wanglab/gogpt-training-data huggingface dataset:
Protein: CCR4-NOT transcription complex subunit 8 (EC 3.1.13.4) (CCR4-associated factor 8) (Q9D8X5)
Organism: Mus musculus (Mouse)
Function: Has 3'-5' poly(A) exoribonuclease activity for synthetic poly(A) RNA substrate. Its function seems to be partially redundant with that of CNOT7. Catalytic component of the CCR4-NOT complex which is linked to various cellular processes including bulk mRNA degradation, miRNA-mediated repression, translational repression during translational initiation and general transcription regulation. During miRNA-mediated repression the complex seems also to act as translational repressor during translational initiation. Additional complex functions may be a consequence of its influence on mRNA expression. Associates with members of the BTG family such as TOB1 and BTG2 and is required for their anti-proliferative activity.
Subcellular location: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}.
Interaction partners:
- CCR4-NOT transcription complex subunit 6-like
- CCR4-NOT transcription complex subunit 6
- CCR4-NOT transcription complex subunit 1
- CCR4-NOT transcription complex subunit 9
- CCR4-NOT transcription complex subunit 2
- CCR4-NOT transcription complex subunit 3
- CCR4-NOT transcription complex subunit 4
- Protein PAT1 homolog 1
- CCR4-NOT transcription complex subunit 7
- CCR4-NOT transcription complex subunit 10
Sequence:
MPAALVENSQVICEVWASNLEEEMRKIREIVLSYSYIAMDTEFPGVVVRPIGEFRSSIDYQYQLLRCNVDLLKIIQLGLTFTNEKGEYPSGINTWQFNFKFNLTEDMYSQDSIDLLANSGLQFQKHEEEGIDTLHFAELLMTSGVVLCDNVKWLSFHSGYDFGYMVKLLTDSRLPEEEHEFFHILNLFFPSIYDVKYLMKSCKNLKGGLQEVADQLDLQRIGRQHQAGSDSLLTGMAFFRMKELFFEDSIDDAKYCGRLYGLGTGVAQKQNEDVDCAQEKMSILAMINNMQQ
Protein: C-C motif chemokine 7 (Monocyte chemoattractant protein 3) (Monocyte chemotactic protein 3) (MCP-3) (Small-inducible cytokine A7) (Q9QXY8)
Organism: Rattus norvegicus (Rat)
Function: Chemotactic factor that attracts monocytes and eosinophils, but not neutrophils. Augments monocyte anti-tumor activity (By similarity).
Subcellular location: Secreted.
Interaction partners:
- C-C motif chemokine 2
- Macrophage inflammatory protein-1 alpha receptor
- C-C chemokine receptor type 3
- C-C motif chemokine 6
- C-C chemokine receptor type 5
- C-C motif chemokine 5
- C-C motif chemokine
- Eotaxin
- C-C motif chemokine ligand 26
- Chemokine
Sequence:
MQISAALLCVLLTAAAFTVHVWAQPDGTNSSTCCYVKKQKIPKRNLKSYRKITSSRCPWEAVIFKTKKGMEVCAEAHQKWVEEAIAYLDMKTSTPKP
Protein: Cytochrome P450, family 96, subfamily A, polypeptide 13 (Cytochrome P450-like protein) (Q9LYZ5)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
- UDP-glycosyltransferase 78D4
- UDP-glycosyltransferase 91A1
Sequence:
MASISLFEASIAIFCFIILHFFLGNWPVLGMLPGLLLEFHRIYDFSVEVLENSDLTFPFKGPWFTGMDMLFTVDPTNIHHIMSSNFSNYTKGPDFKQVFDVFGDGILTTDDSELWKNLKKASLVMLNHQGFQKNGTVVDLQDVFKRFMFDTTLVTVTGSADPRSLSIEMPEVEFAKALDHVGEGIMHRHVRPRLLWKLQKCVGFGQEKKFSKADATLNQACAKYILEKREETRSQGFDYHSNGSESEDILTYHIKIDTTKYELLNPSDDKFLRDTILAFVLAGRDTTASALTWFFWLLLENPQVVTKIRQEINTSNGGQEKPSCEPMEYLNNLVYLHGALYEAMRLYPPVPFERMSPIKPDVLPSGHKVDSSMKILIFIYALGRMRAVWGEDASEFKPERWLSETTSLRHEPSFKFLAFNAGPRSCIGKQLAMTLMKIVVVEILQNYDIKVVKGQKKIEPAPGPILRMKHGLRVTLTKKC
Protein: Ly49 inhibitory receptor 2 (Q8K3G1)
Organism: Rattus norvegicus (Rat)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004606}; Single-pass type II membrane protein {ECO:0000256|ARBA:ARBA00004606}.
Interaction partners:
Sequence:
MTEQEVTYTTVRFHKSSVFQNEVRSEETQSAKEIGHRESSVPWKLIVIALGILCSVLLVTVAVLVTNCLQYNHETHELQETQNSQHNCSTMENDIKLKEEMLRNMSVESTRYNALLDLINREQKRWYNKTKTVLAAPQHTGGCVEMHWLCYGIKCYYFIIDKRTWHKCIQTCQNYSLSFLKIHDKDELKFLQDHIIRDSYWIGLSYNNNKKEWSWIDNTTLNCDLVAMISLHKTGNCKYFSMTGLHDDDCGKRHLCICEKGIEKYPAPLCSVKERSQSAL
Protein: Structural maintenance of chromosomes 6 (C9JMN1)
Organism: Homo sapiens (Human)
Subcellular location: Chromosome {ECO:0000256|ARBA:ARBA00004286}. Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
MAKRKEENFSSPKNAKRPRQEELEDFDKDGDEDECKGTTLTAAEVGIIESIHLKNFMCHSMLGPFKFGSNVNFVVGNNGSWSAVVRSRLNATSASQVQAILLFQPCGKSAVLTALIVGLGGRAVATNRGSSLKGFVKDGQNSADISITLRNRGDDAFKASVYGNSILIQQHISIDGSRSYKLKSATGSVVSTRKEELIAILDHFNIQVDNPVSVLTQEMSKQFLQSKNEGDKYKFFMKATQLEQMKEDYSYIMETKERTKEQIHQGEERLTELKRQCVEKEERFQSIAGLSTMKTNLESLKHEMAWAVVNEIEKQLNAIRDNIKIGEDRAARLDRKMEEQQVRLNEAEQKYKDIQDKLEKISEETNARAPECMALKADVVAKKRAYNEAEVLYNRSLNEYKALKKDDEQLCKRIEELKKSTDQSLEPERLERQKKISWLKERVKAFQNQENSVNQEIEQFQQAIEKDKEEHGKIKREELDVKHALSYNQRQLKELKDSKTDRLKRFGPNVPALLEAIDDAYRQGHFTYKPVGPLGACIHLRDPELALAIESCLKGLLQAYCCHNHADERVLQALMKRFYLPGTSRPPIIVSEFRNEIYDVRHRAAYHPDFPTVLTALEIDNAVVANSLIDMRGIETVLLIKNNSVARAVMQSQKPPKNCREAFTADGDQVFAGRYYSSENTRPKFLSRDVDSEISDLENEVENKTAQILNLQQHLSALEKDIKHNEELLKRCQLHYKELK
Protein: Death-associated protein kinase 3 (DAP kinase 3) (EC 2.7.11.1) (DAP-like kinase) (Dlk) (MYPT1 kinase) (ZIP-kinase) (O88764)
Organism: Rattus norvegicus (Rat)
Function: Serine/threonine kinase which is involved in the regulation of apoptosis, autophagy, transcription, translation and actin cytoskeleton reorganization. Regulates both type I (caspase-dependent) apoptotic and type II (caspase-independent) autophagic cell deaths signal, depending on the cellular setting. Involved in formation of promyelocytic leukemia protein nuclear body (PML-NB). Involved in apoptosis involving PAWR which mediates cytoplasmic relocation; in vitro phosphorylates PAWR. Phosphorylates MYL12B in non-muscle cells leading to reorganization of actin cytoskeleton such as in regulation of cell polarity and cell migration. Positively regulates canonical Wnt/beta-catenin signaling through interaction with NLK and TCF7L2; disrupts the NLK-TCF7L2 complex thereby influencing the phosphorylation of TCF7L2 by NLK. Phosphorylates RPL13A on 'Ser-77' upon interferon-gamma activation which is causing RPL13A release from the ribosome, RPL13A association with the GAIT complex and its subsequent involvement in transcript-selective translation inhibition (By similarity). Phosphorylates STAT3 and enhances its transcriptional activity (By similarity). Enhances transcription from AR-responsive promoters in a hormone- and kinase-dependent manner. Phosphorylates histone H3 on 'Thr-11' at centromeres during mitosis.
Subcellular location: Nucleus {ECO:0000269|PubMed:10602474, ECO:0000269|PubMed:10602480, ECO:0000269|PubMed:17953487, ECO:0000269|PubMed:20854903, ECO:0000269|PubMed:9840928}. Nucleus, PML body {ECO:0000269|PubMed:10602474}. Cytoplasm {ECO:0000303|PubMed:10602480}. Cytoplasm, cytoskeleton, microtubule organizing center {ECO:0000269|PubMed:14582533}. Chromosome, centromere {ECO:0000269|PubMed:12560483, ECO:0000269|PubMed:14582533}. Cytoplasm, cytoskeleton {ECO:0000269|PubMed:15096528}. Cytoplasm, cytoskeleton, spindle {ECO:0000250|UniProtKB:O43293}. Midbody {ECO:0000250|UniProtKB:O43293}. Note=Predominantly localized to the nucleus. Relocates to the cytoplasm on binding PAWR where the complex appears to interact with actin filaments (Probable). Associated with the centrosomes throughout the mitotic cell cycle, with the centromeres from prophase to anaphase and with the contractile ring during cytokinesis. {ECO:0000269|PubMed:14582533, ECO:0000269|PubMed:17953487, ECO:0000303|PubMed:10602474}.
Interaction partners:
- Beclin-1
- Mitogen-activated protein kinase 3
- Mitogen-activated protein kinase 1
- Death-associated protein kinase 1
- Leucine zipper protein 1
- Calmodulin-1
- Calmodulin-like protein 3
Sequence:
MSTFRQEDVEDHYEMGEELGSGQFAIVRKCQQKGTGMEYAAKFIKKRRLPSSRRGVSREEIEREVSILREIRHPNIITLHDVFENKTDVVLILELVSGGELFDFLAEKESLTEDEATQFLKQILDGVHYLHSKRIAHFDLKPENIMLLDKHAASPRIKLIDFGIAHRIEAGSEFKNIFGTPEFVAPEIVNYEPLGLEADMWSIGVITYILLSGASPFLGETKQETLTNISAVNYDFDEEYFSSTSELAKDFIRRLLVKDPKRRMTIAQSLEHSWIKVRRREDGARKPERRRLRAARLREYSLKSHSSMPRNTSYASFERFSRVLEDVAAAEQGLRELQRGRRQCRERVCALRVAAEQREARCRDGSAGLGRDLRRLRTELGRTEALRTRAQEEARAALLGAGGLKRRLCRLENRYDALAAQVAAEVQFVRDLVRALEQERLQAECGVR
Protein: Dynein axonemal assembly factor 1 (A0A140VJN4)
Organism: Homo sapiens (Human)
Subcellular location: Cell projection, cilium {ECO:0000256|ARBA:ARBA00004138, ECO:0000256|RuleBase:RU364076}.
Interaction partners:
Sequence:
MHPEPSEPATGGAAELDCAQEPGVEESAGDHGSAGRGGCKEEINDPKEICVGSSDTSYHSQQKQSGDNGSGGHFAHPREDREDRGPRMTKSSLQKLCKQHKLYITPALNDTLYLHFKGFDRIENLEEYTGLRCLWLQSNGIQKIENLEAQTELRCLFLQMNLLRKIENLEPLQKLDALNLSNNYIKTIENLSCLPVLNTLQMAHNHLETVEDIQHLQECLRLCVLDLSHNKLSDPEILSILESMPDLRVLNLMGNPVIRQIPNYRRTVTVRLKHLTYLDDRPVFPKDRACAEAWARGGYAAEKEERQQWESRERKKITDSIEALAMIKQRAEERKRQRESQERGEMTSSDDGENVPASAEGKEEPPGDRETRQKMELFVKESFEAKDELCPEKPSGEEPPVEAKREDGGPEPEGTLPAETLLLSSPVEVKGEDGDGEPEGTLPAEAPPPPPPVEVKGEDGDQEPEGTLPAETLLLSPPVKVKGEDGDREPEGTLPAEAPPPPPLGAAREEPTPQAVATEGVFVTELDGTRTEDLETIRLETKETFCIDDLPDLEDDDETGKSLEDQNMCFPKIEVISSLSDDSDPELDYTSLPVLENLPTDTLSNIFAVSKDTSKAARVPFTDIFKKEAKRDLEIRKQDTKSPRPLIQELSDEDPSGQLLMPPTCQRDAAPLTSSGDRDSDFLAASSPVPTESAATPPETCVGVAQPSQALPTWDLTAFPAPKAS
Protein: Probable cysteine desulfurase (EC 2.8.1.7) (P9WQ69)
Organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Function: Catalyzes the removal of elemental sulfur and selenium atoms from L-cysteine, L-cystine, L-selenocysteine, and L-selenocystine to produce L-alanine.
Interaction partners:
- Possible nitrogen fixation related protein
- Probable conserved ATP-binding protein ABC transporter
- Iron-sulfur cluster assembly SufBD family protein Rv1462
- Iron-sulfur cluster assembly SufBD family protein Rv1461
- Conserved protein
- Thioredoxin reductase
- Cystathionine gamma-synthase
- Thioredoxin
- Probable transcriptional regulatory protein
- Sphingomyelinase
Sequence:
MTASVNSLDLAAIRADFPILKRIMRGGNPLAYLDSGATSQRPLQVLDAEREFLTASNGAVHRGAHQLMEEATDAYEQGRADIALFVGADTDELVFTKNATEALNLVSYVLGDSRFERAVGPGDVIVTTELEHHANLIPWQELARRTGATLRWYGVTDDGRIDLDSLYLDDRVKVVAFTHHSNVTGVLTPVSELVSRAHQSGALTVLDACQSVPHQPVDLHELGVDFAAFSGHKMLGPNGIGVLYGRRELLAQMPPFLTGGSMIETVTMEGATYAPAPQRFEAGTPMTSQVVGLAAAARYLGAIGMAAVEAHERELVAAAIEGLSGIDGVRILGPTSMRDRGSPVAFVVEGVHAHDVGQVLDDGGVAVRVGHHCALPLHRRFGLAATARASFAVYNTADEVDRLVAGVRRSRHFFGRA
Protein: DnaJ homolog subfamily C member 7 homolog (Q9HGM9)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Subcellular location: Cytoplasm {ECO:0000269|PubMed:16823372}.
Interaction partners:
- Heat shock protein homolog pss1
Sequence:
MTEVETTHMNAGTESQQEPAELAEKQKAIGNAFYKEKKYAEAIKAYTEAIDLGSDSALAIYYSNRAATYMQIGEFELALCDAKQSDRIKPDVPKTQSRIRQAYEGLSILNEAEVYLKNKQAGLALNALDRLQRRIDSTTQPPMSWMYLKAQVYIFQNDMDRAQKIAHDVLRLNPKNVEALVLRGKVMYYSGENAKAITHFQEALKLDPDCTTAKTLFKQVRKLENTKNQGNDLFRQGNYQDAYEKYSEALQIDPDNKETVAKLYMNRATVLLRLKRPEEALSDSDNALAIDSSYLKGLKVRAKAHEALEKWEEAVRDVQSAIELDASDANLRQELRRLQLELKKSKRKDHYKILGVSKEATDIEIKKAYRKLALVYHPDKNAGNLEAEARFKEVGEAYTILSDPESRRRFDSGVDLEPGMEGGAGMDPFDILRAYQAGGSFPGGGFPGGGFPGGSYNSQGFGMGGGFPGFTSFQFS
Protein: non-specific serine/threonine protein kinase (EC 2.7.11.1) (H3BLV9)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
KGERWSGLRHEGQWSPGRGPVLALQARKKRTKAKKDKAQRKSETQHRGSAPHSESDLPEQEEEILGSDDDEQEDPNDYCKGGYHLVKIGDLFNGRYHVIRKLGWGHFSTVWLSWDIQGKKFVAMKVVKSAEHYTETALDEIRLLKSVRNSDPNDPNREMVVQLLDDFKISGVNGTHICMVFEVLGHHLLKWIIKSNYQGLPLPCVKKIIQQVLQGLDYLHTKCRIIHTDIKPENILLSVNEQYIRRLAAEATEWQRSGAPPPSGSAVSTAPQPKPADKMSKNKKKKLKKKQKRQAELLEKRMQEIEEMEKESGPGQKRPNKQEESESPVERPLKENPPNKMTQEKLEESSTIGQDQTLMERDTEGGAAEINCNGVIEVINYTQNSNNETLRHKEDLHNANDCDVQNLNQESSFLSSQNGDSSTSQETDSCTPITSEVSDTMVCQSSSTVGQSFSEQHISQLQESIRAEIPCEDEQEQEHNGPLDNKGKSTAGNFLVNPLEPKNAEKLKVKIADLGNACWVHKHFTEDIQTRQYRSLEVLIGSGYNTPADIWSTACMAFELATGDYLFEPHSGEEYTRDEDHIALIIELLGKVPRKLIVAGKYSKEFFTKKGDLKHITKLKPWGLFEVLVEKYEWSQEEAAGFTDFLLPMLELIPEKRATAAECLRHPWLNS
Protein: Ergosterol biosynthetic protein 28 (O80594)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Subcellular location: Endoplasmic reticulum membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}.
Interaction partners:
- At2g33630/F4P9.40
- Methylsterol monooxygenase 2-2
- Methylsterol monooxygenase 2-1
- Putative Delta
- Delta
- Methylsterol monooxygenase 1-2
- Methylsterol monooxygenase 1-1
- Sterol 14-demethylase
- Putative sterol 14-demethylase-like protein
- 7-dehydrocholesterol reductase
Sequence:
MKALGYWLMVVGSLRLASVWFGFFNIWALRLAVFSQTTMSEVHGRTFGVWTLLTCTLCFLCAFNLENKPLYLATFLSFIYALGHFLTEYLFYQTMTIANLSTVGFFAGTSIVWMLLEWNSLEQPHSKLS
Protein: FXYD domain-containing ion transport regulator 6 (PLM-like protein) (Phosphohippolin) (Q9D164)
Organism: Mus musculus (Mouse)
Subcellular location: Cell membrane {ECO:0000250|UniProtKB:Q91XV6}; Single-pass type I membrane protein {ECO:0000305}.
Interaction partners:
- Sodium/potassium-transporting ATPase subunit beta-1
- Sodium/potassium-transporting ATPase subunit alpha-3
- Sodium/potassium-transporting ATPase subunit beta-2
- Sodium/potassium-transporting ATPase subunit alpha-2
- Sodium/potassium-transporting ATPase subunit beta-3
- Sodium/potassium-transporting ATPase subunit alpha-4
- Sodium/potassium-transporting ATPase subunit alpha-1
Sequence:
METVLVLCSLLAPVVLASAAEKEKEKDPFYYDYQTLRIGGLVFAVVLFSVGILLILSRRCKCSFNQKPRAPGDEEAQVENLITTNAAEPQKAEN
Protein: Small nuclear ribonucleoprotein Sm D1 (Sm-D1) (snRNP core protein D1) (Q02260)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: lays a role in pre-mRNA splicing as a core component of the spliceosomal U1, U2, U4 and U5 small nuclear ribonucleoproteins (snRNPs), the building blocks of the spliceosome. Also binds telomerase RNA and is required for its accumulation.
Subcellular location: Nucleus {ECO:0000250|UniProtKB:O42661}. Cytoplasm {ECO:0000250|UniProtKB:O42661}.
Interaction partners:
- Pre-mRNA-splicing factor SYF1
- Pre-mRNA-splicing factor CWC2
- Cold sensitive U2 snRNA suppressor 1
- LSM complex subunit LSM4
- Small nuclear ribonucleoprotein Sm D3
- Pre-mRNA-splicing factor SNU114
- U2 small nuclear ribonucleoprotein A'
- Protein LUC7
- LSM2-LSM8 complex subunit LSM8
- Pre-mRNA-processing factor 19
Sequence:
MKLVNFLKKLRNEQVTIELKNGTTVWGTLQSVSPQMNAILTDVKLTLPQPRLNKLNSNGIAMASLYLTGGQQPTASDNIASLQYINIRGNTIRQIILPDSLNLDSLLVDQKQLNSLRRSGQIANDPSKKRRRDFGAPANKRPRRGL
Protein: SWI/SNF related, matrix associated, actin dependent regulator of chromatin, subfamily c, member 2 (D4A510)
Organism: Rattus norvegicus (Rat)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
- SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily A member 4
- AT-rich interaction domain 1A
- SWI/SNF related, matrix associated, actin dependent regulator of chromatin, subfamily a, member 2
- SWI/SNF related, matrix associated, actin dependent regulator of chromatin, subfamily d, member 1
- SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily B member 1
- SWI/SNF related, matrix associated, actin dependent regulator of chromatin, subfamily c, member 1
- Protein polybromo-1
- Actin-like protein 6A
- AT-rich interaction domain 1B
- SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily E member 1
Sequence:
MAVRKKDGGPNVKYYEAADTVTQFDNVRLWLGKNYKKYIQAEPPTNKSLSSLVVQLLQFQEEVFGKHVSNAPLTKLPIKCFLDFKAGGSLCHILAAAYKFKSDQGWRRYDFQNPSRMDRNVEMFMTIEKSLVQNNCLSRPNIFLCPEIEPKLLGKLKDIVKRHQGTISEDKSNASHVVYPAPGNLEEEEWVRPVMKRDKQVLLHWGYYPDSYDTWIPASEIEASVEDAPTPEKPRKVHAKWILDTDTFNEWMNEEDYEVSDDKSPVSRRKKISAKTLTDEVNSPDADRRDKKGGNYKKRKRSPSPSPTPEAKKKNAKKGPSTPYTKSKRGHREEEQEDLTKDMDEPSPVPNVEEVTLPKTVNTKKDSESAPVKGGTMTDLDEQDDESMETTGKDEDENSTGNKGEQTKSADLHEDNVTEQTHHIIVPSYAAWFDYNSVHAIERRALPEFFNGKNKSKTPEIYLAYRNFMIDTYRLNPQEYLTSTACRRNLAGDVCAIMRVHAFLEQWGLINYQVDAESRPTPMGPPPTSHFHVLADTPSGLVPLQPKPPQGRQVDADTKAGRKGKELDDLVPEAAKGKPELQGSASQQMLNFPDKGKEKPADMQNFGLRTDMYTKKNIPSKSKAAASATREWTEQETLLLLEALEMYKDDWNKVSEHVGSRTQDECILHFLRLPIEDPYLEDSEASLGPLAYQPIPFSQSGNPVMSTVAFLASVVDPRVASAAAKSALEEFSKMKEEVPTALVEAHVRKVEEAAKVTGKADPAFGLESSGIAGTASDEPERIEESGTEEARAESQAADEKKEPKEPREGGGAVEEEAKEEISEAPKKDEEKGKEADSEKESEKSDGDPIVDPEKDKEPTEGQEEGLKEVAEPEGERKAKVERDIGEGNLSTAAAAALAAAAVKAKHLAAVEERKIKSLVALLVETQMKKLEIKLRHFEELETIMDREREALEYQRQQLLADRQAFHMEQLKYAEMRARQQHFQQMQQQPPPPPPPPPPPALPPGSQPIPPTGAAAPATVHGLAVAPASVASAPPGGGAPPGTLGPSEQIGQAGTTAGPQQPQQAGAPHPSPWAVPGSGHPGVADPGTPLPPDPTAPSPGTVTPVPPPQ
Protein: Eukaryotic translation initiation factor 2 subunit 1 (Eukaryotic translation initiation factor 2 subunit alpha) (eIF-2-alpha) (eIF-2A) (eIF-2alpha) (eIF2-alpha) (P05198)
Organism: Homo sapiens (Human)
Function: Functions in the early steps of protein synthesis by forming a ternary complex with GTP and initiator tRNA. This complex binds to a 40S ribosomal subunit, followed by mRNA binding to form a 43S pre-initiation complex. Junction of the 60S ribosomal subunit to form the 80S initiation complex is preceded by hydrolysis of the GTP bound to eIF-2 and release of an eIF-2-GDP binary complex. In order for eIF-2 to recycle and catalyze another round of initiation, the GDP bound to eIF-2 must exchange with GTP by way of a reaction catalyzed by eIF-2B. EIF2S1/eIF-2-alpha is a key component of the integrated stress response (ISR), required for adaptation to various stress: phosphorylation by metabolic-stress sensing protein kinases (EIF2AK1/HRI, EIF2AK2/PKR, EIF2AK3/PERK and EIF2AK4/GCN2) in response to stress converts EIF2S1/eIF-2-alpha in a global protein synthesis inhibitor, leading to an 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.
Subcellular location: Cytoplasm, Stress granule {ECO:0000250|UniProtKB:Q6ZWX6}. Cytoplasm, cytosol {ECO:0000250|UniProtKB:P56286}. Mitochondrion {ECO:0000269|PubMed:38340717}. Note=Colocalizes with NANOS3 in the stress granules (By similarity). Relocalizes to the surface of mitochondria in response to mitochondrial damage and phosphorylation by EIF2AK1/HRI (PubMed:38340717). {ECO:0000250|UniProtKB:Q6ZWX6, ECO:0000269|PubMed:38340717}.
Interaction partners:
- 26S proteasome non-ATPase regulatory subunit 14
- Eukaryotic translation initiation factor 3 subunit I
- Interferon-induced, double-stranded RNA-activated protein kinase
- Eukaryotic translation initiation factor 2 subunit 2
- eIF-2-alpha kinase GCN2
- Small ribosomal subunit protein uS3
- Small ribosomal subunit protein eS1
- Translation initiation factor eIF2B subunit epsilon
- Translation initiation factor eIF2B subunit delta
- Protein phosphatase 1 regulatory subunit 15A
Sequence:
MPGLSCRFYQHKFPEVEDVVMVNVRSIAEMGAYVSLLEYNNIEGMILLSELSRRRIRSINKLIRIGRNECVVVIRVDKEKGYIDLSKRRVSPEEAIKCEDKFTKSKTVYSILRHVAEVLEYTKDEQLESLFQRTAWVFDDKYKRPGYGAYDAFKHAVSDPSILDSLDLNEDEREVLINNINRRLTPQAVKIRADIEVACYGYEGIDAVKEALRAGLNCSTENMPIKINLIAPPRYVMTTTTLERTEGLSVLSQAMAVIKEKIEEKRGVFNVQMEPKVVTDTDETELARQMERLERENAEVDGDDDAEEMEAKAED
Protein: Thiamine kinase (EC 2.7.1.89) (P75948)
Organism: Escherichia coli (strain K12)
Function: Catalyzes the phosphorylation of thiamine to thiamine phosphate.
Interaction partners:
- Thiamine-monophosphate kinase
- Thiamine-phosphate synthase
- Uncharacterized protein YcfL
- UPF0227 protein YcfP
- Purine nucleoside phosphoramidase
- Penicillin-binding protein activator LpoB
- Small ribosomal subunit biogenesis GTPase RsgA
- Alkaline phosphatase
- Beta-hexosaminidase
- Thiamine transport system permease protein ThiP
Sequence:
MPFRSNNPITRDELLSRFFPQYHPVTTFNSGLSGGSFLIEHQGQRFVVRQPHDPDAPQSAFLRQYRALSQLPACIAPKPHLYLRDWMVVDYLPGAVKTYLPDTNELAGLLYYLHQQPRFGWRITLLPLLELYWQQSDPARRTVGWLRMLKRLRKAREPRPLRLSPLHMDVHAGNLVHSASGLKLIDWEYAGDGDIALELAAVWVENTEQHRQLVNDYATRAKIYPAQLWRQVRRWFPWLLMLKAGWFEYRWRQTGDQQFIRLADDTWRQLLIKQ
Protein: Clotting factor G alpha subunit (EC 3.2.1.-) (Q27082)
Organism: Tachypleus tridentatus (Japanese horseshoe crab)
Function: Component of the heterodimer clotting factor G which may play a role in defense mechanisms against fungi (Probable). Initiates a (1->3)-beta-glucan-sensing clotting pathway whereby the alpha subunit binds to glucans containing (1->3)-beta linkages, which are components of the fungal cell wall, and the beta subunit catalyzes the activation of proclotting enzyme.
Interaction partners:
Sequence:
MLVLLCCVVLHVGVARICCSHEPKWQLVWSDEFTNGISSDWEFEMGNGLNGWGNNELQYYRRENAQVEGGKLVITAKREDYDGFKYTSARLKTQFDKSWKYGKIEAKMAIPSFRGVWVMFWMSGDNTNYVRWPSSGEIDFIEHRNTNNEKVRGTIHWSTPDGAHAHHNRESNTNGIDYHIYSVEWNSSIVKWFVNGNQYFEVKIQGGVNGKSAFRNKVFVILNMAIGGNWPGFDVADEAFPAKMYIDYVRVYQDASTSSPVGDTSLDGYYFVQNRHSELYLDVTDASNEDGAFLQQWSYSGNENQQFDFEHLENNVYKITNKKSGKSLDVYNFGTENGVRIQQWSYGGARNQQFTVQSVGDGYYKIIPRGSGKLVEVADFSKDAGGKIQQWSDNNQLSGQWKLIKSKSYSKLIQAESYFDSSKVQLEDTSDVGGGKNVKCDNEGAWMAYKDIDFPSSGNYRIEYRVASERAGGKLSLDLNAGSIVLGMLDVPSTGGWQKWTTISHTVNVDSGTYNLGIYVQRASWNINWIKITKIPEQSNLNQGRRNSKLIQAESYFSYSEVQLEDTLDVGGGKNVKCDKEGAWMAYKDIDFPSSGSYRVEYRVASERAGGKLSLDLNAGSIVLGMLDIPSTGGLQKWTTISHIVNVDLGTYNLGIYVQKASWNINWIRITKV
Protein: Ribosome binding protein 1 (F1M853)
Organism: Rattus norvegicus (Rat)
Subcellular location: Endoplasmic reticulum membrane {ECO:0000256|ARBA:ARBA00004389}; Single-pass membrane protein {ECO:0000256|ARBA:ARBA00004389}.
Interaction partners:
- Synaptojanin-2-binding protein
- PC-esterase domain containing 1A
- SLX4 interacting protein
Sequence:
MDIYDTQTLGVVVFGGFMVVSAIGIFLVSTFSMKETSYEEALANQRKEMAKTHHQKGEKKKKEKTVEKKGKTKKKEEKPNGKIPEHDLDPNVTIILKEPMRVPAVAVAPTSVHSSVGRTPVATVPAMPQEKLASSPKDKKKKEKKVAKVEPAVSSIVNSIQVLASKSAILEASPKEVPMVAVPPVGSKASAPATSSQGKKGQGAQNQAKKGEGAQNQAKKGEGVQNQAKKGEGAQNQVKKGEGAQNQAKKGEGAQNQAKKGEGTQNQAKKGEGAQNQGKKGEGAQNQAKKGEGAQNQAKKGEGAQNQAKKGEGAQNQAKKGEGGQNQAKKGEGAQNQAKKGEGAQNQAKKGEGVQNQAKKGVEGAQNQGKKGEANQNQAKKGEGGQNQTKKGEGLQNQGKKGEATQKQDKKIEGAQNQGKKPEGTPNQGKKGEGAQNQGKKGEGAQNQGKKGEGAQNQGKKGEGAQNQGKKGEGAQNQGKKGEGAQNQGKKGEGAQNQGKKGEGAQNQGKKGEGSPSQNIKVEGMQNQGRKAEGTPAQGKKMEAAQNQGKKAEGVQSQGKKGEGSQNQGKKGDGNPNQGKKGEGAPNQNRKTDTVANQGTKTEGVSNQVKKSEGSPNQGKKAEGAPNQGKKVEGSPNQAKKVDAAAGQGKKSEMTPAQGKNASMVQSQEAPKQEAPAKKKSKKKGEPGPPDCDSPLFLPYKTLVSTVGSMVFSEGEAQRLIEILSEKTGVIQDTWHKATQKGDPVAVLKRQLEEKEKLLATEQEDAAVAKSKLRELNKEMASEKAKAAAGEAKVKKQLVAREQEIAAVQARMQASYQDHVKEVQQLQGKIRTLQEQLENGPNTQLARLQQENSILRDALNQATSQVESKQNTELAKLRQELSKVNKELVEKSEASRQEEQQRKALEAKAATFEKQILQLQASHKESEEALQKRLEEVTRELCRAQTSHANLRADAEKAQEQQQRVAELHSKLQSSEVEVKSKCEELSDLHGQLKEARAENSQLTERIRSIEALLEAGQAQDSQASRAEADQQQTRLKELESQVSCLEKETSELKEAMEQQKGKNNDLREKNWKAMEALALAERACEEKLRSLTQAKEESEKQLHLAEAQTKEVLLALLPELSIPAHQNYADWLQEVKEKGSELLKKPPVSVEPSLDIVSKLREAEETQNSLQAECDQYRTILAETEGMLKDLQKSVEEEERVWKAKVGAAEEELQKSRFTVKHLEDLVEKLRGELESSDQVREHTSHLEAELEKHMAAASAECQNYAKEVAGLRQLLLDSQSQLEEAKSEAQKQSNELALVRQQLSDMRSHVEDGDVAGSPAVPPAEQDPVKLKTQLERTEATLEDEQTRRQKLTAEFEEAQSTACRLQEELEKLRAAGPLESSGIEEVTQLKERLEKEKRLTSDLGRAATKLQELLKTTQEQLTKEKDTVKKLQEQLGKAEDGSSSKEGTSV
Protein: POU domain class 2-associating factor 1 (B-cell-specific coactivator OBF-1) (BOB-1) (BOB1) (OCA-B) (OCT-binding factor 1) (Q64693)
Organism: Mus musculus (Mouse)
Function: Transcriptional coactivator that specifically associates with either POU2F1/OCT1 or POU2F2/OCT2. It boosts the POU2F1/OCT1 mediated promoter activity and to a lesser extent, that of POU2F2/OCT2. It recognizes the POU domains of POU2F1/OCT1 and POU2F2/OCT2. It is essential for the response of B-cells to antigens and required for the formation of germinal centers. Regulates IL6 expression in B cells as POU2F2/OCT2 coactivator.
Subcellular location: Nucleus {ECO:0000305}.
Interaction partners:
- POU domain, class 2, transcription factor 1
- Marginal zone B- and B1-cell-specific protein
- B-lymphocyte antigen CD20
- POU domain, class 2, transcription factor 2
- B-cell antigen receptor complex-associated protein beta chain
- B-cell antigen receptor complex-associated protein alpha chain
- B-lymphocyte antigen CD19
- Transcription factor Spi-B
- Immunoglobulin J chain
- Paired box protein Pax-5
Sequence:
MLWQKSTAPEQAPAPPRPYQGVRVKEPVKELLRRKRGHTSVGAAGPPTAVVLPHQPLATYSTVGPSCLDMEVSASTVTEEGTLCAGWLSQPAPATLQPLAPWTPYTEYVSHEAVSCPYSTDMYVQPVCPSYTVVGPSSVLTYASPPLITNVTPRSTATPAVGPQLEGPEHQAPLTYFPWPQPLSTLPTSSLQYQPPAPTLSGPQFVQLPISIPEPVLQDMDDPRRAISSLTIDKLLLEEEESNTYELNHTLSVEGF