STK19_HUMAN
ID STK19_HUMAN Reviewed; 368 AA.
AC P49842; A6NF95; A6NFW8; B0QZR5; Q13159; Q31617; Q5JP77; Q5ST72; Q5ST75;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 18-OCT-2001, sequence version 2.
DT 03-AUG-2022, entry version 178.
DE RecName: Full=Serine/threonine-protein kinase 19 {ECO:0000305};
DE EC=2.7.11.1 {ECO:0000305|PubMed:9812991};
DE AltName: Full=Protein G11 {ECO:0000303|PubMed:8012361};
DE AltName: Full=Protein RP1 {ECO:0000303|PubMed:8132574};
GN Name=STK19 {ECO:0000303|PubMed:30712867, ECO:0000312|HGNC:HGNC:11398};
GN Synonyms=G11 {ECO:0000303|PubMed:8012361},
GN RP1 {ECO:0000303|PubMed:8132574};
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 [GENOMIC DNA / MRNA] (ISOFORMS 3 AND 4), AND TISSUE
RP SPECIFICITY.
RX PubMed=8012361; DOI=10.1093/hmg/3.3.481;
RA Sargent C.A., Anderson M.J., Hsieh S.-L., Kendall E., Gomez-Escobar N.,
RA Campbell R.D.;
RT "Characterisation of the novel gene G11 lying adjacent to the complement
RT C4A gene in the human major histocompatibility complex.";
RL Hum. Mol. Genet. 3:481-488(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORM 2).
RX PubMed=8132574; DOI=10.1016/s0021-9258(17)37217-4;
RA Liming S., Wu L., Sanlioglu S., Chen R., Mendoza A.R., Dangel A.W.,
RA Carroll M.C., Zipf W.B., Yu C.;
RT "Structure and genetics of the partially duplicated gene RP located
RT immediately upstream of the complement C4A and the C4B genes in the HLA
RT class III region. Molecular cloning, exon-intron structure, composite
RT retroposon, and breakpoint of gene duplication.";
RL J. Biol. Chem. 269:8466-8476(1994).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=14656967; DOI=10.1101/gr.1736803;
RA Xie T., Rowen L., Aguado B., Ahearn M.E., Madan A., Qin S., Campbell R.D.,
RA Hood L.;
RT "Analysis of the gene-dense major histocompatibility complex class III
RT region and its comparison to mouse.";
RL Genome Res. 13:2621-2636(2003).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND VARIANT GLY-311.
RX PubMed=14574404; DOI=10.1038/nature02055;
RA Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L.,
RA Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., Gilbert J.G.R.,
RA Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D.,
RA Andrews T.D., Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J.,
RA Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H.,
RA Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J.,
RA Brown J.Y., Burford D.C., Burrill W., Burton J., Carder C., Carter N.P.,
RA Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V.,
RA Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J.,
RA Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., Ellington A.E.,
RA Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J.,
RA French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J.,
RA Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C.,
RA Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A.,
RA Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R.,
RA Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M.,
RA Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K.,
RA Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R.,
RA Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M.,
RA Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A.,
RA Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L.,
RA Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I.,
RA Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y.,
RA Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E.,
RA Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A.,
RA Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W.,
RA Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M.,
RA West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J.,
RA Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M.,
RA Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I.,
RA Rogers J., Beck S.;
RT "The DNA sequence and analysis of human chromosome 6.";
RL Nature 425:805-811(2003).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP PARTIAL NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND ALTERNATIVE SPLICING
RP (ISOFORM 4).
RC TISSUE=Blood;
RX PubMed=8575831; DOI=10.1007/bf00587313;
RA Ulgiati D., Townend D.C., Christiansen F.T., Dawkins R.L., Abraham L.J.;
RT "Complete sequence of the complement C4 gene from the HLA-A1, B8, C4AQ0,
RT C4B1, DR3 haplotype.";
RL Immunogenetics 43:250-252(1996).
RN [7]
RP COFACTOR, SUBCELLULAR LOCATION, AND MUTAGENESIS OF LYS-300; LYS-315 AND
RP LYS-317.
RX PubMed=9812991; DOI=10.1074/jbc.273.47.30954;
RA Gomez-Escobar N., Chou C.-F., Lin W.-W., Hsieh S.-L., Campbell R.D.;
RT "The G11 gene located in the major histocompatibility complex encodes a
RT novel nuclear serine/threonine protein kinase.";
RL J. Biol. Chem. 273:30954-30960(1998).
RN [8]
RP INTERACTION WITH BAG1.
RC TISSUE=T-cell;
RX PubMed=15986447; DOI=10.1002/ijc.21259;
RA Wadle A., Mischo A., Henrich P.P., Stenner-Lieven F., Scherer C., Imig J.,
RA Petersen G., Pfreundschuh M., Renner C.;
RT "Characterization of Hap/BAG-1 variants as RP1 binding proteins with
RT antiapoptotic activity.";
RL Int. J. Cancer 117:896-904(2005).
RN [9]
RP VARIANTS [LARGE SCALE ANALYSIS] ASN-89; GLY-311 AND VAL-331.
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).
RN [10]
RP VARIANT ASN-89, CHARACTERIZATION OF VARIANT ASN-89, FUNCTION, CATALYTIC
RP ACTIVITY, ACTIVITY REGULATION, AND MUTAGENESIS OF VAL-134 AND LEU-139.
RX PubMed=30712867; DOI=10.1016/j.cell.2019.01.002;
RA Yin C., Zhu B., Zhang T., Liu T., Chen S., Liu Y., Li X., Miao X., Li S.,
RA Mi X., Zhang J., Li L., Wei G., Xu Z.X., Gao X., Huang C., Wei Z.,
RA Goding C.R., Wang P., Deng X., Cui R.;
RT "Pharmacological targeting of STK19 inhibits oncogenic NRAS-driven
RT melanomagenesis.";
RL Cell 176:1113-1127(2019).
CC -!- FUNCTION: Serine/threonine-protein kinase that acts as a key regulator
CC of NRAS signaling by mediating phosphorylation of NRAS at 'Ser-89',
CC thereby enhancing NRAS-binding to its downstream effectors.
CC {ECO:0000269|PubMed:30712867}.
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:30712867, ECO:0000305|PubMed:9812991};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:17990;
CC Evidence={ECO:0000269|PubMed:30712867, ECO:0000305|PubMed:9812991};
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; Evidence={ECO:0000305|PubMed:9812991};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:46609;
CC Evidence={ECO:0000305|PubMed:9812991};
CC -!- COFACTOR:
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000269|PubMed:9812991};
CC Note=Divalent metal cations. Has a preference for Mn(2+).
CC {ECO:0000269|PubMed:9812991};
CC -!- ACTIVITY REGULATION: Specifically inhibited by ZT-12-037-01 (1a) (N2-
CC cyclopropyl-N4-(1-isopropylpiperidin-4-yl)- 6,7-dimethoxyquinazoline-
CC 2,4-diamine) (PubMed:30712867). Inhibition by ZT-12-037-01 (1a) blocks
CC oncogenic NRAS-driven melanocyte malignant transformation and melanoma
CC growth (PubMed:30712867). {ECO:0000269|PubMed:30712867}.
CC -!- SUBUNIT: Interacts (via N-terminus) with BAG1.
CC {ECO:0000269|PubMed:15986447}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:9812991}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Name=1; Synonyms=G11-Z;
CC IsoId=P49842-1; Sequence=Displayed;
CC Name=2; Synonyms=G11-Z-short;
CC IsoId=P49842-2; Sequence=VSP_004433;
CC Name=3; Synonyms=G11-Y {ECO:0000303|PubMed:8012361};
CC IsoId=P49842-3; Sequence=VSP_004432;
CC Name=4; Synonyms=G11-Y-short {ECO:0000303|PubMed:8012361};
CC IsoId=P49842-4; Sequence=VSP_004432, VSP_004433;
CC -!- TISSUE SPECIFICITY: Monocytes, hepatocytes, epithelial cells, T- and B-
CC lymphocytes. {ECO:0000269|PubMed:8012361}.
CC -!- DISEASE: Note=Gain-of-function variants in STK19 are involved in NRAS-
CC driven melanomagenesis (PubMed:30712867). Melanoma are malignant
CC neoplasm of melanocytes, arising de novo or from a pre-existing benign
CC nevus, which occurs most often in the skin but also may involve other
CC sites (PubMed:30712867). Conditional knockin mice overexpressing Asn-89
CC variant exhibit hyperpigmentation of the skin, ears, and tail, and the
CC melanin content in skin was significantly increased after tamoxifen
CC induction (PubMed:30712867). Moreover, knockin mice overexpressing Asn-
CC 89 variant promote NRAS 'Arg-61'-driven melanomagenesis
CC (PubMed:30712867). {ECO:0000269|PubMed:30712867}.
CC -!- SIMILARITY: Belongs to the STK19 family. {ECO:0000305}.
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DR EMBL; X77474; CAA54622.1; -; Genomic_DNA.
DR EMBL; X77489; CAA54622.1; JOINED; Genomic_DNA.
DR EMBL; X77490; CAA54622.1; JOINED; Genomic_DNA.
DR EMBL; X77491; CAA54622.1; JOINED; Genomic_DNA.
DR EMBL; X77474; CAA54623.1; -; Genomic_DNA.
DR EMBL; X77489; CAA54623.1; JOINED; Genomic_DNA.
DR EMBL; X77490; CAA54623.1; JOINED; Genomic_DNA.
DR EMBL; X77491; CAA54623.1; JOINED; Genomic_DNA.
DR EMBL; X77386; CAA54565.1; -; mRNA.
DR EMBL; L26261; AAA20120.1; -; Genomic_DNA.
DR EMBL; L26260; AAA20122.1; -; mRNA.
DR EMBL; AF019413; AAB67976.1; -; Genomic_DNA.
DR EMBL; AL049547; CAB89303.1; -; Genomic_DNA.
DR EMBL; AL049547; CAB89304.1; -; Genomic_DNA.
DR EMBL; AL645922; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL662849; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL844853; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BX679671; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CR753822; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CR753845; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CR759782; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471081; EAX03566.1; -; Genomic_DNA.
DR EMBL; CH471081; EAX03567.1; -; Genomic_DNA.
DR EMBL; U24578; AAA99716.1; -; Genomic_DNA.
DR CCDS; CCDS34417.1; -. [P49842-4]
DR CCDS; CCDS4733.1; -. [P49842-1]
DR PIR; B53439; A53439.
DR RefSeq; NP_004188.1; NM_004197.1. [P49842-4]
DR RefSeq; NP_115830.1; NM_032454.1. [P49842-1]
DR AlphaFoldDB; P49842; -.
DR BioGRID; 114383; 18.
DR IntAct; P49842; 12.
DR STRING; 9606.ENSP00000364482; -.
DR iPTMnet; P49842; -.
DR PhosphoSitePlus; P49842; -.
DR BioMuta; STK19; -.
DR DMDM; 19860281; -.
DR EPD; P49842; -.
DR jPOST; P49842; -.
DR MassIVE; P49842; -.
DR MaxQB; P49842; -.
DR PaxDb; P49842; -.
DR PeptideAtlas; P49842; -.
DR PRIDE; P49842; -.
DR ProteomicsDB; 56153; -. [P49842-1]
DR ProteomicsDB; 56154; -. [P49842-2]
DR ProteomicsDB; 56155; -. [P49842-3]
DR ProteomicsDB; 56156; -. [P49842-4]
DR Antibodypedia; 28162; 195 antibodies from 24 providers.
DR DNASU; 8859; -.
DR Ensembl; ENST00000375331.7; ENSP00000364480.3; ENSG00000204344.16. [P49842-4]
DR Ensembl; ENST00000375333.3; ENSP00000364482.3; ENSG00000204344.16. [P49842-3]
DR Ensembl; ENST00000383327.8; ENSP00000372817.4; ENSG00000206342.12.
DR Ensembl; ENST00000424104.5; ENSP00000393272.1; ENSG00000236250.8. [P49842-2]
DR Ensembl; ENST00000425138.5; ENSP00000395028.1; ENSG00000234947.8. [P49842-2]
DR Ensembl; ENST00000426802.5; ENSP00000389352.1; ENSG00000226257.9. [P49842-2]
DR Ensembl; ENST00000431383.6; ENSP00000403479.2; ENSG00000226033.11. [P49842-1]
DR Ensembl; ENST00000433397.6; ENSP00000395864.2; ENSG00000234947.8. [P49842-1]
DR Ensembl; ENST00000438256.6; ENSP00000391798.2; ENSG00000236250.8. [P49842-1]
DR Ensembl; ENST00000444147.5; ENSP00000399915.1; ENSG00000226033.11. [P49842-2]
DR Ensembl; ENST00000452688.6; ENSP00000413766.2; ENSG00000226257.9. [P49842-1]
DR Ensembl; ENST00000685781.1; ENSP00000509445.1; ENSG00000204344.16. [P49842-4]
DR GeneID; 8859; -.
DR KEGG; hsa:8859; -.
DR MANE-Select; ENST00000685781.1; ENSP00000509445.1; NM_004197.2; NP_004188.2. [P49842-4]
DR UCSC; uc003nyv.4; human. [P49842-1]
DR CTD; 8859; -.
DR DisGeNET; 8859; -.
DR GeneCards; STK19; -.
DR HGNC; HGNC:11398; STK19.
DR HPA; ENSG00000204344; Low tissue specificity.
DR MIM; 604977; gene.
DR neXtProt; NX_P49842; -.
DR OpenTargets; ENSG00000204344; -.
DR PharmGKB; PA36206; -.
DR VEuPathDB; HostDB:ENSG00000204344; -.
DR eggNOG; ENOG502RDW5; Eukaryota.
DR GeneTree; ENSGT00390000018295; -.
DR HOGENOM; CLU_064399_0_0_1; -.
DR InParanoid; P49842; -.
DR OMA; FERYVIH; -.
DR OrthoDB; 1329271at2759; -.
DR PhylomeDB; P49842; -.
DR TreeFam; TF105332; -.
DR PathwayCommons; P49842; -.
DR SignaLink; P49842; -.
DR SIGNOR; P49842; -.
DR BioGRID-ORCS; 8859; 13 hits in 1110 CRISPR screens.
DR ChiTaRS; STK19; human.
DR GeneWiki; STK19; -.
DR GenomeRNAi; 8859; -.
DR Pharos; P49842; Tbio.
DR PRO; PR:P49842; -.
DR Proteomes; UP000005640; Chromosome 6.
DR RNAct; P49842; protein.
DR Bgee; ENSG00000204344; Expressed in left adrenal gland and 95 other tissues.
DR ExpressionAtlas; P49842; baseline and differential.
DR Genevisible; P49842; HS.
DR GO; GO:0016607; C:nuclear speck; IDA:HPA.
DR GO; GO:0005634; C:nucleus; TAS:ProtInc.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; IDA:UniProtKB.
DR GO; GO:0031267; F:small GTPase binding; IPI:UniProtKB.
DR GO; GO:0046579; P:positive regulation of Ras protein signal transduction; IDA:UniProtKB.
DR GO; GO:0006468; P:protein phosphorylation; IDA:UniProtKB.
DR InterPro; IPR018865; Ser/Thr_kinase_19.
DR PANTHER; PTHR15243; PTHR15243; 1.
DR Pfam; PF10494; Stk19; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; ATP-binding; Kinase; Manganese; Nucleotide-binding;
KW Nucleus; Reference proteome; Serine/threonine-protein kinase; Transferase.
FT CHAIN 1..368
FT /note="Serine/threonine-protein kinase 19"
FT /id="PRO_0000072275"
FT REGION 40..78
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT VAR_SEQ 1..110
FT /note="Missing (in isoform 3 and isoform 4)"
FT /evidence="ECO:0000303|PubMed:8012361"
FT /id="VSP_004432"
FT VAR_SEQ 222..225
FT /note="Missing (in isoform 2 and isoform 4)"
FT /evidence="ECO:0000303|PubMed:8012361,
FT ECO:0000303|PubMed:8132574"
FT /id="VSP_004433"
FT VARIANT 39
FT /note="A -> D (in dbSNP:rs34843142)"
FT /id="VAR_051387"
FT VARIANT 89
FT /note="D -> N (recurrent gain-of-function variant found in
FT metastatic melanoma; promotes NRAS signaling; somatic
FT mutation; dbSNP:rs267600971)"
FT /evidence="ECO:0000269|PubMed:17344846,
FT ECO:0000269|PubMed:30712867"
FT /id="VAR_042361"
FT VARIANT 311
FT /note="S -> G (in dbSNP:rs616634)"
FT /evidence="ECO:0000269|PubMed:14574404,
FT ECO:0000269|PubMed:17344846"
FT /id="VAR_042362"
FT VARIANT 331
FT /note="A -> V (in dbSNP:rs7743647)"
FT /evidence="ECO:0000269|PubMed:17344846"
FT /id="VAR_042363"
FT MUTAGEN 134
FT /note="V->Y: Prevents inhibition by ZT-12-037-01 (1a)
FT without affecting much the serine/threonine-protein kinase
FT activity."
FT /evidence="ECO:0000269|PubMed:30712867"
FT MUTAGEN 139
FT /note="L->V: Prevents inhibition by ZT-12-037-01 (1a)
FT without affecting much the serine/threonine-protein kinase
FT activity."
FT /evidence="ECO:0000269|PubMed:30712867"
FT MUTAGEN 300
FT /note="K->P: Partial loss of activity."
FT /evidence="ECO:0000269|PubMed:9812991"
FT MUTAGEN 315
FT /note="K->P: Partial loss of activity."
FT /evidence="ECO:0000269|PubMed:9812991"
FT MUTAGEN 317
FT /note="K->P: Complete loss of activity."
FT /evidence="ECO:0000269|PubMed:9812991"
FT CONFLICT 195..197
FT /note="QGE -> GQR (in Ref. 6; AAA99716)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 368 AA; 40916 MW; A05AC847081DE8F8 CRC64;
MQKWFSAFDD AIIQRQWRAN PSRGGGGVSF TKEVDTNVAT GAPPRRQRVP GRACPWREPI
RGRRGARPGG GDAGGTPGET VRHCSAPEDP IFRFSSLHSY PFPGTIKSRD MSWKRHHLIP
ETFGVKRRRK RGPVESDPLR GEPGSARAAV SELMQLFPRG LFEDALPPIV LRSQVYSLVP
DRTVADRQLK ELQEQGEIRI VQLGFDLDAH GIIFTEDYRT RVCDCVLKAC DGRPYAGAVQ
KFLASVLPAC GDLSFQQDQM TQTFGFRDSE ITHLVNAGVL TVRDAGSWWL AVPGAGRFIK
YFVKGRQAVL SMVRKAKYRE LLLSELLGRR APVVVRLGLT YHVHDLIGAQ LVDCISTTSG
TLLRLPET
