CSRP2_HUMAN
ID CSRP2_HUMAN Reviewed; 193 AA.
AC Q16527; Q93030;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 176.
DE RecName: Full=Cysteine and glycine-rich protein 2;
DE AltName: Full=Cysteine-rich protein 2;
DE Short=CRP2;
DE AltName: Full=LIM domain only protein 5;
DE Short=LMO-5;
DE AltName: Full=Smooth muscle cell LIM protein;
DE Short=SmLIM;
GN Name=CSRP2; Synonyms=LMO5, SMLIM;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Aorta;
RX PubMed=8626582; DOI=10.1074/jbc.271.17.10194;
RA Jain M., Fujita K.P., Hsieh C.-M., Endege W.O., Sibinga N.E.S., Yet S.-F.,
RA Kashiki S., Lee W.-S., Perrella M.A., Haber E., Lee M.-E.;
RT "Molecular cloning and characterization of SmLIM, a developmentally
RT regulated LIM protein preferentially expressed in aortic smooth muscle
RT cells.";
RL J. Biol. Chem. 271:10194-10199(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
RX PubMed=9286703; DOI=10.1006/geno.1997.4855;
RA Weiskirchen R., Erdel M., Utermann G., Bister K.;
RT "Cloning, structural analysis, and chromosomal localization of the human
RT CSRP2 gene encoding the LIM domain protein CRP2.";
RL Genomics 44:83-93(1997).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S.,
RA Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y.,
RA Phelan M., Farmer A.;
RT "Cloning of human full-length CDSs in BD Creator(TM) system donor vector.";
RL Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Placenta;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [5]
RP INTERACTION WITH KAT14.
RX PubMed=10924333; DOI=10.1006/bbrc.2000.3187;
RA Weiskirchen R., Gressner A.M.;
RT "The cysteine- and glycine-rich LIM domain protein CRP2 specifically
RT interacts with a novel human protein.";
RL Biochem. Biophys. Res. Commun. 274:655-663(2000).
RN [6]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [7]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-91, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=28112733; DOI=10.1038/nsmb.3366;
RA Hendriks I.A., Lyon D., Young C., Jensen L.J., Vertegaal A.C.,
RA Nielsen M.L.;
RT "Site-specific mapping of the human SUMO proteome reveals co-modification
RT with phosphorylation.";
RL Nat. Struct. Mol. Biol. 24:325-336(2017).
CC -!- FUNCTION: Drastically down-regulated in response to PDGF-BB or cell
CC injury, that promote smooth muscle cell proliferation and
CC dedifferentiation. Seems to play a role in the development of the
CC embryonic vascular system.
CC -!- SUBUNIT: Interacts with KAT14. The LIM domain 1 is necessary and
CC sufficient for this interaction. Interacts with GLRX3 (By similarity).
CC {ECO:0000250}.
CC -!- INTERACTION:
CC Q16527; Q7LC44: ARC; NbExp=3; IntAct=EBI-2959737, EBI-750550;
CC Q16527; Q9Y2V7: COG6; NbExp=3; IntAct=EBI-2959737, EBI-3866319;
CC Q16527; P36406: TRIM23; NbExp=3; IntAct=EBI-2959737, EBI-740098;
CC Q16527; P14373: TRIM27; NbExp=3; IntAct=EBI-2959737, EBI-719493;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Highly expressed in the aorta, but not in heart and
CC skeletal muscle.
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DR EMBL; U46006; AAC27344.1; -; mRNA.
DR EMBL; U57646; AAC51753.1; -; mRNA.
DR EMBL; U95018; AAC51755.1; -; Genomic_DNA.
DR EMBL; BT019913; AAV38716.1; -; mRNA.
DR EMBL; BC000992; AAH00992.1; -; mRNA.
DR CCDS; CCDS9015.1; -.
DR RefSeq; NP_001287894.1; NM_001300965.1.
DR RefSeq; NP_001312.1; NM_001321.2.
DR AlphaFoldDB; Q16527; -.
DR SMR; Q16527; -.
DR BioGRID; 107848; 37.
DR IntAct; Q16527; 21.
DR MINT; Q16527; -.
DR STRING; 9606.ENSP00000310901; -.
DR ChEMBL; CHEMBL4295833; -.
DR iPTMnet; Q16527; -.
DR MetOSite; Q16527; -.
DR PhosphoSitePlus; Q16527; -.
DR BioMuta; CSRP2; -.
DR DMDM; 2497674; -.
DR EPD; Q16527; -.
DR jPOST; Q16527; -.
DR MassIVE; Q16527; -.
DR MaxQB; Q16527; -.
DR PaxDb; Q16527; -.
DR PeptideAtlas; Q16527; -.
DR PRIDE; Q16527; -.
DR ProteomicsDB; 60894; -.
DR Antibodypedia; 29699; 244 antibodies from 34 providers.
DR DNASU; 1466; -.
DR Ensembl; ENST00000311083.10; ENSP00000310901.5; ENSG00000175183.10.
DR Ensembl; ENST00000546966.5; ENSP00000450056.1; ENSG00000175183.10.
DR GeneID; 1466; -.
DR KEGG; hsa:1466; -.
DR MANE-Select; ENST00000311083.10; ENSP00000310901.5; NM_001321.3; NP_001312.1.
DR UCSC; uc001syl.2; human.
DR CTD; 1466; -.
DR DisGeNET; 1466; -.
DR GeneCards; CSRP2; -.
DR HGNC; HGNC:2470; CSRP2.
DR HPA; ENSG00000175183; Low tissue specificity.
DR MIM; 601871; gene.
DR neXtProt; NX_Q16527; -.
DR OpenTargets; ENSG00000175183; -.
DR PharmGKB; PA26968; -.
DR VEuPathDB; HostDB:ENSG00000175183; -.
DR eggNOG; KOG1700; Eukaryota.
DR GeneTree; ENSGT00940000154980; -.
DR HOGENOM; CLU_054591_1_0_1; -.
DR InParanoid; Q16527; -.
DR OrthoDB; 1214165at2759; -.
DR PhylomeDB; Q16527; -.
DR TreeFam; TF313758; -.
DR PathwayCommons; Q16527; -.
DR SignaLink; Q16527; -.
DR BioGRID-ORCS; 1466; 9 hits in 1082 CRISPR screens.
DR GeneWiki; CSRP2; -.
DR GenomeRNAi; 1466; -.
DR Pharos; Q16527; Tbio.
DR PRO; PR:Q16527; -.
DR Proteomes; UP000005640; Chromosome 12.
DR RNAct; Q16527; protein.
DR Bgee; ENSG00000175183; Expressed in oocyte and 206 other tissues.
DR ExpressionAtlas; Q16527; baseline and differential.
DR Genevisible; Q16527; HS.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005925; C:focal adhesion; HDA:UniProtKB.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0030018; C:Z disc; IBA:GO_Central.
DR GO; GO:0042805; F:actinin binding; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0008307; F:structural constituent of muscle; IBA:GO_Central.
DR GO; GO:0030036; P:actin cytoskeleton organization; IBA:GO_Central.
DR GO; GO:0030154; P:cell differentiation; NAS:UniProtKB.
DR GO; GO:0060537; P:muscle tissue development; IBA:GO_Central.
DR GO; GO:0045214; P:sarcomere organization; IBA:GO_Central.
DR InterPro; IPR001781; Znf_LIM.
DR Pfam; PF00412; LIM; 2.
DR SMART; SM00132; LIM; 2.
DR PROSITE; PS00478; LIM_DOMAIN_1; 2.
DR PROSITE; PS50023; LIM_DOMAIN_2; 2.
PE 1: Evidence at protein level;
KW Acetylation; Developmental protein; Differentiation; Isopeptide bond;
KW LIM domain; Metal-binding; Nucleus; Reference proteome; Repeat;
KW Ubl conjugation; Zinc.
FT CHAIN 1..193
FT /note="Cysteine and glycine-rich protein 2"
FT /id="PRO_0000075721"
FT DOMAIN 10..61
FT /note="LIM zinc-binding 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00125"
FT DOMAIN 119..170
FT /note="LIM zinc-binding 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00125"
FT MOTIF 64..69
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000255"
FT MOD_RES 112
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P97314"
FT MOD_RES 131
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P21291"
FT MOD_RES 137
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P97315"
FT MOD_RES 137
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P97314"
FT MOD_RES 161
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P97315"
FT CROSSLNK 91
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
SQ SEQUENCE 193 AA; 20954 MW; 2E4231D6427579E7 CRC64;
MPVWGGGNKC GACGRTVYHA EEVQCDGRSF HRCCFLCMVC RKNLDSTTVA IHDEEIYCKS
CYGKKYGPKG YGYGQGAGTL NMDRGERLGI KPESVQPHRP TTNPNTSKFA QKYGGAEKCS
RCGDSVYAAE KIIGAGKPWH KNCFRCAKCG KSLESTTLTE KEGEIYCKGC YAKNFGPKGF
GYGQGAGALV HAQ
