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Protein

Cold-inducible RNA-binding protein

Gene

Cirbp

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

Functioni

Cold-inducible mRNA binding protein that plays a protective role in the genotoxic stress response by stabilizing transcripts of genes involved in cell survival. Promotes assembly of stress granules (SGs), when overexpressed. Seems to play an essential role in cold-induced suppression of cell proliferation. Acts as a translational repressor. Acts as a translational activator. Binds specifically to the 3'-untranslated regions (3'-UTRs) of stress-responsive transcripts RPA2 and TXN.2 Publications

GO - Molecular functioni

GO - Biological processi

  • mRNA stabilization Source: UniProtKB
  • negative regulation of translation Source: GOC
  • positive regulation of translation Source: UniProtKB
  • response to cold Source: Ensembl
  • response to UV Source: UniProtKB
  • stress granule assembly Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Activator, Repressor

Keywords - Biological processi

Stress response

Keywords - Ligandi

RNA-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Cold-inducible RNA-binding protein
Alternative name(s):
A18 hnRNP
Glycine-rich RNA-binding protein CIRP
Gene namesi
Name:Cirbp
Synonyms:Cirp
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 10

Organism-specific databases

MGIiMGI:893588. Cirbp.

Subcellular locationi

  • Nucleusnucleoplasm 1 Publication
  • Cytoplasm 1 Publication

  • Note: Translocates from the nucleus to the cytoplasm after exposure to UV radiation (By similarity). Translocates from the nucleus to the cytoplasm into stress granules upon various cytoplasmic stresses, such as osmotic and heat shocks. Its recruitment into stress granules occurs in the absence of TIAR proteins.By similarity

GO - Cellular componenti

  • cytoplasm Source: UniProtKB
  • cytoplasmic stress granule Source: UniProtKB
  • nucleolus Source: MGI
  • nucleoplasm Source: UniProtKB-SubCell
  • nucleus Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi91 – 911R → K: Inhibits translational repression. 1 Publication
Mutagenesisi94 – 941R → K: Inhibits stress granules localization and translational repression. 1 Publication
Mutagenesisi101 – 1011R → K: Inhibits translational repression. 1 Publication
Mutagenesisi105 – 1051R → K: Inhibits stress granules localization and translational repression. 1 Publication
Mutagenesisi108 – 1081R → K: Inhibits translational repression. 1 Publication
Mutagenesisi110 – 1101R → K: Inhibits translational repression. 1 Publication
Mutagenesisi112 – 1121R → K: Inhibits translational repression. 1 Publication
Mutagenesisi116 – 1161R → K: Inhibits stress granules localization and translational repression. 1 Publication
Mutagenesisi121 – 1211R → K: Inhibits translational repression. 1 Publication
Mutagenesisi127 – 1271R → K: Inhibits translational repression. 1 Publication
Mutagenesisi131 – 1311R → K: Inhibits translational repression. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 172172Cold-inducible RNA-binding proteinPRO_0000081504Add
BLAST

Post-translational modificationi

Methylated on arginine residues. Methylation of the RGG motifs is a prerequisite for recruitment into SGs.1 Publication
Phosphorylated by CK2, GSK3A and GSK3B. Phosphorylation by GSK3B increases RNA-binding activity to the TXN 3'-UTR transcript upon exposure to UV radiation (By similarity).By similarity

Keywords - PTMi

Methylation

Proteomic databases

EPDiP60824.
MaxQBiP60824.
PaxDbiP60824.
PRIDEiP60824.

PTM databases

iPTMnetiP60824.
PhosphoSiteiP60824.

Expressioni

Tissue specificityi

Ubiquitous.

Inductioni

Up-regulated upon mild cold-shock and hypoxia.1 Publication

Gene expression databases

BgeeiP60824.
CleanExiMM_CIRBP.
ExpressionAtlasiP60824. baseline and differential.
GenevisibleiP60824. MM.

Interactioni

Subunit structurei

Interacts with EIF4G1. Associates with ribosomes (By similarity).By similarity

Protein-protein interaction databases

IntActiP60824. 2 interactions.
MINTiMINT-4090864.
STRINGi10090.ENSMUSP00000101004.

Structurei

3D structure databases

ProteinModelPortaliP60824.
SMRiP60824. Positions 1-90.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini6 – 8479RRMPROSITE-ProRule annotationAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi92 – 15867Gly-richAdd
BLAST

Domaini

Both the RRM domain and the arginine, glycine (RGG) rich domain are necessary for binding to the TXN 3'-untranslated region (By similarity). Both the RRM domain and the arginine, glycine (RGG) rich domain (RGG repeats) are necessary for optimal recruitment into SGs upon cellular stress. The C-terminal domain containing RGG repeats is necessary for translational repression.By similarity

Sequence similaritiesi

Contains 1 RRM (RNA recognition motif) domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiKOG0118. Eukaryota.
COG0724. LUCA.
GeneTreeiENSGT00710000106295.
HOGENOMiHOG000276232.
HOVERGENiHBG107480.
InParanoidiP60824.
KOiK13195.
OMAiERCVRCC.
PhylomeDBiP60824.
TreeFamiTF354331.

Family and domain databases

Gene3Di3.30.70.330. 1 hit.
InterProiIPR012677. Nucleotide-bd_a/b_plait.
IPR000504. RRM_dom.
IPR003954. RRM_dom_euk.
[Graphical view]
PfamiPF00076. RRM_1. 1 hit.
[Graphical view]
SMARTiSM00360. RRM. 1 hit.
SM00361. RRM_1. 1 hit.
[Graphical view]
SUPFAMiSSF54928. SSF54928. 1 hit.
PROSITEiPS50102. RRM. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P60824-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MASDEGKLFV GGLSFDTNEQ ALEQVFSKYG QISEVVVVKD RETQRSRGFG
60 70 80 90 100
FVTFENIDDA KDAMMAMNGK SVDGRQIRVD QAGKSSDNRS RGYRGGSAGG
110 120 130 140 150
RGFFRGGRSR GRGFSRGGGD RGYGGGRFES RSGGYGGSRD YYASRSQGGS
160 170
YGYRSSGGSY RDSYDSYATH NE
Length:172
Mass (Da):18,607
Last modified:April 13, 2004 - v1
Checksum:iDA0E53088FBED4C8
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D78135 mRNA. Translation: BAA11213.1.
AK014655 mRNA. Translation: BAB29491.1.
AK132584 mRNA. Translation: BAE21245.1.
BC075699 mRNA. Translation: AAH75699.1.
CCDSiCCDS35975.1.
RefSeqiNP_031731.1. NM_007705.2.
UniGeneiMm.17898.

Genome annotation databases

EnsembliENSMUST00000105365; ENSMUSP00000101004; ENSMUSG00000045193.
GeneIDi12696.
KEGGimmu:12696.
UCSCiuc007gce.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D78135 mRNA. Translation: BAA11213.1.
AK014655 mRNA. Translation: BAB29491.1.
AK132584 mRNA. Translation: BAE21245.1.
BC075699 mRNA. Translation: AAH75699.1.
CCDSiCCDS35975.1.
RefSeqiNP_031731.1. NM_007705.2.
UniGeneiMm.17898.

3D structure databases

ProteinModelPortaliP60824.
SMRiP60824. Positions 1-90.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiP60824. 2 interactions.
MINTiMINT-4090864.
STRINGi10090.ENSMUSP00000101004.

PTM databases

iPTMnetiP60824.
PhosphoSiteiP60824.

Proteomic databases

EPDiP60824.
MaxQBiP60824.
PaxDbiP60824.
PRIDEiP60824.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000105365; ENSMUSP00000101004; ENSMUSG00000045193.
GeneIDi12696.
KEGGimmu:12696.
UCSCiuc007gce.1. mouse.

Organism-specific databases

CTDi1153.
MGIiMGI:893588. Cirbp.

Phylogenomic databases

eggNOGiKOG0118. Eukaryota.
COG0724. LUCA.
GeneTreeiENSGT00710000106295.
HOGENOMiHOG000276232.
HOVERGENiHBG107480.
InParanoidiP60824.
KOiK13195.
OMAiERCVRCC.
PhylomeDBiP60824.
TreeFamiTF354331.

Miscellaneous databases

ChiTaRSiCirbp. mouse.
NextBioi281950.
PROiP60824.
SOURCEiSearch...

Gene expression databases

BgeeiP60824.
CleanExiMM_CIRBP.
ExpressionAtlasiP60824. baseline and differential.
GenevisibleiP60824. MM.

Family and domain databases

Gene3Di3.30.70.330. 1 hit.
InterProiIPR012677. Nucleotide-bd_a/b_plait.
IPR000504. RRM_dom.
IPR003954. RRM_dom_euk.
[Graphical view]
PfamiPF00076. RRM_1. 1 hit.
[Graphical view]
SMARTiSM00360. RRM. 1 hit.
SM00361. RRM_1. 1 hit.
[Graphical view]
SUPFAMiSSF54928. SSF54928. 1 hit.
PROSITEiPS50102. RRM. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "A glycine-rich RNA-binding protein mediating cold-inducible suppression of mammalian cell growth."
    Nishiyama H., Itoh K., Kaneko Y., Kishishita M., Yoshida O., Fujita J.
    J. Cell Biol. 137:899-908(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, INDUCTION BY COLD-SHOCK.
    Strain: DDY/STD.
    Tissue: Testis.
  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: Head.
  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].
    Strain: C57BL/6J.
    Tissue: Eye.
  4. "The cold-inducible RNA-binding protein migrates from the nucleus to cytoplasmic stress granules by a methylation-dependent mechanism and acts as a translational repressor."
    De Leeuw F., Zhang T., Wauquier C., Huez G., Kruys V., Gueydan C.
    Exp. Cell Res. 313:4130-4144(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, METHYLATION, SUBCELLULAR LOCATION, MUTAGENESIS OF ARG-91; ARG-94; ARG-101; ARG-105; ARG-108; ARG-110; ARG-112; ARG-116; ARG-121; ARG-127 AND ARG-131.
  5. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Brain, Brown adipose tissue, Liver, Lung, Pancreas, Spleen and Testis.

Entry informationi

Entry nameiCIRBP_MOUSE
AccessioniPrimary (citable) accession number: P60824
Secondary accession number(s): O09069
, O09148, Q3V1A6, Q61413
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 13, 2004
Last sequence update: April 13, 2004
Last modified: May 11, 2016
This is version 103 of the entry and version 1 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.