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   27-MAR-2024, entry version 185.
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.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
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; 64.
DR   IntAct; Q16527; 21.
DR   MINT; Q16527; -.
DR   STRING; 9606.ENSP00000310901; -.
DR   ChEMBL; CHEMBL4295833; -.
DR   GlyGen; Q16527; 1 site, 1 O-linked glycan (1 site).
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; 9606-ENSP00000310901; -.
DR   PeptideAtlas; Q16527; -.
DR   ProteomicsDB; 60894; -.
DR   Pumba; Q16527; -.
DR   Antibodypedia; 29699; 266 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   AGR; HGNC:2470; -.
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; 7294at2759; -.
DR   PhylomeDB; Q16527; -.
DR   TreeFam; TF313758; -.
DR   PathwayCommons; Q16527; -.
DR   SignaLink; Q16527; -.
DR   BioGRID-ORCS; 1466; 10 hits in 1160 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 208 other cell types or tissues.
DR   ExpressionAtlas; Q16527; baseline and differential.
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: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   CDD; cd09480; LIM1_CRP2; 1.
DR   CDD; cd09840; LIM2_CRP2; 1.
DR   Gene3D; 2.10.110.10; Cysteine Rich Protein; 2.
DR   InterPro; IPR001781; Znf_LIM.
DR   PANTHER; PTHR24215:SF3; CYSTEINE AND GLYCINE-RICH PROTEIN 2; 1.
DR   PANTHER; PTHR24215; RHO-GTPASE-ACTIVATING PROTEIN LRG1; 1.
DR   Pfam; PF00412; LIM; 2.
DR   SMART; SM00132; LIM; 2.
DR   SUPFAM; SSF57716; Glucocorticoid receptor-like (DNA-binding domain); 4.
DR   PROSITE; PS00478; LIM_DOMAIN_1; 2.
DR   PROSITE; PS50023; LIM_DOMAIN_2; 2.
DR   Genevisible; Q16527; HS.
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
//