wanglab/gogpt-training-data huggingface dataset:
Protein: Heme-binding protein 2 (Placental protein 23) (PP23) (Protein SOUL) (Q9Y5Z4)
Organism: Homo sapiens (Human)
Function: Can promote mitochondrial permeability transition and facilitate necrotic cell death under different types of stress conditions.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:17098234}. Mitochondrion {ECO:0000269|PubMed:17098234}. Note=Mainly localized to the cytoplasm with a much lower abundance in the mitochondrion. {ECO:0000269|PubMed:17098234}.
Interaction partners:
- Programmed cell death protein 6
- Chromatin remodeling regulator CECR2
- Leucine-rich PPR motif-containing protein, mitochondrial
- Protein UXT
- Microtubule-associated protein 1S
- Bcl-2-like protein 1
- Transcription elongation factor A protein-like 1
Sequence:
MAEPLQPDPGAAEDAAAQAVETPGWKAPEDAGPQPGSYEIRHYGPAKWVSTSVESMDWDSAIQTGFTKLNSYIQGKNEKEMKIKMTAPVTSYVEPGSGPFSESTITISLYIPSEQQFDPPRPLESDVFIEDRAEMTVFVRSFDGFSSAQKNQEQLLTLASILREDGKVFDEKVYYTAGYNSPVKLLNRNNEVWLIQKNEPTKENE
Protein: Signal-induced proliferation-associated protein 1 (Sipa-1) (GTPase-activating protein Spa-1) (p130 SPA-1) (Q96FS4)
Organism: Homo sapiens (Human)
Function: GTPase activator for the nuclear Ras-related regulatory proteins Rap1 and Rap2 in vitro, converting them to the putatively inactive GDP-bound state. Affects cell cycle progression (By similarity).
Subcellular location: Nucleus {ECO:0000269|PubMed:9346962}. Cytoplasm, perinuclear region {ECO:0000269|PubMed:9346962}. Endomembrane system; Peripheral membrane protein {ECO:0000269|PubMed:9346962}. Note=Mostly localized in the perinuclear membraneous region. {ECO:0000269|PubMed:9346962}.
Interaction partners:
- Afadin
- Ras-related protein Rap-1A
- Ras-related protein Rap-1b
- Ribosomal RNA processing protein 1 homolog B
- Bromodomain-containing protein 4
- Ras-related protein Rap-2a
Sequence:
MPMWAGGVGSPRRGMAPASTDDLFARKLRQPARPPLTPHTFEPRPVRGPLLRSGSDAGEARPPTPASPRARAHSHEEASRPAATSTRLFTDPLALLGLPAEEPEPAFPPVLEPRWFAHYDVQSLLFDWAPRSQGMGSHSEASSGTLASAEDQAASSDLLHGAPGFVCELGGEGELGLGGPASPPVPPALPNAAVSILEEPQNRTSAYSLEHADLGAGYYRKYFYGKEHQNFFGMDESLGPVAVSLRREEKEGSGGGTLHSYRVIVRTTQLRTLRGTISEDALPPGPPRGLSPRKLLEHVAPQLSPSCLRLGSASPKVPRTLLTLDEQVLSFQRKVGILYCRAGQGSEEEMYNNQEAGPAFMQFLTLLGDVVRLKGFESYRAQLDTKTDSTGTHSLYTTYQDHEIMFHVSTMLPYTPNNQQQLLRKRHIGNDIVTIVFQEPGSKPFCPTTIRSHFQHVFLVVRAHTPCTPHTTYRVAVSRTQDTPAFGPALPAGGGPFAANADFRAFLLAKALNGEQAAGHARQFHAMATRTRQQYLQDLATNEVTTTSLDSASRFGLPSLGGRRRAAPRGPGAELQAAGSLVWGVRAAPGARVAAGAQASGPEGIEVPCLLGISAEALVLVAPRDGRVVFNCACRDVLAWTFSEQQLDLYHGRGEAITLRFDGSPGQAVGEVVARLQLVSRGCETRELALPRDGQGRLGFEVDAEGFVTHVERFTFAETAGLRPGARLLRVCGQTLPSLRPEAAAQLLRSAPKVCVTVLPPDESGRPRRSFSELYTLSLQEPSRRGAPDPVQDEVQGVTLLPTTKQLLHLCLQDGGSPPGPGDLAEERTEFLHSQNSLSPRSSLSDEAPVLPNTTPDLLLATTAKPSVPSADSETPLTQDRPGSPSGSEDKGNPAPELRASFLPRTLSLRNSISRIMSEAGSGTLEDEWQAISEIASTCNTILESLSREGQPIPESGDPKGTPKSDAEPEPGNLSEKVSHLESMLRKLQEDLQKEKADRAALEEEVRSLRHNNRRLQAESESAATRLLLASKQLGSPTADLA
Protein: 40S ribosomal protein S3 (Q38EW1)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
- 40S ribosomal protein S13, putative
- 40S ribosomal protein S25
- 40S ribosomal protein S33, putative
- 40S ribosomal protein S14
- 40S ribosomal protein S23, putative
- 40S ribosomal protein S15, putative
- Small ribosomal subunit protein uS4
- 40S ribosomal protein S27, putative
- 40S ribosomal protein S4
- 40S ribosomal protein S5, putative
Sequence:
MFLFSYTTSVLTLFYFPIARVCEYPYNYSLHPPICLRSYTQCEETGRHTTIKMGPLSKKRMMVRDGVFYAELFEFLKRELADDGFAGVEHRVTPTRTEIVIRSTKTREVLGEKGRRIRELTACLQQRFNYKEGKLQLFAERVEVRGLSAMAQAESLRFKLLSNLQVRRAAMGIIRYVMESGAKGCEVTIGGKIKGQRAKSMTFRDGYMIKSGTAHKHFVDTATRHCHLRAGTIGVNVKIMRPQSMIEEDEVLPDVITVIEPKTIEA
Protein: GEL complex subunit OPTI (Obligate partner of TMCO1 insertase) (Rab5-interacting protein) (RIP5) (Respirasome Complex Assembly Factor 1) (Q9BUV8)
Organism: Homo sapiens (Human)
Function: Component of the multi-pass translocon (MPT) complex that mediates insertion of multi-pass membrane proteins into the lipid bilayer of membranes. The MPT complex takes over after the SEC61 complex: following membrane insertion of the first few transmembrane segments of proteins by the SEC61 complex, the MPT complex occludes the lateral gate of the SEC61 complex to promote insertion of subsequent transmembrane regions. Within the MPT complex, the GEL subcomplex may mediate insertion of transmembrane regions into the membrane. In addition to its role in multi-pass membrane insertion, RAB5IF/OPTI also acts as an assembly factor for mitochondrial respiratory complexes.
Subcellular location: Endoplasmic reticulum membrane {ECO:0000269|PubMed:36261522}; Multi-pass membrane protein {ECO:0000255}. Mitochondrion inner membrane {ECO:0000269|PubMed:31536960}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
Sequence:
MSGGRRKEEPPQPQLANGALKVSVWSKVLRSDAAWEDKDEFLDVIYWFRQIIAVVLGVIWGVLPLRGFLGIAGFCLINAGVLYLYFSNYLQIDEEEYGGTWELTKEGFMTSFALFMVCVADSFTTGHLDHLLHCHPL
Protein: Serine/threonine-protein phosphatase Pgam5, mitochondrial (DPGAM5) (EC 3.1.3.16) (Phosphoglycerate mutase family member 5 homolog) (O46084)
Organism: Drosophila melanogaster (Fruit fly)
Function: Displays phosphatase activity for serine/threonine residues, and dephosphorylates and activates Pk92B kinase. Has apparently no phosphoglycerate mutase activity.
Subcellular location: Mitochondrion outer membrane {ECO:0000250}; Single-pass membrane protein {ECO:0000250}.
Interaction partners:
- FI11917p
- Uncharacterized protein, isoform B
- RE45833p
- Serine/threonine-protein kinase Pink1, mitochondrial
- Serine/threonine-protein phosphatase PGAM5, mitochondrial
- Phosphoglycerate mutase
- Phosphoglycerate mutase
- Phosphoglycerate mutase
- Prohibitin
- Presenilins-associated rhomboid-like protein, mitochondrial
Sequence:
MRKLTSFVCGTGAGLAAYYLQRLRDPQTVVQNSWTHSDKPVDPWALWDTNWDCREPRALVRPLRNSQPEEENRYNAELEKAKAKKARHIILVRHGEYLDVGDSDDTHHLTERGRKQAEFTGKRLCELGIKWDKVVASTMVRAQETSDIILKQIDFEKEKVVNCAFLREGAPIPPQPPVGHWKPEASQFLRDGSRIEAGFRRYFHRAYPDQEKESYTLIVGHGNVIRYFVCRALQFPAEGWLRININHASITWLTISPSGNVSIKYLGDSGFMPAELLTNRIPRDVKNVV
Protein: Probable diacyglycerol O-acyltransferase tgs1 (TGS1) (EC 2.3.1.20) (Probable triacylglycerol synthase tgs1) (P9WKC9)
Organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Function: Catalyzes the terminal and only committed step in triacylglycerol synthesis by using diacylglycerol and fatty acyl CoA as substrates. Required for storage lipid synthesis (Probable).
Interaction partners:
- Putative NAD
- Alpha-crystallin
- Putative NAD
- Triacylglycerol lipase
- Uncharacterized protein Rv2627c
- Ferredoxin
- Uncharacterized protein Rv3127
- Uncharacterized protein Rv1738
- Dormancy associated translation inhibitor
- Diacylglycerol kinase
Sequence:
MNHLTTLDAGFLKAEDVDRHVSLAIGALAVIEGPAPDQEAFLSSLAQRLRPCTRFGQRLRLRPFDLGAPKWVDDPDFDLGRHVWRIALPRPGNEDQLFELIADLMARRLDRGRPLWEVWVIEGLADSKWAILTKLHHCMADGIAATHLLAGLSDESMSDSFASNIHTTMQSQSASVRRGGFRVNPSEALTASTAVMAGIVRAAKGASEIAAGVLSPAASSLNGPISDLRRYSAAKVPLADVEQVCRKFDVTINDVALAAITESYRNVLIQRGERPRFDSLRTLVPVSTRSNSALSKTDNRVSLMLPNLPVDQENPLQRLRIVHSRLTRAKAGGQRQFGNTLMAIANRLPFPMTAWAVGLLMRLPQRGVVTVATNVPGPRRPLQIMGRRVLDLYPVSPIAMQLRTSVAMLSYADDLYFGILADYDVVADAGQLARGIEDAVARLVAISKRRKVTRRRGALSLVV
Protein: Nucleocapsid protein (Q9DLK6)
Organism: Influenza A virus (A/WSN/1933(H1N1))
Interaction partners:
Sequence:
ETDGERQNATEIRASVGKMIDGIGRFYIQMCTELKLSDYEGRLIQNSLTIERMVLSAFDERRNKYLEEHPSAGKDPKKTGGPIYRRVDGKWRRELILYDKEEIRRIWRQANNGDDATAGLTHMMIWHSNLNDATYQRTRALVRTGMDPRMCSLMQGSTLPRRSGAAGAAVKGVGTMVMEL
Protein: Protein rhomboid (EC 3.4.21.105) (Protein veinlet) (P20350)
Organism: Drosophila melanogaster (Fruit fly)
Function: Acts early in embryonic development to establish position along the dorsoventral axis and then again later to specify the fate of neuronal precursor cells. Involved in EGF receptor signaling; cleaves Spitz to release the active growth factor.
Subcellular location: Golgi apparatus membrane; Multi-pass membrane protein.
Interaction partners:
- Protein spitz
- Epidermal growth factor receptor
- Protein gurken
- Presenilins-associated rhomboid-like protein, mitochondrial
- Protein giant-lens
- Protein Star
- Membrane-bound transcription factor site-2 protease
- Keren
- Serine/threonine-protein kinase Pink1, mitochondrial
- Protein decapentaplegic
Sequence:
MENLTQNVNETKVDLGQEKEKEASQEEEHATAAKETIIDIPAACSSSSNSSSYDTDCSTASSTCCTRQGEHIYMQREAIPATPLPESEDIGLLKYVHRQHWPWFILVISIIEIAIFAYDRYTMPAQNFGLPVPIPSDSVLVYRPDRRLQVWRFFSYMFLHANWFHLGFNIVIQLFFGIPLEVMHGTARIGVIYMAGVFAGSLGTSVVDSEVFLVGASGGVYALLAAHLANITLNYAHMKSASTQLGSVVIFVSCDLGYALYTQYFDGSAFAKGPQVSYIAHLTGALAGLTIGFLVLKNFGHREYEQLIWWLALGVYCAFTVFAIVFNLINTVTAQLMEEQGEVITQHLLHDLGVS
Protein: 2-oxoglutarate and iron-dependent oxygenase domain-containing protein CP2 (EC 1.14.11.-) (Protein CUPULIFORMIS 2) (P0DO23)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Participates in the epigenetic repression of flowering genes in association with ICU11. Functions in the repression of several members of the MADS-box transcription factors family, including SEP3, during vegetative development via histone modification.
Subcellular location: Nucleus, nucleoplasm {ECO:0000269|PubMed:29915151}.
Interaction partners:
Sequence:
MSSEQREGSQETTTTTVEGNGTIAGQNSHSAAPTTLRATSTMVSCQRLRLNPNNEHRPDSYEDLQLDFPNSVYSSLEKYLPPNMLVSNRDEKIKFMTDIMLRHLPHGERSRAQRHSDYRLKITTNYQPLHKELYTLVPTVCFVPAFLKAINENTEESFRNIISEPSPGVFVFDMLQPSFCEMMLAEIDNFERWVGETKFRIMRPNTMNKYGAVLDDFGLDTMLDKLMEGFIRPISKVFFSDVGGATLDSHHGFVVEYGKDRDVDLGFHVDDSEVTLNVCLGNQFVGGELFFRGTRCEKHVNTATKADETYDYCHIPGQAVLHRGRHRHGARATTCGHRVNMLLWCRSSVFRELKTHHKDFSSWCGECFCEKRDEKVRSIDALRKKLFKPRQTQA
Protein: Nucleotide sugar transporter SLC35D2 (Homolog of Fringe connection protein 1) (HFRC1) (SQV7-like protein) (SQV7L) (Solute carrier family 35 member D2) (UDP-galactose transporter-related protein 8) (UGTrel8) (Q76EJ3)
Organism: Homo sapiens (Human)
Function: Antiporter transporting nucleotide sugars such as UDP-N-acetylglucosamine (UDP-GlcNAc), UDP-glucose (UDP-Glc) and GDP-mannose (GDP-Man) pooled in the cytosol into the lumen of the Golgi in exchange for the corresponding nucleosides monophosphates (UMP for UDP-sugars and GMP for GDP-sugars). May take part in heparan sulfate synthesis by supplying UDP-Glc-NAc, the donor substrate, and thus be involved in growth factor signaling.
Subcellular location: Golgi apparatus membrane {ECO:0000269|PubMed:15082721, ECO:0000269|PubMed:15607426}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
- UDP-N-acetylglucosamine transporter
- CMP-sialic acid transporter
- Nucleotide sugar transporter SLC35B4
- Adenosine 3'-phospho 5'-phosphosulfate transporter 1
- Alpha-mannosidase 2x
- Adenosine 3'-phospho 5'-phosphosulfate transporter 2
- Solute carrier family 35 member B1
- Alpha-mannosidase 2
Sequence:
MTAGGQAEAEGAGGEPGAARLPSRVARLLSALFYGTCSFLIVLVNKALLTTYGFPSPIFLGIGQMAATIMILYVSKLNKIIHFPDFDKKIPVKLFPLPLLYVGNHISGLSSTSKLSLPMFTVLRKFTIPLTLLLETIILGKQYSLNIILSVFAIILGAFIAAGSDLAFNLEGYIFVFLNDIFTAANGVYTKQKMDPKELGKYGVLFYNACFMIIPTLIISVSTGDLQQATEFNQWKNVVFILQFLLSCFLGFLLMYSTVLCSYYNSALTTAVVGAIKNVSVAYIGILIGGDYIFSLLNFVGLNICMAGGLRYSFLTLSSQLKPKPVGEENICLDLKS
Protein: Virion host shutoff protein (Vhs) (EC 3.1.27.-) (P10225)
Organism: Human herpesvirus 1 (strain 17) (HHV-1) (Human herpes simplex virus 1)
Function: Minor structural protein that acts as an endoribonuclease during lytic infection. Degrades host mRNAs in the cytoplasm by cutting them at preferred sites, including some in regions of translation initiation. Together with inhibition of host splicing by ICP27, contributes to an overall decrease in host protein synthesis. Also, after the onset of viral transcription, accelerates the turnover of viral mRNA, thereby facilitating the sequential expression of different classes of viral genes. Binds translation initiation factors eIF4H, eIF4AI, and eIF4AII, thereby may interact directly with the translation initiation complex and thus digest specifically mRNAs. Also impedes antigen presentation by major histocompatibility complex class I and class II molecules, inhibits secretion of cytokines that would otherwise recruit lymphocytes and neutrophils cells to the site of infection and blocks the activation of dendritic cells. Plays a role in the inhibition of interferon-beta activation by the cGAS/STING pathway. Mechanistically, down-regulates the expression of host cGAS/MB21D1. Decreases also the accumulation of other interferon-induced mRNAs such as host IFIT3 or CH25H to subvert their antiviral activity.
Subcellular location: Virion {ECO:0000305}.
Interaction partners:
Sequence:
MGLFGMMKFAHTHHLVKRRGLGAPAGYFTPIAVDLWNVMYTLVVKYQRRYPSYDREAITLHCLCRLLKVFTQKSLFPIFVTDRGVNCMEPVVFGAKAILARTTAQCRTDEEASDVDASPPPSPITDSRPSSAFSNMRRRGTSLASGTRGTAGSGAALPSAAPSKPALRLAHLFCIRVLRALGYAYINSGQLEADDACANLYHTNTVAYVYTTDTDLLLMGCDIVLDISACYIPTINCRDILKYFKMSYPQFLALFVRCHTDLHPNNTYASVEDVLRECHWTPPSRSQTRRAIRREHTSSRSTETRPPLPPAAGGTETRVSWTEILTQQIAGGYEDDEDLPLDPRDVTGGHPGPRSSSSEILTPPELVQVPNAQLLEEHRSYVANPRRHVIHDAPESLDWLPDPMTITELVEHRYIKYVISLIGPKERGPWTLLKRLPIYQDIRDENLARSIVTRHITAPDIADRFLEQLRTQAPPPAFYKDVLAKFWDE
Protein: ATP-dependent (S)-NAD(P)H-hydrate dehydratase (EC 4.2.1.93) (ATP-dependent NAD(P)HX dehydratase) (Q94AF2)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Catalyzes the dehydration of the S-form of NAD(P)HX at the expense of ATP, which is converted to ADP. Together with NAD(P)HX epimerase, which catalyzes the epimerization of the S- and R-forms, the enzyme allows the repair of both epimers of NAD(P)HX, a damaged form of NAD(P)H that is a result of enzymatic or heat-dependent hydration.
Subcellular location: [Isoform 1]: Plastid, chloroplast {ECO:0000255}.; SUBCELLULAR LOCATION: [Isoform 2]: Cytoplasm {ECO:0000305}.
Interaction partners:
- Pyridoxine/pyridoxamine 5'-phosphate oxidase 1, chloroplastic
- Omega-amidase, chloroplastic
- tRNase Z TRZ3, mitochondrial
- 2'-phosphotransferase
- Glycine--tRNA ligase, mitochondrial 1
- Transmembrane protein
Sequence:
MLVKPSIISGLVRLTSHSPSSSSSVLRRQEFLVRTLCGSPIIRAMSSTSEADAESVLRTVTPSLDLKRHKGQAGKIAVIGGCREYTGAPYFAAISALKIGADLSHVFCTKDAAPVIKSYSPELIVHPVLEESYSISQLSEEDKREVQDKVLGEVGKWMERFDCLVIGPGLGRDPFLLECVSIIMLLAKKSNVPFVIDGDGLFLVTNSIDLVHSYPLAVLTPNVNEYKRLVQKVLNCEVDEQNAEDQLRSLAKQIGGVTILRKGKSDLISNGETVKSVSIYGSPRRCGGQGDILSGGVAVFLSWAQQLKSDPESPSENPAILGCIAASGLLRKAASLAFTKHKRSTLTSDIIECLGESLEDICPAS
Protein: [histone H3]-trimethyl-L-lysine(27) demethylase (EC 1.14.11.68) (A0A8I5ZM74)
Organism: Rattus norvegicus (Rat)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
MKSCGVSLATAAAAAAFGDEEKKMAAGKASGESEEASPSLTAEEREALGGLDSRLFGFVRFHEDGARMKALLGKAVRCYESLILKAEGKVESDFFCQLGHFNLLLEEYPKALSAYQRYYSLQSDYWKNAAFLYGLGLVYFHYNAFQWAIKAFQEVLYVDPSFCRAKEIHLRLGLMFKVNTDYESSLKHFQLALVDCNPCTLSNAEIQFHIAHLYETQRKYHSAKEAYEQLLQLENLSAQVKATVLQQLGWMHHTVDLLGDKATKESYAIQYLQKSLEADPNSGQSWYFLGRCYSSIGKVQDAFISYRQSIDKSEASADTWCSIGVLYQQQNQPMDALQAYICAVQLDHGHAAAWMDLGTLYESCNQPQDAIKCYLNATRSKNCSNTSGLAARIKYLQAQLCNLPQGSLQNKTKLLPSIEEAWSLPIPAELTSRQGAMNTAQQNTSDNWSGGNAVPHPPVQQQTHSWCLTPQKLQHLEQLRANRNNLNPAQKLMLEQLESQFVLMQQHQMRQTGVAQVRPTGIPNGPTADSSLPTNSASGQQPQLPLTRMPSVSQPGVQPACPRQALANGPFSAGHVPCSTSRTLGSTDTILIGNNHVTGSGSNGNVPYLQRNAPTLPHNRTNLTSSTEEPWKNQLSNSTQGLHKGQSSHLAGPNGERPLSSTGPSQHLQAAGSGIQNQNGHPTLPSNSVTQGAALNHLSSHTATSGGQQGITLTKESKPSGNTLTLPETNRQTGETPNSTASVEGLPNHVHQVMADAVCSPSHGDSKSPGLLSSDNPQLSALLMGKANNNVGPGTCDIVNNIHPTVHTKTDNSVASSPSSAISTATPSPKSTEQTTTNSVTSLNSPHSGLHTINGEGMEESQSPIKTDLLLVSHRPSPQIIPSVSVSIYPSSAEVLKACRNLGKNGLSNSSILLDKCPPPRPPSSPYPPLPKDKLNPPTPSIYLENKRDAFFPPLHQFCTNPNNPVTVIRGLAGALKLDLGLFSTKTLVEANNEHMVEVRTQLLQPADENWDPTGTKKIWHCESNRSHTTIAKYAQYQASSFQESLREENEKRSHHKDHSDSESTSSDNSGKRRRGPFKTIKFGTNIDLSDDKKWKLQLHELTKLPAFVRVVSAGNLLSHVGHTILGMNTVQLYMKVPGSRTPGHQENNNFCSVNINIGPGDCEWFVVPEGYWGVLNDFCEKNNLNFLMGSWWPNLEDLYEANVPVYRFIQRPGDLVWINAGTVHWVQAIGWCNNIAWNVGPLTACQYKLAVERYEWNKLQSVKSIVPMVHLSWNMARNIKVSDPKLFEMVKYCLLRTLKQCQTLREALIAAGKEIIWHGRTKEEPAHYCSICEVEVFDLLFVTNESNSRKTYIVHCQDCAWKTSGNLENFVVLEQYKMEDLMQVYDQFTLAPPLPSASS
Protein: Mis12 (RE19545p) (Q9VS01)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
- Nnf1a
- Nnf1b
- CG1558-RA protein
- Nuf2
- Kinetochore protein Spc25
- Kinetochore protein NDC80
- HDC12388
- Centromeric protein-C, isoform A
- Spc105-related, isoform B
Sequence:
MDFNSLAYDQKFFNFTAAQLSAEREHIVQDIIKKGIGQIIDKIKTPATAELLEAEKETVERRFQASASKGLKALRELDSKVFHVPPHVLHPEHMFVENQYTSEEEEQKTARLEELKAKYRENMAMLAHLKIEEEKYAAMEDLIQKEIEMQDRVQRSCSSLNITKLKQFWNQVPLQIKKETD
Protein: Endoplasmic reticulum resident protein 27 (ER protein 27) (ERp27) (Inactive protein disulfide-isomerase 27) (Q96DN0)
Organism: Homo sapiens (Human)
Function: Specifically binds unfolded proteins and may recruit protein disulfide isomerase PDIA3 to unfolded substrates. Binds protein substrates via a hydrophobic pocket in the C-terminal domain. May play a role in the unfolded stress response.
Subcellular location: Endoplasmic reticulum lumen {ECO:0000269|PubMed:16940051}.
Interaction partners:
- Protein disulfide-isomerase A3
- Calreticulin
- Elongation factor 1-gamma
- Elongation factor 1-delta
Sequence:
MEAAPSRFMFLLFLLTCELAAEVAAEVEKSSDGPGAAQEPTWLTDVPAAMEFIAATEVAVIGFFQDLEIPAVPILHSMVQKFPGVSFGISTDSEVLTHYNITGNTICLFRLVDNEQLNLEDEDIESIDATKLSRFIEINSLHMVTEYNPVTVIGLFNSVIQIHLLLIMNKASPEYEENMHRYQKAAKLFQGKILFILVDSGMKENGKVISFFKLKESQLPALAIYQTLDDEWDTLPTAEVSVEHVQNFCDGFLSGKLLKENRESEGKTPKVEL
Protein: histone acetyltransferase (EC 2.3.1.48) (A0A669KB12)
Organism: Homo sapiens (Human)
Subcellular location: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}. Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
MAENVVEPGPPSAKRPKLSSPALSASASDGTDFGSLFDLEHDLPDELINSTELGLTNGGDINQLQTSLGMVQDAASKHKQLSELLRSGSSPNLNMGVGGPGQVMASQAQQSSPGLGLINSMVKSPMTQAGLTSPNMGMGTSGPNQGPTQSTGMMNSPVNQPAMGMNTGMNAGMNPGMLAAGNGQGIMPNQVMNGSIGAGRGRQNMQYPNPGMGSAGNLLTEPLQQGSPQMGGQTGLRGPQPLKMGMMNNPNPYGSPYTQNPGQQIGASGLGLQIQTKTVLSNNLSPFAMDKKAVPGGGMPNMGQQPAPQVQQPGLVTPVAQGMGSGAHTADPEKRKLIQQQLVLLLHAHKCQRREQANGEVRQCNLPHCRTMKNVLNHMTHCQSGKSCQVAHCASSRQIISHWKNCTRHDCPVCLPLKNAGDKRNQQPILTGAPVGLGNPSSLGVGQQSAPNLSTVSQIDPSSIERAYAALGLPYQVNQMPTQPQVQAKNQQNQQPGQSPQGMRPMSNMSASPMGVNGGVGVQTPSLLSDSMLHSAINSQNPMMSENASVPSLGPMPTAAQPSTTGIRKQWHEDITQDLRNHLVHKLVQAIFPTPDPAALKDRRMENLVAYARKVEGDMYESANNRAEYYHLLAEKIYKIQKELEEKRRTRLQKQNMLPNAAGMVPVSMNPGPNMGQPQPGMTSSLNQFGQMSMAQPPIVPRQTPPLQHHGQLAQPGALNPPMGYGPRMQQPSNQGQFLPQTQFPSQGMNVTNIPLAPSSGQAPVSQAQMSSSSCPVNSPIMPPGSQGSHIHCPQLPQPALHQNSPSPVPSRTPTPHHTPPSIGAQQPPATTIPAPVPTPPAMPPGPQSQALHPPPRQTPTPPTTQLPQQVQPSLPAAPSADQPQQQPRSQQSTAASVPTPTAPLLPPQPATPLSQPAVSIEGQVSNPPSTSSTEVNSQAIAEKQPSQEVKMEAKMEVDQPEPADTQPEDISESKVEDCKMESTETEERSTELKTEIKEEEDQPSTSATQSSPAPGQSKKKIFKPEELRQALMPTLEALYRQDPESLPFRQPVDPQLLGIPDYFDIVKSPMDLSTIKRKLDTGQYQEPWQYVDDIWLMFNNAWLYNRKTSRVYKYCSKLSEVFEQEIDPVMQSLGYCCGRKLEFSPQTLCCYGKQLCTIPRDATYYSYQNRYHFCEKCFNEIQGESVSLGDDPSQPQTTINKEQFSKRKNDTLDPELFVECTECGRKMHQICVLHHEIIWPAGFVCDGCLKKSARTRKENKFSAKRLPSTRLGTFLENRVNDFLRRQNHPESGEVTVRVVHASDKTVEVKPGMKARFVDSGEMAESFPYRTKALFAFEEIDGVDLCFFGMHVQEYGSDCPPPNQRRVYISYLDSVHFFRPKCLRTAVYHEILIGYLEYVKKLGYTTGHIWACPPSEGDDYIFHCHPPDQKIPKPKRLQEWYKKMLDKAVSERIVHDYKDIFKQATEDRLTSAKELPYFEGDFWPNVLEESIKELEQEEEERKREENTSNESTDVTKGDSKNAKKKNNKKTSKNKSSLSRGNKKKPGMPNVSNDLSQKLYATMEKHKEVFFVIRLIAGPAANSLPPIVDPDPLIPCDLMDGRDAFLTLARDKHLEFSSLRRAQWSTMCMLVELHTQSQDRFVYTCNECKHHVETRWHCTVCEDYDLCITCYNTKNHDHKMEKLGLGLDDESNNQQAAATQSPGDSRRLSIQRCIQSLVHACQCRNANCSLPSCQKMKRVVQHTKGCKRKTNGGCPICKQLIALCCYHAKHCQENKCPVPFCLNIKQKLRQQQLQHRLQQAQMLRRRMASMQRTGVVGQQQGLPSPTPATPTTPTGQQPTTPQTPQPTSQPQPTPPNSMPPYLPRTQAAGPVSQGKAAGQVTPPTPPQTAQPPLPGPPPAAVEMAMQIQRAAETQRQMAHVQIFQRPIQHQMPPMTPMAPMGMNPPPMTRGPSGHLEPGMGPTGMQQQPPWSQGGLPQPQQLQSGMPRPAMMSVAQHGQPLNMAPQPGLGQVGISPLKPGTVSQQALQNLLRTLRSPSSPLQQQQVLSILHANPQLLAAFIKQRAAKYANSNPQPIPGQPGMPQGQPGLQPPTMPGQQGVHSNPAMQNMNPMQAGVQRAGLPQQQPQQQLQPPMGGMSPQAQQMNMNHNTMPSQFRDILRRQQMMQQQQQQGAGPGIGPGMANHNQFQQPQGVGYPPQQQQRMQHHMQQMQQGNMGQIGQLPQALGAEAGASLQAYQQRLLQQQMGSPVQPNPMSPQQHMLPNQAQSPHLQGQQIPNSLSNQVRSPQPVPSPRPQSQPPHSSPSPRMQPQPSPHHVSPQTSSPHPGLVAAQANPMEQGHFASPDQNSMLSQLASNPGMANLHGASATDLGLSTDNSDLNSNLSQSTLDIH
Protein: Tax1-binding protein 1 (TRAF6-binding protein) (Q86VP1)
Organism: Homo sapiens (Human)
Function: Ubiquitin-binding adapter that participates in inflammatory, antiviral and innate immune processes as well as selective autophagy regulation. Plays a key role in the negative regulation of NF-kappa-B and IRF3 signalings by acting as an adapter for the ubiquitin-editing enzyme A20/TNFAIP3 to bind and inactivate its substrates. Disrupts the interactions between the E3 ubiquitin ligase TRAF3 and TBK1/IKBKE to attenuate 'Lys63'-linked polyubiquitination of TBK1 and thereby IFN-beta production. Recruits also A20/TNFAIP3 to ubiquitinated signaling proteins TRAF6 and RIPK1, leading to their deubiquitination and disruption of IL-1 and TNF-induced NF-kappa-B signaling pathways. Inhibits virus-induced apoptosis by inducing the 'Lys-48'-linked polyubiquitination and degradation of MAVS via recruitment of the E3 ligase ITCH, thereby attenuating MAVS-mediated apoptosis signaling. As a macroautophagy/autophagy receptor, facilitates the xenophagic clearance of pathogenic bacteria such as Salmonella typhimurium and Mycobacterium tuberculosis. Upon NBR1 recruitment to the SQSTM1-ubiquitin condensates, acts as the major recruiter of RB1CC1 to these ubiquitin condensates to promote their autophagic degradation.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:30909570}. Mitochondrion {ECO:0000269|PubMed:27736772}. Preautophagosomal structure {ECO:0000269|PubMed:33226137, ECO:0000269|PubMed:34471133}. Cytoplasmic vesicle, autophagosome {ECO:0000269|PubMed:26451915}.
Interaction partners:
- RING finger protein 11
- Tumor necrosis factor alpha-induced protein 3
- Gamma-aminobutyric acid receptor-associated protein
- Contactin-2
- GABA type A receptor associated protein like 1
- Gamma-aminobutyric acid receptor-associated protein-like 2
- TNF receptor-associated factor 6
- Ubiquitin-conjugating enzyme E2 N
- 5-azacytidine-induced protein 2
- Optineurin
Sequence:
MTSFQEVPLQTSNFAHVIFQNVAKSYLPNAHLECHYTLTPYIHPHPKDWVGIFKVGWSTARDYYTFLWSPMPEHYVEGSTVNCVLAFQGYYLPNDDGEFYQFCYVTHKGEIRGASTPFQFRASSPVEELLTMEDEGNSDMLVVTTKAGLLELKIEKTMKEKEELLKLIAVLEKETAQLREQVGRMERELNHEKERCDQLQAEQKGLTEVTQSLKMENEEFKKRFSDATSKAHQLEEDIVSVTHKAIEKETELDSLKDKLKKAQHEREQLECQLKTEKDEKELYKVHLKNTEIENTKLMSEVQTLKNLDGNKESVITHFKEEIGRLQLCLAEKENLQRTFLLTTSSKEDTCFLKEQLRKAEEQVQATRQEVVFLAKELSDAVNVRDRTMADLHTARLENEKVKKQLADAVAELKLNAMKKDQDKTDTLEHELRREVEDLKLRLQMAADHYKEKFKECQRLQKQINKLSDQSANNNNVFTKKTGNQQKVNDASVNTDPATSASTVDVKPSPSAAEADFDIVTKGQVCEMTKEIADKTEKYNKCKQLLQDEKAKCNKYADELAKMELKWKEQVKIAENVKLELAEVQDNYKELKRSLENPAERKMEGQNSQSPQCFKTCSEQNGYVLTLSNAQPVLQYGNPYASQETRDGADGAFYPDEIQRPPVRVPSWGLEDNVVCSQPARNFSRPDGLEDSEDSKEDENVPTAPDPPSQHLRGHGTGFCFDSSFDVHKKCPLCELMFPPNYDQSKFEEHVESHWKVCPMCSEQFPPDYDQQVFERHVQTHFDQNVLNFD
Protein: FI21431p1 (Knockout, isoform A) (Knockout, isoform B) (Q9VP79)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MGTKSPGGPQRCRLILQRCLAIQLTKPGHTPEDFWMYDSGYMIFQNFLAANAQCWWNGPLTAATRALKYAGHVAPGMLLVTAEPCALEVLRGAFARSVLKPPATYVISSVGDIDDCIVTPTVQGQFTPLPEALCDVIMDLTAEGQSATIEHVRSKLGSRFPHMTTPATEVIYDSLAQLMQEQKIYQTSKGYFIFTPERRRSRSRPRSNHHQLNGSLAYGHLAEEEQQHGDDVVPQEARTMLMSNSEALHSLYGEISTERDGDLTHQCIQTNLADVICGGNPNDKIIYPRAAKRRSASFPTPRSLERRHSLRLFGSSKRLQRCASTRSLSKTYAQTLNTTDSSSSEYQSTDSSSPKKGSLLSRLFRRSGRAKQRQIETYSAQFPPAEWFNTRAVHLHSVGTQTAEHDMPVAHTLSNSTFYDGSELSQRSSTLPRRHRRHMSSESTFLISSRDCSPIRRRSPVYCSSSLPRSTQSIPATTAKTNHSSRLSHGHGGSVTPTPPKTAQKSVIGKHIFESSPSRSATLKATAAKRHTDGLIINSCLDNKATYRSLQSSGPSSLESCKTTSMLASGPSSIDSGKVSFSQKTSGHSSLDSQCSTNTAVIAPPSNSNNGSSRSILLLNGSPRGTPRHQAMRARVAEAQAQRQRASTPSRIMEEIYPAGGSNGVPTSNSNNSITLQVTTSNGNQSIPSTKIFVQNSPVRSVITLENGKMLENSNVFIINNETMTNEKGEIIKKTLSKQTSAAPAATSTPVKPETVSEQPLSETEANSETCDSISFISECSPESTCAVEPETPVYDGGKYAKNTNNDATMNNSRKLCLQLANGIAYKNNVLKNESQPNSPSADAPLKMAALAKQDFEIAGSVGNLNFYEKSSKDVGASQSNNMMMNSSTDLKNLCYESVCQLQKCSMNGDELALAHLLHKSSNPLGSEPNLALKDLANDKSIDKEAIDRRLSLTKESLEQGMGSVLANGGEELYNFPSLTDLSFNFTSLAARKILQGVSLNSIDTLVELNMAAAAAAAAVANNAQEKQQNNQPATAGPTASVCTDFGMV