Q9BTV7 (CABL2_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
CDK5 and ABL1 enzyme substrate 2

Alternative name(s):
Interactor with CDK3 2
Short name=Ik3-2

Gene names

Name:	CABLES2
Synonyms:	C20orf150

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	478 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Unknown. Probably involved in G1-S cell cycle transition.
Subunit structure	Binds to CDK3, CDK5 and ABL1. The C-terminal cyclin-box-like region binds to CDK5 By similarity.
Sequence similarities	Belongs to the cyclin family.

Ontologies

Keywords
Biological process	Cell cycle Cell division
Coding sequence diversity	Polymorphism
Molecular function	Cyclin
PTM	Phosphoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	cell cycle Inferred from electronic annotation. Source: UniProtKB-KW cell division Inferred from electronic annotation. Source: UniProtKB-KW regulation of cell cycle Inferred from electronic annotation. Source: InterPro regulation of cell division Inferred from electronic annotation. Source: InterPro
Molecular_function	cyclin-dependent protein serine/threonine kinase regulator activity Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 478	478	CDK5 and ABL1 enzyme substrate 2		PRO_0000080512
Regions
	Compositional bias	2 – 6	5	Poly-Ala
	Compositional bias	10 – 110	101	Pro-rich
Amino acid modifications
	Modified residue	130	1	Phosphoserine Ref.3 Ref.4
	Modified residue	208	1	Phosphoserine Ref.3 Ref.4
Natural variations
	Natural variant	428	1	T → K. Ref.2 Corresponds to variant rs6089219 [ dbSNP | Ensembl ].		VAR_026532
Experimental info
	Sequence conflict	277	1	S → P in AAH03122. Ref.2

Sequences

	Sequence		Length	Mass (Da)
	Q9BTV7 [UniParc]. Last modified May 30, 2006. Version 3. Checksum: 98E99EC72F7573EB	FASTA	478	52,235
	10 20 30 40 50 60 MAAAAAGGAP GPAPGPAGPP PPAAPTSAAR APPQALRRRG DSRRRQAALF FLNNISLDGR 70 80 90 100 110 120 PPSLGPGGEK PPPPPAEARE PPAPPPPEPP TGLPARTPAP QGLLSPTQVP TGLGLDGQRQ 130 140 150 160 170 180 RKRVTSQRCS LEFLEDAVGC APAQRTKHTS GSPRHKGLKK THFIKNMRQY DTRNSRIVLI 190 200 210 220 230 240 CAKRSLCAAF SVLPYGEGLR ISDLRVDSQK QRHPSGGVSV SSEMVFELEG VELGADGKVV 250 260 270 280 290 300 SYAKFLYPTN ALVTHKSDSH GLLPTPRPSV PRTLPGSRHK PAPTKSAPAS TELGSDVGDT 310 320 330 340 350 360 LEYNPNLLDD PQWPCGKHKR VLIFASYMTT VIEYVKPSDL KKDMNETFRE KFPHVKLTLS 370 380 390 400 410 420 KIRSLKREMR SLSEECSLEP VTVAMAYVYF EKLVLQGKLS KQNRKLCAGA CVLLAAKISS 430 440 450 460 470 DLRKSGVTQL IDKLEERFRF NRRDLIGFEF TVLVALELAL YLPENQVLPH YRRLTQQF

References

[1]	"The DNA sequence and comparative analysis of human chromosome 20." Deloukas P., Matthews L.H., Ashurst J.L., Burton J., Gilbert J.G.R., Jones M., Stavrides G., Almeida J.P., Babbage A.K., Bagguley C.L., Bailey J., Barlow K.F., Bates K.N., Beard L.M., Beare D.M., Beasley O.P., Bird C.P., Blakey S.E. , Bridgeman A.M., Brown A.J., Buck D., Burrill W.D., Butler A.P., Carder C., Carter N.P., Chapman J.C., Clamp M., Clark G., Clark L.N., Clark S.Y., Clee C.M., Clegg S., Cobley V.E., Collier R.E., Connor R.E., Corby N.R., Coulson A., Coville G.J., Deadman R., Dhami P.D., Dunn M., Ellington A.G., Frankland J.A., Fraser A., French L., Garner P., Grafham D.V., Griffiths C., Griffiths M.N.D., Gwilliam R., Hall R.E., Hammond S., Harley J.L., Heath P.D., Ho S., Holden J.L., Howden P.J., Huckle E., Hunt A.R., Hunt S.E., Jekosch K., Johnson C.M., Johnson D., Kay M.P., Kimberley A.M., King A., Knights A., Laird G.K., Lawlor S., Lehvaeslaiho M.H., Leversha M.A., Lloyd C., Lloyd D.M., Lovell J.D., Marsh V.L., Martin S.L., McConnachie L.J., McLay K., McMurray A.A., Milne S.A., Mistry D., Moore M.J.F., Mullikin J.C., Nickerson T., Oliver K., Parker A., Patel R., Pearce T.A.V., Peck A.I., Phillimore B.J.C.T., Prathalingam S.R., Plumb R.W., Ramsay H., Rice C.M., Ross M.T., Scott C.E., Sehra H.K., Shownkeen R., Sims S., Skuce C.D., Smith M.L., Soderlund C., Steward C.A., Sulston J.E., Swann R.M., Sycamore N., Taylor R., Tee L., Thomas D.W., Thorpe A., Tracey A., Tromans A.C., Vaudin M., Wall M., Wallis J.M., Whitehead S.L., Whittaker P., Willey D.L., Williams L., Williams S.A., Wilming L., Wray P.W., Hubbard T., Durbin R.M., Bentley D.R., Beck S., Rogers J. Nature 414:865-871(2001) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[2]	"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)." The MGC Project Team Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 154-478, VARIANT LYS-428. Tissue: Eye.
[3]	"Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle." Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., Greff Z., Keri G., Stemmann O., Mann M. Mol. Cell 31:438-448(2008) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-130 AND SER-208, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[4]	"Large-scale proteomics analysis of the human kinome." Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G., Mann M., Daub H. Mol. Cell. Proteomics 8:1751-1764(2009) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-130 AND SER-208, MASS SPECTROMETRY.
[5]	"Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions." Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K. Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. Tissue: Leukemic T-cell.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AL121832 Genomic DNA. Translation: CAI23283.2. BC003122 mRNA. Translation: AAH03122.1.
IPI	IPI00030512.
RefSeq	NP_112492.2. NM_031215.2.
UniGene	Hs.301040.
3D structure databases
ProteinModelPortal	Q9BTV7.
SMR	Q9BTV7. Positions 348-471.
ModBase	Search...
Protein-protein interaction databases
IntAct	Q9BTV7. 1 interaction.
STRING	9606.ENSP00000279101.
PTM databases
PhosphoSite	Q9BTV7.
Polymorphism databases
DMDM	109940186.
Proteomic databases
PaxDb	Q9BTV7.
PRIDE	Q9BTV7.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000279101; ENSP00000279101; ENSG00000149679.
GeneID	81928.
KEGG	hsa:81928.
UCSC	uc002ycv.2. human.
Organism-specific databases
CTD	81928.
GeneCards	GC20M060963.
H-InvDB	HIX0040565.
HGNC	HGNC:16143. CABLES2.
HPA	HPA048253.
neXtProt	NX_Q9BTV7.
PharmGKB	PA25692.
GenAtlas	Search...
Phylogenomic databases
eggNOG	NOG256533.
HOGENOM	HOG000231236.
HOVERGEN	HBG050759.
InParanoid	Q9BTV7.
OMA	RVTSQRC.
OrthoDB	EOG4KKZ34.
PhylomeDB	Q9BTV7.
Enzyme and pathway databases
Reactome	REACT_604. Hemostasis.
Gene expression databases
ArrayExpress	Q9BTV7.
Bgee	Q9BTV7.
CleanEx	HS_CABLES2.
Genevestigator	Q9BTV7.
GermOnline	ENSG00000149679. Homo sapiens.
Family and domain databases
Gene3D	1.10.472.10. 1 hit.
InterPro	IPR012388. Cdk5/c-Abl_linker_Cables. IPR013763. Cyclin-like. IPR006671. Cyclin_N. [Graphical view]
Pfam	PF00134. Cyclin_N. 1 hit. [Graphical view]
PIRSF	PIRSF025798. Cables. 1 hit.
SMART	SM00385. CYCLIN. 1 hit. [Graphical view]
SUPFAM	SSF47954. Cyclin_like. 1 hit.
ProtoNet	Search...
Other
GenomeRNAi	81928.
NextBio	72261.
PMAP-CutDB	Q9BTV7.

Entry information

Entry name

CABL2_HUMAN

Accession

Primary (citable) accession number: Q9BTV7
Secondary accession number(s): Q5JWL0, Q9BYK0

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 12, 2003
Last sequence update:	May 30, 2006
Last modified:	May 1, 2013
This is version 100 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.