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Reviewed, UniProtKB/Swiss-Prot Q9Y2D9 (ZN652_HUMAN)

Last modified January 19, 2010. Version 67. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Binary interactions · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    Zinc finger protein 652
Gene names
Name: ZNF652
Synonyms: KIAA0924
OrganismHomo sapiens (Human) [Complete proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length606 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level.

General annotation (Comments)

Function

Functions as a transcriptional repressor. Ref.6

Subunit structure

Interacts with CBFA2T3. Ref.6

Subcellular location

Nucleus Probable.

Tissue specificity

Widely expressed with higher expression in breast, prostate, vulva and pancreas. Ref.6

Sequence similarities

Belongs to the krueppel C2H2-type zinc-finger protein family.

Contains 9 C2H2-type zinc fingers.

Ontologies

Keywords
   Biological processTranscription
Transcription regulation
   Cellular componentNucleus
   DomainRepeat
Zinc-finger
   LigandDNA-binding
Metal-binding
Zinc
   Molecular functionRepressor
   PTMPhosphoprotein
   Technical termComplete proteome
Gene Ontology (GO)
   Biological processregulation of transcription

Inferred from electronic annotation. Source: UniProtKB-KW

transcription

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular componentnucleus

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular functionDNA binding

Inferred from electronic annotation. Source: UniProtKB-KW

protein binding Ref.6

Inferred from physical interaction. Source: IntAct

zinc ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

Binary interactions

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 606606Zinc finger protein 652
PRO_0000280428

Regions

Zinc finger245 – 26824C2H2-type 1
Zinc finger272 – 29423C2H2-type 2; degenerate
Zinc finger299 – 32224C2H2-type 3
Zinc finger329 – 35123C2H2-type 4
Zinc finger357 – 37923C2H2-type 5
Zinc finger385 – 40723C2H2-type 6
Zinc finger413 – 43523C2H2-type 7
Zinc finger441 – 46323C2H2-type 8
Zinc finger469 – 49224C2H2-type 9; degenerate
Region498 – 606109Mediates interaction with CBFA2T3
Compositional bias74 – 183110Glu-rich
Compositional bias497 – 57478Pro-rich

Amino acid modifications

Modified residue571Phosphoserine Ref.9
Modified residue1971Phosphoserine Ref.9
Modified residue2041Phosphoserine Ref.9 Ref.7
Modified residue3801Phosphoserine Ref.8

Sequences

Sequence LengthMass (Da)Tools
Q9Y2D9-1 [UniParc].

Last modified March 20, 2007. Version 3.
Checksum: C066D10E179985CC

FASTA60669,744
        10         20         30         40         50         60 
MSHTASSCQE LVENCAVHVA GMAQEDSRRG QVPSSFYHGA NQELDLSTKV YKRESGSPYS 

        70         80         90        100        110        120 
VLVDTKMSKP HLHETEEQPY FRETRAVSDV HAVKEDRENS DDTEEEEEEV SYKREQIIVE 

       130        140        150        160        170        180 
VNLNNQTLNV SKGEKGVSSQ SKETPVLKTS SEEEEEESEE EATDDSNDYG ENEKQKKKEK 

       190        200        210        220        230        240 
IVEKVSVTQR RTRRAASVAA ATTSPTPRTT RGRRKSVEPP KRKKRATKEP KAPVQKAKCE 

       250        260        270        280        290        300 
EKETLTCEKC PRVFNTRWYL EKHMNVTHRR MQICDKCGKK FVLESELSLH QQTDCEKNIQ 

       310        320        330        340        350        360 
CVSCNKSFKK LWSLHEHIKI VHGYAEKKFS CEICEKKFYT MAHVRKHMVA HTKDMPFTCE 

       370        380        390        400        410        420 
TCGKSFKRSM SLKVHSLQHS GEKPFRCENC DERFQYKYQL RSHMSIHIGH KQFMCQWCGK 

       430        440        450        460        470        480 
DFNMKQYFDE HMKTHTGEKP FICEICGKSF TSRPNMKRHR RTHTGEKPYP CDVCGQRFRF 

       490        500        510        520        530        540 
SNMLKAHKEK CFRVTSPVNV PPAVQIPLTT SPATPVPSVV NTATTPTPPI NMNPVSTLPP 

       550        560        570        580        590        600 
RPIPHPFSHL HIHPHPHHPH HLPIPPVPHL PPPPALFKSE PLNHRGQSED NFLRHLAEKN 


SSAQHH 

« Hide

References

« Hide 'large scale' references
[1]"Prediction of the coding sequences of unidentified human genes. XIII. The complete sequences of 100 new cDNA clones from brain which code for large proteins in vitro."
Nagase T., Ishikawa K., Suyama M., Kikuno R., Hirosawa M., Miyajima N., Tanaka A., Kotani H., Nomura N., Ohara O.
DNA Res. 6:63-70(1999) [PubMed: 10231032] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Brain.
[2]Ohara O., Nagase T., Kikuno R.
Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases
Cited for: SEQUENCE REVISION.
[3]"The full-ORF clone resource of the German cDNA consortium."
Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U., Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A., Wiemann S., Schupp I.
BMC Genomics 8:399-399(2007) [PubMed: 17974005] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Testis.
[4]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].
[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: 15489334] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[6]"ZNF652, a novel zinc finger protein, interacts with the putative breast tumor suppressor CBFA2T3 to repress transcription."
Kumar R., Manning J., Spendlove H.E., Kremmidiotis G., McKirdy R., Lee J., Millband D.N., Cheney K.M., Stampfer M.R., Dwivedi P.P., Morris H.A., Callen D.F.
Mol. Cancer Res. 4:655-665(2006) [PubMed: 16966434] [Abstract]
Cited for: FUNCTION, INTERACTION WITH CBFA2T3, TISSUE SPECIFICITY.
[7]"Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient phosphoproteomic analysis."
Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D., Yates J.R. III
J. Proteome Res. 7:1346-1351(2008) [PubMed: 18220336] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-204, MASS SPECTROMETRY.
[8]"A quantitative atlas of mitotic phosphorylation."
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed: 18669648] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-380, MASS SPECTROMETRY.
[9]"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: 19690332] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-57; SER-197 AND SER-204, MASS SPECTROMETRY.
Tissue: T-cell.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AB023141 mRNA. Translation: BAA76768.2. Different initiation.
CR933680 mRNA. Translation: CAI45974.1.
CH471109 Genomic DNA. Translation: EAW94682.1.
BC139779 mRNA. Translation: AAI39780.1.
BC152440 mRNA. Translation: AAI52441.1.
IPIIPI00790021.
RefSeqNP_001138837.1.
NP_055712.1.
UniGeneHs.463375

3D structure databases

HSSPHSSP built from PDB template 1SP2 based on UniProtKB P08047.
SMRQ9Y2D9. Positions 296-465, 357-488.
ModBaseSearch...

Protein-protein interaction databases

IntActQ9Y2D9. 3 interactions.
STRINGQ9Y2D9.

PTM databases

PhosphoSiteQ9Y2D9.

Proteomic databases

PRIDEQ9Y2D9.

Genome annotation databases

EnsemblENST00000362063; ENSP00000354686; ENSG00000198740; Homo sapiens. [Genome view]
ENST00000430262; ENSP00000416305; ENSG00000198740; Homo sapiens. [Genome view]
GeneID22834.
KEGGhsa:22834.
UCSCuc002iov.2. human.

Organism-specific databases

CTD22834.
GeneCardsGC17M044728.
HGNCHGNC:29147. ZNF652.
PharmGKBPA134896615.
HUGESearch...
GenAtlasSearch...

Phylogenomic databases

eggNOGprNOG06773.
HOGENOMHBG506587.
HOVERGENQ9Y2D9.
InParanoidQ9Y2D9.
OMAMAQEDSR.
OrthoDBEOG99S8SG.
PhylomeDBQ9Y2D9.

Gene expression databases

ArrayExpressQ9Y2D9.
BgeeQ9Y2D9.
CleanExHS_ZNF652.
GenevestigatorQ9Y2D9.

Family and domain databases

InterProIPR007087. Znf_C2H2.
IPR015880. Znf_C2H2-like.
IPR013087. Znf_C2H2/integrase_DNA-bd.
[Graphical view]
Gene3DG3DSA:3.30.160.60. Znf_C2H2/integrase_DNA-bd. 2 hits.
PfamPF00096. zf-C2H2. 2 hits.
[Graphical view]
SMARTSM00355. ZnF_C2H2. 9 hits.
[Graphical view]
PROSITEPS00028. ZINC_FINGER_C2H2_1. 7 hits.
PS50157. ZINC_FINGER_C2H2_2. 9 hits.
[Graphical view]
ProtoNetSearch...

Other Resources

NextBio43261.

Entry information

Entry nameZN652_HUMAN
AccessionPrimary (citable) accession number: Q9Y2D9
Secondary accession number(s): A4QPD9, Q5H9Q0
Entry history
Integrated into UniProtKB/Swiss-Prot: March 20, 2007
Last sequence update: March 20, 2007
Last modified: January 19, 2010
This is version 67 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHPI (Human Proteome Initiative)
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.

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SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Binary interactions · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents