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Protein

Cold-inducible RNA-binding protein

Gene

CIRBP

Organism
Homo sapiens (Human)
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. Acts as a translational activator. Seems to play an essential role in cold-induced suppression of cell proliferation. Binds specifically to the 3'-untranslated regions (3'-UTRs) of stress-responsive transcripts RPA2 and TXN. Acts as a translational repressor (By similarity). Promotes assembly of stress granules (SGs), when overexpressed.By similarity2 Publications

GO - Molecular functioni

  • mRNA 3'-UTR binding Source: UniProtKB
  • nucleotide binding Source: InterPro
  • poly(A) RNA binding Source: UniProtKB
  • small ribosomal subunit rRNA binding Source: UniProtKB
  • translation repressor activity Source: UniProtKB

GO - Biological processi

  • mRNA stabilization Source: UniProtKB
  • positive regulation of translation Source: UniProtKB
  • response to cold Source: ProtInc
  • 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:A18HNRNP, CIRP
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 19

Organism-specific databases

HGNCiHGNC:1982. CIRBP.

Subcellular locationi

  • Nucleusnucleoplasm 1 Publication
  • Cytoplasm 1 Publication

  • Note: Translocates from the nucleus to the cytoplasm after exposure to UV radiation. 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).By similarity

GO - Cellular componenti

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

Keywords - Cellular componenti

Cytoplasm, Nucleus

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA26519.

Polymorphism and mutation databases

BioMutaiCIRBP.
DMDMi5921786.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 172172Cold-inducible RNA-binding proteinPRO_0000081503Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei130 – 1301PhosphoserineCombined sources
Modified residuei138 – 1381PhosphoserineCombined sources
Modified residuei146 – 1461PhosphoserineCombined sources
Modified residuei156 – 1561PhosphoserineCombined sources
Modified residuei159 – 1591PhosphoserineCombined sources
Modified residuei163 – 1631PhosphoserineCombined sources

Post-translational modificationi

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

Keywords - PTMi

Phosphoprotein

Proteomic databases

EPDiQ14011.
PaxDbiQ14011.
PeptideAtlasiQ14011.
PRIDEiQ14011.

2D gel databases

REPRODUCTION-2DPAGEIPI00180954.

PTM databases

iPTMnetiQ14011.
PhosphoSiteiQ14011.

Expressioni

Tissue specificityi

Ubiquitous.

Inductioni

By cold stress in response to DNA damage induced by UV irradiation or UV mimetic agents. Up-regulated by hypoxia.1 Publication

Gene expression databases

BgeeiQ14011.
CleanExiHS_CIRBP.
ExpressionAtlasiQ14011. baseline and differential.
GenevisibleiQ14011. HS.

Interactioni

Subunit structurei

Interacts with EIF4G1. Associates with ribosomes.1 Publication

Binary interactionsi

WithEntry#Exp.IntActNotes
HNRNPKP619785EBI-538850,EBI-304185
HNRPKQ6IBN13EBI-538850,EBI-3440248
KHDRBS2Q5VWX13EBI-538850,EBI-742808
LNX1Q8TBB13EBI-538850,EBI-739832
RBMXP381594EBI-538850,EBI-743526
RBMY1A1P0DJD33EBI-538850,EBI-8638511
RBMY1JQ154153EBI-538850,EBI-8642021
SNRPAP090123EBI-538850,EBI-607085

Protein-protein interaction databases

BioGridi107573. 78 interactions.
IntActiQ14011. 34 interactions.
MINTiMINT-5004534.
STRINGi9606.ENSP00000322887.

Structurei

Secondary structure

1
172
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi6 – 127Combined sources
Helixi19 – 2911Combined sources
Beta strandi34 – 374Combined sources
Beta strandi41 – 433Combined sources
Beta strandi48 – 536Combined sources
Helixi57 – 6711Combined sources
Beta strandi78 – 836Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1X5SNMR-A1-89[»]
ProteinModelPortaliQ14011.
SMRiQ14011. Positions 1-90.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ14011.

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. 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).By similarity

Sequence similaritiesi

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

Phylogenomic databases

eggNOGiKOG0118. Eukaryota.
COG0724. LUCA.
GeneTreeiENSGT00710000106295.
HOGENOMiHOG000276232.
HOVERGENiHBG107480.
InParanoidiQ14011.
KOiK13195.
OrthoDBiEOG780RPD.
PhylomeDBiQ14011.

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]

Sequences (3)i

Sequence statusi: Complete.

This entry describes 3 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q14011-1) [UniParc]FASTAAdd to basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MASDEGKLFV GGLSFDTNEQ SLEQVFSKYG QISEVVVVKD RETQRSRGFG
60 70 80 90 100
FVTFENIDDA KDAMMAMNGK SVDGRQIRVD QAGKSSDNRS RGYRGGSAGG
110 120 130 140 150
RGFFRGGRGR GRGFSRGGGD RGYGGNRFES RSGGYGGSRD YYSSRSQSGG
160 170
YSDRSSGGSY RDSYDSYATH NE
Length:172
Mass (Da):18,648
Last modified:November 1, 1996 - v1
Checksum:i003FABF28F5405D0
GO
Isoform 2 (identifier: Q14011-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     83-116: Missing.
     167-167: Y → YGKSHSEGAT...PLHCACFLSS

Note: No experimental confirmation available.
Show »
Length:263
Mass (Da):28,359
Checksum:i448CFD5BB4EB08C5
GO
Isoform 3 (identifier: Q14011-3) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-69: MASDEGKLFV...AKDAMMAMNG → MSSRWSRSSQSTDRSL
     167-167: Y → YGKSHSEGAT...PLHCACFLSS

Note: No experimental confirmation available.
Show »
Length:244
Mass (Da):26,130
Checksum:iDAFAD25578042649
GO

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 6969MASDE…MAMNG → MSSRWSRSSQSTDRSL in isoform 3. 1 PublicationVSP_056895Add
BLAST
Alternative sequencei83 – 11634Missing in isoform 2. 1 PublicationVSP_056402Add
BLAST
Alternative sequencei167 – 1671Y → YGKSHSEGATLLWPAVGARF TLVPSPSTLGWTLRPCHCAC PEEAHLSSQSHFYRRTQKPN ETDQKGKGERGPAGQSARCM CGRRPASLGCGGWLLPGRRP RPGLASGVKLPLVASVPLHC ACFLSS in isoform 2 and isoform 3. 1 PublicationVSP_056403

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D78134 mRNA. Translation: BAA11212.1.
AF021336 mRNA. Translation: AAC51787.1.
AK094781 mRNA. Translation: BAG52929.1.
AK304470 mRNA. Translation: BAG65284.1.
AC004221 Genomic DNA. No translation available.
AC004258 Genomic DNA. Translation: AAC04895.1.
BC000403 mRNA. Translation: AAH00403.1.
BC000901 mRNA. Translation: AAH00901.1.
CCDSiCCDS12059.1. [Q14011-1]
RefSeqiNP_001271.1. NM_001280.2. [Q14011-1]
NP_001287744.1. NM_001300815.1.
NP_001287758.1. NM_001300829.1.
XP_006722700.1. XM_006722637.1. [Q14011-1]
UniGeneiHs.618145.
Hs.634522.

Genome annotation databases

EnsembliENST00000320936; ENSP00000322887; ENSG00000099622. [Q14011-1]
ENST00000413636; ENSP00000412831; ENSG00000099622. [Q14011-2]
ENST00000585630; ENSP00000466110; ENSG00000099622. [Q14011-1]
ENST00000586472; ENSP00000465779; ENSG00000099622. [Q14011-1]
ENST00000588030; ENSP00000468788; ENSG00000099622. [Q14011-1]
ENST00000588090; ENSP00000466207; ENSG00000099622. [Q14011-1]
GeneIDi1153.
KEGGihsa:1153.
UCSCiuc010xgl.2. human. [Q14011-1]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D78134 mRNA. Translation: BAA11212.1.
AF021336 mRNA. Translation: AAC51787.1.
AK094781 mRNA. Translation: BAG52929.1.
AK304470 mRNA. Translation: BAG65284.1.
AC004221 Genomic DNA. No translation available.
AC004258 Genomic DNA. Translation: AAC04895.1.
BC000403 mRNA. Translation: AAH00403.1.
BC000901 mRNA. Translation: AAH00901.1.
CCDSiCCDS12059.1. [Q14011-1]
RefSeqiNP_001271.1. NM_001280.2. [Q14011-1]
NP_001287744.1. NM_001300815.1.
NP_001287758.1. NM_001300829.1.
XP_006722700.1. XM_006722637.1. [Q14011-1]
UniGeneiHs.618145.
Hs.634522.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1X5SNMR-A1-89[»]
ProteinModelPortaliQ14011.
SMRiQ14011. Positions 1-90.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi107573. 78 interactions.
IntActiQ14011. 34 interactions.
MINTiMINT-5004534.
STRINGi9606.ENSP00000322887.

PTM databases

iPTMnetiQ14011.
PhosphoSiteiQ14011.

Polymorphism and mutation databases

BioMutaiCIRBP.
DMDMi5921786.

2D gel databases

REPRODUCTION-2DPAGEIPI00180954.

Proteomic databases

EPDiQ14011.
PaxDbiQ14011.
PeptideAtlasiQ14011.
PRIDEiQ14011.

Protocols and materials databases

DNASUi1153.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000320936; ENSP00000322887; ENSG00000099622. [Q14011-1]
ENST00000413636; ENSP00000412831; ENSG00000099622. [Q14011-2]
ENST00000585630; ENSP00000466110; ENSG00000099622. [Q14011-1]
ENST00000586472; ENSP00000465779; ENSG00000099622. [Q14011-1]
ENST00000588030; ENSP00000468788; ENSG00000099622. [Q14011-1]
ENST00000588090; ENSP00000466207; ENSG00000099622. [Q14011-1]
GeneIDi1153.
KEGGihsa:1153.
UCSCiuc010xgl.2. human. [Q14011-1]

Organism-specific databases

CTDi1153.
GeneCardsiCIRBP.
HGNCiHGNC:1982. CIRBP.
MIMi602649. gene.
neXtProtiNX_Q14011.
PharmGKBiPA26519.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG0118. Eukaryota.
COG0724. LUCA.
GeneTreeiENSGT00710000106295.
HOGENOMiHOG000276232.
HOVERGENiHBG107480.
InParanoidiQ14011.
KOiK13195.
OrthoDBiEOG780RPD.
PhylomeDBiQ14011.

Miscellaneous databases

ChiTaRSiCIRBP. human.
EvolutionaryTraceiQ14011.
GeneWikiiCIRBP.
GenomeRNAii1153.
PROiQ14011.
SOURCEiSearch...

Gene expression databases

BgeeiQ14011.
CleanExiHS_CIRBP.
ExpressionAtlasiQ14011. baseline and differential.
GenevisibleiQ14011. HS.

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. "Cloning and characterization of human CIRP (cold-inducible RNA-binding protein) cDNA and chromosomal assignment of the gene."
    Nishiyama H., Higashitsuji H., Yokoi H., Itoh K., Danno S., Matsuda T., Fujita J.
    Gene 204:115-120(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
  2. "Identification of several human homologs of hamster DNA damage-inducible transcripts. Cloning and characterization of a novel UV-inducible cDNA that codes for a putative RNA-binding protein."
    Sheikh M.S., Carrier F., Papathanasiou M.A., Hollander M.C., Zhan Q., Yu K., Fornace A.J. Jr.
    J. Biol. Chem. 272:26720-26726(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
  3. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
    Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
    , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
    Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2 AND 3).
    Tissue: Brain and Uterus.
  4. "The DNA sequence and biology of human chromosome 19."
    Grimwood J., Gordon L.A., Olsen A.S., Terry A., Schmutz J., Lamerdin J.E., Hellsten U., Goodstein D., Couronne O., Tran-Gyamfi M., Aerts A., Altherr M., Ashworth L., Bajorek E., Black S., Branscomb E., Caenepeel S., Carrano A.V.
    , Caoile C., Chan Y.M., Christensen M., Cleland C.A., Copeland A., Dalin E., Dehal P., Denys M., Detter J.C., Escobar J., Flowers D., Fotopulos D., Garcia C., Georgescu A.M., Glavina T., Gomez M., Gonzales E., Groza M., Hammon N., Hawkins T., Haydu L., Ho I., Huang W., Israni S., Jett J., Kadner K., Kimball H., Kobayashi A., Larionov V., Leem S.-H., Lopez F., Lou Y., Lowry S., Malfatti S., Martinez D., McCready P.M., Medina C., Morgan J., Nelson K., Nolan M., Ovcharenko I., Pitluck S., Pollard M., Popkie A.P., Predki P., Quan G., Ramirez L., Rash S., Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A., She X., Smith D., Slezak T., Solovyev V., Thayer N., Tice H., Tsai M., Ustaszewska A., Vo N., Wagner M., Wheeler J., Wu K., Xie G., Yang J., Dubchak I., Furey T.S., DeJong P., Dickson M., Gordon D., Eichler E.E., Pennacchio L.A., Richardson P., Stubbs L., Rokhsar D.S., Myers R.M., Rubin E.M., Lucas S.M.
    Nature 428:529-535(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  5. "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] (ISOFORM 1).
    Tissue: Lung and Placenta.
  6. "The UV-inducible RNA-binding protein A18 (A18 hnRNP) plays a protective role in the genotoxic stress response."
    Yang C., Carrier F.
    J. Biol. Chem. 276:47277-47284(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, RNA-BINDING, SUBCELLULAR LOCATION.
  7. "Oxygen-regulated expression of the RNA-binding proteins RBM3 and CIRP by a HIF-1-independent mechanism."
    Wellmann S., Buehrer C., Moderegger E., Zelmer A., Kirschner R., Koehne P., Fujita J., Seeger K.
    J. Cell Sci. 117:1785-1794(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: INDUCTION BY HYPOXIA.
  8. "Post-transcriptional regulation of thioredoxin by the stress inducible heterogeneous ribonucleoprotein A18."
    Yang R., Weber D.J., Carrier F.
    Nucleic Acids Res. 34:1224-1236(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, PHOSPHORYLATION, RNA-BINDING, INTERACTION WITH EIF4G1, ASSOCIATION WITH RIBOSOMES.
  9. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  10. "Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
    Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
    Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Leukemic T-cell.
  11. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  12. "Toward a comprehensive characterization of a human cancer cell phosphoproteome."
    Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J., Mohammed S.
    J. Proteome Res. 12:260-271(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-130; SER-138; SER-146; SER-156; SER-159 AND SER-163, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma and Erythroleukemia.
  13. "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome."
    Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., Ye M., Zou H.
    J. Proteomics 96:253-262(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  14. "Solution structure of RRM domain in A18 HNRNP."
    RIKEN structural genomics initiative (RSGI)
    Submitted (NOV-2005) to the PDB data bank
    Cited for: STRUCTURE BY NMR OF 1-90.

Entry informationi

Entry nameiCIRBP_HUMAN
AccessioniPrimary (citable) accession number: Q14011
Secondary accession number(s): B3KT17, B4E2X2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 15, 1999
Last sequence update: November 1, 1996
Last modified: July 6, 2016
This is version 159 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 19
    Human chromosome 19: entries, gene names and cross-references to MIM
  2. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. 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.