SubmitCancel

Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

Q8VDP4

- CCAR2_MOUSE

UniProt

Q8VDP4 - CCAR2_MOUSE

(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Protein

Cell cycle and apoptosis regulator protein 2

Gene
Ccar2
Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 4 out of 5 - Experimental evidence at protein leveli

Functioni

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.1 Publication

GO - Molecular functioni

  1. enzyme inhibitor activity Source: UniProtKB
  2. RNA polymerase II core binding Source: UniProtKB

GO - Biological processi

  1. cell cycle Source: UniProtKB-KW
  2. cellular response to DNA damage stimulus Source: UniProtKB-KW
  3. mitochondrial fragmentation involved in apoptotic process Source: Ensembl
  4. mRNA processing Source: UniProtKB-KW
  5. negative regulation of intrinsic apoptotic signaling pathway in response to DNA damage Source: UniProtKB
  6. positive regulation of apoptotic process Source: UniProtKB
  7. positive regulation of DNA damage checkpoint Source: UniProtKB
  8. regulation of DNA-templated transcription, elongation Source: UniProtKB
  9. response to UV Source: UniProtKB
  10. RNA splicing Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Metalloenzyme inhibitor

Keywords - Biological processi

Apoptosis, Cell cycle, DNA damage, mRNA processing, mRNA splicing

Enzyme and pathway databases

ReactomeiREACT_222185. Regulation of HSF1-mediated heat shock response.

Names & Taxonomyi

Protein namesi
Recommended name:
Cell cycle and apoptosis regulator protein 2
Alternative name(s):
Cell division cycle and apoptosis regulator protein 2
Gene namesi
Name:Ccar2
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Chromosome 14

Organism-specific databases

MGIiMGI:2444228. Ccar2.

Subcellular locationi

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

GO - Cellular componenti

  1. DBIRD complex Source: UniProtKB
  2. mitochondrial matrix Source: Ensembl
  3. nuclear chromatin Source: UniProtKB
  4. spliceosomal complex Source: Ensembl
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 922922Cell cycle and apoptosis regulator protein 2PRO_0000050814Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei35 – 351Phosphothreonine By similarity
Modified residuei112 – 1121N6-acetyllysine; by KAT8 By similarity
Modified residuei124 – 1241Phosphoserine By similarity
Modified residuei215 – 2151N6-acetyllysine; by KAT8 By similarity
Modified residuei674 – 6741Phosphoserine1 Publication
Modified residuei677 – 6771Phosphoserine2 Publications
Modified residuei680 – 6801Phosphoserine2 Publications

Post-translational modificationi

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

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

MaxQBiQ8VDP4.
PaxDbiQ8VDP4.
PRIDEiQ8VDP4.

PTM databases

PhosphoSiteiQ8VDP4.

Expressioni

Gene expression databases

BgeeiQ8VDP4.
CleanExiMM_2610301G19RIK.
GenevestigatoriQ8VDP4.

Interactioni

Subunit structurei

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.1 Publication

Protein-protein interaction databases

BioGridi230123. 2 interactions.
IntActiQ8VDP4. 6 interactions.
MINTiMINT-4119906.
STRINGi10090.ENSMUSP00000036924.

Structurei

3D structure databases

ProteinModelPortaliQ8VDP4.
SMRiQ8VDP4. Positions 55-119.

Family & Domainsi

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili573 – 59624 Reviewed predictionAdd
BLAST
Coiled coili828 – 89871 Reviewed predictionAdd
BLAST

Keywords - Domaini

Coiled coil

Phylogenomic databases

eggNOGiNOG307741.
GeneTreeiENSGT00530000063672.
HOGENOMiHOG000113184.
HOVERGENiHBG081843.
InParanoidiQ8VDP4.
OMAiMSQFKRQ.
OrthoDBiEOG7CK365.
PhylomeDBiQ8VDP4.
TreeFamiTF316387.

Family and domain databases

InterProiIPR028811. CCAR2.
IPR025224. DBC1/CARP1.
IPR025954. DBC1/CARP1_inactive_NUDIX_dom.
IPR025223. S1-like_RNA-bd_dom.
[Graphical view]
PANTHERiPTHR14304. PTHR14304. 1 hit.
PTHR14304:SF12. PTHR14304:SF12. 1 hit.
PfamiPF14443. DBC1. 1 hit.
PF14444. S1-like. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q8VDP4-1 [UniParc]FASTAAdd to Basket

« Hide

MSQFKRQRIN PLPGGRNFSG AASTSLLGPP PGLLTPPVAT DLSQNARHLQ    50
SGEKQRVFTG IVTSLHDYFG VVDEEVFFQL SVVKGRLPQL GEKVLVKAAY 100
NPGQAVPWNA VKVQTLSNQP LLKSPAPPLL HVAALGQKQG ILGAQPQLIF 150
QPHRIPPLFP QKPLSLFQTS HTLHLSHLNR FPARGPHGRL DQGRSDDYDS 200
KKRKQRAGGE PWGAKKPRHD LSPYRVHLTP YTVDSPTCDF LELQRRYRSL 250
LVPSDFLSVH LSWLSAFPLG QPFSLHHPSR IQVSSEKEAA PDTGAEPSPE 300
DSDPTYSSKV LLLSSPGLEE FYRCCMLFVD DMAEPRETPE HPLKQLKFLL 350
GRKEEEAVLV GGEWSPSLDG LDPQADPQVL VRTAIRCAQA QTGIDLSTCT 400
KWWRFAEFQY LQPGPPRQLH TVVVYLPDVW TIMPTLEEWE ALCQQKATEA 450
APQPHEASGE AEATEQAPDV SEQADTSKQN TETMEATTQQ DVDTDLPEAP 500
PPPLEPAVMA RPRCVNLSLY GIVEDRRPKE RISFEVVVLA ELFVEMLQRD 550
FGYRIYKTLL SLPEKVVSPP EPEKEEAAKE DAVKEEEAVK EEAVKVSKDE 600
VQNEGTAAES DSPLKEDGLL PKRPSSGGEE EEKARGEAAE DLCEMALDPD 650
LLLLRDDGED EFAGAKLEET EVRSVASNQS EMEYSSLQDM PKELDPSTVL 700
PLDCLLAFVF FDANWCGYLH RRDLERVLLT LGIRLSAEQA KQLVSRVVAQ 750
NICQYRSLQY SRAEVLDDGL PEDVLFGNLD LLPPSGKSTK PGAAPTEHKG 800
LVPHNGSLIN VGSLLQRAEQ QDSGRLYLEN KIHTLELKLE ESHNRFSATE 850
VTNKTLAAEM QELRARLAEA EETARTAERQ KNQLQRQMQD FRRRLTPLHL 900
EMQRIVEKAD SWVEKEEPTP SN 922
Length:922
Mass (Da):103,002
Last modified:March 1, 2004 - v2
Checksum:i19F43ECEE58F461C
GO

Sequence cautioni

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.

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti527 – 5293RPK → HAS in AAH25471. 1 Publication
Sequence conflicti720 – 7201H → L in AAH38346. 1 Publication
Sequence conflicti812 – 8121G → R in BAC27420. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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.
CCDSiCCDS49534.1.
RefSeqiNP_666167.3. NM_146055.3.
XP_006518959.1. XM_006518896.1.
UniGeneiMm.218284.

Genome annotation databases

EnsembliENSMUST00000035612; ENSMUSP00000036924; ENSMUSG00000033712.
GeneIDi219158.
KEGGimmu:219158.
UCSCiuc007unf.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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 .
CCDSi CCDS49534.1.
RefSeqi NP_666167.3. NM_146055.3.
XP_006518959.1. XM_006518896.1.
UniGenei Mm.218284.

3D structure databases

ProteinModelPortali Q8VDP4.
SMRi Q8VDP4. Positions 55-119.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 230123. 2 interactions.
IntActi Q8VDP4. 6 interactions.
MINTi MINT-4119906.
STRINGi 10090.ENSMUSP00000036924.

PTM databases

PhosphoSitei Q8VDP4.

Proteomic databases

MaxQBi Q8VDP4.
PaxDbi Q8VDP4.
PRIDEi Q8VDP4.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSMUST00000035612 ; ENSMUSP00000036924 ; ENSMUSG00000033712 .
GeneIDi 219158.
KEGGi mmu:219158.
UCSCi uc007unf.1. mouse.

Organism-specific databases

CTDi 57805.
MGIi MGI:2444228. Ccar2.

Phylogenomic databases

eggNOGi NOG307741.
GeneTreei ENSGT00530000063672.
HOGENOMi HOG000113184.
HOVERGENi HBG081843.
InParanoidi Q8VDP4.
OMAi MSQFKRQ.
OrthoDBi EOG7CK365.
PhylomeDBi Q8VDP4.
TreeFami TF316387.

Enzyme and pathway databases

Reactomei REACT_222185. Regulation of HSF1-mediated heat shock response.

Miscellaneous databases

NextBioi 376623.
SOURCEi Search...

Gene expression databases

Bgeei Q8VDP4.
CleanExi MM_2610301G19RIK.
Genevestigatori Q8VDP4.

Family and domain databases

InterProi IPR028811. CCAR2.
IPR025224. DBC1/CARP1.
IPR025954. DBC1/CARP1_inactive_NUDIX_dom.
IPR025223. S1-like_RNA-bd_dom.
[Graphical view ]
PANTHERi PTHR14304. PTHR14304. 1 hit.
PTHR14304:SF12. PTHR14304:SF12. 1 hit.
Pfami PF14443. DBC1. 1 hit.
PF14444. S1-like. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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.
    , 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. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-677 AND SER-680, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Embryonic brain.
  5. 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.

Entry informationi

Entry nameiCCAR2_MOUSE
AccessioniPrimary (citable) accession number: Q8VDP4
Secondary accession number(s): Q6PIB1
, Q8BWR5, Q8C0F0, Q8R3G6
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 24, 2006
Last sequence update: March 1, 2004
Last modified: September 3, 2014
This is version 96 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

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

External Data

Dasty 3

Similar proteinsi