Full text data of CSRP1
CSRP1
(CSRP, CYRP)
[Confidence: low (only semi-automatic identification from reviews)]
Cysteine and glycine-rich protein 1 (Cysteine-rich protein 1; CRP; CRP1)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
Cysteine and glycine-rich protein 1 (Cysteine-rich protein 1; CRP; CRP1)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
UniProt
P21291
ID CSRP1_HUMAN Reviewed; 193 AA.
AC P21291;
DT 01-MAY-1991, integrated into UniProtKB/Swiss-Prot.
read moreDT 23-JAN-2007, sequence version 3.
DT 22-JAN-2014, entry version 127.
DE RecName: Full=Cysteine and glycine-rich protein 1;
DE AltName: Full=Cysteine-rich protein 1;
DE Short=CRP;
DE Short=CRP1;
GN Name=CSRP1; Synonyms=CSRP, CYRP;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Term placenta;
RX PubMed=2115670; DOI=10.1093/nar/18.13.3871;
RA Liebhaber S.A., Emery J.G., Urbanek M., Wang X., Cooke N.E.;
RT "Characterization of a human cDNA encoding a widely expressed and
RT highly conserved cysteine-rich protein with an unusual zinc-finger
RT motif.";
RL Nucleic Acids Res. 18:3871-3879(1990).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=1374386;
RA Wang X., Lee G., Liebhaber S.A., Cooke N.E.;
RT "Human cysteine-rich protein. A member of the LIM/double-finger family
RT displaying coordinate serum induction with c-myc.";
RL J. Biol. Chem. 267:9176-9184(1992).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain;
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
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-192, AND MASS
RP SPECTROMETRY.
RC TISSUE=Cervix carcinoma;
RX PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
RA Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,
RA Mann M.;
RT "Global, in vivo, and site-specific phosphorylation dynamics in
RT signaling networks.";
RL Cell 127:635-648(2006).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-192, AND MASS
RP SPECTROMETRY.
RC TISSUE=Cervix carcinoma;
RX PubMed=16964243; DOI=10.1038/nbt1240;
RA Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.;
RT "A probability-based approach for high-throughput protein
RT phosphorylation analysis and site localization.";
RL Nat. Biotechnol. 24:1285-1292(2006).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-192, AND MASS
RP SPECTROMETRY.
RC TISSUE=Cervix carcinoma;
RX PubMed=18220336; DOI=10.1021/pr0705441;
RA Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D.,
RA Yates J.R. III;
RT "Combining protein-based IMAC, peptide-based IMAC, and MudPIT for
RT efficient phosphoproteomic analysis.";
RL J. Proteome Res. 7:1346-1351(2008).
RN [7]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-192, AND MASS
RP SPECTROMETRY.
RC TISSUE=Leukemic T-cell;
RX PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA Rodionov V., Han D.K.;
RT "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT reveals system-wide modulation of protein-protein interactions.";
RL Sci. Signal. 2:RA46-RA46(2009).
RN [9]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-112 AND LYS-131, AND MASS
RP SPECTROMETRY.
RX PubMed=19608861; DOI=10.1126/science.1175371;
RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M.,
RA Walther T.C., Olsen J.V., Mann M.;
RT "Lysine acetylation targets protein complexes and co-regulates major
RT cellular functions.";
RL Science 325:834-840(2009).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-192, AND MASS
RP SPECTROMETRY.
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S.,
RA Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full
RT phosphorylation site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [11]
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.,
RA Buerckstuemmer T., 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 [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-192, AND MASS
RP SPECTROMETRY.
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J.,
RA Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V.,
RA Blagoev B.;
RT "System-wide temporal characterization of the proteome and
RT phosphoproteome of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
CC -!- FUNCTION: Could play a role in neuronal development.
CC -!- SUBUNIT: Monomer (By similarity).
CC -!- SUBCELLULAR LOCATION: Nucleus.
CC -!- SIMILARITY: Contains 2 LIM zinc-binding domains.
CC -----------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution-NoDerivs License
CC -----------------------------------------------------------------------
DR EMBL; M33146; AAA35720.1; -; mRNA.
DR EMBL; M76378; AAA58431.1; -; Genomic_DNA.
DR EMBL; M76376; AAA58431.1; JOINED; Genomic_DNA.
DR EMBL; M76377; AAA58431.1; JOINED; Genomic_DNA.
DR EMBL; BC032493; AAH32493.1; -; mRNA.
DR PIR; S12658; S12658.
DR RefSeq; NP_001180499.1; NM_001193570.1.
DR RefSeq; NP_001180500.1; NM_001193571.1.
DR RefSeq; NP_001180501.1; NM_001193572.1.
DR RefSeq; NP_004069.1; NM_004078.2.
DR UniGene; Hs.108080; -.
DR ProteinModelPortal; P21291; -.
DR SMR; P21291; 1-193.
DR IntAct; P21291; 2.
DR STRING; 9606.ENSP00000345079; -.
DR PhosphoSite; P21291; -.
DR DMDM; 118161; -.
DR OGP; P21291; -.
DR PaxDb; P21291; -.
DR PeptideAtlas; P21291; -.
DR PRIDE; P21291; -.
DR DNASU; 1465; -.
DR Ensembl; ENST00000340006; ENSP00000345079; ENSG00000159176.
DR Ensembl; ENST00000367306; ENSP00000356275; ENSG00000159176.
DR Ensembl; ENST00000532460; ENSP00000434147; ENSG00000159176.
DR Ensembl; ENST00000533432; ENSP00000436792; ENSG00000159176.
DR GeneID; 1465; -.
DR KEGG; hsa:1465; -.
DR UCSC; uc001gws.3; human.
DR CTD; 1465; -.
DR GeneCards; GC01M201452; -.
DR HGNC; HGNC:2469; CSRP1.
DR MIM; 123876; gene.
DR neXtProt; NX_P21291; -.
DR PharmGKB; PA26967; -.
DR eggNOG; NOG281414; -.
DR HOGENOM; HOG000111233; -.
DR HOVERGEN; HBG051143; -.
DR InParanoid; P21291; -.
DR KO; K09377; -.
DR OMA; RCPRCTQ; -.
DR OrthoDB; EOG7CK39M; -.
DR PhylomeDB; P21291; -.
DR GeneWiki; CSRP1; -.
DR GenomeRNAi; 1465; -.
DR NextBio; 6017; -.
DR PRO; PR:P21291; -.
DR ArrayExpress; P21291; -.
DR Bgee; P21291; -.
DR CleanEx; HS_CSRP1; -.
DR Genevestigator; P21291; -.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0008270; F:zinc ion binding; TAS:ProtInc.
DR Gene3D; 2.10.110.10; -; 2.
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; Complete proteome; LIM domain; Metal-binding; Nucleus;
KW Phosphoprotein; Polymorphism; Reference proteome; Repeat; Zinc.
FT CHAIN 1 193 Cysteine and glycine-rich protein 1.
FT /FTId=PRO_0000075715.
FT DOMAIN 10 61 LIM zinc-binding 1.
FT DOMAIN 119 170 LIM zinc-binding 2.
FT MOTIF 64 69 Nuclear localization signal (Potential).
FT COMPBIAS 63 78 Gly-rich.
FT COMPBIAS 176 187 Gly-rich.
FT MOD_RES 112 112 N6-acetyllysine.
FT MOD_RES 131 131 N6-acetyllysine.
FT MOD_RES 192 192 Phosphoserine.
FT VARIANT 108 108 K -> I (in dbSNP:rs3738283).
FT /FTId=VAR_050144.
SQ SEQUENCE 193 AA; 20567 MW; AC6970255D68D69A CRC64;
MPNWGGGKKC GVCQKTVYFA EEVQCEGNSF HKSCFLCMVC KKNLDSTTVA VHGEEIYCKS
CYGKKYGPKG YGYGQGAGTL STDKGESLGI KHEEAPGHRP TTNPNASKFA QKIGGSERCP
RCSQAVYAAE KVIGAGKSWH KACFRCAKCG KGLESTTLAD KDGEIYCKGC YAKNFGPKGF
GFGQGAGALV HSE
//
ID CSRP1_HUMAN Reviewed; 193 AA.
AC P21291;
DT 01-MAY-1991, integrated into UniProtKB/Swiss-Prot.
read moreDT 23-JAN-2007, sequence version 3.
DT 22-JAN-2014, entry version 127.
DE RecName: Full=Cysteine and glycine-rich protein 1;
DE AltName: Full=Cysteine-rich protein 1;
DE Short=CRP;
DE Short=CRP1;
GN Name=CSRP1; Synonyms=CSRP, CYRP;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Term placenta;
RX PubMed=2115670; DOI=10.1093/nar/18.13.3871;
RA Liebhaber S.A., Emery J.G., Urbanek M., Wang X., Cooke N.E.;
RT "Characterization of a human cDNA encoding a widely expressed and
RT highly conserved cysteine-rich protein with an unusual zinc-finger
RT motif.";
RL Nucleic Acids Res. 18:3871-3879(1990).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=1374386;
RA Wang X., Lee G., Liebhaber S.A., Cooke N.E.;
RT "Human cysteine-rich protein. A member of the LIM/double-finger family
RT displaying coordinate serum induction with c-myc.";
RL J. Biol. Chem. 267:9176-9184(1992).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain;
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
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-192, AND MASS
RP SPECTROMETRY.
RC TISSUE=Cervix carcinoma;
RX PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
RA Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,
RA Mann M.;
RT "Global, in vivo, and site-specific phosphorylation dynamics in
RT signaling networks.";
RL Cell 127:635-648(2006).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-192, AND MASS
RP SPECTROMETRY.
RC TISSUE=Cervix carcinoma;
RX PubMed=16964243; DOI=10.1038/nbt1240;
RA Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.;
RT "A probability-based approach for high-throughput protein
RT phosphorylation analysis and site localization.";
RL Nat. Biotechnol. 24:1285-1292(2006).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-192, AND MASS
RP SPECTROMETRY.
RC TISSUE=Cervix carcinoma;
RX PubMed=18220336; DOI=10.1021/pr0705441;
RA Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D.,
RA Yates J.R. III;
RT "Combining protein-based IMAC, peptide-based IMAC, and MudPIT for
RT efficient phosphoproteomic analysis.";
RL J. Proteome Res. 7:1346-1351(2008).
RN [7]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-192, AND MASS
RP SPECTROMETRY.
RC TISSUE=Leukemic T-cell;
RX PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA Rodionov V., Han D.K.;
RT "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT reveals system-wide modulation of protein-protein interactions.";
RL Sci. Signal. 2:RA46-RA46(2009).
RN [9]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-112 AND LYS-131, AND MASS
RP SPECTROMETRY.
RX PubMed=19608861; DOI=10.1126/science.1175371;
RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M.,
RA Walther T.C., Olsen J.V., Mann M.;
RT "Lysine acetylation targets protein complexes and co-regulates major
RT cellular functions.";
RL Science 325:834-840(2009).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-192, AND MASS
RP SPECTROMETRY.
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S.,
RA Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full
RT phosphorylation site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [11]
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.,
RA Buerckstuemmer T., 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 [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-192, AND MASS
RP SPECTROMETRY.
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J.,
RA Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V.,
RA Blagoev B.;
RT "System-wide temporal characterization of the proteome and
RT phosphoproteome of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
CC -!- FUNCTION: Could play a role in neuronal development.
CC -!- SUBUNIT: Monomer (By similarity).
CC -!- SUBCELLULAR LOCATION: Nucleus.
CC -!- SIMILARITY: Contains 2 LIM zinc-binding domains.
CC -----------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution-NoDerivs License
CC -----------------------------------------------------------------------
DR EMBL; M33146; AAA35720.1; -; mRNA.
DR EMBL; M76378; AAA58431.1; -; Genomic_DNA.
DR EMBL; M76376; AAA58431.1; JOINED; Genomic_DNA.
DR EMBL; M76377; AAA58431.1; JOINED; Genomic_DNA.
DR EMBL; BC032493; AAH32493.1; -; mRNA.
DR PIR; S12658; S12658.
DR RefSeq; NP_001180499.1; NM_001193570.1.
DR RefSeq; NP_001180500.1; NM_001193571.1.
DR RefSeq; NP_001180501.1; NM_001193572.1.
DR RefSeq; NP_004069.1; NM_004078.2.
DR UniGene; Hs.108080; -.
DR ProteinModelPortal; P21291; -.
DR SMR; P21291; 1-193.
DR IntAct; P21291; 2.
DR STRING; 9606.ENSP00000345079; -.
DR PhosphoSite; P21291; -.
DR DMDM; 118161; -.
DR OGP; P21291; -.
DR PaxDb; P21291; -.
DR PeptideAtlas; P21291; -.
DR PRIDE; P21291; -.
DR DNASU; 1465; -.
DR Ensembl; ENST00000340006; ENSP00000345079; ENSG00000159176.
DR Ensembl; ENST00000367306; ENSP00000356275; ENSG00000159176.
DR Ensembl; ENST00000532460; ENSP00000434147; ENSG00000159176.
DR Ensembl; ENST00000533432; ENSP00000436792; ENSG00000159176.
DR GeneID; 1465; -.
DR KEGG; hsa:1465; -.
DR UCSC; uc001gws.3; human.
DR CTD; 1465; -.
DR GeneCards; GC01M201452; -.
DR HGNC; HGNC:2469; CSRP1.
DR MIM; 123876; gene.
DR neXtProt; NX_P21291; -.
DR PharmGKB; PA26967; -.
DR eggNOG; NOG281414; -.
DR HOGENOM; HOG000111233; -.
DR HOVERGEN; HBG051143; -.
DR InParanoid; P21291; -.
DR KO; K09377; -.
DR OMA; RCPRCTQ; -.
DR OrthoDB; EOG7CK39M; -.
DR PhylomeDB; P21291; -.
DR GeneWiki; CSRP1; -.
DR GenomeRNAi; 1465; -.
DR NextBio; 6017; -.
DR PRO; PR:P21291; -.
DR ArrayExpress; P21291; -.
DR Bgee; P21291; -.
DR CleanEx; HS_CSRP1; -.
DR Genevestigator; P21291; -.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0008270; F:zinc ion binding; TAS:ProtInc.
DR Gene3D; 2.10.110.10; -; 2.
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; Complete proteome; LIM domain; Metal-binding; Nucleus;
KW Phosphoprotein; Polymorphism; Reference proteome; Repeat; Zinc.
FT CHAIN 1 193 Cysteine and glycine-rich protein 1.
FT /FTId=PRO_0000075715.
FT DOMAIN 10 61 LIM zinc-binding 1.
FT DOMAIN 119 170 LIM zinc-binding 2.
FT MOTIF 64 69 Nuclear localization signal (Potential).
FT COMPBIAS 63 78 Gly-rich.
FT COMPBIAS 176 187 Gly-rich.
FT MOD_RES 112 112 N6-acetyllysine.
FT MOD_RES 131 131 N6-acetyllysine.
FT MOD_RES 192 192 Phosphoserine.
FT VARIANT 108 108 K -> I (in dbSNP:rs3738283).
FT /FTId=VAR_050144.
SQ SEQUENCE 193 AA; 20567 MW; AC6970255D68D69A CRC64;
MPNWGGGKKC GVCQKTVYFA EEVQCEGNSF HKSCFLCMVC KKNLDSTTVA VHGEEIYCKS
CYGKKYGPKG YGYGQGAGTL STDKGESLGI KHEEAPGHRP TTNPNASKFA QKIGGSERCP
RCSQAVYAAE KVIGAGKSWH KACFRCAKCG KGLESTTLAD KDGEIYCKGC YAKNFGPKGF
GFGQGAGALV HSE
//
MIM
123876
*RECORD*
*FIELD* NO
123876
*FIELD* TI
*123876 CYSTEINE- AND GLYCINE-RICH PROTEIN 1; CSRP1
;;CYSTEINE-RICH PROTEIN 1; CRP1;;
read moreCYSTEINE-RICH PROTEIN; CSRP; CRP
*FIELD* TX
DESCRIPTION
The human gene encoding cysteine-rich protein (CSRP) is a highly
conserved, cell cycle-regulated gene that is induced in the immediate
early response to serum repletion in serum-starved, noncycling cells.
The LIM/double zinc finger motif found in cysteine-rich protein is found
in an expanding group of proteins with critical functions in gene
regulation, cell growth, and somatic differentiation (summary by Wang et
al., 1992).
CLONING
By screening a human placenta cDNA library with a human prolactin (PRL;
176760) cDNA, Liebhaber et al. (1990) isolated cDNAs encoding CRP. The
deduced 193-amino acid protein has 2 repeats of a domain that consists
of 2 putative zinc fingers immediately followed by a glycine-rich motif
containing a high proportion of aromatic and basic residues. CRP does
not share regions of significant structural similarity with PRL.
Northern blot and RT-PCR analyses detected CRP expression in all human
nucleated tissues and cell lines examined; CRP is expressed as a 1.8-kb
transcript.
Wang et al. (1992) cloned the human CRP genomic sequence. They showed
that CRP is a primary response gene in both human fibroblasts and mouse
Balb/c 3T3 cells; in the mouse cells, the kinetic profile of its
induction closely paralleled that of c-myc (190080).
GENE STRUCTURE
Wang et al. (1992) determined that the CRP gene contains 6 exons, with a
10.4-kb first intron, and spans approximately 23.2 kb from the cap site
to the polyadenylation site.
GENE FAMILY
Other members of the LIM/double zinc finger group include cysteine-rich
intestinal protein (CRIP; 123875), CSRP2 (601871), CSRP3 (600824), and
the rhombotin genes RBTN1 (186921), RBTN2 (180385), and RBTN3 (180386).
Weiskirchen et al. (1995) described the CRP family of LIM domain
proteins.
MAPPING
Using a panel of human/rodent somatic cell hybrids, Wang et al. (1992)
assigned the CSRP gene to chromosome 1. By in situ hybridization of
(3)H-labeled cDNA, they regionalized the gene to 1q24-q32. A common MspI
polymorphism was found and mapped to intron 4 of the CSRP gene. By FISH,
Erdel and Weiskirchen (1998) mapped the CSRP1 to 1q32.
Alli and Consalez (1998) mapped the Csrp gene to mouse chromosome 3 by
haplotype and linkage analysis of progeny from an interspecific
backcross panel.
*FIELD* RF
1. Alli, C.; Consalez, G. G.: Linkage mapping of Csrp to proximal
mouse chromosome 3. Mammalian Genome 9: 172 only, 1998.
2. Erdel, M.; Weiskirchen, R.: Assignment of CSRP1 encoding the LIM
domain protein CRP1, to human chromosome 1q32 by fluorescence in situ
hybridization. Cytogenet. Cell Genet. 83: 10-11, 1998.
3. Liebhaber, S. A.; Emery, J. G.; Urbanek, M.; Wang, X.; Cooke, N.
E.: Characterization of a human cDNA encoding a widely expressed
and highly conserved cysteine-rich protein with an unusual zinc-finger
motif. Nucleic Acids Res. 18: 3871-3879, 1990.
4. Wang, X.; Lee, G.; Liebhaber, S. A.; Cooke, N. E.: Human cysteine-rich
protein: a member of the LIM/double-finger family displaying coordinate
serum induction with c-myc. J. Biol. Chem. 267: 9176-9184, 1992.
5. Wang, X.; Ray, K.; Szpirer, J.; Levan, G.; Liebhaber, S. A.; Cooke,
N. E.: Analysis of the human cysteine-rich protein gene (CSRP), assignment
to chromosome 1q24-1q32, and identification of an associated MspI
polymorphism. Genomics 14: 391-397, 1992.
6. Weiskirchen, R.; Pino, J. D.; Macalma, T.; Bister, K.; Beckerle,
M. C.: The cysteine-rich protein family of highly related LIM domain
proteins. J. Biol. Chem. 270: 28946-28954, 1995.
*FIELD* CN
Carol A. Bocchini - updated: 4/23/1999
Patti M. Sherman - updated: 12/16/1998
*FIELD* CD
Victor A. McKusick: 10/14/1992
*FIELD* ED
alopez: 09/20/2012
carol: 5/19/2004
terry: 12/2/1999
terry: 4/26/1999
carol: 4/23/1999
carol: 12/21/1998
psherman: 12/16/1998
psherman: 12/15/1998
carol: 8/17/1998
carol: 4/10/1998
dholmes: 3/30/1998
carol: 10/14/1992
*RECORD*
*FIELD* NO
123876
*FIELD* TI
*123876 CYSTEINE- AND GLYCINE-RICH PROTEIN 1; CSRP1
;;CYSTEINE-RICH PROTEIN 1; CRP1;;
read moreCYSTEINE-RICH PROTEIN; CSRP; CRP
*FIELD* TX
DESCRIPTION
The human gene encoding cysteine-rich protein (CSRP) is a highly
conserved, cell cycle-regulated gene that is induced in the immediate
early response to serum repletion in serum-starved, noncycling cells.
The LIM/double zinc finger motif found in cysteine-rich protein is found
in an expanding group of proteins with critical functions in gene
regulation, cell growth, and somatic differentiation (summary by Wang et
al., 1992).
CLONING
By screening a human placenta cDNA library with a human prolactin (PRL;
176760) cDNA, Liebhaber et al. (1990) isolated cDNAs encoding CRP. The
deduced 193-amino acid protein has 2 repeats of a domain that consists
of 2 putative zinc fingers immediately followed by a glycine-rich motif
containing a high proportion of aromatic and basic residues. CRP does
not share regions of significant structural similarity with PRL.
Northern blot and RT-PCR analyses detected CRP expression in all human
nucleated tissues and cell lines examined; CRP is expressed as a 1.8-kb
transcript.
Wang et al. (1992) cloned the human CRP genomic sequence. They showed
that CRP is a primary response gene in both human fibroblasts and mouse
Balb/c 3T3 cells; in the mouse cells, the kinetic profile of its
induction closely paralleled that of c-myc (190080).
GENE STRUCTURE
Wang et al. (1992) determined that the CRP gene contains 6 exons, with a
10.4-kb first intron, and spans approximately 23.2 kb from the cap site
to the polyadenylation site.
GENE FAMILY
Other members of the LIM/double zinc finger group include cysteine-rich
intestinal protein (CRIP; 123875), CSRP2 (601871), CSRP3 (600824), and
the rhombotin genes RBTN1 (186921), RBTN2 (180385), and RBTN3 (180386).
Weiskirchen et al. (1995) described the CRP family of LIM domain
proteins.
MAPPING
Using a panel of human/rodent somatic cell hybrids, Wang et al. (1992)
assigned the CSRP gene to chromosome 1. By in situ hybridization of
(3)H-labeled cDNA, they regionalized the gene to 1q24-q32. A common MspI
polymorphism was found and mapped to intron 4 of the CSRP gene. By FISH,
Erdel and Weiskirchen (1998) mapped the CSRP1 to 1q32.
Alli and Consalez (1998) mapped the Csrp gene to mouse chromosome 3 by
haplotype and linkage analysis of progeny from an interspecific
backcross panel.
*FIELD* RF
1. Alli, C.; Consalez, G. G.: Linkage mapping of Csrp to proximal
mouse chromosome 3. Mammalian Genome 9: 172 only, 1998.
2. Erdel, M.; Weiskirchen, R.: Assignment of CSRP1 encoding the LIM
domain protein CRP1, to human chromosome 1q32 by fluorescence in situ
hybridization. Cytogenet. Cell Genet. 83: 10-11, 1998.
3. Liebhaber, S. A.; Emery, J. G.; Urbanek, M.; Wang, X.; Cooke, N.
E.: Characterization of a human cDNA encoding a widely expressed
and highly conserved cysteine-rich protein with an unusual zinc-finger
motif. Nucleic Acids Res. 18: 3871-3879, 1990.
4. Wang, X.; Lee, G.; Liebhaber, S. A.; Cooke, N. E.: Human cysteine-rich
protein: a member of the LIM/double-finger family displaying coordinate
serum induction with c-myc. J. Biol. Chem. 267: 9176-9184, 1992.
5. Wang, X.; Ray, K.; Szpirer, J.; Levan, G.; Liebhaber, S. A.; Cooke,
N. E.: Analysis of the human cysteine-rich protein gene (CSRP), assignment
to chromosome 1q24-1q32, and identification of an associated MspI
polymorphism. Genomics 14: 391-397, 1992.
6. Weiskirchen, R.; Pino, J. D.; Macalma, T.; Bister, K.; Beckerle,
M. C.: The cysteine-rich protein family of highly related LIM domain
proteins. J. Biol. Chem. 270: 28946-28954, 1995.
*FIELD* CN
Carol A. Bocchini - updated: 4/23/1999
Patti M. Sherman - updated: 12/16/1998
*FIELD* CD
Victor A. McKusick: 10/14/1992
*FIELD* ED
alopez: 09/20/2012
carol: 5/19/2004
terry: 12/2/1999
terry: 4/26/1999
carol: 4/23/1999
carol: 12/21/1998
psherman: 12/16/1998
psherman: 12/15/1998
carol: 8/17/1998
carol: 4/10/1998
dholmes: 3/30/1998
carol: 10/14/1992