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Q9BTV7 (CABL2_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 111. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
CDK5 and ABL1 enzyme substrate 2
Alternative name(s):
Interactor with CDK3 2
Short name=Ik3-2
Gene names
Name:CABLES2
Synonyms:C20orf150
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length478 AA.
Sequence statusComplete.
Protein existenceEvidence 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

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 478478CDK5 and ABL1 enzyme substrate 2
PRO_0000080512

Regions

Compositional bias2 – 65Poly-Ala
Compositional bias10 – 110101Pro-rich

Amino acid modifications

Modified residue1301Phosphoserine Ref.3 Ref.4
Modified residue2081Phosphoserine Ref.3 Ref.4

Natural variations

Natural variant4281T → K. Ref.2
Corresponds to variant rs6089219 [ dbSNP | Ensembl ].
VAR_026532

Experimental info

Sequence conflict2771S → P in AAH03122. Ref.2

Sequences

Sequence LengthMass (Da)Tools
Q9BTV7 [UniParc].

Last modified May 30, 2006. Version 3.
Checksum: 98E99EC72F7573EB

FASTA47852,235
        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 

« Hide

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. expand/collapse author list , 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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[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.
CCDSCCDS33503.1.
RefSeqNP_112492.2. NM_031215.2.
UniGeneHs.301040.

3D structure databases

ProteinModelPortalQ9BTV7.
SMRQ9BTV7. Positions 330-464.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid123628. 4 interactions.
IntActQ9BTV7. 1 interaction.
STRING9606.ENSP00000279101.

PTM databases

PhosphoSiteQ9BTV7.

Polymorphism databases

DMDM109940186.

Proteomic databases

MaxQBQ9BTV7.
PaxDbQ9BTV7.
PRIDEQ9BTV7.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000279101; ENSP00000279101; ENSG00000149679.
GeneID81928.
KEGGhsa:81928.
UCSCuc002ycv.2. human.

Organism-specific databases

CTD81928.
GeneCardsGC20M060963.
H-InvDBHIX0040565.
HGNCHGNC:16143. CABLES2.
HPAHPA048253.
HPA052138.
neXtProtNX_Q9BTV7.
PharmGKBPA25692.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG256533.
HOGENOMHOG000231236.
HOVERGENHBG050759.
InParanoidQ9BTV7.
OMARVTSQRC.
OrthoDBEOG7P5T0S.
PhylomeDBQ9BTV7.
TreeFamTF323936.

Enzyme and pathway databases

ReactomeREACT_604. Hemostasis.
SignaLinkQ9BTV7.

Gene expression databases

BgeeQ9BTV7.
CleanExHS_CABLES2.
GenevestigatorQ9BTV7.

Family and domain databases

Gene3D1.10.472.10. 1 hit.
InterProIPR012388. Cdk5/c-Abl_linker_Cables.
IPR013763. Cyclin-like.
IPR006671. Cyclin_N.
[Graphical view]
PfamPF00134. Cyclin_N. 1 hit.
[Graphical view]
PIRSFPIRSF025798. Cables. 1 hit.
SMARTSM00385. CYCLIN. 1 hit.
[Graphical view]
SUPFAMSSF47954. SSF47954. 1 hit.
ProtoNetSearch...

Other

GenomeRNAi81928.
NextBio72261.
PMAP-CutDBQ9BTV7.
PROQ9BTV7.

Entry information

Entry nameCABL2_HUMAN
AccessionPrimary (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: July 9, 2014
This is version 111 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny 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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 20

Human chromosome 20: entries, gene names and cross-references to MIM