P35227 (PCGF2_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended 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

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	344 AA.
Sequence status	Complete.
Protein existence	Evidence 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 process	Transcription Transcription regulation
Cellular component	Nucleus
Domain	Zinc-finger
Ligand	DNA-binding Metal-binding Zinc
Molecular function	Repressor
PTM	Phosphoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	anterior/posterior pattern specification Inferred from electronic annotation. Source: Compara embryonic skeletal system morphogenesis Inferred from electronic annotation. Source: Compara histone acetylation Inferred from electronic annotation. Source: Compara in utero embryonic development Inferred from electronic annotation. Source: Compara negative regulation of apoptotic process Inferred from electronic annotation. Source: Compara negative regulation of transcription from RNA polymerase II promoter Inferred from mutant phenotype Ref.7. Source: UniProtKB protein ubiquitination Inferred from electronic annotation. Source: GOC transcription, DNA-dependent Inferred from electronic annotation. Source: UniProtKB-KW
Cellular_component	PRC1 complex Inferred from direct assay Ref.7. Source: UniProtKB nuclear body Inferred from electronic annotation. Source: Compara nuclear chromatin Inferred from direct assay Ref.7. Source: UniProtKB sex chromatin Inferred from electronic annotation. Source: Compara
Molecular_function	DNA binding Inferred from electronic annotation. Source: UniProtKB-KW chromatin binding Inferred from electronic annotation. Source: Compara sequence-specific DNA binding transcription factor activity Traceable author statement Ref.1. Source: ProtInc ubiquitin-protein ligase activity Inferred from electronic annotation. Source: Compara zinc ion binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
CBX7	O95931	3	EBI-2129767,EBI-3923843
CBX8	Q9HC52	6	EBI-2129767,EBI-712912
RING1	Q06587	4	EBI-2129767,EBI-752313
RNF2	Q99496	6	EBI-2129767,EBI-722416

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 344	344	Polycomb group RING finger protein 2		PRO_0000055984
Regions
	Zinc finger	18 – 57	40	RING-type
	Motif	81 – 95	15	Nuclear localization signal Potential
	Compositional bias	242 – 344	103	Pro/Ser-rich
Amino acid modifications
	Modified residue	344	1	Phosphothreonine Ref.6

Sequences

	Sequence		Length	Mass (Da)
	P35227 [UniParc]. Last modified February 1, 1994. Version 1. Checksum: A910BCD4C0CE9927	FASTA	344	37,788
	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

References

	« Hide 'large scale' referencesShow '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. , 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. , 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, MASS SPECTROMETRY. 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.
IPI	IPI00017302.
PIR	JN0717.
RefSeq	NP_009075.1. NM_007144.2.
UniGene	Hs.371617. Hs.713595.
3D structure databases
ProteinModelPortal	P35227.
ModBase	Search...
Protein-protein interaction databases
DIP	DIP-41880N.
IntAct	P35227. 22 interactions.
MINT	MINT-158325.
STRING	9606.ENSP00000354033.
PTM databases
PhosphoSite	P35227.
Polymorphism databases
DMDM	462585.
Proteomic databases
PaxDb	P35227.
PRIDE	P35227.
Protocols and materials databases
DNASU	7703.
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000360797; ENSP00000354033; ENSG00000056661. ENST00000580830; ENSP00000461961; ENSG00000056661. ENST00000581345; ENSP00000463440; ENSG00000056661.
GeneID	7703.
KEGG	hsa:7703.
UCSC	uc002hqp.1. human.
Organism-specific databases
CTD	7703.
GeneCards	GC17M036890.
HGNC	HGNC:12929. PCGF2.
HPA	HPA047732.
MIM	600346. gene.
neXtProt	NX_P35227.
PharmGKB	PA37516.
GenAtlas	Search...
Phylogenomic databases
eggNOG	NOG304672.
HOGENOM	HOG000231945.
HOVERGEN	HBG052826.
InParanoid	P35227.
KO	K11460.
OMA	DRDEKKG.
OrthoDB	EOG4KSPKG.
Gene expression databases
Bgee	P35227.
CleanEx	HS_PCGF2.
Genevestigator	P35227.
GermOnline	ENSG00000056661. Homo sapiens.
Family and domain databases
Gene3D	3.30.40.10. 1 hit.
InterPro	IPR018957. Znf_C3HC4_RING-type. IPR001841. Znf_RING. IPR013083. Znf_RING/FYVE/PHD. IPR017907. Znf_RING_CS. [Graphical view]
Pfam	PF00097. zf-C3HC4. 1 hit. [Graphical view]
SMART	SM00184. RING. 1 hit. [Graphical view]
PROSITE	PS00518. ZF_RING_1. 1 hit. PS50089. ZF_RING_2. 1 hit. [Graphical view]
ProtoNet	Search...
Other
GenomeRNAi	7703.
NextBio	29858.
SOURCE	Search...

Entry information

Entry name

PCGF2_HUMAN

Accession

Primary (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:	May 1, 2013
This is version 125 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.