wanglab/gogpt-training-data huggingface dataset:
Protein: RNA binding protein with serine rich domain 1 (H3BTY0)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MDLSGVKKKSLLGVKENNKKSSTRAPSPTKRKDRSDEKSKDRSKDKGATKESSEKDRGRDKTRKRRSASSGSSSTRSRSSSTSSSGSSTSTGSSSGSSSSSASSRSGSSSTSRSSSSSSSSGSPSPSRRRHDNRRRSRSKSKPPKRDEKE
Protein: Methionine--tRNA ligase, mitochondrial (EC 6.1.1.10) (Methionyl-tRNA synthetase 2) (Mitochondrial methionyl-tRNA synthetase) (MtMetRS) (Q96GW9)
Organism: Homo sapiens (Human)
Subcellular location: Mitochondrion matrix {ECO:0000305}.
Interaction partners:
- Isoleucine--tRNA ligase, cytoplasmic
- Leucine--tRNA ligase, mitochondrial
- Isoleucine--tRNA ligase, mitochondrial
- Bifunctional glutamate/proline--tRNA ligase
- Leucine--tRNA ligase, cytoplasmic
- Lysine--tRNA ligase
- Glutamine--tRNA ligase
- Nondiscriminating glutamyl-tRNA synthetase EARS2, mitochondrial
- Tyrosine--tRNA ligase, cytoplasmic
- Probable arginine--tRNA ligase, mitochondrial
Sequence:
MLRTSVLRLLGRTGASRLSLLEDFGPRYYSSGSLSAGDDACDVRAYFTTPIFYVNAAPHIGHLYSALLADALCRHRRLRGPSTAATRFSTGTDEHGLKIQQAAATAGLAPTELCDRVSEQFQQLFQEAGISCTDFIRTTEARHRVAVQHFWGVLKSRGLLYKGVYEGWYCASDECFLPEAKVTQQPGPSGDSFPVSLESGHPVSWTKEENYIFRLSQFRKPLQRWLRGNPQAITPEPFHHVVLQWLDEELPDLSVSRRSSHLHWGIPVPGDDSQTIYVWLDALVNYLTVIGYPNAEFKSWWPATSHIIGKDILKFHAIYWPAFLLGAGMSPPQRICVHSHWTVCGQKMSKSLGNVVDPRTCLNRYTVDGFRYFLLRQGVPNWDCDYYDEKVVKLLNSELADALGGLLNRCTAKRINPSETYPAFCTTCFPSEPGLVGPSVRAQAEDYALVSAVATLPKQVADHYDNFRIYKALEAVSSCVRQTNGFVQRHAPWKLNWESPVDAPWLGTVLHVALECLRVFGTLLQPVTPSLADKLLSRLGVSASERSLGELYFLPRFYGHPCPFEGRRLGPETGLLFPRLDQSRTWLVKAHRT
Protein: Single-minded homolog 1-A (Q98SJ5)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Function: Transcriptional factor that may have pleiotropic effects during embryogenesis and in the adult.
Subcellular location: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00632, ECO:0000255|PROSITE-ProRule:PRU00981}.
Interaction partners:
- Aryl hydrocarbon receptor nuclear translocator 2
- Homeobox protein orthopedia B
- Orthopedia homeobox a
- Oxytocin
- Melanocortin receptor 4
- Iroquois homeobox 3b.
- Pro-thyrotropin-releasing hormone
- Aryl hydrocarbon receptor nuclear translocator.
- Hepatocyte nuclear factor 1-beta-A
Sequence:
MKEKSKNAGRTRREKENSEFYELAKLLPLPSAITSQSDKASIIRLTTSYLKMRIVFPEGLGESWGHVSRTTSLENVGRELGSHLLQTLDGFIFVVAPDGKILYISETASVHLGLSQEELTGNSIYEYIHPADHDEMTAVLTAHQPYHSHFVHEYEMERSFFLRMKCVLAKANAGLTCGGYKVIHCSGYLKIRQYSLDMSPFDGCYQNVGLVAVGHSLPPSAVTEIKLHSNMFMFRASLDMKLIFLDSRVAELTGYEPQDLIEKTLYHHVHSCDTFHLRCAHHLLLVKGQVTTKYYRFLAKQGGWVWVQSYATIVHNSRSSRPHCIVSVNYVLTDTEYKGLQLSLDQAASTKPSFTYNSPSNPVTENRRVGKSRVSRTKTKTRLSPYSQYPGFPTDRSESDQDSPWGGSPLTDSASPQLLEQCEGIESSCVYRQFSDPRSLCYGLPLTEDHHTSNELYSHPHSESCERGCCKAGRYFLGTPQPGREAWWGAARSVLPLPKSSPENGDSFEGVSPHIASIHSLQVRGHWDEDSAVSSAPDGGSASDSGDRFRADQCRSSPQEPSKIETLIRATQQMIKEEESRLQLRKLPTDVPLEPTNSLAKSFHSTDFPQSAMQSVVCRGPAQVISPAPSPVPLSRLSSPLPDRLSKGKDFLQNELSSSQLPLTGTCAVSPTPALYSLHPRQYLEKHAAYSLTSYALEHLYEADTFRGYSLGCSGSSHYDMTTHLRKAEQAPGHKGTSVIITNGS
Protein: CD226 antigen (Platelet and T-cell activation antigen 1) (CD antigen CD226) (Q8K4F0)
Organism: Mus musculus (Mouse)
Function: Involved in intercellular adhesion, lymphocyte signaling, cytotoxicity and lymphokine secretion mediated by cytotoxic T-lymphocyte (CTL) and NK cell. Cell surface receptor for NECTIN2. Upon ligand binding, stimulates T-cell proliferation and cytokine production, including that of IL2, IL5, IL10, IL13, and IFNG. Competes with PVRIG for NECTIN2-binding.
Subcellular location: Cell membrane {ECO:0000250|UniProtKB:Q15762}; Single-pass type I membrane protein {ECO:0000250|UniProtKB:Q15762}. Note=Localizes to lipid rafts. {ECO:0000250|UniProtKB:Q15762}.
Interaction partners:
- Poliovirus receptor
- Nectin-2
- Integrin alpha-L
- T-cell immunoreceptor with Ig and ITIM domains
- Integrin beta-2
- NKG2-D type II integral membrane protein
- Integrin beta-2-like protein
- Killer cell lectin-like receptor subfamily C, member 1
- Natural cytotoxicity triggering receptor 1
- Killer cell lectin-like receptor subfamily C, member 2
Sequence:
MAYVTWLLAILHVHKALCEETLWDTTVRLSETMTLECVYPLTHNLTQVEWTKNTGTKTVSIAVYNPNHNMHIESNYLHRVHFLNSTVGFRNMSLSFYNASEADIGIYSCLFHAFPNGPWEKKIKVVWSDSFEIAAPSDSYLSAEPGQDVTLTCQLPRTWPVQQVIWEKVQPHQVDILASCNLSQETRYTSKYLRQTRSNCSQGSMKSILIIPNAMAADSGLYRCRSEAITGKNKSFVIRLIITDGGTNKHFILPIVGGLVSLLLVILIIIIFILYNRKRRRQVRIPLKEPRDKQSKVATNCRSPTSPIQSTDDEKEDIYVNYPTFSRRPKPRL
Protein: Protein irg-1 (Infection response protein 1) (O16327)
Organism: Caenorhabditis elegans
Interaction partners:
- Protein irg-2
- CUB-like domain-containing protein
- Transcription factor zip-2
- p-GlycoProtein related
- CUB-like domain-containing protein
Sequence:
MHTKVYVSEDRTKVFVLFYEAACVFSNFYPSGFEAKPVENFLKDTEKKEKLLKFTCSEQYFMYNKALLVGDMDIAEQILKETNPMKMKLLGRKLSMTKEQLKLWSQKSKDVMYRACLEKFSQNEDCRMILFRTHGMKLVEASPTDKIWGIGLDKADQRCEDERNWRGSNWLGEVLDQVREELWTRQEFKSNREQILKESLETRCQILEHFSH
Protein: Gametocyte development protein 1 (Q8I2G6)
Organism: Plasmodium falciparum (isolate 3D7)
Interaction partners:
- Heterochromatin protein 1
Sequence:
MNYKKETCVKLKVKGNSRRRNSASRKMFESWYLYLDNHTKGLFYLNTNDSDTNDAGCEDLVHIYKMKKNELCRHVISLNSEEYAIKKEEEAKNNYINIEEDVYYNSDIEQYVDDRKGNSVDLLSSPYIYDRNINNSIGKCFCFEMKKSFNSLMYLDNHLSYFYGNKKEEMGNFLQEYNKKRFEDVCNRGLLNNFKSDIYEIGIYEENIVSFKLLDCPNRHLIKNTYYMNADLIFNEIHNLLNKMYPLKHIMNNHHLVKKYQKKVPEHLKMEKALKFGIVLDFDYVRENFENNLKKTMTLLDFLIILDKIWEIFRQNCVIMFLHVCIFKDNDTNKDINNHRKRYSYMYEDLKNTLDLLKQKGIPVVMRINPFQSFRLFNHNEFSNPFIQDVNDLYMNERVDHIILVTNDSDVISYSYHFDHTIIYCIKDKYKNVTNVPNINSDINVDTITHPETTNNISNHYKNHNTIMFKKPVILICSLNNLPLKNNKIHDDIILDDFCYMTYIIKTLYFRFQSRSIRNMLKSNLNNTTNFVINRITQMNNTNRLLKNKINVLLLDDIIYKIRPRKENKNVSIHHLLQKAYSPFYYPIHYYIKEKCTYK
Protein: HORMA domain-containing protein 1 (Newborn ovary HORMA protein) (Q9D5T7)
Organism: Mus musculus (Mouse)
Function: Plays a key role in meiotic progression. Regulates 3 different functions during meiosis: ensures that sufficient numbers of processed DNA double-strand breaks (DSBs) are available for successful homology search by increasing the steady-state numbers of single-stranded DSB ends. Promotes synaptonemal-complex formation independently of its role in homology search. Plays a key role in the male mid-pachytene checkpoint and the female meiotic prophase checkpoint: required for efficient build-up of ATR activity on unsynapsed chromosome regions, a process believed to form the basis of meiotic silencing of unsynapsed chromatin (MSUC) and meiotic prophase quality control in both sexes.
Subcellular location: [Isoform 1]: Nucleus {ECO:0000269|PubMed:19686734, ECO:0000269|PubMed:19851446}. Chromosome {ECO:0000269|PubMed:19686734, ECO:0000269|PubMed:19851446, ECO:0000269|PubMed:22346761, ECO:0000269|PubMed:22549958, ECO:0000269|PubMed:27723721, ECO:0000269|PubMed:30272023, ECO:0000269|PubMed:30746471}. Note=Preferentially localizes to unsynapsed or desynapsed chromosomal regions during the prophase I stage of meiosis (PubMed:19686734, PubMed:19851446, PubMed:27723721). Accumulates on the chromosomes during the leptotene to zygotene stages of meiotic prophase I (PubMed:19686734, PubMed:19851446, PubMed:27723721). As germ cells progress into the pachytene stage, disappears from the synapsed chromosomal regions (PubMed:19686734, PubMed:19851446, PubMed:27723721). Once the chromosomes desynapse during the diplotene stage, it again accumulates on the chromosome axis of the desynapsed homologs (PubMed:19686734, PubMed:19851446, PubMed:27723721). TRIP13 is required for depletion from synapsed chromosomes (PubMed:19851446). The expression of the phosphorylated form at Ser-375 is restricted to unsynapsed chromosomal regions (PubMed:22346761). {ECO:0000269|PubMed:19686734, ECO:0000269|PubMed:19851446, ECO:0000269|PubMed:22346761, ECO:0000269|PubMed:27723721}.; SUBCELLULAR LOCATION: [Isoform 2]: Cytoplasm {ECO:0000269|PubMed:19686734}.
Interaction partners:
- Interactor of HORMAD1 protein 1
- Meiotic recombination protein SPO11
- Synaptonemal complex protein 1
- Synaptonemal complex central element protein 1
- Synaptonemal complex protein 3
- Meiotic recombination protein REC8 homolog
- Meiotic recombination protein DMC1/LIM15 homolog
- Pachytene checkpoint protein 2 homolog
- Structural maintenance of chromosomes protein 3
- Synaptonemal complex central element protein 2
Sequence:
MATMQLQRTASLSALVFPNKISTEHQSLMFVKRLLAVSVSCITYLRGIFPERAYGTRYLDDLCVKILKEDKNCPGSSQLVKWMLGCYDALQKKYLRMIILAVYTNPGDPQTISECYQFKFKYTKNGPIMDFISKNQNNKSSTTSADTKKASILLIRKIYVLMQNLGPLPNDVCLTMKLFYYDEVTPPDYQPPGFKDGDCEGVIFDGDPTYLNVGEVPTPFHTFRLKVTTEKERMENIDSTILKPKESKTQFEKILMDKDDVEDENHNNFDIKTKMNEQNENSGASEIKEPNLDCKEEETMQFKKSQSPSISHCQVEQLVSKTSELDVSESKTRSGKIFQSKMVNGNNQQGQTSKENRKRSLRQFRKTVLHVLESSQESVLKKRRVSEPKEHT
Protein: FAD/NAD(P)-binding oxidoreductase family protein (Q8GYJ7)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
- 4-hydroxybenzoate polyprenyltransferase, mitochondrial
- Ubiquinone biosynthesis O-methyltransferase, mitochondrial
- Ubiquinone biosynthesis protein
- 2-methoxy-6-polyprenyl-1,4-benzoquinol methylase, mitochondrial
- Ubiquinone biosynthesis monooxygenase COQ6, mitochondrial
- Embryo defective 2737
- Probable phosphopantothenoylcysteine decarboxylase
- Phosphopantothenoylcysteine decarboxylase
- Cytochrome P450, family 89, subfamily A, polypeptide 5
- AT5g10730/MAJ23_90
Sequence:
MAILGLIKRVTRITVNNSRVRVYPVRYFQRKDLSSTNLFNGEDAAKLPVLIVGAGPVGLVLSILLTKLGVKCAVVDKATSFSKHPQAHFINNRSMEIFRELDGLAEEIERSQPPVDLWRKFIYCTSLSGSTLGTVDHMQPQDFEKVVSPASVAHFSQYKLTNLLLKRLEDLGFHVRGSKESDGLEADSVVARQILMGHECVGIDANKDSITATVSFLKGGKHMKRNIQCSLLVGADGAGSAVRKLTVIEMRGERDLQKLVSVHFMSRELGEYLISNRPGMLFFIFNTDGIGVLVAHDLLQGEFVLQIPYYPPQQSLSDFSPEMCKMLIFNLVGHELSDLDVADIKPWVMHAEVAEKFMCCENRVILAGDAAHRFPPAGGFGMNTGIQDAHNLAWKIAALVQGSANSSILKTYETERRPIALSNTSLSVQNFRAAMSVPSALGLDPTVANSVHRFINKTVGSILPTGLQKAILDNVFALGRAQLSESLLNESNPLGNQRLSRLKSIFEGGKSLQLQFPAEDLGFRYLEGAIVPDNESEAGDPEVPSGRRRDYVPCAEPGSRLPHMYVKILSDSTREVIVSTLDLVSTEKVEFLLIISPLQESYELAHATFKVAKEFMASVKVCVVWPSSDDGLERKSNSALAPWENYVDVMEVKKQNGEGTSWWSICKMSERGSILVRPDQHIAWRAKSGITLDPTLHMRDVFTIILGKQ
Protein: Sorting nexin-5 (Q9D8U8)
Organism: Mus musculus (Mouse)
Function: Involved in several stages of intracellular trafficking. Interacts with membranes containing phosphatidylinositol lipids. Acts in part as component of the retromer membrane-deforming SNX-BAR subcomplex. The SNX-BAR retromer mediates retrograde transport of cargo proteins from endosomes to the trans-Golgi network (TGN) and is involved in endosome-to-plasma membrane transport for cargo protein recycling. The SNX-BAR subcomplex functions to deform the donor membrane into a tubular profile called endosome-to-TGN transport carrier (ETC). Does not have in vitro vesicle-to-membrane remodeling activity. Involved in retrograde transport of lysosomal enzyme receptor IGF2R. May function as link between endosomal transport vesicles and dynactin. Plays a role in the internalization of EGFR after EGF stimulation. Involved in EGFR endosomal sorting and degradation; the function involves PIP5K1C and is retromer-independent. Together with PIP5K1C facilitates HGS interaction with ubiquitinated EGFR, which initiates EGFR sorting to intraluminal vesicles (ILVs) of the multivesicular body for subsequent lysosomal degradation. Involved in E-cadherin sorting and degradation; inhibits PIP5K1C-mediated E-cadherin degradation (By similarity). Plays a role in macropinocytosis.
Subcellular location: Endosome {ECO:0000250|UniProtKB:Q9Y5X3}. Early endosome {ECO:0000250|UniProtKB:Q9Y5X3}. Early endosome membrane {ECO:0000250|UniProtKB:Q9Y5X3}; Peripheral membrane protein; Cytoplasmic side. Cell membrane {ECO:0000250|UniProtKB:Q9Y5X3}; Peripheral membrane protein; Cytoplasmic side {ECO:0000250|UniProtKB:Q9Y5X3}. Cytoplasmic vesicle membrane; Peripheral membrane protein; Cytoplasmic side. Cytoplasm. Cell projection, phagocytic cup. Cell projection, ruffle. Note=Recruited to the plasma membrane after EGF stimulation, which leads to increased levels of phosphatidylinositol 3,4-bisphosphate (PdtIns(3,4)P2) (By similarity). Detected on macropinosomes (PubMed:18854019). Targeted to membrane ruffles in response to EGFR stimulation (By similarity). {ECO:0000250|UniProtKB:Q9Y5X3, ECO:0000269|PubMed:18854019}.
Interaction partners:
- Sorting nexin-1
- Sorting nexin-2
- Sorting nexin-6
- Vacuolar protein sorting-associated protein 26A
- Vacuolar protein sorting-associated protein 35
- Vacuolar protein sorting-associated protein 29
- Sorting nexin-27
- Sorting nexin-3
- Dynactin subunit 1
- Sorting nexin-32
Sequence:
MAAVPELLEQQEEDRSKLRSVSVDLNVDPSLQIDIPDALSERDKVKFTVHTKTTLSTFQSPEFSVTRQHEDFVWLHDTLTETTDYAGLIIPPAPTKPDFDGPREKMQKLGEGEGSMTKEEFAKMKQELEAEYLAVFKKTVSTHEVFLQRLSSHPVLSKDRNFHVFLEYDQDLSVRRKNTKEMFGGFFKSVVKSADEVLFSGVKEVDDFFEQEKNFLINYYNRIKDSCAKADKMTRSHKNVADDYIHTAACLHSLALEEPTVIKKYLLKVAELFEKLRKVEGRVSSDEDLKLTELLRYYMLNIEAAKDLLYRRTKALIDYENSNKALDKARLKSKDVKLAETHQQECCQKFEQLSESAKEELINFKRKRVAAFRKNLIEMSELEIKHARNNVSLLQSCIDLFKNN
Protein: E3 ubiquitin-protein ligase TRIM7 (EC 2.3.2.27) (Glycogenin-interacting protein) (RING finger protein 90) (Tripartite motif-containing protein 7) (Q9C029)
Organism: Homo sapiens (Human)
Function: E3 ubiquitin-protein ligase that have both tumor-promoting and tumor-suppressing activities and functions in several biological processes including innate immunity, regulation of ferroptosis as well as cell proliferation and migration. Acts as an antiviral effector against multiple viruses by targeting specific viral proteins for ubiquitination and degradation including norovirus NTPase protein or SARS-CoV-2 NSP5 and NSP8 proteins. Mechanistically, recognizes the C-terminal glutamine-containing motif usually generated by viral proteases that process the polyproteins and trigger their ubiquitination and subsequent degradation. Mediates 'Lys-63'-linked polyubiquitination and stabilization of the JUN coactivator RNF187 in response to growth factor signaling via the MEK/ERK pathway, thereby regulating JUN transactivation and cellular proliferation. Promotes the TLR4-mediated signaling activation through its E3 ligase domain leading to production of pro-inflammatory cytokines and type I interferon (By similarity). Also plays a negative role in the regulation of exogenous cytosolic DNA virus-triggered immune response. Mechanistically, enhances the 'Lys-48'-linked ubiquitination of STING1 leading to its proteasome-dependent degradation. Mediates the ubiquitination of the SIN3-HDAC chromatin remodeling complex component BRMS1. Modulates NCOA4-mediated ferritinophagy and ferroptosis in glioblastoma cells by ubiquitinating NCOA4, leading to its degradation.
Subcellular location: Nucleus {ECO:0000269|PubMed:32853985}. Cytoplasm {ECO:0000269|PubMed:32641828, ECO:0000269|PubMed:32853985, ECO:0000269|PubMed:34062120}. Golgi apparatus {ECO:0000269|PubMed:32641828}.
Interaction partners:
- Glycogenin-1
- Glycogenin-2
- T-cell receptor-associated transmembrane adapter 1
- Gamma-butyrobetaine dioxygenase
- Ubiquitin-conjugating enzyme E2 D1
Sequence:
MAAVGPRTGPGTGAEALALAAELQGEATCSICLELFREPVSVECGHSFCRACIGRCWERPGAGSVGAATRAPPFPLPCPQCREPARPSQLRPNRQLAAVATLLRRFSLPAAAPGEHGSQAAAARAAAARCGQHGEPFKLYCQDDGRAICVVCDRAREHREHAVLPLDEAVQEAKELLESRLRVLKKELEDCEVFRSTEKKESKELLKQMAAEQEKVGAEFQALRAFLVEQEGRLLGRLEELSREVAQKQNENLAQLGVEITQLSKLSSQIQETAQKPDLDFLQEFKSTLSRCSNVPGPKPTTVSSEMKNKVWNVSLKTFVLKGMLKKFKEDLRGELEKEEKVELTLDPDTANPRLILSLDLKGVRLGERAQDLPNHPCRFDTNTRVLASCGFSSGRHHWEVEVGSKDGWAFGVARESVRRKGLTPFTPEEGVWALQLNGGQYWAVTSPERSPLSCGHLSRVRVALDLEVGAVSFYAVEDMRHLYTFRVNFQERVFPLFSVCSTGTYLRIWP
Protein: Cyclin-K (O75909)
Organism: Homo sapiens (Human)
Function: Regulatory subunit of cyclin-dependent kinases that mediates activation of target kinases. Plays a role in transcriptional regulation via its role in regulating the phosphorylation of the C-terminal domain (CTD) of the large subunit of RNA polymerase II (POLR2A).
Subcellular location: Nucleus {ECO:0000269|PubMed:22012619}.
Interaction partners:
- Cyclin-dependent kinase 12
- Cyclin-dependent kinase 13
- Cyclin-dependent kinase 9
- DNA-directed RNA polymerase II subunit RPB1
- DNA damage-binding protein 1
- Cyclin-dependent kinase 7
- Cyclin-T2
- Cyclin-H
- CCR4-NOT transcription complex subunit 2
- RNA polymerase II subunit A C-terminal domain phosphatase
Sequence:
MKENKENSSPSVTSANLDHTKPCWYWDKKDLAHTPSQLEGLDPATEARYRREGARFIFDVGTRLGLHYDTLATGIIYFHRFYMFHSFKQFPRYVTGACCLFLAGKVEETPKKCKDIIKTARSLLNDVQFGQFGDDPKEEVMVLERILLQTIKFDLQVEHPYQFLLKYAKQLKGDKNKIQKLVQMAWTFVNDSLCTTLSLQWEPEIIAVAVMYLAGRLCKFEIQEWTSKPMYRRWWEQFVQDVPVDVLEDICHQILDLYSQGKQQMPHHTPHQLQQPPSLQPTPQVPQVQQSQPSQSSEPSQPQQKDPQQPAQQQQPAQQPKKPSPQPSSPRQVKRAVVVSPKEENKAAEPPPPKIPKIETTHPPLPPAHPPPDRKPPLAAALGEAEPPGPVDATDLPKVQIPPPAHPAPVHQPPPLPHRPPPPPPSSYMTGMSTTSSYMSGEGYQSLQSMMKTEGPSYGALPPAYGPPAHLPYHPHVYPPNPPPPPVPPPPASFPPPAIPPPTPGYPPPPPTYNPNFPPPPPRLPPTHAVPPHPPPGLGLPPASYPPPAVPPGGQPPVPPPIPPPGMPPVGGLGRAAWMR
Protein: Glutamate receptor 3 (GluR-3) (AMPA-selective glutamate receptor 3) (GluR-C) (GluR-K3) (Glutamate receptor ionotropic, AMPA 3) (P42263)
Organism: Homo sapiens (Human)
Function: Receptor for glutamate that functions as ligand-gated ion channel in the central nervous system and plays an important role in excitatory synaptic transmission. L-glutamate acts as an excitatory neurotransmitter at many synapses in the central nervous system. Binding of the excitatory neurotransmitter L-glutamate induces a conformation change, leading to the opening of the cation channel, and thereby converts the chemical signal to an electrical impulse. The receptor then desensitizes rapidly and enters a transient inactive state, characterized by the presence of bound agonist. In the presence of CACNG4 or CACNG7 or CACNG8, shows resensitization which is characterized by a delayed accumulation of current flux upon continued application of glutamate.
Subcellular location: Cell membrane {ECO:0000269|PubMed:17989220}; Multi-pass membrane protein {ECO:0000250|UniProtKB:P19492}. Postsynaptic cell membrane {ECO:0000250|UniProtKB:P19492}; Multi-pass membrane protein {ECO:0000250|UniProtKB:P19492}. Postsynaptic density membrane {ECO:0000250|UniProtKB:P19492}.
Interaction partners:
- Glutamate receptor 2
- Glutamate receptor 1
- Glutamate receptor 4
- PRKCA-binding protein
- Glutamate receptor-interacting protein 1
- Voltage-dependent calcium channel gamma-2 subunit
- Protein cornichon homolog 2
- Protein cornichon homolog 3
- Voltage-dependent calcium channel gamma-8 subunit
- cAMP-dependent protein kinase catalytic subunit beta
Sequence:
MARQKKMGQSVLRAVFFLVLGLLGHSHGGFPNTISIGGLFMRNTVQEHSAFRFAVQLYNTNQNTTEKPFHLNYHVDHLDSSNSFSVTNAFCSQFSRGVYAIFGFYDQMSMNTLTSFCGALHTSFVTPSFPTDADVQFVIQMRPALKGAILSLLGHYKWEKFVYLYDTERGFSILQAIMEAAVQNNWQVTARSVGNIKDVQEFRRIIEEMDRRQEKRYLIDCEVERINTILEQVVILGKHSRGYHYMLANLGFTDILLERVMHGGANITGFQIVNNENPMVQQFIQRWVRLDEREFPEAKNAPLKYTSALTHDAILVIAEAFRYLRRQRVDVSRRGSAGDCLANPAVPWSQGIDIERALKMVQVQGMTGNIQFDTYGRRTNYTIDVYEMKVSGSRKAGYWNEYERFVPFSDQQISNDSASSENRTIVVTTILESPYVMYKKNHEQLEGNERYEGYCVDLAYEIAKHVRIKYKLSIVGDGKYGARDPETKIWNGMVGELVYGRADIAVAPLTITLVREEVIDFSKPFMSLGISIMIKKPQKSKPGVFSFLDPLAYEIWMCIVFAYIGVSVVLFLVSRFSPYEWHLEDNNEEPRDPQSPPDPPNEFGIFNSLWFSLGAFMQQGCDISPRSLSGRIVGGVWWFFTLIIISSYTANLAAFLTVERMVSPIESAEDLAKQTEIAYGTLDSGSTKEFFRRSKIAVYEKMWSYMKSAEPSVFTKTTADGVARVRKSKGKFAFLLESTMNEYIEQRKPCDTMKVGGNLDSKGYGVATPKGSALRNAVNLAVLKLNEQGLLDKLKNKWWYDKGECGSGGGDSKDKTSALSLSNVAGVFYILVGGLGLAMMVALIEFCYKSRAESKRMKLTKNTQNFKPAPATNTQNYATYREGYNVYGTESVKI
Protein: Dicarboxylate/tricarboxylate carrier (Q8IB73)
Organism: Plasmodium falciparum (isolate 3D7)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
Interaction partners:
Sequence:
MDRDIAKYDLESSSSVDVNKKGNNNKSVFEKIKPFAVGGASGMFATFCIQPLDMVKVRIQLNAEGKNVLRNPFIVAKDIIKNEGFLSLYKGLDAGLTRQVIYTTGRLGLFRTFSDMVKKEGEPLPFYKKCFCALAAGGLGAFIGNPADLSLIRLQADNTLPKELKRNYTGVFNALYRISKEEGLFALWKGSVPTIARAMSLNLGMLSTYDQSKEFLQKYLGVGMKTNLVASVISGFFAVTLSLPFDFVKTCMQKMKADPVTKKMPYKNMLDCSIQLYKKGGISIFYSSYATYYVRIAPHAMITLITVDYLNNLLKKIS
Protein: Spectrin repeat containing nuclear envelope protein 1 (A0A8I6B1X1)
Organism: Rattus norvegicus (Rat)
Subcellular location: Nucleus outer membrane {ECO:0000256|ARBA:ARBA00046312}; Single-pass type IV membrane protein {ECO:0000256|ARBA:ARBA00046312}.
Interaction partners:
Sequence:
MVVAEDLRALRMAEDGSVDADLPDCDCDVSRVKKLKETLVAVQQLDKNMGSLRIWLAHMESELAKPIVYDSCNSEEIQKKLSEQQELQRDIEKHSTGVASVLNLCEVLLHDCDACATDAECDSIQQATRNLDRRWRNICAMSMERRLKIEETWRLWQKFLDDYSRFEDWLEISERTAAFPSSSGVLYTVAKEELKKFEAFQRQVHESLTQLELINKQYRRLARENRTDSACSLRQMAHGGNQRWDDLQKRVTSILRRLKHFISQREEFETARDSILVWLTEMDLQLTNIEHFSECDVQAKIKQLKAFQQEISLNHSKIEQIIAQGEQLIEKSEPLDAAVIEEELDELRRYCQEVFGRVERYHKKLIRLPLPDDHDLSDRELDLEDSMALSDLHWQDPSEDGMPSPQPSSNPSLSLPQPLRSERSGRDTPASVDSIPLEWDHDYDLSRDLESASRTLPSEDEEGEEDKEFYLRGAVGLSGDPTSLESQMRQLDKALDDSRFQIQQTANILRGKTPTGPDLGTSYKGYMKLLGECSGSIDSVRRLEHKLAEEESFPGFTNPTSTETQPAGVIDRWELLQAQAMSKELKMKQNLQKWQQFNSDLNNICAWLGETEEELDRLQHLALSTDIHTIKSHIKKLKELQKALDHRKAIILSINLCSSEFTQADSKESHDLQDRLSQMNRRWDRVCSLLEDWRGSLQDALMQCQDFHEMTHALLLLLENTDRRKNEIVPIDSTLDPETLQDHHTQLTQIKQELLKSQLRVASLQNMSRQLLVNAEGSDCLEAKEKVHVIGNRLKLLLKEVSRHIKDLEKLLGMSSSQQDLSSWSSADEVDTSGSVSPTSGRSTPNRQKSPRGKCSLSQPGPSVSSPKSRSTKGGSDSSLSETRPARAGRDFLFRVLRAALPIQLLLLLLIGLTSRVPISEEDYSCALSNNFARSFHPMLRYTNGPPPL
Protein: Formin-like protein 1 (AtFH1) (AtFORMIN-8) (Q9SE97)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Might be involved in the organization and polarity of the actin cytoskeleton. Involved in polar pollen cell growth process by maintaining tip-focused cell membrane expansion for the polar extension of pollen tubes.
Subcellular location: Membrane {ECO:0000305}; Single-pass membrane protein {ECO:0000305}.
Interaction partners:
- Profilin-3
- Profilin-1
- Profilin-4
- Profilin-2
- Profilin-5
- Formin-like protein 12
- Frataxin, mitochondrial
- Exosome complex exonuclease
- Fimbrin-5
- Fimbrin-4
Sequence:
MLFFLFFFYLLLSSSSDLVFADRRVLHEPFFPIDSPPPSPPSPPPLPKLPFSSTTPPSSSDPNASPFFPLYPSSPPPPSPASFASFPANISSLIVPHATKSPPNSKKLLIVAISAVSSAALVALLIALLYWRRSKRNQDLNFSDDSKTYTTDSSRRVYPPPPATAPPTRRNAEARSKQRTTTSSTNNNSSEFLYLGTMVNQRGIDEQSLSNNGSSSRKLESPDLQPLPPLMKRSFRLNPDVGSIGEEDEEDEFYSPRGSQSGREPLNRVGLPGQNPRSVNNDTISCSSSSSGSPGRSTFISISPSMSPKRSEPKPPVISTPEPAELTDYRFVRSPSLSLASLSSGLKNSDEVGLNQIFRSPTVTSLTTSPENNKKENSPLSSTSTSPERRPNDTPEAYLRSPSHSSASTSPYRCFQKSPEVLPAFMSNLRQGLQSQLLSSPSNSHGGQGFLKQLDALRSRSPSSSSSSVCSSPEKASHKSPVTSPKLSSRNSQSLSSSPDRDFSHSLDVSPRISNISPQILQSRVPPPPPPPPPLPLWGRRSQVTTKADTISRPPSLTPPSHPFVIPSENLPVTSSPMETPETVCASEAAEETPKPKLKALHWDKVRASSDREMVWDHLRSSSFKLDEEMIETLFVAKSLNNKPNQSQTTPRCVLPSPNQENRVLDPKKAQNIAILLRALNVTIEEVCEALLEGNADTLGTELLESLLKMAPTKEEERKLKAYNDDSPVKLGHAEKFLKAMLDIPFAFKRVDAMLYVANFESEVEYLKKSFETLEAACEELRNSRMFLKLLEAVLKTGNRMNVGTNRGDAHAFKLDTLLKLVDVKGADGKTTLLHFVVQEIIRAEGTRLSGNNTQTDDIKCRKLGLQVVSSLCSELSNVKKAAAMDSEVLSSYVSKLSQGIAKINEAIQVQSTITEESNSQRFSESMKTFLKRAEEEIIRVQAQESVALSLVKEITEYFHGNSAKEEAHPFRIFLVVRDFLGVVDRVCKEVGMINERTMVSSAHKFPVPVNPMMPQPLPGLVGRRQSSSSSSSSSTSSSDEDEHNSISLVS
Protein: MHC class II regulatory factor RFX1 (Regulatory factor X 1) (Transcription factor RFX1) (P48377)
Organism: Mus musculus (Mouse)
Function: Regulatory factor essential for MHC class II genes expression. Binds to the X boxes of MHC class II genes (By similarity).
Subcellular location: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00858}.
Interaction partners:
- Histone-lysine N-methyltransferase SUV39H1
- Serine/threonine-protein kinase ATR
- Histone deacetylase 1
- Forkhead box protein J2
Sequence:
MATQSYVTELQAAPQASQPPQAPPQALPQPPPPAAPQPPAAATPQPQYVTELQSPQPQTQPPGSQKQYVAELPAAPAPSQPATPAPSPVAQQYIVVTVSEGAMRASETVSEASPSSTASQTGVPTQVVQQVQGTQQRLLVQASVQAKPGHVSPLQLTNIQVPQQAIPTQHLVVQSPAPGTKSGQVSLTVHSAQQVHSAPERSPVQANNSTSKTAGTPAATVQQLQVHSVQQSVPVTQERSVVQATPQTKAGPVQQLTVQGLQPVHVAQEVQQLPQVPVPHVYSSQVQYVEGGDASYTASAIRSSTYQYPETPIYTQTAGTSYYEASGTAAQVSTPATSQTVASSGSVPMYVSGSPIVASSSSSEAGASNSSVGAGGNGGGGSSGGGSGGSSGSGAGTYVIQGGYMLGNASQSYSHTTRASPATVQWLLDNYETAEGVSLPRSTLYCHYLLHCQEQKLEPVNAASFGKLIRSVFMGLRTRRLGTRGNSKYHYYGLRIKASSPLLRLMEDQQHMAMRGQPFSQKQRLKPIQKMEGVANGVAVGQQSTGLSDISAQVQQYQQFLDASRSLPDFAELDLQGKVLPEGVGPGDIKAFQVLYREHCEAIVDVMVNLQFTLVETLWKTFWRYNLSQPSEAPPLAVHDEAEKRLPRASLVLLSKFQPVLQWTKHCDNVLYQGLVEILIPDVLRPIPSALTQAIRNFAKSLESWLTHAMVNIPEEMLRVKVAAAGAFAQTLRRYTSLNHLAQAARAVLQNTAQINQMLSDLNRVDFANVQEQASWVCRCEDRVVQRLEQDFKVTLQQQNSLEQWAAWLDGVVSQVLKPYQGSSGFPKAAKLFLLKWSFYSSMVIRDLTLRSAASFGSFHLIRLLYDEYMYYLIEHRVAQAKGETPIAVMGEFANLATSLNPLDPDKDEEEEEEEESEDELPQDISLAAGSESPALGPEALEPPAKLARTDTRGLFVQALPSS