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P97315 (CSRP1_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified April 3, 2013. Version 100. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Cysteine and glycine-rich protein 1
Alternative name(s):
Cysteine-rich protein 1
Short name=CRP
Short name=CRP1
Gene names
Name:Csrp1
Synonyms:Crp1, Csrp
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

Protein attributes

Sequence length193 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Could play a role in neuronal development By similarity.

Subunit structure

Monomer By similarity.

Subcellular location

Nucleus By similarity.

Sequence similarities

Contains 2 LIM zinc-binding domains.

Ontologies

Keywords
   Cellular componentNucleus
   DomainLIM domain
Repeat
   LigandMetal-binding
Zinc
   PTMAcetylation
Phosphoprotein
   Technical termComplete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processactin cytoskeleton organization

Traceable author statement Ref.2. Source: MGI

   Cellular_componentactin cytoskeleton

Traceable author statement Ref.2. Source: MGI

nucleus

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionzinc ion binding

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 193193Cysteine and glycine-rich protein 1
PRO_0000075716

Regions

Domain10 – 6152LIM zinc-binding 1
Domain119 – 17052LIM zinc-binding 2
Motif64 – 696Nuclear localization signal Potential
Compositional bias63 – 7816Gly-rich
Compositional bias176 – 18712Gly-rich

Amino acid modifications

Modified residue1121N6-acetyllysine By similarity
Modified residue1271Phosphotyrosine Ref.6
Modified residue1311N6-acetyllysine By similarity
Modified residue1921Phosphoserine Ref.7 Ref.8

Sequences

Sequence LengthMass (Da)Tools
P97315 [UniParc].

Last modified January 23, 2007. Version 3.
Checksum: AC69703ABD68C97A

FASTA19320,583
        10         20         30         40         50         60 
MPNWGGGKKC GVCQKTVYFA EEVQCEGNSF HKSCFLCMVC KKNLDSTTVA VHGEEIYCKS 

        70         80         90        100        110        120 
CYGKKYGPKG YGYGQGAGTL STDKGESLGI KHEEAPGHRP TTNPNASKFA QKIGGSERCP 

       130        140        150        160        170        180 
RCSQAVYAAE KVIGAGKSWH KSCFRCAKCG KGLESTTLAD KDGEIYCKGC YAKNFGPKGF 

       190 
GFGQGAGALV HSE

« Hide

References

« Hide 'large scale' references
[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.
[2]"The LIM protein, CRP1, is a smooth muscle marker."
Henderson J.R., Macalma T., Brown D., Richardson J.A., Olson E.N., Beckerle M.C.
Dev. Dyn. 214:229-238(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[3]"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. expand/collapse author list , 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: Eye and Thymus.
[4]"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: Mammary tumor.
[5]Lubec G., Kang S.U.
Submitted (APR-2007) to UniProtKB
Cited for: PROTEIN SEQUENCE OF 122-131, MASS SPECTROMETRY.
Strain: C57BL/6.
Tissue: Brain.
[6]"Protein phosphorylation and expression profiling by Yin-yang multidimensional liquid chromatography (Yin-yang MDLC) mass spectrometry."
Dai J., Jin W.-H., Sheng Q.-H., Shieh C.-H., Wu J.-R., Zeng R.
J. Proteome Res. 6:250-262(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-127, MASS SPECTROMETRY.
Tissue: Liver.
[7]"Qualitative and quantitative analyses of protein phosphorylation in naive and stimulated mouse synaptosomal preparations."
Munton R.P., Tweedie-Cullen R., Livingstone-Zatchej M., Weinandy F., Waidelich M., Longo D., Gehrig P., Potthast F., Rutishauser D., Gerrits B., Panse C., Schlapbach R., Mansuy I.M.
Mol. Cell. Proteomics 6:283-293(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-192, MASS SPECTROMETRY.
Tissue: Brain cortex.
[8]"Solid tumor proteome and phosphoproteome analysis by high resolution mass spectrometry."
Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J., Faessler R., Mann M.
J. Proteome Res. 7:5314-5326(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-192, MASS SPECTROMETRY.
Tissue: Melanoma.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		D88793 mRNA. Translation: BAA13723.1.
AF092921 mRNA. Translation: AAD19352.1.
AK077787 mRNA. Translation: BAC37009.1.
AK087436 mRNA. Translation: BAC39873.1.
BC006912 mRNA. Translation: AAH06912.1.
IPIIPI00123891.
RefSeqNP_031817.1. NM_007791.5.
UniGeneMm.196484.

3D structure databases

ProteinModelPortalP97315.
SMRP97315. Positions 1-193.
ModBaseSearch...

Protein-protein interaction databases

IntActP97315. 2 interactions.

PTM databases

PhosphoSiteP97315.

Proteomic databases

PaxDbP97315.
PRIDEP97315.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000027677; ENSMUSP00000027677; ENSMUSG00000026421.
ENSMUST00000097561; ENSMUSP00000095169; ENSMUSG00000026421.
GeneID13007.
KEGGmmu:13007.

Organism-specific databases

CTD1465.
MGIMGI:88549. Csrp1.

Phylogenomic databases

eggNOGNOG281414.
HOGENOMHOG000111233.
HOVERGENHBG051143.
InParanoidP97315.
KOK09377.
OMANKCGCCQ.
OrthoDBEOG4BRWMS.

Gene expression databases

ArrayExpressP97315.
BgeeP97315.
CleanExMM_CSRP1.
GenevestigatorP97315.
GermOnlineENSMUSG00000026421. Mus musculus.

Family and domain databases

Gene3D2.10.110.10. 2 hits.
InterProIPR001781. Znf_LIM.
[Graphical view]
PfamPF00412. LIM. 2 hits.
[Graphical view]
SMARTSM00132. LIM. 2 hits.
[Graphical view]
PROSITEPS00478. LIM_DOMAIN_1. 2 hits.
PS50023. LIM_DOMAIN_2. 2 hits.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSCSRP1. mouse.
NextBio282836.
SOURCESearch...

Entry information

Entry nameCSRP1_MOUSE
AccessionPrimary (citable) accession number: P97315
Entry history
Integrated into UniProtKB/Swiss-Prot: May 24, 2004
Last sequence update: January 23, 2007
Last modified: April 3, 2013
This is version 100 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot

SIMILARITY comments

Index of protein domains and families

to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents