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Q8CID0 (CSR2B_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 75. 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·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Cysteine-rich protein 2-binding protein

Short name=CSRP2-binding protein
Alternative name(s):
ADA2A-containing complex subunit 2
Short name=ATAC2
CRP2-binding partner
Short name=CRP2BP
Gene names
Name:Csrp2bp
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length779 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Component of the ATAC complex, a complex with histone acetyltransferase activity on histones H3 and H4. May function as a scaffold for the ATAC complex to promote ATAC complex stability. Has also weak histone acetyltransferase activity toward histone H4. Required for the normal progression through G1 and G2/M phases of the cell cycle By similarity.

Subunit structure

Interacts with the LIM 1 domain of CSRP2 By similarity. Component of the ADA2A-containing complex (ATAC), composed of CSRP2BP, KAT2A, TADA2L, TADA3L, ZZ3, MBIP, WDR5, YEATS2, CCDC101 and DR1 By similarity. In the complex, it probably interacts directly with KAT2A, MBIP and WDR5 By similarity.

Subcellular location

Nucleus By similarity. Cytoplasm By similarity. Note: Mainly nuclear By similarity.

Disruption phenotype

Early embryonic lethality. Severe growth retardation, increased apoptosis, and alterations in the cell cycle. Ref.3

Sequence similarities

Contains 1 N-acetyltransferase domain.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 779779Cysteine-rich protein 2-binding protein
PRO_0000304937

Regions

Domain635 – 779145N-acetyltransferase

Amino acid modifications

Modified residue2301N6-acetyllysine Ref.4
Modified residue2911N6-acetyllysine Ref.4

Experimental info

Sequence conflict1441G → V in AAH31563. Ref.2
Sequence conflict4971A → L in AAH31563. Ref.2

Sequences

Sequence LengthMass (Da)Tools
Q8CID0 [UniParc].

Last modified October 2, 2007. Version 2.
Checksum: 6750A26E6DF1B749

FASTA77988,217
        10         20         30         40         50         60 
MDSSIHLSGL LSRHDDDATR TSTSEGLEEG EVEGETLLIV ESEDQASVDL SHDQSGDSLN 

        70         80         90        100        110        120 
SDEGDVSWME EQLSYFCDKC QKWIPASQLR EQLSYLKGDN FFRFTCCDCS ADGKEQYERL 

       130        140        150        160        170        180 
KLTWQQVVML AMYNLSLEGS GRQGYFRWKE DICAFIEKHW TFLLGNRKKT STWWSTVAGC 

       190        200        210        220        230        240 
LSVGSPVYFR SGAQEFGEPG WWKLVHNRPP TMRPEGEKLA ASTLKVKASK PTLDPIITVE 

       250        260        270        280        290        300 
GLRKRASRNP VESAMELKEK RSRTQEAKDI RRAQKEAAGL LDRSTSSTPV KFISRGRRPD 

       310        320        330        340        350        360 
LILEKGEVID FSSLSSSDRT PLTSPSPSPS LDFSAPGTPA SHSATPSLLS EADLIPDVMP 

       370        380        390        400        410        420 
PQALFHDDDE LEGDGVIDPG MEYIPPPAGS ASGLLGSRKK VRAPEQIKQE VDSEEEKPDR 

       430        440        450        460        470        480 
MDGDSEDTDS NISLHTRARE KRKPPLEKDM KPKGPRYTPV SIYEEKLLLK RLEACPGAVA 

       490        500        510        520        530        540 
MTPEARRLKR KLIVRQAKRD RGLPLFDLDE VVNAALLLVD GIYGAKDGGA SRLAAGQATY 

       550        560        570        580        590        600 
RTTCQDFRIL DRYQTALPAR KGFRHQTTRF LYRLVGSEDL AVDQSIISPY TSRILKPYIR 

       610        620        630        640        650        660 
RDYETKPPKL QLLSQIRSHL HRSDPHWTPG PDAPLDYCYV RPNHIPTINS MCQEFFWPGI 

       670        680        690        700        710        720 
DLSECLQYPD FSVVVLYKKV IVAFGFMVPD VKYNEAYISF LLVHPEWRRA GIATFMIYHL 

       730        740        750        760        770 
IQTCMGKDVT LHVSASNPAM LLYQKFGFKT EEYVLDFYDK YYPLESTECK HAFFLRLRR 

« Hide

References

« Hide 'large scale' references
[1]"Lineage-specific biology revealed by a finished genome assembly of the mouse."
Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S. expand/collapse author list , Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K., Eichler E.E., Ponting C.P.
PLoS Biol. 7:E1000112-E1000112(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: C57BL/6J.
[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]"The double-histone-acetyltransferase complex ATAC is essential for mammalian development."
Guelman S., Kozuka K., Mao Y., Pham V., Solloway M.J., Wang J., Wu J., Lill J.R., Zha J.
Mol. Cell. Biol. 29:1176-1188(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: DISRUPTION PHENOTYPE.
[4]"SIRT5-mediated lysine desuccinylation impacts diverse metabolic pathways."
Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y., Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.
Mol. Cell 50:919-930(2013) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-230 AND LYS-291, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Embryonic fibroblast.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AL808123 Genomic DNA. Translation: CAM26792.1.
BC031563 mRNA. Translation: AAH31563.1.
RefSeqNP_852082.2. NM_181417.3.
UniGeneMm.227925.
Mm.490976.

3D structure databases

ProteinModelPortalQ8CID0.
SMRQ8CID0. Positions 633-760.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid230756. 10 interactions.
IntActQ8CID0. 2 interactions.

PTM databases

PhosphoSiteQ8CID0.

Proteomic databases

PRIDEQ8CID0.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000028911; ENSMUSP00000028911; ENSMUSG00000027425.
GeneID228714.
KEGGmmu:228714.
UCSCuc008mqy.2. mouse.

Organism-specific databases

CTD57325.
MGIMGI:1917264. Csrp2bp.

Phylogenomic databases

eggNOGNOG295186.
GeneTreeENSGT00390000001146.
HOGENOMHOG000230880.
HOVERGENHBG051142.
InParanoidQ8CID0.
OMAKEDICAF.
OrthoDBEOG7M6D6R.
PhylomeDBQ8CID0.
TreeFamTF324809.

Gene expression databases

BgeeQ8CID0.
GenevestigatorQ8CID0.

Family and domain databases

Gene3D3.40.630.30. 1 hit.
InterProIPR016181. Acyl_CoA_acyltransferase.
IPR000182. GNAT_dom.
[Graphical view]
PfamPF00583. Acetyltransf_1. 1 hit.
[Graphical view]
SUPFAMSSF55729. SSF55729. 1 hit.
PROSITEPS51186. GNAT. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio379084.
PROQ8CID0.
SOURCESearch...

Entry information

Entry nameCSR2B_MOUSE
AccessionPrimary (citable) accession number: Q8CID0
Secondary accession number(s): A2ANA8
Entry history
Integrated into UniProtKB/Swiss-Prot: October 2, 2007
Last sequence update: October 2, 2007
Last modified: April 16, 2014
This is version 75 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

MGD cross-references

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