GAK_HUMAN
ID GAK_HUMAN Reviewed; 1311 AA.
AC O14976; Q5U4P5; Q9BVY6;
DT 29-AUG-2001, integrated into UniProtKB/Swiss-Prot.
DT 29-AUG-2001, sequence version 2.
DT 03-AUG-2022, entry version 203.
DE RecName: Full=Cyclin-G-associated kinase;
DE EC=2.7.11.1;
GN Name=GAK;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND CHARACTERIZATION.
RC TISSUE=Fibroblast;
RX PubMed=9299234; DOI=10.1006/geno.1997.4873;
RA Kimura S.H., Tsuruga H., Yabuta N., Endo Y., Nojima H.;
RT "Structure, expression, and chromosomal localization of human GAK.";
RL Genomics 44:179-187(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), AND NUCLEOTIDE SEQUENCE
RP [LARGE SCALE MRNA] OF 981-1311 (ISOFORM 1).
RC TISSUE=Ovary, and Placenta;
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 FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=10625686; DOI=10.1074/jbc.275.2.1365;
RA Greener T., Zhao X., Nojima H., Eisenberg E., Greene L.E.;
RT "Role of cyclin G-associated kinase in uncoating clathrin-coated vesicles
RT from non-neuronal cells.";
RL J. Biol. Chem. 275:1365-1370(2000).
RN [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-16; SER-456; SER-770;
RP SER-826; SER-829; SER-834 AND SER-1096, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007;
RA Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,
RA Greff Z., Keri G., Stemmann O., Mann M.;
RT "Kinase-selective enrichment enables quantitative phosphoproteomics of the
RT kinome across the cell cycle.";
RL Mol. Cell 31:438-448(2008).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-826; SER-829 AND SER-834, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [6]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a
RT refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [7]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, PHOSPHORYLATION [LARGE SCALE
RP ANALYSIS] AT SER-16; SER-826; SER-829; SER-834; SER-939; SER-1176 AND
RP SER-1185, CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS], AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19369195; DOI=10.1074/mcp.m800588-mcp200;
RA Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G.,
RA Mann M., Daub H.;
RT "Large-scale proteomics analysis of the human kinome.";
RL Mol. Cell. Proteomics 8:1751-1764(2009).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-826 AND SER-829, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Leukemic T-cell;
RX PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA Rodionov V., Han D.K.;
RT "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT reveals system-wide modulation of protein-protein interactions.";
RL Sci. Signal. 2:RA46-RA46(2009).
RN [9]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-829, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T.,
RA Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.;
RT "System-wide temporal characterization of the proteome and phosphoproteome
RT of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-776; THR-794; SER-826 AND
RP SER-829, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-783, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [13]
RP X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF 12-347.
RG Midwest center for structural genomics (MCSG);
RT "Crystal structure of the human cyclin G associated kinase (GAK).";
RL Submitted (JUL-2011) to the PDB data bank.
RN [14]
RP VARIANTS [LARGE SCALE ANALYSIS] LEU-144; MET-580; TYR-787; ARG-877;
RP ASP-962; MET-1051; HIS-1120; LEU-1137; ASN-1168; ARG-1265 AND ASN-1297.
RX PubMed=17344846; DOI=10.1038/nature05610;
RA Greenman C., Stephens P., Smith R., Dalgliesh G.L., Hunter C., Bignell G.,
RA Davies H., Teague J., Butler A., Stevens C., Edkins S., O'Meara S.,
RA Vastrik I., Schmidt E.E., Avis T., Barthorpe S., Bhamra G., Buck G.,
RA Choudhury B., Clements J., Cole J., Dicks E., Forbes S., Gray K.,
RA Halliday K., Harrison R., Hills K., Hinton J., Jenkinson A., Jones D.,
RA Menzies A., Mironenko T., Perry J., Raine K., Richardson D., Shepherd R.,
RA Small A., Tofts C., Varian J., Webb T., West S., Widaa S., Yates A.,
RA Cahill D.P., Louis D.N., Goldstraw P., Nicholson A.G., Brasseur F.,
RA Looijenga L., Weber B.L., Chiew Y.-E., DeFazio A., Greaves M.F.,
RA Green A.R., Campbell P., Birney E., Easton D.F., Chenevix-Trench G.,
RA Tan M.-H., Khoo S.K., Teh B.T., Yuen S.T., Leung S.Y., Wooster R.,
RA Futreal P.A., Stratton M.R.;
RT "Patterns of somatic mutation in human cancer genomes.";
RL Nature 446:153-158(2007).
CC -!- FUNCTION: Associates with cyclin G and CDK5. Seems to act as an auxilin
CC homolog that is involved in the uncoating of clathrin-coated vesicles
CC by Hsc70 in non-neuronal cells. Expression oscillates slightly during
CC the cell cycle, peaking at G1. {ECO:0000269|PubMed:10625686}.
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 -!- 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 -!- INTERACTION:
CC O14976; Q9NQ11: ATP13A2; NbExp=2; IntAct=EBI-714707, EBI-6308763;
CC O14976; P11142: HSPA8; NbExp=7; IntAct=EBI-714707, EBI-351896;
CC O14976; Q5S007: LRRK2; NbExp=11; IntAct=EBI-714707, EBI-5323863;
CC -!- SUBCELLULAR LOCATION: Cytoplasm, perinuclear region
CC {ECO:0000269|PubMed:10625686}. Golgi apparatus, trans-Golgi network
CC {ECO:0000269|PubMed:10625686}. Cell junction, focal adhesion
CC {ECO:0000305|PubMed:10625686}. Note=Localizes to the perinuclear area
CC and to the trans-Golgi network. Also seen on the plasma membrane,
CC probably at focal adhesions.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=O14976-1; Sequence=Displayed;
CC Name=2;
CC IsoId=O14976-2; Sequence=VSP_054479;
CC -!- TISSUE SPECIFICITY: Ubiquitous. Highest in testis.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr protein
CC kinase family. {ECO:0000255|PROSITE-ProRule:PRU00159}.
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DR EMBL; D88435; BAA22623.1; -; mRNA.
DR EMBL; BC000816; AAH00816.1; -; mRNA.
DR EMBL; BC008668; AAH08668.1; -; mRNA.
DR EMBL; BC085005; AAH85005.1; -; mRNA.
DR CCDS; CCDS3340.1; -. [O14976-1]
DR CCDS; CCDS82902.1; -. [O14976-2]
DR RefSeq; NP_001305063.1; NM_001318134.1. [O14976-2]
DR RefSeq; NP_005246.2; NM_005255.3. [O14976-1]
DR PDB; 4C57; X-ray; 2.55 A; A/B=14-351.
DR PDB; 4C58; X-ray; 2.16 A; A=14-351.
DR PDB; 4C59; X-ray; 2.80 A; A=14-351.
DR PDB; 4O38; X-ray; 2.10 A; A/B=12-347.
DR PDB; 4Y8D; X-ray; 2.10 A; A/B=14-351.
DR PDB; 5Y7Z; X-ray; 2.80 A; A/B=25-335.
DR PDB; 5Y80; X-ray; 2.50 A; A=25-335.
DR PDBsum; 4C57; -.
DR PDBsum; 4C58; -.
DR PDBsum; 4C59; -.
DR PDBsum; 4O38; -.
DR PDBsum; 4Y8D; -.
DR PDBsum; 5Y7Z; -.
DR PDBsum; 5Y80; -.
DR AlphaFoldDB; O14976; -.
DR SMR; O14976; -.
DR BioGRID; 108853; 174.
DR IntAct; O14976; 103.
DR MINT; O14976; -.
DR STRING; 9606.ENSP00000314499; -.
DR BindingDB; O14976; -.
DR ChEMBL; CHEMBL4355; -.
DR DrugBank; DB12010; Fostamatinib.
DR DrugCentral; O14976; -.
DR GuidetoPHARMACOLOGY; 2027; -.
DR DEPOD; GAK; -.
DR GlyGen; O14976; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; O14976; -.
DR PhosphoSitePlus; O14976; -.
DR SwissPalm; O14976; -.
DR BioMuta; GAK; -.
DR EPD; O14976; -.
DR jPOST; O14976; -.
DR MassIVE; O14976; -.
DR MaxQB; O14976; -.
DR PaxDb; O14976; -.
DR PeptideAtlas; O14976; -.
DR PRIDE; O14976; -.
DR ProteomicsDB; 48350; -. [O14976-1]
DR ABCD; O14976; 2 sequenced antibodies.
DR Antibodypedia; 22165; 332 antibodies from 34 providers.
DR DNASU; 2580; -.
DR Ensembl; ENST00000314167.9; ENSP00000314499.4; ENSG00000178950.18. [O14976-1]
DR Ensembl; ENST00000511163.5; ENSP00000421361.1; ENSG00000178950.18. [O14976-2]
DR GeneID; 2580; -.
DR KEGG; hsa:2580; -.
DR MANE-Select; ENST00000314167.9; ENSP00000314499.4; NM_005255.4; NP_005246.2.
DR UCSC; uc003gbm.6; human. [O14976-1]
DR CTD; 2580; -.
DR DisGeNET; 2580; -.
DR GeneCards; GAK; -.
DR HGNC; HGNC:4113; GAK.
DR HPA; ENSG00000178950; Low tissue specificity.
DR MIM; 602052; gene.
DR neXtProt; NX_O14976; -.
DR OpenTargets; ENSG00000178950; -.
DR PharmGKB; PA28528; -.
DR VEuPathDB; HostDB:ENSG00000178950; -.
DR eggNOG; KOG0431; Eukaryota.
DR eggNOG; KOG1989; Eukaryota.
DR eggNOG; KOG2283; Eukaryota.
DR GeneTree; ENSGT00940000159527; -.
DR HOGENOM; CLU_007537_0_0_1; -.
DR InParanoid; O14976; -.
DR OMA; HYKNTNL; -.
DR OrthoDB; 826336at2759; -.
DR PhylomeDB; O14976; -.
DR TreeFam; TF105165; -.
DR PathwayCommons; O14976; -.
DR Reactome; R-HSA-432722; Golgi Associated Vesicle Biogenesis.
DR Reactome; R-HSA-8856828; Clathrin-mediated endocytosis.
DR SignaLink; O14976; -.
DR SIGNOR; O14976; -.
DR BioGRID-ORCS; 2580; 448 hits in 1119 CRISPR screens.
DR ChiTaRS; GAK; human.
DR GeneWiki; GAK_(protein); -.
DR GenomeRNAi; 2580; -.
DR Pharos; O14976; Tchem.
DR PRO; PR:O14976; -.
DR Proteomes; UP000005640; Chromosome 4.
DR RNAct; O14976; protein.
DR Bgee; ENSG00000178950; Expressed in pancreatic ductal cell and 204 other tissues.
DR ExpressionAtlas; O14976; baseline and differential.
DR Genevisible; O14976; HS.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0005925; C:focal adhesion; IEA:UniProtKB-SubCell.
DR GO; GO:0005794; C:Golgi apparatus; IDA:ParkinsonsUK-UCL.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; IDA:HPA.
DR GO; GO:0016020; C:membrane; HDA:UniProtKB.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0098793; C:presynapse; IEA:GOC.
DR GO; GO:0031982; C:vesicle; IDA:ParkinsonsUK-UCL.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0051087; F:chaperone binding; TAS:BHF-UCL.
DR GO; GO:0030276; F:clathrin binding; IBA:GO_Central.
DR GO; GO:0030332; F:cyclin binding; ISS:ParkinsonsUK-UCL.
DR GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; TAS:ProtInc.
DR GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR GO; GO:0051085; P:chaperone cofactor-dependent protein refolding; TAS:BHF-UCL.
DR GO; GO:0072318; P:clathrin coat disassembly; IMP:ParkinsonsUK-UCL.
DR GO; GO:1905224; P:clathrin-coated pit assembly; IMP:ParkinsonsUK-UCL.
DR GO; GO:0072583; P:clathrin-dependent endocytosis; IMP:ParkinsonsUK-UCL.
DR GO; GO:0007029; P:endoplasmic reticulum organization; ISS:ParkinsonsUK-UCL.
DR GO; GO:0007030; P:Golgi organization; IMP:ParkinsonsUK-UCL.
DR GO; GO:0090160; P:Golgi to lysosome transport; IMP:ParkinsonsUK-UCL.
DR GO; GO:0010977; P:negative regulation of neuron projection development; IDA:ParkinsonsUK-UCL.
DR GO; GO:0034067; P:protein localization to Golgi apparatus; IMP:ParkinsonsUK-UCL.
DR GO; GO:0072659; P:protein localization to plasma membrane; IMP:ParkinsonsUK-UCL.
DR GO; GO:0006468; P:protein phosphorylation; IEA:InterPro.
DR GO; GO:0006898; P:receptor-mediated endocytosis; IMP:ParkinsonsUK-UCL.
DR GO; GO:0016191; P:synaptic vesicle uncoating; ISS:BHF-UCL.
DR CDD; cd06257; DnaJ; 1.
DR Gene3D; 1.10.287.110; -; 1.
DR Gene3D; 3.90.190.10; -; 1.
DR InterPro; IPR035892; C2_domain_sf.
DR InterPro; IPR001623; DnaJ_domain.
DR InterPro; IPR036869; J_dom_sf.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR029021; Prot-tyrosine_phosphatase-like.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR InterPro; IPR014020; Tensin_C2-dom.
DR InterPro; IPR029023; Tensin_phosphatase.
DR Pfam; PF00069; Pkinase; 1.
DR Pfam; PF10409; PTEN_C2; 1.
DR SMART; SM00271; DnaJ; 1.
DR SMART; SM01326; PTEN_C2; 1.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF46565; SSF46565; 1.
DR SUPFAM; SSF49562; SSF49562; 1.
DR SUPFAM; SSF52799; SSF52799; 1.
DR SUPFAM; SSF56112; SSF56112; 1.
DR PROSITE; PS51182; C2_TENSIN; 1.
DR PROSITE; PS50076; DNAJ_2; 1.
DR PROSITE; PS51181; PPASE_TENSIN; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Alternative splicing; ATP-binding; Cell cycle;
KW Cell junction; Cytoplasm; Golgi apparatus; Kinase; Methylation;
KW Nucleotide-binding; Phosphoprotein; Reference proteome;
KW Serine/threonine-protein kinase; Transferase.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0007744|PubMed:19369195,
FT ECO:0007744|PubMed:19413330"
FT CHAIN 2..1311
FT /note="Cyclin-G-associated kinase"
FT /id="PRO_0000085958"
FT DOMAIN 40..314
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT DOMAIN 399..566
FT /note="Phosphatase tensin-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00590"
FT DOMAIN 572..710
FT /note="C2 tensin-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00589"
FT DOMAIN 1247..1311
FT /note="J"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00286"
FT REGION 709..729
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 749..788
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 801..860
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 913..1035
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1047..1150
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 801..822
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 965..996
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1066..1080
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1110..1128
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1130..1144
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 173
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT MOD_RES 2
FT /note="N-acetylserine"
FT /evidence="ECO:0007744|PubMed:19369195,
FT ECO:0007744|PubMed:19413330"
FT MOD_RES 2
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P97874"
FT MOD_RES 16
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18691976,
FT ECO:0007744|PubMed:19369195"
FT MOD_RES 456
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18691976"
FT MOD_RES 770
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18691976"
FT MOD_RES 776
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 783
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 794
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 811
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P97874"
FT MOD_RES 826
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:18691976, ECO:0007744|PubMed:19369195,
FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:23186163"
FT MOD_RES 829
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:18691976, ECO:0007744|PubMed:19369195,
FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:21406692,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 834
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:18691976, ECO:0007744|PubMed:19369195"
FT MOD_RES 939
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19369195"
FT MOD_RES 1096
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18691976"
FT MOD_RES 1123
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0000250|UniProtKB:Q99KY4"
FT MOD_RES 1176
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19369195"
FT MOD_RES 1185
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19369195"
FT VAR_SEQ 49..127
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_054479"
FT VARIANT 144
FT /note="S -> L (in dbSNP:rs768962219)"
FT /evidence="ECO:0000269|PubMed:17344846"
FT /id="VAR_040505"
FT VARIANT 580
FT /note="V -> M (in dbSNP:rs34255232)"
FT /evidence="ECO:0000269|PubMed:17344846"
FT /id="VAR_040506"
FT VARIANT 787
FT /note="D -> Y (in dbSNP:rs34585705)"
FT /evidence="ECO:0000269|PubMed:17344846"
FT /id="VAR_040507"
FT VARIANT 877
FT /note="Q -> R (in dbSNP:rs149842313)"
FT /evidence="ECO:0000269|PubMed:17344846"
FT /id="VAR_040508"
FT VARIANT 962
FT /note="G -> D (in a lung neuroendocrine carcinoma sample;
FT somatic mutation; dbSNP:rs773153935)"
FT /evidence="ECO:0000269|PubMed:17344846"
FT /id="VAR_040509"
FT VARIANT 1051
FT /note="T -> M (in dbSNP:rs35227944)"
FT /evidence="ECO:0000269|PubMed:17344846"
FT /id="VAR_040510"
FT VARIANT 1120
FT /note="Q -> H (in dbSNP:rs55801437)"
FT /evidence="ECO:0000269|PubMed:17344846"
FT /id="VAR_040511"
FT VARIANT 1137
FT /note="P -> L (in dbSNP:rs56169884)"
FT /evidence="ECO:0000269|PubMed:17344846"
FT /id="VAR_040512"
FT VARIANT 1168
FT /note="S -> N (in dbSNP:rs56326341)"
FT /evidence="ECO:0000269|PubMed:17344846"
FT /id="VAR_040513"
FT VARIANT 1265
FT /note="K -> R (in dbSNP:rs2306242)"
FT /evidence="ECO:0000269|PubMed:17344846"
FT /id="VAR_040514"
FT VARIANT 1297
FT /note="D -> N (in dbSNP:rs1134921)"
FT /evidence="ECO:0000269|PubMed:17344846"
FT /id="VAR_040515"
FT CONFLICT 607
FT /note="R -> C (in Ref. 2; AAH85005)"
FT /evidence="ECO:0000305"
FT CONFLICT 1113
FT /note="P -> A (in Ref. 1; BAA22623)"
FT /evidence="ECO:0000305"
FT TURN 27..30
FT /evidence="ECO:0007829|PDB:4O38"
FT STRAND 32..35
FT /evidence="ECO:0007829|PDB:4O38"
FT STRAND 38..47
FT /evidence="ECO:0007829|PDB:4O38"
FT STRAND 50..59
FT /evidence="ECO:0007829|PDB:4O38"
FT TURN 60..62
FT /evidence="ECO:0007829|PDB:4O38"
FT STRAND 65..75
FT /evidence="ECO:0007829|PDB:4O38"
FT HELIX 76..92
FT /evidence="ECO:0007829|PDB:4O38"
FT STRAND 101..107
FT /evidence="ECO:0007829|PDB:4O38"
FT TURN 109..111
FT /evidence="ECO:0007829|PDB:4O38"
FT STRAND 115..124
FT /evidence="ECO:0007829|PDB:4O38"
FT STRAND 127..129
FT /evidence="ECO:0007829|PDB:4O38"
FT HELIX 130..138
FT /evidence="ECO:0007829|PDB:4O38"
FT HELIX 145..163
FT /evidence="ECO:0007829|PDB:4O38"
FT STRAND 165..167
FT /evidence="ECO:0007829|PDB:4O38"
FT HELIX 176..178
FT /evidence="ECO:0007829|PDB:4O38"
FT STRAND 179..181
FT /evidence="ECO:0007829|PDB:4Y8D"
FT STRAND 187..189
FT /evidence="ECO:0007829|PDB:4O38"
FT HELIX 208..219
FT /evidence="ECO:0007829|PDB:5Y80"
FT HELIX 224..226
FT /evidence="ECO:0007829|PDB:5Y80"
FT HELIX 229..232
FT /evidence="ECO:0007829|PDB:5Y80"
FT HELIX 242..258
FT /evidence="ECO:0007829|PDB:4O38"
FT TURN 262..265
FT /evidence="ECO:0007829|PDB:5Y80"
FT HELIX 268..272
FT /evidence="ECO:0007829|PDB:5Y80"
FT HELIX 286..288
FT /evidence="ECO:0007829|PDB:4O38"
FT HELIX 289..295
FT /evidence="ECO:0007829|PDB:4O38"
FT HELIX 300..302
FT /evidence="ECO:0007829|PDB:4O38"
FT HELIX 306..319
FT /evidence="ECO:0007829|PDB:4O38"
FT HELIX 329..332
FT /evidence="ECO:0007829|PDB:4O38"
SQ SEQUENCE 1311 AA; 143191 MW; 0ACE45DF57A5F981 CRC64;
MSLLQSALDF LAGPGSLGGA SGRDQSDFVG QTVELGELRL RVRRVLAEGG FAFVYEAQDV
GSGREYALKR LLSNEEEKNR AIIQEVCFMK KLSGHPNIVQ FCSAASIGKE ESDTGQAEFL
LLTELCKGQL VEFLKKMESR GPLSCDTVLK IFYQTCRAVQ HMHRQKPPII HRDLKVENLL
LSNQGTIKLC DFGSATTISH YPDYSWSAQR RALVEEEITR NTTPMYRTPE IIDLYSNFPI
GEKQDIWALG CILYLLCFRQ HPFEDGAKLR IVNGKYSIPP HDTQYTVFHS LIRAMLQVNP
EERLSIAEVV HQLQEIAAAR NVNPKSPITE LLEQNGGYGS ATLSRGPPPP VGPAGSGYSG
GLALAEYDQP YGGFLDILRG GTERLFTNLK DTSSKVIQSV ANYAKGDLDI SYITSRIAVM
SFPAEGVESA LKNNIEDVRL FLDSKHPGHY AVYNLSPRTY RPSRFHNRVS ECGWAARRAP
HLHTLYNICR NMHAWLRQDH KNVCVVHCMD GRAASAVAVC SFLCFCRLFS TAEAAVYMFS
MKRCPPGIWP SHKRYIEYMC DMVAEEPITP HSKPILVRAV VMTPVPLFSK QRSGCRPFCE
VYVGDERVAS TSQEYDKMRD FKIEDGKAVI PLGVTVQGDV LIVIYHARST LGGRLQAKMA
SMKMFQIQFH TGFVPRNATT VKFAKYDLDA CDIQEKYPDL FQVNLEVEVE PRDRPSREAP
PWENSSMRGL NPKILFSSRE EQQDILSKFG KPELPRQPGS TAQYDAGAGS PEAEPTDSDS
PPSSSADASR FLHTLDWQEE KEAETGAENA SSKESESALM EDRDESEVSD EGGSPISSEG
QEPRADPEPP GLAAGLVQQD LVFEVETPAV LPEPVPQEDG VDLLGLHSEV GAGPAVPPQA
CKAPSSNTDL LSCLLGPPEA ASQGPPEDLL SEDPLLLASP APPLSVQSTP RGGPPAAADP
FGPLLPSSGN NSQPCSNPDL FGEFLNSDSV TVPPSFPSAH SAPPPSCSAD FLHLGDLPGE
PSKMTASSSN PDLLGGWAAW TETAASAVAP TPATEGPLFS PGGQPAPCGS QASWTKSQNP
DPFADLGDLS SGLQGSPAGF PPGGFIPKTA TTPKGSSSWQ TSRPPAQGAS WPPQAKPPPK
ACTQPRPNYA SNFSVIGARE ERGVRAPSFA QKPKVSENDF EDLLSNQGFS SRSDKKGPKT
IAEMRKQDLA KDTDPLKLKL LDWIEGKERN IRALLSTLHT VLWDGESRWT PVGMADLVAP
EQVKKHYRRA VLAVHPDKAA GQPYEQHAKM IFMELNDAWS EFENQGSRPL F
