wanglab/gogpt-training-data huggingface dataset:
Protein: Voltage-gated inwardly rectifying potassium channel KCNH3 (Brain-specific eag-like channel 1) (BEC1) (Ether-a-go-go-like potassium channel 2) (ELK channel 2) (ELK2) (Potassium voltage-gated channel subfamily H member 3) (Voltage-gated potassium channel subunit Kv12.2) (Q9ULD8)
Organism: Homo sapiens (Human)
Function: Pore-forming (alpha) subunit of voltage-gated potassium channel. Elicits an outward current with fast inactivation. Channel properties may be modulated by cAMP and subunit assembly.
Subcellular location: Cell membrane {ECO:0000250|UniProtKB:Q9WVJ0}; Multi-pass membrane protein {ECO:0000250|UniProtKB:Q9WVJ0}. Note=Expression on the cell membrane requires at least one of the three glycosylation sites to carry a sugar chain irrespective of their positions. {ECO:0000250|UniProtKB:Q9WVJ0}.
Interaction partners:
- Voltage-gated potassium channel subunit beta-3
- ETS domain-containing protein Elk-1
Sequence:
MPAMRGLLAPQNTFLDTIATRFDGTHSNFVLGNAQVAGLFPVVYCSDGFCDLTGFSRAEVMQRGCACSFLYGPDTSELVRQQIRKALDEHKEFKAELILYRKSGLPFWCLLDVIPIKNEKGEVALFLVSHKDISETKNRGGPDRWKETGGGRRRYGRARSKGFNANRRRSRAVLYHLSGHLQKQPKGKHKLNKGVFGEKPNLPEYKVAAIRKSPFILLHCGALRATWDGFILLATLYVAVTVPYSVCVSTAREPSAARGPPSVCDLAVEVLFILDIVLNFRTTFVSKSGQVVFAPKSICLHYVTTWFLLDVIAALPFDLLHAFKVNVYFGAHLLKTVRLLRLLRLLPRLDRYSQYSAVVLTLLMAVFALLAHWVACVWFYIGQREIESSESELPEIGWLQELARRLETPYYLVGRRPAGGNSSGQSDNCSSSSEANGTGLELLGGPSLRSAYITSLYFALSSLTSVGFGNVSANTDTEKIFSICTMLIGALMHAVVFGNVTAIIQRMYARRFLYHSRTRDLRDYIRIHRIPKPLKQRMLEYFQATWAVNNGIDTTELLQSLPDELRADIAMHLHKEVLQLPLFEAASRGCLRALSLALRPAFCTPGEYLIHQGDALQALYFVCSGSMEVLKGGTVLAILGKGDLIGCELPRREQVVKANADVKGLTYCVLQCLQLAGLHDSLALYPEFAPRFSRGLRGELSYNLGAGGGSAEVDTSSLSGDNTLMSTLEEKETDGEQGPTVSPAPADEPSSPLLSPGCTSSSSAAKLLSPRRTAPRPRLGGRGRPGRAGALKAEAGPSAPPRALEGLRLPPMPWNVPPDLSPRVVDGIEDGCGSDQPKFSFRVGQSGPECSSSPSPGPESGLLTVPHGPSEARNTDTLDKLRQAVTELSEQVLQMREGLQSLRQAVQLVLAPHREGPCPRASGEGPCPASTSGLLQPLCVDTGASSYCLQPPAGSVLSGTWPHPRPGPPPLMAPWPWGPPASQSSPWPRATAFWTSTSDSEPPASGDLCSEPSTPASPPPSEEGARTGPAEPVSQAEATSTGEPPPGSGGLALPWDPHSLEMVLIGCHGSGTVQWTQEEGTGV
Protein: Cell surface hyaluronidase (EC 3.2.1.35) (Cell migration-inducing hyaluronidase 2) (Protein frozen ventricle) (Protein wickham) (Transmembrane protein 2) (A3KPQ7)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Function: Cell surface hyaluronidase that mediates the initial cleavage of extracellular high-molecular-weight hyaluronan into intermediate-size hyaluronan. Acts as a regulator of angiogenesis in embryos by mediating degradation of extracellular hyaluronan, thereby promoting VEGF signaling. Acts as a regulator of heart development during myocardial and endocardial morphogenesis: involved in the looping stage of heart morphogenesis. Stimulates migration of endocardial cells and increases both myocardial and endocardial fusion. Involved in the restriction of endocardial cushions (ECs) formation to the atrioventricular canal (AVC). Also required for muscle fiber attachment. Is very specific to hyaluronan; not able to cleave chondroitin sulfate or dermatan sulfate (By similarity).
Subcellular location: Cell membrane {ECO:0000269|PubMed:28118600}; Single-pass type II membrane protein {ECO:0000269|PubMed:28118600}.
Interaction partners:
- Hyaluronidase.
- Hyaluronidase.
Sequence:
MQVNDGPSSHPIFVAPVNGNAQRSSGYVPGRIVPVRSPPPAKAPPPPPLKPPVPPPARPSVFNLSEDGNRREQAQNQQRKNTYICVGIFFGIFLLILILVLSLTSKDVLDENCPHQNPALRSWKPGHDLKKVVVIHSGEHYRLDSSATLYSITIQAGGSVVFADDKKGSKNITLRTRHILIEDGGALHIGAPKCRYRSLATITLVGRSDETAVTEVPGMGRKFLGVNSGGTLELHGSERMSWTFLTRTVPASGLATGDHAFQKNFSRGINLRVVDQDTAEVLVNERFDTHESQDDSKRLGELLKALPAGRIVALATGDSAVKNLVFETKQTIHDLLGSNYISDLKYRDAWALVSVIGGGNGSCTEDVREHENHDTGGKALARQDFFTVDGVGFTVTAYSEWSNGYPTTGFQVDAVDKVVLNLQDDVSSWNPGDRIVVASTDYSMYQAEEFTLLPCPNCNRKQVQIQGKPQFSHVGEILDGVDMRAEVALLSRNILIHGEMENSCYGGNWCQYFSYDTFGGHIKILGNFTSVHLSHIELKHMGQQREKGRYPLNFHRCGDVDQSGGYSNPAYVDSLSIHHSFSRCVTVHATNGLLVKDTVGYDTLGHCFFLKDGIEQRNIFFHNLGLLTRPGTILPTDRNDSMCTEITDRVYKGYIPIPANECKAVSSFWIAHPNNHLISNSAAGSQDAGIWYVFHNSSTGDSHGMISETKAELTPLGTFFNNRVHSNFKAGLFIDRKVKSTNATAADPREYLCLDNSARFRPHESSDPSRPRVAAIIDTLISFKNNDLGAWIRGGDIIIRNSGDGSYPKDEGSSQEVSQSLFIGESRNRGTNGGQNKYWGIGGVDGKMRTLPRNKTFPIRGFQINDGPVRIFDSTFRAFSPTADRFTMAVGFSLKNIWQLTPRNNLSALAFHPSVTLRAFFGRPGDWFEQNDLDGDKNSIFHDLDGSISGYADTYVARADNFLIRHPQCVDMPQWNGVVCSGKYSQVYIQTQAASNLSLSISRDEYPDKPMVLRGIRTKTSPSQQYQPVLMMGKSYTMHWNGPAPRETVLSLINFDQDDWALLGLCYPNETVFQITSDIYNKQNNGFEGIEDYGPVTSIADLEKRQQERKYFFDKSAGLLWLYARARHRRDGNSYCSSAGCERVKIIATIRANQKTETCNCTANAYPKYSKPASNIVPMPKPNTEPCGACGASQFAFSSDPWNSYLQTQIKSLSVKEEQDNDTQAYITVNAQRFDLSQSGFLLVTVDACSGKVTKNSMFSSLDTKMEQFFKTGIMKRSIVLLATRGQPASFAGVAQYLESLGSAKTPDLQNKVAIAFFGFLGQGGPSPQPWSTLLTCQGAKILGLQERFIPLSLEEYSCPPKKDSPTRMDLELLKKIS
Protein: Stretch-activated cation channel yam8 (Q10063)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Required for Ca(2+) influx and for vitality of cells in a late, pheromone-induced event of the mating process requiring calcium-induced signaling.
Subcellular location: Cell membrane {ECO:0000250|UniProtKB:P41821}; Single-pass membrane protein {ECO:0000255}.
Interaction partners:
- Calcium-channel protein cch1
- Putative metal ion transporter C17A12.14
- Putative metal ion transporter C27B12.12c
- Transcriptional regulator prz1
- Tyrosine-protein phosphatase pmp1
- Uncharacterized membrane protein C1322.03
- Mitogen-activated protein kinase spm1
- Uncharacterized membrane protein C663.14c
- MAP kinase kinase skh1/pek1
- Protein kinase C-like 2
Sequence:
MFFFSTHLILKILFFWSITRNIFGATYTSLLLNNTINGNINDQSTAYYNLTWEGNTAYNVSLTLSTCTAFDGANDLMLYISNNTFDEALPLDNFTITASENGLATIFVTGYSPLYIAVSSAFSQFAPNFFVESGESTLEGNNVINYELAAGIDTPFSQYNATKFLFAQDTDFQAALLITGNLTTNETSIIPSYEIYVNPSNSTYDNTFNKFSSSFCAFQNNPSTVNTNNADRSMTLRGLGPFAKEQFYLKGLDPNVTYTAYLVEPNIGQPGGTVYPGVTFTTKTSPACQLIYDLQFCSEVAYAVPGNSSLFSASALAEWYDQQAYGYYQNFTYTLDLIPCNATSWSAYSLLKNCSDCANSYKNWLCASVIPRCADINDNSSYLIYKNYDSRYPLIDEVIQPGPYKEVLPCSYLCYSLASSCPLDLGFACPKAGYGLEFSYGEVSNVTGLITCNAPGVEFYESGSALLNISWRTFFISLIFWILFVE
Protein: Tyrosine-protein phosphatase non-receptor type 22 (EC 3.1.3.48) (Hematopoietic cell protein-tyrosine phosphatase 70Z-PEP) (Lymphoid phosphatase) (LyP) (PEST-domain phosphatase) (PEP) (Q9Y2R2)
Organism: Homo sapiens (Human)
Function: Acts as negative regulator of T-cell receptor (TCR) signaling by direct dephosphorylation of the Src family kinases LCK and FYN, ITAMs of the TCRz/CD3 complex, as well as ZAP70, VAV, VCP and other key signaling molecules. Associates with and probably dephosphorylates CBL. Dephosphorylates LCK at its activating 'Tyr-394' residue. Dephosphorylates ZAP70 at its activating 'Tyr-493' residue. Dephosphorylates the immune system activator SKAP2. Positively regulates toll-like receptor (TLR)-induced type 1 interferon production. Promotes host antiviral responses mediated by type 1 interferon (By similarity). Regulates NOD2-induced pro-inflammatory cytokine secretion and autophagy. Acts as an activator of NLRP3 inflammasome assembly by mediating dephosphorylation of 'Tyr-861' of NLRP3. Dephosphorylates phospho-anandamide (p-AEA), an endocannabinoid to anandamide (also called N-arachidonoylethanolamide) (By similarity).
Subcellular location: Cytoplasm {ECO:0000250|UniProtKB:P29352}.
Interaction partners:
- Tyrosine-protein kinase CSK
- HLA class II histocompatibility antigen, DRB1 beta chain
- Proline-serine-threonine phosphatase-interacting protein 1
- Complement component 1 Q subcomponent-binding protein, mitochondrial
- Tyrosine-protein kinase Lck
- Tyrosine-protein kinase ZAP-70
- T-cell surface glycoprotein CD8 alpha chain
- HLA class II histocompatibility antigen DQ alpha chain
- Protein-arginine deiminase type-4
- Cytotoxic T-lymphocyte protein 4
Sequence:
MDQREILQKFLDEAQSKKITKEEFANEFLKLKRQSTKYKADKTYPTTVAEKPKNIKKNRYKDILPYDYSRVELSLITSDEDSSYINANFIKGVYGPKAYIATQGPLSTTLLDFWRMIWEYSVLIIVMACMEYEMGKKKCERYWAEPGEMQLEFGPFSVSCEAEKRKSDYIIRTLKVKFNSETRTIYQFHYKNWPDHDVPSSIDPILELIWDVRCYQEDDSVPICIHCSAGCGRTGVICAIDYTWMLLKDGIIPENFSVFSLIREMRTQRPSLVQTQEQYELVYNAVLELFKRQMDVIRDKHSGTESQAKHCIPEKNHTLQADSYSPNLPKSTTKAAKMMNQQRTKMEIKESSSFDFRTSEISAKEELVLHPAKSSTSFDFLELNYSFDKNADTTMKWQTKAFPIVGEPLQKHQSLDLGSLLFEGCSNSKPVNAAGRYFNSKVPITRTKSTPFELIQQRETKEVDSKENFSYLESQPHDSCFVEMQAQKVMHVSSAELNYSLPYDSKHQIRNASNVKHHDSSALGVYSYIPLVENPYFSSWPPSGTSSKMSLDLPEKQDGTVFPSSLLPTSSTSLFSYYNSHDSLSLNSPTNISSLLNQESAVLATAPRIDDEIPPPLPVRTPESFIVVEEAGEFSPNVPKSLSSAVKVKIGTSLEWGGTSEPKKFDDSVILRPSKSVKLRSPKSELHQDRSSPPPPLPERTLESFFLADEDCMQAQSIETYSTSYPDTMENSTSSKQTLKTPGKSFTRSKSLKILRNMKKSICNSCPPNKPAESVQSNNSSSFLNFGFANRFSKPKGPRNPPPTWNI
Protein: Receptor expression-enhancing protein (A0A0B4LG73)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Membrane {ECO:0000256|RuleBase:RU362006}; Multi-pass membrane protein {ECO:0000256|RuleBase:RU362006}.
Interaction partners:
Sequence:
MISSLFSRLIILFCGTLYPAYASYKAVRTKDVKEYVKWMMYWIVFAFFTCIETFTDIFISWLPFYYEVKVALVFWLLSPATKGSSTLYRKFVHPMLTRHEQEIDEYVNQAKERGYSAVLQLGSKGVNYATNVLMQTAIKGGGNLVQTIKRSYSLSDLSEPDMHRTQDELDDVMMSSMTSSAVVMRSTATGARLLRPRNQTPVGRSGSGTRHSTGMYFTEVDVTAKNAGDFNYNIRSQDDISSGYSSAEPVSGLSRTSSMTNASKARAKSKRNEDKSMSASCTTLPRSSSRKSERSQGGTATGQMKTRNKSEK
Protein: Solute carrier family 25 member 3 (F8VYH5)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MFSSVAHLARANPFNTPHLQLVHDGLGDLRSSSPGPTGQPRRPRNLAAAAVEGEIRPCPIQSCGLLVGRPAFEAWTRLGGQGRTSPARCTVGRRPVACPGVSAFSTIGGCQILGLPSRAWKR
Protein: Elongation factor 1-alpha 1 (EF-1-alpha 1) (P86934)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Function: This protein promotes the GTP-dependent binding of aminoacyl-tRNA to the A-site of ribosomes during protein biosynthesis.
Subcellular location: Cytoplasm {ECO:0000250}.
Interaction partners:
- GST N-terminal domain-containing protein
- GTP-binding nuclear protein
- Elongation factor 2
- Eukaryotic peptide chain release factor subunit 1
- Small ribosomal subunit protein uS5
- Translation elongation factor 1-beta, putative
- Translation elongation factor 1-beta, putative
- Translation elongation factor 1-beta, putative
- 60S ribosomal protein L4
- 60S ribosomal protein L5, putative
Sequence:
MGKEKVHMNLVVVGHVDAGKSTATGHLIYKCGGIDKRTIEKFEKEAADIGKASFKYAWVLDKLKAERERGITIDIALWKFESPKSVFTIIDAPGHRDFIKNMITGTSQADAAILIIASAQGEFEAGISKDGQTREHALLAFTLGVKQMVVCCNKMDDKTVNYGQERYDEIVKEVSAYIKKVGYNVEKVRFVPISGWQGDNMIEKSEKMPWYKGPTLLEALDMLEPPVRPSDKPLRLPLQDVYKIGGIGTVPVGRVETGVMKPGDVVTFAPANVTTEVKSIEMHHEQLAEATPGDNVGFNVKNVSVKDIRRGNVCGNTKNDPPKEAADFTAQVIILNHPGQIGNGYAPVLDCHTSHIACKFAEIESKIDRRSGKELEKAPKSIKSGDAAIVRMVPQKPMCVEVFNDYAPLGRFAVRDMRQTVAVGIIKAVTKKDGSGGKVTKAAVKASKK
Protein: GDP-L-galactose phosphorylase 1 (EC 2.7.7.69) (Protein VITAMIN C DEFECTIVE 2) (Q8RWE8)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Catalyzes a reaction of the Smirnoff-Wheeler pathway, the major route to ascorbate biosynthesis in plants. Acts as a phosphorylase rather than as a transferase. Uses preferentially GDP-L-galactose and GDP-D-glucose as substrates. Lower activity with GDP-L-fucose, very low activity with GDP-D-mannose, and no activity with UDP-D-glucose, UDP-D-galactose or ADP-D-glucose. Highly specific for inorganic phosphate as the guanylyl acceptor.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:18516687}. Nucleus {ECO:0000269|PubMed:18516687}.
Interaction partners:
- GDP-mannose 3,5-epimerase
- Inositol-phosphate phosphatase
- Bifunctional phosphatase IMPL2, chloroplastic
- Mannose-1-phosphate guanylyltransferase 1
- L-galactono-1,4-lactone dehydrogenase, mitochondrial
- L-galactose dehydrogenase
- GDP-L-galactose phosphorylase 2
- Phosphomannomutase
- Monodehydroascorbate reductase 3
- Mannose-6-phosphate isomerase 2
Sequence:
MLKIKRVPTVVSNYQKDDGAEDPVGCGRNCLGACCLNGARLPLYACKNLVKSGEKLVISHEAIEPPVAFLESLVLGEWEDRFQRGLFRYDVTACETKVIPGKYGFVAQLNEGRHLKKRPTEFRVDKVLQSFDGSKFNFTKVGQEELLFQFEAGEDAQVQFFPCMPIDPENSPSVVAINVSPIEYGHVLLIPRVLDCLPQRIDHKSLLLAVHMAAEAANPYFRLGYNSLGAFATINHLHFQAYYLAMPFPLEKAPTKKITTTVSGVKISELLSYPVRSLLFEGGSSMQELSDTVSDCCVCLQNNNIPFNILISDCGRQIFLMPQCYAEKQALGEVSPEVLETQVNPAVWEISGHMVLKRKEDYEGASEDNAWRLLAEASLSEERFKEVTALAFEAIGCSNQEEDLEGTIVHQQNSSGNVNQKSNRTHGGPITNGTAAECLVLQ
Protein: Formate-dependent nitrite reductase complex subunit NrfG (P32712)
Organism: Escherichia coli (strain K12)
Function: Required for formate-dependent nitrite reduction. Not required for the biosynthesis of any of the c-type cytochromes nor for the secretion of the periplasmic cytochromes.
Interaction partners:
- Formate-dependent nitrite reductase complex subunit NrfF
- Probable cytochrome c-type biogenesis protein NrfE
- Cytochrome c-type protein NrfB
- Cytochrome c-552
- Protein NrfD
- Cytochrome c-type biogenesis protein CcmF
- Protein NrfC
- Thiol:disulfide interchange protein DsbE
- Cytochrome c-type biogenesis protein CcmE
- Cytochrome c-type biogenesis protein CcmH
Sequence:
MKQPKIPVKMLTTLTILMVFLCVGSYLLSPKWQAVRAEYQRQRDPLHQFASQQTPEAQLQALQDKIRANPQNSEQWALLGEYYLWQNDYSNSLLAYRQALQLRGENAELYAALATVLYYQASQHMTAQTRAMIDKALALDSNEITALMLLASDAFMQANYAQAIELWQKVMDLNSPRVNRTQLVESINMAKLLQRRLD
Protein: Mediator of RNA polymerase II transcription subunit 27 (Mediator complex subunit 27) (RNA polymerase II mediator complex protein pmc3) (Q10477)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Component of the Mediator complex, a coactivator involved in the regulated transcription of nearly all RNA polymerase II-dependent genes. Mediator functions as a bridge to convey information from gene-specific regulatory proteins to the basal RNA polymerase II transcription machinery. Mediator is recruited to promoters by direct interactions with regulatory proteins and serves as a scaffold for the assembly of a functional preinitiation complex with RNA polymerase II and the general transcription factors.
Subcellular location: Nucleus {ECO:0000305}.
Interaction partners:
- Mediator of RNA polymerase II transcription subunit 20
- Mediator of RNA polymerase II transcription subunit 7
- Mediator of RNA polymerase II transcription subunit 8
- Mediator of RNA polymerase II transcription subunit 18
- Mediator of RNA polymerase II transcription subunit 17
- Mediator of RNA polymerase II transcription subunit 31
- Mediator of RNA polymerase II transcription subunit 1
- Mediator of RNA polymerase II transcription subunit 21
- Mediator of RNA polymerase II transcription subunit 6
- Mediator of RNA polymerase II transcription subunit 14
Sequence:
MSLEEQRTRDELKHKLLDLNQLHEQLAELRTICPSLLKLLHPETGTSRKFEKSAQEAIEKVNSFYTHLKSSQNVFDYAEKSLQADSSNLLPTYLYNSEDLSNDTENNETKSINGKSALDLKEPHHSELHDNDNFQNSDINIESFKGDIEASGSILTTHENKSFTLKLANELEFIFFHDTRGKFSVYCSSSKDDAITFSINRNNNFLGNLWSLMPKILDYQHLYSKPCDFCKSLISPVYLELPSVRRNANSTVKPTSKDILALHAECVPAQSDL
Protein: Fatty-acid and retinol-binding protein 1 (Bm-FAR-1) (Bm20) (Q93142)
Organism: Brugia malayi (Filarial nematode worm)
Function: Binds retinol. Also binds the fluorescent fatty acid 11-((5-dimethylaminonaphthalene-1-sulfonyl)amino)undecanoic acid (DAUDA). The long chain fatty acid oleic acid can act competitively to displace bound DAUDA and retinol.
Subcellular location: Secreted {ECO:0000250|UniProtKB:Q25619}.
Interaction partners:
Sequence:
MYHRLILLALVGTTMANVIPFSMSNIPEEYKEFIPEEVRNFYKDLTVEDKEILRELASKHATFANEDAALEALKDKSDKLYKNAVELRNFVKAKIDSLKPDAKIFVDEIIAKARSLRSDDGHKLDTEKIKQAARDIIAKYQALSEETKEELKVTFPAIAKIIGNEKLKRNASTFLQKN
Protein: 3-ketoacyl-CoA thiolase 1, peroxisomal (EC 2.3.1.16) (Acetyl-CoA acyltransferase 1) (Beta-ketothiolase 1) (Peroxisomal 3-oxoacyl-CoA thiolase 1) (Q8LF48)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Involved in fatty-acid beta-oxidation prior to gluconeogenesis during germination and subsequent seedling growth. Implicated in jasmonic acid (JA) biosynthesis (By similarity).
Subcellular location: Peroxisome {ECO:0000250}.
Interaction partners:
- Hydroxymethylglutaryl-CoA synthase
- Peroxisomal fatty acid beta-oxidation multifunctional protein MFP2
- Peroxisomal fatty acid beta-oxidation multifunctional protein AIM1
- Putative peroxisomal acyl-coenzyme A oxidase 1.2
- Peroxisomal acyl-coenzyme A oxidase 1
- Acyl-coenzyme A oxidase 3, peroxisomal
- Putative acyl-coenzyme A oxidase 3.2, peroxisomal
- Acyl-coenzyme A oxidase 2, peroxisomal
- Putative acyl-coenzyme A oxidase At3g06690
- Acyl-coenzyme A oxidase 4, peroxisomal
Sequence:
MEKATERQRILLRHLQPSSSSDASLSASACLSKDSAAYQYGDDVVIVAAQRTALCKAKRGSFKDTFPDELLASVLRALIEKTNVNPSEVGDIVVGTVLGPGSQRASECRMAAFYAGFPETVPIRTVNRQCSSGLQAVADVAAAIKAGFYDIGIGAGLESMTTNPRGWKGSVNPNVKKFEQAHNCLLPMGITSENVAHRFNVSREEQDQAAVDSHRKAASATASGKFKDEITPVKTKIVDPKTGDEKPITVSVDDGIRPNTTLSGLAKLKPVFKEDGTTTAGNSSQLSDGAGAVLLMRRNVAMQKGLPILGVFRTFSAVGVDPAIMGVGPAVAIPAAVKAAGLELNDVDLFEINEAFASQFVYCRNKLGLDAEKINVNGGAIAIGHPLGATGARCVATLLHEMKRRGKDCRFGVVSMCIGSGMGAAAVFERGGGVDELCDVRKV
Protein: G-protein-signaling modulator 1 (Activator of G-protein signaling 3) (Q9R080)
Organism: Rattus norvegicus (Rat)
Function: Guanine nucleotide dissociation inhibitor (GDI) which functions as a receptor-independent activator of heterotrimeric G-protein signaling. Keeps G(i/o) alpha subunit in its GDP-bound form thus uncoupling heterotrimeric G-proteins signaling from G protein-coupled receptors. Controls spindle orientation and asymmetric cell fate of cerebral cortical progenitors. May also be involved in macroautophagy in intestinal cells. May play a role in drug addiction.
Subcellular location: Endoplasmic reticulum membrane; Peripheral membrane protein; Cytoplasmic side. Golgi apparatus membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}; Cytoplasmic side {ECO:0000250}. Cell membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}; Cytoplasmic side {ECO:0000250}. Cytoplasm, cytosol. Note=Isoform 2 is not associated with membranes.
Interaction partners:
- Guanine nucleotide-binding protein G
- Guanine nucleotide-binding protein G
- Guanine nucleotide-binding protein G
- FERM and PDZ domain-containing protein 1
- G-protein-signaling modulator 3
- Protein inscuteable homolog
Sequence:
MASPAPPAAEELPGPAARRLYSRMEASCLELALEGERLCKAGDFKAGVAFFEAAVQVGTEDLKTLSAIYSQLGNAYFYLKEYARALQFHKHDLLLARTIGDRMGEAKASGNLGNTLKVLGRFDEAIVCCQRHLDIAQEQGDKVGEARALYNIGNVYHAKGKQLSWNAAQDPGHLPPDVRETLHRASEFYERNLSLVKELGDRAAQGRAYGNLGNTHYLLGNFTEATTFHKERLAIAKEFGDKAAERRAYSNLGNAHIFLGRFDVAAEHYKKTLQLSRQIRDQAVEAQACYSLGNTYTLLQDYERAAEYHLRHLVIAQELADRVGEGRACWSLGNAYVSMGSPAQALTFAKKHLQISQEIGDRNGELTARMNIAHLQLALGRLTSPAAAEKPDLAGYEAQGARPKRTQRLSAETWDLLRLPLDREQNGETHHTGDWRGPSRDSLPLPMRSRKYQEGPDAIERRPREGSHSPLDSADVRVQVPRTGIPRAPSSDEECFFDLLSKFQSSRMDDQRCPLEEGQAGAAEATAAPTLEERAAQPSVTASPQTEEFFDLIASSQSRRLDDQRASVGSLPGLRITLNNVGHLRGDGDPQEPGDEFFNMLIKYQSSRIDDQRCPPPDVLPRGPTMPDEDFFSLIQRVQAKRMDEQRVDLAGSPDQEASGLPDPRQQCPPGAS
Protein: PBX homeobox 1 (A0A8I5ZR45)
Organism: Rattus norvegicus (Rat)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123, ECO:0000256|PROSITE-ProRule:PRU00108}.
Interaction partners:
Sequence:
MDEQPRLMHSHAGVGMAGHPGLSQHLQDGAGGTEGEGGRKQDIGDILQQIMTITDQSLDEAQARKHALNCHRMKPALFNVLCEIKEKTVLSIRGAQEEEPTDPQLMRLDNMLLAEGVAGPEKGGGSAAAAAAAAASGGAGSDNSVEHSDYRAKLSQIRQIYHTELEKYEQACNEFTTHVMNLLREQSRTRPISPKEIERMVSIIHRKFSSIQMQLKQSTCEAVMILRSRFLDARRKRRNFNKQATEILNEYFYSHLSNPYPSEEAKEELAKKCGITVSQVSNWFGNKRIRYKKNIGKFQEEANIYAAKTAVTATNVSAHGSQANSPSTPNSAGSSSSFNMSNSGDLFMSVQSLNGDSYQGAQVGANVQSQVDTLRHVISQTGGYSDGLAASQMYSPQGISANGGWQDATTPSSVTSPTEGPGSVHSDTSN
Protein: Dynein regulatory complex protein 9 (Flagellar associated protein 122) (A8HQ54)
Organism: Chlamydomonas reinhardtii (Chlamydomonas smithii)
Function: Component of the nexin-dynein regulatory complex (N-DRC), a key regulator of ciliary/flagellar motility which maintains the alignment and integrity of the distal axoneme and regulates microtubule sliding in motile axonemes.
Subcellular location: Cytoplasm, cytoskeleton, flagellum axoneme {ECO:0000269|PubMed:23427265, ECO:0000269|PubMed:25411337}.
Interaction partners:
Sequence:
MVGIDTGGKIPPEIMRQATEKTAQLAPLEGGHIYSILKQTLEKLALVGQLQVDPKVQAHELTQSVGEEISRMITEQKKLESRFEELVALQHVLRHQPNKTKLMENQVASERQALQLLLSNCLNEIEVFGKVQPLVESVMAQQAAEQAMKETIEREKNTTAAVRQLRNDLREEKLDHEEKMKEKKKGLSTLKEQLKALKMDTAVSTRYLSKDLTAGNEHERRLQRTQLEDLLKDLGLVQQQIDIEKAVHATQAEFLRQIAAKMADDSSNWASRHDGDLAAREKELEMLKQQHARDLIELKKAEEKFKMEQALKKEREMKATEERERAEFEEMRETRRAQAAVIIQAWWRGHKVRMVMSGGGKKGAKKGGAKKKK
Protein: TBC1 domain family member 20 (Q96BZ9)
Organism: Homo sapiens (Human)
Function: GTPase-activating protein specific for Rab1 and Rab2 small GTPase families for which it can accelerate the intrinsic GTP hydrolysis rate by more than five orders of magnitude. Involved in maintaining endoplasmic reticulum structure.
Subcellular location: Membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}.
Interaction partners:
- Ras-related protein Rab-1B
- Ubiquitin carboxyl-terminal hydrolase 6
- Ras-related protein Rab-1A
- Cell division cycle protein 16 homolog
- Rab3 GTPase-activating protein non-catalytic subunit
- Ras-related protein Rab-18
- Rab3 GTPase-activating protein catalytic subunit
- TBC1 domain family member 23
Sequence:
MALRSAQGDGPTSGHWDGGAEKADFNAKRKKKVAEIHQALNSDPTDVAALRRMAISEGGLLTDEIRRKVWPKLLNVNANDPPPISGKNLRQMSKDYQQVLLDVRRSLRRFPPGMPEEQREGLQEELIDIILLILERNPQLHYYQGYHDIVVTFLLVVGERLATSLVEKLSTHHLRDFMDPTMDNTKHILNYLMPIIDQVNPELHDFMQSAEVGTIFALSWLITWFGHVLSDFRHVVRLYDFFLACHPLMPIYFAAVIVLYREQEVLDCDCDMASVHHLLSQIPQDLPYETLISRAGDLFVQFPPSELAREAAAQQQAERTAASTFKDFELASAQQRPDMVLRQRFRGLLRPEDRTKDVLTKPRTNRFVKLAVMGLTVALGAAALAVVKSALEWAPKFQLQLFP
Protein: CCR4-NOT transcription complex subunit 10 (Q9H9A5)
Organism: Homo sapiens (Human)
Function: Component of the CCR4-NOT complex which is one of the major cellular mRNA deadenylases and is linked to various cellular processes including bulk mRNA degradation, miRNA-mediated repression, translational repression during translational initiation and general transcription regulation. Additional complex functions may be a consequence of its influence on mRNA expression. Is not required for association of CNOT7 to the CCR4-NOT complex.
Subcellular location: Cytoplasm {ECO:0000305}. Nucleus {ECO:0000305}.
Interaction partners:
- CCR4-NOT transcription complex subunit 9
- CCR4-NOT transcription complex subunit 7
- CCR4-NOT transcription complex subunit 2
- CCR4-NOT transcription complex subunit 3
- CCR4-NOT transcription complex subunit 6
- CCR4-NOT transcription complex subunit 1
- CCR4-NOT transcription complex subunit 11
- CCR4-NOT transcription complex subunit 6-like
- CCR4-NOT transcription complex subunit 8
- 182 kDa tankyrase-1-binding protein
Sequence:
MAADKPADQGAEKHEGTGQSSGITDQEKELSTNAFQAFTSGNYDACLQHLACLQDINKDDYKIILNTAVAEFFKSNQTTTDNLRQTLNQLKNQVHSAVEEMDGLDDVENSMLYYNQAVILYHLRQYTEAISVGEKLYQFIEPFEEKFAQAVCFLLVDLYILTYQAEKALHLLAVLEKMISQGNNNKNGKNETGNNNNKDGSNHKAESGALIEAAKSKIHQYKVRAYIQMKSLKACKREIKSVMNTAGNSAPSLFLKSNFEYLRGNYRKAVKLLNSSNIAEHPGFMKTGECLRCMFWNNLGCIHFAMSKHNLGIFYFKKALQENDNVCAQLSAGSTDPGKKFSGRPMCTLLTNKRYELLYNCGIQLLHIGRPLAAFECLIEAVQVYHANPRLWLRLAECCIAANKGTSEQETKGLPSKKGIVQSIVGQGYHRKIVLASQSIQNTVYNDGQSSAIPVASMEFAAICLRNALLLLPEEQQDPKQENGAKNSNQLGGNTESSESSETCSSKSHDGDKFIPAPPSSPLRKQELENLKCSILACSAYVALALGDNLMALNHADKLLQQPKLSGSLKFLGHLYAAEALISLDRISDAITHLNPENVTDVSLGISSNEQDQGSDKGENEAMESSGKRAPQCYPSSVNSARTVMLFNLGSAYCLRSEYDKARKCLHQAASMIHPKEVPPEAILLAVYLELQNGNTQLALQIIKRNQLLPAVKTHSEVRKKPVFQPVHPIQPIQMPAFTTVQRK
Protein: RNA-binding (RRM/RBD/RNP motifs) family protein (Ribonucleoprotein-like) (Similarity to RNA binding protein) (Q9FM47)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
- tRNA
- tRNA
Sequence:
MDPYGTETVIEDEIHDPKPSEDIEDDDDKSQPHSGGGVDSAGKIFVGGLARETTSAEFLKHFGKYGEITDSVIMKDRKTGQPRGFGFVTYADSSVVDKVIQDNHIIIGKQVEIKRTIPRGSMSSNDFKTKKIFVGGIPSSVDDDEFKEFFMQFGELKEHQIMRDHSTGRSRGFGFVTYESEDMVDHLLAKGNRIELSGTQVEIKKAEPKKPNSVTTPSKRFGDSRSNFGGGYGDGYGGGHGGGYGGPGGPYKSGGGYGGGRSGGYGGYGGEFGGYGGGGYGGGVGPYRGEPALGYSGRYGGGGGGYNRGGYSMGGGGGYGGGPGDMYGGSYGEPGGGYGGPSGSYGGGYGSSGIGGYGGGMGGAGGGGYRGGGGYDMGGVGGGGAGGYGAGGGGNGGGSFYGGGGGRGGYGGGGSGRYHPYGR