Full text data of CIRBP
CIRBP
(A18HNRNP, CIRP)
[Confidence: medium (present in either hRBCD or BSc_CH or PM22954596)]
Cold-inducible RNA-binding protein (A18 hnRNP; Glycine-rich RNA-binding protein CIRP)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
Cold-inducible RNA-binding protein (A18 hnRNP; Glycine-rich RNA-binding protein CIRP)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
UniProt
Q14011
ID CIRBP_HUMAN Reviewed; 172 AA.
AC Q14011;
DT 15-JUL-1999, integrated into UniProtKB/Swiss-Prot.
read moreDT 01-NOV-1996, sequence version 1.
DT 22-JAN-2014, entry version 134.
DE RecName: Full=Cold-inducible RNA-binding protein;
DE AltName: Full=A18 hnRNP;
DE AltName: Full=Glycine-rich RNA-binding protein CIRP;
GN Name=CIRBP; Synonyms=A18HNRNP, CIRP;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=9434172; DOI=10.1016/S0378-1119(97)00530-1;
RA Nishiyama H., Higashitsuji H., Yokoi H., Itoh K., Danno S.,
RA Matsuda T., Fujita J.;
RT "Cloning and characterization of human CIRP (cold-inducible RNA-
RT binding protein) cDNA and chromosomal assignment of the gene.";
RL Gene 204:115-120(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=9334257; DOI=10.1074/jbc.272.42.26720;
RA Sheikh M.S., Carrier F., Papathanasiou M.A., Hollander M.C., Zhan Q.,
RA Yu K., Fornace A.J. Jr.;
RT "Identification of several human homologs of hamster DNA damage-
RT inducible transcripts. Cloning and characterization of a novel UV-
RT inducible cDNA that codes for a putative RNA-binding protein.";
RL J. Biol. Chem. 272:26720-26726(1997).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15057824; DOI=10.1038/nature02399;
RA Grimwood J., Gordon L.A., Olsen A.S., Terry A., Schmutz J.,
RA Lamerdin J.E., Hellsten U., Goodstein D., Couronne O., Tran-Gyamfi M.,
RA Aerts A., Altherr M., Ashworth L., Bajorek E., Black S., Branscomb E.,
RA Caenepeel S., Carrano A.V., Caoile C., Chan Y.M., Christensen M.,
RA Cleland C.A., Copeland A., Dalin E., Dehal P., Denys M., Detter J.C.,
RA Escobar J., Flowers D., Fotopulos D., Garcia C., Georgescu A.M.,
RA Glavina T., Gomez M., Gonzales E., Groza M., Hammon N., Hawkins T.,
RA Haydu L., Ho I., Huang W., Israni S., Jett J., Kadner K., Kimball H.,
RA Kobayashi A., Larionov V., Leem S.-H., Lopez F., Lou Y., Lowry S.,
RA Malfatti S., Martinez D., McCready P.M., Medina C., Morgan J.,
RA Nelson K., Nolan M., Ovcharenko I., Pitluck S., Pollard M.,
RA Popkie A.P., Predki P., Quan G., Ramirez L., Rash S., Retterer J.,
RA Rodriguez A., Rogers S., Salamov A., Salazar A., She X., Smith D.,
RA Slezak T., Solovyev V., Thayer N., Tice H., Tsai M., Ustaszewska A.,
RA Vo N., Wagner M., Wheeler J., Wu K., Xie G., Yang J., Dubchak I.,
RA Furey T.S., DeJong P., Dickson M., Gordon D., Eichler E.E.,
RA Pennacchio L.A., Richardson P., Stubbs L., Rokhsar D.S., Myers R.M.,
RA Rubin E.M., Lucas S.M.;
RT "The DNA sequence and biology of human chromosome 19.";
RL Nature 428:529-535(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Lung, and Placenta;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [5]
RP FUNCTION, RNA-BINDING, AND SUBCELLULAR LOCATION.
RX PubMed=11574538; DOI=10.1074/jbc.M105396200;
RA Yang C., Carrier F.;
RT "The UV-inducible RNA-binding protein A18 (A18 hnRNP) plays a
RT protective role in the genotoxic stress response.";
RL J. Biol. Chem. 276:47277-47284(2001).
RN [6]
RP INDUCTION BY HYPOXIA.
RX PubMed=15075239; DOI=10.1242/jcs.01026;
RA Wellmann S., Buehrer C., Moderegger E., Zelmer A., Kirschner R.,
RA Koehne P., Fujita J., Seeger K.;
RT "Oxygen-regulated expression of the RNA-binding proteins RBM3 and CIRP
RT by a HIF-1-independent mechanism.";
RL J. Cell Sci. 117:1785-1794(2004).
RN [7]
RP FUNCTION, PHOSPHORYLATION, RNA-BINDING, INTERACTION WITH EIF4G1, AND
RP ASSOCIATION WITH RIBOSOMES.
RX PubMed=16513844; DOI=10.1093/nar/gkj519;
RA Yang R., Weber D.J., Carrier F.;
RT "Post-transcriptional regulation of thioredoxin by the stress
RT inducible heterogeneous ribonucleoprotein A18.";
RL Nucleic Acids Res. 34:1224-1236(2006).
RN [8]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [9]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Leukemic T-cell;
RX PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA Rodionov V., Han D.K.;
RT "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT reveals system-wide modulation of protein-protein interactions.";
RL Sci. Signal. 2:RA46-RA46(2009).
RN [10]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
RA Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [11]
RP STRUCTURE BY NMR OF 1-90.
RG RIKEN structural genomics initiative (RSGI);
RT "Solution structure of RRM domain in A18 HNRNP.";
RL Submitted (NOV-2005) to the PDB data bank.
CC -!- FUNCTION: Cold-inducible mRNA binding protein that plays a
CC protective role in the genotoxic stress response by stabilizing
CC transcripts of genes involved in cell survival. Acts as a
CC translational activator. Seems to play an essential role in cold-
CC induced suppression of cell proliferation. Binds specifically to
CC the 3'-untranslated regions (3'-UTRs) of stress-responsive
CC transcripts RPA2 and TXN. Acts as a translational repressor (By
CC similarity). Promotes assembly of stress granules (SGs), when
CC overexpressed.
CC -!- SUBUNIT: Interacts with EIF4G1. Associates with ribosomes.
CC -!- SUBCELLULAR LOCATION: Nucleus, nucleoplasm. Cytoplasm.
CC Note=Translocates from the nucleus to the cytoplasm after exposure
CC to UV radiation. Translocates from the nucleus to the cytoplasm
CC into stress granules upon various cytoplasmic stresses, such as
CC osmotic and heat shocks. Its recruitment into stress granules
CC occurs in the absence of TIAR proteins (By similarity).
CC -!- TISSUE SPECIFICITY: Ubiquitous.
CC -!- INDUCTION: By cold stress in response to DNA damage induced by UV
CC irradiation or UV mimetic agents. Up-regulated by hypoxia.
CC -!- DOMAIN: Both the RRM domain and the arginine, glycine (RGG) rich
CC domain are necessary for binding to the TXN 3'-untranslated
CC region. Both the RRM domain and the arginine, glycine (RGG) rich
CC domain (RGG repeats) are necessary for optimal recruitment into
CC SGs upon cellular stress. The C-terminal domain containing RGG
CC repeats is necessary for translational repression (By similarity).
CC -!- PTM: Methylated on arginine residues. Methylation of the RGG
CC motifs is a prerequisite for recruitment into SGs (By similarity).
CC -!- PTM: Phosphorylated by CK2, GSK3A and GSK3B. Phosphorylation by
CC GSK3B increases RNA-binding activity to the TXN 3'-UTR transcript
CC upon exposure to UV radiation.
CC -!- SIMILARITY: Contains 1 RRM (RNA recognition motif) domain.
CC -----------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution-NoDerivs License
CC -----------------------------------------------------------------------
DR EMBL; D78134; BAA11212.1; -; mRNA.
DR EMBL; AF021336; AAC51787.1; -; mRNA.
DR EMBL; AC004258; AAC04895.1; -; Genomic_DNA.
DR EMBL; BC000403; AAH00403.1; -; mRNA.
DR EMBL; BC000901; AAH00901.1; -; mRNA.
DR RefSeq; NP_001271.1; NM_001280.2.
DR UniGene; Hs.618145; -.
DR UniGene; Hs.634522; -.
DR PDB; 1X5S; NMR; -; A=1-89.
DR PDBsum; 1X5S; -.
DR ProteinModelPortal; Q14011; -.
DR SMR; Q14011; 1-90.
DR IntAct; Q14011; 15.
DR MINT; MINT-5004534; -.
DR STRING; 9606.ENSP00000322887; -.
DR PhosphoSite; Q14011; -.
DR DMDM; 5921786; -.
DR REPRODUCTION-2DPAGE; IPI00180954; -.
DR PaxDb; Q14011; -.
DR PRIDE; Q14011; -.
DR DNASU; 1153; -.
DR Ensembl; ENST00000320936; ENSP00000322887; ENSG00000099622.
DR Ensembl; ENST00000585630; ENSP00000466110; ENSG00000099622.
DR Ensembl; ENST00000586472; ENSP00000465779; ENSG00000099622.
DR Ensembl; ENST00000588030; ENSP00000468788; ENSG00000099622.
DR Ensembl; ENST00000588090; ENSP00000466207; ENSG00000099622.
DR Ensembl; ENST00000589660; ENSP00000468224; ENSG00000099622.
DR GeneID; 1153; -.
DR KEGG; hsa:1153; -.
DR UCSC; uc002lrr.4; human.
DR CTD; 1153; -.
DR GeneCards; GC19P001269; -.
DR HGNC; HGNC:1982; CIRBP.
DR MIM; 602649; gene.
DR neXtProt; NX_Q14011; -.
DR PharmGKB; PA26519; -.
DR eggNOG; COG0724; -.
DR HOGENOM; HOG000276232; -.
DR HOVERGEN; HBG107480; -.
DR InParanoid; Q14011; -.
DR KO; K13195; -.
DR OrthoDB; EOG780RPD; -.
DR PhylomeDB; Q14011; -.
DR ChiTaRS; CIRBP; human.
DR EvolutionaryTrace; Q14011; -.
DR GeneWiki; CIRBP; -.
DR GenomeRNAi; 1153; -.
DR NextBio; 4788; -.
DR PRO; PR:Q14011; -.
DR ArrayExpress; Q14011; -.
DR Bgee; Q14011; -.
DR CleanEx; HS_CIRBP; -.
DR Genevestigator; Q14011; -.
DR GO; GO:0010494; C:cytoplasmic stress granule; ISS:UniProtKB.
DR GO; GO:0005654; C:nucleoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0003730; F:mRNA 3'-UTR binding; IDA:UniProtKB.
DR GO; GO:0000166; F:nucleotide binding; IEA:InterPro.
DR GO; GO:0070181; F:SSU rRNA binding; IDA:UniProtKB.
DR GO; GO:0030371; F:translation repressor activity; ISS:UniProtKB.
DR GO; GO:0048255; P:mRNA stabilization; IDA:UniProtKB.
DR GO; GO:0045727; P:positive regulation of translation; IDA:UniProtKB.
DR GO; GO:0009409; P:response to cold; TAS:ProtInc.
DR GO; GO:0009411; P:response to UV; IDA:UniProtKB.
DR GO; GO:0034063; P:stress granule assembly; ISS:UniProtKB.
DR Gene3D; 3.30.70.330; -; 1.
DR InterPro; IPR012677; Nucleotide-bd_a/b_plait.
DR InterPro; IPR000504; RRM_dom.
DR Pfam; PF00076; RRM_1; 1.
DR SMART; SM00360; RRM; 1.
DR PROSITE; PS50102; RRM; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Activator; Complete proteome; Cytoplasm; Nucleus;
KW Reference proteome; Repressor; RNA-binding; Stress response.
FT CHAIN 1 172 Cold-inducible RNA-binding protein.
FT /FTId=PRO_0000081503.
FT DOMAIN 6 84 RRM.
FT COMPBIAS 92 158 Gly-rich.
FT STRAND 6 12
FT HELIX 19 29
FT STRAND 34 37
FT STRAND 41 43
FT STRAND 48 53
FT HELIX 57 67
FT STRAND 78 83
SQ SEQUENCE 172 AA; 18648 MW; 003FABF28F5405D0 CRC64;
MASDEGKLFV GGLSFDTNEQ SLEQVFSKYG QISEVVVVKD RETQRSRGFG FVTFENIDDA
KDAMMAMNGK SVDGRQIRVD QAGKSSDNRS RGYRGGSAGG RGFFRGGRGR GRGFSRGGGD
RGYGGNRFES RSGGYGGSRD YYSSRSQSGG YSDRSSGGSY RDSYDSYATH NE
//
ID CIRBP_HUMAN Reviewed; 172 AA.
AC Q14011;
DT 15-JUL-1999, integrated into UniProtKB/Swiss-Prot.
read moreDT 01-NOV-1996, sequence version 1.
DT 22-JAN-2014, entry version 134.
DE RecName: Full=Cold-inducible RNA-binding protein;
DE AltName: Full=A18 hnRNP;
DE AltName: Full=Glycine-rich RNA-binding protein CIRP;
GN Name=CIRBP; Synonyms=A18HNRNP, CIRP;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=9434172; DOI=10.1016/S0378-1119(97)00530-1;
RA Nishiyama H., Higashitsuji H., Yokoi H., Itoh K., Danno S.,
RA Matsuda T., Fujita J.;
RT "Cloning and characterization of human CIRP (cold-inducible RNA-
RT binding protein) cDNA and chromosomal assignment of the gene.";
RL Gene 204:115-120(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=9334257; DOI=10.1074/jbc.272.42.26720;
RA Sheikh M.S., Carrier F., Papathanasiou M.A., Hollander M.C., Zhan Q.,
RA Yu K., Fornace A.J. Jr.;
RT "Identification of several human homologs of hamster DNA damage-
RT inducible transcripts. Cloning and characterization of a novel UV-
RT inducible cDNA that codes for a putative RNA-binding protein.";
RL J. Biol. Chem. 272:26720-26726(1997).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15057824; DOI=10.1038/nature02399;
RA Grimwood J., Gordon L.A., Olsen A.S., Terry A., Schmutz J.,
RA Lamerdin J.E., Hellsten U., Goodstein D., Couronne O., Tran-Gyamfi M.,
RA Aerts A., Altherr M., Ashworth L., Bajorek E., Black S., Branscomb E.,
RA Caenepeel S., Carrano A.V., Caoile C., Chan Y.M., Christensen M.,
RA Cleland C.A., Copeland A., Dalin E., Dehal P., Denys M., Detter J.C.,
RA Escobar J., Flowers D., Fotopulos D., Garcia C., Georgescu A.M.,
RA Glavina T., Gomez M., Gonzales E., Groza M., Hammon N., Hawkins T.,
RA Haydu L., Ho I., Huang W., Israni S., Jett J., Kadner K., Kimball H.,
RA Kobayashi A., Larionov V., Leem S.-H., Lopez F., Lou Y., Lowry S.,
RA Malfatti S., Martinez D., McCready P.M., Medina C., Morgan J.,
RA Nelson K., Nolan M., Ovcharenko I., Pitluck S., Pollard M.,
RA Popkie A.P., Predki P., Quan G., Ramirez L., Rash S., Retterer J.,
RA Rodriguez A., Rogers S., Salamov A., Salazar A., She X., Smith D.,
RA Slezak T., Solovyev V., Thayer N., Tice H., Tsai M., Ustaszewska A.,
RA Vo N., Wagner M., Wheeler J., Wu K., Xie G., Yang J., Dubchak I.,
RA Furey T.S., DeJong P., Dickson M., Gordon D., Eichler E.E.,
RA Pennacchio L.A., Richardson P., Stubbs L., Rokhsar D.S., Myers R.M.,
RA Rubin E.M., Lucas S.M.;
RT "The DNA sequence and biology of human chromosome 19.";
RL Nature 428:529-535(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Lung, and Placenta;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [5]
RP FUNCTION, RNA-BINDING, AND SUBCELLULAR LOCATION.
RX PubMed=11574538; DOI=10.1074/jbc.M105396200;
RA Yang C., Carrier F.;
RT "The UV-inducible RNA-binding protein A18 (A18 hnRNP) plays a
RT protective role in the genotoxic stress response.";
RL J. Biol. Chem. 276:47277-47284(2001).
RN [6]
RP INDUCTION BY HYPOXIA.
RX PubMed=15075239; DOI=10.1242/jcs.01026;
RA Wellmann S., Buehrer C., Moderegger E., Zelmer A., Kirschner R.,
RA Koehne P., Fujita J., Seeger K.;
RT "Oxygen-regulated expression of the RNA-binding proteins RBM3 and CIRP
RT by a HIF-1-independent mechanism.";
RL J. Cell Sci. 117:1785-1794(2004).
RN [7]
RP FUNCTION, PHOSPHORYLATION, RNA-BINDING, INTERACTION WITH EIF4G1, AND
RP ASSOCIATION WITH RIBOSOMES.
RX PubMed=16513844; DOI=10.1093/nar/gkj519;
RA Yang R., Weber D.J., Carrier F.;
RT "Post-transcriptional regulation of thioredoxin by the stress
RT inducible heterogeneous ribonucleoprotein A18.";
RL Nucleic Acids Res. 34:1224-1236(2006).
RN [8]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [9]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Leukemic T-cell;
RX PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA Rodionov V., Han D.K.;
RT "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT reveals system-wide modulation of protein-protein interactions.";
RL Sci. Signal. 2:RA46-RA46(2009).
RN [10]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
RA Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [11]
RP STRUCTURE BY NMR OF 1-90.
RG RIKEN structural genomics initiative (RSGI);
RT "Solution structure of RRM domain in A18 HNRNP.";
RL Submitted (NOV-2005) to the PDB data bank.
CC -!- FUNCTION: Cold-inducible mRNA binding protein that plays a
CC protective role in the genotoxic stress response by stabilizing
CC transcripts of genes involved in cell survival. Acts as a
CC translational activator. Seems to play an essential role in cold-
CC induced suppression of cell proliferation. Binds specifically to
CC the 3'-untranslated regions (3'-UTRs) of stress-responsive
CC transcripts RPA2 and TXN. Acts as a translational repressor (By
CC similarity). Promotes assembly of stress granules (SGs), when
CC overexpressed.
CC -!- SUBUNIT: Interacts with EIF4G1. Associates with ribosomes.
CC -!- SUBCELLULAR LOCATION: Nucleus, nucleoplasm. Cytoplasm.
CC Note=Translocates from the nucleus to the cytoplasm after exposure
CC to UV radiation. Translocates from the nucleus to the cytoplasm
CC into stress granules upon various cytoplasmic stresses, such as
CC osmotic and heat shocks. Its recruitment into stress granules
CC occurs in the absence of TIAR proteins (By similarity).
CC -!- TISSUE SPECIFICITY: Ubiquitous.
CC -!- INDUCTION: By cold stress in response to DNA damage induced by UV
CC irradiation or UV mimetic agents. Up-regulated by hypoxia.
CC -!- DOMAIN: Both the RRM domain and the arginine, glycine (RGG) rich
CC domain are necessary for binding to the TXN 3'-untranslated
CC region. Both the RRM domain and the arginine, glycine (RGG) rich
CC domain (RGG repeats) are necessary for optimal recruitment into
CC SGs upon cellular stress. The C-terminal domain containing RGG
CC repeats is necessary for translational repression (By similarity).
CC -!- PTM: Methylated on arginine residues. Methylation of the RGG
CC motifs is a prerequisite for recruitment into SGs (By similarity).
CC -!- PTM: Phosphorylated by CK2, GSK3A and GSK3B. Phosphorylation by
CC GSK3B increases RNA-binding activity to the TXN 3'-UTR transcript
CC upon exposure to UV radiation.
CC -!- SIMILARITY: Contains 1 RRM (RNA recognition motif) domain.
CC -----------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution-NoDerivs License
CC -----------------------------------------------------------------------
DR EMBL; D78134; BAA11212.1; -; mRNA.
DR EMBL; AF021336; AAC51787.1; -; mRNA.
DR EMBL; AC004258; AAC04895.1; -; Genomic_DNA.
DR EMBL; BC000403; AAH00403.1; -; mRNA.
DR EMBL; BC000901; AAH00901.1; -; mRNA.
DR RefSeq; NP_001271.1; NM_001280.2.
DR UniGene; Hs.618145; -.
DR UniGene; Hs.634522; -.
DR PDB; 1X5S; NMR; -; A=1-89.
DR PDBsum; 1X5S; -.
DR ProteinModelPortal; Q14011; -.
DR SMR; Q14011; 1-90.
DR IntAct; Q14011; 15.
DR MINT; MINT-5004534; -.
DR STRING; 9606.ENSP00000322887; -.
DR PhosphoSite; Q14011; -.
DR DMDM; 5921786; -.
DR REPRODUCTION-2DPAGE; IPI00180954; -.
DR PaxDb; Q14011; -.
DR PRIDE; Q14011; -.
DR DNASU; 1153; -.
DR Ensembl; ENST00000320936; ENSP00000322887; ENSG00000099622.
DR Ensembl; ENST00000585630; ENSP00000466110; ENSG00000099622.
DR Ensembl; ENST00000586472; ENSP00000465779; ENSG00000099622.
DR Ensembl; ENST00000588030; ENSP00000468788; ENSG00000099622.
DR Ensembl; ENST00000588090; ENSP00000466207; ENSG00000099622.
DR Ensembl; ENST00000589660; ENSP00000468224; ENSG00000099622.
DR GeneID; 1153; -.
DR KEGG; hsa:1153; -.
DR UCSC; uc002lrr.4; human.
DR CTD; 1153; -.
DR GeneCards; GC19P001269; -.
DR HGNC; HGNC:1982; CIRBP.
DR MIM; 602649; gene.
DR neXtProt; NX_Q14011; -.
DR PharmGKB; PA26519; -.
DR eggNOG; COG0724; -.
DR HOGENOM; HOG000276232; -.
DR HOVERGEN; HBG107480; -.
DR InParanoid; Q14011; -.
DR KO; K13195; -.
DR OrthoDB; EOG780RPD; -.
DR PhylomeDB; Q14011; -.
DR ChiTaRS; CIRBP; human.
DR EvolutionaryTrace; Q14011; -.
DR GeneWiki; CIRBP; -.
DR GenomeRNAi; 1153; -.
DR NextBio; 4788; -.
DR PRO; PR:Q14011; -.
DR ArrayExpress; Q14011; -.
DR Bgee; Q14011; -.
DR CleanEx; HS_CIRBP; -.
DR Genevestigator; Q14011; -.
DR GO; GO:0010494; C:cytoplasmic stress granule; ISS:UniProtKB.
DR GO; GO:0005654; C:nucleoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0003730; F:mRNA 3'-UTR binding; IDA:UniProtKB.
DR GO; GO:0000166; F:nucleotide binding; IEA:InterPro.
DR GO; GO:0070181; F:SSU rRNA binding; IDA:UniProtKB.
DR GO; GO:0030371; F:translation repressor activity; ISS:UniProtKB.
DR GO; GO:0048255; P:mRNA stabilization; IDA:UniProtKB.
DR GO; GO:0045727; P:positive regulation of translation; IDA:UniProtKB.
DR GO; GO:0009409; P:response to cold; TAS:ProtInc.
DR GO; GO:0009411; P:response to UV; IDA:UniProtKB.
DR GO; GO:0034063; P:stress granule assembly; ISS:UniProtKB.
DR Gene3D; 3.30.70.330; -; 1.
DR InterPro; IPR012677; Nucleotide-bd_a/b_plait.
DR InterPro; IPR000504; RRM_dom.
DR Pfam; PF00076; RRM_1; 1.
DR SMART; SM00360; RRM; 1.
DR PROSITE; PS50102; RRM; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Activator; Complete proteome; Cytoplasm; Nucleus;
KW Reference proteome; Repressor; RNA-binding; Stress response.
FT CHAIN 1 172 Cold-inducible RNA-binding protein.
FT /FTId=PRO_0000081503.
FT DOMAIN 6 84 RRM.
FT COMPBIAS 92 158 Gly-rich.
FT STRAND 6 12
FT HELIX 19 29
FT STRAND 34 37
FT STRAND 41 43
FT STRAND 48 53
FT HELIX 57 67
FT STRAND 78 83
SQ SEQUENCE 172 AA; 18648 MW; 003FABF28F5405D0 CRC64;
MASDEGKLFV GGLSFDTNEQ SLEQVFSKYG QISEVVVVKD RETQRSRGFG FVTFENIDDA
KDAMMAMNGK SVDGRQIRVD QAGKSSDNRS RGYRGGSAGG RGFFRGGRGR GRGFSRGGGD
RGYGGNRFES RSGGYGGSRD YYSSRSQSGG YSDRSSGGSY RDSYDSYATH NE
//
MIM
602649
*RECORD*
*FIELD* NO
602649
*FIELD* TI
*602649 COLD-INDUCIBLE RNA-BINDING PROTEIN; CIRBP
;;CIRP
*FIELD* TX
CLONING
Cold stress induces in microorganisms the synthesis of several proteins
read morethat are involved in various cellular processes such as transcription,
translation, and recombination. The cold-inducible RNA-binding protein
(Cirp) is induced in rodent cells by mild cold stress (32 degrees C).
Cirp consists of an N-terminal RNA-binding domain and a C-terminal
gly-rich domain, and plays an essential role in cold-induced suppression
of cell proliferation. Nishiyama et al. (1997) cloned a cDNA encoding an
18-kD protein with 95.3% amino acid sequence identity to the mouse Cirp
protein. CIRBP mRNA was constitutively expressed in all cell lines
examined. In all of the cell lines, the levels of CIRBP mRNA and protein
were increased within 12 hours after a temperature downshift from 37
degrees C to 32 degrees C. These results demonstrated that CIRBP is a
cold-shock protein in human cells.
MAPPING
By fluorescence in situ hybridization, Nishiyama et al. (1997) mapped
the CIRBP gene to chromosome 19p13.3.
GENE FUNCTION
Morf et al. (2012) showed that simulated body temperature cycles, but
not peripheral oscillators, controlled the rhythmic expression of
cold-inducible RNA-binding protein (CIRBP) in cultured fibroblasts. In
turn, loss-of-function experiments indicated that CIRBP was required for
high-amplitude circadian gene expression. The transcriptomewide
identification of CIRBP-bound RNAs by a biotin-streptavidin-based
crosslinking and immunoprecipitation (CLIP) procedure revealed several
transcripts encoding circadian oscillator proteins, including CLOCK
(601851). Moreover, CLOCK accumulation was strongly reduced in
CIRBP-depleted fibroblasts. Because ectopic expression of CLOCK improved
circadian gene expression in these cells, Morf et al. (2012) concluded
that CIRBP confers robustness to circadian oscillators through
regulation of CLOCK expression.
*FIELD* RF
1. Morf, J.; Rey, G.; Schneider, K.; Stratmann, M.; Fujita, J.; Naef,
F.; Schibler, U.: Cold-inducible RNA-binding protein modulates circadian
gene expression posttranscriptionally. Science 338: 379-383, 2012.
2. Nishiyama, H.; Higashitsuji, H.; Yokoi, H.; Itoh, K.; Danno, S.;
Matsuda, T.; Fujita, J.: Cloning and characterization of human CIRP
(cold-inducible RNA-binding protein) cDNA and chromosomal assignment
of the gene. Gene 204: 115-120, 1997.
*FIELD* CN
Ada Hamosh - updated: 11/7/2012
*FIELD* CD
Victor A. McKusick: 5/22/1998
*FIELD* ED
alopez: 11/07/2012
terry: 11/7/2012
carol: 5/22/1998
*RECORD*
*FIELD* NO
602649
*FIELD* TI
*602649 COLD-INDUCIBLE RNA-BINDING PROTEIN; CIRBP
;;CIRP
*FIELD* TX
CLONING
Cold stress induces in microorganisms the synthesis of several proteins
read morethat are involved in various cellular processes such as transcription,
translation, and recombination. The cold-inducible RNA-binding protein
(Cirp) is induced in rodent cells by mild cold stress (32 degrees C).
Cirp consists of an N-terminal RNA-binding domain and a C-terminal
gly-rich domain, and plays an essential role in cold-induced suppression
of cell proliferation. Nishiyama et al. (1997) cloned a cDNA encoding an
18-kD protein with 95.3% amino acid sequence identity to the mouse Cirp
protein. CIRBP mRNA was constitutively expressed in all cell lines
examined. In all of the cell lines, the levels of CIRBP mRNA and protein
were increased within 12 hours after a temperature downshift from 37
degrees C to 32 degrees C. These results demonstrated that CIRBP is a
cold-shock protein in human cells.
MAPPING
By fluorescence in situ hybridization, Nishiyama et al. (1997) mapped
the CIRBP gene to chromosome 19p13.3.
GENE FUNCTION
Morf et al. (2012) showed that simulated body temperature cycles, but
not peripheral oscillators, controlled the rhythmic expression of
cold-inducible RNA-binding protein (CIRBP) in cultured fibroblasts. In
turn, loss-of-function experiments indicated that CIRBP was required for
high-amplitude circadian gene expression. The transcriptomewide
identification of CIRBP-bound RNAs by a biotin-streptavidin-based
crosslinking and immunoprecipitation (CLIP) procedure revealed several
transcripts encoding circadian oscillator proteins, including CLOCK
(601851). Moreover, CLOCK accumulation was strongly reduced in
CIRBP-depleted fibroblasts. Because ectopic expression of CLOCK improved
circadian gene expression in these cells, Morf et al. (2012) concluded
that CIRBP confers robustness to circadian oscillators through
regulation of CLOCK expression.
*FIELD* RF
1. Morf, J.; Rey, G.; Schneider, K.; Stratmann, M.; Fujita, J.; Naef,
F.; Schibler, U.: Cold-inducible RNA-binding protein modulates circadian
gene expression posttranscriptionally. Science 338: 379-383, 2012.
2. Nishiyama, H.; Higashitsuji, H.; Yokoi, H.; Itoh, K.; Danno, S.;
Matsuda, T.; Fujita, J.: Cloning and characterization of human CIRP
(cold-inducible RNA-binding protein) cDNA and chromosomal assignment
of the gene. Gene 204: 115-120, 1997.
*FIELD* CN
Ada Hamosh - updated: 11/7/2012
*FIELD* CD
Victor A. McKusick: 5/22/1998
*FIELD* ED
alopez: 11/07/2012
terry: 11/7/2012
carol: 5/22/1998