CSRP2 binding protein is a protein that in humans is encoded by the CSRP2BP gene.[5]

KAT14
Available structures
PDBOrtholog search: PDBe RCSB
Identifiers
AliasesKAT14, ATAC2, CRP2BP, PRO1194, dJ717M23.1, CSRP2BP, lysine acetyltransferase 14
External IDsOMIM: 617501 MGI: 1917264 HomoloGene: 10745 GeneCards: KAT14
Orthologs
SpeciesHumanMouse
Entrez
Ensembl
UniProt
RefSeq (mRNA)

NM_020536
NM_177926

NM_001166640
NM_181417

RefSeq (protein)

NP_065397
NP_001371121

NP_001160112
NP_852082

Location (UCSC)Chr 20: 18.14 – 18.19 MbChr 2: 144.21 – 144.25 Mb
PubMed search[3][4]
Wikidata
View/Edit HumanView/Edit Mouse

CSRP2 is a protein containing two LIM domains, which are double zinc finger motifs found in proteins of diverse function. CSRP2 and some related proteins are thought to act as protein adapters, bridging two or more proteins to form a larger protein complex. The protein encoded by this gene binds to one of the LIM domains of CSRP2 and contains an acetyltransferase domain. Although the encoded protein has been detected in the cytoplasm, it is predominantly a nuclear protein. Alternatively spliced transcript variants have been described.[5]

References edit

  1. ^ a b c GRCh38: Ensembl release 89: ENSG00000149474 - Ensembl, May 2017
  2. ^ a b c GRCm38: Ensembl release 89: ENSMUSG00000027425 - Ensembl, May 2017
  3. ^ "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  4. ^ "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  5. ^ a b "Entrez Gene: CSRP2 binding protein". Retrieved 2011-09-20.

External links edit

Further reading edit

Weiskirchen R, Gressner AM (August 2000). "The cysteine- and glycine-rich LIM domain protein CRP2 specifically interacts with a novel human protein (CRP2BP)". Biochemical and Biophysical Research Communications. 274 (3): 655–663. doi:10.1006/bbrc.2000.3187. PMID 10924333. Wang YL, Faiola F, Xu M, Pan S, Martinez E (December 2008). "Human ATAC Is a GCN5/PCAF-containing acetylase complex with a novel NC2-like histone fold module that interacts with the TATA-binding protein". The Journal of Biological Chemistry. 283 (49): 33808–33815. doi:10.1074/jbc.M806936200. PMC 2590711. PMID 18838386. Guelman S, Kozuka K, Mao Y, Pham V, Solloway MJ, Wang J, et al. (March 2009). "The double-histone-acetyltransferase complex ATAC is essential for mammalian development". Molecular and Cellular Biology. 29 (5): 1176–1188. doi:10.1128/MCB.01599-08. PMC 2643826. PMID 19103755. Wang K, Zhang H, Bloss CS, Duvvuri V, Kaye W, Schork NJ, et al. (September 2011). "A genome-wide association study on common SNPs and rare CNVs in anorexia nervosa". Molecular Psychiatry. 16 (9): 949–959. doi:10.1038/mp.2010.107. PMID 21079607. S2CID 15188506.