CABL2_HUMAN
ID CABL2_HUMAN Reviewed; 478 AA.
AC Q9BTV7; Q5JWL0; Q9BYK0;
DT 12-FEB-2003, integrated into UniProtKB/Swiss-Prot.
DT 30-MAY-2006, sequence version 3.
DT 03-AUG-2022, entry version 164.
DE RecName: Full=CDK5 and ABL1 enzyme substrate 2;
DE AltName: Full=Interactor with CDK3 2;
DE Short=Ik3-2;
GN Name=CABLES2; Synonyms=C20orf150;
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 [LARGE SCALE GENOMIC DNA].
RX PubMed=11780052; DOI=10.1038/414865a;
RA Deloukas P., Matthews L.H., Ashurst J.L., Burton J., Gilbert J.G.R.,
RA Jones M., Stavrides G., Almeida J.P., Babbage A.K., Bagguley C.L.,
RA Bailey J., Barlow K.F., Bates K.N., Beard L.M., Beare D.M., Beasley O.P.,
RA Bird C.P., Blakey S.E., Bridgeman A.M., Brown A.J., Buck D., Burrill W.D.,
RA Butler A.P., Carder C., Carter N.P., Chapman J.C., Clamp M., Clark G.,
RA Clark L.N., Clark S.Y., Clee C.M., Clegg S., Cobley V.E., Collier R.E.,
RA Connor R.E., Corby N.R., Coulson A., Coville G.J., Deadman R., Dhami P.D.,
RA Dunn M., Ellington A.G., Frankland J.A., Fraser A., French L., Garner P.,
RA Grafham D.V., Griffiths C., Griffiths M.N.D., Gwilliam R., Hall R.E.,
RA Hammond S., Harley J.L., Heath P.D., Ho S., Holden J.L., Howden P.J.,
RA Huckle E., Hunt A.R., Hunt S.E., Jekosch K., Johnson C.M., Johnson D.,
RA Kay M.P., Kimberley A.M., King A., Knights A., Laird G.K., Lawlor S.,
RA Lehvaeslaiho M.H., Leversha M.A., Lloyd C., Lloyd D.M., Lovell J.D.,
RA Marsh V.L., Martin S.L., McConnachie L.J., McLay K., McMurray A.A.,
RA Milne S.A., Mistry D., Moore M.J.F., Mullikin J.C., Nickerson T.,
RA Oliver K., Parker A., Patel R., Pearce T.A.V., Peck A.I.,
RA Phillimore B.J.C.T., Prathalingam S.R., Plumb R.W., Ramsay H., Rice C.M.,
RA Ross M.T., Scott C.E., Sehra H.K., Shownkeen R., Sims S., Skuce C.D.,
RA Smith M.L., Soderlund C., Steward C.A., Sulston J.E., Swann R.M.,
RA Sycamore N., Taylor R., Tee L., Thomas D.W., Thorpe A., Tracey A.,
RA Tromans A.C., Vaudin M., Wall M., Wallis J.M., Whitehead S.L.,
RA Whittaker P., Willey D.L., Williams L., Williams S.A., Wilming L.,
RA Wray P.W., Hubbard T., Durbin R.M., Bentley D.R., Beck S., Rogers J.;
RT "The DNA sequence and comparative analysis of human chromosome 20.";
RL Nature 414:865-871(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 154-478, AND VARIANT LYS-428.
RC TISSUE=Eye;
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 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-130 AND SER-208, AND
RP IDENTIFICATION BY MASS 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 [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-130 AND SER-208, 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 [5]
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).
CC -!- FUNCTION: Unknown. Probably involved in G1-S cell cycle transition.
CC -!- SUBUNIT: Binds to CDK3, CDK5 and ABL1. The C-terminal cyclin-box-like
CC region binds to CDK5 (By similarity). {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the cyclin family. {ECO:0000305}.
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DR EMBL; AL121832; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC003122; AAH03122.1; -; mRNA.
DR CCDS; CCDS33503.1; -.
DR RefSeq; NP_112492.2; NM_031215.2.
DR AlphaFoldDB; Q9BTV7; -.
DR SMR; Q9BTV7; -.
DR BioGRID; 123628; 14.
DR IntAct; Q9BTV7; 4.
DR STRING; 9606.ENSP00000279101; -.
DR GlyGen; Q9BTV7; 1 site, 2 O-linked glycans (1 site).
DR iPTMnet; Q9BTV7; -.
DR PhosphoSitePlus; Q9BTV7; -.
DR BioMuta; CABLES2; -.
DR DMDM; 109940186; -.
DR EPD; Q9BTV7; -.
DR jPOST; Q9BTV7; -.
DR MassIVE; Q9BTV7; -.
DR MaxQB; Q9BTV7; -.
DR PaxDb; Q9BTV7; -.
DR PeptideAtlas; Q9BTV7; -.
DR PRIDE; Q9BTV7; -.
DR ProteomicsDB; 79015; -.
DR Antibodypedia; 29526; 118 antibodies from 22 providers.
DR DNASU; 81928; -.
DR Ensembl; ENST00000279101.10; ENSP00000279101.5; ENSG00000149679.12.
DR GeneID; 81928; -.
DR KEGG; hsa:81928; -.
DR MANE-Select; ENST00000279101.10; ENSP00000279101.5; NM_031215.3; NP_112492.2.
DR UCSC; uc002ycv.3; human.
DR CTD; 81928; -.
DR DisGeNET; 81928; -.
DR GeneCards; CABLES2; -.
DR HGNC; HGNC:16143; CABLES2.
DR HPA; ENSG00000149679; Tissue enhanced (testis).
DR MIM; 618772; gene.
DR neXtProt; NX_Q9BTV7; -.
DR OpenTargets; ENSG00000149679; -.
DR PharmGKB; PA25692; -.
DR VEuPathDB; HostDB:ENSG00000149679; -.
DR eggNOG; KOG4164; Eukaryota.
DR GeneTree; ENSGT00400000022086; -.
DR HOGENOM; CLU_021942_2_1_1; -.
DR InParanoid; Q9BTV7; -.
DR OMA; IAFEFTV; -.
DR OrthoDB; 1441217at2759; -.
DR PhylomeDB; Q9BTV7; -.
DR TreeFam; TF323936; -.
DR PathwayCommons; Q9BTV7; -.
DR Reactome; R-HSA-983231; Factors involved in megakaryocyte development and platelet production.
DR SignaLink; Q9BTV7; -.
DR BioGRID-ORCS; 81928; 11 hits in 1083 CRISPR screens.
DR ChiTaRS; CABLES2; human.
DR GenomeRNAi; 81928; -.
DR Pharos; Q9BTV7; Tdark.
DR PRO; PR:Q9BTV7; -.
DR Proteomes; UP000005640; Chromosome 20.
DR RNAct; Q9BTV7; protein.
DR Bgee; ENSG00000149679; Expressed in sperm and 145 other tissues.
DR ExpressionAtlas; Q9BTV7; baseline and differential.
DR Genevisible; Q9BTV7; HS.
DR GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR GO; GO:0051726; P:regulation of cell cycle; IEA:InterPro.
DR CDD; cd00043; CYCLIN; 1.
DR InterPro; IPR012388; CABLES1/2.
DR InterPro; IPR013763; Cyclin-like.
DR InterPro; IPR036915; Cyclin-like_sf.
DR InterPro; IPR006671; Cyclin_N.
DR PANTHER; PTHR22896; PTHR22896; 1.
DR Pfam; PF00134; Cyclin_N; 1.
DR PIRSF; PIRSF025798; Cables; 1.
DR SUPFAM; SSF47954; SSF47954; 1.
PE 1: Evidence at protein level;
KW Cell cycle; Cell division; Cyclin; Phosphoprotein; Reference proteome.
FT CHAIN 1..478
FT /note="CDK5 and ABL1 enzyme substrate 2"
FT /id="PRO_0000080512"
FT REGION 1..121
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 257..296
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 12..28
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 65..96
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 130
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18691976,
FT ECO:0007744|PubMed:19369195"
FT MOD_RES 208
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18691976,
FT ECO:0007744|PubMed:19369195"
FT VARIANT 428
FT /note="T -> K (in dbSNP:rs6089219)"
FT /evidence="ECO:0000269|PubMed:15489334"
FT /id="VAR_026532"
FT CONFLICT 277
FT /note="S -> P (in Ref. 2; AAH03122)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 478 AA; 52235 MW; 98E99EC72F7573EB CRC64;
MAAAAAGGAP GPAPGPAGPP PPAAPTSAAR APPQALRRRG DSRRRQAALF FLNNISLDGR
PPSLGPGGEK PPPPPAEARE PPAPPPPEPP TGLPARTPAP QGLLSPTQVP TGLGLDGQRQ
RKRVTSQRCS LEFLEDAVGC APAQRTKHTS GSPRHKGLKK THFIKNMRQY DTRNSRIVLI
CAKRSLCAAF SVLPYGEGLR ISDLRVDSQK QRHPSGGVSV SSEMVFELEG VELGADGKVV
SYAKFLYPTN ALVTHKSDSH GLLPTPRPSV PRTLPGSRHK PAPTKSAPAS TELGSDVGDT
LEYNPNLLDD PQWPCGKHKR VLIFASYMTT VIEYVKPSDL KKDMNETFRE KFPHVKLTLS
KIRSLKREMR SLSEECSLEP VTVAMAYVYF EKLVLQGKLS KQNRKLCAGA CVLLAAKISS
DLRKSGVTQL IDKLEERFRF NRRDLIGFEF TVLVALELAL YLPENQVLPH YRRLTQQF
