wanglab/gogpt-training-data huggingface dataset:
Protein: SUMO-activating enzyme subunit aos-1 (Q17820)
Organism: Caenorhabditis elegans
Function: The dimeric enzyme acts as an E1 ligase for smo-1. It mediates ATP-dependent activation of smo-1 and formation of a thioester with a conserved cysteine residue on uba-2 (Probable).
Interaction partners:
- SUMO-activating enzyme subunit uba-2
- Small ubiquitin-related modifier
- SUMO-conjugating enzyme UBC9
- Rad60/SUMO-like domain-containing protein
- Sentrin-specific protease
- E3 SUMO-protein ligase gei-17
- UBC core domain-containing protein
- Ubiquitin-like protease 2
- Molybdopterin synthase catalytic subunit
- Serpentine Receptor, class T
Sequence:
MEVSKAEQAIYDRQIRLWGMEAQNKIRNSKVLIIGGKQLGAEVAKTLSLAGVDEMHLVDHRLVDTEEIGMNFLYDASVDNSKMTKWAASYNFLYNLNRNVKLFIVEEDVLSKNDSEIEEYLTKFTLVVVLDESYERTAKVNNICRKHHIRFISGAIYGWIGYAFFDFDGHAYLVKAKSPDCLNEEESETGKTSTVVTVDEEFVLETFSYPSFVETLNSDFTAKKIVRKCKRIVPTSYFLVKSMLRASSENKLTGVTENDIEKLIPIWNEEVAAGNHTIDMQPVQPDRFDHLFGPNFGPTAACVGGVIGQEAIKSISEGKNPLRNLFIYTGFESTGFMCNFPPV
Protein: RE01412p (Q8MT65)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Cytoplasm, cytoskeleton {ECO:0000256|ARBA:ARBA00004245}.
Interaction partners:
Sequence:
MATVAECNHSVLDLVTKMATMLVADEMKPKKQTAVLVAKKRSKIYESLLHSETMSSQDKLEMLHQVTSEVAKNPDRVDMMLRFQNLLEGQDKEESEITQDQDEENQSEVVIKRIKAGPLQLIETIEIVEEALHPKAFPDINQMNRALKPLQLQPYSDILTTSNLNINFPPEKLIPKIIPSTVIRMGLSESITRMRNEMEKPMHPPPRLPVLAKKVVAPLEDERPFVAQPGPEKHFVSDKLLTNELKILRNKNLVLNYLDEATLIDHLKKAACGIESLTFPISSADKLELRVRPNTTLPTMLPEVLADFANHFIRAGCAFLRLSSRTKWNNIAEMRLERPLNRAMRETIMDYLSTTRQFLLSLQADSLFQLLNNTSTAIQLLCQLDRMFENEPRLNLNTGITGSFLLSSIWLAIDTCGNKDFLHLLIYFLRCISRNYFIQLQRWIYHGELDESVNEIFISRCLNTSPSFTNQCSKEFFDKSYQVDNEAIPEFLVGCEEEILQCGKYNLVLRAYNAQHPVFDVQYPDIVVCLTEQQLKNMRRNLADKYAIIYKRFGWCSMQSIFEDRMATKRVFANLMVKRTQAHLDAWAQKQRELQIKANAQKKLQNDQLNAEQERIQQNHLEKRRQDNVNELAFQRECERMEDKLLEREKQELQKKVVQLAAVLSSSPDRSTVSDLSFASCIEEPDCLAESSSDKDDANTENSEDEATKQLDKTLNVPLEQPEAEYQADVDVDQPRGKECSLPNVFQYQRSHSDVINSNEHPTTQAEFNRNRQHGLSSDQFQQCHATVHLQESDLLKTAASTSSGLHAEIPQDINANLNCPDTKELTELQRNRKRNEHHDGFFSFNSTEDEHTHRLRSLLNSNTERGRNRLRVMETEFGLGYKNTDIETKATPCLPLEIDKLHVEIPLAVLTPMSTTSDVDFGDPSPRELPEIADTANNNNVSGSIESLSPELPKPVLAIAKPTSLLPKLDFGMKDERETEQDRDKVSTLPEACNPFMARRCLQLSVMAPLNAYYGLLRNEVLRIFQEQRIYEHFRKLRNYFFLVDGQFGATLTNEILGRIRAGVGPRSLSQKGILDTILTNALAACSADETTVSENLTLNCTTIPDTLNFLSVEATSMLKLNCKIDWPLNMVISSETISKYGQIFGYLLKLRHVSFVLDGTYEYLQQMGKLLGPELRTCTHFRHMQMMRHKMSHFMTSFQTHLVAKALLSTWKSFKEELCTADSIEALYKQHVAYLKRVAFLALLNRRSAKVKETIDNILVIILRFCKVIQSQSFIVDQDNYFVHPRFKRLQQEEAEFEKFLQYLIYLGNKAAASGYQEEIGDLICIINFNHYYKVSGNHTGSSMEDKKC
Protein: Candida glabrata strain CBS138 chromosome E complete sequence (Q6FVH4)
Organism: Candida glabrata (strain ATCC 2001 / BCRC 20586 / JCM 3761 / NBRC 0622 / NRRL Y-65 / CBS 138) (Yeast) (Nakaseomyces glabratus)
Interaction partners:
- Candida glabrata strain CBS138 chromosome K complete sequence
Sequence:
MLFLVPFLSVAQAYVALDFEKSHGDDLVKRDVQDVKLINSQKAMLYNIQLSVGTPPQNITAQLDTGSSDLWFPDSTNPYCKANKKQAPKSIASLDAGTRPTSPAQVPKSLRNLDCAEFGLFNSSASTTFNSNKTEFFISYLDSSYAEGVWATDNLYLNGLNISGLNFGLAYFSNSSNSVLGVGLTPLEASYDTDIKQDDSPRFQYPNFPQILKQKGAISKVTYSLYLNDTKSKYGQILFGGVDHSKYVGQLYTIPLVNSKYQKSPGVIADLEVTLNGLGIRDNTTNTNTTLYTQKLPALFDSGTSYSYVPYTMAQVIASQVNGTIDNKTEAIRLPKCPSKKDTREVVFNFNGVEIAIPLKQFYQKKSGKCYLDLMVAPPNNGPGLLLGDTFLRQVYTVFDLEAQELSIARANFNSSLPADVEEIKSTVPSAIKAPQYYNTFSAYDNATQVVGNIFDATATASMAPKNQSNSSNLSRRALNYENNSARSSTLSIVLVLAAITTLFM
Protein: Iron-sulfur cluster assembly transcription factor IscR (A6V0U7)
Organism: Pseudomonas aeruginosa (strain PA7)
Interaction partners:
Sequence:
MRLTTKGRYAVTAMLDLALHAQQGPVSLADISERQGISLSYLEQLFAKLRRGNLVTSVRGPGGGYQLSRHMSGIHVAQVIDAVNESVDATRCQGQGDCHSGDTCLTHHLWCDLSLQIHEFLSGISLADLVSRQEVQEVALRQDERRCSGKTPRLDKIEASAID
Protein: Keratin 83 (A0A0G2KA07)
Organism: Rattus norvegicus (Rat)
Interaction partners:
Sequence:
MTCGFQTGNFGCASACGPRPGRCCITAAPYRGISCYRGLSGGFGSRSVCGAFRSGSCGRSFGYRSGGVCGPSPPCITTVSVNESLLTPLNLEIDPNAQCVKHEEKEQIKCLNSRFAAFIDKVRFLEQQNKLLETKWQFFQNRKCCESNVEPLFEGYIETLRREAECVEADSGRLAAELNHAQEAMEGYKKRYEEEVALRATAENEFVALKKDVDCAYLRKSDLEANAEALTQEIDFLRRLYEEETRILHAHISDTSVIVKMDNSRDLNMDCVIAEIKAQYDDIASRSRAEAESWYRTKCEEIKATVIRHGETLRRTREEINELNRIIQRLTAEIENAKCQNTKLEAAVTQSEQQGEAALTDARCKLAELEAALQKAKQDMACLLKEYQEVMNSKLGLDIEIATYRRLLEGEEQRWTHIHNSGFLAPKRRLLYTTYKLKTEAFCAIPQRAGVNKRTKGRCQQLPWWSCVRGPLCVWFKACDRQCLQCPMQRECGSEHRPVCTLWKWPLSPGEVLAYKADLGGLKVCCPSSVAAPPATCWQGACC
Protein: E3 ubiquitin-protein ligase MIB1 (EC 2.3.2.27) (DAPK-interacting protein 1) (DIP-1) (Mind bomb homolog 1) (RING-type E3 ubiquitin transferase MIB1) (Zinc finger ZZ type with ankyrin repeat domain protein 2) (Q86YT6)
Organism: Homo sapiens (Human)
Function: E3 ubiquitin-protein ligase that mediates ubiquitination of Delta receptors, which act as ligands of Notch proteins. Positively regulates the Delta-mediated Notch signaling by ubiquitinating the intracellular domain of Delta, leading to endocytosis of Delta receptors. Probably mediates ubiquitination and subsequent proteasomal degradation of DAPK1, thereby antagonizing anti-apoptotic effects of DAPK1 to promote TNF-induced apoptosis (By similarity). Involved in ubiquitination of centriolar satellite CEP131, CEP290 and PCM1 proteins and hence inhibits primary cilium formation in proliferating cells. Mediates 'Lys-63'-linked polyubiquitination of TBK1, which probably participates in kinase activation.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:24121310}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome, centriolar satellite {ECO:0000269|PubMed:24121310}. Cell membrane {ECO:0000250}. Note=Localizes to the plasma membrane (By similarity). According to PubMed:15048887, it is mitochondrial, however such localization remains unclear. Displaced from centriolar satellites in response to cellular stress, such as ultraviolet light (UV) radiation or heat shock. {ECO:0000250}.
Interaction partners:
- Protein jagged-1
- Pericentriolar material 1 protein
- Delta-like protein 1
- Zinc finger MYM-type protein 4
- Bromodomain-containing protein 2
- Death-associated protein kinase 1
Sequence:
MSNSRNNRVMVEGVGARVVRGPDWKWGKQDGGEGHVGTVRSFESPEEVVVVWDNGTAANYRCSGAYDLRILDSAPTGIKHDGTMCDTCRQQPIIGIRWKCAECTNYDLCTVCYHGDKHHLRHRFYRITTPGSERVLLESRRKSKKITARGIFAGARVVRGVDWQWEDQDGGNGRRGKVTEIQDWSASSPHSAAYVLWDNGAKNLYRVGFEGMSDLKCVQDAKGGSFYRDHCPVLGEQNGNRNPGGLQIGDLVNIDLDLEIVQSLQHGHGGWTDGMFETLTTTGTVCGIDEDHDIVVQYPSGNRWTFNPAVLTKANIVRSGDAAQGAEGGTSQFQVGDLVQVCYDLERIKLLQRGHGEWAEAMLPTLGKVGRVQQIYSDSDLKVEVCGTSWTYNPAAVSKVASAGSAISNASGERLSQLLKKLFETQESGDLNEELVKAAANGDVAKVEDLLKRPDVDVNGQCAGHTAMQAASQNGHVDILKLLLKQNVDVEAEDKDGDRAVHHAAFGDEGAVIEVLHRGSADLNARNKRRQTPLHIAVNKGHLQVVKTLLDFGCHPSLQDSEGDTPLHDAISKKRDDILAVLLEAGADVTITNNNGFNALHHAALRGNPSAMRVLLSKLPRPWIVDEKKDDGYTALHLAALNNHVEVAELLVHQGNANLDIQNVNQQTALHLAVERQHTQIVRLLVRAGAKLDIQDKDGDTPLHEALRHHTLSQLRQLQDMQDVGKVDAAWEPSKNTLIMGLGTQGAEKKSAASIACFLAANGADLSIRNKKGQSPLDLCPDPNLCKALAKCHKEKVSGQVGSRSPSMISNDSETLEECMVCSDMKRDTLFGPCGHIATCSLCSPRVKKCLICKEQVQSRTKIEECVVCSDKKAAVLFQPCGHMCACENCANLMKKCVQCRAVVERRVPFIMCCGGKSSEDATDDISSGNIPVLQKDKDNTNVNADVQKLQQQLQDIKEQTMCPVCLDRLKNMIFLCGHGTCQLCGDRMSECPICRKAIERRILLY
Protein: Large ribosomal subunit protein eL39 (60S ribosomal protein L39) (P62893)
Organism: Rattus norvegicus (Rat)
Function: RNA-binding component of the large ribosomal subunit. The ribosome is a large ribonucleoprotein complex responsible for the synthesis of proteins in the cell.
Subcellular location: Cytoplasm {ECO:0000250|UniProtKB:P62891}.
Interaction partners:
- Large ribosomal subunit protein eL18
- Large ribosomal subunit protein eL42
- Large ribosomal subunit protein eL24
- Small ribosomal subunit protein uS14
- Large ribosomal subunit protein uL5
- Large ribosomal subunit protein eL38
- Large ribosomal subunit protein eL6
- Small ribosomal subunit protein eS28
- Small ribosomal subunit protein uS12
- Small ribosomal subunit protein eS21
Sequence:
MSSHKTFRIKRFLAKKQKQNRPIPQWIRMKTGNKIRYNSKRRHWRRTKLGL
Protein: Delta-amaurobitoxin-Pl1c (Delta-AMATX-Pl1c) (Delta-palutoxin IT3) (Delta-paluIT3) (P83258)
Organism: Pireneitega luctuosa (Tangled nest spider) (Paracoelotes luctuosus)
Function: Binds at site 4 of sodium channels (Nav) and inhibits the fast inactivation of cockroach channels. This toxin is active only on insects (By similarity). Has a potent activity against S.litura larvae.
Subcellular location: Secreted {ECO:0000269|PubMed:10971590}.
Interaction partners:
Sequence:
ADCLNEGDWCADWSGPSCCGEMWCSCPGFGKCRCKK
Protein: Uncharacterized protein, isoform A (Uncharacterized protein, isoform B) (Q9VIS0)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
- BUD13 homolog
- RE68879p
- PHD finger-like domain-containing protein 5A
- Splicing factor 3B subunit 1
- LD45152p
- Splicing factor 3B subunit 4
- Splicing factor 3B subunit 3
- Cell division cycle 5, isoform A
- U5 small nuclear ribonucleoprotein 200 kDa helicase
- Pre-mRNA-processing factor 19
Sequence:
MNPLTNMKNVLKLSEHELQHGGKKSWHDMYKDSAWIFVAGFPYTLTEGDLVCVFSQYGEVVNINLIRDSKTGKSKGFCFLCYEDQRSTVLAVDNLNGIKILDRTLRVDHVADYKPPKENEKMDEETLRLYMEGCAPKPQLQHIKTEKKDSKNYR
Protein: Fibroblast growth factor (FGF) (A0A8I5ZL19)
Organism: Rattus norvegicus (Rat)
Interaction partners:
Sequence:
MGSPRSALSCLLLHLLVLCLQAQEGPGGGPALGREPASLLRAGREPQGVSQQVTVQSSPNFTQHVREQSLVTDQLSRRLIRTYQLYSRTSGKHVQVLANKRINAMAEDGDPFAKLIVETDTFGSRVRVRGAETGLYICMNKKGKLIAKSNGKGKDCVFTEIVLENNYTALQNAKYEGWYMAFTRKGRPRKGSKTRQHQREVHFMKRLPRGHHTTEQSLRFEFLNYPPFTRSLRGSQRTWAPEPR
Protein: Reticulon (F1QT89)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Subcellular location: Endoplasmic reticulum membrane {ECO:0000256|ARBA:ARBA00004477, ECO:0000256|RuleBase:RU210713}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004477, ECO:0000256|RuleBase:RU210713}.
Interaction partners:
Sequence:
MSEMDSKQVVELLYWRDLQRTGVVFGAGLFLLLSLSMCSIISVLSYVALALLSVTVSFRIYKGILQAVQKSEDGHPFKMYLDKDTALPAEMVHKYSDSTLVHINTVIKELRRLFLVEDLVDSLKFAVLMWILTYVGALFNGLTLIILGFIGAFSCPVIYEKHQAQIDHYYGLVNKQFKDVVGKIQAKIPGAKPKTE
Protein: Sm protein G (Q382A6)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
- Small nuclear ribonucleoprotein E
- Sm protein F
- U1 small nuclear ribonucleoprotein, putative
- U2 small nuclear ribonucleoprotein B, putative
- PRP8 protein homologue
- PRP1 splicing factor N-terminal domain-containing protein
- Small nuclear ribonucleoprotein Sm D2
- G10 protein
- U5 small nuclear ribonucleoprotein component, putative
- Sm protein B
Sequence:
MPAKKRIANLNHFMEKRVKVKLTSGRSISGELRGVDEFMSIVLYDAVDETPTSGTVENEDKTSLGTAVVRGAMIVDIVGLEV
Protein: Glycogen synthase kinase-3 alpha (GSK-3 alpha) (EC 2.7.11.26) (Serine/threonine-protein kinase GSK3A) (EC 2.7.11.1) (P49840)
Organism: Homo sapiens (Human)
Function: Constitutively active protein kinase that acts as a negative regulator in the hormonal control of glucose homeostasis, Wnt signaling and regulation of transcription factors and microtubules, by phosphorylating and inactivating glycogen synthase (GYS1 or GYS2), CTNNB1/beta-catenin, APC and AXIN1. Requires primed phosphorylation of the majority of its substrates. Contributes to insulin regulation of glycogen synthesis by phosphorylating and inhibiting GYS1 activity and hence glycogen synthesis. Regulates glycogen metabolism in liver, but not in muscle (By similarity). May also mediate the development of insulin resistance by regulating activation of transcription factors. In Wnt signaling, regulates the level and transcriptional activity of nuclear CTNNB1/beta-catenin. Facilitates amyloid precursor protein (APP) processing and the generation of APP-derived amyloid plaques found in Alzheimer disease. May be involved in the regulation of replication in pancreatic beta-cells (By similarity). Is necessary for the establishment of neuronal polarity and axon outgrowth (By similarity). Through phosphorylation of the anti-apoptotic protein MCL1, may control cell apoptosis in response to growth factors deprivation (By similarity). Acts as a regulator of autophagy by mediating phosphorylation of KAT5/TIP60 under starvation conditions which activates KAT5/TIP60 acetyltransferase activity and promotes acetylation of key autophagy regulators, such as ULK1 and RUBCNL/Pacer. Negatively regulates extrinsic apoptotic signaling pathway via death domain receptors. Promotes the formation of an anti-apoptotic complex, made of DDX3X, BRIC2 and GSK3B, at death receptors, including TNFRSF10B. The anti-apoptotic function is most effective with weak apoptotic signals and can be overcome by stronger stimulation (By similarity). Phosphorylates mTORC2 complex component RICTOR at 'Thr-1695' which facilitates FBXW7-mediated ubiquitination and subsequent degradation of RICTOR.
Interaction partners:
- Axin-1
- Adenomatous polyposis coli protein
- Catenin beta-1
- RAC-alpha serine/threonine-protein kinase
- Casein kinase I isoform alpha
- Glycogen synthase kinase-3 beta
- Axin-2
- RAC-gamma serine/threonine-protein kinase
- RAC-beta serine/threonine-protein kinase
- Amyloid-beta precursor protein
Sequence:
MSGGGPSGGGPGGSGRARTSSFAEPGGGGGGGGGGPGGSASGPGGTGGGKASVGAMGGGVGASSSGGGPGGSGGGGSGGPGAGTSFPPPGVKLGRDSGKVTTVVATLGQGPERSQEVAYTDIKVIGNGSFGVVYQARLAETRELVAIKKVLQDKRFKNRELQIMRKLDHCNIVRLRYFFYSSGEKKDELYLNLVLEYVPETVYRVARHFTKAKLTIPILYVKVYMYQLFRSLAYIHSQGVCHRDIKPQNLLVDPDTAVLKLCDFGSAKQLVRGEPNVSYICSRYYRAPELIFGATDYTSSIDVWSAGCVLAELLLGQPIFPGDSGVDQLVEIIKVLGTPTREQIREMNPNYTEFKFPQIKAHPWTKVFKSRTPPEAIALCSSLLEYTPSSRLSPLEACAHSFFDELRCLGTQLPNNRPLPPLFNFSAGELSIQPSLNAILIPPHLRSPAGTTTLTPSSQALTETPTSSDWQSTDATPTLTNSS
Protein: Uncharacterized protein F54C8.7 (P34445)
Organism: Caenorhabditis elegans
Interaction partners:
- ADP-ribosylation factor-like protein 1
- Resistance to inhibitors of cholinesterase protein 19
- ADP-ribosylation factor 6
Sequence:
MTGSTASPPEPSAPPADSPFAPVTQNDSSPTSDSTETMSRIPTGIKVPDVVANIDTAQVAAKVESFKKWTIGTFKNSKQQLLEHMGKIDKTVDPEFEAQCEVLKDIHRRYGLVVAAAKNFSHVLTQMAEAEKKLSESFYQLSMKEEQIKAQCTMTSETMRGVGEQAASLDACLRYFISSMETVYNQTITDTLHTIYNTESARIEYDVDRNDISAATNPPQGQLTKNLPVGATEKCEEKKAKYEKLKNDAKIKMRLLEENRISVVAAQLEKLQSALAAYYSGNAKLLEASVRELSFLQSPQPSFIPTM
Protein: Sperm protamine alpha isoform 2 (Scombrine alpha-2) (P83265)
Organism: Scomber scombrus (Atlantic mackerel) (Scomber vernalis)
Function: Protamines substitute for histones in the chromatin of sperm during the haploid phase of spermatogenesis. They compact sperm DNA into a highly condensed, stable and inactive complex.
Subcellular location: Nucleus {ECO:0000269|PubMed:9530815}. Chromosome {ECO:0000269|PubMed:9530815}.
Interaction partners:
Sequence:
MPRRRRRASRPIRRRRRARRSTAVRRRRRVVRRRR
Protein: Protein seu-1 (Suppressor of ectopic unc-5) (A9D2P7)
Organism: Caenorhabditis elegans
Function: Together with unc-5, involved in touch neuron axon guidance. During gonad morphogenesis, plays a role in the unc-5-/unc-6-mediated migration of distal tip cells along the body.
Subcellular location: Nucleus {ECO:0000269|PubMed:17716643}.
Interaction partners:
Sequence:
MSSIRNQNDNRRPTFRDHRTPQFSGRGGSGGGGRRLQNPAHYPQRRDMSPIRRSSAISPVRRSQDHRQRSPEVRRHRSPEKESKDAVVTSTGSSRGATSASVTSSSRRHESGERHRETHRREDKEKKPEKSTDRDADRSNNIAARIQAPVVSSSTHHHHSNRHENRKSTAVKRPAADNRPMTYSTDVSVSRHSENRRKSSSDVSRRHGDKEKRDRKREDVKKKSNGERSSSSGRRREEDHKRKSESSRKEKKDEDVKEKVVDENKVEDEAVEMQGLVEVDCCEEEETIEQAKEHGSDEPERPESHQSAHSAAVSNASHHSDSEEELDYEEDDIDVDLDGDIDVETMKMAARGDLKVDDTTDEDEINDVKDETMEEQKEDGEPEKKKPRTSENDDKDKKHHGSSSSNSHRRREDDKDRRQSSDHHKERRRSPATRQRATDHKESRRSEGTSTRVESAASAAGTEIQRIPSLLTMRIAAPPGIKKLETLYHSGSGGSSSSSSHSSEMIIVGETFSNRWCQCSCAHHLPTTSSAAAAAGSLDASPASSSSSSSNSDASVSRIPSLMSLRTPFNNSCLFLAPPPPPSSSSSSKRSHEAAARIRAPSPPRRSFGDRGNRSDEHHGGSRHMDVGPQRRRLQDHRVRDDGRRVSSFEDRKRPERGFQDSGRVSLSLKHL
Protein: DNA-3-methyladenine glycosylase (EC 3.2.2.21) (3-methyladenine DNA glycosidase) (3MEA DNA glycosylase) (P22134)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Hydrolysis of the deoxyribose N-glycosidic bond to excise 3-methyladenine or 7-methyladenine from the damaged DNA polymer formed by alkylation lesions.
Subcellular location: Nucleus {ECO:0000269|PubMed:11502169}.
Interaction partners:
- Apurinic-apyrimidinic endonuclease 1
- DNA polymerase zeta catalytic subunit
- DNA-
- ATP-dependent DNA helicase MPH1
Sequence:
MKLKREYDELIKADAVKEIAKELGSRPLEVALPEKYIARHEEKFNMACEHILEKDPSLFPILKNNEFTLYLKETQVPNTLEDYFIRLASTILSQQISGQAAESIKARVVSLYGGAFPDYKILFEDFKDPAKCAEIAKCGLSKRKMIYLESLAVYFTEKYKDIEKLFGQKDNDEEVIESLVTNVKGIGPWSAKMFLISGLKRMDVFAPEDLGIARGFSKYLSDKPELEKELMRERKVVKKSKIKHKKYNWKIYDDDIMEKCSETFSPYRSVFMFILWRLASTNTDAMMKAEENFVKS
Protein: Corticotropin releasing hormone receptor 2 (A0A090N7T4)
Organism: Homo sapiens (Human)
Subcellular location: Cell membrane {ECO:0000256|ARBA:ARBA00004651}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004651}.
Interaction partners:
Sequence:
MDAALLHSLLEANCSLALAEELLLDGWGPPLDPEGPYSYCNTTLDQIGTCWPRSAAGALVERPCPEYFNGVKYNTTRNAYRECLENGTWASKINYSQCEPILDDKQRKYDLHYRIALVVNYLGHCVSVAALVAAFLLFLALRSIRCLRNVIHWNLITTFILRNVMWFLLQLVDHEVHESNEVWCRCITTIFNYFVVTNFFWMFVEGCYLHTAIVMTYSTERLRKCLFLFIGWCIPFPIIVAWAIGKLYYENEQCWFGKEPGDLVDYIYQGPIILVLLINFVFLFNIVRILMTKLRASTTSETIQYRKAVKATLVLLPLLGITYMLFFVNPGEDDLSQIMFIYFNSFLQSFQGFFVSVFYCFFNGEVRSAVRKRWHRWQDHHSLRVPMARAMSIPTSPTRISFHSIKQTAAV
Protein: Pleckstrin homology domain-containing family A member 6 (PH domain-containing family A member 6) (Phosphoinositol 3-phosphate-binding protein 3) (PEPP-3) (Q9Y2H5)
Organism: Homo sapiens (Human)
Interaction partners:
- Vesicle transport protein GOT1A
Sequence:
MSNKTGGKRPATTNSDIPNHNMVSEVPPERPSVRATRTARKAVAFGKRSHSMKRNPNAPVTKAGWLFKQASSGVKQWNKRWFVLVDRCLFYYKDEKEESILGSIPLLSFRVAAVQPSDNISRKHTFKAEHAGVRTYFFSAESPEEQEAWIQAMGEAARVQIPPAQKSVPQAVRHSHEKPDSENVPPSKHHQQPPHNSLPKPEPEAKTRGEGDGRGCEKAERRPERPEVKKEPPVKANGLPAGPEPASEPGSPYPEGPRVPGGGEQPAQPNGWQYHSPSRPGSTAFPSQDGETGGHRRSFPPRTNPDKIAQRKSSMNQLQQWVNLRRGVPPPEDLRSPSRFYPVSRRVPEYYGPYSSQYPDDYQYYPPGVRPESICSMPAYDRISPPWALEDKRHAFRNGGGPAYQLREWKEPASYGRQDATVWIPSPSRQPVYYDELDAASSSLRRLSLQPRSHSVPRSPSQGSYSRARIYSPVRSPSARFERLPPRSEDIYADPAAYVMRRSISSPKVPPYPEVFRDSLHTYKLNEQDTDKLLGKLCEQNKVVREQDRLVQQLRAEKESLESALMGTHQELEMFGSQPAYPEKLRHKKDSLQNQLINIRVELSQATTALTNSTIEYEHLESEVSALHDDLWEQLNLDTQNEVLNRQIQKEIWRIQDVMEGLRKNNPSRGTDTAKHRGGLGPSATYSSNSPASPLSSASLTSPLSPFSLVSGSQGSPTKPGSNEPKANYEQSKKDPHQTLPLDTPRDISLVPTRQEVEAEKQAALNKVGVVPPRTKSPTDDEVTPSAVVRRNASGLTNGLSSQERPKSAVFPGEGKVKMSVEEQIDRMRRHQSGSMREKRRSLQLPASPAPDPSPRPAYKVVRRHRSIHEVDISNLEAALRAEEPGGHAYETPREEIARLRKMELEPQHYDVDINKELSTPDKVLIPERYIDLEPDTPLSPEELKEKQKKVERIKTLIAKSSMQNVVPIGEGDSVDVPQDSESQLQEQEKRIEISCALATEASRRGRMLSVQCATPSPPTSPASPAPPANPLSSESPRGADSSYTMRV
Protein: Inositol hexakisphosphate and diphosphoinositol-pentakisphosphate kinase (EC 2.7.4.24) (F8W9A8)
Organism: Homo sapiens (Human)
Subcellular location: Cell membrane {ECO:0000256|ARBA:ARBA00004236}. Cytoplasm, cytosol {ECO:0000256|ARBA:ARBA00004514, ECO:0000256|RuleBase:RU365032}.
Interaction partners:
Sequence:
MWSLTASEGESTTAHFFLGAGDEGLGTRGIGMRPEESDSELLEDEEDEVPPEPQIIVGICAMTKKSKSKPMTQILERLCRFDYLTVVILGEDVILNEPVENWPSCHCLISFHSKGFPLDKAVAYSKLRNPFLINDLAMQYYIQDRREVYRILQEEGIDLPRYAVLNRDPARPEECNLIEGEDQVEVNGAVFPKPFVEKPVSAEDHNVYIYYPSSAGGGSQRLFRKIGSRSSVYSPESSVRKTGSYIYEEFMPTDGTDVKVYTVGPDYAHAEARKSPALDGKVERDSEGKEIRYPVMLTAMEKLVARKVCVAFKQTVCGFDLLRANGHSFVCDVNGFSFVKNSMKYYDDCAKILGNTIMRELAPQFQIPWSIPTEAEDIPIVPTTSGTMMELRCVIAIIRHGDRTPKQKMKMEVKHPRFFALFEKHGGYKTGKLKLKRPEQLQEVLDITRLLLAELEKEPGGEIEEKTGKLEQLKSVLEMYGHFSGINRKVQLTYYPHGVKASNEGQDPQRETLAPSLLLVLKWGGELTPAGRVQAEELGRAFRCMYPGGQGDYAGFPGCGLLRLHSTFRHDLKIYASDEGRVQMTAAAFAKGLLALEGELTPILVQMVKSANMNGLLDSDGDSLSSCQHRVKARLHHILQQDAPFGPEDYDQLAPTRSTSLLNSMTIIQNPVKVCDQVFALIENLTHQIRERMQDPRSVDLQLYHSETLELMLQRWSKLERDFRQKSGRYDISKIPDIYDCVKYDVQHNGSLGLQGTAELLRLSKALADVVIPQEYGISREEKLEIAVGFCLPLLRKILLDLQRTHEDESVNKLHPLESHVHSLLSVFRYGGLLDETQDAQWQRALDYLSAISELNYMTQIVIMLYEDNTQDPLSEERFHVELHFSPGVKGVEEEGSAPAGCGFRPASSENEEMKTNQGSMENLCPGKASDEPDRALQTSPQPPEGPGLPRRSPLIRNRKAGSMEVLSETSSSRPGGYRLFSSSRPPTEMKQSGLGSQCTGLFSTTVLGGSSSAPNLQDYARSHGKKLPPASLKHRDELLFVPAVKRFSVSFAKHPTNGFEGCSMVPTIYPLETLHNALSLRQVSEFLSRVCQRHTDAQAQASAALFDSMHSSQASDNPFSPPRTLHSPPLQLQQRSEKPPWYSSGPSSTVSSAGPSSPTTVDGNSQFGFSDQPSLNSHVAEEHQGLGLLQETPGSGAQELSIEGEQELFEPNQSPQVPPMETSQPYEEVSQPCQEVPDISQPCQDISEALSQPCQKVPDISQQCQENHDNGNHTCQEVPHISQPCQKSSQLCQKVSEEVCQLCLENSEEVSQPCQGVSVEVGKLVHKFHVGVGSLVQETLVEVGSPAEEIPEEVIQPYQEFSVEVGRLAQETSAINLLSQGIPEIDKPSQEFPEEIDLQAQEVPEEIN
Protein: Caspase-5 (CASP-5) (EC 3.4.22.58) (ICE(rel)-III) (Protease ICH-3) (Protease TY) [Cleaved into: Caspase-5 subunit p20; Caspase-5 subunit p10] (P51878)
Organism: Homo sapiens (Human)
Function: Thiol protease that acts as a mediator of programmed cell death. Initiates pyroptosis, a programmed lytic cell death pathway through cleavage of Gasdermin-D (GSDMD): cleavage releases the N-terminal gasdermin moiety (Gasdermin-D, N-terminal) that binds to membranes and forms pores, triggering pyroptosis. During non-canonical inflammasome activation, cuts CGAS and may play a role in the regulation of antiviral innate immune activation.
Interaction partners:
- NACHT, LRR and PYD domains-containing protein 1
- Apoptosis-associated speck-like protein containing a CARD
- Caspase-1
- NACHT, LRR and PYD domains-containing protein 3
- Caspase recruitment domain-containing protein 8
- Interferon-inducible protein AIM2
- Caspase-4
- Gasdermin-D
- NLR family CARD domain-containing protein 4
- NACHT, LRR and PYD domains-containing protein 6
Sequence:
MAEDSGKKKRRKNFEAMFKGILQSGLDNFVINHMLKNNVAGQTSIQTLVPNTDQKSTSVKKDNHKKKTVKMLEYLGKDVLHGVFNYLAKHDVLTLKEEEKKKYYDTKIEDKALILVDSLRKNRVAHQMFTQTLLNMDQKITSVKPLLQIEAGPPESAESTNILKLCPREEFLRLCKKNHDEIYPIKKREDRRRLALIICNTKFDHLPARNGAHYDIVGMKRLLQGLGYTVVDEKNLTARDMESVLRAFAARPEHKSSDSTFLVLMSHGILEGICGTAHKKKKPDVLLYDTIFQIFNNRNCLSLKDKPKVIIVQACRGEKHGELWVRDSPASLALISSQSSENLEADSVCKIHEEKDFIAFCSSTPHNVSWRDRTRGSIFITELITCFQKYSCCCHLMEIFRKVQKSFEVPQAKAQMPTIERATLTRDFYLFPGN
Protein: RIM-binding protein, isoform N (E1JIL7)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MPYESMHHHQSAAAAVAAGTTPNGMLDALSLQLRDAEMRRTEIERAHQETLAQIRNLSGSARPDAEAVENLQSRARELEKKVALENVRCEELQIELTSALKAKQASRSACSGMGSVSSGGGATIPTSASSSTVTWAPTISHQDQGSEIDIIMAKIEQDNRVLAELEQPRTSASASMSALPPSSMLSTVNSEFRTISKSELEEELNRYKRAVLGGSGGGGGGVGGGGGGVSALSSGYSSLPQSLASTLPNGGASTSLSGTSLGSHSAAAAAAAHSVSAGSGGVVGGGGQGGLSSISALVPNSISGISSSLSSHAIQSMQYGTGQTSVEKLLSGTSGITGIPPLPVNIHTMKAMPTALSQSTTMPLLSLNSHNLPPAGSTSYSALGAGGGTSLTHPTMANLGLLDTGTLLGSTGLSGLGVGPSVGGITGATSLYGLSGGGGGAGGLGSSYGPPFLDVASSASYPFTAAALRQASKMKMLDEIDIPLTRYNRSSPCSPIPPNNWGLDEFTDGLSVSMMHNRGGLALGALDLDTRNHGLNGASEPQVDMLDIPGKGRCCVFIARFPYDPPDVHNEFLSMPCREAEGELSLCAGDYLLVWTSGEPQGGYLDAELLDGRRGLVPASFVQRLVGDDLLEFHQAVLSTLRDAEDGSMQCDTTSLPSLPPHNPLLTHTHEDLARLSETHTDLEHDQDDISDNVPAPKHLTLERQLNKSVLIGWSPPEPVGYNLIDSYHVYVDGVLKVTVKANERTRALIEGVDSTRPHRISVRSVTQNRQTSRDAACTMIIGRDTAHLGPSAVRASHITCSSAVISWLPANSNHQHVVCVNNVEVRTVKPGMYRHTITGLAPSTQYRVTVRAKHLRAVGQHAANVGQTGGAGRPGQEEAPGAYADFRTLTKGLPDPPQEIQLEAGPQDGTILVTWQPVNRPTSTGPVTGYAVYADGKKVTDINSPTGDHALIDIGKLGVFNPRAVTIRTKSRDSQSADSAPILIPNTVRNAVARRGPNQMGMGPQLPQGPHGMTVQQQMGGMPGQPGQQGQHMMGGQQDHGQYDPNQMQQQQQQQGQPGQPGHQPDAGSGLLGGLLGGLFSKPTQNQVNQNGYQPGQPGAQRGMVPIPGRPQGPQQQQQQPYGPQGPMGGPRFRGPVPGQLNMQGQQMQGQMQGQMQGQMQGQMSGQMPGQMPGQMPGQMPGQMAGQMAGQMPGQMPGQMPGQMSGQMPGQMMGPRGPLNQQQQQQQQMQQGQMMPGQQAGQQQAQPGQPGQPGQMPGAQKKPRYFVAMFDYDPSTMSPNPDGCDEELPFQEGDTIKVFGDKDADGFYWGELRGRRGYVPHNMVSEVEDTTASMTAGGQMPGQMPGQMGQGQGVGVGGTAQVMPGQGAPQQSMRNVSRDRWGDIYANMPVKRMIALYDYDPQELSPNVDAEQVELCFKTGEIILVYGDMDEDGFYMGELDGVRGLVPSNFLADAPDQYNNQMGPGGVAGRGGLSQRGRGQGPGARGPPPPPRDNMMPGMGGRGQPGKNARPASPTLLDNTGHPAPDHQTQGMIGRVGNVGLQQQQQQQQQQQQLQQQQQYGQQQTQMGQQQQQQQQMGQPGMMGQQMGQPMGQQMGQMGQMGQMGQQQMGQQQMGQQQQPPTTQAQTGGLFSGATSLLSGATSAATGGLFGSKQPPKTDPMQPQGGVQPAQQQANAFGAQQPGMGMQQQGGMQSGMQQGMQQGMQQGMQQGMQQGMQQGMQQGMQQGMQPGMQQQQQQPQQVPPQAQAPPPGPGAGLLGGLKGIAAAAPGGDVLSKGKDLFGKFGFGFGK
Protein: Uncharacterized oxidoreductase AN7799 (EC 1.-.-.-) (Q5AV81)
Organism: Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) (Aspergillus nidulans)
Function: Involved in osmoadaptation.
Interaction partners:
Sequence:
MVRIFITGSSDGIGQAAAKVLSEQGHSVVLHARNADRAASAQEAVPGAEAVLVGDLSSIAETKALAEEANKLPPFDTVIHNAGIGYGATASQEITADKISAVFAVNTLAPYILTCLMHKPKARLLYMSSDSHYGGDESLRNITQSHSYGNTKLHDVMLANAFSRRWGNAIQVVSMHPGWVRTKMGGVMAPGALDRPARVLADWAIGKGDLARLKSGTFFTTSGPESAHPGADNVQKQEELLRICKEVSGVGVPGG