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Q8VDP4 (CCAR2_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 95. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | 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:
Cell cycle and apoptosis regulator protein 2
Alternative name(s):
Cell division cycle and apoptosis regulator protein 2
Gene names
Name:Ccar2
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length922 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Core component of the DBIRD complex, a multiprotein complex that acts at the interface between core mRNP particles and RNA polymerase II (RNAPII) and integrates transcript elongation with the regulation of alternative splicing: the DBIRD complex affects local transcript elongation rates and alternative splicing of a large set of exons embedded in (A + T)-rich DNA regions. Inhibits SIRT1 deacetylase activity leading to increasing levels of p53/TP53 acetylation and p53-mediated apoptosis By similarity. As part of a histone H3-specific methyltransferase complex may mediate ligand-dependent transcriptional activation by nuclear hormone receptors By similarity. Inhibits SUV39H1 methyltransferase activity. Plays a critical role in maintaining genomic stability and cellular integrity following UV-induced genotoxic stress By similarity. Ref.6

Subunit structure

Component of the DBIRD complex. Interacts with ZNF326/ZIRD; the interaction is direct. Interacts (via N-terminus) with SIRT1, which inhibits the deacetylation of substrates. Interacts (via N-terminus) with SUV39H1; this interaction abolishes the interaction with SIRT1. Part of a complex composed at least of ASCL2, C11orf30/EMSY, HCFC1, HSPA8, CCAR2, MATR3, MKI67, RBBP5, TUBB2A, WDR5 and ZNF335; this complex may have a histone H3-specific methyltransferase activity. Ref.6

Subcellular location

Nucleus By similarity. Note: Recruited to chromatin, post-UV irradiation By similarity.

Post-translational modification

Acetylation at Lys-112 and Lys-215 by KAT8 prevents inhibitory binding to SIRT1 and increases its deacetylase activity By similarity.

Sequence caution

The sequence BAC27420.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.

The sequence BAC34139.2 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.

Ontologies

Keywords
   Biological processApoptosis
Cell cycle
DNA damage
mRNA processing
mRNA splicing
   Cellular componentNucleus
   DomainCoiled coil
   Molecular functionMetalloenzyme inhibitor
   PTMAcetylation
Phosphoprotein
   Technical termComplete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processRNA splicing

Inferred from sequence or structural similarity. Source: UniProtKB

cell cycle

Inferred from electronic annotation. Source: UniProtKB-KW

cellular response to DNA damage stimulus

Inferred from electronic annotation. Source: UniProtKB-KW

mRNA processing

Inferred from electronic annotation. Source: UniProtKB-KW

mitochondrial fragmentation involved in apoptotic process

Inferred from electronic annotation. Source: Ensembl

negative regulation of intrinsic apoptotic signaling pathway in response to DNA damage

Inferred from sequence or structural similarity. Source: UniProtKB

positive regulation of DNA damage checkpoint

Inferred from sequence or structural similarity. Source: UniProtKB

positive regulation of apoptotic process

Inferred from sequence or structural similarity. Source: UniProtKB

regulation of DNA-templated transcription, elongation

Inferred from sequence or structural similarity. Source: UniProtKB

response to UV

Inferred from sequence or structural similarity. Source: UniProtKB

   Cellular_componentDBIRD complex

Inferred from sequence or structural similarity. Source: UniProtKB

mitochondrial matrix

Inferred from electronic annotation. Source: Ensembl

nuclear chromatin

Inferred from sequence or structural similarity. Source: UniProtKB

spliceosomal complex

Inferred from electronic annotation. Source: Ensembl

   Molecular_functionRNA polymerase II core binding

Inferred from sequence or structural similarity. Source: UniProtKB

enzyme inhibitor activity

Inferred from direct assay Ref.6. Source: UniProtKB

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 922922Cell cycle and apoptosis regulator protein 2
PRO_0000050814

Regions

Coiled coil573 – 59624 Potential
Coiled coil828 – 89871 Potential

Amino acid modifications

Modified residue351Phosphothreonine By similarity
Modified residue1121N6-acetyllysine; by KAT8 By similarity
Modified residue1241Phosphoserine By similarity
Modified residue2151N6-acetyllysine; by KAT8 By similarity
Modified residue6741Phosphoserine Ref.5
Modified residue6771Phosphoserine Ref.4 Ref.5
Modified residue6801Phosphoserine Ref.4 Ref.5

Experimental info

Sequence conflict527 – 5293RPK → HAS in AAH25471. Ref.2
Sequence conflict7201H → L in AAH38346. Ref.2
Sequence conflict8121G → R in BAC27420. Ref.1

Sequences

Sequence LengthMass (Da)Tools
Q8VDP4 [UniParc].

Last modified March 1, 2004. Version 2.
Checksum: 19F43ECEE58F461C

FASTA922103,002
        10         20         30         40         50         60 
MSQFKRQRIN PLPGGRNFSG AASTSLLGPP PGLLTPPVAT DLSQNARHLQ SGEKQRVFTG 

        70         80         90        100        110        120 
IVTSLHDYFG VVDEEVFFQL SVVKGRLPQL GEKVLVKAAY NPGQAVPWNA VKVQTLSNQP 

       130        140        150        160        170        180 
LLKSPAPPLL HVAALGQKQG ILGAQPQLIF QPHRIPPLFP QKPLSLFQTS HTLHLSHLNR 

       190        200        210        220        230        240 
FPARGPHGRL DQGRSDDYDS KKRKQRAGGE PWGAKKPRHD LSPYRVHLTP YTVDSPTCDF 

       250        260        270        280        290        300 
LELQRRYRSL LVPSDFLSVH LSWLSAFPLG QPFSLHHPSR IQVSSEKEAA PDTGAEPSPE 

       310        320        330        340        350        360 
DSDPTYSSKV LLLSSPGLEE FYRCCMLFVD DMAEPRETPE HPLKQLKFLL GRKEEEAVLV 

       370        380        390        400        410        420 
GGEWSPSLDG LDPQADPQVL VRTAIRCAQA QTGIDLSTCT KWWRFAEFQY LQPGPPRQLH 

       430        440        450        460        470        480 
TVVVYLPDVW TIMPTLEEWE ALCQQKATEA APQPHEASGE AEATEQAPDV SEQADTSKQN 

       490        500        510        520        530        540 
TETMEATTQQ DVDTDLPEAP PPPLEPAVMA RPRCVNLSLY GIVEDRRPKE RISFEVVVLA 

       550        560        570        580        590        600 
ELFVEMLQRD FGYRIYKTLL SLPEKVVSPP EPEKEEAAKE DAVKEEEAVK EEAVKVSKDE 

       610        620        630        640        650        660 
VQNEGTAAES DSPLKEDGLL PKRPSSGGEE EEKARGEAAE DLCEMALDPD LLLLRDDGED 

       670        680        690        700        710        720 
EFAGAKLEET EVRSVASNQS EMEYSSLQDM PKELDPSTVL PLDCLLAFVF FDANWCGYLH 

       730        740        750        760        770        780 
RRDLERVLLT LGIRLSAEQA KQLVSRVVAQ NICQYRSLQY SRAEVLDDGL PEDVLFGNLD 

       790        800        810        820        830        840 
LLPPSGKSTK PGAAPTEHKG LVPHNGSLIN VGSLLQRAEQ QDSGRLYLEN KIHTLELKLE 

       850        860        870        880        890        900 
ESHNRFSATE VTNKTLAAEM QELRARLAEA EETARTAERQ KNQLQRQMQD FRRRLTPLHL 

       910        920 
EMQRIVEKAD SWVEKEEPTP SN 

« Hide

References

« Hide 'large scale' references
[1]"The transcriptional landscape of the mammalian genome."
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J. expand/collapse author list , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: C57BL/6J.
Tissue: Liver and Testis.
[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].
Strain: FVB/N.
Tissue: Mammary tumor.
[3]Lubec G., Sunyer B., Chen W.-Q.
Submitted (JAN-2009) to UniProtKB
Cited for: PROTEIN SEQUENCE OF 226-248, IDENTIFICATION BY MASS SPECTROMETRY.
Strain: OF1.
Tissue: Hippocampus.
[4]"Phosphoproteomic analysis of the developing mouse brain."
Ballif B.A., Villen J., Beausoleil S.A., Schwartz D., Gygi S.P.
Mol. Cell. Proteomics 3:1093-1101(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-677 AND SER-680, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Embryonic brain.
[5]"Large-scale phosphorylation analysis of mouse liver."
Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-674; SER-677 AND SER-680, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Liver.
[6]"Inhibition of SUV39H1 methyltransferase activity by DBC1."
Li Z., Chen L., Kabra N., Wang C., Fang J., Chen J.
J. Biol. Chem. 284:10361-10366(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION AS SUV39H1 INHIBITOR, INTERACTION WITH SUV39H1.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AK031472 mRNA. Translation: BAC27420.1. Different initiation.
AK050238 mRNA. Translation: BAC34139.2. Different initiation.
BC021475 mRNA. Translation: AAH21475.2.
BC025471 mRNA. Translation: AAH25471.1.
BC038346 mRNA. Translation: AAH38346.1.
CCDSCCDS49534.1.
RefSeqNP_666167.3. NM_146055.3.
XP_006518959.1. XM_006518896.1.
UniGeneMm.218284.

3D structure databases

ProteinModelPortalQ8VDP4.
SMRQ8VDP4. Positions 55-119.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid230123. 2 interactions.
IntActQ8VDP4. 6 interactions.
MINTMINT-4119906.
STRING10090.ENSMUSP00000036924.

PTM databases

PhosphoSiteQ8VDP4.

Proteomic databases

MaxQBQ8VDP4.
PaxDbQ8VDP4.
PRIDEQ8VDP4.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000035612; ENSMUSP00000036924; ENSMUSG00000033712.
GeneID219158.
KEGGmmu:219158.
UCSCuc007unf.1. mouse.

Organism-specific databases

CTD57805.
MGIMGI:2444228. Ccar2.

Phylogenomic databases

eggNOGNOG307741.
GeneTreeENSGT00530000063672.
HOGENOMHOG000113184.
HOVERGENHBG081843.
InParanoidQ8VDP4.
OMAMSQFKRQ.
OrthoDBEOG7CK365.
PhylomeDBQ8VDP4.
TreeFamTF316387.

Gene expression databases

BgeeQ8VDP4.
CleanExMM_2610301G19RIK.
GenevestigatorQ8VDP4.

Family and domain databases

InterProIPR028811. CCAR2.
IPR025224. DBC1/CARP1.
IPR025954. DBC1/CARP1_inactive_NUDIX_dom.
IPR025223. S1-like_RNA-bd_dom.
[Graphical view]
PANTHERPTHR14304. PTHR14304. 1 hit.
PTHR14304:SF12. PTHR14304:SF12. 1 hit.
PfamPF14443. DBC1. 1 hit.
PF14444. S1-like. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio376623.
SOURCESearch...

Entry information

Entry nameCCAR2_MOUSE
AccessionPrimary (citable) accession number: Q8VDP4
Secondary accession number(s): Q6PIB1 expand/collapse secondary AC list , Q8BWR5, Q8C0F0, Q8R3G6
Entry history
Integrated into UniProtKB/Swiss-Prot: January 24, 2006
Last sequence update: March 1, 2004
Last modified: July 9, 2014
This is version 95 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot