CDK6_MOUSE
ID CDK6_MOUSE Reviewed; 326 AA.
AC Q64261; Q9R1D2; Q9R1D3;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 30-APR-2003, sequence version 2.
DT 03-AUG-2022, entry version 193.
DE RecName: Full=Cyclin-dependent kinase 6;
DE EC=2.7.11.22;
DE AltName: Full=CR2 protein kinase;
DE Short=CRK2;
DE AltName: Full=Cell division protein kinase 6;
DE AltName: Full=Serine/threonine-protein kinase PLSTIRE;
GN Name=Cdk6; Synonyms=Cdkn6, Crk2;
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 [MRNA].
RC STRAIN=BALB/cJ, C57BL/6J, and SPRET/Ei; TISSUE=Testis;
RX PubMed=10384057; DOI=10.1007/s003359901088;
RA Thomas J.W., Lee-Lin S.Q., Green E.D.;
RT "Human-mouse comparative mapping of the genomic region containing CDK6:
RT localization of an evolutionary breakpoint.";
RL Mamm. Genome 10:764-767(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Cecum;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 149-183.
RC STRAIN=CBA/J; TISSUE=Bone marrow;
RX PubMed=8444355; DOI=10.1016/0378-1119(93)90411-u;
RA Ershler M.A., Nagorskaya T.V., Visser J.W.M., Belyavsky A.V.;
RT "Novel CDC2-related protein kinases produced in murine hematopoietic stem
RT cells.";
RL Gene 124:305-306(1993).
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 149-183.
RC STRAIN=CBA/J; TISSUE=Bone marrow;
RX PubMed=1459009;
RA Ershler M.A., Nagorskaya T.V., Visser J.W.M., Belyavsky A.V.;
RT "Identification of new protein kinase genes, similar to kinases of the cdc2
RT family and expressed in murine hematopoietic stem cells.";
RL Dokl. Akad. Nauk SSSR 324:893-897(1992).
RN [5]
RP DISRUPTION PHENOTYPE.
RX PubMed=15315761; DOI=10.1016/j.cell.2004.08.002;
RA Malumbres M., Sotillo R., Santamaria D., Galan J., Cerezo A., Ortega S.,
RA Dubus P., Barbacid M.;
RT "Mammalian cells cycle without the D-type cyclin-dependent kinases Cdk4 and
RT Cdk6.";
RL Cell 118:493-504(2004).
RN [6]
RP FUNCTION IN CELL DIFFERENTIATION.
RX PubMed=16767702; DOI=10.1002/jcb.20966;
RA Slomiany P., Baker T., Elliott E.R., Grossel M.J.;
RT "Changes in motility, gene expression and actin dynamics: Cdk6-induced
RT cytoskeletal changes associated with differentiation in mouse astrocytes.";
RL J. Cell. Biochem. 99:635-646(2006).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-319, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brown adipose tissue, Heart, Liver, Lung, and Spleen;
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 [8]
RP FUNCTION IN THYMOCYTE DEVELOPMENT, DISRUPTION PHENOTYPE, AND MUTAGENESIS OF
RP ARG-31 AND LYS-43.
RX PubMed=21508411; DOI=10.1182/blood-2010-08-300517;
RA Hu M.G., Deshpande A., Schlichting N., Hinds E.A., Mao C., Dose M.,
RA Hu G.F., Van Etten R.A., Gounari F., Hinds P.W.;
RT "CDK6 kinase activity is required for thymocyte development.";
RL Blood 117:6120-6131(2011).
RN [9]
RP FUNCTION IN NEURON PRODUCTION, DISRUPTION PHENOTYPE, AND TISSUE
RP SPECIFICITY.
RX PubMed=21319271; DOI=10.1002/stem.616;
RA Beukelaers P., Vandenbosch R., Caron N., Nguyen L., Belachew S., Moonen G.,
RA Kiyokawa H., Barbacid M., Santamaria D., Malgrange B.;
RT "Cdk6-dependent regulation of G(1) length controls adult neurogenesis.";
RL Stem Cells 29:713-724(2011).
RN [10]
RP TISSUE SPECIFICITY, AND SUBCELLULAR LOCATION.
RX PubMed=23918663; DOI=10.1093/hmg/ddt374;
RA Hussain M.S., Baig S.M., Neumann S., Peche V.S., Szczepanski S.,
RA Nurnberg G., Tariq M., Jameel M., Khan T.N., Fatima A., Malik N.A.,
RA Ahmad I., Altmuller J., Frommolt P., Thiele H., Hohne W., Yigit G.,
RA Wollnik B., Neubauer B.A., Nurnberg P., Noegel A.A.;
RT "CDK6 associates with the centrosome during mitosis and is mutated in a
RT large Pakistani family with primary microcephaly.";
RL Hum. Mol. Genet. 22:5199-5214(2013).
CC -!- FUNCTION: Serine/threonine-protein kinase involved in the control of
CC the cell cycle and differentiation; promotes G1/S transition.
CC Phosphorylates pRB/RB1 and NPM1. Interacts with D-type G1 cyclins
CC during interphase at G1 to form a pRB/RB1 kinase and controls the
CC entrance into the cell cycle. Involved in initiation and maintenance of
CC cell cycle exit during cell differentiation; prevents cell
CC proliferation and regulates negatively cell differentiation, but is
CC required for the proliferation of specific cell types (e.g. erythroid
CC and hematopoietic cells). Essential for cell proliferation within the
CC dentate gyrus of the hippocampus and the subventricular zone of the
CC lateral ventricles. Required during thymocyte development. Promotes the
CC production of newborn neurons, probably by modulating G1 length.
CC Promotes, at least in astrocytes, changes in patterns of gene
CC expression, changes in the actin cytoskeleton including loss of stress
CC fibers, and enhanced motility during cell differentiation. Prevents
CC myeloid differentiation by interfering with RUNX1 and reducing its
CC transcription transactivation activity, but promotes proliferation of
CC normal myeloid progenitors. Delays senescence. Promotes the
CC proliferation of beta-cells in pancreatic islets of Langerhans (By
CC similarity). May play a role in the centrosome organization during the
CC cell cycle phases. {ECO:0000250|UniProtKB:Q00534,
CC ECO:0000269|PubMed:16767702, ECO:0000269|PubMed:21319271,
CC ECO:0000269|PubMed:21508411}.
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=2.7.11.22;
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=2.7.11.22;
CC -!- ACTIVITY REGULATION: Activated by Thr-177 phosphorylation and Tyr-24
CC dephosphorylation (By similarity). Rapidly down-regulated prior to cell
CC differentiation (e.g. erythroid and osteoblast) (By similarity).
CC {ECO:0000250}.
CC -!- SUBUNIT: Interaction with D-type G1 cyclins. Cyclin binding promotes
CC enzyme activation by phosphorylation at Thr-177 (By similarity). Binds
CC to RUNX1, CDKN2D, FBXO7 and CDKN2C/p18-INK4c. Forms a cytoplasmic
CC complex with Hsp90/HSP90AB1 and CDC37. FBXO7-binding promotes D-type
CC cyclin binding (By similarity). {ECO:0000250}.
CC -!- INTERACTION:
CC Q64261; P30282: Ccnd3; NbExp=2; IntAct=EBI-847380, EBI-847337;
CC Q64261; P05627: Jun; NbExp=2; IntAct=EBI-847380, EBI-764369;
CC Q64261; P42227: Stat3; NbExp=3; IntAct=EBI-847380, EBI-602878;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q00534}. Nucleus
CC {ECO:0000250|UniProtKB:Q00534}. Cell projection, ruffle
CC {ECO:0000250|UniProtKB:Q00534}. Cytoplasm, cytoskeleton, microtubule
CC organizing center, centrosome {ECO:0000250|UniProtKB:Q00534}.
CC Note=Localized to the ruffling edge of spreading fibroblasts. Kinase
CC activity only in nucleus (By similarity). Present in the cytosol and in
CC the nucleus in interphase cells and at the centrosome during mitosis
CC from prophase to telophase (By similarity). Localized to the cytosol of
CC neurons and showed prominent staining around either side of the
CC nucleus. {ECO:0000250|UniProtKB:Q00534, ECO:0000269|PubMed:23918663}.
CC -!- TISSUE SPECIFICITY: Expressed in subgranular zone (SGZ) of the
CC hippocampal dentate gyrus (DG) and the subventricular zone (SVZ) of the
CC lateral ventricles whose neural precursor cells (NPC) give rise to
CC dentate granule neurons and olfactory bulb (OB) interneurons,
CC respectively. Expressed in the neuroepithelium of the cerebral cortex
CC of the developing brain. {ECO:0000269|PubMed:21319271,
CC ECO:0000269|PubMed:23918663}.
CC -!- PTM: Thr-177 phosphorylation and Tyr-24 dephosphorylation promotes
CC kinase activity. {ECO:0000250}.
CC -!- DISRUPTION PHENOTYPE: Slight anemia and defective proliferation of some
CC hematopoietic cells, thymocytes and progenitor cells. Females are
CC reduced in size and often sterile. Prevents the expansion of neuronally
CC committed precursors by prematurely exiting the cell cycle and
CC lengthening G1 phase duration, reducing concomitantly the production of
CC newborn neurons. {ECO:0000269|PubMed:15315761,
CC ECO:0000269|PubMed:21319271, ECO:0000269|PubMed:21508411}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. CMGC Ser/Thr
CC protein kinase family. CDC2/CDKX subfamily. {ECO:0000305}.
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DR EMBL; AF132483; AAD43504.1; -; mRNA.
DR EMBL; AF132482; AAD43503.1; -; mRNA.
DR EMBL; AK078973; BAC37489.1; -; mRNA.
DR EMBL; X65068; CAA46201.1; -; mRNA.
DR CCDS; CCDS19062.1; -.
DR PIR; PN0483; PN0483.
DR RefSeq; NP_034003.1; NM_009873.3.
DR AlphaFoldDB; Q64261; -.
DR SMR; Q64261; -.
DR BioGRID; 198649; 14.
DR ComplexPortal; CPX-2079; Cyclin D3-CDK6 complex.
DR ComplexPortal; CPX-2080; Cyclin D1-CDK6 complex.
DR CORUM; Q64261; -.
DR DIP; DIP-24175N; -.
DR IntAct; Q64261; 6.
DR STRING; 10090.ENSMUSP00000126024; -.
DR iPTMnet; Q64261; -.
DR PhosphoSitePlus; Q64261; -.
DR EPD; Q64261; -.
DR jPOST; Q64261; -.
DR MaxQB; Q64261; -.
DR PaxDb; Q64261; -.
DR PRIDE; Q64261; -.
DR ProteomicsDB; 280040; -.
DR Antibodypedia; 1130; 1004 antibodies from 43 providers.
DR DNASU; 12571; -.
DR Ensembl; ENSMUST00000042410; ENSMUSP00000037925; ENSMUSG00000040274.
DR Ensembl; ENSMUST00000165117; ENSMUSP00000126024; ENSMUSG00000040274.
DR GeneID; 12571; -.
DR KEGG; mmu:12571; -.
DR UCSC; uc008wgu.1; mouse.
DR CTD; 1021; -.
DR MGI; MGI:1277162; Cdk6.
DR VEuPathDB; HostDB:ENSMUSG00000040274; -.
DR eggNOG; KOG0594; Eukaryota.
DR GeneTree; ENSGT00940000157957; -.
DR HOGENOM; CLU_000288_181_1_1; -.
DR InParanoid; Q64261; -.
DR OMA; MLSYDLH; -.
DR OrthoDB; 988547at2759; -.
DR PhylomeDB; Q64261; -.
DR TreeFam; TF101022; -.
DR Reactome; R-MMU-2559580; Oxidative Stress Induced Senescence.
DR Reactome; R-MMU-2559582; Senescence-Associated Secretory Phenotype (SASP).
DR Reactome; R-MMU-2559585; Oncogene Induced Senescence.
DR Reactome; R-MMU-69231; Cyclin D associated events in G1.
DR Reactome; R-MMU-8934593; Regulation of RUNX1 Expression and Activity.
DR Reactome; R-MMU-9754119; Drug-mediated inhibition of CDK4/CDK6 activity.
DR BioGRID-ORCS; 12571; 11 hits in 78 CRISPR screens.
DR ChiTaRS; Cdk6; mouse.
DR PRO; PR:Q64261; -.
DR Proteomes; UP000000589; Chromosome 5.
DR RNAct; Q64261; protein.
DR Bgee; ENSMUSG00000040274; Expressed in gastrula and 190 other tissues.
DR ExpressionAtlas; Q64261; baseline and differential.
DR Genevisible; Q64261; MM.
DR GO; GO:0005813; C:centrosome; ISS:UniProtKB.
DR GO; GO:0097132; C:cyclin D2-CDK6 complex; IDA:MGI.
DR GO; GO:0000307; C:cyclin-dependent protein kinase holoenzyme complex; ISO:MGI.
DR GO; GO:0005737; C:cytoplasm; ISO:MGI.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0016592; C:mediator complex; IBA:GO_Central.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005634; C:nucleus; ISO:MGI.
DR GO; GO:0001726; C:ruffle; ISO:MGI.
DR GO; GO:0005524; F:ATP binding; ISO:MGI.
DR GO; GO:0030332; F:cyclin binding; ISO:MGI.
DR GO; GO:0004693; F:cyclin-dependent protein serine/threonine kinase activity; ISO:MGI.
DR GO; GO:0098770; F:FBXO family protein binding; ISO:MGI.
DR GO; GO:0016301; F:kinase activity; IDA:MGI.
DR GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA.
DR GO; GO:0008353; F:RNA polymerase II CTD heptapeptide repeat kinase activity; IBA:GO_Central.
DR GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR GO; GO:0043697; P:cell dedifferentiation; ISO:MGI.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR GO; GO:0042063; P:gliogenesis; ISO:MGI.
DR GO; GO:0002244; P:hematopoietic progenitor cell differentiation; IMP:MGI.
DR GO; GO:0060218; P:hematopoietic stem cell differentiation; IMP:MGI.
DR GO; GO:0030097; P:hemopoiesis; IMP:BHF-UCL.
DR GO; GO:0045786; P:negative regulation of cell cycle; ISO:MGI.
DR GO; GO:2000773; P:negative regulation of cellular senescence; ISO:MGI.
DR GO; GO:0050680; P:negative regulation of epithelial cell proliferation; ISO:MGI.
DR GO; GO:0045656; P:negative regulation of monocyte differentiation; ISS:UniProtKB.
DR GO; GO:0045638; P:negative regulation of myeloid cell differentiation; ISO:MGI.
DR GO; GO:0045668; P:negative regulation of osteoblast differentiation; ISO:MGI.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IMP:MGI.
DR GO; GO:0007219; P:Notch signaling pathway; IDA:MGI.
DR GO; GO:0001954; P:positive regulation of cell-matrix adhesion; ISO:MGI.
DR GO; GO:0048146; P:positive regulation of fibroblast proliferation; ISO:MGI.
DR GO; GO:0010628; P:positive regulation of gene expression; IDA:MGI.
DR GO; GO:0006468; P:protein phosphorylation; ISO:MGI.
DR GO; GO:0051726; P:regulation of cell cycle; IBA:GO_Central.
DR GO; GO:0045646; P:regulation of erythrocyte differentiation; ISO:MGI.
DR GO; GO:0010468; P:regulation of gene expression; ISO:MGI.
DR GO; GO:1902036; P:regulation of hematopoietic stem cell differentiation; IMP:MGI.
DR GO; GO:0009615; P:response to virus; IEA:Ensembl.
DR GO; GO:0033077; P:T cell differentiation in thymus; IMP:MGI.
DR GO; GO:0003323; P:type B pancreatic cell development; ISO:MGI.
DR CDD; cd07862; STKc_CDK6; 1.
DR InterPro; IPR028788; CDK6.
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 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; Cell cycle; Cell division; Cell projection;
KW Cytoplasm; Cytoskeleton; Differentiation; Kinase; Nucleotide-binding;
KW Nucleus; Phosphoprotein; Reference proteome;
KW Serine/threonine-protein kinase; Transferase.
FT CHAIN 1..326
FT /note="Cyclin-dependent kinase 6"
FT /id="PRO_0000085790"
FT DOMAIN 13..300
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT ACT_SITE 145
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 19..27
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 43
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0000250|UniProtKB:Q00534"
FT MOD_RES 13
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:Q00534"
FT MOD_RES 24
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:Q00534"
FT MOD_RES 49
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q00534"
FT MOD_RES 70
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q00534"
FT MOD_RES 177
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q00534"
FT MOD_RES 264
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q00534"
FT MOD_RES 319
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 325
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q00534"
FT VARIANT 321
FT /note="S -> A (in strain: SPRET/Ei)"
FT MUTAGEN 31
FT /note="R->C: Enhanced kinase activity. Over-production of
FT thymocytes and hematopoietic stem cells and progenitor
FT cells."
FT /evidence="ECO:0000269|PubMed:21508411"
FT MUTAGEN 43
FT /note="K->M: Loss of kinase activity. Pronounced reduction
FT in thymocytes and hematopoietic stem cells and progenitor
FT cells."
FT /evidence="ECO:0000269|PubMed:21508411"
SQ SEQUENCE 326 AA; 37028 MW; 127B7ECFFC54C3AC CRC64;
MEKDSLSRAD QQYECVAEIG EGAYGKVFKA RDLKNGGRFV ALKRVRVQTS EEGMPLSTIR
EVAVLRHLET FEHPNVVRLF DVCTVSRTDR ETKLTLVFEH VDQDLTTYLD KVPEPGVPTE
TIKDMMFQLL RGLDFLHSHR VVHRDLKPQN ILVTSSGQIK LADFGLARIY SFQMALTSVV
VTLWYRAPEV LLQSSYATPV DLWSVGCIFA EMFRRKPLFR GSSDVDQLGK ILDIIGLPGE
EDWPRDVALP RQAFHSKSAQ PIEKFVTDID ELGKDLLLKC LTFNPAKRIS AYGALNHPYF
QDLERYKDNL NSHLPSNQST SELNTA
