wanglab/gogpt-training-data huggingface dataset:
Protein: Acetyl-coenzyme A synthetase 2-like, mitochondrial (EC 6.2.1.1) (Acetate--CoA ligase 2) (Acetyl-CoA synthetase 2) (AceCS2) (Acyl-CoA synthetase short-chain family member 1) (Propionate--CoA ligase) (EC 6.2.1.17) (Q99NB1)
Organism: Mus musculus (Mouse)
Function: Catalyzes the synthesis of acetyl-CoA from short-chain fatty acids. Acetate is the preferred substrate. Can also utilize propionate with a much lower affinity. Provides acetyl-CoA that is utilized mainly for oxidation under ketogenic conditions. Involved in thermogenesis under ketogenic conditions, using acetate as a vital fuel when carbohydrate availability is insufficient.
Subcellular location: Mitochondrion matrix {ECO:0000269|PubMed:11150295}.
Interaction partners:
- NAD-dependent protein deacetylase sirtuin-3
- Citrate synthase, mitochondrial
- Citrate synthase
- Acetyl-CoA carboxylase 1
- Acetyl-coenzyme A thioesterase
- Methylmalonate-semialdehyde/malonate-semialdehyde dehydrogenase [acylating], mitochondrial
- Peroxisomal acyl-coenzyme A oxidase 1
- Acetyl-CoA carboxylase 2
- Acetyl-CoA acetyltransferase, mitochondrial
- Short-chain specific acyl-CoA dehydrogenase, mitochondrial
Sequence:
MAARSLGSGVGRLLRGLQGRSGQSGWSLSVSRSTATRLPGCVPAAAQPGSYPALSAQAAQEPAAFWGPLARDTLVWDTPYHTVWDCDFRTGKIGWFLGGQLNVSVNCLDQHVQKSPETIALIWERDEPGTEVRITYRELLETTCRLANTLKRHGVHRGDRVAIYMPVSPLAVAAMLACARIGAIHTVVFAGFSAESLAGRINDAKCKAVITFNQGLRGGRVVELKKIVDEAVKSCPTVQHVLVAHRTDTKVPMGSLDIPLEQEMAKEAPVCTPESMSSEDMLFMLYTSGSTGTPKGLVHTQAGYLLYAAMTHKLVFDYQPGDVFGCVADIGWITGHSYVVYGPLCNGATTVLFESTPVYPDAGRYWETVQRLKINQFYGAPTAVRLLLKYGDAWVKKYDRSSLRTLGSVGEPINHEAWEWLHKVVGDGRCTLVDTWWQTETGGICIAPRPSEDGAEILPGMAMRPFFGIVPVLMDEKGNVLEGGDVSGALCISQAWPGMARTIYGDHQRFVDAYFRAYPGYYFTGDGAHRTEGGYYQITGRMDDVINISGHRLGTAEIEDAMADHPAVPETAVIGYPHDIKGEAAFAFIVLKDNISDENMVVNELKLSVATKIAKYAVPDQILVVKRLPKTRSGKVMRRLLRKIITSRGQDLGDTTTLEDPSVITEILSAFQKYEEQRAATN
Protein: F-box protein At1g11270 (Q7X7A9)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
- PsbP domain-containing protein 7, chloroplastic
- At1g50440
- Bromo-adjacent homology
- Protein ROOT HAIR SPECIFIC 17
- Cytochrome oxidase complex assembly protein
- Arogenate dehydrogenase 2, chloroplastic
- RNA binding / RNA-directed DNA polymerase
- F28K20.8 protein
- Putative receptor-like protein kinase At2g30940
- DExH-box ATP-dependent RNA helicase DExH18, mitochondrial
Sequence:
MLKRDCSSVVGSERERDGSSLALKRHCSSVVKLLLPHDVVGLILERLPVESLLRFKCVSNQWKSTIESQCFQERQLIRRMESRGPDVLVVSFADDEDKYGRKAVFGSSIVSTFRFPTLHTLICYGSCEGLICIYCVYSPNIVVNPATKWHRSCPLSNLQQFLDDKFEKKEYDFPTPKLAFGKDKLNGTYKQVWLYNSSEFRLDDVTTCEVFDFSNNAWRYVHPASPYRINDYQDPVYSDGSVHWLTEGKESKILSFHLHTETFQVLCEAPFLRERDPVGDSMCILDNRLCVSEINGPAQLIWSLDSSGGNKC
Protein: Brain-specific homeobox protein homolog (Q6R3Q6)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Function: DNA binding protein that function as transcriptional activator. May play a role in the determination and function of cell types in the brain.
Subcellular location: Nucleus {ECO:0000250|UniProtKB:Q810B3}.
Interaction partners:
- Agouti-related neuropeptide.
Sequence:
MNLNYTSPVPQMPTQRSTSFFIEDILLHKPKPLREVFPSPFSNSIASRMPLLEYGYPLMPTPILAPHPHHPLHKPEHHPYFFTSGMQMPALFQHHPELPGKHCRRRKARTVFSDSQLSGLEKRFEIQRYLSTPERVELATALSLSETQVKTWFQNRRMKHKKQLRKTQDDQKTPNDVDRSLENTSESEMHEKNTDGKNGMSPDRYTLDDNEDDVDIEDDICSPEHLL
Protein: Patatin-like phospholipase domain containing 3 (D3Z9J9)
Organism: Rattus norvegicus (Rat)
Interaction partners:
- Diacylglycerol O-acyltransferase 2
- Diacylglycerol O-acyltransferase 1
- Lipoprotein lipase
- Hepatic triacylglycerol lipase
- Gastric triacylglycerol lipase
- Endothelial lipase
- Pancreatic lipase-related protein 2
- Pancreatic triacylglycerol lipase
- Patatin-like phospholipase domain-containing protein 2
- Bile salt-activated lipase
Sequence:
MYDPERRWSLSFAGCGFLGFYHIGATLCLSERAPHILREARTFFGCSAGALHAVTFVCSLPLDHIMEILMDLVRKARSRNIGTLHPFFNINKCVRDGLQETLPDNVHQIISGKVYISLTRVSDGENVLVSEFHSKDEVVDALVCSCFIPLFSGLIPPSFRGERYVDGGVSDNVPVLDAKTTITVSPFYGEHDICPKVKSTNFLQVNITNLSLRLCTGNLHLLTRALFPSDVKVMGELCFQGYLDAFRFLEENGICNGPQRSLSLSLEKEMAPETMIPCLENGHLVAGNKVPVSCVCLTAVPSDESIWEMLSPKLSTALTEAIKDRGGYLNKVCNLLPIRILSYILLPCTLPVESAIAAVHRLVMWLPDIHEDIQWLQWATSQVCARMTMCLLPSTRSRASKDNHQTLKHGYHPSLHKPQGSSAGL
Protein: Centromere/kinetochore protein zw10 homolog (AtZW10) (MAG2-interacting protein 1) (O48626)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: May be required for accurate chromosome segregation. Required for proper maturation of seed storage proteins. Forms a complex with MAG2, MIP2 and MIP3 on the endoplasmic reticulum that may be responsible for efficient transport of seed storage proteins.
Subcellular location: Cytoplasm, cytoskeleton, spindle. Cytoplasm. Chromosome, centromere. Chromosome, centromere, kinetochore. Endoplasmic reticulum membrane; Peripheral membrane protein {ECO:0000269|PubMed:24118572}. Note=In prometaphase, associated with the kinetochore. At metaphase, mostly associated with the spindle. In early anaphase, found in the vicinity of the centromere. As anaphase progresses, dispersed in the cytoplasm.
Interaction partners:
- Syntaxin-81
- MAG2-interacting protein 2
- At3g24315
- RINT1-like protein MAG2
- RINT1-like protein MAG2L
- Homeobox protein LUMINIDEPENDENS
- Sec1 family domain-containing protein MIP3
- Coatomer subunit delta
- At3g55600
- Membrane fusion protein Use1
Sequence:
MPEIDALFESINVRDLLAGHDLNDPTTPLSAPDLRLLINRLESHSLRIKSKVQSYLVAHHSDFSELFSLCQDTVSRTRLISDDVSDVLQLVSDRPIDVEIRSVVDEITEKTKEVKLKRESLDLVNAIVGICEALQETKEALKNGRFRFAAERIRELKVVLRIGEEEDGEPVAYALLRKEWSNCFDEIQEVLAKFMENAVRFELDSSRIRIKYQLSVGETAGIALSTVLEAMEVIGILDYGLAKAADSIFKHVITPAVTHASTFAAVEDLCKSAGEVTEATLRLEQSSDHKFEDVDGDAMYSGILKVVKFICSSLCFGNVTWIHSFGRLTWPRISELIISKFLSKVVPEDASKLADFQKIIERTSQFEAALKELNFVSSSDAESRLSKYAEDVEVHFASRKKIEILAKARNLLLQCNFTIPQDIAMRNAKHIVCLLFSSERCVVSEAASQLMNLVHKTLEDVCVSSARVASEFYNAARDSILLYEAVVPVKLEKQLDGLNEAAVLLHNDCLYLFEEILGLAFEYRASFPSSIKEYAVFADIAPRFKLMAEEVLQKQVHLVISSLREAIDSADGFQNTHQIKQFKSAEFSIDQVVFSLKNVHMIWEPVLRPKTYKQSMCAVLESVFRRIARDILLLDDMAADETFELQKLIYLMLKNLSSVLDSVRSADETSRPLDDIIPSLRKTRKLAELLDMPLMSITSAWESGELFRCNFTRTEVQDFIKAIFTDSPLRKECLWRIDEVNQ
Protein: Always early (Q2PNP6)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
MSRHQLKKPRKMVAAWQNDELFIKRPNFAPRIRISEKPEIQGRIKPGVASKRTENFTKKPSKISVDVSEDEKAKEKEKEQDPYSNDFILGKRLYNFLKYLSSHRWIWCEFVDSFLDKPTLTMGYDMKRFIAEYCPLLHSCFMPRRGWQLVRRNMGKARRFSAAFIELEREXLECQRRIVRQLQQHKFNPKENVGYLDQIPKRVPLPLAKDATVSSFLHGNSFEGIVNGTVMGYDPQDYTYLVRFNRNDNAVVLSLPDSQLYSDEETAAVPLSIIMRGNKSSSVISESAKTEKFGNKRYTKELLESVLRVGKLQDVKHKILMDLARMNEDFETFKEIGSSSSRRDAKVTPQRENLQRRYSASMITLHRVNADILEPLCILHDYMVEYQKQDEEEESKRGRPASEVYQKCRMQAEQDLKTAADEKFLKIESDRTQEFVRNLHTILYLNGKLGRESSSNLETIIADLVTHMVDNIQPSLGRKLKDGVDSLEPLRQQVVQIFKDVKKPERFQITQQAPMQTEDGIYNFVVEAQPDTPS
Protein: ATP synthase peripheral stalk subunit OSCP, mitochondrial (ATP synthase subunit O) (Oligomycin sensitivity conferral protein) (OSCP) (Q9DB20)
Organism: Mus musculus (Mouse)
Function: Mitochondrial membrane ATP synthase (F(1)F(0) ATP synthase or Complex V) produces ATP from ADP in the presence of a proton gradient across the membrane which is generated by electron transport complexes of the respiratory chain. F-type ATPases consist of two structural domains, F(1) - containing the extramembraneous catalytic core and F(0) - containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation. Part of the complex F(0) domain and the peripheric stalk, which acts as a stator to hold the catalytic alpha(3)beta(3) subcomplex and subunit a/ATP6 static relative to the rotary elements.
Subcellular location: Mitochondrion {ECO:0000250}. Mitochondrion inner membrane {ECO:0000250}.
Interaction partners:
- ATP synthase F
- ATP synthase F
- ATP synthase peripheral stalk subunit d, mitochondrial
- ATP synthase peripheral stalk subunit b, mitochondrial
- ATP synthase F
- ATP synthase F
- ATP synthase F
- ATP synthase peripheral stalk subunit F6, mitochondrial
- ATP synthase F
- ATP synthase F
Sequence:
MAAPAASGLSRQVRSFSTSVVRPFAKLVRPPVQVYGIEGRYATALYSAASKEKKLDQVEKELLRVGQLLKDPKVSLAVLNPYIKRTVKVKSLNDITKREKFSPLTANLMNLLAENGRLGNTQGIISAFSTIMSVHRGEVPCTVTTASPLDDAVLSELKTVLKSFLSPNQILKLEIKTDPSIMGGMIVRIGEKYVDMSAKSKIQKLSKAMREML
Protein: FUN14 domain-containing protein 2 (Hepatitis C virus core-binding protein 6) (Q9D6K8)
Organism: Mus musculus (Mouse)
Function: Binds directly and specifically 1,2-Diacyl-sn-glycero-3-phospho-(1'-myo-inositol-3',4',5'-bisphosphate) (PIP3) leading to the recruitment of PIP3 to mitochondria and may play a role in the regulation of the platelet activation via AKT/GSK3B/cGMP signaling pathways. May act as transcription factor that regulates SREBP1 (isoform SREBP-1C) expression in order to modulate triglyceride (TG) homeostasis in hepatocytes (By similarity).
Subcellular location: Mitochondrion outer membrane {ECO:0000250|UniProtKB:Q9BWH2}; Multi-pass membrane protein {ECO:0000255}. Nucleus {ECO:0000250|UniProtKB:Q9BWH2}.
Interaction partners:
Sequence:
MAANSQGNFDGKFEALDLAELTKKQPWWRKLFGQESGPSAEKYSVATQLVIGGVTGWCTGFVFQKVGKLAATAVGGGFFLLQLANHTGYIKVDWQRVEKDMKKAKEQLKIRKNKQIPTEVKSKAEEVVSFVKKNVLVTGGFFGGFLLGMAS
Protein: cDNA FLJ12599 fis, clone NT2RM4001410 (E2PSM9)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MLLSLPEKVVSPPEPEKEEAAKEEATKEEEAIKEEVVKEPKDEAQNEGPATESEAPLKEDGLLPKPLSSGGEEEEKPRGEASEDLCEMALDPELLLLRDDGEEEFAGAKLEDSEVRSVASNQSEMEFSSLQDMPKELDPSAVLPLDCLLAFVFFDANWCGYLHRRDLERILLTLGIRLSAEQAKQLVSRVVTQNICQYRSLQYSRQEGLDGGLPEEVLFGNLDLLPPPGKSTKPGAAPTEHKALVSHNGSLINVGSLLQRAEQQDSGRLYLENKIHTLELKLEESHNRFSATEVTNKTLAAEMQELRVRLAEAEETARTAERQKSQLQRLLQELRRRLTPLQLEIQRVVEKADSWVEKEEPAPSN
Protein: UPF1 (A0A024R7L5)
Organism: Homo sapiens (Human)
Subcellular location: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
Interaction partners:
Sequence:
MSVEAYGPSSQTLTFLDTEEAELLGADTQGSEFEFTDFTLPSQTQTPPGGPGGPGGGGAGGPGGAGAGAAAGQLDAQVGPEGILQNGAVDDSVAKTSQLLAELNFEEDEEDTYYTKDLPIHACSYCGIHDPACVVYCNTSKKWFCNGRGNTSGSHIVNHLVRAKCKEVTLHKDGPLGETVLECYNCGCRNVFLLGFIPAKADSVVVLLCRQPCASQSSLKDINWDSSQWQPLIQDRCFLSWLVKIPSEQEQLRARQITAQQINKLEELWKENPSATLEDLEKPGVDEEPQHVLLRYEDAYQYQNIFGPLVKLEADYDKKLKESQTQDNITVRWDLGLNKKRIAYFTLPKTDSDMRLMQGDEICLRYKGDLAPLWKGIGHVIKVPDNYGDEIAIELRSSVGAPVEVTHNFQVDFVWKSTSFDRMQSALKTFAVDETSVSGYIYHKLLGHEVEDVIIKCQLPKRFTAQGLPDLNHSQVYAVKTVLQRPLSLIQGPPGTGKTVTSATIVYHLARQGNGPVLVCAPSNIAVDQLTEKIHQTGLKVVRLCAKSREAIDSPVSFLALHNQIRNMDSMPELQKLQQLKDETGELSSADEKRYRALKRTAERELLMNADVICCTCVGAGDPRLAKMQFRSILIDESTQATEPECMVPVVLGAKQLILVGDHCQLGPVVMCKKAAKAGLSQSLFERLVVLGIRPIRLQVQYRMHPALSAFPSNIFYEGSLQNGVTAADRVKKGFDFQWPQPDKPMFFYVTQGQEEIASSGTSYLNRTEAANVEKITTKLLKAGAKPDQIGIITPYEGQRSYLVQYMQFSGSLHTKLYQEVEIASVDAFQGREKDFIILSCVRANEHQGIGFLNDPRRLNVALTRARYGVIIVGNPKALSKQPLWNHLLNYYKEQKVLVEGPLNNLRESLMQFSKPRKLVNTINPGARFMTTAMYDAREAIIPGSVYDRSSQGRPSSMYFQTHDQIGMISAGPSHVAAMNIPIPFNLVMPPMPPPGYFGQANGPAAGRGTPKGKTGRGGRQKNRFGLPGPSQTNLPNSQASQDVASQPFSQGALTQGYISMSQPSQMSQPGLSQPELSQDSYLGDEFKSQIDVALSQDSTYQGERAYQHGGVTGLSQY
Protein: Sorting nexin-3 (Q9VG51)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}. Golgi apparatus membrane {ECO:0000256|ARBA:ARBA00004255}; Peripheral membrane protein {ECO:0000256|ARBA:ARBA00004255}; Cytoplasmic side {ECO:0000256|ARBA:ARBA00004255}. Prevacuolar compartment membrane {ECO:0000256|ARBA:ARBA00004179}; Peripheral membrane protein {ECO:0000256|ARBA:ARBA00004179}; Cytoplasmic side {ECO:0000256|ARBA:ARBA00004179}.
Interaction partners:
- Vacuolar protein sorting-associated protein 35
- Vacuolar protein sorting-associated protein 26
- Vacuolar protein sorting-associated protein 29
- Sorting nexin 6, isoform B
- LD13361p
- FI18122p1
- Protein wntless
- LD15323p
- von Willebrand factor A domain-containing protein 8
- Vacuolar protein sorting-associated protein 26C
Sequence:
MMVESDGTADATRRLNVKKQTLDDAYAVPANFLEIDVVNPLTTMAAGKKRYTDYEVRMRTNLPVFKVKESSVRRRYSDFEWLRNELERDSKIVVPPLPGKAWKRQMPFRGDEGIFDESFIEERRKGLEAFINKIAGHPLAQNERCLHMFLQENVIDKNYVPGKIRNT
Protein: Two-component response regulator-like PRR1 (Pseudo-response regulator 1) (OsPRR1) (Q689G9)
Organism: Oryza sativa subsp. japonica (Rice)
Function: Controls photoperiodic flowering response. Seems to be one of the component of the circadian clock. Expression of several members of the ARR-like family is controlled by circadian rhythm. The particular coordinated sequential expression of PRR73, PRR37, PRR95, PRR59 and PPR1 result to circadian waves that may be at the basis of the endogenous circadian clock (By similarity).
Subcellular location: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00357, ECO:0000269|PubMed:21549224}.
Interaction partners:
- Putative adagio-like protein 2
- Adagio-like protein 1
- Protein GIGANTEA
- Os04g0526000 protein
- Two-component response regulator-like PRR95
- Os02g0635800 protein
- Os02g0828566 protein
- Os03g0422702 protein
- Os11g0157600 protein
- Adagio-like protein 3
Sequence:
MVGAGEGDRVGGGAAVGGGQQFVDRSKVRILLCDSDPSSSREVLRLLCNCSYQVTCAKSPRQVINVLNCEAGEIDIILAEVDLPVSKCFKMLKYIARNKELRHIPIIMMSNRDEVSVVVKCLRLGAAEYLVKPLRMNELLNLWTHVWRRRRMLGLSEKNFFNDNFELALSEPSDANTNSTTLLSDDTDDKPKENINQETSTSNQHEYESNPSDAEPKQKGTPEGLLVSTEGGDQASSPGVMFSRPIKTNLRVAESSAFLAYVKSSTPTTSSFDSELQKGGNRLDSSDHRGNFSSTTDRSDTGTDVNIRDKEAFEMPVQYPVVCFSSSNLHLERSNEGQNDASGTPPVYHFPFYYPGMMDHGMTHPPVQNFQGNINNAQVHTPQTLLPQYNVYPQCHGVSMMPPFQYNPAGMSIQSNQLPTQNMWPQASSTPMPEETCSRSERRAAALAKFRLKRKERCFDKKVRYVNRKKLAETRPRVRGQFVRQANYTDITSTGDDISEDEDDDPSSREVEMVSSPE
Protein: Polycomb protein SCMH1 (Sex comb on midleg homolog 1) (Q96GD3)
Organism: Homo sapiens (Human)
Function: Associates with Polycomb group (PcG) multiprotein complexes; the complex class is required to maintain the transcriptionally repressive state of some genes.
Subcellular location: Nucleus {ECO:0000305}.
Interaction partners:
- Polycomb group RING finger protein 2
- Polycomb complex protein BMI-1
- Polyhomeotic-like protein 1
- E3 ubiquitin-protein ligase RING2
- E3 ubiquitin-protein ligase RING1
- Chromobox protein homolog 2
- Chromobox protein homolog 8
- Polyhomeotic-like protein 3
- E3 SUMO-protein ligase CBX4
- Polyhomeotic-like protein 2
Sequence:
MLVCYSVLACEILWDLPCSIMGSPLGHFTWDKYLKETCSVPAPVHCFKQSYTPPSNEFKISMKLEAQDPRNTTSTCIATVVGLTGARLRLRLDGSDNKNDFWRLVDSAEIQPIGNCEKNGGMLQPPLGFRLNASSWPMFLLKTLNGAEMAPIRIFHKEPPSPSHNFFKMGMKLEAVDRKNPHFICPATIGEVRGSEVLVTFDGWRGAFDYWCRFDSRDIFPVGWCSLTGDNLQPPGTKVVIPKNPYPASDVNTEKPSIHSSTKTVLEHQPGQRGRKPGKKRGRTPKTLISHPISAPSKTAEPLKFPKKRGPKPGSKRKPRTLLNPPPASPTTSTPEPDTSTVPQDAATIPSSAMQAPTVCIYLNKNGSTGPHLDKKKVQQLPDHFGPARASVVLQQAVQACIDCAYHQKTVFSFLKQGHGGEVISAVFDREQHTLNLPAVNSITYVLRFLEKLCHNLRSDNLFGNQPFTQTHLSLTAIEYSHSHDRYLPGETFVLGNSLARSLEPHSDSMDSASNPTNLVSTSQRHRPLLSSCGLPPSTASAVRRLCSRGVLKGSNERRDMESFWKLNRSPGSDRYLESRDASRLSGRDPSSWTVEDVMQFVREADPQLGPHADLFRKHEIDGKALLLLRSDMMMKYMGLKLGPALKLSYHIDRLKQGKF
Protein: Fumarate and nitrate reduction regulatory protein (P0A2T8)
Organism: Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)
Function: Global transcription factor that controls the expression of over 100 target genes in response to anoxia. It facilitates the adaptation to anaerobic growth conditions by regulating the expression of gene products that are involved in anaerobic energy metabolism. When the terminal electron acceptor, O(2), is no longer available, it represses the synthesis of enzymes involved in aerobic respiration and increases the synthesis of enzymes required for anaerobic respiration (By similarity).
Subcellular location: Cytoplasm {ECO:0000305}.
Interaction partners:
- Universal stress protein E
- Pyruvate formate lyase activating enzyme
- Methylated-DNA--protein-cysteine methyltransferase
- Transcriptional GntR family regulator for lct operon
Sequence:
MIPEKRIIRRIQSGGCAIHCQDCSISQLCIPFTLNEHELDQLDNIIERKKPIQKGQTLFKAGDELKSLYAIRSGTIKSYTITEQGDEQITGFHLAGDLVGFDAIGSGHHPSFAQALETSMVCEIPFETLDDLSGKMPNLRQQMMRLMSGEIKGDQDMILLLSKKNAEERLAAFIYNLSRRFAQRGFSPREFRLTMTRGDIGNYLGLTVETISRLLGRFQKSGMLAVKGKYITIENSDALAALAGHTRNVA
Protein: Glutaminyl-tRNA synthetase 1 (A0A0U1RQT0)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MAALDSLSLFTSLGLSEQKARETLKNSALSAQLREAATQAQQTLGSTIDKATGILLYGLASRLRDTRRLSFLVSYIASKKIHTEPQLSAALEYVRSHPLDPIDTVDFERECGVGVIVTPEQIEEAVEAAINRHRPQLLVERYHFNMGLLMGEARAVLKWADGKMIKNEVDMQVLHLLGPKLEADLEKKFKVAKARLEETDRRTAKDVVENGETADQTLSLMEQLRGEALKFHKPGENYKTPGYVVTPHTMNLLKQHLEITGGQANNGICFLRFDDTNPEKEEAKFFTAICDMVAWLGYTPYKVTYASDYFDQLYAWAVELIRRGLAYVCHQRGEELKGHNTL
Protein: ERAD-associated E3 ubiquitin-protein ligase hrd1 (EC 2.3.2.27) (RING-type E3 ubiquitin transferase hrd1) (O74757)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: E3 ubiquitin-protein ligase which accepts ubiquitin specifically from endoplasmic reticulum-associated E2 ligases, and transfers it to substrates promoting their degradation. Mediates the degradation of endoplasmic reticulum proteins (ERQC), also called ER-associated degradation (ERAD). Component of the hrd1 ubiquitin ligase complex, which is part of the ERAD-L and ERAD-M pathways responsible for the rapid degradation of soluble lumenal and membrane proteins with misfolded lumenal domains (ERAD-L), or ER-membrane proteins with misfolded transmembrane domains (ERAD-M) (By similarity). Together with ubc7, required for the degradation of the transcription factor sre1 precursor in the absence of its binding partner scp1.
Subcellular location: Endoplasmic reticulum membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}.
Interaction partners:
- Uncharacterized derlin-like protein C365.08c
- Protein OS-9 homolog
- Ubiquitin-conjugating enzyme E2-18 kDa
- Cell division cycle protein 48
- Uncharacterized derlin-like protein C1687.17c
- Putative ERAD-associated E3 ubiquitin-protein ligase component
- ERAD-associated E3 ubiquitin-protein ligase doa10
- Nuclear protein localization protein 4
- 3-hydroxy-3-methylglutaryl-coenzyme A reductase
- Ubiquitin fusion degradation protein 1
Sequence:
MKFILYVLASLVLFGLSVLLSLYSSANVYSATVMISQSPVHITIGLNVCLCLFFAIANALKTLLFGSLQTFELELLYEQFWITLTEIMLAITVFREAISISFFMLLSTLMFARVFHSICSFRTERLQIQLTDQRFHIFSRLTCAYFVLSILDASLIYLCFTSEHLGDKSTRMLFVCEFSVLLLNLTIEASKLCIYLYEARHLDQVWDEKSTYLFRLEVCRDGLRLLAYSLLFMYQFPYVSVPIYSIRQMYTCFYSLFRRIREHARFRQATRDMNAMYPTATEEQLTNSDRTCTICREEMFHPDHPPENTDEMEPLPRGLDMTPKRLPCGHILHFHCLRNWLERQQTCPICRRSVIGNQSSPTGIPASPNVRATQIATQVPNPQNTPTTTAVPGITNSSNQGDPQASTFNGVPNANSSGFAAHTQDLSSVIPRRIALRDGWTMLPIPGTRRIPTYSQSTSTTNPSATPTTGDPSNSTYGGPQTFPNSGNNPNFNRGIAGIVPPGWRLVSSNTQSLSTNSAMTSLYQNASSADNNLGSSLPNVVPLSRGLTQSNETSNTFPAASSNISSQLRELHTKIDELRETVSNFRADYNSIRTSLNQLEAASGINERIQTTSADSLLNSNGMSGTEGFENTQTSITTNDNQSSILTSSDQTSPFATDEDRQNSRNVQLETVDENF
Protein: PHO85 cyclin PHO80 (Aminoglycoside antibiotic sensitivity protein 3) (Phosphate system cyclin PHO80) (P20052)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Cyclin partner of the cyclin-dependent kinase (CDK) PHO85. Negatively regulates the expression of phosphate-starvation-responsive genes under phosphate-rich conditions. The PHO80-PHO85 cyclin-CDK holoenzyme phosphorylates and inactivates the transcription factor PHO4, by preventing its association with the transcription factor PHO2 and the nuclear import receptor PSE1, and by promoting association with the nuclear export receptor MSN5, excluding PHO4 from the nucleus. PHO80-PHO85 phosphorylates and inactivates protein kinase RIM15 by retaining it in the cytoplasm, antagonizing RIM15-induced entry into stationary phase. PHO80-PHO85 also phosphorylates and inactivates the calcineurin-responsive transcription factor CRZ1, linking PHO85 to calcium signaling.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:9853758}. Nucleus {ECO:0000269|PubMed:9853758}. Note=Localizes predominantly to the cytoplasm under phosphate-rich conditions and concentrates in the nucleus upon phosphate starvation.
Interaction partners:
- Phosphate system positive regulatory protein PHO81
- Phosphate system positive regulatory protein PHO4
- Cyclin-dependent protein kinase PHO85
- Cyclin-dependent kinase 1
- Inorganic phosphate transporter PHO84
- Serine/threonine-protein kinase RIM15
- 26S proteasome regulatory subunit RPN8
- PHO85 cyclin-5
- Repressible acid phosphatase
- Regulatory protein PHO2
Sequence:
MESTSGERSENIHEDQGIPKVILPADFNKCSRTDLVVLISRMLVSLIAINENSATKKSDDQITLTRYHSKIPPNISIFNYFIRLTKFSSLEHCVLMTSLYYIDLLQTVYPDFTLNSLTAHRFLLTATTVATKGLCDSFSTNAHYAKVGGVRCHELNILENDFLKRVNYRIIPRDHNITLCSIEQKQKKFVIDKNALGSLDLDSYSYVNRPKSGYNVLDKYYRRIVQLVGSFNASPDKSRKVDYVLPPNIDIVSESGSQTTQLKGSSSPNSHSSQKRYSEAKDAHIYNKRSKPD
Protein: Protein kinase, putative (EC 2.7.1.-) (Q384A9)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
- Atg6 BARA domain-containing protein
- phosphatidylinositol 3-kinase
- non-specific serine/threonine protein kinase
- Protein kinase, putative
- Autophagocytosis associated protein, putative
- Uncharacterized protein
- Autophagy-related protein 9
- CBS domain-containing protein
- Association with the SNF1 complex
- Uncharacterized protein
Sequence:
MGNQLAAATVVNVSDVTSSLELIAPLSCMHRNYFRSFRCSKEASAAVPSDTLRSLYSFSRGDNRDQSALHHRPSNRGGSTEVVLKVFVRTLYNEEEQKVVEFCYNHLLSIERRMAGAKPANMQNTGSCETAASNGSSHDSSNCGVATTPPPCNVLFYSCMEIQNDRFCMLQRPYVAFSLAERLATRPYWSTANRLFATYQLLQGTVQLHEVWGTVHGDLKVDNILVNTSGWLYITDICPFNPALLPANNPALFNYFYDTNESHICSLAPEKFVDHPTNVNTSNLNATVHTPGMDIFSLACVVVYIFTEEPLFRLSEVLELRSLQTQREREEMINSILQERGLAPNLCRMLSDMLCTNPNSRPTSRQLLERYTPTVFPPYFEYLYRDILPALLPRPPEHQVQLLWSRLDDIFAEVECRGSFNSGGGSGHNGEADDGEFPPLVPSSDAKKVTVLVLIPIILNAGLHLMASETCCRVVSIVQRILPHCTLEVQADVILPYMLRFLRTETLPVVARVLALRTLSTICHNIPFSTGEATVFDDLILPCVEDLVAKADTQNVTLLLEVAAQLPSLFLMARSFMEQQQALVTSNERQSTYGEQLNRLLERGWDALRTLYKHNHSAVVIAALQRSVDVVKFLGEERTQHDFIPFLTTAIASTIDVQRELYPQAILCHTNLQRPPLKTLRFFVEEALRRTDAIILRRAIESVSVVASSKLVDVSDVMSLAECVLPHILDKDKWVSLAARQLVEVVAQTYRMSDVCTRLPSTLIPLLRYKVPFSTLTSLPEELVNEISQRPSFSLRHRDERPTVRVVGGDSKLSRRFMNGSRSSDNSITERNVINGGAGGFVQCQSNYILQHGTTKRFPPNFPLRAAFFDVTFDPSVRAGTPSALDAAAVHDSSDATAAYAWGLTFKPTHREKKRLLLRQQTYTNRVDSNGDIVGGALFTSTTESTTGRRPWLLGPPTGSLSVQPSPALYPGVTWADKELKPIAAPYFTRRAHSGAIYSSATVGSGTLVTAGGKGEALLWSVTATGVNLSSRLNVGDASSKNTFLFVHFARGGVSPLLCIGGTDGTWQLCDIASNKVVQERKLDGSPLTAACALSEDVMLVSSALGGLFAMDYRAGREVWKSGSILPVEFGTISGVYPLCSECRAYGAAVTTMGGGVALFDLRFELLLQKHWLHGAPIQGSRSIDNPYAILCVSPDAACKPVHQLNEHPGLLLGTRSGMVYHMDLISGRSCVSLRPATPNNPTRAMLLQPRHRLLFTAGDDMQIRRWCLSNSALSSTVVFPPYNSYAYARRTSGSTMEVRPSSKSSNGQLAPTAAGATTAVSAPLVRPVVPQHHSDAILTLCGVSVSGGDETYLVSGSRDGQLTLWFNAE
Protein: Sterol regulatory element-binding protein 2 (Sterol regulatory element-binding transcription factor 2) (Q98SH5)
Organism: Gallus gallus (Chicken)
Subcellular location: Cytoplasmic vesicle, COPII-coated vesicle membrane {ECO:0000256|ARBA:ARBA00004557}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004557}. Endoplasmic reticulum membrane {ECO:0000256|ARBA:ARBA00004477}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004477}. Golgi apparatus membrane {ECO:0000256|ARBA:ARBA00004653}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004653}. Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
APTFSSAPQTRIIQQPVLYQNAATSFQVLQPQVQSLVTSPQVQPVTIQQQVQAVPAPRVLTQAAGGTIQALAPATVQTVAAPQVQQVPVLVQPQIIKTDSLVLTTLKTDGNPVMAAVQNPALTALTTPIQTTAPQTLVGSNGTILTTMPVMMGQEKVPIKQVPGGVKQPDPPKEGERRTTHNIIEKRYRSSINDKIIELKDLIMGTDAKMHKSGVLRKAIDYIKYLQQGNHKLRQENMVLKLANQKNKLLKGIDLSSLVDNDADLKIDDFNQNVLLMSPPASDSGSQAGFSPYSIDSEPGSPLLDDAKVKDEPDSPPVALGMVDRSRILLCALTFLCLSFNPLTSLLDARGSPESDSLTRHGSGRNMLTIESDTGGWFGWMMPTLILXLVNGVXVL