CDK20_HUMAN
ID CDK20_HUMAN Reviewed; 346 AA.
AC Q8IZL9; A2A389; A2A390; B4DQX1; O95137; Q5EDC4; Q5VYW1; Q9BUF4;
DT 20-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 164.
DE RecName: Full=Cyclin-dependent kinase 20;
DE EC=2.7.11.22;
DE AltName: Full=CDK-activating kinase p42;
DE Short=CAK-kinase p42;
DE AltName: Full=Cell cycle-related kinase;
DE AltName: Full=Cell division protein kinase 20;
DE AltName: Full=Cyclin-dependent protein kinase H;
DE AltName: Full=Cyclin-kinase-activating kinase p42;
GN Name=CDK20; Synonyms=CCRK, CDCH;
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 5).
RA Jiang Y., Zhao K.;
RL Submitted (NOV-1997) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 5).
RA Chen J.H., Luo W.Q., Hu S.N., Huang X.W., Tan X.Y., Yuan J.G., Qiang B.Q.;
RT "Cloning a cyclin-dependent protein kinase CDCH.";
RL Submitted (DEC-1998) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
RC TISSUE=Heart;
RA Qiu H., Depre C.;
RT "Cardiac CCRK splice variant.";
RL Submitted (JAN-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANTS LEU-86; THR-137 AND
RP ARG-281.
RG NIEHS SNPs program;
RL Submitted (SEP-2002) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2 AND 4).
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15164053; DOI=10.1038/nature02465;
RA Humphray S.J., Oliver K., Hunt A.R., Plumb R.W., Loveland J.E., Howe K.L.,
RA Andrews T.D., Searle S., Hunt S.E., Scott C.E., Jones M.C., Ainscough R.,
RA Almeida J.P., Ambrose K.D., Ashwell R.I.S., Babbage A.K., Babbage S.,
RA Bagguley C.L., Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K.,
RA Beasley H., Beasley O., Bird C.P., Bray-Allen S., Brown A.J., Brown J.Y.,
RA Burford D., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C.,
RA Chen Y., Clarke G., Clark S.Y., Clee C.M., Clegg S., Collier R.E.,
RA Corby N., Crosier M., Cummings A.T., Davies J., Dhami P., Dunn M.,
RA Dutta I., Dyer L.W., Earthrowl M.E., Faulkner L., Fleming C.J.,
RA Frankish A., Frankland J.A., French L., Fricker D.G., Garner P.,
RA Garnett J., Ghori J., Gilbert J.G.R., Glison C., Grafham D.V., Gribble S.,
RA Griffiths C., Griffiths-Jones S., Grocock R., Guy J., Hall R.E.,
RA Hammond S., Harley J.L., Harrison E.S.I., Hart E.A., Heath P.D.,
RA Henderson C.D., Hopkins B.L., Howard P.J., Howden P.J., Huckle E.,
RA Johnson C., Johnson D., Joy A.A., Kay M., Keenan S., Kershaw J.K.,
RA Kimberley A.M., King A., Knights A., Laird G.K., Langford C., Lawlor S.,
RA Leongamornlert D.A., Leversha M., Lloyd C., Lloyd D.M., Lovell J.,
RA Martin S., Mashreghi-Mohammadi M., Matthews L., McLaren S., McLay K.E.,
RA McMurray A., Milne S., Nickerson T., Nisbett J., Nordsiek G., Pearce A.V.,
RA Peck A.I., Porter K.M., Pandian R., Pelan S., Phillimore B., Povey S.,
RA Ramsey Y., Rand V., Scharfe M., Sehra H.K., Shownkeen R., Sims S.K.,
RA Skuce C.D., Smith M., Steward C.A., Swarbreck D., Sycamore N., Tester J.,
RA Thorpe A., Tracey A., Tromans A., Thomas D.W., Wall M., Wallis J.M.,
RA West A.P., Whitehead S.L., Willey D.L., Williams S.A., Wilming L.,
RA Wray P.W., Young L., Ashurst J.L., Coulson A., Blocker H., Durbin R.M.,
RA Sulston J.E., Hubbard T., Jackson M.J., Bentley D.R., Beck S., Rogers J.,
RA Dunham I.;
RT "DNA sequence and analysis of human chromosome 9.";
RL Nature 429:369-374(2004).
RN [7]
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 [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
RC TISSUE=Uterus;
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 [9]
RP FUNCTION, SUBUNIT, SUBCELLULAR LOCATION, AND MUTAGENESIS OF THR-161.
RX PubMed=14597612; DOI=10.1074/jbc.m309995200;
RA Liu Y., Wu C., Galaktionov K.;
RT "p42, a novel cyclin-dependent kinase-activating kinase in mammalian
RT cells.";
RL J. Biol. Chem. 279:4507-4514(2004).
RN [10]
RP INTERACTION WITH MAK.
RX PubMed=21986944; DOI=10.1038/onc.2011.464;
RA Wang L.Y., Kung H.J.;
RT "Male germ cell-associated kinase is overexpressed in prostate cancer cells
RT and causes mitotic defects via deregulation of APC/C(CDH1).";
RL Oncogene 31:2907-2918(2012).
RN [11]
RP VARIANT [LARGE SCALE ANALYSIS] ASN-106.
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: Required for high-level Shh responses in the developing
CC neural tube. Together with TBC1D32, controls the structure of the
CC primary cilium by coordinating assembly of the ciliary membrane and
CC axoneme, allowing GLI2 to be properly activated in response to SHH
CC signaling (By similarity). Involved in cell growth. Activates CDK2, a
CC kinase involved in the control of the cell cycle, by phosphorylating
CC residue 'Thr-160'. {ECO:0000250, ECO:0000269|PubMed:14597612}.
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 -!- SUBUNIT: Monomer. Interacts with TBC1D32 (By similarity). Interacts
CC with MAK. {ECO:0000250, ECO:0000269|PubMed:14597612,
CC ECO:0000269|PubMed:21986944}.
CC -!- INTERACTION:
CC Q8IZL9; Q9C040: TRIM2; NbExp=3; IntAct=EBI-6128565, EBI-749840;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:14597612}. Cytoplasm
CC {ECO:0000250}. Cell projection, cilium {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=5;
CC Name=1;
CC IsoId=Q8IZL9-1; Sequence=Displayed;
CC Name=2; Synonyms=Cardiac CCRK;
CC IsoId=Q8IZL9-2; Sequence=VSP_016748, VSP_016750;
CC Name=3;
CC IsoId=Q8IZL9-3; Sequence=VSP_016749, VSP_016751, VSP_016752;
CC Name=4;
CC IsoId=Q8IZL9-4; Sequence=VSP_043294, VSP_016749;
CC Name=5;
CC IsoId=Q8IZL9-5; Sequence=VSP_016749;
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. CMGC Ser/Thr
CC protein kinase family. CDC2/CDKX subfamily. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAC98920.1; Type=Frameshift; Evidence={ECO:0000305};
CC -!- WEB RESOURCE: Name=NIEHS-SNPs;
CC URL="http://egp.gs.washington.edu/data/ccrk/";
CC -!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology and
CC Haematology;
CC URL="http://atlasgeneticsoncology.org/Genes/CCRKID43196ch9q22.html";
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AF035013; AAC98920.1; ALT_FRAME; mRNA.
DR EMBL; AF113130; AAF43778.1; -; mRNA.
DR EMBL; AY904367; AAW82349.1; -; mRNA.
DR EMBL; AF547664; AAN28684.1; -; Genomic_DNA.
DR EMBL; AK075325; BAG52110.1; -; mRNA.
DR EMBL; AK298993; BAG61083.1; -; mRNA.
DR EMBL; AL353572; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471089; EAW62746.1; -; Genomic_DNA.
DR EMBL; CH471089; EAW62748.1; -; Genomic_DNA.
DR EMBL; BC002655; AAH02655.1; -; mRNA.
DR CCDS; CCDS35060.1; -. [Q8IZL9-1]
DR CCDS; CCDS55324.1; -. [Q8IZL9-2]
DR CCDS; CCDS65075.1; -. [Q8IZL9-3]
DR CCDS; CCDS6677.1; -. [Q8IZL9-5]
DR CCDS; CCDS6678.1; -. [Q8IZL9-4]
DR RefSeq; NP_001034892.1; NM_001039803.2. [Q8IZL9-1]
DR RefSeq; NP_001164110.1; NM_001170639.1. [Q8IZL9-3]
DR RefSeq; NP_001164111.1; NM_001170640.1. [Q8IZL9-2]
DR RefSeq; NP_036251.2; NM_012119.4. [Q8IZL9-5]
DR RefSeq; NP_848519.1; NM_178432.3. [Q8IZL9-4]
DR AlphaFoldDB; Q8IZL9; -.
DR SMR; Q8IZL9; -.
DR BioGRID; 117096; 116.
DR IntAct; Q8IZL9; 43.
DR STRING; 9606.ENSP00000322343; -.
DR BindingDB; Q8IZL9; -.
DR ChEMBL; CHEMBL3559690; -.
DR GlyGen; Q8IZL9; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q8IZL9; -.
DR PhosphoSitePlus; Q8IZL9; -.
DR BioMuta; CDK20; -.
DR DMDM; 74759739; -.
DR EPD; Q8IZL9; -.
DR jPOST; Q8IZL9; -.
DR MassIVE; Q8IZL9; -.
DR MaxQB; Q8IZL9; -.
DR PaxDb; Q8IZL9; -.
DR PeptideAtlas; Q8IZL9; -.
DR PRIDE; Q8IZL9; -.
DR ProteomicsDB; 71369; -. [Q8IZL9-1]
DR ProteomicsDB; 71370; -. [Q8IZL9-2]
DR ProteomicsDB; 71371; -. [Q8IZL9-3]
DR ProteomicsDB; 71372; -. [Q8IZL9-4]
DR Antibodypedia; 27918; 353 antibodies from 30 providers.
DR DNASU; 23552; -.
DR Ensembl; ENST00000325303.9; ENSP00000322343.8; ENSG00000156345.18. [Q8IZL9-1]
DR Ensembl; ENST00000336654.9; ENSP00000338975.5; ENSG00000156345.18. [Q8IZL9-4]
DR Ensembl; ENST00000375871.8; ENSP00000365031.3; ENSG00000156345.18. [Q8IZL9-2]
DR Ensembl; ENST00000375883.7; ENSP00000365043.3; ENSG00000156345.18. [Q8IZL9-5]
DR Ensembl; ENST00000605159.5; ENSP00000474485.1; ENSG00000156345.18. [Q8IZL9-3]
DR GeneID; 23552; -.
DR KEGG; hsa:23552; -.
DR MANE-Select; ENST00000325303.9; ENSP00000322343.8; NM_001039803.3; NP_001034892.1.
DR UCSC; uc004apr.4; human. [Q8IZL9-1]
DR CTD; 23552; -.
DR DisGeNET; 23552; -.
DR GeneCards; CDK20; -.
DR HGNC; HGNC:21420; CDK20.
DR HPA; ENSG00000156345; Low tissue specificity.
DR MalaCards; CDK20; -.
DR MIM; 610076; gene.
DR neXtProt; NX_Q8IZL9; -.
DR OpenTargets; ENSG00000156345; -.
DR PharmGKB; PA165585688; -.
DR VEuPathDB; HostDB:ENSG00000156345; -.
DR eggNOG; KOG0659; Eukaryota.
DR GeneTree; ENSGT00940000159128; -.
DR HOGENOM; CLU_000288_181_6_1; -.
DR InParanoid; Q8IZL9; -.
DR OMA; KITFPYH; -.
DR OrthoDB; 1367115at2759; -.
DR PhylomeDB; Q8IZL9; -.
DR TreeFam; TF327240; -.
DR PathwayCommons; Q8IZL9; -.
DR SignaLink; Q8IZL9; -.
DR SIGNOR; Q8IZL9; -.
DR BioGRID-ORCS; 23552; 10 hits in 1105 CRISPR screens.
DR ChiTaRS; CDK20; human.
DR GenomeRNAi; 23552; -.
DR Pharos; Q8IZL9; Tbio.
DR PRO; PR:Q8IZL9; -.
DR Proteomes; UP000005640; Chromosome 9.
DR RNAct; Q8IZL9; protein.
DR Bgee; ENSG00000156345; Expressed in right uterine tube and 121 other tissues.
DR ExpressionAtlas; Q8IZL9; baseline and differential.
DR Genevisible; Q8IZL9; HS.
DR GO; GO:0005929; C:cilium; IEA:UniProtKB-SubCell.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004693; F:cyclin-dependent protein serine/threonine kinase activity; IBA:GO_Central.
DR GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA.
DR GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR GO; GO:1990403; P:embryonic brain development; IEA:Ensembl.
DR GO; GO:0031076; P:embryonic camera-type eye development; IEA:Ensembl.
DR GO; GO:0048706; P:embryonic skeletal system development; IEA:Ensembl.
DR GO; GO:0021508; P:floor plate formation; IEA:Ensembl.
DR GO; GO:1901621; P:negative regulation of smoothened signaling pathway involved in dorsal/ventral neural tube patterning; IEA:Ensembl.
DR GO; GO:0001843; P:neural tube closure; IEA:Ensembl.
DR GO; GO:0061512; P:protein localization to cilium; IEA:Ensembl.
DR GO; GO:0006468; P:protein phosphorylation; IBA:GO_Central.
DR GO; GO:1903317; P:regulation of protein maturation; IEA:Ensembl.
DR GO; GO:0060021; P:roof of mouth development; IEA:Ensembl.
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 Alternative splicing; ATP-binding; Cell cycle; Cell division;
KW Cell projection; Cilium; Cytoplasm; Developmental protein; Kinase;
KW Nucleotide-binding; Nucleus; Reference proteome;
KW Serine/threonine-protein kinase; Transferase.
FT CHAIN 1..346
FT /note="Cyclin-dependent kinase 20"
FT /id="PRO_0000085701"
FT DOMAIN 4..288
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT ACT_SITE 127
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 10..18
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 33
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT VAR_SEQ 25
FT /note="E -> EPRVGWQCLPSILQ (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_043294"
FT VAR_SEQ 168..243
FT /note="WYRAPELLYGARQYDQGVDLWSVGCIMGELLNGSPLFPGKNDIEQLCYVLRI
FT LGTPNPQVWPELTELPDYNKISFK -> SSLSCRTTTRSPLRSRCPCPWRRCCLTSLPR
FT HWICWVNSFSTLLTSASQLPRLSSISTSSQLPCLPIHLSCRFLSV (in isoform
FT 2)"
FT /evidence="ECO:0000303|PubMed:14702039, ECO:0000303|Ref.3"
FT /id="VSP_016748"
FT VAR_SEQ 168..188
FT /note="Missing (in isoform 3, isoform 4 and isoform 5)"
FT /evidence="ECO:0000303|PubMed:14702039,
FT ECO:0000303|PubMed:15489334, ECO:0000303|Ref.1,
FT ECO:0000303|Ref.2"
FT /id="VSP_016749"
FT VAR_SEQ 244..346
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039, ECO:0000303|Ref.3"
FT /id="VSP_016750"
FT VAR_SEQ 282..296
FT /note="ALLHQYFFTAPLPAH -> LPCLPIHLSCRFLSV (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_016751"
FT VAR_SEQ 297..346
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_016752"
FT VARIANT 86
FT /note="S -> L (in dbSNP:rs28364953)"
FT /evidence="ECO:0000269|Ref.4"
FT /id="VAR_024762"
FT VARIANT 106
FT /note="S -> N (in dbSNP:rs41286029)"
FT /evidence="ECO:0000269|PubMed:17344846"
FT /id="VAR_041957"
FT VARIANT 137
FT /note="A -> T (in dbSNP:rs28364955)"
FT /evidence="ECO:0000269|Ref.4"
FT /id="VAR_024763"
FT VARIANT 281
FT /note="K -> R (in dbSNP:rs28364963)"
FT /evidence="ECO:0000269|Ref.4"
FT /id="VAR_024764"
FT MUTAGEN 161
FT /note="T->A: Impairs CDK2 T-160 phosphorylation and
FT activity."
FT /evidence="ECO:0000269|PubMed:14597612"
FT CONFLICT 30
FT /note="V -> I (in Ref. 1; AAC98920 and 2; AAF43778)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 346 AA; 38695 MW; EB6A53E97301D5AE CRC64;
MDQYCILGRI GEGAHGIVFK AKHVETGEIV ALKKVALRRL EDGFPNQALR EIKALQEMED
NQYVVQLKAV FPHGGGFVLA FEFMLSDLAE VVRHAQRPLA QAQVKSYLQM LLKGVAFCHA
NNIVHRDLKP ANLLISASGQ LKIADFGLAR VFSPDGSRLY THQVATRWYR APELLYGARQ
YDQGVDLWSV GCIMGELLNG SPLFPGKNDI EQLCYVLRIL GTPNPQVWPE LTELPDYNKI
SFKEQVPMPL EEVLPDVSPQ ALDLLGQFLL YPPHQRIAAS KALLHQYFFT APLPAHPSEL
PIPQRLGGPA PKAHPGPPHI HDFHVDRPLE ESLLNPELIR PFILEG
