IP3KB_HUMAN
ID IP3KB_HUMAN Reviewed; 946 AA.
AC P27987; Q5VWL9; Q5VWM0; Q96BZ2; Q96JS1; Q9UH47;
DT 01-AUG-1992, integrated into UniProtKB/Swiss-Prot.
DT 26-APR-2005, sequence version 5.
DT 03-AUG-2022, entry version 191.
DE RecName: Full=Inositol-trisphosphate 3-kinase B {ECO:0000305};
DE EC=2.7.1.127 {ECO:0000269|PubMed:11846419, ECO:0000269|PubMed:1654894};
DE AltName: Full=Inositol 1,4,5-trisphosphate 3-kinase B;
DE Short=IP3 3-kinase B;
DE Short=IP3K B;
DE Short=InsP 3-kinase B;
GN Name=ITPKB {ECO:0000312|HGNC:HGNC:6179};
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), VARIANTS ALA-408 AND GLN-552,
RP CATALYTIC ACTIVITY, FUNCTION, AND ACTIVITY REGULATION.
RC TISSUE=Hippocampus;
RX PubMed=11846419; DOI=10.1006/bbrc.2002.6456;
RA Dewaste V., Roymans D., Moreau C., Erneux C.;
RT "Cloning and expression of a full-length cDNA encoding human inositol
RT 1,4,5-trisphosphate 3-kinase B.";
RL Biochem. Biophys. Res. Commun. 291:400-405(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND VARIANT GLN-552.
RC TISSUE=Colon;
RA Bertsch U., Suesse S., Frerk S., Fanick W.;
RT "Cloning of the complete protein coding regions for inositol 1,4,5-
RT trisphosphate 3-kinase B-isoforms from rat and human.";
RL Submitted (MAY-1999) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16710414; DOI=10.1038/nature04727;
RA Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A.,
RA Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C.,
RA Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.,
RA Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C.,
RA Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W.,
RA Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J.,
RA Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J.,
RA Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y.,
RA Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J.,
RA Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
RA Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
RA Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
RA Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S.,
RA Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K.,
RA Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R.,
RA Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M.,
RA Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S.,
RA Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J.,
RA Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W.,
RA McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
RA Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
RA Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
RA Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
RA Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S.,
RA Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M.,
RA White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H.,
RA Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E.,
RA Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G.,
RA Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.;
RT "The DNA sequence and biological annotation of human chromosome 1.";
RL Nature 441:315-321(2006).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), AND VARIANTS ALA-408
RP AND GLN-552.
RC TISSUE=Skin;
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 [5]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 442-946 (ISOFORM 1), VARIANT GLN-552,
RP FUNCTION, CATALYTIC ACTIVITY, AND BIOPHYSICOCHEMICAL PROPERTIES.
RC TISSUE=Hippocampus;
RX PubMed=1654894; DOI=10.1042/bj2780883;
RA Takazawa K., Perret J., Dumont J.E., Erneux C.;
RT "Molecular cloning and expression of a new putative inositol 1,4,5-
RT trisphosphate 3-kinase isoenzyme.";
RL Biochem. J. 278:883-886(1991).
RN [6]
RP SUBCELLULAR LOCATION, ACTIVITY REGULATION, FUNCTION, AND MUTAGENESIS OF
RP ASP-897.
RX PubMed=12747803; DOI=10.1042/bj20021963;
RA Dewaste V., Moreau C., De Smedt F., Bex F., De Smedt H., Wuytack F.,
RA Missiaen L., Erneux C.;
RT "The three isoenzymes of human inositol-1,4,5-trisphosphate 3-kinase show
RT specific intracellular localization but comparable Ca2+ responses on
RT transfection in COS-7 cells.";
RL Biochem. J. 374:41-49(2003).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-43 AND SER-49, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Platelet;
RX PubMed=18088087; DOI=10.1021/pr0704130;
RA Zahedi R.P., Lewandrowski U., Wiesner J., Wortelkamp S., Moebius J.,
RA Schuetz C., Walter U., Gambaryan S., Sickmann A.;
RT "Phosphoproteome of resting human platelets.";
RL J. Proteome Res. 7:526-534(2008).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-43; SER-49 AND SER-71, 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 [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-71, AND IDENTIFICATION BY
RP 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 [10]
RP INTERACTION WITH DMTN.
RX PubMed=23060452; DOI=10.1074/jbc.m112.364679;
RA Wieschhaus A.J., Le Breton G.C., Chishti A.H.;
RT "Headpiece domain of dematin regulates calcium mobilization and signaling
RT in platelets.";
RL J. Biol. Chem. 287:41218-41231(2012).
RN [11]
RP IDENTIFICATION BY 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).
CC -!- FUNCTION: Catalyzes the phosphorylation of 1D-myo-inositol 1,4,5-
CC trisphosphate (InsP3) into 1D-myo-inositol 1,3,4,5-tetrakisphosphate
CC and participates to the regulation of calcium homeostasis.
CC {ECO:0000269|PubMed:11846419, ECO:0000269|PubMed:12747803,
CC ECO:0000269|PubMed:1654894}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1D-myo-inositol 1,4,5-trisphosphate + ATP = 1D-myo-inositol
CC 1,3,4,5-tetrakisphosphate + ADP + H(+); Xref=Rhea:RHEA:11020,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:57895,
CC ChEBI:CHEBI:203600, ChEBI:CHEBI:456216; EC=2.7.1.127;
CC Evidence={ECO:0000269|PubMed:11846419, ECO:0000269|PubMed:12747803,
CC ECO:0000269|PubMed:1654894};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:11021;
CC Evidence={ECO:0000269|PubMed:11846419, ECO:0000269|PubMed:12747803,
CC ECO:0000269|PubMed:1654894};
CC -!- ACTIVITY REGULATION: IP3K is activated by calcium and calmodulin. Form
CC B is much more sensitive to calcium/calmodulin than form A.
CC {ECO:0000269|PubMed:11846419, ECO:0000269|PubMed:12747803}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=1.6 uM for 1D-myo-inositol 1,4,5-trisphosphate
CC {ECO:0000269|PubMed:1654894};
CC -!- SUBUNIT: Interacts with DMTN. {ECO:0000269|PubMed:23060452}.
CC -!- INTERACTION:
CC P27987; Q8NHQ1: CEP70; NbExp=3; IntAct=EBI-751388, EBI-739624;
CC P27987; Q9GZU7: CTDSP1; NbExp=5; IntAct=EBI-751388, EBI-751587;
CC P27987; Q08379: GOLGA2; NbExp=4; IntAct=EBI-751388, EBI-618309;
CC P27987; Q13099: IFT88; NbExp=3; IntAct=EBI-751388, EBI-347427;
CC P27987; O76011: KRT34; NbExp=3; IntAct=EBI-751388, EBI-1047093;
CC P27987; Q08209-2: PPP3CA; NbExp=3; IntAct=EBI-751388, EBI-11959013;
CC P27987; Q8N9R8: SCAI; NbExp=3; IntAct=EBI-751388, EBI-4395514;
CC P27987; Q9BYV2: TRIM54; NbExp=3; IntAct=EBI-751388, EBI-2130429;
CC P27987; Q9UHD9: UBQLN2; NbExp=5; IntAct=EBI-751388, EBI-947187;
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton
CC {ECO:0000269|PubMed:12747803}. Cytoplasm {ECO:0000269|PubMed:12747803}.
CC Endoplasmic reticulum {ECO:0000269|PubMed:12747803}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=P27987-1; Sequence=Displayed;
CC Name=2;
CC IsoId=P27987-2; Sequence=VSP_016092;
CC -!- SIMILARITY: Belongs to the inositol phosphokinase (IPK) family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAA40491.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; Y18024; CAB65055.3; -; mRNA.
DR EMBL; AJ242780; CAC40650.1; -; mRNA.
DR EMBL; AL365444; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC015009; AAH15009.1; -; mRNA.
DR EMBL; X57206; CAA40491.1; ALT_INIT; mRNA.
DR CCDS; CCDS1555.1; -. [P27987-1]
DR PIR; JC7810; JC7810.
DR PIR; S17682; S17682.
DR RefSeq; NP_002212.3; NM_002221.3. [P27987-1]
DR RefSeq; XP_005273177.1; XM_005273120.2. [P27987-2]
DR AlphaFoldDB; P27987; -.
DR SMR; P27987; -.
DR BioGRID; 109912; 23.
DR IntAct; P27987; 16.
DR MINT; P27987; -.
DR STRING; 9606.ENSP00000411152; -.
DR ChEMBL; CHEMBL5165; -.
DR GuidetoPHARMACOLOGY; 1448; -.
DR iPTMnet; P27987; -.
DR PhosphoSitePlus; P27987; -.
DR BioMuta; ITPKB; -.
DR DMDM; 62906885; -.
DR EPD; P27987; -.
DR jPOST; P27987; -.
DR MassIVE; P27987; -.
DR MaxQB; P27987; -.
DR PaxDb; P27987; -.
DR PeptideAtlas; P27987; -.
DR PRIDE; P27987; -.
DR ProteomicsDB; 54433; -. [P27987-1]
DR ProteomicsDB; 54434; -. [P27987-2]
DR Antibodypedia; 34652; 227 antibodies from 27 providers.
DR DNASU; 3707; -.
DR Ensembl; ENST00000272117.8; ENSP00000272117.3; ENSG00000143772.11. [P27987-1]
DR Ensembl; ENST00000366784.1; ENSP00000355748.1; ENSG00000143772.11. [P27987-2]
DR Ensembl; ENST00000429204.6; ENSP00000411152.1; ENSG00000143772.11. [P27987-1]
DR GeneID; 3707; -.
DR KEGG; hsa:3707; -.
DR MANE-Select; ENST00000429204.6; ENSP00000411152.1; NM_002221.4; NP_002212.3.
DR UCSC; uc001hqh.4; human. [P27987-1]
DR CTD; 3707; -.
DR DisGeNET; 3707; -.
DR GeneCards; ITPKB; -.
DR HGNC; HGNC:6179; ITPKB.
DR HPA; ENSG00000143772; Tissue enhanced (brain, choroid plexus).
DR MIM; 147522; gene.
DR neXtProt; NX_P27987; -.
DR OpenTargets; ENSG00000143772; -.
DR PharmGKB; PA29976; -.
DR VEuPathDB; HostDB:ENSG00000143772; -.
DR eggNOG; KOG1621; Eukaryota.
DR GeneTree; ENSGT00940000156764; -.
DR HOGENOM; CLU_017767_4_0_1; -.
DR InParanoid; P27987; -.
DR OMA; RTKSWGD; -.
DR PhylomeDB; P27987; -.
DR TreeFam; TF318394; -.
DR BioCyc; MetaCyc:HS07103-MON; -.
DR BRENDA; 2.7.1.127; 2681.
DR PathwayCommons; P27987; -.
DR Reactome; R-HSA-1855204; Synthesis of IP3 and IP4 in the cytosol.
DR SignaLink; P27987; -.
DR SIGNOR; P27987; -.
DR BioGRID-ORCS; 3707; 14 hits in 1073 CRISPR screens.
DR ChiTaRS; ITPKB; human.
DR GeneWiki; ITPKB; -.
DR GenomeRNAi; 3707; -.
DR Pharos; P27987; Tchem.
DR PRO; PR:P27987; -.
DR Proteomes; UP000005640; Chromosome 1.
DR RNAct; P27987; protein.
DR Bgee; ENSG00000143772; Expressed in lateral globus pallidus and 180 other tissues.
DR Genevisible; P27987; HS.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005856; C:cytoskeleton; IDA:UniProtKB.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0005783; C:endoplasmic reticulum; IDA:UniProtKB.
DR GO; GO:0016020; C:membrane; IEA:Ensembl.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0005516; F:calmodulin binding; IEA:UniProtKB-KW.
DR GO; GO:0000828; F:inositol hexakisphosphate kinase activity; IBA:GO_Central.
DR GO; GO:0008440; F:inositol-1,4,5-trisphosphate 3-kinase activity; IDA:UniProtKB.
DR GO; GO:0016301; F:kinase activity; IBA:GO_Central.
DR GO; GO:0007166; P:cell surface receptor signaling pathway; IEA:Ensembl.
DR GO; GO:0071277; P:cellular response to calcium ion; IDA:UniProtKB.
DR GO; GO:0035726; P:common myeloid progenitor cell proliferation; IEA:Ensembl.
DR GO; GO:0032958; P:inositol phosphate biosynthetic process; IBA:GO_Central.
DR GO; GO:0032957; P:inositol trisphosphate metabolic process; IDA:UniProtKB.
DR GO; GO:0000165; P:MAPK cascade; IEA:Ensembl.
DR GO; GO:0002262; P:myeloid cell homeostasis; IEA:Ensembl.
DR GO; GO:0045638; P:negative regulation of myeloid cell differentiation; IEA:Ensembl.
DR GO; GO:0033030; P:negative regulation of neutrophil apoptotic process; IEA:Ensembl.
DR GO; GO:0046854; P:phosphatidylinositol phosphate biosynthetic process; IDA:UniProtKB.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR GO; GO:0046638; P:positive regulation of alpha-beta T cell differentiation; IEA:Ensembl.
DR GO; GO:0046579; P:positive regulation of Ras protein signal transduction; IEA:Ensembl.
DR GO; GO:0045059; P:positive thymic T cell selection; IEA:Ensembl.
DR GO; GO:0001932; P:regulation of protein phosphorylation; IEA:Ensembl.
DR GO; GO:0007165; P:signal transduction; TAS:ProtInc.
DR Gene3D; 3.30.470.160; -; 1.
DR InterPro; IPR005522; IPK.
DR InterPro; IPR038286; IPK_sf.
DR PANTHER; PTHR12400; PTHR12400; 2.
DR Pfam; PF03770; IPK; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; ATP-binding; Calmodulin-binding; Cytoplasm;
KW Cytoskeleton; Endoplasmic reticulum; Kinase; Nucleotide-binding;
KW Phosphoprotein; Reference proteome; Transferase.
FT CHAIN 1..946
FT /note="Inositol-trisphosphate 3-kinase B"
FT /id="PRO_0000066868"
FT REGION 19..128
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 156..288
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 308..472
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 486..561
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 580..638
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 768..776
FT /note="Calmodulin-binding"
FT /evidence="ECO:0000250"
FT COMPBIAS 78..102
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 207..224
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 395..413
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 524..541
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 592..614
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 679
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 690
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 730..732
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 743
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 745
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 766
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 793..800
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 817
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 897
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 900
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT MOD_RES 43
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18088087,
FT ECO:0007744|PubMed:18669648"
FT MOD_RES 49
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18088087,
FT ECO:0007744|PubMed:18669648"
FT MOD_RES 71
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:19690332"
FT MOD_RES 204
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P42335"
FT MOD_RES 269
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P42335"
FT VAR_SEQ 645..946
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_016092"
FT VARIANT 322
FT /note="A -> T (in dbSNP:rs3754413)"
FT /id="VAR_053444"
FT VARIANT 408
FT /note="S -> A (in dbSNP:rs6667260)"
FT /evidence="ECO:0000269|PubMed:11846419,
FT ECO:0000269|PubMed:15489334"
FT /id="VAR_023768"
FT VARIANT 552
FT /note="P -> Q (in dbSNP:rs708776)"
FT /evidence="ECO:0000269|PubMed:11846419,
FT ECO:0000269|PubMed:15489334, ECO:0000269|PubMed:1654894,
FT ECO:0000269|Ref.2"
FT /id="VAR_022380"
FT MUTAGEN 897
FT /note="D->N: Loss of kinase activity."
FT /evidence="ECO:0000269|PubMed:12747803"
FT CONFLICT 173
FT /note="R -> H (in Ref. 2; CAC40650 and 4; AAH15009)"
FT /evidence="ECO:0000305"
FT CONFLICT 210
FT /note="P -> S (in Ref. 2; CAC40650)"
FT /evidence="ECO:0000305"
FT CONFLICT 297..301
FT /note="GASLT -> APSFP (in Ref. 2; CAC40650)"
FT /evidence="ECO:0000305"
FT CONFLICT 442..443
FT /note="RV -> IP (in Ref. 5)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 946 AA; 102376 MW; 2CCBCBE7AEF26848 CRC64;
MAVYCYALNS LVIMNSANEM KSGGGPGPSG SETPPPPRRA VLSPGSVFSP GRGASFLFPP
AESLSPEEPR SPGGWRSGRR RLNSSSGSGS GSSGSSVSSP SWAGRLRGDR QQVVAAGTLS
PPGPEEAKRK LRILQRELQN VQVNQKVGMF EAHIQAQSSA IQAPRSPRLG RARSPSPCPF
RSSSQPPGRV LVQGARSEER RTKSWGEQCP ETSGTDSGRK GGPSLCSSQV KKGMPPLPGR
AAPTGSEAQG PSAFVRMEKG IPASPRCGSP TAMEIDKRGS PTPGTRSCLA PSLGLFGASL
TMATEVAARV TSTGPHRPQD LALTEPSGRA RELEDLQPPE ALVERQGQFL GSETSPAPER
GGPRDGEPPG KMGKGYLPCG MPGSGEPEVG KRPEETTVSV QSAESSDSLS WSRLPRALAS
VGPEEARSGA PVGGGRWQLS DRVEGGSPTL GLLGGSPSAQ PGTGNVEAGI PSGRMLEPLP
CWDAAKDLKE PQCPPGDRVG VQPGNSRVWQ GTMEKAGLAW TRGTGVQSEG TWESQRQDSD
ALPSPELLPQ DPDKPFLRKA CSPSNIPAVI ITDMGTQEDG ALEETQGSPR GNLPLRKLSS
SSASSTGFSS SYEDSEEDIS SDPERTLDPN SAFLHTLDQQ KPRVSKSWRK IKNMVHWSPF
VMSFKKKYPW IQLAGHAGSF KAAANGRILK KHCESEQRCL DRLMVDVLRP FVPAYHGDVV
KDGERYNQMD DLLADFDSPC VMDCKMGIRT YLEEELTKAR KKPSLRKDMY QKMIEVDPEA
PTEEEKAQRA VTKPRYMQWR ETISSTATLG FRIEGIKKED GTVNRDFKKT KTREQVTEAF
REFTKGNHNI LIAYRDRLKA IRTTLEVSPF FKCHEVIGSS LLFIHDKKEQ AKVWMIDFGK
TTPLPEGQTL QHDVPWQEGN REDGYLSGLN NLVDILTEMS QDAPLA
