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Q8N163 (CCAR2_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 114. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Web links·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
DBIRD complex subunit KIAA1967
Deleted in breast cancer gene 1 protein
Short name=DBC-1
Short name=DBC.1
p30 DBC
Gene names
Name:CCAR2
Synonyms:DBC1, KIAA1967
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length923 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. Inhibits SUV39H1 methyltransferase activity. As part of a histone H3-specific methyltransferase complex may mediate ligand-dependent transcriptional activation by nuclear hormone receptors. Plays a critical role in maintaining genomic stability and cellular integrity following UV-induced genotoxic stress. Ref.9 Ref.10 Ref.13 Ref.14 Ref.20 Ref.21

Subunit structure

Component of the DBIRD complex. Interacts with ZNF326/ZIRD; the interaction is direct. Interacts (via N-terminus) with SIRT1. 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.9 Ref.10 Ref.13 Ref.14 Ref.20 Ref.21

Subcellular location

Nucleus. Note: Recruited to chromatin, post-UV irradiation. Ref.21

Tissue specificity

Expressed ubiquitously in normal tissues. Expressed in 84 to 100% of neoplastic breast, lung, and colon tissues. Ref.7

Sequence caution

The sequence AAG02472.1 differs from that shown. Reason: Frameshift at positions 610, 622, 794 and 810.

The sequence BAB85553.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.

Ontologies

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

Inferred from mutant phenotype Ref.20. 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 direct assay PubMed 15824730. Source: UniProtKB

negative regulation of catalytic activity

Inferred from direct assay Ref.9Ref.10. Source: GOC

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

Inferred from mutant phenotype Ref.21. Source: UniProtKB

positive regulation of DNA damage checkpoint

Inferred from mutant phenotype Ref.21. Source: UniProtKB

positive regulation of apoptotic process

Inferred from mutant phenotype Ref.9Ref.10. Source: UniProtKB

regulation of DNA-templated transcription, elongation

Inferred from mutant phenotype Ref.20. Source: UniProtKB

response to UV

Inferred from mutant phenotype Ref.21. Source: UniProtKB

   Cellular_componentDBIRD complex

Inferred from direct assay Ref.20. Source: UniProtKB

cytoplasm

Inferred from direct assay PubMed 15824730. Source: UniProtKB

mitochondrial matrix

Inferred from direct assay PubMed 15824730. Source: UniProtKB

nuclear chromatin

Inferred from direct assay Ref.21. Source: UniProtKB

nucleus

Inferred from direct assay PubMed 15824730. Source: UniProtKB

   Molecular_functionRNA polymerase II core binding

Inferred from direct assay Ref.20. Source: UniProtKB

enzyme binding

Inferred from physical interaction Ref.9Ref.14. Source: UniProtKB

enzyme inhibitor activity

Inferred from direct assay Ref.9Ref.10. Source: UniProtKB

poly(A) RNA binding

Inferred from direct assay PubMed 22658674PubMed 22681889. Source: UniProtKB

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

MYCP011068EBI-355410,EBI-447544
ORFQ9Q2G45EBI-355410,EBI-6248094From a different organism.
SIRT1Q96EB69EBI-355410,EBI-1802965

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q8N163-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
Isoform 2 (identifier: Q8N163-2)

The sequence of this isoform differs from the canonical sequence as follows:
     910-923: ADSWVEKEEPAPSN → VRWGWTRRQHSSFP
Note: No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 923923Cell cycle and apoptosis regulator protein 2
PRO_0000050813

Regions

Coiled coil829 – 90981 Potential

Amino acid modifications

Modified residue351Phosphothreonine Ref.15 Ref.17
Modified residue1241Phosphoserine Ref.11 Ref.17
Modified residue2151N6-acetyllysine Ref.16
Modified residue6751Phosphoserine Ref.8 Ref.11 Ref.15 Ref.17
Modified residue6781Phosphoserine Ref.8 Ref.11 Ref.15 Ref.17 Ref.19
Modified residue6811Phosphoserine Ref.8 Ref.11 Ref.15 Ref.17

Natural variations

Alternative sequence910 – 92314ADSWV…PAPSN → VRWGWTRRQHSSFP in isoform 2.
VSP_017092

Experimental info

Mutagenesis243 – 26422Missing: Abolishes binding to SIRT1. Ref.9
Sequence conflict471R → S in CAD38866. Ref.2
Sequence conflict471R → S in CAD39017. Ref.2
Sequence conflict8501T → S in AAH65495. Ref.5
Sequence conflict9081E → G in CAD38866. Ref.2
Sequence conflict9081E → G in CAD39017. Ref.2

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified January 24, 2006. Version 2.
Checksum: 1733934377E35D21

FASTA923102,902
        10         20         30         40         50         60 
MSQFKRQRIN PLPGGRNFSG TASTSLLGPP PGLLTPPVAT ELSQNARHLQ GGEKQRVFTG 

        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 LPPYRVHLTP YTVDSPICDF 

       250        260        270        280        290        300 
LELQRRYRSL LVPSDFLSVH LSWLSAFPLS QPFSLHHPSR IQVSSEKEAA PDAGAEPITA 

       310        320        330        340        350        360 
DSDPAYSSKV LLLSSPGLEE LYRCCMLFVD DMAEPRETPE HPLKQIKFLL GRKEEEAVLV 

       370        380        390        400        410        420 
GGEWSPSLDG LDPQADPQVL VRTAIRCAQA QTGIDLSGCT KWWRFAEFQY LQPGPPRRLQ 

       430        440        450        460        470        480 
TVVVYLPDVW TIMPTLEEWE ALCQQKAAEA APPTQEAQGE TEPTEQAPDA LEQAADTSRR 

       490        500        510        520        530        540 
NAETPEATTQ QETDTDLPEA PPPPLEPAVI ARPGCVNLSL HGIVEDRRPK ERISFEVMVL 

       550        560        570        580        590        600 
AELFLEMLQR DFGYRVYKML LSLPEKVVSP PEPEKEEAAK EEATKEEEAI KEEVVKEPKD 

       610        620        630        640        650        660 
EAQNEGPATE SEAPLKEDGL LPKPLSSGGE EEEKPRGEAS EDLCEMALDP ELLLLRDDGE 

       670        680        690        700        710        720 
EEFAGAKLED SEVRSVASNQ SEMEFSSLQD MPKELDPSAV LPLDCLLAFV FFDANWCGYL 

       730        740        750        760        770        780 
HRRDLERILL TLGIRLSAEQ AKQLVSRVVT QNICQYRSLQ YSRQEGLDGG LPEEVLFGNL 

       790        800        810        820        830        840 
DLLPPPGKST KPGAAPTEHK ALVSHNGSLI NVGSLLQRAE QQDSGRLYLE NKIHTLELKL 

       850        860        870        880        890        900 
EESHNRFSAT EVTNKTLAAE MQELRVRLAE AEETARTAER QKSQLQRLLQ ELRRRLTPLQ 

       910        920 
LEIQRVVEKA DSWVEKEEPA PSN 

« Hide

Isoform 2 [UniParc].

Checksum: 3C1BB0DE06A20926
Show »

FASTA923103,143

References

« Hide 'large scale' references
[1]"Complete sequencing and characterization of 21,243 full-length human cDNAs."
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. expand/collapse author list , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
Tissue: Placenta.
[2]"The full-ORF clone resource of the German cDNA consortium."
Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U., Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A., Wiemann S., Schupp I.
BMC Genomics 8:399-399(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
Tissue: Amygdala and Testis.
[3]"DNA sequence and analysis of human chromosome 8."
Nusbaum C., Mikkelsen T.S., Zody M.C., Asakawa S., Taudien S., Garber M., Kodira C.D., Schueler M.G., Shimizu A., Whittaker C.A., Chang J.L., Cuomo C.A., Dewar K., FitzGerald M.G., Yang X., Allen N.R., Anderson S., Asakawa T. expand/collapse author list , Blechschmidt K., Bloom T., Borowsky M.L., Butler J., Cook A., Corum B., DeArellano K., DeCaprio D., Dooley K.T., Dorris L. III, Engels R., Gloeckner G., Hafez N., Hagopian D.S., Hall J.L., Ishikawa S.K., Jaffe D.B., Kamat A., Kudoh J., Lehmann R., Lokitsang T., Macdonald P., Major J.E., Matthews C.D., Mauceli E., Menzel U., Mihalev A.H., Minoshima S., Murayama Y., Naylor J.W., Nicol R., Nguyen C., O'Leary S.B., O'Neill K., Parker S.C.J., Polley A., Raymond C.K., Reichwald K., Rodriguez J., Sasaki T., Schilhabel M., Siddiqui R., Smith C.L., Sneddon T.P., Talamas J.A., Tenzin P., Topham K., Venkataraman V., Wen G., Yamazaki S., Young S.K., Zeng Q., Zimmer A.R., Rosenthal A., Birren B.W., Platzer M., Shimizu N., Lander E.S.
Nature 439:331-335(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[4]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[5]"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] (ISOFORM 1).
Tissue: Lymph and Placenta.
[6]"Prediction of the coding sequences of unidentified human genes. XXII. The complete sequences of 50 new cDNA clones which code for large proteins."
Nagase T., Kikuno R., Ohara O.
DNA Res. 8:319-327(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 133-923 (ISOFORM 2).
Tissue: Brain.
[7]"DBC2, a candidate for a tumor suppressor gene involved in breast cancer."
Hamaguchi M., Meth J.L., von Klitzing C., Wei W., Esposito D., Rodgers L., Walsh T., Welcsh P., King M.C., Wigler M.H.
Proc. Natl. Acad. Sci. U.S.A. 99:13647-13652(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 439-845, TISSUE SPECIFICITY.
[8]"Global, in vivo, and site-specific phosphorylation dynamics in signaling networks."
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.
Cell 127:635-648(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-675; SER-678 AND SER-681, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[9]"DBC1 is a negative regulator of SIRT1."
Kim J.-E., Chen J., Lou Z.
Nature 451:583-586(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION AS SIRT1 INHIBITOR, INTERACTION WITH SIRT1, MUTAGENESIS OF 243-LEU--LEU-264, IDENTIFICATION BY MASS SPECTROMETRY.
[10]"Negative regulation of the deacetylase SIRT1 by DBC1."
Zhao W., Kruse J.-P., Tang Y., Jung S.Y., Qin J., Gu W.
Nature 451:587-590(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION IN APOPTOSIS, INTERACTION WITH SIRT1.
[11]"A quantitative atlas of mitotic phosphorylation."
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-124; SER-675; SER-678 AND SER-681, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[12]"Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[13]"Identification and characterization of a novel nuclear protein complex involved in nuclear hormone receptor-mediated gene regulation."
Garapaty S., Xu C.F., Trojer P., Mahajan M.A., Neubert T.A., Samuels H.H.
J. Biol. Chem. 284:7542-7552(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION IN TRANSCRIPTIONAL REGULATION, IDENTIFICATION IN A COMPLEX WITH HCFC1; MKI67; C11ORF30; MATR3; HSPA8; TUBB2A; ZNF335; ASCL2; RBBP5 AND WDR5.
[14]"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.
[15]"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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-35; SER-675; SER-678 AND SER-681, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Leukemic T-cell.
[16]"Lysine acetylation targets protein complexes and co-regulates major cellular functions."
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M.
Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-215, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[17]"Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-35; SER-124; SER-675; SER-678 AND SER-681, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[18]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[19]"System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-678, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[20]"DBIRD complex integrates alternative mRNA splicing with RNA polymerase II transcript elongation."
Close P., East P., Dirac-Svejstrup A.B., Hartmann H., Heron M., Maslen S., Chariot A., Soding J., Skehel M., Svejstrup J.Q.
Nature 484:386-389(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION IN THE DBIRD COMPLEX, FUNCTION, INTERACTION WITH ZNF326.
[21]"Deleted in breast cancer 1 (DBC1) deficiency results in apoptosis of breast cancer cells through impaired responses to UV-induced DNA damage."
Kim W., Kim J.E.
Cancer Lett. 333:180-186(2013) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH SIRT1.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AK096547 mRNA. No translation available.
AK314535 mRNA. Translation: BAG37126.1.
AL834162 mRNA. Translation: CAD38866.1.
AL834351 mRNA. Translation: CAD39016.1.
AL834352 mRNA. Translation: CAD39017.1.
BX640952 mRNA. Translation: CAE45976.1.
AL137523 mRNA. Translation: CAB70788.3.
AC037459 Genomic DNA. No translation available.
CH471080 Genomic DNA. Translation: EAW63658.1.
CH471080 Genomic DNA. Translation: EAW63661.1.
BC018269 mRNA. Translation: AAH18269.2.
BC065495 mRNA. Translation: AAH65495.1.
AB075847 mRNA. Translation: BAB85553.1. Different initiation.
AF293335 mRNA. Translation: AAG02472.1. Frameshift.
PIRT46368.
RefSeqNP_066997.3. NM_021174.5.
UniGeneHs.744848.

3D structure databases

ProteinModelPortalQ8N163.
SMRQ8N163. Positions 57-119.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid121775. 67 interactions.
DIPDIP-38122N.
IntActQ8N163. 36 interactions.
MINTMINT-5003338.

PTM databases

PhosphoSiteQ8N163.

Polymorphism databases

DMDM85701135.

Proteomic databases

PaxDbQ8N163.
PRIDEQ8N163.

Protocols and materials databases

DNASU57805.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000308511; ENSP00000310670; ENSG00000158941. [Q8N163-1]
ENST00000389279; ENSP00000373930; ENSG00000158941. [Q8N163-1]
GeneID57805.
KEGGhsa:57805.
UCSCuc003xch.3. human. [Q8N163-1]

Organism-specific databases

CTD57805.
GeneCardsGC08P022463.
HGNCHGNC:23360. CCAR2.
HPAHPA019907.
HPA019943.
MIM607359. gene.
neXtProtNX_Q8N163.
PharmGKBPA134993792.
HUGESearch...
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG307741.
HOVERGENHBG081843.
InParanoidQ8N163.
OMAMSQFKRQ.
OrthoDBEOG7CK365.
PhylomeDBQ8N163.
TreeFamTF316387.

Gene expression databases

ArrayExpressQ8N163.
BgeeQ8N163.
CleanExHS_DBC1.
GenevestigatorQ8N163.

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:SF5. PTHR14304:SF5. 1 hit.
PfamPF14443. DBC1. 1 hit.
PF14444. S1-like. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSKIAA1967. human.
GeneWikiKIAA1967.
GenomeRNAi57805.
NextBio64756.
SOURCESearch...

Entry information

Entry nameCCAR2_HUMAN
AccessionPrimary (citable) accession number: Q8N163
Secondary accession number(s): A6NL03 expand/collapse secondary AC list , B2RB79, D3DSR6, Q6P0Q9, Q8N3G7, Q8N8M1, Q8TF34, Q9H9Q9, Q9HD12, Q9NT55
Entry history
Integrated into UniProtKB/Swiss-Prot: January 24, 2006
Last sequence update: January 24, 2006
Last modified: April 16, 2014
This is version 114 of the entry and version 2 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

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human chromosome 8

Human chromosome 8: entries, gene names and cross-references to MIM