wanglab/gogpt-training-data huggingface dataset:
Protein: Gamma-aminobutyric acid type B receptor subunit 2 (G5ECB2)
Organism: Caenorhabditis elegans
Function: Component of a heterodimeric G-protein coupled receptor for GABA, formed by gbb-1 and gbb-2 (By similarity). Within the heterodimeric GABA receptor, only gbb-1 seems to bind agonists, while gbb-2 mediates coupling to G proteins (By similarity). Ligand binding causes a conformation change that triggers signaling via guanine nucleotide-binding proteins (G proteins) and modulates the activity of down-stream effectors, such as adenylate cyclase (By similarity). Signaling inhibits adenylate cyclase, stimulates phospholipase A2, activates potassium channels, inactivates voltage-dependent calcium-channels and modulates inositol phospholipid hydrolysis (By similarity). Plays a critical role in the fine-tuning of inhibitory synaptic transmission (By similarity). Pre-synaptic GABA receptor inhibits neurotransmitter release by down-regulating high-voltage activated calcium channels, whereas postsynaptic GABA receptor decreases neuronal excitability by activating a prominent inwardly rectifying potassium (Kir) conductance that underlies the late inhibitory postsynaptic potentials (By similarity). Along with gbb-1, may couple to the G(o)-alpha G-protein goa-1 to negatively regulate cholinergic receptor activity in the presence of high levels of acetylcholine in ventral cord motor neurons. As acetylcholine depolarizes body wall muscles, modulation of acetylcholine levels most likely results in the control of locomotory behavior. Regulates locomotory behavior in response to GABA release by GABAergic motor neurons.
Subcellular location: Cell membrane {ECO:0000250|UniProtKB:O75899}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
- Gamma-aminobutyric acid type B receptor subunit 1
- RING-type E3 ubiquitin transferase
- Glutamate decarboxylase 1
- Muscarinic acetylcholine receptor gar-2
- Transporter
Sequence:
MSRWLSLLLFAVQAVGGYEAGEELSCKRRHGGIPLPLGVFTVQKEGFPDALPAIRTALSHVHSRSCILQGYRLEMIVKDTHCKTSQGMKALFDLIASRPRPVAILGGQCTEVNEPIAMALKYWQIVQLSYAETHAKFASSDSHELFTTFFRVVPGSRNTNMAKCKFVNHFGWKRVGTVKQNDQPRYALPHEALTTRLEHGFGVKIVHTAGVNWEQIETVGGELDELKERDVRIILVDVDEEMAATVLCAGYHRGMYGDNYVWILPGYHSDKWLNQTHDNCTVEEMREAAKNHFSVEFALTRRDVDTKIVGNTRAGDVWNEITQLDPNNTWRGYLYDGLWTLAIALSHSMGDNAEFSHHKMMEAIDNSSFQGLTGKVKFANNERLGLVDIKQWSDGQYVPFAVYDGADDEFKIIDSTTKGWSPPLDSTITERRREHISSILFLAMSLLALIGIFLALIFLLINFRYRNHRFIKMSSPNLNNIIIAGSICTFASVIMLGLDTRIVSPDVFVWLCYTKTWTLCIGFTLSFGAMFSKTWRVHSIFTNIRMDRKAIKDSKLFIILGILLFIDICVLVTWAFVSPFSYTVTELPHIPEDNIVIIPEVEKCNSSHSGVFQAVLYAVKGVLMILGCFLAWETRHVNVPALNDSKYIGTSVYCCVVMSVLGLSTSVILQERVNEMFSLASFFVIFSTTLTLCLVFVPKVIELARNPVGNEPRAYRRGLMKSVVAKTSQPMSPQPRSDSSGDLIGKAESENKLRRRYLHQKSTQLWDLVEKLRAQGDTRFLQQEWCLSSASPSSQERETSLLLRQPSSSNNREETSLTAAGPNGERSSDWPWVDPDEPSTKL
Protein: Guanine nucleotide-binding protein subunit beta-like protein (Q381F6)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
Sequence:
MEVVGRGRHAVMSIAASSTCPTTFGSLDTVGAVTLWDTRLKQKDYARVEAGPTVAAEGDATELLLAADVHMALVLAGEWITSYDLRRHAKLCSYRHTCELATFLGGTHPQRETTTLVVDEDGAITPFSLLECSPTAHLPACFSGGGQTIDAPSFGSLSNWCCGLGFVKRQQQDVAPLLCAIGMDGGGAIFSSPNRQEGEFNLLGDDWLVPSSGEVINPPLLTTCSFMESYVAIGRANGMYSIATATEDGDSIMEIFASPGHAHNNLSVIGWTGTPRPRLVTCSVCGEVSAWDVLPLLELEMEESVGDVEEGDPPPLDTSGSVREATGQMASVNCGVVIGGSRLVVGDTMGFVTTCNVA
Protein: Cellulose synthase catalytic subunit A [UDP-forming] (DcsA) (EC 2.4.1.12) (Q9U720)
Organism: Dictyostelium discoideum (Social amoeba)
Function: Catalytic subunit of cellulose synthase. It incorporates glucose from uridine 5'-diphosphate glucose (UDP-alpha-D-glucose) to cellulose (a (1->4)-beta-D-glucan), which is produced as an extracellular component for mechanical and chemical protection at the onset of the stalk formation, when the cells exhibit multicellular behavior during culmination.
Subcellular location: Membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}.
Interaction partners:
- UTP--glucose-1-phosphate uridylyltransferase 2
- Glycogen [starch] synthase
- Endoglucanase
- Endoglucanase
- cellulase
- Endoglucanase
- cellulose 1,4-beta-cellobiosidase
- Endoglucanase
- UTP--glucose-1-phosphate uridylyltransferase 1
- Glycoside hydrolase family 5 domain-containing protein
Sequence:
MDRNEGGDFPINTPNNINSSGGSYNNSMNNSSNNIGRDIGNNQSSRNLKPKPSQSNLKWIARDLKKKSVRKDSERKLKSSGVLKKKNTVMDFGEDDGGSGDDGNITEGLPISEGMDDLPSSSNSRGGSGNDEQKKQFPKEMNSPSSEYGTTSGGQRFDTLVDPDISLAEMEEKMRQHKVYQEQQQQQQQQQQQQKQKDKELSSQKKKPSSMQLSKKKHVAKEDSETLETIIGEEKKEVVFEVKPYFSHAILQATMAVFLIWNIFYFAYRAGWTMNRTDYITFSYSILFIIVEFISFLGSALHLNNFTNPCTFVLVVTLEQILAKRRKKHPTVMMYVCTYKEPPSIVSRTFRTAISMDYPSENLWIGLLDDSVNYRESRGWAHLQSVEKNFLYVLLQKAVYSVHNIRPPVTSQHEDPHGILNETSSKIESSTKEVIEAEVQWFIEYFLLNSWFGVGQEIPRDADDAERALIAKLRDDNFSPYRTFTKSESEKISNFTIDSLQSLWHGSAFFRPLIRSILLKKDYVRNFVSELNNQHRLRFLNTEALAMAQYQVLMMGRQELPWDEISSGNVRIDFDTCDGPIVSPKCTYLRRRKPPIPHNKAGNINNALFNESTKADYEFLGLLDADQQPHPDFLKRVLPYFYSDEGQDLAFVQTPQFFSNIYPVDDPLGHRNMEFYGPVMEGRSANNACPFVGTNAIFRRQPLYDIGGIMYNSVTEDMYTGMKLQVSGYKSWYHNEVLVVGTAPVDLKETLEQRKRWAQGAVEIFSLTPWGYIRGKLGWRKMLYNLDSCIYPFLSPTAFFYGASPLIMSIWTVPIVVKDPIIFILVGMIPVMVLPRVIQYMILRAKRPYEAGKSGPSLWVEATDLWRAEQTFFGFAGTYISSWREGSASIVKLLKARKISRHKLAMWNWKRDFVKKPVVCEVFRQTKLVNENDNAQESSGKHKAEQSFRTSNKESDTIKNSRLFLPNIILFVVNILAMMSAVLRFNCFQNDMWLLVVVAGFSFSTLWHLWSFIPMALRQSEKQWPYASSYHAHNIVLFLVLGFLVLLFVDVKVCIPRVG
Protein: Carnitine O-acetyltransferase, mitochondrial (Carnitine acetylase) (EC 2.3.1.7) (P32796)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Carnitine acetylase is specific for short chain fatty acids. Carnitine acetylase seems to affect the flux through the pyruvate dehydrogenase complex. It may be involved as well in the transport of acetyl-CoA into mitochondria.
Subcellular location: [Isoform Mitochondrial]: Mitochondrion inner membrane; Peripheral membrane protein; Matrix side {ECO:0000269|PubMed:7628448}.; SUBCELLULAR LOCATION: [Isoform Peroxisomal]: Peroxisome {ECO:0000269|PubMed:7628448}.
Interaction partners:
- Carnitine O-acetyltransferase YAT2
- Mitochondrial carnitine carrier
- Peroxisomal hydratase-dehydrogenase-epimerase
- Putative mitochondrial carnitine O-acetyltransferase
- Acyl-coenzyme A oxidase
- Peroxisomal targeting signal receptor
- Acetyl-coenzyme A synthetase 1
- Citrate synthase, peroxisomal
- Succinate/fumarate mitochondrial transporter
- Citrate synthase 3, mitochondrial
Sequence:
MRICHSRTLSNLKDLPITSRRAMHSAIVNYSTQKAQFPVETNNGEHYWAEKPNKFYQNKRPNFQGITFAKQQDLPSLPVPELKSTLDKYLQTIRPFCNDVETFERQQLLCKDFSEHMGPILQDRLKEYANDKRNWMAKFWDEQSYLQYNDPIVPYVSYFYSHMPLPNHLSKIDNDPLIKATAIISTVVKFIEAIKDESLPVEIIKGMPFCMNSFSLMFNTSRLPGKPEDNQDTNIFYSVYENNFVTIAYKGKFYKLMTHDGNDKPLSENEIWRQLYSVVFQGSQSDPKLGGIGSLTSLPRDQWREVHLELMKDPISQDSLETIHKSSFMLCLDLDQSPVTLEEKSRNCWHGDGINRFYDKSLQFLVTGNGSSGFLAEHSKMDGTPTLFLNNYVCQQLNKLDVDDFMRKVITPSSTVAMKPMELPFIITPKIHKAIESAQLQFKETIGEHDLRVWHYNKYGKTFIKRHGMSPDAFIQQVIQLAVFKYLKRQLPTYEAASTRKYFKGRTETGRSVSTASLEFVSKWQNGDVPIAEKIQALKHSAKEHSTYLKNAANGNGVDRHFFGLKNMLKSNDDQIPPLFKDPLFNYSSTWLISTSQLSSEYFDGYGWSQVNDNGFGLAYMLNNEWLHINIVNKPAKSGASVNRLHYYLSQAADEIFDALENENKRKAKL
Protein: Krueppel-like factor 12 (Transcriptional repressor AP-2rep) (O35738)
Organism: Mus musculus (Mouse)
Function: Confers strong transcriptional repression to the AP-2-alpha gene. Binds to a regulatory element (A32) in the AP-2-alpha gene promoter.
Subcellular location: Nucleus.
Interaction partners:
Sequence:
MNIHMKRKTIKNLSALENRMLMLDGMPAVRVKTELVESEQGSPNVHNYPDMEAVPLLLNNVKGEPPEDSLPVDHFQTQTEPVDLSINKARTSPTAASSSPVSMTASASSPSSTSTSSSSSSRPASSPTVITSVSSASSSSTVLSPGPLVASASGVGGQQFLHIIHPVPPSSPMNLQSNKLSHVHRIPVVVQSVPVVYTAVRSPGNVNNTIVVPLLEDGRSHGKAQMEPRGLSPRQSKSDSDDDDLPNVTLDSVNETGSTALSIARAVQEVHPSPVSRVRGNRMNNQKFACSISPFSIESTRRQRRSESPDSRKRRIHRCDFEGCNKVYTKSSHLKAHRRTHTGEKPYKCTWEGCTWKFARSDELTRHYRKHTGVKPFKCADCDRSFSRSDHLALHRRRHMLV
Protein: Tetratricopeptide repeat (TPR)-like superfamily protein (Q8L606)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
Sequence:
MESLGKLQLHHQPFHLSFTHTSSSTFPKNLFKSSIQPISSLKSASIKASSSKFQNSITPLPKSTPFRLFKSTCITLTTAAALLLANLHLKSPAIAAPIAPPPSVESKENVTLEEEERALDEHLITHPSDVDALRSLMEVKIKSRKLTEAVEVIDRLIKLEPEEKEWPVLKANIFTYSGDLDLAKTGFEEILAKDPLRVEAYHGLLMAYSDAGLDLKEVESRIEEAMLKCKKENNQNDFRDFKLLVAQIRVIEGKHSEALKLYQELVKEEPRDFRPYLCQGIIYTLLKKKDKAEEQFDNFRKLVPKNHPYREYFMDNMIATKLFSEKAQREMAEEMAGSTS
Protein: Tachykinin-related peptide 1 (TKRP-1) (P86594)
Organism: Pyrrhocoris apterus (Sap sucking bug) (Cimex apterus)
Subcellular location: Secreted {ECO:0000269|PubMed:19084564, ECO:0000305}.
Interaction partners:
Sequence:
GPSGFLGMR
Protein: Myosin-binding protein C, fast-type (Fast MyBP-C) (C-protein, skeletal muscle fast isoform) (P16419)
Organism: Gallus gallus (Chicken)
Function: Thick filament-associated protein located in the crossbridge region of vertebrate striated muscle a bands. In vitro it binds MHC, F-actin and native thin filaments, and modifies the activity of actin-activated myosin ATPase. It may modulate muscle contraction or may play a more structural role.
Interaction partners:
Sequence:
MPEPSKAAPKKEAKKKEEKKEEKKEAPPPQEHKDEAPDDVHPPETPDPEGLFLSKPQNVMVESGRDVTVSARVAGAALPCAPAVKWFKGKWAELGDKSARCRLRHSVDDDKVHTFELTITKVAMGDRGDYRCEVTAKEQKDSCSFSIDVEAPRSSEGNVLQAFKRTGEGKDDTAGELDFSGLLKKREVQVEEKKKKKDEDDQFPPEIWELLKGVTKKSEYERIAFQYGITDLRGMLKRLKKVHVEPKKSEAFIRKLDPAYQVDKGNKIKLVVELSDPDLPLKWYKNGQLLKPSTKYVFENVGLKRILTIHKCSLADDAAYECRVNDEKCFTEVFVKEPPVTVVRGLEDQQVVVGDRVVLEAEVSEEGAQVMWLKDGVDVTRDDAFKYRFKKDGKKHFLIINEAELSDSAHYKIMTNGGESEAELSVEEKQLEVLQDMADLTVKASEQAVFKCEVSDEKVTGRWFRNGVEVKPSKRIHISHNGRFHKLVIDDVRPEDEGDYTFIPDGYALSLSAKLNFLEIKVEYVPKQEPPKIHLDCSGKAAENTIVVVAGNKVRLDVPISGEPAPTVTWKRGDQLFTATEGRVHIDSQADLSSFVIESAERSDEGRYCITVTNPVGEDSATLHVRVVDVPDPPQSVRVTSVGEDWAVLSWEAPPFDGGMPITGYLMERKKKGSMRWMKLNFEVFPDTTYESTKMIEGVFYEMRVFAVNAIGVSQPSLNTQPFMPIAPTSEPTHVVLEDVTDTTATIKWRPPERIGAGGVDGYLVEWCREGSNEWVAANTELVERCGLTARGLPTGERLLFRVISVNMAGKSPPATMAQPVTIREIVERPKIRLPRHLRQTYIRRVGEQVNLVIPFQGKPRPQVTWSREGGALPAEVQTRTSDVDSVFFIRSAARPLSGNYEMRVRIDNMEDCATLRLRVVERPGPPQAVRVMEVWGSNALLQWEPPKDDGNAEISGYTVQKADTRTMEWFTVLEHSRPTRCTVSELVMGNEYRFRVYSENVCGTSQEPATSHNTARIAKEGLTLKMVPYKERDLRAAPQFLTPLVDRSVVAGYTVTLNCAVRGHPKPKVTWLKNSVEIGADPKFLSRHGLGVLSLLIRRPGPFDGGTYGCRAVNEMGEATTECRLDVRVPQ
Protein: Large ribosomal subunit protein mL54 (54S ribosomal protein L37, mitochondrial) (YmL37) (P36532)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Component of the mitochondrial ribosome (mitoribosome), a dedicated translation machinery responsible for the synthesis of mitochondrial genome-encoded proteins, including at least some of the essential transmembrane subunits of the mitochondrial respiratory chain. The mitoribosomes are attached to the mitochondrial inner membrane and translation products are cotranslationally integrated into the membrane. mL54 may have a meiosis-specific role as it accumulates during the middle stage of sporulation.
Subcellular location: Mitochondrion {ECO:0000269|PubMed:14562095, ECO:0000269|PubMed:14576278}. Note=Mitoribosomes are tethered to the mitochondrial inner membrane and spatially aligned with the membrane insertion machinery through two distinct membrane contact sites, formed by the 21S rRNA expansion segment 96-ES1 and the inner membrane protein MBA1. {ECO:0000269|PubMed:25609543}.
Interaction partners:
- Large ribosomal subunit protein uL23m
- Large ribosomal subunit protein mL46
- Large ribosomal subunit protein uL11m
- Large ribosomal subunit protein mL41
- Large ribosomal subunit protein mL43
- Large ribosomal subunit protein uL10m
- Large ribosomal subunit protein uL29m
- Large ribosomal subunit protein mL61
- Small ribosomal subunit protein bS18m
- Large ribosomal subunit protein mL40
Sequence:
MLARSLGYRLISTSRILYNKPTVKSVVSSCPAGTSLNLNIWKSGKDAVALEDKEYPNWLWSVLDSDHVVEHAAEDPEGQALLKRRKNIRKANRQRIKQNNFLSQL
Protein: Probable ATP-dependent DNA helicase CHR23 (EC 3.6.4.12) (Protein CHROMATIN REMODELING 23) (AtCHR23) (Protein MINUSCULE 2) (F4K128)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Probable chromatin-remodeling factor that is functionally redundant with CHR12 in root and shoot stem cell initiation and root apical meristem (RAM) and shoot apical meristem (SAM) maintenance. Can associate with the promoter region of WOX5. May promote seed maturation and repress initiation of germination. May repress plant growth.
Subcellular location: Nucleus {ECO:0000269|PubMed:23062007}.
Interaction partners:
- SWI/SNF complex subunit SWI3A
- Chromatin structure-remodeling complex protein BSH
- SWI/SNF complex subunit SWI3B
- SWI/SNF complex subunit SWI3D
- SWI/SNF complex subunit SWI3C
- SWI/SNF complex component SNF12 homolog
- At3g01890
- Actin-related protein 7
- High mobility group B protein 10
- Actin-related protein 4
Sequence:
MVKQLQEQEENDPVEKTKSLISALNYLSRDLLLPSHLYASVSSIYHASVSDLSPSPPLRGNSYTPNRGDLMSEFEDALLQQRLNYESGSRLAELKETRYKNRIHNRLSQLEGLPSNRGEDLQEKCLLELYGLKLQELQCRVRGEVSAEYWLRLNCADPERQLYDWGMMRLPRRMYGVGDSFVMEADDQFRNKRDAERLLRLEEEEKNLIETTQRKFFAEVLNAVREFQLQIQASHRRCKQRNDGVQAWHGKQRQRATRAEKLRIMALKSDDQEEYMKLAKESKNEKLTLFLEETNKIFVSLGAAVQRQKDAKLSENTKLLKGSESDLSDVDAPEDVLPAQDIEIIDSDNNDDSNDLLEGERQFNLAIHSIQEKVTKQPSLLQGGELRSYQLEGLQWMVSLYNNDYNGILADEMGLGKTIQTIALIAYLLESKDLHGPHLILAPKAVLPNWENEFALWAPSISAFLYDGSKEKRTEIRARIAGGKFNVLITHYDLIMRDKAFLKKIDWNYMIVDEGHRLKNHECALAKTLGTGYRIKRRLLLTGTPIQNSLQELWSLLNFLLPHIFNSIHNFEEWFNTPFAECGSASLTDEEELLIINRLHHVIRPFLLRRKKSEVEKFLPGKTQVILKCDMSAWQKLYYKQVTDVGRVGLHSGNGKSKSLQNLTMQLRKCCNHPYLFVGADYNMCKKPEIVRASGKFELLDRLLPKLKKAGHRILLFSQMTRLIDLLEIYLSLNDYMYLRLDGSTKTDQRGILLKQFNEPDSPYFMFLLSTRAGGLGLNLQTADTIIIFDSDWNPQMDQQAEDRAHRIGQKKEVRVFVLVSIGSIEEVILERAKQKMGIDAKVIQAGLFNTTSTAQDRREMLEEIMSKGTSSLGEDVPSEREINRLAARTEEEFWMFEQMDEERRKKENYKTRLMEEKEVPEWAYTSETQEDKTNAKNHFGSLTGKRKRKEAVYSDSLSDLQWMKAMESEDEDASKVSQKRKRTDTKTRMSNGSKAEAVLSESDEEKEEEEEERKEESGKESEEENEKPLHSWKTNKKKRSRYPVMTSSPNSRGKGSSKGSKRN
Protein: Small ribosomal subunit protein bS6m (37S ribosomal protein MRP17, mitochondrial) (Q9UT82)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Subcellular location: Mitochondrion {ECO:0000269|PubMed:16823372}.
Interaction partners:
- Large ribosomal subunit protein bL27m
- Small ribosomal subunit protein bS16m
- Large ribosomal subunit protein bL32m
- Small ribosomal subunit protein uS9m
- Small ribosomal subunit protein uS14m
- Large ribosomal subunit protein uL3m
- Large ribosomal subunit protein bL28m
- Large ribosomal subunit protein bL17m
- Small ribosomal subunit protein uS2m
- Small ribosomal subunit protein uS15m
Sequence:
MVMYELFCITRPAANATRTSSPTLAMNIAKNCGRAILDNKGVVVDVESMGLKELAKPIKKLNQSYSFGHWWSMTFYSNPTVQSEIQRILRLEPSVLRYMIVKKADKLSDLM
Protein: Small ribosomal subunit protein eS1B (40S ribosomal protein S1-B) (S3aE-B) (O94438)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Subcellular location: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_03122, ECO:0000269|PubMed:16823372}.
Interaction partners:
- Small ribosomal subunit protein uS15
- Small ribosomal subunit protein uS10
- Small ribosomal subunit protein uS5
- Small ribosomal subunit protein eS27
- Small ribosomal subunit protein uS3
- Small ribosomal subunit protein uS14
- Elongation factor 3
- mRNA export factor elf1
- Small ribosomal subunit protein eS7
- Small ribosomal subunit protein eS21
Sequence:
MAVGKNKRLSKGKKGIKKRVVDPFSRKEWYDIKAPAFFEVKNVGKTLVNRTAGLKNANDSLKGRILEVSLADLQKDEEHAFRKVKLRVEDIQGKSCLTSFNGLSITSDKLRSLVRKWQTTIEADQTIKTTDGYLCRVFVIGFTRRRANQVKKTTYAQSSQIRAIRQKMFQVIQNQTSSCSMRELVQKLIPEVIGREIERATGSIFPLQNVLVRKVKILKAPKHDAQKLLELHGESQDVGTKVVKDVAPLESV
Protein: Dolichyl-diphosphooligosaccharide--protein glycosyltransferase subunit DAD1 (Oligosaccharyl transferase subunit DAD1) (Defender against cell death 1) (DAD-1) (E2R4X3)
Organism: Canis lupus familiaris (Dog) (Canis familiaris)
Function: Subunit of the oligosaccharyl transferase (OST) complex that catalyzes the initial transfer of a defined glycan (Glc(3)Man(9)GlcNAc(2) in eukaryotes) from the lipid carrier dolichol-pyrophosphate to an asparagine residue within an Asn-X-Ser/Thr consensus motif in nascent polypeptide chains, the first step in protein N-glycosylation. N-glycosylation occurs cotranslationally and the complex associates with the Sec61 complex at the channel-forming translocon complex that mediates protein translocation across the endoplasmic reticulum (ER). All subunits are required for a maximal enzyme activity.
Subcellular location: Endoplasmic reticulum membrane {ECO:0000255|RuleBase:RU361136}; Multi-pass membrane protein {ECO:0000269|PubMed:29519914}.
Interaction partners:
- Dolichyl-diphosphooligosaccharide--protein glycosyltransferase subunit 2
- Dolichyl-diphosphooligosaccharide--protein glycosyltransferase subunit 1
- Dolichyl-diphosphooligosaccharide--protein glycosyltransferase 48 kDa subunit
- Dolichyl-diphosphooligosaccharide--protein glycosyltransferase subunit STT3A
- Dolichyl-diphosphooligosaccharide--protein glycosyltransferase subunit STT3B
- Tumor suppressor candidate 3.
- Mannosyl-oligosaccharide glucosidase.
- Dol-P-Glc:Glc
- Protein transport protein Sec61 subunit beta
- Dolichyl-diphosphooligosaccharide--protein glycosyltransferase subunit TMEM258
Sequence:
MSASVASVISRFLEEYLSSTPQRLKLLDAYLLYILLTGALQFGYCLLVGTFPFNSFLSGFISCVGSFILAGNGSLRNRSNNVFTLVRCFSSLVTLFYSRSPPREVPRGACIALFCERGN
Protein: Saposin-related, isoform B (Q8IMH4)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MVTQARDQLKSNQTEEELKEVFEGSCKLIPIKPIQKECIKVADDFLPELVEALASQMNPDQVCSVAGLCNSARIDELYKNGIQAGLDGTVQNEDDSSEETELAMQPNQLSCGNCNLLSRLMHSKFAATDRDDMVETMLHMCGSLSSFSDACANIVLTYFNDIYDHVSKHLTTDAVCHVSGVCASRYHQHEEEKQPQEALVALDAGDDIPCELCEQLVKHLRDVLVANTTETEFKQVMEGFCKQSKGFKDECLSIVDQYYHVIYETLVSKLDANGACCMIGICQKNSASSMKDVPIMPLLPVIEPAQVKITIEKLEKHEKKQLGASEPKFSQQEILDMQLPIDHLMGAANPGALVEGGELCTLCEYMLHFIQETLATPSTDDEIKHTVENICAKLPSGVAGQCRNFVEMYGDAVIALLVQGLNPRDVCPLMQMCPKNLPKKEDVEVFNPQPASDEQDPPTCPLCLFAVEQAQMKIRDNKSKDNIKKVLNGLCSHLPNEIKEECVDFVNTYSNELIDMLITDFKPQEICVQLKLCPKTTYALWDLRISLEDDVDGEDKSSSEEISFNDIESLEELPPQLAFDPGFTAAPNCLICEELVKTLEKRMGKHPTRDSIKHILEESCDRMRKPMNTKCHKVIDKYGDKIADLLLKEMDPKLICTELGMCILADLDDLEVDEALKYDVIALPRQDNKLSSSIKEPPTCVLCEFIMTKLDADLKNKTEQDDIKRAIEAVCNRLPATVRKQCDTFVDGYASAVLKLLSDVPPKQVCQKLQLCFSVAVTDEVLECGVCHGVTQALLPFLREKKDNVSEVTALQMTSVGCENLPAKYYKICSEMISIYGSSIKNLAKRPYIDQSHICAEIGKCFESEKSSLAFARISA
Protein: NEDD8-activating enzyme E1 catalytic subunit (EC 6.2.1.64) (NEDD8-activating enzyme E1C) (Ubiquitin-activating enzyme E1C) (Ubiquitin-like modifier-activating enzyme 3) (Ubiquitin-activating enzyme 3) (Q99MI7)
Organism: Rattus norvegicus (Rat)
Function: Catalytic subunit of the dimeric UBA3-NAE1 E1 enzyme. E1 activates NEDD8 by first adenylating its C-terminal glycine residue with ATP, thereafter linking this residue to the side chain of the catalytic cysteine, yielding a NEDD8-UBA3 thioester and free AMP. E1 finally transfers NEDD8 to the catalytic cysteine of UBE2M. Down-regulates steroid receptor activity. Necessary for cell cycle progression.
Interaction partners:
- NEDD8-activating enzyme E1 regulatory subunit
- Ubiquitin-like protein NEDD8
- NEDD8-conjugating enzyme UBC12
- NEDD8-conjugating enzyme UBE2F
- E3 ubiquitin-protein ligase RBX1
- Cullin-1
- Cullin 2
- Cullin-5
- Sentrin-specific protease 8
- RING-box protein 2
Sequence:
MADGEEPEKKRRRIEELLAEKMAVDGGCGDTGDWEGRWNHVKKFLERSGPFTHPDFEPSTESLQFLLDTCKVLVIGAGGLGCELLKNLALSGFRQIHVIDMDTIDVSNLNRQFLFRPKDVGRPKAEVAAEFLNDRVPNCNVVPHFNKIQDFNDTFYRQFHIIVCGLDSIIARRWINGMLISLLNYEDGVLDPSSIVPLIDGGTEGFKGNARVILPGMTACIECTLELYPPQVNFPMCTIASMPRLPEHCIEYVRMLQWPKEQPFGDGVPLDGDDPEHIQWIFQKSVERASQYNIRGVTYRLTQGVVKRIIPAVASTNAVIAAVCATEVFKIATSAYIPLNNYLVFNDVDGLYTYTFEAERKENCPACSQLPQNIQFSPSAKLQEVLDYLTNSASLQMKSPAITATLEGKNRTLYLQSVTSIEERTRPNLSKTLKELGLVDGQELAVADVTTPQTVLFKLHFT
Protein: D-xylulose reductase (EC 1.1.1.9) (Xylitol dehydrogenase) (XDH) (Q07993)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Interaction partners:
- Xylulose kinase
- NADPH-dependent aldose reductase GRE3
- Transaldolase
- Transketolase 1
- 4-nitrophenylphosphatase
- Transketolase 2
- Transaldolase NQM1
- Ribulose-phosphate 3-epimerase
- High-affinity hexose transporter HXT7
- Alcohol dehydrogenase 4
Sequence:
MTDLTTQEAIVLERPGKITLTNVSIPKISDPNEVIIQIKATGICGSDIHYYTHGRIANYVVESPMVLGHESSGIVALIGENVKTLKVGDRVALEPGIPDRFSPEMKEGRYNLDPNLKFAATPPFDGTLTKYYKTMKDFVYKLPDDVSFEEGALIEPLSVAIHANKLAKIKFGARCVVFGAGPIGLLAGKVASVFGAADVVFVDLLENKLETARQFGATHIVNSGDLPHGVTVDSVIKKAIGKKGADVVFECSGAEPCVRAGIEVCKAGGTIVQVGMGQEEIQFPISIIPTKELTFQGCFRYCQGDYSDSIELVSSRKLSLKPFITHRYSFKDAVEAFEETSHHPLNNIKTIIEGPE
Protein: WASH complex subunit 3 (Coiled-coil domain-containing protein 53) (Q9CR27)
Organism: Mus musculus (Mouse)
Function: Acts as a component of the WASH core complex that functions as a nucleation-promoting factor (NPF) at the surface of endosomes, where it recruits and activates the Arp2/3 complex to induce actin polymerization, playing a key role in the fission of tubules that serve as transport intermediates during endosome sortingg.
Subcellular location: Early endosome {ECO:0000305}.
Interaction partners:
- WASH complex subunit 4
- WASH complex subunit 2
- WASH complex subunit 1
- WASH complex subunit 5
- Sorting nexin-27
- Nucleoporin Nup37
- TBC1 domain family member 23
- Heat shock factor-binding protein 1
- Heat shock factor-binding protein 1-like protein 1
- DnaJ heat shock protein family
Sequence:
MDEDGLPLMGSGIDLTKVPAIQQKRTVAFLNQFVVHTVQFLNRFSAVCEEKLADLSLRIQQIETTLNILDAKLSSIPGLEDVTVEVSPLNVTAVTNGSHSETTSEQTQQNSTQDSGAQESEAPSENVLTVAKDPRYARYLKMVQVGVPVMAIRDKMISEGLDPELLEKPDAPVPNGESERAVEESSDSDSSFSD
Protein: Hmx1p (Q5AB97)
Organism: Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast)
Interaction partners:
- coproporphyrinogen oxidase
- Ferrochelatase
Sequence:
MQYKSSGATSKLSQVEIIPAKTDVGALANRINLETRSLHDRADKTVTLKFALALRNYKVYRQGLQAFYHVFASIEKALYRQLEKKDEWSEMLEQVWKPEIARAGKAEQDLLFFYDDNKEKFIKPIMPAQIEFCKHILEVTEEKPYLLFAYLHVMYLALFAGGRIMRSSVLKATGMYPQRDGLSHDDVVRMGTNFFTFDVPDEDLLRLTYKRDYELVTRNGLTEEQKLEIIEESKYIFEHDVKCVAELEKHNMDKLSGTWTYFLVTRGYYAALVLFSLLALIYLRRVVNKLT
Protein: Stevor (Q8I2C6)
Organism: Plasmodium falciparum (isolate 3D7)
Interaction partners:
Sequence:
MNMYYLKMILFTFLINTLVLPHYENYLNNHYNVSLIQSKTKRTTIKSRLLAQTQIRNPHYHNDPELKEIIDKMNEEAIKKYQNTHHPYKQLKEVVEKNVTKHVGGNDTEPMSTLEKELLETYEEMFGNERDIMLKSGMYQNDDDGSDDSSTCECTDTNNSELAKTKGKDKYLKHLKHRCTHGIGYCSIGSTFLTLIGLALAKKAAFDTLNVTFHGVSYSKCASSISIFNMLDGPSMFAGGTACSADLTGNAAFAAMGALYPWGIAALVLLILAIILIILYIWLYRRRKNSWKHECKKHLCR
Protein: ribonuclease III (EC 3.1.26.3) (Q2Q3V5)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
PRGYQLRLVDHLTKSNGIVYLPTGSGKTFVAILVLKRFSQDFDKPIESGGKRALFMCNTVELARQQAMAVRRCTNFKVGFYVGEQGVDDWTRGMWSDEIKKNQVLVGTAQVFLDMVTQTYVALSSLSVVIIDECHHGTGHHPFREFMRLFTIANQTKLPRVVGLTGVLIKGNEITNVATKLKELEITYRGNIITVSDTKEMENVMLYATKPTEVMVSFPHQEQVLTVTRLISAEIEKFYVSLDLMNIGVQPIRRSKSLQCLRDPSKKSFVKQLFNDFLYQMKEYGIYAASIAIISLIVEFDIKRRQAETLSVKLMHRTALTLCEKIRHLLVQKLQDMTYDDDDDNVNTEEVIMNFSTPKVQRFLMSLKVSFADKDPKDICCLVFVERRYTCKCIYGLLLNYIQSTPELRNVLTPQFMVGRNNISPDFESVLERKWQKSAIQQFRDGNANLMICSSVLEEGIDVQACNHVFILDPVKTFNMYVQSKGRARTTEAKFVLFTADKEREKTIQQIYQYRKAHNDIAEYLKDRVLEKTEPELYEIKGHFQDDIDPFTNENGAVLLPNNALAILHRYCQTIPTDAFGFVIPWFHVLQEDERDRIFGVSAKGKHVISINMPVNCMLRDTIYSDPMDNVKTAKISAAFKACKVLYSLGELNERFVPKTLKERVAAIADVHFEHWNKYGDSVTATVNKADKSKDRTYKTECPLEFYDALPRVGEICYAYEIFLEPQFESCEYTEHMYLNLQTPRNYAILLRNKLPRLAEMPLFSNQGKLHVRVANAPLEVIIQNSEQLELLHQFHGMVFRDILKIWHPFFVLDRRSKENSYLVVPLILGAGEQKCFDWELMTNFRRLPQSHGSNVQQREQQPAPRPEDFEGKIVTQWYANYDKRMLVTKVHRELTPLSYMEKNQQDKTYYEFTMSKYGNRIGDVVHKDKFMIEVRDLTEQLTFYVHNRGKFNAKSKAKMKVILIPELCFNFNFPGDLWLKLIFLPSILNRMYFLLHAEALRKRFNTYLNLHLLPFNGTDYMPRPLEIDYSLKRNVDPLGNVIPTEDIEEPKSLLEPMPTKSIEASVANLEITEFENPWQKYMEPVDLSRNLLSTYPVELDYYYHFSVGNVCEMNEMDFEDKEYWAKNQFHMPTGNIYGNRTPAKTNANVPALMPSKPTVRGKVKPLLILQKTVSKEHITPAEQGEFLAAITASSAADVFDMERLEILGDSFLKLSATLYLASKYSDWNEGTLTEVKSKLVSNRNLLFCLIDADIPKTLNTIQFTPRYTWLPPGISLPHNVLALWRENPEFAKIIGPHNLRDLALGDEESLVKGNCSDINYNRFVEGCRANGQSFYAGADFSSEVNFCVGLVTIPNKVIADTLEALLGVIVKNYGLQHAFKMLEYFKICRADIDKPLTQLLNLELGGKKMRANVNTTEIDGFLINHSYLEKNLGYTFKDRRYLLQALTHPSYPTNRITGSYQELEFIGDAILDFLISAYIFENNTKMNPGALTDLRSALVNNTTLACICVRHRLHFFILAENAKLSEIISKFVNFQESQGHRVTNYVRILLEEADVQPTPLDLDDELDMTELPHANKCISQEAEKGVPPKGEFNMSTNVDVPKALGDVLEALIAAVYLDCRDLQRTWEVIFNLFEPELQEFTRKVPINHIRQLVEHKHAKPVFSSPIVEGETVMVSCQFTCMEKTIKVYGFGSNKDQAKLSAAKHALQQLSKCDA