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P62633 (CNBP_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 108. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Cellular nucleic acid-binding protein

Short name=CNBP
Alternative name(s):
Zinc finger protein 9
Gene names
Name:CNBP
Synonyms:RNF163, ZNF9
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length177 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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

Subcellular location

Cytoplasm By similarity. Endoplasmic reticulum By similarity.

Tissue specificity

Present in all tissues examined.

Post-translational modification

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

Involvement in disease

Dystrophia myotonica 2 (DM2) [MIM:602668]: A multisystem disease characterized by the association of proximal muscle weakness with myotonia, cardiac manifestations and cataract. Additional features can include hyperhidrosis, testicular atrophy, insulin resistance and diabetes and central nervous system anomalies in rare cases.
Note: The disease is caused by mutations affecting the gene represented in this entry. The causative mutation is a CCTG expansion (mean approximately 5000 repeats) located in intron 1 of the CNBP gene. Ref.3

Sequence similarities

Contains 7 CCHC-type zinc fingers.

Ontologies

Keywords
   Biological processTranscription
Transcription regulation
   Cellular componentCytoplasm
Endoplasmic reticulum
   Coding sequence diversityAlternative splicing
   DomainRepeat
Zinc-finger
   LigandDNA-binding
Metal-binding
Zinc
   Molecular functionRepressor
   PTMAcetylation
Methylation
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processcholesterol biosynthetic process

Traceable author statement Ref.1. Source: ProtInc

positive regulation of cell proliferation

Inferred from sequence or structural similarity. Source: UniProtKB

positive regulation of transcription from RNA polymerase II promoter

Inferred from sequence or structural similarity. Source: UniProtKB

positive regulation of transcription, DNA-templated

Inferred from sequence or structural similarity. Source: UniProtKB

regulation of transcription, DNA-templated

Traceable author statement Ref.1. Source: ProtInc

transcription, DNA-templated

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular_componentcytosol

Inferred from sequence or structural similarity. Source: UniProtKB

endoplasmic reticulum

Inferred from sequence or structural similarity. Source: UniProtKB

nucleus

Inferred from sequence or structural similarity. Source: UniProtKB

   Molecular_functionpoly(A) RNA binding

Inferred from direct assay PubMed 22658674PubMed 22681889. Source: UniProtKB

sequence-specific DNA binding transcription factor activity

Traceable author statement Ref.1. Source: ProtInc

single-stranded DNA binding

Inferred from electronic annotation. Source: Ensembl

single-stranded RNA binding

Inferred from electronic annotation. Source: Ensembl

zinc ion binding

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Alternative products

This entry describes 8 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: P62633-1)

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.
Isoform 2 (identifier: P62633-2)

The sequence of this isoform differs from the canonical sequence as follows:
     36-42: Missing.
Isoform 3 (identifier: P62633-3)

The sequence of this isoform differs from the canonical sequence as follows:
     42-51: Missing.
Isoform 4 (identifier: P62633-4)

The sequence of this isoform differs from the canonical sequence as follows:
     72-72: D → DE
Isoform 5 (identifier: P62633-5)

The sequence of this isoform differs from the canonical sequence as follows:
     36-42: Missing.
     72-72: D → DVE
Note: No experimental confirmation available.
Isoform 6 (identifier: P62633-6)

The sequence of this isoform differs from the canonical sequence as follows:
     72-72: D → DVE
Note: No experimental confirmation available.
Isoform 7 (identifier: P62633-7)

The sequence of this isoform differs from the canonical sequence as follows:
     35-51: Missing.
Note: No experimental confirmation available.
Isoform 8 (identifier: P62633-8)

The sequence of this isoform differs from the canonical sequence as follows:
     36-42: Missing.
     72-72: D → DE

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.11
Chain2 – 177176Cellular nucleic acid-binding protein
PRO_0000089965

Regions

Zinc finger4 – 2118CCHC-type 1
Zinc finger52 – 6918CCHC-type 2
Zinc finger72 – 8918CCHC-type 3
Zinc finger96 – 11318CCHC-type 4
Zinc finger117 – 13418CCHC-type 5
Zinc finger135 – 15218CCHC-type 6
Zinc finger156 – 17318CCHC-type 7
Compositional bias22 – 4221Arg/Gly-rich

Amino acid modifications

Modified residue21N-acetylserine Ref.11
Modified residue81N6-acetyllysine By similarity
Modified residue251Omega-N-methylarginine; by PRMT1 Ref.12
Modified residue271Omega-N-methylarginine; by PRMT1 Ref.12

Natural variations

Alternative sequence35 – 5117Missing in isoform 7.
VSP_055084
Alternative sequence36 – 427Missing in isoform 2, isoform 5 and isoform 8.
VSP_010981
Alternative sequence42 – 5110Missing in isoform 3.
VSP_010982
Alternative sequence721D → DE in isoform 4 and isoform 8.
VSP_043304
Alternative sequence721D → DVE in isoform 5 and isoform 6.
VSP_043424

Experimental info

Mutagenesis251R → K: Significantly reduces methylation; when associated with K-27. Ref.12
Mutagenesis271R → K: Significantly reduces methylation; when associated with K-25. Ref.12
Sequence conflict61C → R in BAF84808. Ref.5

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified July 19, 2004. Version 1.
Checksum: 996F398285F52618

FASTA17719,463
        10         20         30         40         50         60 
MSSNECFKCG RSGHWARECP TGGGRGRGMR SRGRGGFTSD RGFQFVSSSL PDICYRCGES 

        70         80         90        100        110        120 
GHLAKDCDLQ EDACYNCGRG GHIAKDCKEP KREREQCCYN CGKPGHLARD CDHADEQKCY 

       130        140        150        160        170 
SCGEFGHIQK DCTKVKCYRC GETGHVAINC SKTSEVNCYR CGESGHLARE CTIEATA 

« Hide

Isoform 2 [UniParc].

Checksum: 152BEC42881358E8
Show »

FASTA17018,742
Isoform 3 [UniParc].

Checksum: D59B4E42A6477FF2
Show »

FASTA16718,413
Isoform 4 [UniParc].

Checksum: DF0CDAB9BF3D96BB
Show »

FASTA17819,592
Isoform 5 [UniParc].

Checksum: E2C0B3EF2820CD94
Show »

FASTA17218,970
Isoform 6 [UniParc].

Checksum: AB793FABFDE0C072
Show »

FASTA17919,691
Isoform 7 [UniParc].

Checksum: 1C2D9D62F90EFCFB
Show »

FASTA16017,692
Isoform 8 [UniParc].

Checksum: 46809E6C7F3070C5
Show »

FASTA17118,871

References

« Hide 'large scale' references
[1]"Identification of a zinc finger protein that binds to the sterol regulatory element."
Rajavashisth T.B., Taylor A.K., Andalibi A., Svenson K.L., Lusis A.J.
Science 245:640-643(1989) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
[2]"Organization of the gene encoding cellular nucleic acid-binding protein."
Flink I.L., Morkin E.
Gene 163:279-282(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Tissue: Placenta.
[3]"Myotonic dystrophy type 2 caused by a CCTG expansion in intron 1 of ZNF9."
Liquori C.L., Ricker K., Moseley M.L., Jacobsen J.F., Kress W., Naylor S.L., Day J.W., Ranum L.P.
Science 293:864-867(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], DISEASE.
[4]"Cloning of novel transcript variants of human cellular nucleic acid binding protein."
Yang F., Yan H., Zhang S.
Submitted (JUN-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 4; 5 AND 8).
[5]"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. expand/collapse author list , 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 1; 3; 6 AND 7).
Tissue: Placenta and Synovium.
[6]"Cloning of human full-length CDSs in BD Creator(TM) system donor vector."
Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., Phelan M., Farmer A.
Submitted (OCT-2004) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 4).
[7]"The DNA sequence, annotation and analysis of human chromosome 3."
Muzny D.M., Scherer S.E., Kaul R., Wang J., Yu J., Sudbrak R., Buhay C.J., Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V., Hume J. expand/collapse author list , Jackson A., Khan Z.M., Kovar-Smith C., Lewis L.R., Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R., Morgan M.B., Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D., Wei S., Wheeler D.A., Wright M.W., Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z., Clendenning J., Clerc-Blankenburg K.P., Chen R., Chen Z., Davis C., Delgado O., Dinh H.H., Dong W., Draper H., Ernst S., Fu G., Gonzalez-Garay M.L., Garcia D.K., Gillett W., Gu J., Hao B., Haugen E., Havlak P., He X., Hennig S., Hu S., Huang W., Jackson L.R., Jacob L.S., Kelly S.H., Kube M., Levy R., Li Z., Liu B., Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O., Palmeiri A., Pasternak S., Perez L.M., Phelps K.A., Plopper F.J., Qiang B., Raymond C., Rodriguez R., Saenphimmachak C., Santibanez J., Shen H., Shen Y., Subramanian S., Tabor P.E., Verduzco D., Waldron L., Wang J., Wang J., Wang Q., Williams G.A., Wong G.K.-S., Yao Z., Zhang J., Zhang X., Zhao G., Zhou J., Zhou Y., Nelson D., Lehrach H., Reinhardt R., Naylor S.L., Yang H., Olson M., Weinstock G., Gibbs R.A.
Nature 440:1194-1198(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[8]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[9]"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] (ISOFORMS 1 AND 2).
Tissue: Brain, Lung and Uterus.
[10]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[11]"N-terminal acetylome analyses and functional insights of the N-terminal acetyltransferase NatB."
Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A., Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
[12]"Arginine methylation of the cellular nucleic acid binding protein does not affect its subcellular localization but impedes RNA binding."
Wei H.M., Hu H.H., Chang G.Y., Lee Y.J., Li Y.C., Chang H.H., Li C.
FEBS Lett. 588:1542-1548(2014) [PubMed] [Europe PMC] [Abstract]
Cited for: METHYLATION AT ARG-25 AND ARG-27, MUTAGENESIS OF ARG-25 AND ARG-27.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M28372 mRNA. Translation: AAA61975.1.
U19765 Genomic DNA. Translation: AAA91782.1.
AY329622 Genomic DNA. Translation: AAR89462.1.
DQ092366 mRNA. Translation: AAY96754.1.
DQ092367 mRNA. Translation: AAY96755.1.
DQ091187 mRNA. Translation: AAY89856.1.
AK054592 mRNA. Translation: BAB70769.1.
AK298154 mRNA. Translation: BAG60429.1.
AK292119 mRNA. Translation: BAF84808.1.
AK314380 mRNA. Translation: BAG37006.1.
BT019613 mRNA. Translation: AAV38419.1.
AC108673 Genomic DNA. No translation available.
AC135587 Genomic DNA. No translation available.
CH471052 Genomic DNA. Translation: EAW79271.1.
CH471052 Genomic DNA. Translation: EAW79272.1.
CH471052 Genomic DNA. Translation: EAW79273.1.
CH471052 Genomic DNA. Translation: EAW79274.1.
CH471052 Genomic DNA. Translation: EAW79275.1.
CH471052 Genomic DNA. Translation: EAW79277.1.
BC000288 mRNA. Translation: AAH00288.1.
BC014911 mRNA. Translation: AAH14911.1.
BC093058 mRNA. Translation: AAH93058.1.
CCDSCCDS3056.1. [P62633-1]
CCDS46906.1. [P62633-6]
CCDS46907.1. [P62633-4]
CCDS46908.1. [P62633-5]
CCDS54637.1. [P62633-2]
PIRA32760.
RefSeqNP_001120664.1. NM_001127192.1. [P62633-6]
NP_001120665.1. NM_001127193.1. [P62633-4]
NP_001120666.1. NM_001127194.1. [P62633-5]
NP_001120668.1. NM_001127196.1. [P62633-2]
NP_003409.1. NM_003418.4. [P62633-1]
UniGeneHs.518249.

3D structure databases

ProteinModelPortalP62633.
SMRP62633. Positions 4-70, 74-112, 135-174.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid113387. 49 interactions.
IntActP62633. 5 interactions.
MINTMINT-4589059.
STRING9606.ENSP00000303844.

PTM databases

PhosphoSiteP62633.

Polymorphism databases

DMDM50401852.

Proteomic databases

MaxQBP62633.
PaxDbP62633.
PRIDEP62633.

Protocols and materials databases

DNASU7555.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000422453; ENSP00000410619; ENSG00000169714. [P62633-1]
ENST00000441626; ENSP00000410769; ENSG00000169714. [P62633-6]
ENST00000446936; ENSP00000400444; ENSG00000169714. [P62633-5]
ENST00000451728; ENSP00000399488; ENSG00000169714. [P62633-4]
ENST00000500450; ENSP00000426223; ENSG00000169714.
ENST00000502976; ENSP00000421323; ENSG00000169714. [P62633-2]
ENST00000504813; ENSP00000422110; ENSG00000169714. [P62633-3]
GeneID7555.
KEGGhsa:7555.
UCSCuc003elq.4. human. [P62633-1]
uc003elr.4. human. [P62633-2]
uc021xdt.1. human. [P62633-5]

Organism-specific databases

CTD7555.
GeneCardsGC03M128886.
GeneReviewsCNBP.
HGNCHGNC:13164. CNBP.
MIM116955. gene.
602668. phenotype.
neXtProtNX_P62633.
Orphanet606. Proximal myotonic myopathy.
PharmGKBPA37737.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG5082.
HOGENOMHOG000186262.
HOVERGENHBG000397.
InParanoidP62633.
KOK09250.
OMACPNGQGG.
OrthoDBEOG790G22.
PhylomeDBP62633.
TreeFamTF316974.

Gene expression databases

ArrayExpressP62633.
BgeeP62633.
CleanExHS_CNBP.
GenevestigatorP62633.

Family and domain databases

Gene3D4.10.60.10. 4 hits.
InterProIPR001878. Znf_CCHC.
[Graphical view]
PfamPF00098. zf-CCHC. 7 hits.
[Graphical view]
SMARTSM00343. ZnF_C2HC. 7 hits.
[Graphical view]
SUPFAMSSF57756. SSF57756. 4 hits.
PROSITEPS50158. ZF_CCHC. 7 hits.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSCNBP. human.
GeneWikiCNBP.
GenomeRNAi7555.
NextBio29559.
PROP62633.
SOURCESearch...

Entry information

Entry nameCNBP_HUMAN
AccessionPrimary (citable) accession number: P62633
Secondary accession number(s): A8K7V4 expand/collapse secondary AC list , B2RAV9, B4DP17, D3DNB9, D3DNC0, D3DNC1, E9PDR7, P20694, Q4JGY0, Q4JGY1, Q5QJR0, Q5U0E9, Q6PJI7, Q96NV3
Entry history
Integrated into UniProtKB/Swiss-Prot: July 19, 2004
Last sequence update: July 19, 2004
Last modified: July 9, 2014
This is version 108 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human chromosome 3

Human chromosome 3: entries, gene names and cross-references to MIM