CSRP2

Protein-coding gene in humans

CSRP2

Available structures

PDB

Ortholog search: PDBe RCSB

List of PDB id codes
2CU8

Identifiers

Aliases

CSRP2, CRP2, LMO5, SmLIM, cysteine and glycine rich protein 2

External IDs

OMIM: 601871; MGI: 1202907; HomoloGene: 111061; GeneCards: CSRP2; OMA:CSRP2 - orthologs

Gene location (Human)

Chr.	Chromosome 12 (human)^[1]

Band	12q21.2	Start	76,858,709 bp^[1]
Band	12q21.2	End	76,879,023 bp^[1]

Gene location (Mouse)

Chr.	Chromosome 10 (mouse)^[2]

Band	10\|10 D1	Start	110,755,650 bp^[2]
Band	10\|10 D1	End	110,775,483 bp^[2]

RNA expression pattern

Bgee

Human

Mouse (ortholog)

Top expressed in

oocyte

secondary oocyte

ganglionic eminence

tibial arteries

right coronary artery

mucosa of paranasal sinus

parietal pleura

gingival epithelium

gastric mucosa

optic nerve

Top expressed in

ascending aorta

aortic valve

tunica media of zone of aorta

belly cord

endocardial cushion

atrium

mandibular prominence

external carotid artery

atrioventricular valve

internal carotid artery

More reference expression data

BioGPS


More reference expression data

Gene ontology
Molecular function	protein binding metal ion binding molecular function structural constituent of muscle actinin binding
Cellular component	nucleus focal adhesion cytoplasm Z discdkac
Biological process	multicellular organism development cell differentiation actin cytoskeleton organization sarcomere organization muscle tissue development
Sources:Amigo / QuickGO

Orthologs

Species

Human

Mouse

Entrez


1466


13008

Ensembl


ENSG00000175183


ENSMUSG00000020186

UniProt


Q16527


P97314

RefSeq (mRNA)


NM_001300965 NM_001321


NM_007792

RefSeq (protein)


NP_001287894 NP_001312


NP_031818

Location (UCSC)

Chr 12: 76.86 – 76.88 Mb

Chr 10: 110.76 – 110.78 Mb

PubMed search

^[3]

^[4]

Wikidata

View/Edit Human

View/Edit Mouse

Cysteine and glycine-rich protein 2 is a protein that in humans is encoded by the CSRP2 gene.^[5]^[6]^[7]

CSRP2 is a member of the CSRP family of genes, encoding a group of LIM domain proteins, which may be involved in regulatory processes important for development and cellular differentiation. CRP2 contains two copies of the cysteine-rich amino acid sequence motif (LIM) with putative zinc-binding activity, and may be involved in regulating ordered cell growth. Other genes in the family include CSRP1 and CSRP3.^[7]

References

^ ^a ^b ^c GRCh38: Ensembl release 89: ENSG00000175183 – Ensembl, May 2017
^ ^a ^b ^c GRCm38: Ensembl release 89: ENSMUSG00000020186 – Ensembl, May 2017
^ "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
^ "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
^ Weiskirchen R, Pino JD, Macalma T, Bister K, Beckerle MC (Jan 1996). "The cysteine-rich protein family of highly related LIM domain proteins". J Biol Chem. 270 (48): 28946–54. doi:10.1074/jbc.270.48.28946. PMID 7499425.
^ Weiskirchen R, Erdel M, Utermann G, Bister K (Nov 1997). "Cloning, structural analysis, and chromosomal localization of the human CSRP2 gene encoding the LIM domain protein CRP2". Genomics. 44 (1): 83–93. doi:10.1006/geno.1997.4855. PMID 9286703.
^ ^a ^b "Entrez Gene: CSRP2 cysteine and glycine-rich protein 2".

External links

Human CSRP2 genome location and CSRP2 gene details page in the UCSC Genome Browser.

Jain MK, Fujita KP, Hsieh CM, Endege WO, Sibinga NE, Yet SF, Kashiki S, Lee WS, Perrella MA (1996). "Molecular cloning and characterization of SmLIM, a developmentally regulated LIM protein preferentially expressed in aortic smooth muscle cells". J. Biol. Chem. 271 (17): 10194–9. doi:10.1074/jbc.271.17.10194. PMID 8626582.
Karim MA, Ohta K, Egashira M, Jinno Y, Niikawa N, Matsuda I, Indo Y (1997). "Human ESP1/CRP2, a member of the LIM domain protein family: characterization of the cDNA and assignment of the gene locus to chromosome 14q32.3". Genomics. 31 (2): 167–76. doi:10.1006/geno.1996.0028. PMID 8824798.
Weiskirchen R, Gressner AM (2000). "The cysteine- and glycine-rich LIM domain protein CRP2 specifically interacts with a novel human protein (CRP2BP)". Biochem. Biophys. Res. Commun. 274 (3): 655–63. doi:10.1006/bbrc.2000.3187. PMID 10924333.
Weiskirchen R, Moser M, Weiskirchen S, Erdel M, Dahmen S, Buettner R, Gressner AM (2001). "LIM-domain protein cysteine- and glycine-rich protein 2 (CRP2) is a novel marker of hepatic stellate cells and binding partner of the protein inhibitor of activated STAT1". Biochem. J. 359 (Pt 3): 485–96. doi:10.1042/0264-6021:3590485. PMC 1222169. PMID 11672422.
Strausberg RL, Feingold EA, Grouse LH, Derge JG, Klausner RD, Collins FS, Wagner L, Shenmen CM, Schuler GD (2003). "Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences". Proc. Natl. Acad. Sci. U.S.A. 99 (26): 16899–903. Bibcode:2002PNAS...9916899M. doi:10.1073/pnas.242603899. PMC 139241. PMID 12477932.
Wang M, Hu Y, Shima I, Stearns ME (2003). "IL-10/IL-10 receptor signaling regulates TIMP-1 expression in primary human prostate tumor lines". Cancer Biol. Ther. 1 (5): 556–63. doi:10.4161/cbt.1.5.222. PMID 12496489.
Stearns ME, Wang M, Hu Y, Garcia FU (2004). "Interleukin-10 activation of the interleukin-10E1 pathway and tissue inhibitor of metalloproteinase-1 expression is enhanced by proteasome inhibitors in primary prostate tumor lines". Mol. Cancer Res. 1 (9): 631–42. PMID 12861049.
Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R (2004). "The Status, Quality, and Expansion of the NIH Full-Length cDNA Project: The Mammalian Gene Collection (MGC)". Genome Res. 14 (10B): 2121–7. doi:10.1101/gr.2596504. PMC 528928. PMID 15489334.

PDB gallery

1a7i: AMINO-TERMINAL LIM DOMAIN FROM QUAIL CYSTEINE AND GLYCINE-RICH PROTEIN, NMR, MINIMIZED AVERAGE STRUCTURE
1cxx: MUTANT R122A OF QUAIL CYSTEINE AND GLYCINE-RICH PROTEIN, NMR, MINIMIZED STRUCTURE
1ibi: QUAIL CYSTEINE AND GLYCINE-RICH PROTEIN, NMR, 15 MINIMIZED MODEL STRUCTURES
1qli: QUAIL CYSTEINE AND GLYCINE-RICH PROTEIN, NMR, MINIMIZED AVERAGE STRUCTURE