wanglab/gogpt-training-data huggingface dataset:
Protein: Acetylcholine receptor subunit alpha (P02708)
Organism: Homo sapiens (Human)
Function: Upon acetylcholine binding, the AChR responds by an extensive change in conformation that affects all subunits and leads to opening of an ion-conducting channel across the plasma membrane.
Subcellular location: Postsynaptic cell membrane {ECO:0000305|PubMed:27375219}; Multi-pass membrane protein {ECO:0000255}. Cell membrane {ECO:0000269|PubMed:27375219}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
- Acetylcholine receptor subunit delta
- Acetylcholine receptor subunit epsilon
- Acetylcholine receptor subunit gamma
- Acetylcholine receptor subunit beta
- 43 kDa receptor-associated protein of the synapse
- Neuronal acetylcholine receptor subunit alpha-3
- Neuronal acetylcholine receptor subunit alpha-9
- Neuronal acetylcholine receptor subunit alpha-4
- Neuronal acetylcholine receptor subunit beta-4
- Autoimmune regulator
Sequence:
MEPWPLLLLFSLCSAGLVLGSEHETRLVAKLFKDYSSVVRPVEDHRQVVEVTVGLQLIQLINVDEVNQIVTTNVRLKQQWVDYNLKWNPDDYGGVKKIHIPSEKIWRPDLVLYNNADGDFAIVKFTKVLLQYTGHITWTPPAIFKSYCEIIVTHFPFDEQNCSMKLGTWTYDGSVVAINPESDQPDLSNFMESGEWVIKESRGWKHSVTYSCCPDTPYLDITYHFVMQRLPLYFIVNVIIPCLLFSFLTGLVFYLPTDSGEKMTLSISVLLSLTVFLLVIVELIPSTSSAVPLIGKYMLFTMVFVIASIIITVIVINTHHRSPSTHVMPNWVRKVFIDTIPNIMFFSTMKRPSREKQDKKIFTEDIDISDISGKPGPPPMGFHSPLIKHPEVKSAIEGIKYIAETMKSDQESNNAAAEWKYVAMVMDHILLGVFMLVCIIGTLAVFAGRLIELNQQG
Protein: NADPH--cytochrome P450 reductase (CPR) (P450R) (EC 1.6.2.4) (P16603)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: This enzyme is required for electron transfer from NADP to cytochrome P450 in microsomes. It can also provide electron transfer to heme oxygenase and cytochrome B5. Involved in ergosterol biosynthesis. Has NADPH-dependent ferrireductase activity on the plasma membrane.
Subcellular location: Endoplasmic reticulum membrane {ECO:0000255|HAMAP-Rule:MF_03212, ECO:0000269|PubMed:14562095, ECO:0000269|PubMed:9468503}; Single-pass membrane protein {ECO:0000255|HAMAP-Rule:MF_03212, ECO:0000305|PubMed:11485306, ECO:0000305|PubMed:9468503}; Cytoplasmic side {ECO:0000255|HAMAP-Rule:MF_03212, ECO:0000305|PubMed:11485306, ECO:0000305|PubMed:9468503}. Mitochondrion outer membrane {ECO:0000255|HAMAP-Rule:MF_03212, ECO:0000269|PubMed:14576278, ECO:0000269|PubMed:16407407}; Single-pass membrane protein {ECO:0000255|HAMAP-Rule:MF_03212, ECO:0000305|PubMed:11485306, ECO:0000305|PubMed:9468503}; Cytoplasmic side {ECO:0000255|HAMAP-Rule:MF_03212, ECO:0000305|PubMed:11485306, ECO:0000305|PubMed:9468503}. Cell membrane {ECO:0000255|HAMAP-Rule:MF_03212, ECO:0000269|PubMed:9368374}; Single-pass membrane protein {ECO:0000255|HAMAP-Rule:MF_03212, ECO:0000305|PubMed:11485306, ECO:0000305|PubMed:9468503}; Cytoplasmic side {ECO:0000255|HAMAP-Rule:MF_03212, ECO:0000305|PubMed:11485306, ECO:0000305|PubMed:9468503}.
Interaction partners:
- Sulfite reductase subunit beta
- Cytochrome b5
- Lanosterol 14-alpha demethylase CYP51
- Calcium-transporting ATPase 2
- Adrenodoxin homolog, mitochondrial
- Delta
- Adenylyl-sulfate kinase
- ATP-dependent molecular chaperone HSP82
- ATP-dependent molecular chaperone HSC82
- Heme-binding protein HMX1
Sequence:
MPFGIDNTDFTVLAGLVLAVLLYVKRNSIKELLMSDDGDITAVSSGNRDIAQVVTENNKNYLVLYASQTGTAEDYAKKFSKELVAKFNLNVMCADVENYDFESLNDVPVIVSIFISTYGEGDFPDGAVNFEDFICNAEAGALSNLRYNMFGLGNSTYEFFNGAAKKAEKHLSAAGAIRLGKLGEADDGAGTTDEDYMAWKDSILEVLKDELHLDEQEAKFTSQFQYTVLNEITDSMSLGEPSAHYLPSHQLNRNADGIQLGPFDLSQPYIAPIVKSRELFSSNDRNCIHSEFDLSGSNIKYSTGDHLAVWPSNPLEKVEQFLSIFNLDPETIFDLKPLDPTVKVPFPTPTTIGAAIKHYLEITGPVSRQLFSSLIQFAPNADVKEKLTLLSKDKDQFAVEITSKYFNIADALKYLSDGAKWDTVPMQFLVESVPQMTPRYYSISSSSLSEKQTVHVTSIVENFPNPELPDAPPVVGVTTNLLRNIQLAQNNVNIAETNLPVHYDLNGPRKLFANYKLPVHVRRSNFRLPSNPSTPVIMIGPGTGVAPFRGFIRERVAFLESQKKGGNNVSLGKHILFYGSRNTDDFLYQDEWPEYAKKLDGSFEMVVAHSRLPNTKKVYVQDKLKDYEDQVFEMINNGAFIYVCGDAKGMAKGVSTALVGILSRGKSITTDEATELIKMLKTSGRYQEDVW
Protein: ER lumen protein-retaining receptor 1 (KDEL endoplasmic reticulum protein retention receptor 1) (KDEL receptor 1) (Putative MAPK-activating protein PM23) (P24390)
Organism: Homo sapiens (Human)
Function: Receptor for the C-terminal sequence motif K-D-E-L that is present on endoplasmic reticulum resident proteins and that mediates their recycling from the Golgi back to the endoplasmic reticulum.
Subcellular location: Golgi apparatus membrane {ECO:0000269|PubMed:18086916, ECO:0000269|PubMed:2172835, ECO:0000269|PubMed:30846601, ECO:0000269|PubMed:8392934}; Multi-pass membrane protein {ECO:0000250|UniProtKB:P33946}. Cytoplasmic vesicle, COPI-coated vesicle membrane {ECO:0000269|PubMed:18086916}; Multi-pass membrane protein {ECO:0000250|UniProtKB:P33946}. Endoplasmic reticulum membrane {ECO:0000269|PubMed:18086916, ECO:0000269|PubMed:30846601, ECO:0000269|PubMed:8392934}; Multi-pass membrane protein {ECO:0000250|UniProtKB:P33946}. Endoplasmic reticulum-Golgi intermediate compartment membrane {ECO:0000250|UniProtKB:P33946}; Multi-pass membrane protein {ECO:0000250|UniProtKB:P33946}. Note=Localized in the Golgi in the absence of bound proteins with the sequence motif K-D-E-L. Trafficks back to the endoplasmic reticulum together with cargo proteins containing the sequence motif K-D-E-L. {ECO:0000269|PubMed:18086916, ECO:0000269|PubMed:30846601, ECO:0000269|PubMed:8392934}.
Interaction partners:
- Coatomer subunit beta
- ER lumen protein-retaining receptor 2
- ER lumen protein-retaining receptor 3
- Surfeit locus protein 4
- Stromal cell-derived factor 2-like protein 1
- Stromal cell-derived factor 2
- Reticulocalbin-1
- ADP-ribosylation factor GTPase-activating protein 1
- ADP-ribosylation factor 1
- Reticulocalbin-2
Sequence:
MNLFRFLGDLSHLLAIILLLLKIWKSRSCAGISGKSQVLFAVVFTARYLDLFTNYISLYNTCMKVVYIACSFTTVWLIYSKFKATYDGNHDTFRVEFLVVPTAILAFLVNHDFTPLEILWTFSIYLESVAILPQLFMVSKTGEAETITSHYLFALGVYRTLYLFNWIWRYHFEGFFDLIAIVAGLVQTVLYCDFFYLYITKVLKGKKLSLPA
Protein: Dolichyl-phosphate-mannose--protein mannosyltransferase 6 (Protein mannosyltransferase 6) (EC 2.4.1.109) (Q5A688)
Organism: Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast)
Function: Protein mannosyltransferase (PMT) involved in hyphal morphogenesis and drug sensitivity. Transfers mannose from Dol-P-mannose to Ser or Thr residues on proteins. PMT1, PMT2 and PMT4 account for most of the protein-O-glycosylation activity, while PMT5 and PMT6 may specifically modulate a much narrower spectrum of target proteins. Required for biofilm formation and virulence.
Subcellular location: Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:P33775}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
- Dolichyl-phosphate-mannose--protein mannosyltransferase 5
Sequence:
MATGYSTGVSPFDLDENNHNDSIHHRHQNHHSQSHDSSGERDDTEIEDIIQKTSKLNINTSTSTKIKNFFFQSSNRHDSSNSPPLREVFIKTINPLILTAISSFVRLYRIDVANSVVWDEAHFGKFGSQYLKRQFYFDVHPPLGKLLIGLSGYLADYDGNFDFESSNVYPDNVNYVFMRIFNCFFGILVTPLAYKTAVILGYNQFTCWLIAFMVIFEQLSLTLSKFILLDSMLLFFTVLTMYCLVKVHTLAIARVGSNSKTPLTKLEIKWYILTGISIGCVCSVKWVGLFVTALVGFYTIVDLWIKFYQTFAIDKKSPKKMSVVNYLIHWVVRIFTLIIIPMTIYVATFKVHFMVLNHTGPDDGTLSTLLQGSLIGNDLQSGPRSVAFGSLVTIRSQGLSPNLIHSHPHNYPQGSQEQQVTTYGFKDDNNEFLFEFGVDAGLRNQHATLENENSTRNGGNDDDYYHVIIHDGDTVRINHKNTGSYLRANAVGAPITSSSYEVSCFGDVESNDWADEWVIEIQSQDQSPDPMFQDEDPSEIHSVSTSFRLKHKQLGCYLATTGKSYPAWGYQQGEVVCKYSVFSRDKNTWWNIEKHVNNKLPLPATEYVPPKPKFWKEFILLNYAMMASNNALIPDPDRFDKLSSEWWEWPILNTGLRMNSWGDADIKYFLLGNPLITWISTIALIVCPLYLLVVGIKYQRQWILLSATDTSNANPANSQSLSLLAARALLPLAGWVLHYVPFILMGRVKYLHHYVPALYFAIFVAGFIVDAILNLDFSYHNNKFQYIFKVVIYSTLYLVICISFWYFKDLSFGMEGSSVDYRHLRLLGSWMI
Protein: Protein DDI1 homolog 1 (EC 3.4.23.-) (Q8WTU0)
Organism: Homo sapiens (Human)
Function: Probable aspartic protease (Probable). Seems to act as a proteasomal shuttle which links the proteasome and replication fork proteins like RTF2 (Probable). Required, with DDI2, for cellular survival following replication stress. Together or redudantly with DDI2, removes RTF2 from stalled forks to allow cell cycle progression after replication stress and maintains genome integrity.
Interaction partners:
- Regulatory solute carrier protein family 1 member 1
- Proteasomal ubiquitin receptor ADRM1
- Nuclear receptor-interacting protein 3
- Ubiquilin-1
- 26S proteasome non-ATPase regulatory subunit 4
- Ubiquilin-2
- Beta-alanine-activating enzyme
- C-C motif chemokine 28
Sequence:
MLITVYCVRRDLSEVTFSLQVSPDFELRNFKVLCEAESRVPVEEIQIIHMERLLIEDHCSLGSYGLKDGDIVVLLQKDNVGPRAPGRAPNQPRVDFSGIAVPGTSSSRPQHPGQQQQRTPAAQRSQGLASGEKVAGLQGLGSPALIRSMLLSNPHDLSLLKERNPPLAEALLSGSLETFSQVLMEQQREKALREQERLRLYTADPLDREAQAKIEEEIRQQNIEENMNIAIEEAPESFGQVTMLYINCKVNGHPLKAFVDSGAQMTIMSQACAERCNIMRLVDRRWAGVAKGVGTQRIIGRVHLAQIQIEGDFLQCSFSILEDQPMDMLLGLDMLRRHQCSIDLKKNVLVIGTTGTQTYFLPEGELPLCSRMVSGQDESSDKEITHSVMDSGRKEH
Protein: Kunitz-type protease inhibitor 1a precursor (Serine protease inhibitor, Kunitz type 1 b) (Spint1a protein) (Q7T363)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004370}.
Interaction partners:
Sequence:
MTLAQLRLFGTAVFLLLFLHQSPSAAQEEEKLCKDKFSVGKEDFVLNTDESVKEGATFLGSPQVSKPEDCVMACCNDPNCNLALMEHREDPKSINTCFIINCLYKQKKVCHFVRKKGFTNYLRKSVFSDYLEQKATDVEDRPPRARAGQDRVVQPNEDVTLNGIESSDDKKIVKYEWEQVVGDPSAVMTKGHFADSVTVSNLSPGMYKFRLTVSDEAGQTGSAEVSILVLTREQSLHHCLVPKKEGPCRGSFPRWHYNAATEKCEEFKFGGCVPNRNNYLALNECQSACNKVSVSNIGSPAPHPSGRIGPIDAVEQCDRPCSPEHFTCDNKCCIGKDLVCDKEKQCSDGSDEKECDKWDYDLVKLRGISPDVSKARCVKPPVTGTCPGSQTKWYYNPNKRLCYRFNYGGCEGNQNRFETEAGCMTFCSGVTENDKFPEESQFDKQEGKSNNTVAIVMVIILAFAIAILLVIIIAYCLVKGRKKSRNKHQQLAVNGGHIYRYEDSEKLVYNSTTKPI
Protein: Small ribosomal subunit protein uS4A (40S ribosomal protein S9-A) (RP21) (S13) (YP28) (YS11) (O13516)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Component of the ribosome, a large ribonucleoprotein complex responsible for the synthesis of proteins in the cell. The small ribosomal subunit (SSU) binds messenger RNAs (mRNAs) and translates the encoded message by selecting cognate aminoacyl-transfer RNA (tRNA) molecules. The large subunit (LSU) contains the ribosomal catalytic site termed the peptidyl transferase center (PTC), which catalyzes the formation of peptide bonds, thereby polymerizing the amino acids delivered by tRNAs into a polypeptide chain. The nascent polypeptides leave the ribosome through a tunnel in the LSU and interact with protein factors that function in enzymatic processing, targeting, and the membrane insertion of nascent chains at the exit of the ribosomal tunnel. uS4 is involved in nucleolar processing of pre-18S ribosomal RNA and ribosome assembly.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:22096102}. Nucleus, nucleolus {ECO:0000269|PubMed:15590835}.
Interaction partners:
- Small ribosomal subunit protein eS1A
- Small ribosomal subunit protein eS4A
- Small ribosomal subunit protein uS11B
- Small ribosomal subunit protein eS10A
- Small ribosomal subunit protein uS14B
- Small ribosomal subunit protein eS27A
- Small ribosomal subunit protein uS5
- Serine/threonine-protein kinase RIO2
- Small ribosomal subunit protein uS2A
- Small ribosomal subunit protein uS3
Sequence:
MPRAPRTYSKTYSTPKRPYESSRLDAELKLAGEFGLKNKKEIYRISFQLSKIRRAARDLLTRDEKDPKRLFEGNALIRRLVRVGVLSEDKKKLDYVLALKVEDFLERRLQTQVYKLGLAKSVHHARVLITQRHIAVGKQIVNIPSFMVRLDSEKHIDFAPTSPFGGARPGRVARRNAARKAEASGEAADEADEADEE
Protein: Mannosyl-oligosaccharide glucosidase (EC 3.2.1.106) (Glucosidase I) (A0A3B3IRK6)
Organism: Homo sapiens (Human)
Subcellular location: Endoplasmic reticulum membrane {ECO:0000256|ARBA:ARBA00004648, ECO:0000256|RuleBase:RU368089}; Single-pass type II membrane protein {ECO:0000256|ARBA:ARBA00004648, ECO:0000256|RuleBase:RU368089}.
Interaction partners:
Sequence:
XRDGRGGGPRSTAGGVALAVVVLSLALGMSGRWVLAWYRARRAVTLHSAPPVLPADSSSPAVAPDLFWGTYRPHVYFGMKTRSPKPLLTDGKEVLLPEVGAKGQLKFISGHTSELGDFRFTLLPPTSPGDTAPKYGSYNVFWTSNPGLPLLTEMVKSRLNSWFQHRPPGAPPERYLGLPGSLKWEDRGPSGQGQGQFLIQQVTLKIPISIEFVFESGSAQAGGNQALPRLAGSLLTQALESHAEGFRERFEKTFQLKEKGLSSGEQVLGQAALSGLLGGIGYFYGQGLVLPDIGVEGSEQKVDPALFPPVPLFTAVPSRSFFPRGFLWDEGFHQLVVQRWDPSLTREALGHWLGLLNADGWIGREQILGDEARARVPPEFLVQRAVHANPPTLLLPVAHMLEVGDPDDLAFLRKALPRLHAWFSWLHQSQAGPLPLSYRWRGRDPALPTLLNPKTLPSGLDDYPRASHPSVTERHLDLRCWVALGARVLTRLAEHLGEAEVAAELGPLAASLEAAESLDELHWAPELGVFADFGNHTKAVQLKPRPPQGLVRVVGRPQPQLQYVDALGYVSLFPLLLRLLDPTSSRLGPLLDILADSRHLWSPFGLRSLAASSSFYGQRNSEHDPPYWRGAVWLNVNYLALGALHHYGHLEGPHQARAAKLHGELRANVVGNVWRQYQATGFLWEQYSDRDGRGMGCRPFHGWTSLVLLAMAEDY
Protein: NADP(+)-dependent glutamate dehydrogenase (NADP-GDH) (EC 1.4.1.4) (A3MWK6)
Organism: Pyrobaculum calidifontis (strain DSM 21063 / JCM 11548 / VA1)
Function: Catalyzes the reversible oxidative deamination of L-glutamate to 2-oxoglutarate and ammonia, thereby playing a key role at the intersection of the carbon and nitrogen metabolic pathways. Shows a high preference for NADP(+)/NADPH as the acceptor/donor over NAD(+)/NADH. May function in vivo in the synthetic direction. Also catalyzes at very low rates the oxidative deamination of L-2-aminobutyrate, and the reductive amination of 2-oxovalerate and 2-oxobutyrate.
Interaction partners:
- Sulfide dehydrogenase
- isocitrate dehydrogenase
- L-glutamine synthetase
- Archaeal glutamate synthase
- Aminotransferase
- Aminotransferase
- Carbamate kinase
- Citrate synthase
- Citrate synthase
- Phosphoribosylformylglycinamidine synthase subunit PurQ
Sequence:
MSQNGQFLEYTLQVIRRGVEMGGFPEDFYKLLSRPKRIIQVSIPVKMDNGSYEVFEGYRVQHNDALGPFKGGIRFHPEVTLADDIALAMLMTLKNSLAGLPYGGAKGAVRVDPRRLSRRELEELARGYARAVAPLIGEQLDIPAPDVGTDSQVMAWMVDEYSKLAGRNAPAVFTSKPPELWGNPVREYSTGFGVAVAAREVAKRLWGGIEGKTVAVHGAGNTGAWAAYWLEKMGAKVVAISDTRGTVVNKAGIPGEQILKVYMEKKRDKSATVLALEGEKIADSNASLYQDVDILVPAAIENVVREDNVGLVRARLVVEGANGPTTPGAERRLYERGVVVVPDILANAGGVIMSYLEWVENLQWLFWDEEETRRRLEAIMSNNVARVYARWEKEKSWTMRDAAVVTALERIYNAMKTRGWI
Protein: Serine/threonine-protein phosphatase 4 regulatory subunit 4 (Q8C0Y0)
Organism: Mus musculus (Mouse)
Function: Putative regulatory subunit of serine/threonine-protein phosphatase 4.
Subcellular location: Cytoplasm.
Interaction partners:
- Serine/threonine-protein phosphatase 4 catalytic subunit
- Serine/threonine-protein phosphatase 4 regulatory subunit 2
- Serine/threonine-protein phosphatase 4 regulatory subunit 1
- Serine/threonine-protein phosphatase 2A activator
Sequence:
MHPPPPDAGVAMDFGQNSLFGYMEDLQELTIIERPVRRSLKTPEEIERLTVDEDLSDIDRAVYLLSAGQDVQGASVIANLPFLMRQNPTETLRRVLPKVREVLHVASVEMQLTAAVSFLTILQEESMSVHTCAHSFLQVILLHLEHRDTGVSNAWLETLLSAVELLPKETLRHEILNPLVSKAQLSQTVQSRLVSCKILGKITNKFDAHSIKREILPLVKSLCQDVEYEVRSCMCRQLENIAQGIGAELTKNVVLPELIELSRDESGSVRLAAFETLVNMLDMFDTDDRSQTILPLVKSFCEKSFKADESILISLSFHLGKLCHGLYGIFTPDQHLRFLEFYKKLCTLGLQQENGHNESQIPSQIVEQEKKYTSVRKNCAYNFPAMIVFVDPKNFHMELYSTFFCLCHDPEVPVRHTIAICFYEVSKLLNSGVHLIHKELITLLQDESLEVLDALINHLPEILELMSTGGENSVQENKFSSVPDLIPALTAAEQRAAASLKWRTHEKLLQKYTCLPHIISSDQIYYRFLQRMFTIMMTNNVLPVQRAAARTLCIFLRYNRKQEQRHEVIQKLIEQLGQGKSYWNRLRFLDTCEFIIEIFSRSFFCKYFFLPVIELTHDPVANVRMKLCYLLPKVKSALKIPADMHLLQQLEMCVRKLLCQEKDKDVLAIVKKTVLELDRMEMSMDMFQKKNYEKDLLDQEKEREELLFLEMEQLEKEKHQSDGRLASDKSFEKKRRDSRTSTQSLSKNLPISVPGPSSSTASTSKEIKKSKLTRSQSFNNQAFHAKYGTLDKCASKSSTLAHTSSVSGLVRTAMLSLTDDSFRTRNASSVPASFSPNPVMPSTSRGPGNTADPKSSGSKDAQPRKATLKSRKSNP
Protein: Eukaryotic translation initiation factor 3 subunit E (eIF3e) (Eukaryotic translation initiation factor 3 subunit 6) (O77410)
Organism: Drosophila melanogaster (Fruit fly)
Function: Component of the eukaryotic translation initiation factor 3 (eIF-3) complex, which is involved in protein synthesis of a specialized repertoire of mRNAs and, together with other initiation factors, stimulates binding of mRNA and methionyl-tRNAi to the 40S ribosome. The eIF-3 complex specifically targets and initiates translation of a subset of mRNAs involved in cell proliferation. In addition to its role in the eIF-3 complex, also functions in protein ubiquitination and degradation. During mitosis required for regulating mitotic microtubule growth and kinetochore formation, and consequently is required for satisfying the spindle assembly checkpoint (SAC) during metaphase to prevent delays in mitotic progression. This is likely by promoting the ubiquitination and degradation of Klp67A, a kinesin-like protein that suppresses microtubule polymerization at plus ends. Acts in the COP9 signalosome (CSN) mediated regulation of cullin neddylation by promoting Cul1 and Cul3 neddylation and negatively regulating the CSN complex subunit CSN5.
Subcellular location: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_03004, ECO:0000269|PubMed:28505193}. Microsome {ECO:0000269|PubMed:10375641}. Endoplasmic reticulum {ECO:0000269|PubMed:10375641}. Note=Uniformly distributed in interphase and mitotic cells. {ECO:0000269|PubMed:28505193}.
Interaction partners:
- Eukaryotic translation initiation factor 3 subunit L
- Eukaryotic translation initiation factor 3 subunit I
- Eukaryotic translation initiation factor 3 subunit C
- Eukaryotic translation initiation factor 3 subunit M
- Eukaryotic translation initiation factor 3 subunit A
- Eukaryotic translation initiation factor 3 subunit B
- Eukaryotic translation initiation factor 3 subunit K
- Eukaryotic translation initiation factor 3 subunit H
- Eukaryotic translation initiation factor 3 subunit G-1
- Eukaryotic translation initiation factor 3 subunit D-1
Sequence:
MANFDLTRINCQFLDRHLTFPLLEFLCGKEIYNQQELLEYILETVNKTNMIDYTMDTRKRLNLSQEMPEELVQRKAEVLATLKQLQNEVAPIMKATDILKNGESMKDSKTFVNALQKDYNFKVEHLESAYKLAKYLYECGNYQESTSYLYFCLIVMSPNDKNYLNVLWGKLAAEILTLNWNTALEDLTRLRDYIDNANFSTIQALQQRTWLIHWSVLVFFNHPKGRDLIIEMFLYKPLYLNAIQTMCPHIMRYLATAVVINRTRRNALKDLIKVIQQESYTYRDPITEFLECLYVNFDFEGARLKLHECQTVILNDFFIVACLNEFVEDARLMIFETFCRIHQCITISMLADKLNMKPNEAECWIVNLIRNARLNAKIDSKLGHVVMGTQPLSPYQQLVEKIDSLSMRSEHLAGLIERKSKQKQNQESADSWKYY
Protein: Potassium/sodium hyperpolarization-activated cyclic nucleotide-gated channel 1 (Brain cyclic nucleotide-gated channel 1) (BCNG-1) (Hyperpolarization-activated cation channel 2) (HAC-2) (O88704)
Organism: Mus musculus (Mouse)
Function: Hyperpolarization-activated ion channel exhibiting weak selectivity for potassium over sodium ions. Contributes to the native pacemaker currents in heart (If) and in neurons (Ih). May mediate responses to sour stimuli.
Subcellular location: Cell membrane {ECO:0000269|PubMed:11459060, ECO:0000269|PubMed:22006928, ECO:0000269|PubMed:9630217}; Multi-pass membrane protein {ECO:0000269|PubMed:22006928}.
Interaction partners:
- Potassium/sodium hyperpolarization-activated cyclic nucleotide-gated channel 2
- Potassium/sodium hyperpolarization-activated cyclic nucleotide-gated channel 3
- PEX5-related protein
- Potassium/sodium hyperpolarization-activated cyclic nucleotide-gated channel 4
Sequence:
MEGGGKPNSASNSRDDGNSVFPSKAPATGPVAADKRLGTPPGGGAAGKEHGNSVCFKVDGGGGEEPAGSFEDAEGPRRQYGFMQRQFTSMLQPGVNKFSLRMFGSQKAVEKEQERVKTAGFWIIHPYSDFRFYWDLIMLIMMVGNLVIIPVGITFFTEQTTTPWIIFNVASDTVFLLDLIMNFRTGTVNEDSSEIILDPKVIKMNYLKSWFVVDFISSIPVDYIFLIVEKGMDSEVYKTARALRIVRFTKILSLLRLLRLSRLIRYIHQWEEIFHMTYDLASAVVRIFNLIGMMLLLCHWDGCLQFLVPLLQDFPPDCWVSLNEMVNDSWGKQYSYALFKAMSHMLCIGYGAQAPVSMSDLWITMLSMIVGATCYAMFVGHATALIQSLDSSRRQYQEKYKQVEQYMSFHKLPADMRQKIHDYYEHRYQGKIFDEENILSELNDPLREEIVNFNCRKLVATMPLFANADPNFVTAMLSKLRFEVFQPGDYIIREGAVGKKMYFIQHGVAGVITKSSKEMKLTDGSYFGEICLLTKGRRTASVRADTYCRLYSLSVDNFNEVLEEYPMMRRAFETVAIDRLDRIGKKNSILLQKFQKDLNTGVFNNQENEILKQIVKHDREMVQAIPPINYPQMTALNCTSSTTTPTSRMRTQSPPVYTATSLSHSNLHSPSPSTQTPQPSAILSPCSYTTAVCSPPIQSPLATRTFHYASPTASQLSLMQQPQQQLPQSQVQQTQTQTQQQQQQQQQQQQQQQQQQQQQQQQQQQQQQQQQQQQQPQTPGSSTPKNEVHKSTQALHNTNLTKEVRPLSASQPSLPHEVSTLISRPHPTVGESLASIPQPVAAVHSTGLQAGSRSTVPQRVTLFRQMSSGAIPPNRGVPPAPPPPAAVQRESPSVLNTDPDAEKPRFASNL
Protein: Tumor necrosis factor receptor superfamily member 25 (Apo-3) (Apoptosis-inducing receptor AIR) (Apoptosis-mediating receptor DR3) (Apoptosis-mediating receptor TRAMP) (Death receptor 3) (Lymphocyte-associated receptor of death) (LARD) (Protein WSL) (Protein WSL-1) (Q93038)
Organism: Homo sapiens (Human)
Function: Receptor for TNFSF12/APO3L/TWEAK. Interacts directly with the adapter TRADD. Mediates activation of NF-kappa-B and induces apoptosis. May play a role in regulating lymphocyte homeostasis.
Subcellular location: [Isoform 1]: Cell membrane; Single-pass type I membrane protein.; SUBCELLULAR LOCATION: [Isoform 2]: Cell membrane; Single-pass type I membrane protein.; SUBCELLULAR LOCATION: [Isoform 9]: Cell membrane; Single-pass type I membrane protein.; SUBCELLULAR LOCATION: [Isoform 11]: Cell membrane; Single-pass type I membrane protein.; SUBCELLULAR LOCATION: [Isoform 3]: Secreted.; SUBCELLULAR LOCATION: [Isoform 4]: Secreted.; SUBCELLULAR LOCATION: [Isoform 5]: Secreted.; SUBCELLULAR LOCATION: [Isoform 6]: Secreted.; SUBCELLULAR LOCATION: [Isoform 7]: Secreted.; SUBCELLULAR LOCATION: [Isoform 8]: Secreted.; SUBCELLULAR LOCATION: [Isoform 10]: Secreted.; SUBCELLULAR LOCATION: [Isoform 12]: Secreted.
Interaction partners:
- Torsin-1A
- Tumor necrosis factor ligand superfamily member 15
- Tumor necrosis factor receptor superfamily member 10A
- Tumor necrosis factor receptor type 1-associated DEATH domain protein
- Tumor necrosis factor ligand superfamily member 12
- Tumor necrosis factor ligand superfamily member 6
- Tumor necrosis factor
- Tumor necrosis factor ligand superfamily member 10
- HLA class II histocompatibility antigen DQ alpha chain
- FAS-associated death domain protein
Sequence:
MEQRPRGCAAVAAALLLVLLGARAQGGTRSPRCDCAGDFHKKIGLFCCRGCPAGHYLKAPCTEPCGNSTCLVCPQDTFLAWENHHNSECARCQACDEQASQVALENCSAVADTRCGCKPGWFVECQVSQCVSSSPFYCQPCLDCGALHRHTRLLCSRRDTDCGTCLPGFYEHGDGCVSCPTSTLGSCPERCAAVCGWRQMFWVQVLLAGLVVPLLLGATLTYTYRHCWPHKPLVTADEAGMEALTPPPATHLSPLDSAHTLLAPPDSSEKICTVQLVGNSWTPGYPETQEALCPQVTWSWDQLPSRALGPAAAPTLSPESPAGSPAMMLQPGPQLYDVMDAVPARRWKEFVRTLGLREAEIEAVEVEIGRFRDQQYEMLKRWRQQQPAGLGAVYAALERMGLDGCVEDLRSRLQRGP