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Protein

Cysteine and glycine-rich protein 2

Gene

Csrp2

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

Functioni

Drastically down-regulated in response to PDGF-BB or cell injury, that promote smooth muscle cell proliferation and dedifferentiation. Seems to play a role in the development of the embryonic vascular system (By similarity).By similarity

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Developmental protein

Keywords - Biological processi

Differentiation

Keywords - Ligandi

Metal-binding, Zinc

Names & Taxonomyi

Protein namesi
Recommended name:
Cysteine and glycine-rich protein 2
Alternative name(s):
Cysteine-rich protein 2
Short name:
CRP2
Double LIM protein 1
Short name:
DLP-1
Gene namesi
Name:Csrp2
Synonyms:Dlp1
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 10

Organism-specific databases

MGIiMGI:1202907. Csrp2.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 193193Cysteine and glycine-rich protein 2PRO_0000075722Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei112 – 1121N6-acetyllysineCombined sources
Modified residuei137 – 1371N6-succinyllysineCombined sources

Keywords - PTMi

Acetylation

Proteomic databases

EPDiP97314.
MaxQBiP97314.
PaxDbiP97314.
PRIDEiP97314.

PTM databases

iPTMnetiP97314.
PhosphoSiteiP97314.

Expressioni

Gene expression databases

BgeeiP97314.
CleanExiMM_CSRP2.
GenevisibleiP97314. MM.

Interactioni

Subunit structurei

Interacts with CSRP2BP. The LIM domain 1 is necessary and sufficient for this interaction (By similarity). Interacts with GLRX3.By similarity1 Publication

Protein-protein interaction databases

BioGridi198953. 1 interaction.
IntActiP97314. 2 interactions.
MINTiMINT-4092329.
STRINGi10090.ENSMUSP00000020403.

Structurei

3D structure databases

ProteinModelPortaliP97314.
SMRiP97314. Positions 1-193.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini10 – 6152LIM zinc-binding 1PROSITE-ProRule annotationAdd
BLAST
Domaini119 – 17052LIM zinc-binding 2PROSITE-ProRule annotationAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi64 – 696Nuclear localization signalSequence analysis

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi63 – 7816Gly-richAdd
BLAST
Compositional biasi176 – 18712Gly-richAdd
BLAST

Sequence similaritiesi

Contains 2 LIM zinc-binding domains.PROSITE-ProRule annotation

Keywords - Domaini

LIM domain, Repeat

Phylogenomic databases

eggNOGiENOG410ITI2. Eukaryota.
ENOG4111F44. LUCA.
GeneTreeiENSGT00550000074548.
HOGENOMiHOG000111233.
HOVERGENiHBG051143.
InParanoidiP97314.
KOiK09377.
OMAiHERRFSC.
OrthoDBiEOG7CK39M.
PhylomeDBiP97314.
TreeFamiTF313758.

Family and domain databases

Gene3Di2.10.110.10. 2 hits.
InterProiIPR001781. Znf_LIM.
[Graphical view]
PfamiPF00412. LIM. 2 hits.
[Graphical view]
SMARTiSM00132. LIM. 2 hits.
[Graphical view]
PROSITEiPS00478. LIM_DOMAIN_1. 2 hits.
PS50023. LIM_DOMAIN_2. 2 hits.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P97314-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MPVWGGGNKC GACGRTVYHA EEVQCDGRSF HRCCFLCMVC RKNLDSTTVA
60 70 80 90 100
IHDEEIYCKS CYGKKYGPKG YGYGQGAGTL NMDRGERLGI KPESAQPHRP
110 120 130 140 150
TTNPNTSKFA QKYGGAEKCS RCGDSVYAAE KIIGAGKPWH KNCFRCAKCG
160 170 180 190
KSLESTTLTE KEGEIYCKGC YAKNFGPKGF GYGQGAGALV HAQ
Length:193
Mass (Da):20,926
Last modified:January 23, 2007 - v3
Checksum:iBF792F284C9597E9
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti30 – 301F → Y in BAB28379 (Ref. 1) Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D88792 mRNA. Translation: BAA13722.1.
AK010626 mRNA. Translation: BAB27072.1.
AK012647 mRNA. Translation: BAB28379.1.
BC012663 mRNA. Translation: AAH12663.1.
CCDSiCCDS24165.1.
RefSeqiNP_031818.3. NM_007792.4.
UniGeneiMm.2020.

Genome annotation databases

EnsembliENSMUST00000020403; ENSMUSP00000020403; ENSMUSG00000020186.
GeneIDi13008.
KEGGimmu:13008.
UCSCiuc007gzs.2. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D88792 mRNA. Translation: BAA13722.1.
AK010626 mRNA. Translation: BAB27072.1.
AK012647 mRNA. Translation: BAB28379.1.
BC012663 mRNA. Translation: AAH12663.1.
CCDSiCCDS24165.1.
RefSeqiNP_031818.3. NM_007792.4.
UniGeneiMm.2020.

3D structure databases

ProteinModelPortaliP97314.
SMRiP97314. Positions 1-193.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi198953. 1 interaction.
IntActiP97314. 2 interactions.
MINTiMINT-4092329.
STRINGi10090.ENSMUSP00000020403.

PTM databases

iPTMnetiP97314.
PhosphoSiteiP97314.

Proteomic databases

EPDiP97314.
MaxQBiP97314.
PaxDbiP97314.
PRIDEiP97314.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000020403; ENSMUSP00000020403; ENSMUSG00000020186.
GeneIDi13008.
KEGGimmu:13008.
UCSCiuc007gzs.2. mouse.

Organism-specific databases

CTDi1466.
MGIiMGI:1202907. Csrp2.

Phylogenomic databases

eggNOGiENOG410ITI2. Eukaryota.
ENOG4111F44. LUCA.
GeneTreeiENSGT00550000074548.
HOGENOMiHOG000111233.
HOVERGENiHBG051143.
InParanoidiP97314.
KOiK09377.
OMAiHERRFSC.
OrthoDBiEOG7CK39M.
PhylomeDBiP97314.
TreeFamiTF313758.

Miscellaneous databases

NextBioi282840.
PROiP97314.
SOURCEiSearch...

Gene expression databases

BgeeiP97314.
CleanExiMM_CSRP2.
GenevisibleiP97314. MM.

Family and domain databases

Gene3Di2.10.110.10. 2 hits.
InterProiIPR001781. Znf_LIM.
[Graphical view]
PfamiPF00412. LIM. 2 hits.
[Graphical view]
SMARTiSM00132. LIM. 2 hits.
[Graphical view]
PROSITEiPS00478. LIM_DOMAIN_1. 2 hits.
PS50023. LIM_DOMAIN_2. 2 hits.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Differential expression of three double LIM proteins during the skeletal muscle terminal differentiation."
    Hashimoto N., Ogashiwa M.
    Submitted (NOV-1996) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Strain: C3H/HeJ.
  2. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: C57BL/6J.
    Tissue: Embryo and Embryonic stem cell.
  3. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Liver.
  4. "PICOT attenuates cardiac hypertrophy by disrupting calcineurin-NFAT signaling."
    Jeong D., Kim J.M., Cha H., Oh J.G., Park J., Yun S.H., Ju E.S., Jeon E.S., Hajjar R.J., Park W.J.
    Circ. Res. 102:711-719(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH GLRX3.
  5. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Kidney, Liver, Lung, Pancreas and Spleen.
  6. "SIRT5-mediated lysine desuccinylation impacts diverse metabolic pathways."
    Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y., Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.
    Mol. Cell 50:919-930(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-112, SUCCINYLATION [LARGE SCALE ANALYSIS] AT LYS-137, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Embryonic fibroblast.

Entry informationi

Entry nameiCSRP2_MOUSE
AccessioniPrimary (citable) accession number: P97314
Secondary accession number(s): Q9CZG5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 24, 2004
Last sequence update: January 23, 2007
Last modified: May 11, 2016
This is version 122 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.