wanglab/gogpt-training-data huggingface dataset:
Protein: Collagen alpha-1(II) chain (Alpha-1 type II collagen) [Cleaved into: Collagen alpha-1(II) chain; Chondrocalcin] (P02458)
Organism: Homo sapiens (Human)
Function: Type II collagen is specific for cartilaginous tissues. It is essential for the normal embryonic development of the skeleton, for linear growth and for the ability of cartilage to resist compressive forces.
Subcellular location: Secreted, extracellular space, extracellular matrix {ECO:0000255|PROSITE-ProRule:PRU00793}.
Interaction partners:
- Collagen alpha-1
- Collagen alpha-2
- Transcription factor SOX-9
- CD44 antigen
- Collagen alpha-1
- Platelet glycoprotein VI
- Collagen alpha-2
- Collagen alpha-2
- Collagen alpha-1
- Collagen alpha-1
Sequence:
MIRLGAPQTLVLLTLLVAAVLRCQGQDVQEAGSCVQDGQRYNDKDVWKPEPCRICVCDTGTVLCDDIICEDVKDCLSPEIPFGECCPICPTDLATASGQPGPKGQKGEPGDIKDIVGPKGPPGPQGPAGEQGPRGDRGDKGEKGAPGPRGRDGEPGTPGNPGPPGPPGPPGPPGLGGNFAAQMAGGFDEKAGGAQLGVMQGPMGPMGPRGPPGPAGAPGPQGFQGNPGEPGEPGVSGPMGPRGPPGPPGKPGDDGEAGKPGKAGERGPPGPQGARGFPGTPGLPGVKGHRGYPGLDGAKGEAGAPGVKGESGSPGENGSPGPMGPRGLPGERGRTGPAGAAGARGNDGQPGPAGPPGPVGPAGGPGFPGAPGAKGEAGPTGARGPEGAQGPRGEPGTPGSPGPAGASGNPGTDGIPGAKGSAGAPGIAGAPGFPGPRGPPGPQGATGPLGPKGQTGEPGIAGFKGEQGPKGEPGPAGPQGAPGPAGEEGKRGARGEPGGVGPIGPPGERGAPGNRGFPGQDGLAGPKGAPGERGPSGLAGPKGANGDPGRPGEPGLPGARGLTGRPGDAGPQGKVGPSGAPGEDGRPGPPGPQGARGQPGVMGFPGPKGANGEPGKAGEKGLPGAPGLRGLPGKDGETGAAGPPGPAGPAGERGEQGAPGPSGFQGLPGPPGPPGEGGKPGDQGVPGEAGAPGLVGPRGERGFPGERGSPGAQGLQGPRGLPGTPGTDGPKGASGPAGPPGAQGPPGLQGMPGERGAAGIAGPKGDRGDVGEKGPEGAPGKDGGRGLTGPIGPPGPAGANGEKGEVGPPGPAGSAGARGAPGERGETGPPGPAGFAGPPGADGQPGAKGEQGEAGQKGDAGAPGPQGPSGAPGPQGPTGVTGPKGARGAQGPPGATGFPGAAGRVGPPGSNGNPGPPGPPGPSGKDGPKGARGDSGPPGRAGEPGLQGPAGPPGEKGEPGDDGPSGAEGPPGPQGLAGQRGIVGLPGQRGERGFPGLPGPSGEPGKQGAPGASGDRGPPGPVGPPGLTGPAGEPGREGSPGADGPPGRDGAAGVKGDRGETGAVGAPGAPGPPGSPGPAGPTGKQGDRGEAGAQGPMGPSGPAGARGIQGPQGPRGDKGEAGEPGERGLKGHRGFTGLQGLPGPPGPSGDQGASGPAGPSGPRGPPGPVGPSGKDGANGIPGPIGPPGPRGRSGETGPAGPPGNPGPPGPPGPPGPGIDMSAFAGLGPREKGPDPLQYMRADQAAGGLRQHDAEVDATLKSLNNQIESIRSPEGSRKNPARTCRDLKLCHPEWKSGDYWIDPNQGCTLDAMKVFCNMETGETCVYPNPANVPKKNWWSSKSKEKKHIWFGETINGGFHFSYGDDNLAPNTANVQMTFLRLLSTEGSQNITYHCKNSIAYLDEAAGNLKKALLIQGSNDVEIRAEGNSRFTYTALKDGCTKHTGKWGKTVIEYRSQKTSRLPIIDIAPMDIGGPEQEFGVDIGPVCFL
Protein: Fused isobutyryl-CoA mutase [Includes: Isobutyryl-CoA mutase (ICM) (EC 5.4.99.13); P-loop GTPase (EC 3.6.5.-) (G-protein chaperone)] (Q5Z110)
Organism: Nocardia farcinica (strain IFM 10152)
Function: Catalyzes the reversible interconversion of isobutyryl-CoA and n-butyryl-CoA, using radical chemistry. Also exhibits GTPase activity, associated with its G-protein domain (MeaI) that functions as a chaperone that assists cofactor delivery and proper holo-enzyme assembly (By similarity). Does not exhibit methylmalonyl-CoA mutase (MCM) activity.
Interaction partners:
- Probable methylmalonyl-CoA mutase large subunit
- methylmalonyl-CoA mutase
- Putative 2-oxoglutarate ferredoxin oxidoreductase alpha subunit
- VOC domain-containing protein
- Methionine synthase
- Putative transporter ATPase/kinase
- Putative acetyl-CoA carboxylase beta subunit
- Putative pyruvate carboxylase
- Putative fatty acid synthase
- Cobalamin-binding protein
Sequence:
MADSTLHQPAYPVRFVTSAALFDGHDAAINIMRRILQSQGAEVIHLGHNRAVHEVVAAAVEEDVQGVAVSSYQGGHVEYFEYLASALRDAGAGHVRVFGGGGGVIVPEEIERLARSGVRIFSPEDGQRLGLPGMINELIQTCDVDLTGERPAVEAVLAGERTALARVITCLQQDALPAADRDALLAAARDRTVPVLGITGTGGSGKSSLTDELVRRLRTDQQDKLRVAILAVDPTRRRGGGALLGDRIRMNSLDGTHVFFRSLATRGGHELPHDIDAVIAACKAAGYDLVILETPGIGQGDAAIVDHVDVAMYVMTPEFGAASQLEKIDMLDFADVVAINKFERRGGADAVRDVSRQLLRNREAFGADPADMPVFGTSAATFNDDGVTALYQHLLELLGARGLPVDEGVLPRVQTRVSTRFAQIIPTARVRYLAEIADTVRTYHARTRDQVAAAQRVQRLELVAAELPGDAAVADLLARARAELDPENAALLARWPEVAESYRGPEQVVRVRDREIRTTLRRESLSGSSIPRVALPRFTDHGELLRFLRSENLPGHFPFTAGVFPFKRDNEDPARMFAGEGDPFRTNRRFKVLSEHSEAKRLSTAFDSVTLYGRDPDERPDIYGKVGTSGVSIATVDDMKALYDGFDLTAPTTSVSMTINGPAPTILAFFLNTAIDQALDRFRAAEGREPTADEAADLRARTLATVRGTVQADILKEDQGQNTCIFSTEFSLRMMADIQEWFVRNKVRNFYSVSISGYHIAEAGANPISQLAFTLANGFTYVEAYLARGMHIDDFAPNLSFFFSNGMDPEYSVIGRVARRIWAIALRDKYGAAERSQKLKYHVQTSGRSLHAQEMNFNDIRTTLQALIAIYDNCNSLHTNAYDEAVTTPTEDSVRRALAIQLIINREWGLAMNENPLQGSFIIDELTDLAEEAVLTEFERISERGGVLGAMETGYQRGKIQDESMLYEHRKHDGSLPIIGVNTFRNPHGEPERTLELARATEREKQSQLDRVREFQRRHRTQAQAALARLEEVARTDENIFEVLMDAARVCSLQQVTETFFTVGGQYRRNV
Protein: Casein kinase I homolog 1 (EC 2.7.11.1) (P40233)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Casein kinases are operationally defined by their preferential utilization of acidic proteins such as caseins as substrates.
Subcellular location: Cytoplasm.
Interaction partners:
- Casein kinase I homolog 3
- Pheromone P-factor receptor
- Casein kinase I homolog 2
- Pheromone M-factor receptor
- Meiotic recombination protein rec8
- Meiotic recombination protein rec11
- Separin
- Linear element protein rec10
Sequence:
MSGQNNVVGVHYKVGRRIGEGSFGVIFEGTNLLNNQQVAIKFEPRRSDAPQLRDEYRTYKLLAGCTGIPNVYYFGQEGLHNILVIDLLGPSLEDLLDLCGRKFSVKTVAMAAKQMLARVQSIHEKSLVYRDIKPDNFLIGRPNSKNANMIYVVDFGMVKFYRDPVTKQHIPYREKKNLSGTARYMSINTHLGREQSRRDDLEALGHVFMYFLRGSLPWQGLKAATNKQKYERIGEKKQSTPLRELCAGFPEEFYKYMHYARNLAFDATPDYDYLQGLFSKVLERLNTTEDENFDWNLLNNGKGWQSLKSRNAETENQRSSKPPAPKLESKSPALQNHASTQNVVSKRSDYEKPFAEPHLNSASDSAEPNQNSLPNPPTETKATTTVPDRSGLATNQPAPVDVHDSSEERVTREQVQNATKETEAPKKKKSFWASILSCCSGSNEDT
Protein: Methionine synthase (EC 2.1.1.13) (5-methyltetrahydrofolate--homocysteine methyltransferase) (Methionine synthase, vitamin-B12-dependent) (MS) (P13009)
Organism: Escherichia coli (strain K12)
Function: Catalyzes the transfer of a methyl group from methyl-cobalamin to homocysteine, yielding enzyme-bound cob(I)alamin and methionine. Subsequently, remethylates the cofactor using methyltetrahydrofolate.
Interaction partners:
- 5,10-methylenetetrahydrofolate reductase
- 5-methyltetrahydropteroyltriglutamate--homocysteine methyltransferase
- Cystathionine gamma-synthase
- S-adenosylmethionine synthase
- Cystathionine beta-lyase MetC
- Serine hydroxymethyltransferase
- Aminomethyltransferase
- Bifunctional aspartokinase/homoserine dehydrogenase 2
- Bifunctional aspartokinase/homoserine dehydrogenase 1
- S-ribosylhomocysteine lyase
Sequence:
MSSKVEQLRAQLNERILVLDGGMGTMIQSYRLNEADFRGERFADWPCDLKGNNDLLVLSKPEVIAAIHNAYFEAGADIIETNTFNSTTIAMADYQMESLSAEINFAAAKLARACADEWTARTPEKPRYVAGVLGPTNRTASISPDVNDPAFRNITFDGLVAAYRESTKALVEGGADLILIETVFDTLNAKAAVFAVKTEFEALGVELPIMISGTITDASGRTLSGQTTEAFYNSLRHAEALTFGLNCALGPDELRQYVQELSRIAECYVTAHPNAGLPNAFGEYDLDADTMAKQIREWAQAGFLNIVGGCCGTTPQHIAAMSRAVEGLAPRKLPEIPVACRLSGLEPLNIGEDSLFVNVGERTNVTGSAKFKRLIKEEKYSEALDVARQQVENGAQIIDINMDEGMLDAEAAMVRFLNLIAGEPDIARVPIMIDSSKWDVIEKGLKCIQGKGIVNSISMKEGVDAFIHHAKLLRRYGAAVVVMAFDEQGQADTRARKIEICRRAYKILTEEVGFPPEDIIFDPNIFAVATGIEEHNNYAQDFIGACEDIKRELPHALISGGVSNVSFSFRGNDPVREAIHAVFLYYAIRNGMDMGIVNAGQLAIYDDLPAELRDAVEDVILNRRDDGTERLLELAEKYRGSKTDDTANAQQAEWRSWEVNKRLEYSLVKGITEFIEQDTEEARQQATRPIEVIEGPLMDGMNVVGDLFGEGKMFLPQVVKSARVMKQAVAYLEPFIEASKEQGKTNGKMVIATVKGDVHDIGKNIVGVVLQCNNYEIVDLGVMVPAEKILRTAKEVNADLIGLSGLITPSLDEMVNVAKEMERQGFTIPLLIGGATTSKAHTAVKIEQNYSGPTVYVQNASRTVGVVAALLSDTQRDDFVARTRKEYETVRIQHGRKKPRTPPVTLEAARDNDFAFDWQAYTPPVAHRLGVQEVEASIETLRNYIDWTPFFMTWSLAGKYPRILEDEVVGVEAQRLFKDANDMLDKLSAEKTLNPRGVVGLFPANRVGDDIEIYRDETRTHVINVSHHLRQQTEKTGFANYCLADFVAPKLSGKADYIGAFAVTGGLEEDALADAFEAQHDDYNKIMVKALADRLAEAFAEYLHERVRKVYWGYAPNENLSNEELIRENYQGIRPAPGYPACPEHTEKATIWELLEVEKHTGMKLTESFAMWPGASVSGWYFSHPDSKYYAVAQIQRDQVEDYARRKGMSVTEVERWLAPNLGYDAD
Protein: IP11858p (Q9VBS9)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
- EG:BACR43E12.1 protein
- Chitin-binding type-2 domain-containing protein
Sequence:
MAEESFNDDELNPPEWLNVQFMTQVLRGYEKDSNLKVINLSFTPASAKGDHYASIMFRARVEYTAQNGNFTKSLIIKTMIVEEGIKKDMFKDSPLFTTEIGMYTKVLPEWERILRRANDPAKLYVECIYHSLQPHQILIFDDLVEMGYAVVRDRFLTREEISSAYSKLAKIHAISMKFIHEQPEYLKEFKNGLCEMPGLIDSSIISGGMDPFMEMLGRIPELSKYQPHFKKISLHFKDRLRETMQEYRNNPQPGYNVLCHADFHSRNMMFKNNKETGCFEDCMLLDYQGCNVAPMAVDLMYSIYMLMGPAQRREELDILLNYYLSILLETLKKIGYQGSMPTEQGFWAEMKRHRYYEFLLLSTFLPVSIGLRTHKLDIGDMMHNEETRKKLYQLEDFMEETKSILDRFQKSGYFDDF
Protein: A kinase anchor protein 10 isoform 5 (A0A0S2Z551)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MRGAGPSPRQSPRTLRPDPGPAMSFFRRKVKGKEQEKTSDVKSIKGSMFSQAMKKWVQGNTDEAQEELAWKIAKMIVSDIMQQAQYDQPLEKSTKL
Protein: RalA-binding protein 1 (RalBP1) (Cytocentrin) (Dinitrophenyl S-glutathione ATPase) (DNP-SG ATPase) (EC 7.6.2.2, EC 7.6.2.3) (Ral-interacting protein 1) (Q62796)
Organism: Rattus norvegicus (Rat)
Function: Multifunctional protein that functions as a downstream effector of RALA and RALB. As a GTPase-activating protein/GAP can inactivate CDC42 and RAC1 by stimulating their GTPase activity. As part of the Ral signaling pathway, may also regulate ligand-dependent EGF and insulin receptors-mediated endocytosis. During mitosis, may act as a scaffold protein in the phosphorylation of EPSIN/EPN1 by the mitotic kinase cyclin B-CDK1, preventing endocytosis during that phase of the cell cycle. During mitosis, also controls mitochondrial fission as an effector of RALA. Recruited to mitochondrion by RALA, acts as a scaffold to foster the mitotic kinase cyclin B-CDK1-mediated phosphorylation and activation of DNM1L (By similarity).
Subcellular location: Cell membrane {ECO:0000250|UniProtKB:Q15311}; Peripheral membrane protein {ECO:0000250|UniProtKB:Q15311}. Cytoplasm, cytosol {ECO:0000269|PubMed:9973605}. Cytoplasm, cytoskeleton, spindle pole {ECO:0000269|PubMed:9973605}. Nucleus {ECO:0000250|UniProtKB:Q15311}. Mitochondrion {ECO:0000250|UniProtKB:Q15311}. Note=Cytosolic protein that transiently associates with the mitotic spindle poles in early prophase, and dissociates from them after completion of mitosis (PubMed:9973605). Targeted to the plasma membrane through its interaction with RALB, directed by FGF signaling. Docking on the membrane is required to transduce the Ral signal (By similarity). Recruited by RALA to the mitochondrion during mitosis where it regulates mitochondrial fission. Nuclear localization is cell cycle dependent while membrane localization is seen in adherent cells. The region involved in membrane association could form transmembrane domains and expose a part of the protein extracellularly (By similarity). {ECO:0000250|UniProtKB:Q15311, ECO:0000250|UniProtKB:Q9PT60, ECO:0000269|PubMed:9973605}.
Interaction partners:
- Ras-related protein Ral-A
- Ras-related protein Ral-B
- Ras-related protein R-Ras
- Cell division control protein 42 homolog
- GTPase NRas
- GTPase HRas
- ADP-ribosylation factor 6
- Ras-related C3 botulinum toxin substrate 1
- RAS related 2
- Ras-related protein M-Ras
Sequence:
MTECFLPPTSSPSEHRRAEHGSGLTRTPSSEEISPTKFPELYRTGEPSPPHDILHEPPDIVSDDEKDHGKKKGKFKKKEKRTEGYVAFQEDSSGDEAESPSKMKRSKGIHVFKKPSFSKKKEKDFKIKEKPKEEKHKEEKHKEEKHKEKKCKDFTAADVVKQWKEKKKKKKPTQEPEVPQTDAPSLRPIFGAPFADAVERTMMYDGIRLPAVFRECVDYMEKHGMKCEGIYRVSGIKSKVDELKAAYDREESPNLEEYEPNTVASLLKQYLRDLPENLLTKELMPRFEEACGRTTEVEKVQEFQRLLRELPEYNHLLLSWLIVHMDHVIAKELETKMNIQNISIVLSPTVQISNRVLYVLFTHVQELFGTVLLKQVTRPLRWSNMATMPTLPETQAGIKEEIRRQEFLLNCLHRDLQGGIKDFSKEERLWEVQRILTALKRKLREAKRQECETKIAQEIASLSKEDVSKEETNENEEVINILLAQENEILTEQEELLAMEQFLRRQIASEKEEIDRLRAEIAEIQSRQHGRSETEEYSSDSESESEDEEELQIILEDLQRQNEELEIKNNHLNQAVHEEREAIVELRVQLRLLQMLRAKSEQQLQEEEEPERRGGTGPLPCEGVLEVRAAKEQAKPSPSKDRKETPI
Protein: Phosphomannomutase (AtPMM) (EC 5.4.2.8) (O80840)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Catalyzes the interconversion of mannose-6-phosphate to mannose-1-phosphate, the precursor for the synthesis of GDP-mannose. GDP-mannose is an essential sugar nucleotide for the synthesis of D-mannose-containing cell wall polysaccharides (galactomannans and glucomannans), glycolipids, glycoproteins and the antioxidant L-ascorbate (Probable). Can complement the yeast temperature-sensitive mutant sec53-6.
Subcellular location: Cytoplasm {ECO:0000250|UniProtKB:A0A0U1WZ18}.
Interaction partners:
- Mannose-6-phosphate isomerase 1
- Mannose-1-phosphate guanylyltransferase 1
- Mannose-6-phosphate isomerase 2
- ADP-glucose pyrophosphorylase family protein
- ADP-glucose pyrophosphorylase family protein
- Probable mannose-1-phosphate guanylyltransferase 2
- Probable mannose-1-phosphate guanylyltransferase 3
- Hexokinase-like 1 protein
- Hexokinase-1
- Probable hexokinase-like 2 protein
Sequence:
MAAKIPGVIALFDVDGTLTAPRKEATPELLDFIRELRKVVTIGVVGGSDLSKISEQLGKTVTNDYDYCFSENGLVAHKDGKSIGIQSLKLHLGDDKLKELINFTLHYIADLDIPIKRGTFIEFRNGMLNVSPIGRNCSQEERDEFERYDKVQNIRPKMVAELRERFAHLNLTFSIGGQISFDVFPKGWDKTYCLQYLEDFSEIHFFGDKTYEGGNDYEIYESPKTIGHSVTSPDDTVAKCKALFMS
Protein: 1,4-alpha-glucan branching enzyme TTHA1902 (EC 2.4.1.18) (1,4-alpha-D-glucan:1,4-alpha-D-glucan 6-glucosyl-transferase) (Alpha-(1->4)-glucan branching enzyme) (Branching enzyme) (BE) (Q5SH28)
Organism: Thermus thermophilus (strain ATCC 27634 / DSM 579 / HB8)
Function: Catalyzes the formation of branch points in alpha-glucans by cleavage of an alpha-1,4 glycosidic bond and subsequent transfer of the cleaved-off oligosaccharide to a new alpha-1,6 position. The branch chain-length distribution of the reaction products shows degree of polymerization (DP) of 3 to 13, with two local maxima at DP 7 and DP 11. Exhibits an alpha-retaining catalytic mechanism. Is involved in glycogen biosynthesis. Shows a secondary activity, i.e. the hydrolysis of the substrate, being 4% of the total activity. Can use amylose as substrate but not alpha-1,4-linked oligosaccharides of 2-7 glucose residues, beta-cyclodextrin, 6-O-glucosyl-beta-cyclodextrin and 6-O-maltosyl-beta-cyclodextrin. Is not able to branch amylopectin further, it only hydrolyzes amylopectin. Thus, displays preference for linear and long substrates (amylose) over branched structures (amylopectin).
Interaction partners:
Sequence:
MARFALVLHAHLPYVRAHGMWPFGEETLYEAMAETYLPLIRVLERLRAEGVEAPFTLGITPILAEQLADARIKEGFWAYAKDRLERAQGDYQRYRGTALEASARHQVAFWELTLDHFQRLSGDLVAAFRKAEEGGQVELITSNATHGYSPLLGYDEALWAQIKTGVSTYRRHFAKDPTGFWLPEMAYRPKGPWKPPVEGPPEGVRPGVDELLMRAGIRYTFVDAHLVQGGEPLSPYGEAALGPVESQEATYHVHELESGLRVLARNPETTLQVWSADYGYPGEGLYREFHRKDPLSGLHHWRVTHRKADLAEKAPYDPEAAFAKTEEHARHFVGLLERLAGRHPEGVILSPYDAELFGHWWYEGVAWLEAVLRLLAQNPKVRPVTAREAVQGPAVRTALPEGSWGRGGDHRVWLNEKTLDYWEKVYRAEGAMREAARRGVLPEGVLRQAMRELLLLEASDWPFLMETGQAEAYARERYEEHARAFFHLLKGASPEELRALEERDNPFPEADPRLYLFREA
Protein: Bitesize, isoform F (B7Z0K2)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MKQVTRLIGPRRMASSKPKEAPSYNAFASASTSSKKSQPASTAPAPLARVHNYGRVKSQPAGSSLPSSSAGKIQYAALNRMRKKRSEDEGKKLKRKSKWRQLFGQCWWKKRRRQRSYQDYWSSSREKSKKSHFFCYCCRRRTNGYGYDSEEEDDDIDAKVASYIVEMKQREAAANGQKEAKVAAEELSRSPVIGQRQADGSGSPIQSRASSETWPTQSDEDIDRLVAMHQNRSSLSSLGVRSESMASVYSGAGEGRYGTVVVKGQVEFAMQYNYKLSALEVHVVRCKDLAAVDAKRNRSDPYVKVYLLPDKSKAGKRKTKVKKHTLNPIFDETMRFHTPISSLESRTLWLTVWHSDMFGRNDFLGEVSVNLQGRLFDNPQSQWYLLQERSEPFDEVATYRGDIVVGLKYIPPENIKSSFFSRGSSITGSSSNLRKFGGSIKSVASKSERTSKGGQLHVLVKEAKHLSPIKANGTCDAFCKSYLLPDRTRSSKQKTPVVKRTLHPSWNYTFVYEDVSLEELSERALELTVWDHDRLASNEFVGGIRFSLGTGRSYGRQVEWMDATGKELSLWQNMLDRPNFWVEGSLVLRSSLDGIRANLP
Protein: Guanine nucleotide-binding protein G(i) subunit alpha-3 (G(i) alpha-3) (P08754)
Organism: Homo sapiens (Human)
Function: Heterotrimeric guanine nucleotide-binding proteins (G proteins) function as transducers downstream of G protein-coupled receptors (GPCRs) in numerous signaling cascades. The alpha chain contains the guanine nucleotide binding site and alternates between an active, GTP-bound state and an inactive, GDP-bound state. Signaling by an activated GPCR promotes GDP release and GTP binding. The alpha subunit has a low GTPase activity that converts bound GTP to GDP, thereby terminating the signal. Both GDP release and GTP hydrolysis are modulated by numerous regulatory proteins. Signaling is mediated via effector proteins, such as adenylate cyclase. Inhibits adenylate cyclase activity, leading to decreased intracellular cAMP levels. Stimulates the activity of receptor-regulated K(+) channels. The active GTP-bound form prevents the association of RGS14 with centrosomes and is required for the translocation of RGS14 from the cytoplasm to the plasma membrane. May play a role in cell division.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:17635935}. Cell membrane {ECO:0000269|PubMed:17635935, ECO:0000269|PubMed:27864364}; Lipid-anchor {ECO:0000305}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000269|PubMed:17635935}. Note=Localizes in the centrosomes of interphase and mitotic cells. Detected at the cleavage furrow and/or the midbody. {ECO:0000269|PubMed:17635935}.
Interaction partners:
- Guanine nucleotide-binding protein G
- Guanine nucleotide-binding protein G
- Somatostatin receptor type 2
- Guanine nucleotide-binding protein subunit beta-4
- G-protein-signaling modulator 1
- Guanine nucleotide-binding protein G
- Guanine nucleotide-binding protein G
- Regulator of G-protein signaling 2
- Regulator of G-protein signaling 10
- Chaperone Ric-8A
Sequence:
MGCTLSAEDKAAVERSKMIDRNLREDGEKAAKEVKLLLLGAGESGKSTIVKQMKIIHEDGYSEDECKQYKVVVYSNTIQSIIAIIRAMGRLKIDFGEAARADDARQLFVLAGSAEEGVMTPELAGVIKRLWRDGGVQACFSRSREYQLNDSASYYLNDLDRISQSNYIPTQQDVLRTRVKTTGIVETHFTFKDLYFKMFDVGGQRSERKKWIHCFEGVTAIIFCVALSDYDLVLAEDEEMNRMHESMKLFDSICNNKWFTETSIILFLNKKDLFEEKIKRSPLTICYPEYTGSNTYEEAAAYIQCQFEDLNRRKDTKEIYTHFTCATDTKNVQFVFDAVTDVIIKNNLKECGLY
Protein: dITP/XTP pyrophosphatase (EC 3.6.1.66) (Non-canonical purine NTP pyrophosphatase) (Non-standard purine NTP pyrophosphatase) (Nucleoside-triphosphate diphosphatase) (Nucleoside-triphosphate pyrophosphatase) (NTPase) (O28046)
Organism: Archaeoglobus fulgidus (strain ATCC 49558 / DSM 4304 / JCM 9628 / NBRC 100126 / VC-16)
Function: Pyrophosphatase that catalyzes the hydrolysis of nucleoside triphosphates to their monophosphate derivatives, with a high preference for the non-canonical purine nucleotides xanthosine triphosphate (XTP), deoxyinosine triphosphate (dITP) and ITP. Probably functions as a house-cleaning enzyme that removes non-canonical purine nucleotides from the nucleotide pool, thus preventing their incorporation into DNA/RNA and avoiding chromosomal lesions. Shows very low activity on dGTP or dUTP, and has nearly no activity toward the canonical nucleotides ATP, CTP, and TTP.
Interaction partners:
- Nucleoside diphosphate kinase
- GMP synthase subunit B
- GMP synthase subunit A
- 5'-nucleotidase SurE
- Small ribosomal subunit protein eS1
- Exosome complex component Rrp41
- Dihydropteroate synthase
- Adenylosuccinate synthetase
- Phosphoesterase
- Phosphoesterase
Sequence:
MYFITSNEGKFREVREMASKYGIEIEWLKMEYIEPQGSSLEEIARLSAEMLAEKVEGEFVIEDSGLFVEALKGFPGPYSSYVFKTIGNEGILKLMEGVENRKAYFMAVVAYFDGKEVRTFTGKVEGEISREMRGTQGFGYDPIFLYGNKTFAEMATEEKNQVSHRRKAFEEFFRWLKENKI
Protein: Ribosomal protein S6 kinase beta (EC 2.7.11.1) (Q9NAH6)
Organism: Caenorhabditis elegans
Function: Serine/threonine-protein kinase which regulates mRNA translation. Negatively regulates lifespan and resistance to starvation, oxidative stress, protein aggregation and P.aeruginosa-mediated infection. May regulate these processes by preventing the activation of transcription factor hif-1. Required, probably downstream of let-363/TOR, for the establishment of the proper number of germline progenitors by promoting cell cycle progression and preventing differentiation during larval development. Regulates germ cell size. In addition required for sperm production and embryo viability. Involved in axon regeneration of PLM and ALM neurons by inhibiting growth cone formation early after axotomy and later by inhibiting axon extension. Functions in axon regeneration and lifespan probably by preventing aak-2/AMPK activation. Negatively regulates autophagy.
Subcellular location: Cell projection, axon {ECO:0000269|PubMed:24431434}. Perikaryon {ECO:0000269|PubMed:24431434}. Note=Enriched in the synaptic branch of PLM neurons. {ECO:0000269|PubMed:24431434}.
Interaction partners:
- Target of rapamycin homolog
- DAF-15
- Defective pharyngeal development protein 4
- Small ribosomal subunit protein eS6
- 5'-AMP-activated protein kinase catalytic subunit alpha-2
- Target of rapamycin complex subunit lst8
- 5'-AMP-activated protein kinase catalytic subunit alpha-1
- GTP-binding protein
- Serine/threonine-protein phosphatase 2A catalytic subunit
- cAMP-dependent protein kinase regulatory subunit
Sequence:
MADVFEFELEGHESQASPQRHAYHYDNCTEIMEDDHMYSNVADGQISAPPPSSSYMEDPMMESIQLCASAINPPNVRVGPEDFQLLKVLGKGGYGKVFQVRKTTGSDNGQIFAMKVLQKATIVRNQKDTAHTKAERNILEAVKSPFICDLLYAFQTGGKLYLILEYLSGGELFMHLEREGMFMENVAKFYLSEIVVSLEHLHQQGIIYRDLKPENILLDAYGHVKLTDFGLCKEEIEGDQKTHTFCGTIEYMAPEILMRCGHGKAVDWWSLGALMFDMLTGGPPFTAENRRKTIDKILKGRLTLPAYLSNEARDLIKKLLKRHVDTRLGAGLSDAEEIKSHAFFKTTDWNLVYARQLEAPFKPNIENDEDTSLFDARFTKMTPVDSPCETNFSLNGDNPFVGFTYVAPSVLEMMNKGGHGGISVAHLASSMSRAGAAKSPRKPGDPETASILHGGHSNLFGHGPNSEAPQAFGYGIGSQMTTTTAGGAGIQQPYQSFSGGYPEDDAMDTSTPRASESRETTTGNGSTTTTRPSNVGSSASTPIPLPKRVM
Protein: NEK6-subfamily protein kinase (EC 2.7.11.34) (Q5TBG7)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MAGQPGHMPHGGSSNNLCHTLGPVHPPDPQRHPNTLSFRCSLADFQIEKKIGRGQFSEVYKATCLLDRKTVALKKVQIFEMMDAKARQDCVKEIGLLKQLNHPNIIKYLDSFIEDNELNIVLELADAGDLSQMIKYFKKQKRLIPERTVWKYFVQLCSAVEHMHSRRVMHRDIKPANVFITATGVVKLGDLGLGRFFSSETTAAHSLVGTPYYMSPERI
Protein: Chloride voltage-gated channel 3 (D6RIX3)
Organism: Homo sapiens (Human)
Subcellular location: Cell membrane {ECO:0000256|ARBA:ARBA00004651}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004651}.
Interaction partners:
Sequence:
MESEQLFHRGYYRNSYNSITSASSDEELLDGAGVIMDFQTSEDDNLLDGDTAVGTHYTMTNGGSINSSTHLLDLLDEPIPGVGTYDDFHTIDWVREKCKDRERHRRINSKKKESAWEMTKSLYDAWSGWLVVTLTGLA
Protein: 3-oxoacyl-[acyl-carrier-protein] synthase, mitochondrial (EC 2.3.1.41) (Beta-ketoacyl-ACP synthase) (Q9NWU1)
Organism: Homo sapiens (Human)
Function: May play a role in the biosynthesis of lipoic acid as well as longer chain fatty acids required for optimal mitochondrial function.
Subcellular location: Mitochondrion {ECO:0000269|PubMed:15668256}.
Interaction partners:
- Malonyl-CoA-acyl carrier protein transacylase, mitochondrial
- Acyl carrier protein, mitochondrial
- 3-oxoacyl-[acyl-carrier-protein] reductase
- Enoyl-[acyl-carrier-protein] reductase, mitochondrial
- (3R)-3-hydroxyacyl-CoA dehydrogenase (17-beta-hydroxysteroid dehydrogenase 8) (17-beta-HSD 8) (HSD17B8) (KAR alpha subunit) (Estradiol 17-beta-dehydrogenase 8) (Protein Ke6) (Ke6) (Testosterone 17-beta-dehydrogenase 8)
- Partner and localizer of BRCA2
- Fatty acid synthase
- Very long chain fatty acid elongase 6
- Lipoyl amidotransferase LIPT1, mitochondrial
- Octanoyl-[acyl-carrier-protein]:protein N-octanoyltransferase LIPT2, mitochondrial
Sequence:
MSNCLQNFLKITSTRLLCSRLCQQLRSKRKFFGTVPISRLHRRVVITGIGLVTPLGVGTHLVWDRLIGGESGIVSLVGEEYKSIPCSVAAYVPRGSDEGQFNEQNFVSKSDIKSMSSPTIMAIGAAELAMKDSGWHPQSEADQVATGVAIGMGMIPLEVVSETALNFQTKGYNKVSPFFVPKILVNMAAGQVSIRYKLKGPNHAVSTACTTGAHAVGDSFRFIAHGDADVMVAGGTDSCISPLSLAGFSRARALSTNSDPKLACRPFHPKRDGFVMGEGAAVLVLEEYEHAVQRRARIYAEVLGYGLSGDAGHITAPDPEGEGALRCMAAALKDAGVQPEEISYINAHATSTPLGDAAENKAIKHLFKDHAYALAVSSTKGATGHLLGAAGAVEAAFTTLACYYQKLPPTLNLDCSEPEFDLNYVPLKAQEWKTEKRFIGLTNSFGFGGTNATLCIAGL
Protein: Large ribosomal subunit protein eL34 (60S ribosomal protein L34) (Q9D1R9)
Organism: Mus musculus (Mouse)
Function: Component of the large ribosomal subunit. The ribosome is a large ribonucleoprotein complex responsible for the synthesis of proteins in the cell.
Subcellular location: Cytoplasm, cytosol {ECO:0000250|UniProtKB:P49207}. Cytoplasm {ECO:0000269|PubMed:36517592}. Endoplasmic reticulum {ECO:0000250|UniProtKB:Q29223}. Note=Detected on cytosolic polysomes (By similarity). Detected in ribosomes that are associated with the rough endoplasmic reticulum (By similarity). {ECO:0000250|UniProtKB:P49207, ECO:0000250|UniProtKB:Q29223}.
Interaction partners:
- Large ribosomal subunit protein eL8
- Large ribosomal subunit protein uL3
- Large ribosomal subunit protein uL10
- Small ribosomal subunit protein RACK1
- Large ribosomal subunit protein eL27
- Large ribosomal subunit protein uL15
- Large ribosomal subunit protein eL30
- Small ribosomal subunit protein eS8
- Ubiquitin-like protein FUBI
- Large ribosomal subunit protein uL29
Sequence:
MVQRLTYRRRLSYNTASNKTRLSRTPGNRIVYLYTKKVGKAPKSACGVCPGRLRGVRAVRPKVLMRLSKTQKHVSRAYGGSMCAKCVRDRIKRAFLIEEQKIVVKVLKAQAQSQKAK