wanglab/gogpt-training-data huggingface dataset:
Protein: Eukaryotic translation initiation factor 2 subunit 2 (Eukaryotic translation initiation factor 2 subunit beta) (A0A8I6G5P0)
Organism: Rattus norvegicus (Rat)
Interaction partners:
Sequence:
MSGDEMIFDPTMSKKKKKKKKPFMLDEEGDAQTEETQPSETKEVEPEPAEEKDVEADEEDSRKKDASDDLDDLNFFNQKKKKKKTKKIFDIDEAEEAIKDVKIESDAQEPAEPEDDLDIMLGNKKKKKKNVKFPDEDEILEKDEALEDEDSKKDDGISFSNQTGPAWAGSERDYTYEELLNRVFNIMREKNPDMVAGEKRKFVMKPPQVVRVGTKKTSFVNFTDICKLLHRQPKHLLAFLLAELGTSGSIDGNNQLVIKGRFQQKQIENVLRRYIKEYVTCHTCRSPDTILQKDTRLYFLQCETCHSRCSVASIKTGFQAVTGKRAQLRFGWTGYHQSGCTIELKTR
Protein: Galectin (C0PUZ0)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MISVNGQHFAAYTHRIPYRDVRILEVKGDVSNVEMKRTLVLKYPERLPQSEANNIELHIDDGINEIDASVEETVKIPHEWCIISAPNTQSDSSPKRNNSSNDLGLTLPYYGALPPNSLVDGRCLKIEGRVRLLPHSFYINLQQGQDIWPHPVIAFHLNPRFSKASSGAIGKAVVCRNAWLNGAWAQEERSEFDTNFRPGRSFCLAIVCTKTSFEVYVNRQFMTDFKYKVSPEVVDTVYIQGDVKLWNVTLEKNQMIKGKNMRVYQNPWFFSE
Protein: Trehalose synthase complex regulatory subunit TSL1 (Alpha,alpha-trehalose-phosphate synthase [UDP-forming] 123 kDa subunit) (P38427)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Regulatory subunit of the trehalose synthase complex that catalyzes the production of trehalose from glucose-6-phosphate and UDP-glucose in a two step process. May stabilize the trehalose synthase complex, and confer sensitivity to physiological concentrations of phosphate and to fructose 6-phosphate.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:14562095}.
Interaction partners:
- Alpha,alpha-trehalose-phosphate synthase 56 kDa subunit
- Trehalose synthase complex regulatory subunit TPS3
- Trehalose-phosphatase
- Glycogen [starch] synthase isoform 2
- Cytosolic neutral trehalase
- Glycogen [starch] synthase isoform 1
- Periplasmic acid trehalase ATH1
- UTP--glucose-1-phosphate uridylyltransferase
- Probable trehalase
- Probable UTP--glucose-1-phosphate uridylyltransferase
Sequence:
MALIVASLFLPYQPQFELDTSLPENSQVDSSLVNIQAMANDQQQQRALSNNISQESLVAPAPEQGVPPAISRSATRSPSAFNRASSTTNTATLDDLVSSDIFMENLTANATTSHTPTSKTMLKPRKNGSVERFFSPSSNIPTDRIASPIQHEHDSGSRIASPIQQQQQDPTTNLLKNVNKSLLVHSLLNNTSQTSLEGPNNHIVTPKSRAGNRPTSAATSLVNRTKQGSASSGSSGSSAPPSIKRITPHLTASAAKQRPLLAKQPSNLKYSELADISSSETSSQHNESDPDDLTTAPDEEYVSDLEMDDAKQDYKVPKFGGYSNKSKLKKYALLRSSQELFSRLPWSIVPSIKGNGAMKNAINTAVLENIIPHRHVKWVGTVGIPTDEIPENILANISDSLKDKYDSYPVLTDDDTFKAAYKNYCKQILWPTLHYQIPDNPNSKAFEDHSWKFYRNLNQRFADAIVKIYKKGDTIWIHDYHLMLVPQMVRDVLPFAKIGFTLHVSFPSSEVFRCLAQREKILEGLTGADFVGFQTREYARHFLQTSNRLLMADVVHDEELKYNGRVVSVRFTPVGIDAFDLQSQLKDGSVMQWRQLIRERWQGKKLIVCRDQFDRIRGIHKKLLAYEKFLVENPEYVEKSTLIQICIGSSKDVELERQIMIVVDRINSLSTNISISQPVVFLHQDLDFSQYLALSSEADLFVVSSLREGMNLTCHEFIVCSEDKNAPLLLSEFTGSASLLNDGAIIINPWDTKNFSQAILKGLEMPFDKRRPQWKKLMKDIINNDSTNWIKTSLQDIHISWQFNQEGSKIFKLNTKTLMEDYQSSKKRMFVFNIAEPPSSRMISILNDMTSKGNIVYIMNSFPKPILENLYSRVQNIGLIAENGAYVSLNGVWYNIVDQVDWRNDVAKILEDKVERLPGSYYKINESMIKFHTENAEDQDRVASVIGDAITHINTVFDHRGIHAYVYKNVVSVQQVGLSLSAAQFLFRFYNSASDPLDTSSGQITNIQTPSQQNPSDQEQQPPASPTVSMNHIDFACVSGSSSPVLEPLFKLVNDEASEGQVKAGHAIVYGDATSTYAKEHVNGLNELFTIISRIIED
Protein: Squalene monooxygenase (EC 1.14.14.17) (Squalene epoxidase) (SE) (P52020)
Organism: Rattus norvegicus (Rat)
Function: Catalyzes the stereospecific oxidation of squalene to (S)-2,3-epoxysqualene, and is considered to be a rate-limiting enzyme in steroid biosynthesis.
Subcellular location: Microsome membrane {ECO:0000269|PubMed:7814369}; Peripheral membrane protein {ECO:0000250|UniProtKB:Q14534}. Endoplasmic reticulum membrane; Peripheral membrane protein {ECO:0000250|UniProtKB:Q14534}.
Interaction partners:
- Lanosterol synthase
- Squalene synthase
- Lanosterol 14-alpha demethylase
- Methylsterol monooxygenase 1
- Hydroxymethylglutaryl-CoA synthase, cytoplasmic
- 3-hydroxy-3-methylglutaryl-coenzyme A reductase
- Sterol-4-alpha-carboxylate 3-dehydrogenase, decarboxylating
- 7-dehydrocholesterol reductase
- Sigma non-opioid intracellular receptor 1
- Hydroxymethylglutaryl-CoA synthase, mitochondrial
Sequence:
MWTFLGIATFTYFYKKCGDVTLANKELLLCVLVFLSLGLVLSYRCRHRNGGLLGRHQSGSQFAAFSDILSALPLIGFFWAKSPPESEKKEQLESKRRRKEVNLSETTLTGAATSVSTSSVTDPEVIIIGSGVLGSALATVLSRDGRTVTVIERDLKEPDRILGECLQPGGYRVLRELGLGDTVESLNAHHIHGYVIHDCESRSEVQIPYPVSENNQVQSGVAFHHGKFIMSLRKAAMAEPNVKFIEGVVLRLLEEDDAVIGVQYKDKETGDTKELHAPLTVVADGLFSKFRKNLISNKVSVSSHFVGFIMKDAPQFKANFAELVLVDPSPVLIYQISPSETRVLVDIRGELPRNLREYMTEQIYPQIPDHLKESFLEACQNARLRTMPASFLPPSSVNKRGVLLLGDAYNLRHPLTGGGMTVALKDIKIWRQLLKDIPDLYDDAAIFQAKKSFFWSRKRSHSFVVNVLAQALYELFSATDDSLRQLRKACFLYFKLGGECLTGPVGLLSILSPDPLLLIRHFFSVAVYATYFCFKSEPWATKPRALFSSGAILYKACSIIFPLIYSEMKYLVH
Protein: Minichromosome maintenance protein MCM (EC 3.6.4.12) (Q9UXG1)
Organism: Saccharolobus solfataricus (strain ATCC 35092 / DSM 1617 / JCM 11322 / P2) (Sulfolobus solfataricus)
Function: Presumptive replicative helicase. Has ATPase and DNA helicase activities. The latter preferentially melts 5'-tailed oligonucleotides and is stimulated by the SSB protein (single-stranded DNA binding protein). The active ATPase sites in the MCM ring are formed through the interaction surfaces of two neighboring subunits such that a critical structure of a conserved arginine finger motif is provided in trans relative to the ATP-binding site of the Walker A box of the adjacent subunit. The helicase function is proposed to use a partially sequential mode of ATP hydrolysis; the complex appears to tolerate multiple catalytically inactive subunits.
Interaction partners:
- ORC1-type DNA replication protein 2
- ORC1-type DNA replication protein 1
- ORC1-type DNA replication protein 3
- DNA primase large subunit PriL
- DNA primase small subunit PriS
- DNA polymerase 2
- DNA polymerase 3
- DNA polymerase 1
- Single-stranded DNA binding protein Ssb
- Replication factor C small subunit
Sequence:
MEIPSKQIDYRDVFIEFLTTFKGNNNQNKYIERINELVAYRKKSLIIEFSDVLSFNENLAYEIINNTKIILPILEGALYDHILQLDPTYQRDIEKVHVRIVGIPRVIELRKIRSTDIGKLITIDGILVKVTPVKERIYKATYKHIHPDCMQEFEWPEDEEMPEVLEMPTICPKCGKPGQFRLIPEKTKLIDWQKAVIQERPEEVPSGQLPRQLEIILEDDLVDSARPGDRVKVTGILDIKQDSPVKRGSRAVFDIYMKVSSIEVSQKVLDEVIISEEDEKKIKDLAKDPWIRDRIISSIAPSIYGHWELKEALALALFGGVPKVLEDTRIRGDIHILIIGDPGTAKSQMLQFISRVAPRAVYTTGKGSTAAGLTAAVVREKGTGEYYLEAGALVLADGGIAVIDEIDKMRDEDRVAIHEAMEQQTVSIAKAGIVAKLNARAAVIAAGNPKFGRYISERPVSDNINLPPTILSRFDLIFILKDQPGEQDRELANYILDVHSGKSTKNIIDIDTLRKYIAYARKYVTPKITSEAKNLITDFFVEMRKKSSETPDSPILITPRQLEALIRISEAYAKMALKAEVTREDAERAINIMRLFLESVGVDMESGKIDIDTIMTGKPKSAREKMMKIIEIIDSLAVSSECAKVKDILKEAQQVGIEKSNIEKLLTDMRKSGIIYEAKPECYKKV
Protein: Vicilin Pin k 2.0101 (7S globulin) (7S seed storage protein) (Allergen Pin k 2) (Vicilin-type seed storage protein) (allergen Pin k 2.0101) (V9VGU0)
Organism: Pinus koraiensis (Korean pine)
Function: Seed storage protein.
Interaction partners:
Sequence:
MAFVSLLTILLAISSSSVALTEPVASMADQGVFPEQHGRGHHGVFPEEHGRGHHRGGREEEREENPYVFHSDRFRIRASSEAGEIRALPNFGEVSELLEGISRYRVTCIEMKPNTVMLPHYIDAKWILYVTGGRGYIAYVQQNELVKRKLEEGDVFGVPSGHTFYLVNNDDHNSLRIASLLRTESTMRGEYEPFYVAGGRNPETVYSAFSDDVLEAAFNTDVQKLEHIFGAHRRGVIFYANEEQIREMMRRGGFSAESTSASEQPKPFNLRNQKPDFENDNGRFTRAGPKDNPFLDSVDVTVGFGVLNPGTMTAPSHNTKATSIAIVMEGEGRIEMACPHLGQEHGWSSPRERGHQDINYERVRARLRTGTVYVVPAGHPITEIASTNGRLEILWFDINTSGNEREFLAGKNNVLQTLEKEVRHLSFNIPRGEEIEEVLQAQKDQVILRGPQRQRRDEPRSSS
Protein: SUP35 protein (Q91855)
Organism: Xenopus laevis (African clawed frog)
Interaction partners:
Sequence:
ITGTTLFPPTWEVLPTLPTPCLTPSAPLIKQLVYPNPTHPEMDASDSAPDSWEQADMEATEAQLNNSMAALNVNAKPFVPNVNAVEFVPSFLVGSAPSDGQEEEQQQQGSCTTVGMDVSEPVVENGETEMSPEESWDHKEEPIEAEPGGGSEGDGGTTEEGTSEMMEEEEEIPKPKTIVVPPDAPKKEHVNVVFIGHVDAGKSTIGGQIMYLTGMVEKRTLEKYEREAKEKNRETWYLSWALDTNQEERDKGKTVEVGRAYFETEKKHFTILDAPGHKSFVPNMIGGASQADLAVLVISARKGEFETGFEKGGQTREHAMLAKTAGVKHLIVLINKMDDPTVNWSNDRYEECKEKLVPFLKKVGFNPKKDIYFMPCSGLTGANLKEPVETCPWYIGLAFISYLDSLPNFNRSLDGPVRLPIVDKYKDMGTVILGKLESGSICKGQQLAMMPNKHIVEVLSLLSDEVETELVAPGENLKLRLKGIEEEEILPGFILCDPNNLCHSGRTFDAQIVIIEHKSIICPGYNAVLHIHTCIEEVEITALICMVDKKSGEKSKTRPRFVKQDQVCIARLRTAGTICLETFKDFPQMGRFTLRDEGKTIAIGKVLKLVPEKD
Protein: Recoverin a (Recoverin-1a) (Zgc:114180) (Q4V8S2)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Interaction partners:
- Rhodopsin kinase grk7a
- G protein-coupled receptor kinase
- G protein-coupled receptor kinase
- Rhodopsin kinase grk7-b
- Rhodopsin
- Green-sensitive opsin-2
- Rhodopsin
- Green-sensitive opsin-4
- Rhodopsin.
- Green-sensitive opsin-3
Sequence:
MGNTKSGALSKELLEDLKLNTKYTEEELCAWYTSFLKECPSGRITKEQFEGIYASFFPDADPTAYARHVFRSFDTNADGTLDFKEYIVALHLTSSGKTLRKLEWAFALYDVDGNGTISKNEVQEIVRSIFNMVPVEDQKNLPDDENTPEKRADKIWAFFGKQDNDKIGEGEFIQGVMENKDILRLIQYDEPKKIQEKLKEKKH
Protein: Decaprenylphosphoryl-beta-D-ribose oxidase (EC 1.1.98.3) (Decaprenylphospho-beta-D-ribofuranose 2-dehydrogenase) (Decaprenylphosphoryl-beta-D-ribofuranose 2'-epimerase subunit DprE1) (Decaprenyl-phosphoribose 2'-epimerase subunit 1) (Decaprenylphosphoryl-beta-D-ribofuranose 2'-oxidase) (Decaprenylphosphoryl-beta-D-ribose 2-epimerase flavoprotein subunit) (FAD-dependent decaprenylphosphoryl-beta-D-ribofuranose 2-oxidase) (P9WJF1)
Organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Function: Component of the DprE1-DprE2 complex that catalyzes the 2-step epimerization of decaprenyl-phospho-ribose (DPR) to decaprenyl-phospho-arabinose (DPA), a key precursor that serves as the arabinose donor required for the synthesis of cell-wall arabinans. DprE1 catalyzes the first step of epimerization, namely FAD-dependent oxidation of the C2' hydroxyl of DPR to yield the keto intermediate decaprenyl-phospho-2'-keto-D-arabinose (DPX). The intermediate DPX is then transferred to DprE2 subunit of the epimerase complex, most probably through a 'substrate channel' at the interface of DprE1-DprE2 complex. Can also use farnesyl-phosphoryl-beta-D-ribofuranose (FPR) as substrate in vitro. Appears to be essential for the growth and survival of M.tuberculosis.
Subcellular location: Periplasm {ECO:0000269|PubMed:25906160}.
Interaction partners:
- Decaprenylphosphoryl-2-keto-beta-D-erythro-pentose reductase
- Probable arabinosyltransferase C
- Decaprenyl-phosphate phosphoribosyltransferase
- Arabinogalactan biosynthesis recruiting protein Rv3789
- Galactan 5-O-arabinofuranosyltransferase
- Decaprenylphosphoryl-5-phosphoribose phosphatase
- Probable arabinosyltransferase A
- Probable arabinosyltransferase B
- Uncharacterized oxidoreductase Rv2073c
- Trehalose monomycolate exporter MmpL3
Sequence:
MLSVGATTTATRLTGWGRTAPSVANVLRTPDAEMIVKAVARVAESGGGRGAIARGLGRSYGDNAQNGGGLVIDMTPLNTIHSIDADTKLVDIDAGVNLDQLMKAALPFGLWVPVLPGTRQVTVGGAIACDIHGKNHHSAGSFGNHVRSMDLLTADGEIRHLTPTGEDAELFWATVGGNGLTGIIMRATIEMTPTSTAYFIADGDVTASLDETIALHSDGSEARYTYSSAWFDAISAPPKLGRAAVSRGRLATVEQLPAKLRSEPLKFDAPQLLTLPDVFPNGLANKYTFGPIGELWYRKSGTYRGKVQNLTQFYHPLDMFGEWNRAYGPAGFLQYQFVIPTEAVDEFKKIIGVIQASGHYSFLNVFKLFGPRNQAPLSFPIPGWNICVDFPIKDGLGKFVSELDRRVLEFGGRLYTAKDSRTTAETFHAMYPRVDEWISVRRKVDPLRVFASDMARRLELL
Protein: Nucleosome assembly protein 1-like 3 (Q8IYV1)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MAEADFKMVSEPVAHGVAEEEMASSTSDSGEESDSSSSSSSTSDSSSSSSTSGSSSGSGSSSSSSGSTSSRSRLYRKKRVPEPSRRARRAPLGTNFVDRLPQAVRNRVQALRNIQDECDKVDTLFLKAIHDLERKYAELNKPLYDRRFQIINAEYEPTEEECEWNSEDEEFSSDEEVQDNTPSEMPPLEGEEEENPKENPEVKAEEKEVPKEIPEVKDEEKEVAKEITEVKAEEKADSKDCMEATPEVKEDPKEVPQVKADDKEQPKATEAKARAAVRETHKRVPEERLQDSVDLKRARKGKPKREDPKGIPDYWLIVLKNVDKLGPMIQKYDEPILKFLSDVSLKFSKPGQPVSYTFEFHFLPNPYFRNEVLVKTYIIKAKPDHNDPFFSWGWEIEDCKGCKIDWRRGKDVTVTTTQSRTTATGEIEIQPRVVPNASFFNFFSPPEIPMIGKLEPREDAILDEDFEIGQILHDNVILKSIYYYTGEVNGTYYQFGKHYGNKKYRK
Protein: Non-structural protein V (Non-structural protein NS1) (P30927)
Organism: Mumps virus (strain Enders) (MuV)
Function: Plays an essential role in the inhibition of host immune response. Prevents the establishment of cellular antiviral state by blocking interferon-alpha/beta (IFN-alpha/beta) production and signaling pathway. Interacts with host IFIH1/MDA5 and DHX58/LGP2 to inhibit the transduction pathway involved in the activation of IFN-beta promoter, thus protecting the virus against cell antiviral state. Blocks the type I and II interferon signaling pathways by interacting with host STAT1, STAT2 and STAT3, and mediating their ubiquitination and subsequent proteasomal degradation (By similarity).
Subcellular location: Virion {ECO:0000250|UniProtKB:Q8QV69}. Host cytoplasm {ECO:0000305}.
Interaction partners:
Sequence:
MDQFIKQDETGDLIETGMNVANHFLSAPIQGTNSLSKASIIPGVAPVLIGNPEQKNIQHPTASHQGSKSKGRGSGVRSIIVPPSEAGNGGTQIPEPLFAQTGQGGIVTTVYQDPTIQPTGSYRSVELTKIGKERMINRFVEKPRISTPVTEFKRGAGSGCSRPDNPRGGHRREWSLSWVQGEVRVFEWCNPICSPITAAARFHSCKCGNCPAKCDQCERDYGPP
Protein: Evasin P1126 (A0A023FF81)
Organism: Amblyomma cajennense (Cayenne tick) (Acarus cajennensis)
Function: Salivary chemokine-binding protein which binds to host chemokines CXCL1, CXCL2, CXCL3, CXCL4, CXCL5, CXCL6, CXCL7, CXCL10 and CXCL11.
Subcellular location: Secreted {ECO:0000305}.
Interaction partners:
Sequence:
MTSHSAVRIAIFAVIALHSIFECLSKPQILQRTDKSTDSEWDPQTCPETCIPSKNITCSDGCVCVKLGEEEEGTCFNMTGVDWLGSPSDD
Protein: A-factor-processing enzyme (EC 3.4.24.-) (Insulin-degrading enzyme homolog) (Q06010)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Involved in the N-terminal endoproteolytic cleavage of the P2 precursor of the a-factor mating pheromone. Capable of proteolysing the established mammalian insulin-degrading enzymes (IDEs) substrates amyloid-beta peptide and insulin B-chain.
Subcellular location: Membrane {ECO:0000269|PubMed:15944156}; Peripheral membrane protein {ECO:0000269|PubMed:15944156}.
Interaction partners:
- CAAX prenyl protease 1
- Presequence protease, mitochondrial
- CAAX prenyl protease 2
- Ubiquitin-ribosomal protein eS31 fusion protein
- Protein-S-isoprenylcysteine O-methyltransferase
- Ubiquitin carboxyl-terminal hydrolase 12
Sequence:
MGVSLLASSSAFVTKPLLTQLVHLSPISLNFTVRRFKPFTCLSRYYTTNPYNMTSNFKTFNLDFLKPDLDERSYRFIELPNKLKALLIQDPKADKAAASLDVNIGAFEDPKNLPGLAHFCEHLLFMGSEKFPDENEYSSYLSKHGGSSNAYTASQNTNYFFEVNHQHLFGALDRFSGFFSCPLFNKDSTDKEINAVNSENKKNLQNDIWRIYQLDKSLTNTKHPYHKFSTGNIETLGTLPKENGLNVRDELLKFHKNFYSANLMKLCILGREDLDTLSDWTYDLFKDVANNGREVPLYAEPIMQPEHLQKIIQVRPVKDLKKLEISFTVPDMEEHWESKPPRILSHLIGHEGSGSLLAHLKKLGWANELSAGGHTVSKGNAFFAVDIDLTDNGLTHYRDVIVLIFQYIEMLKNSLPQKWIFNELQDISNATFKFKQAGSPSSTVSSLAKCLEKDYIPVSRILAMGLLTKYEPDLLTQYTDALVPENSRVTLISRSLETDSAEKWYGTAYKVVDYPADLIKNMKSPGLNPALTLPRPNEFVSTNFKVDKIDGIKPLDEPVLLLSDDVSKLWYKKDDRFWQPRGYIYLSFKLPHTHASIINSMLSTLYTQLANDALKDVQYDAACADLRISFNKTNQGLAITASGFNEKLIILLTRFLQGVNSFEPKKDRFEILKDKTIRHLKNLLYEVPYSQMSNYYNAIINERSWSTAEKLQVFEKLTFEQLINFIPTIYEGVYFETLIHGNIKHEEALEVDSLIKSLIPNNIHNLQVSNNRLRSYLLPKGKTFRYETALKDSQNVNSCIQHVTQLDVYSEDLSALSGLFAQLIHEPCFDTLRTKEQLGYVVFSSSLNNHGTANIRILIQSEHTTPYLEWRINNFYETFGQVLRDMPEEDFEKHKEALCNSLLQKFKNMAEESARYTAAIYLGDYNFTHRQKKAKLVANITKQQMIDFYENYIMSENASKLILHLKSQVENKELNENELDTAKYPTGQLIEDVGAFKSTLFVAPVRQPMKDFEISAPPKLNNSSESE
Protein: Eukaryotic translation initiation factor 2-alpha kinase 3 (EC 2.7.11.1) (PRKR-like endoplasmic reticulum kinase) (Pancreatic eIF2-alpha kinase) (Protein tyrosine kinase EIF2AK3) (EC 2.7.10.2) (Q9Z2B5)
Organism: Mus musculus (Mouse)
Function: Metabolic-stress sensing protein kinase that phosphorylates the alpha subunit of eukaryotic translation initiation factor 2 (EIF2S1/eIF-2-alpha) in response to various stress conditions. Key activator of the integrated stress response (ISR) required for adaptation to various stress, such as unfolded protein response (UPR) and low amino acid availability. EIF2S1/eIF-2-alpha phosphorylation in response to stress converts EIF2S1/eIF-2-alpha in a global protein synthesis inhibitor, leading to a global attenuation of cap-dependent translation, while concomitantly initiating the preferential translation of ISR-specific mRNAs, such as the transcriptional activators ATF4 and QRICH1, and hence allowing ATF4- and QRICH1-mediated reprogramming. Serves as a critical effector of unfolded protein response (UPR)-induced G1 growth arrest due to the loss of cyclin-D1 (CCND1). Involved in control of mitochondrial morphology and function.
Subcellular location: Endoplasmic reticulum membrane {ECO:0000269|PubMed:9930704}; Single-pass type I membrane protein {ECO:0000255}. Note=Localizes to the Localizes to endoplasmic reticulum membrane (PubMed:11430819). Also present at mitochondria-endoplasmic reticulum contact sites; where it interacts with ATAD3A (By similarity). {ECO:0000250|UniProtKB:Q9NZJ5, ECO:0000269|PubMed:11430819}.
Interaction partners:
- Endoplasmic reticulum chaperone BiP
- Eukaryotic translation initiation factor 2 subunit 1
- Cyclic AMP-dependent transcription factor ATF-4
- Nuclear factor erythroid 2-related factor 2
- Presenilin-1
- Inhibitor of nuclear factor kappa-B kinase subunit alpha
- Inhibitor of nuclear factor kappa-B kinase subunit beta
- NF-kappa-B essential modulator
- Presenilin-2
- Interferon induced protein with tetratricpeptide repeats 1B like 1
Sequence:
MERATRPGPRALLLLLFLLLGCAAGISAVAPARSLLAPASETVFGLGAAAAPTSAARVPAVATAEVTVEDAEALPAAAGEPESRATEPDDDVELRPRGRSLVIISTLDGRIAALDAENDGKKQWDLDVGSGSLVSSSLSKPEVFGNKMIIPSLDGDLFQWDRDRESMEAVPFTVESLLESSYKFGDDVVLVGGKSLITYGLSAYSGKLRYICSALGCRRWDSDEMEEEEDILLLQRTQKTVRAVGPRSGSEKWNFSVGHFELRYIPDMETRAGFIESTFKPGGNKEDSKIISDVEEQEATMLDTVIKVSVADWKVMAFSRKGGRLEWEYQFCTPIASAWLVRDGKVIPISLFDDTSYTASEEALGDEEDIVEAARGATENSVYLGMYRGQLYLQSSVRVSEKFPTSPKALESVNGENAIIPLPTIKWKPLIHSPSRTPVLVGSDEFDKCLSNDKYSHEEYSNGALSILQYPYDNGYYLPYYKRERNKRSTQITVRFLDSPHYSKNIRKKDPILLLHWWKEIFGTILLCIVATTFIVRRLFHPQPHRQRKESETQCQTESKYDSVSADVSDNSWNDMKYSGYVSRYLTDFEPIQCMGRGGFGVVFEAKNKVDDCNYAIKRIRLPNRELAREKVMREVKALAKLEHPGIVRYFNAWLETPPEKWQEEMDEIWLKDESTDWPLSSPSPMDAPSVKIRRMDPFSTKEQIEVIAPSPERSRSFSVGISCGQTSSSESQFSPLEFSGTDCGDNSDSADAAYNLQDSCLTDCEDVEDGTVDGNDEGHSFELCPSEASPYTRSREGTSSSIVFEDSGCGNASSKEEPRGNRLHDGNHYVNKLTDLKCSSSRSSSEATTLSTSPTRPTTLSLDFTKNTVGQLQPSSPKVYLYIQMQLCRKENLKDWMNRRCSLEDREHGVCLHIFLQIAEAVEFLHSKGLMHRDLKPSNIFFTMDDVVKVGDFGLVTAMDQDEEEQTVLTPMPAYATHTGQVGTKLYMSPEQIHGNNYSHKVDIFSLGLILFELLYPFSTQMERVRILTDVRNLKFPLLFTQKYPQEHMMVQDMLSPSPTERPEATDIIENAIFENLEFPGKTVLRQRSRSMSSSGTKHSRQPSCSYSPLPGN
Protein: Eukaryotic translation elongation factor, selenocysteine-specific (RE67487p) (Q9W2H0)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
- GH01354p
- tRNA selenocysteine-associated protein 1
- Eukaryotic translation initiation factor 2 subunit 2
- Eukaryotic translation initiation factor 2 subunit 1
- Phosphoseryl tRNA kinase, isoform A
- O-phosphoseryl-tRNA
- Small ribosomal subunit protein uS3
- Small ribosomal subunit protein eS6
- Eukaryotic translation initiation factor 5
- Eukaryotic translation initiation factor 3 subunit B
Sequence:
MPINFNIGLLGHVDSGKTTLAKALSSISSTAAFDKNPQSVERGITLDLGFSGLLVDAPAHLPQGEQLQFTFVDCPGHASLIRTIIGGAQIIDLMLLVVDAQKGKQTQTAECLIIGELLQKKLIVVINKIDVYPENQRASKLEKLRLRLAKTLEATTFGGQVPICAVSALQGTHIAELREVLREAYFQPQRNLADPLFMYVDHCFGIKGQGTVCTGTLLQGKVQVNNVIELPALGEQRKVKSIQMFRKNVTSASMGDRIGLCVTQFNAKLLERGIITQPGYLKPIYAVCLQFKPIRYYKEVIKSMRKMHISVGHNTVMANVTLFRDTDGTTSTFQLDKEYEYMEDVQPAEVQHNDVIYALLQFESPVLSPPHSTLIASKLDMDVHSTSCRLAFWGRIAWQTHSSKYFQEELPKLRIFKRKQKVGSIQRVVNSSEVIVQNLFKDAKRDLYVGKNVELSTGEKGRIERTFGQTSKVAITFQDALSPETISNVKNVKVLLNCKKYVFNKQAGLFQ
Protein: Toll-like receptor 3 (CD antigen CD283) (O15455)
Organism: Homo sapiens (Human)
Function: Key component of innate and adaptive immunity. TLRs (Toll-like receptors) control host immune response against pathogens through recognition of molecular patterns specific to microorganisms. TLR3 is a nucleotide-sensing TLR which is activated by double-stranded RNA, a sign of viral infection. Acts via the adapter TRIF/TICAM1, leading to NF-kappa-B activation, IRF3 nuclear translocation, cytokine secretion and the inflammatory response.
Subcellular location: Endoplasmic reticulum membrane; Single-pass type I membrane protein. Endosome membrane. Early endosome {ECO:0000269|PubMed:25736436}.
Interaction partners:
- Protein unc-93 homolog B1
- Myeloid differentiation primary response protein MyD88
- TIR domain-containing adapter molecule 1
- TNF receptor-associated factor 6
- Receptor-interacting serine/threonine-protein kinase 1
- Interferon beta
- Serine/threonine-protein kinase TBK1
- TGF-beta-activated kinase 1 and MAP3K7-binding protein 2
- Mitogen-activated protein kinase kinase kinase 7
- TNF receptor-associated factor 3
Sequence:
MRQTLPCIYFWGGLLPFGMLCASSTTKCTVSHEVADCSHLKLTQVPDDLPTNITVLNLTHNQLRRLPAANFTRYSQLTSLDVGFNTISKLEPELCQKLPMLKVLNLQHNELSQLSDKTFAFCTNLTELHLMSNSIQKIKNNPFVKQKNLITLDLSHNGLSSTKLGTQVQLENLQELLLSNNKIQALKSEELDIFANSSLKKLELSSNQIKEFSPGCFHAIGRLFGLFLNNVQLGPSLTEKLCLELANTSIRNLSLSNSQLSTTSNTTFLGLKWTNLTMLDLSYNNLNVVGNDSFAWLPQLEYFFLEYNNIQHLFSHSLHGLFNVRYLNLKRSFTKQSISLASLPKIDDFSFQWLKCLEHLNMEDNDIPGIKSNMFTGLINLKYLSLSNSFTSLRTLTNETFVSLAHSPLHILNLTKNKISKIESDAFSWLGHLEVLDLGLNEIGQELTGQEWRGLENIFEIYLSYNKYLQLTRNSFALVPSLQRLMLRRVALKNVDSSPSPFQPLRNLTILDLSNNNIANINDDMLEGLEKLEILDLQHNNLARLWKHANPGGPIYFLKGLSHLHILNLESNGFDEIPVEVFKDLFELKIIDLGLNNLNTLPASVFNNQVSLKSLNLQKNLITSVEKKVFGPAFRNLTELDMRFNPFDCTCESIAWFVNWINETHTNIPELSSHYLCNTPPHYHGFPVRLFDTSSCKDSAPFELFFMINTSILLIFIFIVLLIHFEGWRISFYWNVSVHRVLGFKEIDRQTEQFEYAAYIIHAYKDKDWVWEHFSSMEKEDQSLKFCLEERDFEAGVFELEAIVNSIKRSRKIIFVITHHLLKDPLCKRFKVHHAVQQAIEQNLDSIILVFLEEIPDYKLNHALCLRRGMFKSHCILNWPVQKERIGAFRHKLQVALGSKNSVH
Protein: Mitogen-activated protein kinase 7 (MAP kinase 7) (MAPK 7) (EC 2.7.11.24) (Big MAP kinase 1) (BMK-1) (Extracellular signal-regulated kinase 5) (ERK-5) (P0C865)
Organism: Rattus norvegicus (Rat)
Function: Plays a role in various cellular processes such as proliferation, differentiation and cell survival. The upstream activator of MAPK7 is the MAPK kinase MAP2K5. Upon activation, it translocates to the nucleus and phosphorylates various downstream targets including MEF2C. EGF activates MAPK7 through a Ras-independent and MAP2K5-dependent pathway. May have a role in muscle cell differentiation. May be important for endothelial function and maintenance of blood vessel integrity. MAP2K5 and MAPK7 interact specifically with one another and not with MEK1/ERK1 or MEK2/ERK2 pathways. Phosphorylates SGK1 at Ser-78 and this is required for growth factor-induced cell cycle progression (By similarity). Involved in the regulation of p53/TP53 by disrupting the PML-MDM2 interaction (By similarity).
Subcellular location: Cytoplasm. Nucleus. Nucleus, PML body {ECO:0000250}. Note=Translocates to the nucleus upon activation. {ECO:0000250}.
Interaction partners:
- Dual specificity mitogen-activated protein kinase kinase 5
- Ribosomal protein S6 kinase alpha-1
- Ribosomal protein S6 kinase
- Rap guanine nucleotide exchange factor 3
- Ribosomal protein S6 kinase
- Ribosomal protein S6 kinase
- Nuclear factor erythroid 2-related factor 2
- Nuclear receptor subfamily 4 group A member 1
- Gap junction alpha-1 protein
- Protein kinase C zeta type
Sequence:
MAEPLKEEDGEDGSGEPPGRVKAEPVHTAASVVAKNLALLKARSFDVTFDVGDEYEIIETIGNGAYGVVSSARRRLTGQQVAIKKIPNAFDVVTNAKRTLRELKILKHFKHDNIIAIKDILRPTVPYGEFRSVYVVLDLMESDLHQIIHSSQPLTLEHVRYFLYQLLRGLKYMHSAQVIHRDLKPSNLLVNENCELKIGDFGMARGLCTSPAEHQYFMTEYVATRWYRAPELMLSLHEYTQAIDLWSVGCIFGEMLARRQLFPGKNYVHQLQLIMMVLGTPSPAVIQAVGAERVRAYIQSLPPRQPVPWETVYPGADRQALSLLGRMLRFEPSARISAAAALRHPFLAKYHDPDDEPDCAPPFDFAFDREALTRERIKEAIVAEIEDFHARREGIRQQIRFQPSLQPVASEPVCPDVEMPSPWAPSGDCAMESPPPALPPCSGPAPDTVDLTLQPAPPASELAPPKREGAISDNTKAALKAALLKSLRSRLRDGPSAPLEAPEPRKPVTAQERQREREEKRRRRQERAKEREKRRQERERKERGAGTLGGPSTDPLAGLVLSDNDRSLLERWTRMARPPVPAPAPAPAPTPKPSSAQPTSPPNGPVSQSTAPLQPAGSIPGPASQPVCPPPGPVPQPAGPVPAPLQTAPSTSLLASQSLVPPSGLPGSGAPEVLPYFPSGPPPPDPGLTPQPSTSESPDVNLVTQQLSKSQVEDPLPPVFSGTPKGSGAGYGVGFDLEEFLNQSFDMGVADGPQDGQADSASLSASLLADWLEGHGMNPADIESLQREIQMDSPMLLSDLPDLQEP
Protein: Stac-like, isoform C (A8DYE7)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Cell membrane {ECO:0000256|ARBA:ARBA00004413}; Peripheral membrane protein {ECO:0000256|ARBA:ARBA00004413}; Cytoplasmic side {ECO:0000256|ARBA:ARBA00004413}. Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
Interaction partners:
Sequence:
MKTKWLKAFKSLKPAGSGSAQQADRRNGASSTASEPLRPNLDGSHHLQEYTYKKITACDVCSQILRGHTRQGLRCRICKLNAHGDCAPNLPRCQPKQKLLRRQKSTSELENRVDIEEETSANPKSETTRPFGEPLMLLKSTESNPDESKGNRRVR