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Q9DCT8 (CRIP2_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 99. 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

Names and origin

Protein namesRecommended name:
Cysteine-rich protein 2

Short name=CRP-2
Alternative name(s):
Heart LIM protein
Gene names
Name:Crip2
Synonyms:Crp2, Hlp
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length208 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Subunit structure

Interacts with TGFB1I1. Ref.5

Developmental stage

In the embryo, its expression is primarily restricted to the developing heart. In situ hybridization showed expression at E7.75 in the paired heart-forming primordia prior to linear heart-tube formation. At E8.5, strong expression is detected in the heart, with equal expression in both heart chambers. Expression is detected in both myocardium and endocardium, and in vascular endothelium. Later in fetal development low levels of expression is detected outside the heart, including dorsal root ganglia and the spinal cord. In the adult, it is expressed at highest levels in the heart, and at lower levels in the brain, skeletal muscle and aorta. Ref.1

Sequence similarities

Contains 2 LIM zinc-binding domains.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 208208Cysteine-rich protein 2
PRO_0000075711

Regions

Domain5 – 5753LIM zinc-binding 1
Domain126 – 17853LIM zinc-binding 2
Compositional bias63 – 7311Gly-rich
Compositional bias180 – 19415Gly-rich

Amino acid modifications

Modified residue231N6-acetyllysine Ref.6
Modified residue1381N6-acetyllysine Ref.6
Modified residue1441N6-acetyllysine Ref.6

Sequences

Sequence LengthMass (Da)Tools
Q9DCT8 [UniParc].

Last modified June 1, 2001. Version 1.
Checksum: 9A3AEF8A8FBA1D19

FASTA20822,727
        10         20         30         40         50         60 
MASKCPKCDK TVYFAEKVSS LGKDWHKFCL KCERCNKTLT PGGHAEHDGK PFCHKPCYAT 

        70         80         90        100        110        120 
LFGPKGVNIG GAGSYIYEKP QTEAPQVTGP IEVPVVRTEE RKTSGPPKGP SKASSVTTFT 

       130        140        150        160        170        180 
GEPNMCPRCN KRVYFAEKVT SLGKDWHRPC LRCERCSKTL TPGGHAEHDG QPYCHKPCYG 

       190        200 
ILFGPKGVNT GAVGSYIYDK DPEGTVQP 

« Hide

References

« Hide 'large scale' references
[1]"The heart LIM protein gene (Hlp), expressed in the developing and adult heart, defines a new tissue-specific LIM-only protein family."
Yu T.S., Moctezuma-Anaya M., Kubo A., Keller G., Robertson S.
Mech. Dev. 116:187-192(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA], DEVELOPMENTAL STAGE.
Strain: 129/Sv.
Tissue: Heart.
[2]"The origin of a developmentally regulated Igh replicon is located near the border of regulatory domains for Igh replication and expression."
Zhou J., Ashouian N., Delepine M., Matsuda F., Chevillard C., Riblet R., Schildkraut C.L., Birshtein B.K.
Proc. Natl. Acad. Sci. U.S.A. 99:13693-13698(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: 129/Sv.
[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: Kidney.
[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].
[5]"Uni-axial stretching regulates intracellular localization of Hic-5 expressed in smooth-muscle cells in vivo."
Kim-Kaneyama J.-R., Suzuki W., Ichikawa K., Ohki T., Kohno Y., Sata M., Nose K., Shibanuma M.
J. Cell Sci. 118:937-949(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH TGFB1I1.
[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-23; LYS-138 AND LYS-144, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Embryonic fibroblast.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF469648 mRNA. Translation: AAM89218.1.
AF470625 Genomic DNA. Translation: AAM89219.1.
AF450245 Genomic DNA. Translation: AAM97586.1.
AK002484 mRNA. Translation: BAB22136.1.
BC002093 mRNA. Translation: AAH02093.1.
BC002096 mRNA. Translation: AAH02096.1.
CCDSCCDS26204.1.
RefSeqNP_077185.1. NM_024223.2.
UniGeneMm.133825.

3D structure databases

ProteinModelPortalQ9DCT8.
SMRQ9DCT8. Positions 1-63, 126-184.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

IntActQ9DCT8. 5 interactions.
MINTMINT-1863492.

PTM databases

PhosphoSiteQ9DCT8.

Proteomic databases

MaxQBQ9DCT8.
PaxDbQ9DCT8.
PRIDEQ9DCT8.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000084882; ENSMUSP00000081943; ENSMUSG00000006356.
GeneID68337.
KEGGmmu:68337.
UCSCuc007pfy.2. mouse.

Organism-specific databases

CTD1397.
MGIMGI:1915587. Crip2.

Phylogenomic databases

eggNOGNOG246818.
GeneTreeENSGT00550000074548.
HOGENOMHOG000111234.
HOVERGENHBG051143.
InParanoidQ9DCT8.
OMAIEGQTAP.
OrthoDBEOG7CK39M.
PhylomeDBQ9DCT8.
TreeFamTF313758.

Gene expression databases

ArrayExpressQ9DCT8.
BgeeQ9DCT8.
CleanExMM_CRIP2.
GenevestigatorQ9DCT8.

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

ChiTaRSCRIP2. mouse.
NextBio327013.
PROQ9DCT8.
SOURCESearch...

Entry information

Entry nameCRIP2_MOUSE
AccessionPrimary (citable) accession number: Q9DCT8
Entry history
Integrated into UniProtKB/Swiss-Prot: May 24, 2004
Last sequence update: June 1, 2001
Last modified: July 9, 2014
This is version 99 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

MGD cross-references

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