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Protein

CDK5 and ABL1 enzyme substrate 2

Gene

CABLES2

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

Functioni

Unknown. Probably involved in G1-S cell cycle transition.

GO - Biological processi

  1. cell cycle Source: UniProtKB-KW
  2. cell division Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Cyclin

Keywords - Biological processi

Cell cycle, Cell division

Enzyme and pathway databases

ReactomeiREACT_24970. Factors involved in megakaryocyte development and platelet production.
SignaLinkiQ9BTV7.

Names & Taxonomyi

Protein namesi
Recommended name:
CDK5 and ABL1 enzyme substrate 2
Alternative name(s):
Interactor with CDK3 2
Short name:
Ik3-2
Gene namesi
Name:CABLES2
Synonyms:C20orf150
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome 20

Organism-specific databases

HGNCiHGNC:16143. CABLES2.

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA25692.

Polymorphism and mutation databases

BioMutaiCABLES2.
DMDMi109940186.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 478478CDK5 and ABL1 enzyme substrate 2PRO_0000080512Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei130 – 1301Phosphoserine2 Publications
Modified residuei208 – 2081Phosphoserine2 Publications

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiQ9BTV7.
PaxDbiQ9BTV7.
PRIDEiQ9BTV7.

PTM databases

PhosphoSiteiQ9BTV7.

Miscellaneous databases

PMAP-CutDBQ9BTV7.

Expressioni

Gene expression databases

BgeeiQ9BTV7.
CleanExiHS_CABLES2.
GenevestigatoriQ9BTV7.

Organism-specific databases

HPAiHPA048253.
HPA052138.

Interactioni

Subunit structurei

Binds to CDK3, CDK5 and ABL1. The C-terminal cyclin-box-like region binds to CDK5 (By similarity).By similarity

Protein-protein interaction databases

BioGridi123628. 6 interactions.
IntActiQ9BTV7. 1 interaction.
STRINGi9606.ENSP00000279101.

Structurei

3D structure databases

ProteinModelPortaliQ9BTV7.
SMRiQ9BTV7. Positions 330-464.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi2 – 65Poly-Ala
Compositional biasi10 – 110101Pro-richAdd
BLAST

Sequence similaritiesi

Belongs to the cyclin family.Curated

Phylogenomic databases

eggNOGiNOG256533.
GeneTreeiENSGT00400000022086.
HOGENOMiHOG000231236.
HOVERGENiHBG050759.
InParanoidiQ9BTV7.
OMAiEDTVGCP.
OrthoDBiEOG7P5T0S.
PhylomeDBiQ9BTV7.
TreeFamiTF323936.

Family and domain databases

Gene3Di1.10.472.10. 1 hit.
InterProiIPR012388. CABLES1/2.
IPR013763. Cyclin-like.
IPR006671. Cyclin_N.
[Graphical view]
PANTHERiPTHR22896. PTHR22896. 1 hit.
PfamiPF00134. Cyclin_N. 1 hit.
[Graphical view]
SMARTiSM00385. CYCLIN. 1 hit.
[Graphical view]
SUPFAMiSSF47954. SSF47954. 1 hit.

Sequencei

Sequence statusi: Complete.

Q9BTV7-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAAAAAGGAP GPAPGPAGPP PPAAPTSAAR APPQALRRRG DSRRRQAALF
60 70 80 90 100
FLNNISLDGR PPSLGPGGEK PPPPPAEARE PPAPPPPEPP TGLPARTPAP
110 120 130 140 150
QGLLSPTQVP TGLGLDGQRQ RKRVTSQRCS LEFLEDAVGC APAQRTKHTS
160 170 180 190 200
GSPRHKGLKK THFIKNMRQY DTRNSRIVLI CAKRSLCAAF SVLPYGEGLR
210 220 230 240 250
ISDLRVDSQK QRHPSGGVSV SSEMVFELEG VELGADGKVV SYAKFLYPTN
260 270 280 290 300
ALVTHKSDSH GLLPTPRPSV PRTLPGSRHK PAPTKSAPAS TELGSDVGDT
310 320 330 340 350
LEYNPNLLDD PQWPCGKHKR VLIFASYMTT VIEYVKPSDL KKDMNETFRE
360 370 380 390 400
KFPHVKLTLS KIRSLKREMR SLSEECSLEP VTVAMAYVYF EKLVLQGKLS
410 420 430 440 450
KQNRKLCAGA CVLLAAKISS DLRKSGVTQL IDKLEERFRF NRRDLIGFEF
460 470
TVLVALELAL YLPENQVLPH YRRLTQQF
Length:478
Mass (Da):52,235
Last modified:May 30, 2006 - v3
Checksum:i98E99EC72F7573EB
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti277 – 2771S → P in AAH03122 (PubMed:15489334).Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti428 – 4281T → K.1 Publication
Corresponds to variant rs6089219 [ dbSNP | Ensembl ].
VAR_026532

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AL121832 Genomic DNA. Translation: CAI23283.2.
BC003122 mRNA. Translation: AAH03122.1.
CCDSiCCDS33503.1.
RefSeqiNP_112492.2. NM_031215.2.
UniGeneiHs.301040.

Genome annotation databases

EnsembliENST00000279101; ENSP00000279101; ENSG00000149679.
GeneIDi81928.
KEGGihsa:81928.
UCSCiuc002ycv.2. human.

Polymorphism and mutation databases

BioMutaiCABLES2.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AL121832 Genomic DNA. Translation: CAI23283.2.
BC003122 mRNA. Translation: AAH03122.1.
CCDSiCCDS33503.1.
RefSeqiNP_112492.2. NM_031215.2.
UniGeneiHs.301040.

3D structure databases

ProteinModelPortaliQ9BTV7.
SMRiQ9BTV7. Positions 330-464.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi123628. 6 interactions.
IntActiQ9BTV7. 1 interaction.
STRINGi9606.ENSP00000279101.

PTM databases

PhosphoSiteiQ9BTV7.

Polymorphism and mutation databases

BioMutaiCABLES2.
DMDMi109940186.

Proteomic databases

MaxQBiQ9BTV7.
PaxDbiQ9BTV7.
PRIDEiQ9BTV7.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000279101; ENSP00000279101; ENSG00000149679.
GeneIDi81928.
KEGGihsa:81928.
UCSCiuc002ycv.2. human.

Organism-specific databases

CTDi81928.
GeneCardsiGC20M060963.
H-InvDBHIX0040565.
HGNCiHGNC:16143. CABLES2.
HPAiHPA048253.
HPA052138.
neXtProtiNX_Q9BTV7.
PharmGKBiPA25692.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiNOG256533.
GeneTreeiENSGT00400000022086.
HOGENOMiHOG000231236.
HOVERGENiHBG050759.
InParanoidiQ9BTV7.
OMAiEDTVGCP.
OrthoDBiEOG7P5T0S.
PhylomeDBiQ9BTV7.
TreeFamiTF323936.

Enzyme and pathway databases

ReactomeiREACT_24970. Factors involved in megakaryocyte development and platelet production.
SignaLinkiQ9BTV7.

Miscellaneous databases

ChiTaRSiCABLES2. human.
GenomeRNAii81928.
NextBioi72261.
PMAP-CutDBQ9BTV7.
PROiQ9BTV7.

Gene expression databases

BgeeiQ9BTV7.
CleanExiHS_CABLES2.
GenevestigatoriQ9BTV7.

Family and domain databases

Gene3Di1.10.472.10. 1 hit.
InterProiIPR012388. CABLES1/2.
IPR013763. Cyclin-like.
IPR006671. Cyclin_N.
[Graphical view]
PANTHERiPTHR22896. PTHR22896. 1 hit.
PfamiPF00134. Cyclin_N. 1 hit.
[Graphical view]
SMARTiSM00385. CYCLIN. 1 hit.
[Graphical view]
SUPFAMiSSF47954. SSF47954. 1 hit.
ProtoNetiSearch...

Publicationsi

  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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  4. 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.

Entry informationi

Entry nameiCABL2_HUMAN
AccessioniPrimary (citable) accession number: Q9BTV7
Secondary accession number(s): Q5JWL0, Q9BYK0
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 12, 2003
Last sequence update: May 30, 2006
Last modified: April 29, 2015
This is version 119 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (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.

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Human chromosome 20
    Human chromosome 20: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.