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P35227 (PCGF2_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 136. 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·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Polycomb group RING finger protein 2
Alternative name(s):
DNA-binding protein Mel-18
RING finger protein 110
Zinc finger protein 144
Gene names
Name:PCGF2
Synonyms:MEL18, RNF110, ZNF144
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length344 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Transcriptional repressor. Binds specifically to the DNA sequence 5'-GACTNGACT-3'. Has tumor suppressor activity. May play a role in control of cell proliferation and/or neural cell development. Regulates proliferation of early T progenitor cells by maintaining expression of HES1. Also plays a role in antero-posterior specification of the axial skeleton and negative regulation of the self-renewal activity of hematopoietic stem cells. Component of a Polycomb group (PcG) multiprotein PRC1-like complex, a complex class required to maintain the transcriptionally repressive state of many genes, including Hox genes, throughout development. PcG PRC1 complex acts via chromatin remodeling and modification of histones; it mediates monoubiquitination of histone H2A 'Lys-119', rendering chromatin heritably changed in its expressibility. Is not functionally redundant with BMI1; unlike BMI1 does not stimulate the E3 ubiquitin-protein ligase activity in a reconstituted PRC1-like complex By similarity.

Subunit structure

Exists as both a monomer and homodimer By similarity. Component of a PRC1-like complex. Interacts WITH CBX8, RING1 AND RNF2. Ref.7 Ref.8

Subcellular location

Nucleus Ref.8.

Tissue specificity

Detected in all tissues examined with high expression found in placenta lung and kidney and low expression, in liver, pancreas and skeletal muscle.

Post-translational modification

Phosphorylated. Homodimer formation is regulated by phosphorylation state with unphosphorylated protein forming homodimers By similarity.

Sequence similarities

Contains 1 RING-type zinc finger.

Ontologies

Keywords
   Biological processTranscription
Transcription regulation
   Cellular componentNucleus
   DomainZinc-finger
   LigandDNA-binding
Metal-binding
Zinc
   Molecular functionRepressor
   PTMPhosphoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processanterior/posterior pattern specification

Inferred from electronic annotation. Source: Ensembl

embryonic skeletal system morphogenesis

Inferred from electronic annotation. Source: Ensembl

histone acetylation

Inferred from electronic annotation. Source: Ensembl

in utero embryonic development

Inferred from electronic annotation. Source: Ensembl

negative regulation of apoptotic signaling pathway

Inferred from electronic annotation. Source: Ensembl

negative regulation of transcription from RNA polymerase II promoter

Inferred from mutant phenotype Ref.7. Source: UniProtKB

transcription, DNA-templated

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular_componentPRC1 complex

Inferred from direct assay Ref.7. Source: UniProtKB

PcG protein complex

Inferred from direct assay Ref.8. Source: UniProtKB

nuclear body

Inferred from electronic annotation. Source: Ensembl

nuclear chromatin

Inferred from direct assay Ref.7. Source: UniProtKB

nucleus

Inferred from direct assay Ref.8. Source: UniProtKB

sex chromatin

Inferred from electronic annotation. Source: Ensembl

   Molecular_functionDNA binding

Inferred from electronic annotation. Source: UniProtKB-KW

chromatin binding

Inferred from electronic annotation. Source: Ensembl

protein binding

Inferred from physical interaction Ref.7PubMed 20601937Ref.8PubMed 22493164. Source: IntAct

sequence-specific DNA binding transcription factor activity

Traceable author statement Ref.1. Source: ProtInc

ubiquitin-protein transferase activity

Inferred from electronic annotation. Source: Ensembl

zinc ion binding

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 344344Polycomb group RING finger protein 2
PRO_0000055984

Regions

Zinc finger18 – 5740RING-type
Motif81 – 9515Nuclear localization signal Potential
Compositional bias242 – 344103Pro/Ser-rich

Amino acid modifications

Modified residue3441Phosphothreonine Ref.6

Sequences

Sequence LengthMass (Da)Tools
P35227 [UniParc].

Last modified February 1, 1994. Version 1.
Checksum: A910BCD4C0CE9927

FASTA34437,788
        10         20         30         40         50         60 
MHRTTRIKIT ELNPHLMCAL CGGYFIDATT IVECLHSFCK TCIVRYLETN KYCPMCDVQV 

        70         80         90        100        110        120 
HKTRPLLSIR SDKTLQDIVY KLVPGLFKDE MKRRRDFYAA YPLTEVPNGS NEDRGEVLEQ 

       130        140        150        160        170        180 
EKGALSDDEI VSLSIEFYEG ARDRDEKKGP LENGDGDKEK TGVRFLRCPA AMTVMHLAKF 

       190        200        210        220        230        240 
LRNKMDVPSK YKVEVLYEDE PLKEYYTLMD IAYIYPWRRN GPLPLKYRVQ PACKRLTLAT 

       250        260        270        280        290        300 
VPTPSEGTNT SGASECESVS DKAPSPATLP ATSSSLPSPA TPSHGSPSSH GPPATHPTSP 

       310        320        330        340 
TPPSTASGAT TAANGGSLNC LQTPSSTSRG RKMTVNGAPV PPLT 

« Hide

References

« Hide 'large scale' references
[1]"Cloning and chromosome mapping of the human Mel-18 gene which encodes a DNA-binding protein with a new 'RING-finger' motif."
Ishida A., Asano H., Hasegawa M., Koseki H., Ono T., Yoshida M.C., Taniguchi M., Kanno M.
Gene 129:249-255(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]"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] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Colon endothelium.
[3]"DNA sequence of human chromosome 17 and analysis of rearrangement in the human lineage."
Zody M.C., Garber M., Adams D.J., Sharpe T., Harrow J., Lupski J.R., Nicholson C., Searle S.M., Wilming L., Young S.K., Abouelleil A., Allen N.R., Bi W., Bloom T., Borowsky M.L., Bugalter B.E., Butler J., Chang J.L. expand/collapse author list , Chen C.-K., Cook A., Corum B., Cuomo C.A., de Jong P.J., DeCaprio D., Dewar K., FitzGerald M., Gilbert J., Gibson R., Gnerre S., Goldstein S., Grafham D.V., Grocock R., Hafez N., Hagopian D.S., Hart E., Norman C.H., Humphray S., Jaffe D.B., Jones M., Kamal M., Khodiyar V.K., LaButti K., Laird G., Lehoczky J., Liu X., Lokyitsang T., Loveland J., Lui A., Macdonald P., Major J.E., Matthews L., Mauceli E., McCarroll S.A., Mihalev A.H., Mudge J., Nguyen C., Nicol R., O'Leary S.B., Osoegawa K., Schwartz D.C., Shaw-Smith C., Stankiewicz P., Steward C., Swarbreck D., Venkataraman V., Whittaker C.A., Yang X., Zimmer A.R., Bradley A., Hubbard T., Birren B.W., Rogers J., Lander E.S., Nusbaum C.
Nature 440:1045-1049(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[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 (JUL-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] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Placenta and Uterus.
[6]"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] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-344, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[7]"Several distinct polycomb complexes regulate and co-localize on the INK4a tumor suppressor locus."
Maertens G.N., El Messaoudi-Aubert S., Racek T., Stock J.K., Nicholls J., Rodriguez-Niedenfuhr M., Gil J., Peters G.
PLoS ONE 4:E6380-E6380(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION IN A PRC1-LIKE COMPLEX, INTERACTION WITH CBX8; RING1 AND RNF2.
[8]"Interaction proteomics analysis of polycomb proteins defines distinct PRC1 Complexes in mammalian cells."
Vandamme J., Volkel P., Rosnoblet C., Le Faou P., Angrand P.O.
Mol. Cell. Proteomics 0:0-0(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION IN A PRC1-LIKE COMPLEX, SUBCELLULAR LOCATION.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
D13969 mRNA. Translation: BAA03074.1.
BX647429 mRNA. No translation available.
AC006449 Genomic DNA. No translation available.
CH471152 Genomic DNA. Translation: EAW60528.1.
BC004858 mRNA. Translation: AAH04858.1.
BC024255 mRNA. Translation: AAH24255.1.
CCDSCCDS32638.1.
PIRJN0717.
RefSeqNP_009075.1. NM_007144.2.
XP_005257697.1. XM_005257640.1.
XP_005257698.1. XM_005257641.2.
XP_005257699.1. XM_005257642.1.
XP_006722134.1. XM_006722071.1.
XP_006725405.1. XM_006725342.1.
XP_006725406.1. XM_006725343.1.
XP_006725407.1. XM_006725344.1.
XP_006725408.1. XM_006725345.1.
UniGeneHs.371617.
Hs.713595.

3D structure databases

ProteinModelPortalP35227.
SMRP35227. Positions 5-101.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid113497. 45 interactions.
DIPDIP-41880N.
IntActP35227. 27 interactions.
MINTMINT-158325.
STRING9606.ENSP00000354033.

PTM databases

PhosphoSiteP35227.

Polymorphism databases

DMDM462585.

Proteomic databases

MaxQBP35227.
PaxDbP35227.
PRIDEP35227.

Protocols and materials databases

DNASU7703.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000360797; ENSP00000354033; ENSG00000056661.
ENST00000580830; ENSP00000461961; ENSG00000056661.
ENST00000581345; ENSP00000463440; ENSG00000056661.
GeneID7703.
KEGGhsa:7703.
UCSCuc002hqp.1. human.

Organism-specific databases

CTD7703.
GeneCardsGC17M036890.
HGNCHGNC:12929. PCGF2.
HPAHPA047732.
MIM600346. gene.
neXtProtNX_P35227.
PharmGKBPA37516.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG304672.
HOGENOMHOG000231945.
HOVERGENHBG052826.
InParanoidP35227.
KOK11460.
OMAWAVESSC.
OrthoDBEOG77T14W.
PhylomeDBP35227.
TreeFamTF324206.

Gene expression databases

ArrayExpressP35227.
BgeeP35227.
CleanExHS_PCGF2.
GenevestigatorP35227.

Family and domain databases

Gene3D3.30.40.10. 1 hit.
InterProIPR018957. Znf_C3HC4_RING-type.
IPR001841. Znf_RING.
IPR013083. Znf_RING/FYVE/PHD.
IPR017907. Znf_RING_CS.
[Graphical view]
PfamPF00097. zf-C3HC4. 1 hit.
[Graphical view]
SMARTSM00184. RING. 1 hit.
[Graphical view]
PROSITEPS00518. ZF_RING_1. 1 hit.
PS50089. ZF_RING_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

GeneWikiPCGF2.
GenomeRNAi7703.
NextBio29858.
PROP35227.
SOURCESearch...

Entry information

Entry namePCGF2_HUMAN
AccessionPrimary (citable) accession number: P35227
Secondary accession number(s): A6NGD8
Entry history
Integrated into UniProtKB/Swiss-Prot: February 1, 1994
Last sequence update: February 1, 1994
Last modified: July 9, 2014
This is version 136 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 17

Human chromosome 17: entries, gene names and cross-references to MIM