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Q8VDP4

- CCAR2_MOUSE

UniProt

Q8VDP4 - CCAR2_MOUSE

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
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    • History
      Entry version 97 (01 Oct 2014)
      Sequence version 2 (01 Mar 2004)
      Previous versions | rss
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    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.By similarity

    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

    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

    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 – 351PhosphothreonineBy similarity
    Modified residuei112 – 1121N6-acetyllysine; by KAT8By similarity
    Modified residuei124 – 1241PhosphoserineBy similarity
    Modified residuei215 – 2151N6-acetyllysine; by KAT8By 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.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Coiled coil

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Coiled coili573 – 59624Sequence AnalysisAdd
    BLAST
    Coiled coili828 – 89871Sequence AnalysisAdd
    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.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti527 – 5293RPK → HAS in AAH25471. (PubMed:15489334)Curated
    Sequence conflicti720 – 7201H → L in AAH38346. (PubMed:15489334)Curated
    Sequence conflicti812 – 8121G → R in BAC27420. (PubMed:16141072)Curated

    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

    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: October 1, 2014
    This is version 97 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