHRVPTFQGPLPPAGSLGLPFSPDVQSETTEKDPPIASRSKKNKNKKNSIKPMDKTTPAPPPVPSANDNASNKPKVTLQALNLPMFTQISQASATTEAPNIQASVTSQTQKAKTMRVTPKVSLTGSEDATTQLKPPLQALNLPVTTPTIQTPVANESANSLASTAVNKSKKASTANNAANKTVPSAAEISLASAATHTVTTQGQAAKETGSIQTIAATARSKKNSKGKRTPAKTTNTDNEYVEASNAIEASSRQIGASGRQTEASNRQIEASSRQTEASNRQTEASSRQTEASSRQTETSNRQIGASNRQIMASNRQIGASNRQIEASNRQIGASNRQTEVSSRQIEASNRQIGASNRQTEASNRQIGASNRQTEASNRQIGASNRQTDASNRQTDASNRQTEASSRQTEASSRQTEASSRQTEASSRQIEASAAAVRPKKPRGKKGNNKGSNSASEPSEAPPAIQTVTNHALSVTVRIRRGSRARKAANKNRATESQAQIAEQGAQASEASISALETQVAAAVQALADDYLAQLSLEPTTRTRGKRNRKSKHPNGEERTGNNYRRIPWGRRLPPPRDVAILQERANKLVKYLLVKDQTKIPIKRSDMLKDVIQEYEDYFPEIIERASYALEKMFRVNLKEIDKQNNLYILISTQESSAGIMGTTKDTPKLGLLMVILSVIFMNGNKASEAVIWEVLRKLGLHPGVKHSLFGEVKKLITDEFVKQKYLEYKRVPNSRPPEYEFFWGLRSYHETSKMKVLKFACKACSPCLQITLTATILPMEPMCSFGIVVHAAA
Protein: Large ribosomal subunit protein uL11 (50S ribosomal protein L11) (P0A463)
Organism: Streptomyces coelicolor (strain ATCC BAA-471 / A3(2) / M145)
Function: Forms part of the ribosomal stalk which helps the ribosome interact with GTP-bound translation factors.
Interaction partners:
- Large ribosomal subunit protein uL6
- Large ribosomal subunit protein uL3
- Transcription termination/antitermination protein NusG
- Large ribosomal subunit protein bL12
- Large ribosomal subunit protein uL14
- Large ribosomal subunit protein uL1
- Small ribosomal subunit protein uS19
- Small ribosomal subunit protein uS10
- Large ribosomal subunit protein uL13
- Small ribosomal subunit protein uS3
Sequence:
MPPKKKKVTGLIKLQIQAGAANPAPPVGPALGQHGVNIMEFCKAYNAATESQRGWVIPVEITVYEDRSFTFITKTPPAAKMILKAAGVEKGSGEPHKTKVAKITRDQVREIATTKMPDLNANDLDQAEKIIAGTARSMGVTVEG
Protein: non-specific serine/threonine protein kinase (EC 2.7.11.1) (B4DG22)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MDEPMGEEEINPQTEEVSIKEIAITHHVKEGHEKADPSQFELLKVLGQGSFGKVFLVKKISGSDARQLYAMKVLKKATLKVRDRVRTKMERDILVEVNHPFIVKLHYAFQTEGKLYLILDFLRGGDLFTRLSKEVMFTEEDVKFYLAELALALDHLHSLGIIYRDLKPENILLDEEGHIKLTDFGLSKESIDHEKKAYSFCGTVEYMAPEVVNRRGHTQSADWWSFGVLMFEMLTGTLPFQGKDRKETMTMILKAKLGMPQFLSPEAQSLLRMLFKRNPANRLGAGPDGVEEIKRHSFFSTIDWNKLYRREIHPPFKPATGRPEDTFYFDPEFTAKTPKDSPGIPPSANAHQLFRGFSFVAITSDDESQAMQTVGVHSIVQLHRNSIQFTDGYEVKEDIGVGSYSVCKRCIHKATNMEFAVKIIDKSKRDPTEEIEILLRYGQHPNIITLKDVYDDGKYVYVVTELMKGGELLDKILRQKFFSEREASAVLFTITKTVEYLHAQGVVHRDLKPSNILYVDESGNPESIRICDFGFAKQLRAENGLLMTPCYTANFVAPEVLKRQGYDAACDIWSLGVLLYTMLTGYTPFANGPDDTPEEILARIGSGKFSLSGGYWNSVSDTAKDLVSKMLHVDPHQRLTAALVLRHPWIVHWDQLPQYQLNRQDAPHLVKGAMAATYSALNRNQSPVLEPVGRSTLAQRRGIKKITSTAL
Protein: Cytochrome b-c1 complex subunit 9, mitochondrial (Complex III subunit 9) (Complex III subunit X) (Cytochrome c1 non-heme 7.3 kDa protein) (Ubiquinol-cytochrome c oxidoreductase subunit 9) (Ubiquinol-cytochrome c reductase 7.3 kDa protein) (P22289)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Component of the ubiquinol-cytochrome c oxidoreductase, a multisubunit transmembrane complex that is part of the mitochondrial electron transport chain which drives oxidative phosphorylation. The respiratory chain contains 3 multisubunit complexes succinate dehydrogenase (complex II, CII), ubiquinol-cytochrome c oxidoreductase (cytochrome b-c1 complex, complex III, CIII) and cytochrome c oxidase (complex IV, CIV), that cooperate to transfer electrons derived from NADH and succinate to molecular oxygen, creating an electrochemical gradient over the inner membrane that drives transmembrane transport and the ATP synthase. The cytochrome b-c1 complex catalyzes electron transfer from ubiquinol to cytochrome c, linking this redox reaction to translocation of protons across the mitochondrial inner membrane, with protons being carried across the membrane as hydrogens on the quinol. In the process called Q cycle, 2 protons are consumed from the matrix, 4 protons are released into the intermembrane space and 2 electrons are passed to cytochrome c.
Subcellular location: Mitochondrion inner membrane {ECO:0000269|PubMed:18390544, ECO:0000269|PubMed:30598554}; Single-pass membrane protein {ECO:0000269|PubMed:18390544, ECO:0000269|PubMed:30598554}.
Interaction partners:
- Cytochrome c1, heme protein, mitochondrial
- Cytochrome c oxidase subunit 2
- Cytochrome b-c1 complex subunit Rieske, mitochondrial
- Cytochrome c oxidase subunit 3
- Cytochrome c oxidase subunit 13, mitochondrial
- Cytochrome b-c1 complex subunit 1, mitochondrial
- Cytochrome c oxidase subunit 8, mitochondrial
- Cytochrome b
- Cytochrome b-c1 complex subunit 10, mitochondrial
- Cytochrome b-c1 complex subunit 2, mitochondrial
Sequence:
MSFSSLYKTFFKRNAVFVGTIFAGAFVFQTVFDTAITSWYENHNKGKLWKDVKARIAAGDGDDDDE
Protein: Ciliogenesis and planar polarity effector 2 (REM2- and Rab-like small GTPase 1) (A2A825)
Organism: Mus musculus (Mouse)
Function: Potential effector of the planar cell polarity signaling pathway. Plays a role in targeted membrane trafficking most probably at the level of vesicle fusion with membranes. Involved in cilium biogenesis by regulating the transport of cargo proteins to the basal body and to the apical tips of cilia. More generally involved in exocytosis in secretory cells (By similarity).
Subcellular location: Cytoplasm, cytoskeleton, cilium basal body {ECO:0000269|PubMed:29038301}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome, centriole {ECO:0000269|PubMed:29038301}. Note=Localizes at the transition zone, a region between the basal body and the ciliary axoneme. Recruitment to the centriole depends on TTBK2, INTU, and its own GTPase activity. {ECO:0000269|PubMed:29038301}.
Interaction partners:
- Protein inturned
- Protein fuzzy homolog
- WD repeat-containing and planar cell polarity effector protein fritz homolog
- Ras-related protein Rab-23
- Intraflagellar transport protein 22 homolog
Sequence:
MARPPMHGSVIVPDWHETVEGKEYLACILRKNRRREFGLLERPVLPPSVVIDTASYKIFVSGKSGVGKTALVAKLAGLEVPIVHHETTGIQTTVVFWPAKLKASDCVVMFRFEFWDCGESALKKFDHMLPACKENADAFLFLFSFTDRASFEDLPGQLTRVAGEAPGLVKIVIGSKFDQYMHTDVPARDLTAFRQAWELPLFRVKSVPGRRLADGRTLDGRAGLADTAHVLNGLAEQLWHQDQVAAGLLPSSPESAPG
Protein: 1-acylglycerol-3-phosphate O-acyltransferase ABHD5 (EC 2.3.1.51) (Abhydrolase domain-containing protein 5) (Lipid droplet-binding protein CGI-58) (Protein CGI-58) (Q9DBL9)
Organism: Mus musculus (Mouse)
Function: Coenzyme A-dependent lysophosphatidic acid acyltransferase that catalyzes the transfert of an acyl group on a lysophosphatidic acid. Functions preferentially with 1-oleoyl-lysophosphatidic acid followed by 1-palmitoyl-lysophosphatidic acid, 1-stearoyl-lysophosphatidic acid and 1-arachidonoyl-lysophosphatidic acid as lipid acceptor. Functions preferentially with arachidonoyl-CoA followed by oleoyl-CoA as acyl group donors. Functions in phosphatidic acid biosynthesis (By similarity). May regulate the cellular storage of triacylglycerol through activation of the phospholipase PNPLA2. Involved in keratinocyte differentiation (By similarity). Regulates lipid droplet fusion.
Subcellular location: Cytoplasm. Lipid droplet {ECO:0000269|PubMed:18606822}. Cytoplasm, cytosol {ECO:0000269|PubMed:18606822}. Note=Colocalized with PLIN and ADRP on the surface of lipid droplets. The localization is dependent upon the metabolic status of the adipocytes and the activity of PKA.
Interaction partners:
- Perilipin-1
- Patatin-like phospholipase domain-containing protein 2
- Perilipin-5
- Perilipin-2
- Hormone-sensitive lipase
- Perilipin-3
- Omega-hydroxyceramide transacylase
- G0/G1 switch protein 2
- Patatin-like phospholipase domain-containing protein 5
- Monoglyceride lipase
Sequence:
MKAMAAEEEVDSADAGGGSGWLTGWLPTWCPTSTSHLKEAEEKMLKCVPCTYKKEPVRISNGNRIWTLMFSHNISSKTPLVLLHGFGGGLGLWALNFEDLSTDRPVYAFDLLGFGRSSRPRFDSDAEEVENQFVESIEEWRCALRLDKMILLGHNLGGFLAAAYSLKYPSRVSHLILVEPWGFPERPDLADQERPIPVWIRALGAALTPFNPLAGLRIAGPFGLSLVQRLRPDFKRKYSSMFEDDTVTEYIYHCNVQTPSGETAFKNMTIPYGWAKRPMLQRIGGLHPDIPVSVIFGARSCIDGNSGTSIQSLRPKSYVKTIAILGAGHYVYADQPEEFNQKVKEICHTVD
Protein: Ariadne RBR E3 ubiquitin protein ligase 2 (C9JBC5)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MSVDMNSQGSDSNEEDYDPNCEEEEEEEEDDPGDIEDYYVGVASDVEQQGADAFDPEEYQFTCLTYKESEGALNEHMTSLASVLKVSHSVAKLILVNFHWQVSEILD
Protein: Glutathione S-transferase F10 (AtGSTF10) (EC 2.5.1.18) (AtGSTF4) (GST class-phi member 10) (Protein EARLY RESPONSE TO DEHYDRATION 13) (P42761)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: In vitro, possesses glutathione S-transferase activity toward 1-chloro-2,4-dinitrobenzene (CDNB) and benzyl isothiocyanate (BITC). May be involved in the conjugation of reduced glutathione to a wide number of exogenous and endogenous hydrophobic electrophiles and have a detoxification role against certain herbicides.
Subcellular location: Cytoplasm, cytosol {ECO:0000305}.
Interaction partners:
- Methionine--tRNA ligase, cytoplasmic
- Glutathione S-transferase U20
- Glutathione S-transferase U13
- Glutathione S-transferase U19
- Gamma-glutamyl peptidase 1
- Glutathione S-transferase U28
- Glutathione S-transferase U5
- Probable phospholipid hydroperoxide glutathione peroxidase 6, mitochondrial
- Phospholipid hydroperoxide glutathione peroxidase 1, chloroplastic
- Glutathione S-transferase DHAR1, mitochondrial
Sequence:
MVLTIYAPLFASSKRAVVTLVEKGVSFETVNVDLMKGEQRQPEYLAIQPFGKIPVLVDGDYKIFESRAIMRYIAEKYRSQGPDLLGKTIEERGQVEQWLDVEATSYHPPLLALTLNIVFAPLMGFPADEKVIKESEEKLAEVLDVYEAQLSKNEYLAGDFVSLADLAHLPFTEYLVGPIGKAHLIKDRKHVSAWWDKISSRAAWKEVSAKYSLPV
Protein: Troponin T, skeletal muscle (O44556)
Organism: Caenorhabditis elegans
Interaction partners:
Sequence:
MSDEEYSEYEDEEVEEEEVEEVEEAEAEEEEDTEQQEEESGEALNEGEKAMLAAKRRHENDEQAKLEDYEKARRSEREKEEEELEKLKEKQAQRKLAREQEEREAAERKRLDEERRQKEEQERRARAEEEKKRKEEEKLKKAQMMGGGFPGQQGGRNFVIQKKEESAGVGDRFGNIVQAKQEMGMTKEQQEEAKSVAMAGIRKSIAEASTILPNDMKAKIKELHQRICKLEAQKYDLEKRHERQEYDLKELNERSRQVARANNAKNGQVSGDDTGGRHPPKVQISSKYDRQIDRRNFKERRQVYENKIAFPCFPGVAPPPALYEKVIKKMDYEIQQELEAAEEEEDY
Protein: Perilipin (Q6FHZ7)
Organism: Homo sapiens (Human)
Subcellular location: Lipid droplet {ECO:0000256|ARBA:ARBA00004502}.
Interaction partners:
Sequence:
MASVAVDPQPSVVTRVVNLPLVSSTYDLMSSAYLSTKDQYPYLKSVCEMAENGVKTITSVAMTSALPIIQKLEPQIAVANTYACKGLDRIEERLPILNQPSTQIVANAKGAVTGAKDAVTTTVTGAKDSVASTITGVMDKTKGAVTGSVEKTKSVVSGSINTVLGSRMMQLVSSGVENALTKSELLVEQYLPLTEEELEKEAKKVEGFDLVQKPSYYVRLGSLSTKLHSRAYQQALSRVKEAKQKSQQTISQLHSTVHLIEFARKNVYSANQKIQDAQDKLYLSWVEWKRSIGYDDTDESHCAEHIESRTLAIARNLTQQLQTTCHTLLSNIQGVPQNIQDQAKHMGVMAGDIYSVFRNAASFKEVSDSLLTSSKGQLQKMKESLDDVMDYLVNNTPLNWLVGPFYPQLTESQNAQDQGAEMDKSSQETQRSEHKTH
Protein: Two-component response regulator ORR7 (Type A response regulator 7) (OsRR7) (Q4GZK4)
Organism: Oryza sativa subsp. indica (Rice)
Function: Functions as response regulator involved in His-to-Asp phosphorelay signal transduction system. Phosphorylation of the Asp residue in the receiver domain activates the ability of the protein to promote the transcription of target genes. Type-A response regulators seem to act as negative regulators of the cytokinin signaling.
Interaction partners:
Sequence:
MRVPAAVTGGCGCGVDGGGGCCRGGGKLADWEEGKDDEMKSVVVKGWTRMAQVVPLHDNASAEDDDDDEEDDDEDDDDDDDEDDEEEAAPPYVMAVDDSSVDRAVITALLRRSKYRDSGKRALEILGSEPNVSMIITDYWMPEMTGYDLLKKIKESSELKQIPVVIMSSENVPTRISRCLEEGAEDFLLKPVRPADISRITSRMLQ
Protein: LysR-family transcriptional regulator (A0A0H3CCL0)
Organism: Caulobacter vibrioides (strain NA1000 / CB15N) (Caulobacter crescentus)
Interaction partners:
Sequence:
MLLPTLRQLQYLKLLSEHGSFSRAAENAHVTQPTLSAGIQELEKILGAPVVDRARSGVILTAAGQEAVRRAEDILARAEDLVQAARGAGQPLAGRFRLGVIPTVAPYLLPRALPVLRDRFPKLKLFLREDLTHRLIGALKTGALDAALIALPYDMGGLDWAHVEDDELLAAAPANHPMAASTQVDPDSLAGEDLILLEDGHCLRDHALAACGLEPPRGVGEEETFAATSLPTLVQMIGSGLGVSFLPKMAVQAGLTDKAAVTVRPLATAHPSREIVVAWRAGSSRGVEGRLLADTLRQAV
Protein: Mothers against decapentaplegic homolog (MAD homolog) (Mothers against DPP homolog) (SMAD family member) (D3ZAQ2)
Organism: Rattus norvegicus (Rat)
Subcellular location: Cytoplasm {ECO:0000256|RuleBase:RU361195}. Nucleus {ECO:0000256|RuleBase:RU361195}.
Interaction partners:
- E3 ubiquitin-protein ligase
- E3 ubiquitin-protein ligase
- Mothers against decapentaplegic homolog 1
- Mothers against decapentaplegic homolog 7
- Mothers against decapentaplegic homolog 4
- Mothers against decapentaplegic homolog 9
- TGF-beta receptor type-1
- Mothers against decapentaplegic homolog 2
- Mothers against decapentaplegic homolog 3
- Mothers against decapentaplegic homolog 5
Sequence:
MFRSKRSGLVRRLWRSRVVPDREEGSGGGCGGDEDGSLGSRAEPAPRAREGGGCGRSEVRSVAPRRLRDAVGPRGALIAGRRRRTGGPPRPVSEPGAGAGGSPLDVVEPGGPGWLPESDCETVTCCLFSERDAAGAPRDSGDPQARQSPEPEEGGGPRSREARSRLLLLEQELKTVTYSLLKRLKERSLDTLLEAVESRGGVPGGCVLVPRADLRLGGQPAPPQLLLGRLFRWPDLQHAVELKPLCGCHSFAAAADGPTVCCNPYHFSRLCGPESPPPPYSRLSPPDQHKPLDLSDSTLSYTETEATNSLITAPGEFSDASMSPDATKPSHWCSVAYWEHRTRVGRLYAVYDQAVSIFYDLPQGSGFCLGQLNLEQRSESVRRTRSKIGFGILLSKEPDGVWAYNRGEHPIFVNSPTLDAPGGRALVVRKVPPGYSIKVFDFERSGLLQHADAAHGPYDPHSVRISFAKGWGPCYSRQFITSCPCWLEILLNNHR
Protein: LTBP1 protein (A7YY58)
Organism: Bos taurus (Bovine)
Subcellular location: Secreted, extracellular space, extracellular matrix {ECO:0000256|ARBA:ARBA00004498}.
Interaction partners:
Sequence:
MDTKLMCLLFFFSLPPLLVSNHTGRIKVVFTPSICKVTCTKGSCQNSCEKGNTTTLISENGHAADTLTATNFRVVICHLPCMNGGQCSSRDKCQCPPNFTGKLCQIPVHGASLPKVYQHSQQSGKALGTHVVHSTHTLPLTMTSQQGVKVKFPPNIVNIHVKHPPEASVQIHQVSRVDGPTGQKVKEAQPGQSQAPYQGLPVQKTQTVHSSYQQVIPHVYPVAAKTQLGRCFQETIGSQCGKALPGLSKQEDCCGTVGTSWGFHKCQKCPKKPSYHGYNQMMECLQGYKRVNNTFCQDINECQLQGVCPNGECLNTMGSYRCTCKVGFGPDPTFSSCVPDTPVISEEKGPCYRLVSSGRQCMHPLSVHLTKQLCCCSVGKAWGPHCEKCPLPGTAKEEPVEALTFSREQGPGAVEPEVATVPPEKEIPSLDQEKTRLEPGQPQLSPGISTIHLHPQFPVVIEKTSPPMPVEVAPEASTSSASQVIAPTQVTEINECTVNPDICGAGHCINLPVRYTCICYDGYKFNEQQRKCVDIDECAQDQHLCSQGRCENTEGSFLCICPAGFMASEEGTNCIDVDECLRPDVCGEGHCVNTMGAFRCEYCDSGYHMTPGGQCEDVDECLTPSTCPDEQCVNSPGSYQCVPCTEGFRGWNGQCLDVDECLEPKICTNGTCSNLEGSYMCSCHKGYSPTPDHKHCEDIDECQQGTMCMNGQCKNTDGSFRCTCGQGYQLSAAKDQCEDIDECQHHHLCSNGQCRNTEGSFRCVCDHGYRASALGDHCEDINECLEDKSVCQGGDCINTKGSYECTCPDGFQLNDNKGCQDINECEQPGLCGPHGECLNTDSSFHCICEQGFSISADGRTCEDIDECVNNTICDSHGFCDNTAGSFRCLCYQGFQAPQDGQGCVDVNECELLSGVCGEAFCENVEGSFLCVCADESQEYSPMTGQCRSRLSMDSEVDEPREEKKECYYNLNDASLCDNVLAPNVTKQECCCTSGAGWGDNCEIFPCPVPGTAEFTEMCPRGKGFVPSEESSYGVDGENYKDADECLLFGQEICKNGFCMNTQPGYECYCKQGTYYDPVKLQCFDIDECQDPNSCIDGQCINTEGSYNCFCTHPMVLDASEKRCIRPTESHEQIEETDVYQDLCWEHLSDEYVCSRPLVGKQTTYTECCCLYGEAWGMQCALCPMKDSDDYAQLCNIPVTGRRRPYGRDALVDFSEQYAPEADPYFVRDRFLNSFEELQAEECGILNGCENGRCVRVQEGYTCDCFDGYHLDMAKMTCVDVNECDELNNRMSLCKNAKCINTEGSYKCVCLPGFVPSDKPNYCTPLNTALNLEKDSDLE
Protein: T-complex protein 1 subunit zeta (TCP-1-zeta) (Acute morphine dependence-related protein 2) (CCT-zeta-1) (Chaperonin containing T-complex polypeptide 1 subunit 6A) (HTR3) (Tcp20) (P40227)
Organism: Homo sapiens (Human)
Function: Component of the chaperonin-containing T-complex (TRiC), a molecular chaperone complex that assists the folding of proteins upon ATP hydrolysis. The TRiC complex mediates the folding of WRAP53/TCAB1, thereby regulating telomere maintenance. The TRiC complex plays a role in the folding of actin and tubulin (Probable).
Subcellular location: Cytoplasm {ECO:0000269|PubMed:8034610}.
Interaction partners:
- T-complex protein 1 subunit epsilon
- T-complex protein 1 subunit delta
- T-complex protein 1 subunit eta
- T-complex protein 1 subunit gamma
- T-complex protein 1 subunit alpha
- T-complex protein 1 subunit theta
- T-complex protein 1 subunit beta
- Serine/threonine-protein phosphatase 2A 55 kDa regulatory subunit B gamma isoform
- Cell division cycle protein 20 homolog
- Serine/threonine-protein phosphatase 2A catalytic subunit alpha isoform
Sequence:
MAAVKTLNPKAEVARAQAALAVNISAARGLQDVLRTNLGPKGTMKMLVSGAGDIKLTKDGNVLLHEMQIQHPTASLIAKVATAQDDITGDGTTSNVLIIGELLKQADLYISEGLHPRIITEGFEAAKEKALQFLEEVKVSREMDRETLIDVARTSLRTKVHAELADVLTEAVVDSILAIKKQDEPIDLFMIEIMEMKHKSETDTSLIRGLVLDHGARHPDMKKRVEDAYILTCNVSLEYEKTEVNSGFFYKSAEEREKLVKAERKFIEDRVKKIIELKRKVCGDSDKGFVVINQKGIDPFSLDALSKEGIVALRRAKRRNMERLTLACGGVALNSFDDLSPDCLGHAGLVYEYTLGEEKFTFIEKCNNPRSVTLLIKGPNKHTLTQIKDAVRDGLRAVKNAIDDGCVVPGAGAVEVAMAEALIKHKPSVKGRAQLGVQAFADALLIIPKVLAQNSGFDLQETLVKIQAEHSESGQLVGVDLNTGEPMVAAEVGVWDNYCVKKQLLHSCTVIATNILLVDEIMRAGMSSLKG