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Protein

Cellular nucleic acid-binding protein

Gene

Cnbp

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at transcript leveli

Functioni

Single-stranded DNA-binding protein, with specificity to the sterol regulatory element (SRE). Involved in sterol-mediated repression.

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri4 – 2118CCHC-type 1PROSITE-ProRule annotationAdd
BLAST
Zinc fingeri52 – 6918CCHC-type 2PROSITE-ProRule annotationAdd
BLAST
Zinc fingeri72 – 8918CCHC-type 3PROSITE-ProRule annotationAdd
BLAST
Zinc fingeri96 – 11318CCHC-type 4PROSITE-ProRule annotationAdd
BLAST
Zinc fingeri117 – 13418CCHC-type 5PROSITE-ProRule annotationAdd
BLAST
Zinc fingeri135 – 15218CCHC-type 6PROSITE-ProRule annotationAdd
BLAST
Zinc fingeri156 – 17318CCHC-type 7PROSITE-ProRule annotationAdd
BLAST

GO - Molecular functioni

  • poly(A) RNA binding Source: Ensembl
  • single-stranded DNA binding Source: RGD
  • single-stranded RNA binding Source: RGD
  • zinc ion binding Source: InterPro

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Repressor

Keywords - Biological processi

Transcription, Transcription regulation

Keywords - Ligandi

DNA-binding, Metal-binding, Zinc

Names & Taxonomyi

Protein namesi
Recommended name:
Cellular nucleic acid-binding protein
Short name:
CNBP
Alternative name(s):
Zinc finger protein 9
Gene namesi
Name:Cnbp
Synonyms:Znf9
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Chromosome 4

Organism-specific databases

RGDi621807. Cnbp.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Endoplasmic reticulum

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methionineiRemovedBy similarity
Chaini2 – 177176Cellular nucleic acid-binding proteinPRO_0000089968Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylserineBy similarity
Modified residuei8 – 81N6-acetyllysineBy similarity
Modified residuei25 – 251Omega-N-methylarginine; by PRMT1By similarity
Modified residuei27 – 271Omega-N-methylarginine; by PRMT1By similarity
Modified residuei49 – 491PhosphoserineBy similarity

Post-translational modificationi

Arginine methylation by PRMT1 in the Arg/Gly-rich region impedes RNA binding.By similarity

Keywords - PTMi

Acetylation, Methylation, Phosphoprotein

Proteomic databases

PaxDbiP62634.
PRIDEiP62634.

PTM databases

iPTMnetiP62634.
PhosphoSiteiP62634.

Expressioni

Tissue specificityi

Present in all tissues examined.

Gene expression databases

GenevisibleiP62634. RN.

Interactioni

Protein-protein interaction databases

BioGridi249114. 1 interaction.
STRINGi10116.ENSRNOP00000013884.

Structurei

3D structure databases

ProteinModelPortaliP62634.
SMRiP62634. Positions 4-70, 74-112, 135-175.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi22 – 4221Arg/Gly-richAdd
BLAST

Sequence similaritiesi

Contains 7 CCHC-type zinc fingers.PROSITE-ProRule annotation

Zinc finger

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri4 – 2118CCHC-type 1PROSITE-ProRule annotationAdd
BLAST
Zinc fingeri52 – 6918CCHC-type 2PROSITE-ProRule annotationAdd
BLAST
Zinc fingeri72 – 8918CCHC-type 3PROSITE-ProRule annotationAdd
BLAST
Zinc fingeri96 – 11318CCHC-type 4PROSITE-ProRule annotationAdd
BLAST
Zinc fingeri117 – 13418CCHC-type 5PROSITE-ProRule annotationAdd
BLAST
Zinc fingeri135 – 15218CCHC-type 6PROSITE-ProRule annotationAdd
BLAST
Zinc fingeri156 – 17318CCHC-type 7PROSITE-ProRule annotationAdd
BLAST

Keywords - Domaini

Repeat, Zinc-finger

Phylogenomic databases

eggNOGiKOG4400. Eukaryota.
COG5082. LUCA.
GeneTreeiENSGT00510000047065.
HOGENOMiHOG000186262.
HOVERGENiHBG000397.
InParanoidiP62634.
KOiK09250.
OMAiCPNGQGG.
OrthoDBiEOG790G22.
PhylomeDBiP62634.

Family and domain databases

Gene3Di4.10.60.10. 4 hits.
InterProiIPR001878. Znf_CCHC.
[Graphical view]
PfamiPF00098. zf-CCHC. 7 hits.
[Graphical view]
SMARTiSM00343. ZnF_C2HC. 7 hits.
[Graphical view]
SUPFAMiSSF57756. SSF57756. 4 hits.
PROSITEiPS50158. ZF_CCHC. 7 hits.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P62634-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSSNECFKCG RSGHWARECP TGGGRGRGMR SRGRGGFTSD RGFQFVSSSL
60 70 80 90 100
PDICYRCGES GHLAKDCDLQ EDACYNCGRG GHIAKDCKEP KREREQCCYN
110 120 130 140 150
CGKPGHLARD CDHADEQKCY SCGEFGHIQK DCTKVKCYRC GETGHVAINC
160 170
SKTSEVNCYR CGESGHLARE CTIEATA
Length:177
Mass (Da):19,463
Last modified:July 19, 2004 - v1
Checksum:i996F398285F52618
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D45254 mRNA. Translation: BAA08212.1.
AF242550 mRNA. Translation: AAF78224.1.
AY329624 Genomic DNA. Translation: AAR89464.1.
AB158421 mRNA. Translation: BAE16993.1.
AB158422 mRNA. Translation: BAE16994.1.
BC062225 mRNA. Translation: AAH62225.1.
PIRiJC2512.
RefSeqiNP_072120.1. NM_022598.1.
UniGeneiRn.6187.

Genome annotation databases

EnsembliENSRNOT00000013884; ENSRNOP00000013884; ENSRNOG00000010239.
GeneIDi64530.
KEGGirno:64530.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D45254 mRNA. Translation: BAA08212.1.
AF242550 mRNA. Translation: AAF78224.1.
AY329624 Genomic DNA. Translation: AAR89464.1.
AB158421 mRNA. Translation: BAE16993.1.
AB158422 mRNA. Translation: BAE16994.1.
BC062225 mRNA. Translation: AAH62225.1.
PIRiJC2512.
RefSeqiNP_072120.1. NM_022598.1.
UniGeneiRn.6187.

3D structure databases

ProteinModelPortaliP62634.
SMRiP62634. Positions 4-70, 74-112, 135-175.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi249114. 1 interaction.
STRINGi10116.ENSRNOP00000013884.

PTM databases

iPTMnetiP62634.
PhosphoSiteiP62634.

Proteomic databases

PaxDbiP62634.
PRIDEiP62634.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSRNOT00000013884; ENSRNOP00000013884; ENSRNOG00000010239.
GeneIDi64530.
KEGGirno:64530.

Organism-specific databases

CTDi7555.
RGDi621807. Cnbp.

Phylogenomic databases

eggNOGiKOG4400. Eukaryota.
COG5082. LUCA.
GeneTreeiENSGT00510000047065.
HOGENOMiHOG000186262.
HOVERGENiHBG000397.
InParanoidiP62634.
KOiK09250.
OMAiCPNGQGG.
OrthoDBiEOG790G22.
PhylomeDBiP62634.

Miscellaneous databases

PROiP62634.

Gene expression databases

GenevisibleiP62634. RN.

Family and domain databases

Gene3Di4.10.60.10. 4 hits.
InterProiIPR001878. Znf_CCHC.
[Graphical view]
PfamiPF00098. zf-CCHC. 7 hits.
[Graphical view]
SMARTiSM00343. ZnF_C2HC. 7 hits.
[Graphical view]
SUPFAMiSSF57756. SSF57756. 4 hits.
PROSITEiPS50158. ZF_CCHC. 7 hits.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Cloning and characterization of rat cellular nucleic acid binding protein (CNBP) cDNA."
    Yasuda J., Mashiyama S., Makino R., Ohyama S., Sekiya T., Hayashi K.
    DNA Res. 2:45-49(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Strain: Sprague-Dawley.
  2. "Identification and characterization of a distal repression region that represses clusterin expression."
    Wang Z., Tenniswood M.
    Submitted (MAR-2000) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Strain: Sprague-Dawley.
    Tissue: Kidney.
  3. "Myotonic dystrophy type 2: human founder haplotype and evolutionary conservation of the repeat tract."
    Liquori C.L., Ikeda Y., Weatherspoon M., Ricker K., Schoser B.G., Dalton J.C., Day J.W., Ranum L.P.
    Am. J. Hum. Genet. 73:849-862(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: Brown Norway.
  4. "Fine mapping of radiation susceptibility and gene expression analysis of LEC congenic rat lines."
    Tsuji A.B., Sugyo A., Ogiu T., Sagara M., Kimura T., Ishikawa A., Sudo H., Ohtsuki M., Aburatani H., Imai T., Harada Y.N.
    Genomics 86:271-279(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Strain: Fischer 344/DuCrj and LEC/Crj.
  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].
    Tissue: Pituitary.

Entry informationi

Entry nameiCNBP_RAT
AccessioniPrimary (citable) accession number: P62634
Secondary accession number(s): P20694, Q5QJQ8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 19, 2004
Last sequence update: July 19, 2004
Last modified: June 8, 2016
This is version 93 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. 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.