wanglab/gogpt-training-data huggingface dataset:
Protein: Protein SMAX1-LIKE 4 (AtSMXL4) (Protein HEAT SHOCK PROTEIN-RELATED) (AtHSPR) (EC 3.6.3.-) (Q9SZR3)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Probable component of a transcriptional corepressor complex involved in salt tolerance through modulation of reactive oxygen species levels, abscisic acid-dependent stomatal closure, photosynthesis and K(+) /Na(+) homeostasis. Has an in vitro ATPase activity.
Subcellular location: Nucleus {ECO:0000269|PubMed:26603028}.
Interaction partners:
- F-box protein MAX2
- Probable esterase KAI2
- ATP-dependent Clp protease adapter protein CLPS1
Sequence:
MRTGAYTVHQTLTPEAASVLKQSLTLARRRGHSQVTPLHVASTLLTSSRSNLFRRACLKSNPFTALGRQMAHPSLHCRALELCFNVSLNRLPTNPNPLFQTQPSLSNALVAALKRAQAHQRRGCVEQQQSQQNQPFLAVKVELEQLVVSILDDPSVSRVMREAGLSSVSVKSNIEDDSSVVSPVFYGSSSSVGVFSSPCSPSSSENNQGGGTLSPNPSKIWHAHLTNHHSFEQNPFFHFPKGKTFTPDQAFPVREDANPVIEVLLGKKNNKKRNTVIVGDSVSLTEGVVAKLMGRIERGEVPDDLKQTHFIKFQFSQVGLNFMKKEDIEGQVRELKRKIDSFTSWGGKGVIVCLGDLDWAVWGGGNSASSSNYSAADHLVEEIGRLVYDYSNTGAKVWLLGTASYQTYMRCQMKQPPLDVHWALQAVSIPSGGLSLTLHASSSEMASQVMEMKPFRVKEEEEGAREEEEEDKLNFCGECAFNYEKEAKAFISAQHKILPPWLQPHGDNNNINQKDELSGLRKKWNRFCQALHHKKPSMTAWRAEQSSSVLPGSLMDSSLKQNSRASSSVAKFRRQNSCTIEFSFGSNRQEGLKKTDELSLDGFKSNNDEGVKTKITLALGHSPFPSDSENSEEEEPEKAIKMSKLLEKLHENIPWQKDVLPSIVEAMEESVKRSKRKDAWMLVSGNDVTAKRRLAITLTTSLFGSHENMLKINLRTSKASEACEELKNALKKKEEVVILIERVDLADAQFMNILVDRFEAGDLDGFQGKKSQIIFLLTREDDECVENEHFVIPMVLNCNKSGSGLVNNKRKPEYDAAPTMIKKKNPRIEEDDDESNVACDISNIKKEFSRQLKFESNALDLNLRVDADEDEEEEAKPATEISSGFEERFLDSIQNRFDFTVLSDEDITKFFVTKIKDSCEEILGQREERFGFTVDAELIEKFYKGCGFFANGLFEEWVKEVFQRGLVTVKNGGKEGISVINLCLGGIDMIDQGEVYEEEEGFMGTCLPNRIHVSFVD
Protein: DNA polymerase IV (POL IV) (EC 2.7.7.7) (P25615)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Repair polymerase. Involved in gap-filling in DNA nonhomologous end joining (NHEJ) required for double-strand break repair. Seems to conduct DNA synthesis in a stepwise distributive fashion rather than in a processive fashion as for other DNA polymerases. Preferentially acts upon short gaps formed by the alignment of linear duplexes with complementary single-strand ends. Required for filling gaps that need removal of a 5'- or 3'-terminal mismatch, however lacks nuclease activities.
Subcellular location: Nucleus.
Interaction partners:
- DNA ligase 4
- ATP-dependent DNA helicase II subunit 1
- rDNA transcriptional regulator POL5
- Flap endonuclease 1
- Non-homologous end-joining protein 1
- Non-homologous end-joining factor LIF1
- Tyrosyl-DNA phosphodiesterase 1
- DNA polymerase eta
- DNA polymerase delta catalytic subunit
- DNA repair protein REV1
Sequence:
MSLKGKFFAFLPNPNTSSNKFFKSILEKKGATIVSSIQNCLQSSRKEVVILIEDSFVDSDMHLTQKDIFQREAGLNDVDEFLGKIEQSGIQCVKTSCITKWVQNDKFAFQKDDLIKFQPSIIVISDNADDGQSSTDKESEISTDVESERNDDSNNKDMIQASKPLKRLLQGDKGRASLVTDKTKYKNNELIIGALKRLTKKYEIEGEKFRARSYRLAKQSMENCDFNVRSGEEAHTKLRNIGPSIAKKIQVILDTGVLPGLNDSVGLEDKLKYFKNCYGIGSEIAKRWNLLNFESFCVAAKKDPEEFVSDWTILFGWSYYDDWLCKMSRNECFTHLKKVQKALRGIDPECQVELQGSYNRGYSKCGDIDLLFFKPFCNDTTELAKIMETLCIKLYKDGYIHCFLQLTPNLEKLFLKRIVERFRTAKIVGYGERKRWYSSEIIKKFFMGVKLSPRELEELKEMKNDEGTLLIEEEEEEETKLKPIDQYMSLNAKDGNYCRRLDFFCCKWDELGAGRIHYTGSKEYNRWIRILAAQKGFKLTQHGLFRNNILLESFNERRIFELLNLKYAEPEHRNIEWEKKTA
Protein: Keratin, type I cytoskeletal 20 (Cytokeratin-20) (CK-20) (Keratin-20) (K20) (Q9D312)
Organism: Mus musculus (Mouse)
Function: Plays a significant role in maintaining keratin filament organization in intestinal epithelia. When phosphorylated, plays a role in the secretion of mucin in the small intestine.
Interaction partners:
- Homeobox protein CDX-2
Sequence:
MDFSRQSFHRSLSSSSQGPALSMSGSLYRKGTVQRLGAAPSVYGGAGGHGTRISVSKAVMSYGGDLSNGSDLFGGNGKLAMQNLNDRLANYLEKVRSLEQSNSRLEAQIKQWYETNAPSTIRDYSSYYAQIKELQNQVKDAQVQNAQCVLRIDNAKLAAEDFRLKFETERGMRIAVEADLQGLSKVYDNLTLQKTDLEIQIEELNKDLALLKKEHQEEVEVLRRQLGNNVNVEVDAAPGLNLGEIMNEMRQRYEVLAQKNLQEAKEQFERQSQTLQQQVTVNTEELKGFEVQVTELRRTYQNLEIELQSHLSMKESLERNLEDVKARYASQLAAIQEMLSSLEAQLMQIRSDTERQNQEHNILLDIKTRLEQEIATYRRLLEGEDIKTTEYQLSTLEMKDIKKTRKIKTVVEEVVDGKVVSSEVKEIEESV
Protein: Malonyl CoA-acyl carrier protein transacylase, mitochondrial (MCT) (EC 2.3.1.39) (Malonyl-CoA:ACP transferase) (O13698)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Involved in biosynthesis of fatty acids in mitochondria.
Subcellular location: Mitochondrion {ECO:0000269|PubMed:16823372}.
Interaction partners:
- Putative 3-oxoacyl-[acyl-carrier-protein] synthase, mitochondrial
- Putative acyl carrier protein, mitochondrial
- Acetyl-CoA carboxylase
- 3-oxoacyl-[acyl-carrier-protein] reductase
- Fatty acid synthase subunit alpha
- Small ribosomal subunit protein uS2m
- Enoyl-[acyl-carrier-protein] reductase, mitochondrial
- Hydroxyacyl-thioester dehydratase type 2, mitochondrial
- Small ribosomal subunit protein bS6m
- Fatty acid synthase subunit beta dehydratase; Enoyl-[acyl-carrier-protein] reductase; [Acyl-carrier-protein] acetyltransferase; [Acyl-carrier-protein] malonyltransferase; S-acyl fatty acid synthase thioesterase]
Sequence:
MSAILFPGQGVDWKTWMQPYLENNIVQNTLKEAENVTEIEIRKYIVEAEAKSNLRQPITTIAQPAILACSIALLRAFPPFTKKFRFYVGHSLGEYSAFVASQTLSFSSALKLVQARAKAMSYASALCQNPTSMLAITLTSRFPTDNFLNTVYSAVQKYRLIDIANVNSDRQIVLSGDKKELESITSTLSELVRSLGKLRSNWLDVSGAFHSRYMLPARDSLKNALGETEFNISPELCYTDSGKRFLPIISNVTAELYPADEEDIRRQLLLQCFRPVLFKNCLKTVKSKYGANLFYAYGPGTTMQSIAKQNGISTKSRP
Protein: Natural resistance-associated macrophage protein 1 (NRAMP 1) (Solute carrier family 11 member 1) (P51027)
Organism: Gallus gallus (Chicken)
Function: Divalent transition metal (iron and manganese) transporter involved in iron metabolism and host resistance to certain pathogens. Macrophage-specific membrane transport function. Controls natural resistance to infection with intracellular parasites. Pathogen resistance involves sequestration of Fe(2+) and Mn(2+), cofactors of both prokaryotic and eukaryotic catalases and superoxide dismutases, not only to protect the macrophage against its own generation of reactive oxygen species, but to deny the cations to the pathogen for synthesis of its protective enzymes (By similarity).
Subcellular location: Late endosome membrane {ECO:0000250|UniProtKB:P49279}; Multi-pass membrane protein {ECO:0000255}. Lysosome membrane {ECO:0000250|UniProtKB:P49279}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
- Uncharacterized protein.
Sequence:
MSGSGPAMASLEPGLAGSLNRGQTDASNVPVPPHHPVPHAQTYLDELISIPKGSTPGFSFRKLWAFTGPGFLMSIAYLDPGNVESDLQCGAVAGFKLLWVLLWATVLGLLCQRLAIRLGVVTGKDLAEICYLYYPRVPRVLLWLMMEIAIIGSDMQEVIGTAIAFSLLSAGRIPLWGGVLITITDTLFFLFLDKYGLRKLEAFFGFLITIMALTFGYEYVMVRPAQTEVLKGIFLPYCPGCGREELLQAVGIVGAIIMPHNIFLHSSLVKTRAIDRSKKEEVKEANMYFLTESCLALFVSFLINLFVMAVFGEAFYHQRNEDVHNKCVNSSVSRYASIFPINNETVSVDIYQGGVILGCYFGAAALYIWAVGILAAGQSSTMTGTYAGQFVMEGFLQLRWSRFTRVLFTRSLAILPTLFVAAFRDVSQLTGMNDLLNVLQSILLPFAVLPVLTFTSLRPLMHDFANGLLGQVLMSLITGLVCAINVYFVVDFLPTLRGLGYLIPLGLLLVAYVAFVTYLLWTCSIAHGARFLARGRYNRFSFDVTADVPGLAGPH
Protein: Protein BREAST CANCER SUSCEPTIBILITY 2 homolog B (AtBRCA2B) (Q7Y1C4)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Involved in double-strand break repair and/or homologous recombination by mediating RAD51- and DMC1-facilitated DNA repair. Plays an essential role in both somatic and meiotic homologous recombination. Is crucial for the formation of RAD51 and DMC1 foci during male meiotic homologous recombination in prophase I.
Interaction partners:
- Protein DSS1 HOMOLOG ON CHROMOSOME V
- Protein DELETION OF SUV3 SUPPRESSOR 1
- Meiotic recombination protein DMC1 homolog
- Protein BREAST CANCER SUSCEPTIBILITY 1 homolog
- DNA repair protein RAD51 homolog 3
- DNA repair protein RAD51 homolog 1
- DNA repair protein XRCC3 homolog
- Fanconi anemia group D2 protein
- BRCA1-associated RING domain protein 1
- Nibrin homolog
Sequence:
MSTWHLFSDSSGDGFRWEVAGRILQSVSDSTPTKALESTAPLPSMADLLLQGCSKLIEREESMPGEIPMFRTGLGKSVVLKESSIAKAKSILAENVAYSDLQNTNCSIPQTRQVDTAETMPMFRTALGKTVPLKESSIAKPLSILGSDMIIDSDNVLPRESGFGVPNSLFQTASNKKVNVSSAGLARAKALLGLEEDDLNGFNHVNQSSSSLQQHGWSGLKTHEEFDATVVKHHSGTPGQYENYVSGKRSEILNPSLKVPPTKFQTAGGKSLSVSAEALKRARNLLGDPELGSFFDDVAGGDQFFTPQKDERLSDIAINNGSVNTGYIAHEEKTSNKHTSNSFVSPLHSSSKQFRSVNLENLASGGNLIKKFDTAVDETNCALNISKPATHGLSNNRPLASDMAVNNSKGNGFIPRARQLGRPADQPLVDITNRRDTAYANNKQDSTQKKRLGKTVSVSPFKRPRISSFKTPLKKNAQQASSGLSVVSCDTLTSKKVLSTRYPEKSPRVYIKEFFGMHPTATTRMDYVPDHVRRIKSSNADKYVFCDESSSNKVGAETFLQMLAESGASLQHASRKWVTNHYRWIVWKLACYDIYYPAKCRGNFLTITNVLEELKYRYEREVNHGHCSAIKRILSGDAPASSMMVLCISAINPRTDNGSQEAHCSDNCSNVKVELTDGWYSMNAALDVVLTKQLNAGKLFVGQKLRILGAGLSGWATPTSPLEAVISSTICLLLNINGTYRAHWADRLGFCKEIGVPLAFNCIKCNGGPVPKTLAGITRIYPILYKERLGEKKSIVRSERIESRIIQLHNQRRSALVEGIMCEYQRGINGVHSQNDTDSEEGAKVFKLLETAAEPELLMAEMSLEQLTSFTTYKAKFEAAKQMQMEKSVAKALEDAGLGERNVTPFMRIRLVGLTSLSNEGEHNPKEGIVTIWDPTERQRTELTEGKIYIMKGLVPMNSDSETLYLHARGSSSRWQPLSPKDSENFQPFFNPRKPISLSNLGEIPLSSEFDIAAYVVYVGDAYTDVLQKKQWVFVTDGSTQHSGEISNSLLAISFSTPFMDDSSVSHISHNLVGSVVGFCNLIKRAKDATNEMWVAETTENSVYFINAEAAYSSHLKTRSAHIQTWAKLYSSKSVIHELRQRVLFIIGACKSPSC
Protein: Shar pei/DRhoGEF2 (O44381)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}. Membrane {ECO:0000256|ARBA:ARBA00004370}.
Interaction partners:
Sequence:
MDDPSIKKRLLDLYTDEHEYDEVQEIPEESSIQPPETSTSHTSTNGSSHSGPGTATGPGATSAGPSAGAPQSPVIVVDSVPELPAPKQKSVKNSKSKQKQKQLANKSKIPRSPSLASSLSSLASSLSGHRDRDKDRDKDRENQNAVPPQTPPLPPSYKQNQMNGDSTAAAGGGVSAPATPTTANNNNASHNNGSIMGGGVQLNQSDNSNPVLQAPGERSSLNLTPLSRDLSGGHTQESTTPATTPSTPSLALPKNFQYLTLTVRKDSNGYGMKVSGDNPVFVESVKPGGAAEIAGLVAGDMILRVNGHEVRLEKHPTVVGLIKASTTVELAVKRSQKLTRPSSVSVVTPSTPILSGRDRTASITGPQPVDSIKRREMETYKIQTLQKMLEQEKLNLERLKSDQNNPSYKLSEANIRKLREQLHQVGAEDAPTVKLQAAAGNKNTALLTPNQIQHLSASATHSNQQFHHLHHHHNLHNNNYPPQQQPASTSPAFLSLLPRSLSSLSLGTRKNKTEKDLTTSSPFGLTTDFLQQQRMSHQAESMSQSMHQHTSTPTSQQFFHPHQQQHRFKETGPTSKGKNKFLISRSLIEEDVPPPLPQRNPPRQLNLDLKNGNASPGGSHLVAPVSDLDRATSPQLNRSQQQQLPRSTDNSPSNAKSKRSKIKTKALSDPKMSTQMLLQMESASAAGAAGGSIEVDGGPPPLPPRLPGMMTEDMSRGSCQNLAQPNSVGTAFNYPLVSTTTAVQNDNLNIAFPLSQRPNIVQQLQQYQQQQQHQMSGGQATGALGQTPNLGKNKHRRVGSSPDNMHPRHPDRITKTTSGSWEIVEKDGESSPPGTPPLPYLSSSHMTVLEDPNENNRGAAAAGPGVFIESHQFTPMAGASSPIPISLHSSHMHAAQSNDTQKEIISMEDENSDLDEPFIDENGPFNNLTRLLEAENVTFLAIFLNYVISNSDPAPLLFYLITELYKEGTSKDMRKWAYEIHSTFLVPRAPLSWYRQDESLAREVDNVLQLEYDKVEILRTVFLRSRKRAKDLISEQLREFQQKRTAGLGTIYGPTDDKLAEAKTDKLREQIIDKYLMPNLHALIEDENGSPPEDVRKVALCSALSTVIYRIFNTRPPPSSIVERVHHFVSRDKSFKSRIMGKNRKMNVRGHPLVLRQYYEVTHCNHCQTIIWGVSPQGYHCTDCKLNIHRQCSKVVDESCPGPLPQAKRLAHNDKISKFMGKIRPRTSDVIGNEKRSRQDEELDVELTPDRGQASIVRQPSDRRPDANISIRSNGNTSCNTSGLNTTDLQSSFHGSCANDSINPGGGAGCNMDLSTSVASTTPSTSGSVAAGLSAFAELNALDTVDKEARRERYSQHPEHKSAPVSVNRSESYKERLSNKRNRNSRRKTSDPSLSSRPNDEQLDLGLSNATYVGSSNSSLSSAGGSESPSTSMEHFAAPGAAGGVQVPPMGLNQNQHPHLLIQQHAQQYCQQDSFQAGLAGAAGSSAASNSSFWNAGHPLPVARWTLESEDEDDVNEADWSSMVAAEVLAALTDAEKKRQEIINEIYQTERNHVRTLKLLDRLFFLPLYESGLLSQDHLLLLFPPALLSLREIHGAFEQSLKQRRIEHNHVVNTIGDLLADMFDGQSGVVLCEFAAQFCARQQIALEALKEKRNKDEMLQKLLKKSESHKACRRLELKDLLPTVLQRLTKYPLLFENLYKVTVRLLPENTTEAEAIQRAVESSKRILVEVNQAVKTAEDAHKLQNIQRKLDRSSYDKEEFKKLDLTQHHLIHDGNLTIKKNPSVQLHGLLFENMIVLLTKQDDKYYLKNLHTPLSITNKPVSPIMSIDADTLIRQEAADKNSFFLIKMKTSQMLELRAPSSSECKTWFKHFSDVAARQSKNRSKNASSNHDTSISDPALAAIPHSNTKESLELSTDTVQPLAATATLTTTPLAPMLPIATVTPAPATNNSNVSSLTGVQLRNPQRDATASESDADYVNTPKPRSSQNEVNRTMSIRSTGEPIQKYSANGTEANDVTLRHSQSTRESVRPGSTGEERNSTYGMVGGNSKRDSASIVCSNNSNNTRTLLMQSPLVDPTAIQVSISPAHTAEPVLTPGEKLRRLDASIRNDLLEKQKIICDIFRLPVEHYDQIVDIAMMPEAPKDSADIALAAYDQIQTLTKMLNEYMHVTPEQEVSAVSTAVCGHCHEKEKLRKKVAPSSSFSSSPPPLPPPNRQHAQAQAQIPPSRLMPKLQTLDLDEVAIHEDDDGYCEIDELRLPAIPSKPHERPTTPLAPFNTEPKTSQSVIDASKRQSTDAVPEGLLEQEPLEGDKTETKGEDNEVKTVPSDKLSESCNEERQCVEADITKEVADPTTSKNEAAASVDELPSQSREIKTAENASKSVADKKEDNEETIEEGVASTVDSSTQTSPTESPKETDKLTGGSSSTCGPNRIQHASVLEPSVPCHALSSIVTILNEQISMLLPKINERDMERERLRKENQHLRELLSALHDRQRVDEVKETPFDLKKLMHAEDVEFDDDIDAISNSSLTPTPTPIPTASPSASGQVETAEAMRITSTEDEE
Protein: Thioredoxin family protein (Q940I2)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
- At1g54500/F20D21_31
- Protein HHL1, chloroplastic
- Light-harvesting complex-like protein 3 isotype 1, chloroplastic
- Heat shock 70 kDa protein 18
- Protein ACTIVITY OF BC1 COMPLEX KINASE 3, chloroplastic
- DnaJ
Sequence:
MAGILVNNILPQPPILRSLSSSSRRSSIRTLVMVKASSSEPSESVSVSTKTSDDTGAVVVFTAPPGFKPPEPKRFAVKSGKLFDVLGAAIGLFFRFGTGVFVSGYSASFVSKEEIPADQYALRLGGITVKETAKVGPRPEKPIEIYEFEGCPFCRKVREMVAVLDLDILYYPCPRGSPNFRPKVKQMGGKQQFPYMVDPNTGVSMYESDGIIKYLSEKYGDGTVPLSLSLGALTAITAGFAMIGRMGKGNLYTPAKLPPKPLEFWAYEGSPFCKLVREVLVELELPHIQRSCARGSPKRQVLLEKAGHFQVPYLEDPNTGVAMFESAEIVEYLKQTYAA
Protein: E3 ubiquitin-protein ligase NHLRC1 (EC 2.3.2.27) (Malin) (NHL repeat-containing protein 1) (RING-type E3 ubiquitin transferase NHLRC1) (Q6VVB1)
Organism: Homo sapiens (Human)
Function: E3 ubiquitin-protein ligase. Together with the phosphatase EPM2A/laforin, appears to be involved in the clearance of toxic polyglucosan and protein aggregates via multiple pathways. In complex with EPM2A/laforin and HSP70, suppresses the cellular toxicity of misfolded proteins by promoting their degradation through the ubiquitin-proteasome system (UPS). Ubiquitinates the glycogen-targeting protein phosphatase subunits PPP1R3C/PTG and PPP1R3D in a laforin-dependent manner and targets them for proteasome-dependent degradation, thus decreasing glycogen accumulation. Polyubiquitinates EPM2A/laforin and ubiquitinates AGL and targets them for proteasome-dependent degradation. Also promotes proteasome-independent protein degradation through the macroautophagy pathway.
Subcellular location: Endoplasmic reticulum. Nucleus. Note=Localizes at the endoplasmic reticulum and, to a lesser extent, in the nucleus.
Interaction partners:
- Laforin
- Glycogen [starch] synthase, muscle
- Protein phosphatase 1 regulatory subunit 3C
- Glycogen debranching enzyme
- Cystatin-B
- PR domain zinc finger protein 8
- E3 ubiquitin-protein ligase CHIP
- BTB/POZ domain-containing protein KCTD7
- Glycogenin-1
- EPM2A-interacting protein 1
Sequence:
MAAEASESGPALHELMREAEISLLECKVCFEKFGHRQQRRPRNLSCGHVVCLACVAALAHPRTLALECPFCRRACRGCDTSDCLPVLHLIELLGSALRQSPAAHRAAPSAPGALTCHHTFGGWGTLVNPTGLALCPKTGRVVVVHDGRRRVKIFDSGGGCAHQFGEKGDAAQDIRYPVDVTITNDCHVVVTDAGDRSIKVFDFFGQIKLVIGGQFSLPWGVETTPQNGIVVTDAEAGSLHLLDVDFAEGVLRRTERLQAHLCNPRGVAVSWLTGAIAVLEHPLALGTGVCSTRVKVFSSSMQLVGQVDTFGLSLYFPSKITASAVTFDHQGNVIVADTSGPAILCLGKPEEFPVPKPMVTHGLSHPVALTFTKENSLLVLDTASHSIKVYKVDWG
Protein: RNA polymerase II subunit A C-terminal domain phosphatase (EC 3.1.3.16) (A0A8I6G995)
Organism: Rattus norvegicus (Rat)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123, ECO:0000256|RuleBase:RU366066}.
Interaction partners:
Sequence:
MTQHAPRKWVRSERRVKPVSEREQQCRRRPRWAPRPERPVFSFLTSVVTVRAARWVTMEAPPLAGVPTECTPAVAGAEVRCPGPAPLRLLEWKVTAGATVRIGSVLAVYEAAVSAQPAGPAPARAASGGCVRASRTERRLRSERAGVVRELCAQPGQVVAPGALLVRLEGCSHPVVMKGLCAECGQDLTQLQSKNGKQQVPLSTATVSMVHSVPELMVSSEQAEKLGREDQQRLHRNRKLVLMVDLDQTLIHTTEQHCPQMSNKGIFHFQLGRGEPMLHTRLRPHCKDFLEKIAKLYELHVFTFGSRLYAHTIAGFLDPEKKLFSHRILSRDECIDPFSKTGNLRNLFPCGDSMVCIIDDREDVWKFAPNLITVKKYVYFPGTGDVNAPPGARESQTRKKVNHSSKGADILEQALPVKDPEEGKPPGVEQSNGLGKASRELNGGEAVPGVFSSKTDEKETWSLTRASPASSSGGRELTEAPELPVSCEWDSRTAPGAHPTQGDATQGLDFDLSSDSESSESSRSEGQKSFSSASDGENEERRRRKKSPATQDRTKVPQHSGPHDTSGGRSAASPSGESGPLHPHDKVSDPDTQEEGERDSLCGLGNGSVDRKEAETESQNSEQSGVTAGESLDQSVGEEEEEDTDDDDHLIHLEEILVRVHTDYYTKYDRYLNKELEEAPDIRKIVPELKSKVLADVAVIFSGLHPTNFPVEKTREHYHATALGAKVLTQLVLSPDAPDRATHLIAARAGTEKVRQAQECKHLHVVSPEWLWSCLERWDKVEEQLFPLMDEDTRTHRDNSPAVFPDRHSMLPTALFHPTPIHSKAHPGPEVRIYDSNTGKLIRMGTQGPAPALSSAPLIHGEPSSFRWTTSLEKAVMTVRARRRRQKTKTVSRREHASPGSPGPQAPEESSRQGCPHLARGAPLARVRPEATREN
Protein: Rho GTPase activating protein 6 (cDNA FLJ59725, highly similar to Rho-GTPase-activating protein 6) (B4DN07)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MKRLHIFGPKIHSSGGLWQQKGDFTWNSMSGRSVRLRSVPIQSLSELERARLQEVAFYQLQQDCDLSCQITIPKDGQKRKKSLRKKLDSLGKEKNKDKEFIPQAFGMPLSQVIANDRAYKLKQDLQRDEQKDASDFVASLLPFGNKRQNKELSSSNSSLSSTSETPNESTSPNTPEPAPRARRRGAMSVDSITDLDDNQSRLLEALQLSLPAEAQSKKEKARDKKLSLNPIYRQVPRLVDSCCQHLEKHGLQTVGIFRVGSSKKRVRQLREEFDRGIDVSLEEEHSVHDVAALLKEFLRDMPDPLLTRELYTAFINTLLLEPEEQLGTLQLLIYLLPPCNCDTLHRLLQFLSIVARHADDNISKDGQEVTGNKMTSLNLATIFGPNLLHKQKSSDKEFSVQSSARAEESTAIIAVVQKMIENYEALFMVPPDLQNEVLISLLETDPDVVDYLLRRKASQSSSPDMLQSEVSFSVGGRHSSTDSNKASSGDISPYDNNSPVLSERSLLAMQEDAAPGGSEKLYRVPGQFMLVGHLSSSKSRESSPGPRLGKDLSEEPFDIWGTWHSTLKSGSKDPGMTGTTPLLNISSQEDHRQKDLRLIFKIYP
Protein: Sodium/hydrogen exchanger (B7YZY2)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
Interaction partners:
- Anion exchange protein
Sequence:
MSIRTEQDYDSATPALAQQMNLARRACWRIKSYSSESLFKTYASVITDTSANEIDAEAPPPPRDKTKTRIEPQIAPAKRNSSCTSSDWRGMFSKRTLLICALALILGSAQARPNTSAVGVAPRKVSQDIVDAVTQLNLGQSAPIDAVDVGLDPTPSARVPRPEPLKSGDENAKGDEGHKMERYPLSSVDFARVKTPFIIGIWILSASIAKIGFHMTPKLHLIFPESCLLIVVGVVIGVVLYFCTDVAVSPLTPNTFFFYMLPPIILDAGYFMPNRLFFDNLGTILLMAVVGTIFNIATIGGSLYACGKMGIYGESETPGLMDVFLFASLISAVDPVAVLAVFEEIHVNEILYIVVFGESLLNDAVTVVMYHMMESYNEIGLDKIIAQDIASGVGSFFVVALGGTAIGIIWGFLTGLVTRFTDHVRVIEPIFIFVMAYLAYLNAEIFHMSGILAITFCGITMKNYVESNISQKSHTTVKYALKMLSSSAETIIFMFLGVATVNNMHVWNTWFVVLTIAFCSVFRVIGVILLSALANRFRLHKLSRVDQFVMSYGGLRGAVAFALVLLVDENVVKQKNMFVTTTIAVIYFTVFLQGITIKPLVKILNVKRANKRKPTMNERIHERFMDHLMAGIEDIVGKTGNYNVRDKFKRFDNRFIRPLLIRDLKGAEPKIIETYSKLTMRDAMEVMRRNPSTIGQMTGTESMSALFRNYTNNYIGGSPSLTNLDNTCSRNLDMAELDYNPSKKDLTDARIHHLLAEELKPYRRHRRLSYSRHAVDDRDLSTQVNYKMQMNFRRMFNDRKHHKRSKRGASNKEAKENVKQNHVSFHDFQQNGTTKQLTNGTESSSNHSRKKSYRKRHTHNSLNKYRRLEIAEECQQNPNEINVVGPSDDWDDGLTFTAKSSPDSDRANNNSLIAHIQNLPGFDASKARIVVQHYAPKADDNPDTDIESPEQAIGPTAAELILPWRRDRSYQSIVAEHPIPEEDRNLSRESDGERRVATPTATESQLPWKRQGDECTDAVQQNEFPAWASNKEYLAYNSPSATFLGGINKPKQPKSVIGLFRRESSSSKAGSVGVGSTGAMDSAASGSETMVVSMSSQPPNAPSTSIHNPRLDKRSQSISSSSLGAGAHQLGPEGHSGPFPVTASHRRNVRRGSMLELSGDTIPEESSYQHGHSKSLCEPADSDEWEGAPLSAAGGANSELLMRMSGREPLLPRPSNTPRAQIRRMNAGAVGGAGVSQAGRKNQVTKALLDYEDSETDSDENDDDEDEDFDSYDDENIVVTTFTTPATGRRPGSSPGSGSEANTATTTTTSIRLTRNNDESII
Protein: Epsin-5 (Q03769)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Involved in the recruitment of clathrin to the Golgi network and endosomes to form clathrin coated vesicles. Plays a role in the trafficking of clathrin between the Golgi network and endosomes. Binds to membranes enriched in phosphatidylinositol-3,5-bisphosphate (PtdIns(3,5)P2) and, in association with VPS27, is involved in protein sorting at the multivesicular body (MVB).
Subcellular location: Cytoplasm. Endosome membrane; Peripheral membrane protein. Note=Found predominantly on endosomal structures.
Interaction partners:
- Clathrin heavy chain
- AP-1 complex subunit gamma-1
- Epsin-3
- Clathrin light chain
- AP-1 complex subunit beta-1
- ADP-ribosylation factor-binding protein GGA2
- AP-1 complex subunit sigma-1
- AP-1 complex subunit mu-1-I
- AP-2 complex subunit beta
- AP-2 complex subunit alpha
Sequence:
MDSLSKKIQNLGIHDIRNAARFAQNVIVQYEPYQIDIRRATNTDAWGPTPKHLAKVLRNRYQVPLYLMTEYTLKRLVDHIATRPKNLYEKARKDYVNYGSEWRVVLKCLVVIEFLLLNVDTGDELNQIRSCLLTHKHILTREIAQFKVKFSNDGKMEIHERGIRKKGELILQYLEDSQFLKKERAKNKKNALKIRQQGESSIYNANQISTSASYDNIDDDEFDADADGFDSEMDANNVTNFNVPVETEANSNTRRRSHMEEQRRQRREILREQIKNKEQQRKRKQQQDSIPDLIDLDDSTSTTNNITIDNGNNDNKNNNINSNSDDDDDEFGDFQSETSPDTTAPKTSNSKIDDLLDWDGPKSDTDTTAAAQTSLPFAEKKQQKARPQATKDKSKGNDAFSDLFSYSKSLV
Protein: Prostaglandin E synthase (EC 2.5.1.18) (EC 5.3.99.3) (Glutathione peroxidase PTGES) (Glutathione transferase PTGES) (Microsomal prostaglandin E synthase 1) (Q5IHX7)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Subcellular location: Cytoplasm, perinuclear region {ECO:0000256|ARBA:ARBA00004556}. Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
Interaction partners:
- Prostaglandin E synthase 3
- Prostaglandin-endoperoxide synthase 2a.
- Prostaglandin-endoperoxide synthase 1.
- Prostaglandin G/H synthase 2
- Prostaglandin E synthase 2
- Lipocalin-type prostaglandin D synthase-like protein
- Prostamide/prostaglandin F synthase
- Thromboxane-A synthase
- Prostaglandin D2 synthase b, tandem duplicate 2
- Carbonyl reductase 1-like
Sequence:
MLGSDIQLCFIFYSTLLILKMYIIAIITGQVRLRKKAFANPEDAERHGGVQFCRTDPYVERCRRAQQNDMENILPFLFLGAVYSMTSPSYAAAQLHFLIFFLGRVLHSVAYLLALKAPTRSLAYVIAQVPCISMAIQILMEVASFA
Protein: Rho GTPase activating protein 4 (A0A0G2JVF0)
Organism: Rattus norvegicus (Rat)
Interaction partners:
- Ral GTPase-activating protein subunit alpha-2
- Intersectin 2
- Actin nucleation-promoting factor WAS
Sequence:
MAAHGKLRRERGLQPEYEAQVKVMRGQLSEQLHCLELQGELRRDLLLELAEFMRRRAEVELEYSRGLDKLAERFTSRSGRLGGSSREQQSFRKEPTLLSPLHCWAMLLEHTRQQSRESATLSEVLAGPLAQRLSHIAEDVGRIVKKSKDLVQQLQDELLEVVSELQTQGYLAWASLQTKKTYHVYHLESMNAETKLREAERQEEKRSGKSALPTTTAASATTTITIETELHRKGSLKKGGRLVEKRQAKFLEHKLKCTKARNEYLLSLASVNAAVSNYYLHDILDLMDCCDTGFHLALEQALRSYTAAESRTQTSHMQGLGSLEEALEALDPPGDKAKVLEVHAMAFCPPLRFDYQPHEGDEVAEIQVEMELRDEILPRAQNIQSRLDQKTIETEEVNKTLKATLQALLEVVASEDGDILDSLQASPSTESLKSTSSDPGTRQAGRRRNQQQETETFYITKLQEYLSGRSILAKLQAKHEKLQEAIQRGNKEEQETSSWTQCTERKFHKSHHPYPGSQCTQRLFGGDLEKFIQSTGQPVPLVVKSCIRFINLNGLQHEGIFRVSGAQARILEIRDAFERGEDPLVEGCTAHDLDSVAGVLKLYFRSLEPPLFPLDMFNELLASAELEVVGERVELVSHLLSRLPRPVLVVLRYLFTFLNHLAQYSDENMMDSYNLAVCFGPTLLPVPAGQDPVALQGRVNQLVQTLILQPAWVFPPTAMLPGPIYEKCMAPPSASCLGDGQLESLAGEPELELKTGTKAQEDDSEGVVEAVACFAYTGRTAQELTFQQGDTLRLYARASSDWWRGEHAGVRGLIPHKYITLSEGDEKQMTGSGLQAMGESLSHPESVLTLEFTNRLELGTPPEALGPSGHRRHCLVPTSPEQHVEMDKAVAQNMDSVFKELLGKAAVRQGHGLASTASPSLGTRNLKPLACSSFSKNKVFSRGPGAPVSPSVSHPQGPDSTRKPV
Protein: COP9 signalosome complex subunit 9 (CSN acidic protein) (CSNAP) (Myeloma-overexpressed gene 2 protein) (Q8WXC6)
Organism: Homo sapiens (Human)
Function: Component of the COP9 signalosome complex (CSN), a complex involved in various cellular and developmental processes. The CSN complex is an essential regulator of the ubiquitin (Ubl) conjugation pathway by mediating the deneddylation of the cullin subunits of SCF-type E3 ligase complexes, leading to decrease the Ubl ligase activity of SCF-type complexes such as SCF, CSA or DDB2. The complex is also involved in phosphorylation of p53/TP53, c-jun/JUN, IkappaBalpha/NFKBIA, ITPK1 and IRF8/ICSBP, possibly via its association with CK2 and PKD kinases. CSN-dependent phosphorylation of TP53 and JUN promotes and protects degradation by the Ubl system, respectively. Plays a role in cell proliferation.
Subcellular location: [Isoform 1]: Nucleus {ECO:0000269|PubMed:26456823}. Cytoplasm {ECO:0000269|PubMed:26456823}. Nucleus, nucleoplasm {ECO:0000269|PubMed:26456823}. Note=Excluded from the nucleolus. Recruited to the nucleoplasm and chromatin following DNA damage induction. {ECO:0000269|PubMed:26456823}.; SUBCELLULAR LOCATION: [Isoform 2]: Nucleus, nucleoplasm {ECO:0000269|PubMed:23776465}. Note=Excluded from the nucleolus. {ECO:0000269|PubMed:23776465}.
Interaction partners:
- COP9 signalosome complex subunit 8
- COP9 signalosome complex subunit 6
- COP9 signalosome complex subunit 5
- COP9 signalosome complex subunit 3
- COP9 signalosome complex subunit 1
- COP9 signalosome complex subunit 2
- COP9 signalosome complex subunit 4
- COP9 signalosome complex subunit 7a
- COP9 signalosome complex subunit 7b
- Growth factor receptor-bound protein 2
Sequence:
MKPAVDEMFPEGAGPYVDLDEAGGSTGLLMDLAANEKAVHADFFNDFEDLFDDDDIQ