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GSK3A_MOUSE
ID   GSK3A_MOUSE             Reviewed;         490 AA.
AC   Q2NL51;
DT   20-MAR-2007, integrated into UniProtKB/Swiss-Prot.
DT   20-MAR-2007, sequence version 2.
DT   03-AUG-2022, entry version 138.
DE   RecName: Full=Glycogen synthase kinase-3 alpha;
DE            Short=GSK-3 alpha;
DE            EC=2.7.11.26;
DE   AltName: Full=Serine/threonine-protein kinase GSK3A;
DE            EC=2.7.11.1 {ECO:0000269|PubMed:22539723};
GN   Name=Gsk3a;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6J;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA   Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA   Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA   Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA   Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA   Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of the
RT   mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 227-490.
RC   TISSUE=Eye;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA project:
RT   the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [3]
RP   INTERACTION WITH ARRB2.
RX   PubMed=16051150; DOI=10.1016/j.cell.2005.05.012;
RA   Beaulieu J.-M., Sotnikova T.D., Marion S., Lefkowitz R.J.,
RA   Gainetdinov R.R., Caron M.G.;
RT   "An Akt/beta-arrestin 2/PP2A signaling complex mediates dopaminergic
RT   neurotransmission and behavior.";
RL   Cell 122:261-273(2005).
RN   [4]
RP   FUNCTION, MUTAGENESIS OF SER-21, AND PHOSPHORYLATION AT SER-21.
RX   PubMed=15791206; DOI=10.1038/sj.emboj.7600633;
RA   McManus E.J., Sakamoto K., Armit L.J., Ronaldson L., Shpiro N., Marquez R.,
RA   Alessi D.R.;
RT   "Role that phosphorylation of GSK3 plays in insulin and Wnt signalling
RT   defined by knockin analysis.";
RL   EMBO J. 24:1571-1583(2005).
RN   [5]
RP   FUNCTION IN MCL1 PHOSPHORYLATION.
RX   PubMed=16543145; DOI=10.1016/j.molcel.2006.02.009;
RA   Maurer U., Charvet C., Wagman A.S., Dejardin E., Green D.R.;
RT   "Glycogen synthase kinase-3 regulates mitochondrial outer membrane
RT   permeabilization and apoptosis by destabilization of MCL-1.";
RL   Mol. Cell 21:749-760(2006).
RN   [6]
RP   FUNCTION IN AXON FORMATION, AND TISSUE SPECIFICITY.
RX   PubMed=17391670; DOI=10.1016/j.febslet.2007.03.018;
RA   Garrido J.J., Simon D., Varea O., Wandosell F.;
RT   "GSK3 alpha and GSK3 beta are necessary for axon formation.";
RL   FEBS Lett. 581:1579-1586(2007).
RN   [7]
RP   FUNCTION IN HEPATIC GLYCOGEN METABOLISM, AND DISRUPTION PHENOTYPE.
RX   PubMed=17908561; DOI=10.1016/j.cmet.2007.08.013;
RA   MacAulay K., Doble B.W., Patel S., Hansotia T., Sinclair E.M.,
RA   Drucker D.J., Nagy A., Woodgett J.R.;
RT   "Glycogen synthase kinase 3alpha-specific regulation of murine hepatic
RT   glycogen metabolism.";
RL   Cell Metab. 6:329-337(2007).
RN   [8]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Brain, Brown adipose tissue, Heart, Lung, Spleen, and Testis;
RX   PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA   Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA   Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT   "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL   Cell 143:1174-1189(2010).
RN   [9]
RP   FUNCTION, AND CATALYTIC ACTIVITY.
RX   PubMed=22539723; DOI=10.1126/science.1217032;
RA   Lin S.Y., Li T.Y., Liu Q., Zhang C., Li X., Chen Y., Zhang S.M., Lian G.,
RA   Liu Q., Ruan K., Wang Z., Zhang C.S., Chien K.Y., Wu J., Li Q., Han J.,
RA   Lin S.C.;
RT   "GSK3-TIP60-ULK1 signaling pathway links growth factor deprivation to
RT   autophagy.";
RL   Science 336:477-481(2012).
CC   -!- FUNCTION: Constitutively active protein kinase that acts as a negative
CC       regulator in the hormonal control of glucose homeostasis, Wnt signaling
CC       and regulation of transcription factors and microtubules, by
CC       phosphorylating and inactivating glycogen synthase (GYS1 or GYS2),
CC       CTNNB1/beta-catenin, APC and AXIN1 (PubMed:15791206, PubMed:17908561).
CC       Requires primed phosphorylation of the majority of its substrates
CC       (PubMed:22539723). Contributes to insulin regulation of glycogen
CC       synthesis by phosphorylating and inhibiting GYS1 activity and hence
CC       glycogen synthesis (PubMed:15791206, PubMed:17908561). Regulates
CC       glycogen metabolism in liver, but not in muscle (PubMed:17908561). May
CC       also mediate the development of insulin resistance by regulating
CC       activation of transcription factors (By similarity). In Wnt signaling,
CC       regulates the level and transcriptional activity of nuclear
CC       CTNNB1/beta-catenin (PubMed:15791206). Facilitates amyloid precursor
CC       protein (APP) processing and the generation of APP-derived amyloid
CC       plaques found in Alzheimer disease (By similarity). May be involved in
CC       the regulation of replication in pancreatic beta-cells (By similarity).
CC       Is necessary for the establishment of neuronal polarity and axon
CC       outgrowth (PubMed:17391670). Through phosphorylation of the anti-
CC       apoptotic protein MCL1, may control cell apoptosis in response to
CC       growth factors deprivation (PubMed:16543145). Acts as a regulator of
CC       autophagy by mediating phosphorylation of KAT5/TIP60 under starvation
CC       conditions, activating KAT5/TIP60 acetyltransferase activity and
CC       promoting acetylation of key autophagy regulators, such as ULK1 and
CC       RUBCNL/Pacer (PubMed:22539723). Negatively regulates extrinsic
CC       apoptotic signaling pathway via death domain receptors. Promotes the
CC       formation of an anti-apoptotic complex, made of DDX3X, BRIC2 and GSK3B,
CC       at death receptors, including TNFRSF10B. The anti-apoptotic function is
CC       most effective with weak apoptotic signals and can be overcome by
CC       stronger stimulation (By similarity). {ECO:0000250|UniProtKB:P49840,
CC       ECO:0000250|UniProtKB:P49841, ECO:0000269|PubMed:15791206,
CC       ECO:0000269|PubMed:16543145, ECO:0000269|PubMed:17391670,
CC       ECO:0000269|PubMed:17908561, ECO:0000269|PubMed:22539723}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + L-seryl-[tau protein] = ADP + H(+) + O-phospho-L-seryl-
CC         [tau protein]; Xref=Rhea:RHEA:12801, Rhea:RHEA-COMP:13701, Rhea:RHEA-
CC         COMP:13702, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616,
CC         ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.26;
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + L-threonyl-[tau protein] = ADP + H(+) + O-phospho-L-
CC         threonyl-[tau protein]; Xref=Rhea:RHEA:53904, Rhea:RHEA-COMP:13703,
CC         Rhea:RHEA-COMP:13704, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013,
CC         ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216;
CC         EC=2.7.11.26;
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-
CC         [protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-
CC         COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616,
CC         ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.1;
CC         Evidence={ECO:0000269|PubMed:22539723};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L-
CC         threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060,
CC         Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013,
CC         ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216;
CC         EC=2.7.11.1;
CC   -!- ACTIVITY REGULATION: Activated by phosphorylation at Tyr-279. In
CC       response to insulin, inhibited by phosphorylation at Ser-21 by
CC       PKB/AKT1; phosphorylation at this site causes a conformational change,
CC       preventing access of substrates to the active site. Inhibited by
CC       lithium.
CC   -!- SUBUNIT: Monomer. Interacts with AXIN1 and CTNNB1/beta-catenin (By
CC       similarity). Interacts with ARRB2 (PubMed:16051150). Interacts with
CC       CTNND2 (By similarity). Interacts with LMBR1L (By similarity).
CC       Interacts with DDX3X (By similarity). Interacts with TNFRSF10B (By
CC       similarity). {ECO:0000250|UniProtKB:P49840,
CC       ECO:0000269|PubMed:16051150}.
CC   -!- PTM: Phosphorylated by AKT1 at Ser-21: upon insulin-mediated signaling,
CC       the activated PKB/AKT1 protein kinase phosphorylates and deactivates
CC       GSK3A, resulting in the dephosphorylation and activation of GYS1.
CC       Activated by phosphorylation at Tyr-279. {ECO:0000269|PubMed:15791206}.
CC   -!- DISRUPTION PHENOTYPE: Enhanced glucose tolerance and insulin
CC       sensitivity, increased activity of hepatic glycogen synthase, elevated
CC       hepatic glycogen storage and reduced fat mass.
CC       {ECO:0000269|PubMed:17908561}.
CC   -!- SIMILARITY: Belongs to the protein kinase superfamily. CMGC Ser/Thr
CC       protein kinase family. GSK-3 subfamily. {ECO:0000305}.
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DR   EMBL; AC156992; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; BC111032; AAI11033.1; -; mRNA.
DR   CCDS; CCDS20976.1; -.
DR   RefSeq; NP_001026837.1; NM_001031667.1.
DR   AlphaFoldDB; Q2NL51; -.
DR   SMR; Q2NL51; -.
DR   BioGRID; 546781; 16.
DR   ComplexPortal; CPX-453; Beta-catenin destruction core complex, variant 5.
DR   ComplexPortal; CPX-456; Beta-catenin destruction core complex, variant 6.
DR   ComplexPortal; CPX-457; Beta-catenin destruction core complex, variant 7.
DR   ComplexPortal; CPX-458; Beta-catenin destruction core complex, variant 8.
DR   IntAct; Q2NL51; 2.
DR   STRING; 10090.ENSMUSP00000071654; -.
DR   ChEMBL; CHEMBL2176843; -.
DR   iPTMnet; Q2NL51; -.
DR   PhosphoSitePlus; Q2NL51; -.
DR   EPD; Q2NL51; -.
DR   jPOST; Q2NL51; -.
DR   MaxQB; Q2NL51; -.
DR   PaxDb; Q2NL51; -.
DR   PRIDE; Q2NL51; -.
DR   ProteomicsDB; 269640; -.
DR   Antibodypedia; 3833; 1230 antibodies from 49 providers.
DR   Ensembl; ENSMUST00000071739; ENSMUSP00000071654; ENSMUSG00000057177.
DR   GeneID; 606496; -.
DR   KEGG; mmu:606496; -.
DR   UCSC; uc009frx.1; mouse.
DR   CTD; 2931; -.
DR   MGI; MGI:2152453; Gsk3a.
DR   VEuPathDB; HostDB:ENSMUSG00000057177; -.
DR   eggNOG; KOG0658; Eukaryota.
DR   GeneTree; ENSGT00520000055635; -.
DR   InParanoid; Q2NL51; -.
DR   OMA; CLHAFFD; -.
DR   OrthoDB; 990896at2759; -.
DR   PhylomeDB; Q2NL51; -.
DR   TreeFam; TF101104; -.
DR   BRENDA; 2.7.11.26; 3474.
DR   BioGRID-ORCS; 606496; 4 hits in 74 CRISPR screens.
DR   ChiTaRS; Gsk3a; mouse.
DR   PRO; PR:Q2NL51; -.
DR   Proteomes; UP000000589; Chromosome 7.
DR   RNAct; Q2NL51; protein.
DR   Bgee; ENSMUSG00000057177; Expressed in motor neuron and 248 other tissues.
DR   ExpressionAtlas; Q2NL51; baseline and differential.
DR   Genevisible; Q2NL51; MM.
DR   GO; GO:0030424; C:axon; IBA:GO_Central.
DR   GO; GO:0030877; C:beta-catenin destruction complex; IC:ComplexPortal.
DR   GO; GO:0005737; C:cytoplasm; ISO:MGI.
DR   GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR   GO; GO:0005874; C:microtubule; ISO:MGI.
DR   GO; GO:0005739; C:mitochondrion; IEA:GOC.
DR   GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0034236; F:protein kinase A catalytic subunit binding; ISO:MGI.
DR   GO; GO:0004672; F:protein kinase activity; IDA:UniProtKB.
DR   GO; GO:0019901; F:protein kinase binding; ISO:MGI.
DR   GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA.
DR   GO; GO:0004674; F:protein serine/threonine kinase activity; IDA:MGI.
DR   GO; GO:0005102; F:signaling receptor binding; IPI:ARUK-UCL.
DR   GO; GO:0050321; F:tau-protein kinase activity; IEA:UniProtKB-EC.
DR   GO; GO:0007568; P:aging; ISO:MGI.
DR   GO; GO:0003214; P:cardiac left ventricle morphogenesis; IMP:BHF-UCL.
DR   GO; GO:0016477; P:cell migration; IGI:MGI.
DR   GO; GO:0071385; P:cellular response to glucocorticoid stimulus; IGI:ARUK-UCL.
DR   GO; GO:0032869; P:cellular response to insulin stimulus; ISO:MGI.
DR   GO; GO:0036016; P:cellular response to interleukin-3; IDA:UniProtKB.
DR   GO; GO:0071285; P:cellular response to lithium ion; IDA:MGI.
DR   GO; GO:0071407; P:cellular response to organic cyclic compound; IDA:MGI.
DR   GO; GO:0097191; P:extrinsic apoptotic signaling pathway; IGI:ARUK-UCL.
DR   GO; GO:0097192; P:extrinsic apoptotic signaling pathway in absence of ligand; IDA:UniProtKB.
DR   GO; GO:0005977; P:glycogen metabolic process; IEA:UniProtKB-KW.
DR   GO; GO:0044027; P:hypermethylation of CpG island; IMP:BHF-UCL.
DR   GO; GO:0008286; P:insulin receptor signaling pathway; IDA:BHF-UCL.
DR   GO; GO:0090090; P:negative regulation of canonical Wnt signaling pathway; IBA:GO_Central.
DR   GO; GO:0061052; P:negative regulation of cell growth involved in cardiac muscle cell development; IMP:BHF-UCL.
DR   GO; GO:2000171; P:negative regulation of dendrite development; ISO:MGI.
DR   GO; GO:0046325; P:negative regulation of glucose import; ISO:MGI.
DR   GO; GO:1904227; P:negative regulation of glycogen synthase activity, transferring glucose-1-phosphate; ISO:MGI.
DR   GO; GO:0046627; P:negative regulation of insulin receptor signaling pathway; ISO:MGI.
DR   GO; GO:0032007; P:negative regulation of TOR signaling; IMP:BHF-UCL.
DR   GO; GO:0007399; P:nervous system development; IEA:UniProtKB-KW.
DR   GO; GO:0018105; P:peptidyl-serine phosphorylation; IDA:MGI.
DR   GO; GO:0018107; P:peptidyl-threonine phosphorylation; ISO:MGI.
DR   GO; GO:0071879; P:positive regulation of adenylate cyclase-activating adrenergic receptor signaling pathway; IMP:BHF-UCL.
DR   GO; GO:0106071; P:positive regulation of adenylate cyclase-activating G protein-coupled receptor signaling pathway; IMP:BHF-UCL.
DR   GO; GO:1902004; P:positive regulation of amyloid-beta formation; ISO:MGI.
DR   GO; GO:0010508; P:positive regulation of autophagy; IDA:UniProtKB.
DR   GO; GO:0010628; P:positive regulation of gene expression; IGI:ARUK-UCL.
DR   GO; GO:2000467; P:positive regulation of glycogen (starch) synthase activity; IMP:BHF-UCL.
DR   GO; GO:0045823; P:positive regulation of heart contraction; IMP:BHF-UCL.
DR   GO; GO:1901030; P:positive regulation of mitochondrial outer membrane permeabilization involved in apoptotic signaling pathway; IDA:UniProtKB.
DR   GO; GO:0043525; P:positive regulation of neuron apoptotic process; ISO:MGI.
DR   GO; GO:0033138; P:positive regulation of peptidyl-serine phosphorylation; IDA:MGI.
DR   GO; GO:0010800; P:positive regulation of peptidyl-threonine phosphorylation; IDA:MGI.
DR   GO; GO:0032436; P:positive regulation of proteasomal ubiquitin-dependent protein catabolic process; ISO:MGI.
DR   GO; GO:1903955; P:positive regulation of protein targeting to mitochondrion; ISO:MGI.
DR   GO; GO:0031398; P:positive regulation of protein ubiquitination; ISO:MGI.
DR   GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IMP:BHF-UCL.
DR   GO; GO:0043161; P:proteasome-mediated ubiquitin-dependent protein catabolic process; IDA:UniProtKB.
DR   GO; GO:0006468; P:protein phosphorylation; IDA:MGI.
DR   GO; GO:1903146; P:regulation of autophagy of mitochondrion; ISO:MGI.
DR   GO; GO:0006349; P:regulation of gene expression by genomic imprinting; IMP:BHF-UCL.
DR   GO; GO:0010975; P:regulation of neuron projection development; IBA:GO_Central.
DR   GO; GO:0003073; P:regulation of systemic arterial blood pressure; IMP:BHF-UCL.
DR   GO; GO:0007165; P:signal transduction; IBA:GO_Central.
DR   GO; GO:0016055; P:Wnt signaling pathway; IEA:UniProtKB-KW.
DR   CDD; cd14137; STKc_GSK3; 1.
DR   InterPro; IPR011009; Kinase-like_dom_sf.
DR   InterPro; IPR000719; Prot_kinase_dom.
DR   InterPro; IPR017441; Protein_kinase_ATP_BS.
DR   InterPro; IPR008271; Ser/Thr_kinase_AS.
DR   InterPro; IPR039192; STKc_GSK3.
DR   Pfam; PF00069; Pkinase; 1.
DR   SMART; SM00220; S_TKc; 1.
DR   SUPFAM; SSF56112; SSF56112; 1.
DR   PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR   PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR   PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE   1: Evidence at protein level;
KW   Acetylation; ATP-binding; Carbohydrate metabolism; Glycogen metabolism;
KW   Kinase; Neurogenesis; Nucleotide-binding; Phosphoprotein;
KW   Reference proteome; Serine/threonine-protein kinase;
KW   Signal transduction inhibitor; Transferase; Wnt signaling pathway.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000250|UniProtKB:P49840"
FT   CHAIN           2..490
FT                   /note="Glycogen synthase kinase-3 alpha"
FT                   /id="PRO_0000280395"
FT   DOMAIN          119..404
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   REGION          1..97
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          451..490
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        452..490
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        244
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT                   ECO:0000255|PROSITE-ProRule:PRU10027"
FT   BINDING         125..133
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   BINDING         148
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   MOD_RES         2
FT                   /note="N-acetylserine"
FT                   /evidence="ECO:0000250|UniProtKB:P49840"
FT   MOD_RES         2
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P49840"
FT   MOD_RES         21
FT                   /note="Phosphoserine; by PKB/AKT1"
FT                   /evidence="ECO:0000269|PubMed:15791206"
FT   MOD_RES         72
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P49840"
FT   MOD_RES         77
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P49840"
FT   MOD_RES         97
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P49840"
FT   MOD_RES         279
FT                   /note="Phosphotyrosine"
FT                   /evidence="ECO:0000250|UniProtKB:P18265"
FT   MUTAGEN         21
FT                   /note="S->A: Loss of phosphorylation; No inhibition of
FT                   activity and constitutively active."
FT                   /evidence="ECO:0000269|PubMed:15791206"
SQ   SEQUENCE   490 AA;  51661 MW;  739CDD86BBFB497B CRC64;
     MSGGGPSGGG PGGSGRARTS SFAEPGGGGG GGGGGPGGSA SGPGGTGGGK ASVGAMGGGV
     GASSSGGGPS GSGGGGSGGP GAGTSFPPPG VKLGRDSGKV TTVVATVGQG PERSQEVAYT
     DIKVIGNGSF GVVYQARLAE TRELVAIKKV LQDKRFKNRE LQIMRKLDHC NIVRLRYFFY
     SSGEKKDELY LNLVLEYVPE TVYRVARHFT KAKLITPIIY IKVYMYQLFR SLAYIHSQGV
     CHRDIKPQNL LVDPDTAVLK LCDFGSAKQL VRGEPNVSYI CSRYYRAPEL IFGATDYTSS
     IDVWSAGCVL AELLLGQPIF PGDSGVDQLV EIIKVLGTPT REQIREMNPN YTEFKFPQIK
     AHPWTKVFKS SKTPPEAIAL CSSLLEYTPS SRLSPLEACA HSFFDELRRL GAQLPNDRPL
     PPLFNFSPGE LSIQPSLNAI LIPPHLRSPA GPASPLTTSY NPSSQALTEA QTGQDWQPSD
     ATTATLASSS
 
 
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