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Protein

Polycomb group RING finger protein 2

Gene

PCGF2

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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).By similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri18 – 5740RING-typePROSITE-ProRule annotationAdd
BLAST

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Repressor

Keywords - Biological processi

Transcription, Transcription regulation

Keywords - Ligandi

DNA-binding, Metal-binding, Zinc

Enzyme and pathway databases

ReactomeiREACT_355174. SUMOylation of DNA damage response and repair proteins.

Names & Taxonomyi

Protein namesi
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 namesi
Name:PCGF2
Synonyms:MEL18, RNF110, ZNF144
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componentsi: Chromosome 17, Unplaced

Organism-specific databases

HGNCiHGNC:12929. PCGF2.

Subcellular locationi

GO - Cellular componenti

  • nuclear body Source: Ensembl
  • nuclear chromatin Source: UniProtKB
  • nucleoplasm Source: HPA
  • nucleus Source: UniProtKB
  • PcG protein complex Source: UniProtKB
  • PRC1 complex Source: UniProtKB
  • sex chromatin Source: Ensembl
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA37516.

Polymorphism and mutation databases

BioMutaiPCGF2.
DMDMi462585.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 344344Polycomb group RING finger protein 2PRO_0000055984Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei344 – 3441Phosphothreonine1 Publication

Post-translational modificationi

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

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiP35227.
PaxDbiP35227.
PRIDEiP35227.

PTM databases

PhosphoSiteiP35227.

Expressioni

Tissue specificityi

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

Gene expression databases

BgeeiP35227.
CleanExiHS_PCGF2.
ExpressionAtlasiP35227. baseline and differential.
GenevisibleiP35227. HS.

Organism-specific databases

HPAiHPA047732.
HPA063531.

Interactioni

Subunit structurei

Exists as both a monomer and homodimer (By similarity). Component of a PRC1-like complex. Interacts WITH CBX8, RING1 AND RNF2.By similarity2 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
CBX7O959313EBI-2129767,EBI-3923843
CBX8Q9HC527EBI-2129767,EBI-712912
PHC2Q8IXK06EBI-2129767,EBI-713786
RING1Q065875EBI-2129767,EBI-752313
RNF2Q994967EBI-2129767,EBI-722416
UBCP0CG482EBI-2129767,EBI-3390054
USP11P517845EBI-2129767,EBI-306876
USP7Q930095EBI-2129767,EBI-302474

Protein-protein interaction databases

BioGridi113497. 45 interactions.
DIPiDIP-41880N.
IntActiP35227. 27 interactions.
MINTiMINT-158325.
STRINGi9606.ENSP00000354033.

Structurei

3D structure databases

ProteinModelPortaliP35227.
SMRiP35227. Positions 3-101.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi81 – 9515Nuclear localization signalSequence AnalysisAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi242 – 344103Pro/Ser-richAdd
BLAST

Sequence similaritiesi

Contains 1 RING-type zinc finger.PROSITE-ProRule annotation

Zinc finger

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri18 – 5740RING-typePROSITE-ProRule annotationAdd
BLAST

Keywords - Domaini

Zinc-finger

Phylogenomic databases

eggNOGiNOG304672.
GeneTreeiENSGT00550000074463.
HOGENOMiHOG000231945.
HOVERGENiHBG052826.
InParanoidiP35227.
KOiK11460.
OMAiKGPLENG.
OrthoDBiEOG77T14W.
PhylomeDBiP35227.
TreeFamiTF324206.

Family and domain databases

Gene3Di3.30.40.10. 1 hit.
InterProiIPR018957. Znf_C3HC4_RING-type.
IPR001841. Znf_RING.
IPR013083. Znf_RING/FYVE/PHD.
IPR017907. Znf_RING_CS.
[Graphical view]
PfamiPF00097. zf-C3HC4. 1 hit.
[Graphical view]
SMARTiSM00184. RING. 1 hit.
[Graphical view]
PROSITEiPS00518. ZF_RING_1. 1 hit.
PS50089. ZF_RING_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P35227-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MHRTTRIKIT ELNPHLMCAL CGGYFIDATT IVECLHSFCK TCIVRYLETN
60 70 80 90 100
KYCPMCDVQV HKTRPLLSIR SDKTLQDIVY KLVPGLFKDE MKRRRDFYAA
110 120 130 140 150
YPLTEVPNGS NEDRGEVLEQ EKGALSDDEI VSLSIEFYEG ARDRDEKKGP
160 170 180 190 200
LENGDGDKEK TGVRFLRCPA AMTVMHLAKF LRNKMDVPSK YKVEVLYEDE
210 220 230 240 250
PLKEYYTLMD IAYIYPWRRN GPLPLKYRVQ PACKRLTLAT VPTPSEGTNT
260 270 280 290 300
SGASECESVS DKAPSPATLP ATSSSLPSPA TPSHGSPSSH GPPATHPTSP
310 320 330 340
TPPSTASGAT TAANGGSLNC LQTPSSTSRG RKMTVNGAPV PPLT
Length:344
Mass (Da):37,788
Last modified:February 1, 1994 - v1
Checksum:iA910BCD4C0CE9927
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS32638.1.
PIRiJN0717.
RefSeqiNP_009075.1. NM_007144.2.
XP_005257697.1. XM_005257640.1.
XP_005257698.1. XM_005257641.3.
XP_005257699.1. XM_005257642.2.
XP_006725405.1. XM_006725342.1.
XP_006725407.1. XM_006725344.2.
XP_006725408.1. XM_006725345.2.
UniGeneiHs.371617.
Hs.713595.

Genome annotation databases

EnsembliENST00000610440; ENSP00000478517; ENSG00000278644.
ENST00000611883; ENSP00000478970; ENSG00000277258.
ENST00000616199; ENSP00000482063; ENSG00000277258.
ENST00000620225; ENSP00000482815; ENSG00000277258.
GeneIDi7703.
KEGGihsa:7703.
UCSCiuc002hqp.1. human.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS32638.1.
PIRiJN0717.
RefSeqiNP_009075.1. NM_007144.2.
XP_005257697.1. XM_005257640.1.
XP_005257698.1. XM_005257641.3.
XP_005257699.1. XM_005257642.2.
XP_006725405.1. XM_006725342.1.
XP_006725407.1. XM_006725344.2.
XP_006725408.1. XM_006725345.2.
UniGeneiHs.371617.
Hs.713595.

3D structure databases

ProteinModelPortaliP35227.
SMRiP35227. Positions 3-101.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi113497. 45 interactions.
DIPiDIP-41880N.
IntActiP35227. 27 interactions.
MINTiMINT-158325.
STRINGi9606.ENSP00000354033.

PTM databases

PhosphoSiteiP35227.

Polymorphism and mutation databases

BioMutaiPCGF2.
DMDMi462585.

Proteomic databases

MaxQBiP35227.
PaxDbiP35227.
PRIDEiP35227.

Protocols and materials databases

DNASUi7703.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000610440; ENSP00000478517; ENSG00000278644.
ENST00000611883; ENSP00000478970; ENSG00000277258.
ENST00000616199; ENSP00000482063; ENSG00000277258.
ENST00000620225; ENSP00000482815; ENSG00000277258.
GeneIDi7703.
KEGGihsa:7703.
UCSCiuc002hqp.1. human.

Organism-specific databases

CTDi7703.
GeneCardsiGC17M036890.
HGNCiHGNC:12929. PCGF2.
HPAiHPA047732.
HPA063531.
MIMi600346. gene.
neXtProtiNX_P35227.
PharmGKBiPA37516.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiNOG304672.
GeneTreeiENSGT00550000074463.
HOGENOMiHOG000231945.
HOVERGENiHBG052826.
InParanoidiP35227.
KOiK11460.
OMAiKGPLENG.
OrthoDBiEOG77T14W.
PhylomeDBiP35227.
TreeFamiTF324206.

Enzyme and pathway databases

ReactomeiREACT_355174. SUMOylation of DNA damage response and repair proteins.

Miscellaneous databases

ChiTaRSiPCGF2. human.
GeneWikiiPCGF2.
GenomeRNAii7703.
NextBioi29858.
PROiP35227.
SOURCEiSearch...

Gene expression databases

BgeeiP35227.
CleanExiHS_PCGF2.
ExpressionAtlasiP35227. baseline and differential.
GenevisibleiP35227. HS.

Family and domain databases

Gene3Di3.30.40.10. 1 hit.
InterProiIPR018957. Znf_C3HC4_RING-type.
IPR001841. Znf_RING.
IPR013083. Znf_RING/FYVE/PHD.
IPR017907. Znf_RING_CS.
[Graphical view]
PfamiPF00097. zf-C3HC4. 1 hit.
[Graphical view]
SMARTiSM00184. RING. 1 hit.
[Graphical view]
PROSITEiPS00518. ZF_RING_1. 1 hit.
PS50089. ZF_RING_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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. 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. 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. 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.

Entry informationi

Entry nameiPCGF2_HUMAN
AccessioniPrimary (citable) accession number: P35227
Secondary accession number(s): A6NGD8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 1994
Last sequence update: February 1, 1994
Last modified: June 24, 2015
This is version 146 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (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.

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Human chromosome 17
    Human chromosome 17: entries, gene names and cross-references to MIM
  2. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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 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.