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Q9BSM1 (PCGF1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 104. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Polycomb group RING finger protein 1
Alternative name(s):
Nervous system Polycomb-1
Short name=NSPc1
RING finger protein 68
Gene names
Name:PCGF1
Synonyms:NSPC1, RNF68
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length259 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Component of the Polycomb group (PcG) multiprotein BCOR complex, a complex required to maintain the transcriptionally repressive state of some genes, such as BCL6 and the cyclin-dependent kinase inhibitor, CDKN1A. Transcriptional repressor that may be targeted to the DNA by BCL6; this transcription repressor activity may be related to PKC signaling pathway. Represses CDKN1A expression by binding to its promoter, and this repression is dependent on the retinoic acid response element (RARE element). Promotes cell cycle progression and enhances cell proliferation as well. May have a positive role in tumor cell growth by down-regulating CDKN1A. 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. Ref.5 Ref.6 Ref.7

Subunit structure

Component of the repressive BCOR complex containing a Polycomb group subcomplex at least composed of RYBP, RING1 and RNF2/RING2. Specifically interacts with BCOR, RING1 and RNF2/RING2. Also interacts with BCORL1, the interaction is direct. Component of a PRC1-like complex. Interacts with CBX6, CBX7 and CBX8. Ref.6 Ref.9 Ref.10

Subcellular location

Nucleus Ref.5 Ref.9.

Tissue specificity

Ubiquitous. Ref.4

Sequence similarities

Contains 1 RING-type zinc finger.

Sequence caution

The sequence AAH04952.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.

The sequence AAP97183.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q9BSM1-1)

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: Q9BSM1-3)

The sequence of this isoform differs from the canonical sequence as follows:
     1-83: Missing.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.8
Chain2 – 259258Polycomb group RING finger protein 1
PRO_0000277855

Regions

Zinc finger47 – 8640RING-type
Region86 – 247162Required for repressor activity
Region167 – 25589Sufficient for interaction with BCOR and BCORL1

Amino acid modifications

Modified residue21N-acetylalanine Ref.8
Modified residue31Phosphoserine Ref.8

Natural variations

Alternative sequence1 – 8383Missing in isoform 2.
VSP_036393

Experimental info

Mutagenesis1091Y → F: Marked decrease of repressor activity. May be a kinase phosphorylation site. Ref.5
Mutagenesis1911Y → A: Abolishes interaction with BCOR and BCORL1. Ref.10
Mutagenesis1931R → A: Abolishes interaction with BCOR and BCORL1. Ref.10
Mutagenesis1951S → F: Abolishes repressor activity. May be a PKC phosphorylation site. Ref.5
Mutagenesis2061V → D: Abolishes interaction with BCOR and BCORL1. Ref.10

Secondary structure

................ 259
Helix Strand Turn

Details...

Sequences

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

Last modified February 10, 2009. Version 2.
Checksum: 456C9417E53A01B6

FASTA25930,346
        10         20         30         40         50         60 
MASPQGGQIA IAMRLRNQLQ SVYKMDPLRN EEEVRVKIKD LNEHIVCCLC AGYFVDATTI 

        70         80         90        100        110        120 
TECLHTFCKS CIVKYLQTSK YCPMCNIKIH ETQPLLNLKL DRVMQDIVYK LVPGLQDSEE 

       130        140        150        160        170        180 
KRIREFYQSR GLDRVTQPTG EEPALSNLGL PFSSFDHSKA HYYRYDEQLN LCLERLSSGK 

       190        200        210        220        230        240 
DKNKSVLQNK YVRCSVRAEV RHLRRVLCHR LMLNPQHVQL LFDNEVLPDH MTMKQIWLSR 

       250 
WFGKPSPLLL QYSVKEKRR 

« Hide

Isoform 2 [UniParc].

Checksum: 18CE151AA03179E4
Show »

FASTA17620,904

References

« Hide 'large scale' references
[1]"Cloning of a new human cDNA homology to human RNF3A mRNA."
Ding J.B., Yu L., Chu J.H., Ge H.P., Wang X.K., Zhao S.Y.
Submitted (JUL-2003) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
[2]"Generation and annotation of the DNA sequences of human chromosomes 2 and 4."
Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L., Du H. expand/collapse author list , Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K., McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C., Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S., Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H., Wilson R.K.
Nature 434:724-731(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[3]"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] OF 4-259 (ISOFORM 1).
Tissue: Uterus.
[4]"NSPc1, a novel mammalian Polycomb gene, is expressed in neural crest-derived structures of the peripheral nervous system."
Nunes M., Blanc I., Maes J., Fellous M., Robert B., McElreavey K.
Mech. Dev. 102:219-222(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: TISSUE SPECIFICITY.
[5]"NSPc1, a mainly nuclear localized protein of novel PcG family members, has a transcription repression activity related to its PKC phosphorylation site at S183."
Gong Y., Wang X., Liu J., Shi L., Yin B., Peng X., Qiang B., Yuan J.
FEBS Lett. 579:115-121(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, SUBCELLULAR LOCATION, REGION, MUTAGENESIS OF TYR-109 AND SER-195.
[6]"Polycomb group and SCF ubiquitin ligases are found in a novel BCOR complex that is recruited to BCL6 targets."
Gearhart M.D., Corcoran C.M., Wamstad J.A., Bardwell V.J.
Mol. Cell. Biol. 26:6880-6889(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, SUBUNIT.
[7]"NSPc1 is a cell growth regulator that acts as a transcriptional repressor of p21Waf1/Cip1 via the RARE element."
Gong Y., Yue J., Wu X., Wang X., Wen J., Lu L., Peng X., Qiang B., Yuan J.
Nucleic Acids Res. 34:6158-6169(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[8]"Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-3, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[9]"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, INTERACTION WITH CBX6; CBX7 AND CBX8, SUBCELLULAR LOCATION.
[10]"Structure of the polycomb group protein PCGF1 in complex with BCOR reveals basis for binding selectivity of PCGF homologs."
Junco S.E., Wang R., Gaipa J.C., Taylor A.B., Schirf V., Gearhart M.D., Bardwell V.J., Demeler B., Hart P.J., Kim C.A.
Structure 21:665-671(2013) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.85 ANGSTROMS) OF 167-255 IN COMPLEXES WITH BCOR AND BCORL1, INTERACTION WITH BCOR AND BCORL1, MUTAGENESIS OF TYR-191; ARG-193 AND VAL-206.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF087884 mRNA. Translation: AAP97183.1. Different initiation.
AC005041 Genomic DNA. No translation available.
BC004952 mRNA. Translation: AAH04952.1. Different initiation.
CCDSCCDS1946.2. [Q9BSM1-1]
RefSeqNP_116062.2. NM_032673.2. [Q9BSM1-1]
XP_005264675.1. XM_005264618.2. [Q9BSM1-3]
UniGeneHs.316750.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
4HPLX-ray2.00B167-255[»]
4HPMX-ray1.85B/D167-255[»]
ProteinModelPortalQ9BSM1.
SMRQ9BSM1. Positions 35-129, 167-254.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid124243. 24 interactions.
DIPDIP-52708N.
IntActQ9BSM1. 16 interactions.
MINTMINT-1460887.
STRING9606.ENSP00000233630.

PTM databases

PhosphoSiteQ9BSM1.

Polymorphism databases

DMDM223590124.

Proteomic databases

MaxQBQ9BSM1.
PaxDbQ9BSM1.
PRIDEQ9BSM1.

Protocols and materials databases

DNASU84759.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000233630; ENSP00000233630; ENSG00000115289. [Q9BSM1-1]
GeneID84759.
KEGGhsa:84759.
UCSCuc002sly.3. human. [Q9BSM1-1]

Organism-specific databases

CTD84759.
GeneCardsGC02M074732.
HGNCHGNC:17615. PCGF1.
HPAHPA011356.
MIM610231. gene.
neXtProtNX_Q9BSM1.
PharmGKBPA134976631.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG277991.
HOGENOMHOG000231946.
HOVERGENHBG052826.
InParanoidQ9BSM1.
KOK11487.
OMAFVRCSVR.
OrthoDBEOG754HQ5.
PhylomeDBQ9BSM1.
TreeFamTF324206.

Gene expression databases

BgeeQ9BSM1.
CleanExHS_PCGF1.
GenevestigatorQ9BSM1.

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

ChiTaRSPCGF1. human.
GeneWikiPCGF1.
GenomeRNAi84759.
NextBio74901.
PROQ9BSM1.
SOURCESearch...

Entry information

Entry namePCGF1_HUMAN
AccessionPrimary (citable) accession number: Q9BSM1
Secondary accession number(s): Q7Z506
Entry history
Integrated into UniProtKB/Swiss-Prot: February 20, 2007
Last sequence update: February 10, 2009
Last modified: July 9, 2014
This is version 104 of the entry and version 2 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

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

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

Human chromosome 2

Human chromosome 2: entries, gene names and cross-references to MIM