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Protein

Cysteine and glycine-rich protein 1

Gene

Csrp1

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

Functioni

Could play a role in neuronal development.By similarity

GO - Molecular functioni

GO - Biological processi

  • actin cytoskeleton organization Source: MGI
  • platelet aggregation Source: MGI
Complete GO annotation...

Keywords - Ligandi

Metal-binding, Zinc

Names & Taxonomyi

Protein namesi
Recommended name:
Cysteine and glycine-rich protein 1
Alternative name(s):
Cysteine-rich protein 1
Short name:
CRP
Short name:
CRP1
Gene namesi
Name:Csrp1
Synonyms:Crp1, Csrp
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 1

Organism-specific databases

MGIiMGI:88549. Csrp1.

Subcellular locationi

GO - Cellular componenti

  • actin cytoskeleton Source: MGI
  • extracellular exosome Source: MGI
  • focal adhesion Source: MGI
  • nucleus Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 193193Cysteine and glycine-rich protein 1PRO_0000075716Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei81 – 811PhosphoserineBy similarity
Modified residuei84 – 841N6-acetyllysineCombined sources
Modified residuei112 – 1121N6-acetyllysineCombined sources
Modified residuei131 – 1311N6-acetyllysineCombined sources
Modified residuei137 – 1371N6-acetyllysineCombined sources
Modified residuei161 – 1611N6-acetyllysineCombined sources
Modified residuei192 – 1921PhosphoserineCombined sources

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

EPDiP97315.
PaxDbiP97315.
PRIDEiP97315.

PTM databases

iPTMnetiP97315.
PhosphoSiteiP97315.
SwissPalmiP97315.

Expressioni

Gene expression databases

BgeeiP97315.
CleanExiMM_CSRP1.
ExpressionAtlasiP97315. baseline and differential.
GenevisibleiP97315. MM.

Interactioni

Subunit structurei

Monomer.By similarity

Protein-protein interaction databases

BioGridi198952. 3 interactions.
IntActiP97315. 4 interactions.
MINTiMINT-4092312.
STRINGi10090.ENSMUSP00000027677.

Structurei

3D structure databases

ProteinModelPortaliP97315.
SMRiP97315. 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

eggNOGiENOG410ITI1. Eukaryota.
ENOG4111F3Y. LUCA.
HOGENOMiHOG000111233.
HOVERGENiHBG051143.
InParanoidiP97315.
KOiK09377.
OMAiRCPRCTQ.
OrthoDBiEOG7CK39M.
PhylomeDBiP97315.
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.

P97315-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MPNWGGGKKC GVCQKTVYFA EEVQCEGNSF HKSCFLCMVC KKNLDSTTVA
60 70 80 90 100
VHGEEIYCKS CYGKKYGPKG YGYGQGAGTL STDKGESLGI KHEEAPGHRP
110 120 130 140 150
TTNPNASKFA QKIGGSERCP RCSQAVYAAE KVIGAGKSWH KSCFRCAKCG
160 170 180 190
KGLESTTLAD KDGEIYCKGC YAKNFGPKGF GFGQGAGALV HSE
Length:193
Mass (Da):20,583
Last modified:January 23, 2007 - v3
Checksum:iAC69703ABD68C97A
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS15320.1.
RefSeqiNP_031817.1. NM_007791.5.
UniGeneiMm.196484.

Genome annotation databases

EnsembliENSMUST00000027677; ENSMUSP00000027677; ENSMUSG00000026421.
ENSMUST00000097561; ENSMUSP00000095169; ENSMUSG00000026421.
GeneIDi13007.
KEGGimmu:13007.
UCSCiuc007cto.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS15320.1.
RefSeqiNP_031817.1. NM_007791.5.
UniGeneiMm.196484.

3D structure databases

ProteinModelPortaliP97315.
SMRiP97315. Positions 1-193.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi198952. 3 interactions.
IntActiP97315. 4 interactions.
MINTiMINT-4092312.
STRINGi10090.ENSMUSP00000027677.

PTM databases

iPTMnetiP97315.
PhosphoSiteiP97315.
SwissPalmiP97315.

Proteomic databases

EPDiP97315.
PaxDbiP97315.
PRIDEiP97315.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000027677; ENSMUSP00000027677; ENSMUSG00000026421.
ENSMUST00000097561; ENSMUSP00000095169; ENSMUSG00000026421.
GeneIDi13007.
KEGGimmu:13007.
UCSCiuc007cto.1. mouse.

Organism-specific databases

CTDi1465.
MGIiMGI:88549. Csrp1.

Phylogenomic databases

eggNOGiENOG410ITI1. Eukaryota.
ENOG4111F3Y. LUCA.
HOGENOMiHOG000111233.
HOVERGENiHBG051143.
InParanoidiP97315.
KOiK09377.
OMAiRCPRCTQ.
OrthoDBiEOG7CK39M.
PhylomeDBiP97315.
TreeFamiTF313758.

Miscellaneous databases

ChiTaRSiCsrp1. mouse.
NextBioi282836.
PROiP97315.
SOURCEiSearch...

Gene expression databases

BgeeiP97315.
CleanExiMM_CSRP1.
ExpressionAtlasiP97315. baseline and differential.
GenevisibleiP97315. 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. 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.
    , 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, IDENTIFICATION BY MASS SPECTROMETRY.
    Strain: C57BL/6J.
    Tissue: Brain.
  6. "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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Brain cortex.
  7. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-192, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas, Spleen and Testis.
  8. "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-84; LYS-112; LYS-131; LYS-137 AND LYS-161, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Embryonic fibroblast.

Entry informationi

Entry nameiCSRP1_MOUSE
AccessioniPrimary (citable) accession number: P97315
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 24, 2004
Last sequence update: January 23, 2007
Last modified: March 16, 2016
This is version 127 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, Direct protein sequencing, 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.