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Q9BSM1

- PCGF1_HUMAN

UniProt

Q9BSM1 - PCGF1_HUMAN

Protein

Polycomb group RING finger protein 1

Gene

PCGF1

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 105 (01 Oct 2014)
      Sequence version 2 (10 Feb 2009)
      Previous versions | rss
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    Functioni

    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.3 Publications

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Zinc fingeri47 – 8640RING-typePROSITE-ProRule annotationAdd
    BLAST

    GO - Molecular functioni

    1. protein binding Source: IntAct
    2. protein C-terminus binding Source: UniProtKB
    3. zinc ion binding Source: InterPro

    GO - Biological processi

    1. histone H2A monoubiquitination Source: UniProtKB
    2. regulation of transcription, DNA-templated Source: UniProtKB-KW
    3. transcription, DNA-templated Source: UniProtKB-KW

    Keywords - Molecular functioni

    Repressor

    Keywords - Biological processi

    Transcription, Transcription regulation

    Keywords - Ligandi

    Metal-binding, Zinc

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Polycomb group RING finger protein 1
    Alternative name(s):
    Nervous system Polycomb-1
    Short name:
    NSPc1
    RING finger protein 68
    Gene namesi
    Name:PCGF1
    Synonyms:NSPC1, RNF68
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 2

    Organism-specific databases

    HGNCiHGNC:17615. PCGF1.

    Subcellular locationi

    Nucleus 2 Publications

    GO - Cellular componenti

    1. nucleus Source: UniProtKB
    2. PcG protein complex Source: UniProtKB

    Keywords - Cellular componenti

    Nucleus

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi109 – 1091Y → F: Marked decrease of repressor activity. May be a kinase phosphorylation site. 1 Publication
    Mutagenesisi191 – 1911Y → A: Abolishes interaction with BCOR and BCORL1. 1 Publication
    Mutagenesisi193 – 1931R → A: Abolishes interaction with BCOR and BCORL1. 1 Publication
    Mutagenesisi195 – 1951S → F: Abolishes repressor activity. May be a PKC phosphorylation site. 1 Publication
    Mutagenesisi206 – 2061V → D: Abolishes interaction with BCOR and BCORL1. 1 Publication

    Organism-specific databases

    PharmGKBiPA134976631.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed1 Publication
    Chaini2 – 259258Polycomb group RING finger protein 1PRO_0000277855Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei2 – 21N-acetylalanine1 Publication
    Modified residuei3 – 31Phosphoserine1 Publication

    Keywords - PTMi

    Acetylation, Phosphoprotein

    Proteomic databases

    MaxQBiQ9BSM1.
    PaxDbiQ9BSM1.
    PRIDEiQ9BSM1.

    PTM databases

    PhosphoSiteiQ9BSM1.

    Expressioni

    Tissue specificityi

    Ubiquitous.1 Publication

    Gene expression databases

    BgeeiQ9BSM1.
    CleanExiHS_PCGF1.
    GenevestigatoriQ9BSM1.

    Organism-specific databases

    HPAiHPA011356.

    Interactioni

    Subunit structurei

    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 CBX8.3 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    BCORQ6W2J96EBI-749901,EBI-950027
    CBX8Q9HC522EBI-749901,EBI-712912
    RING1Q065875EBI-749901,EBI-752313
    RNF2Q994964EBI-749901,EBI-722416

    Protein-protein interaction databases

    BioGridi124243. 24 interactions.
    DIPiDIP-52708N.
    IntActiQ9BSM1. 16 interactions.
    MINTiMINT-1460887.
    STRINGi9606.ENSP00000233630.

    Structurei

    Secondary structure

    1
    259
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi168 – 1769
    Beta strandi191 – 1955
    Helixi200 – 21112
    Helixi215 – 2173
    Beta strandi219 – 2224
    Helixi233 – 2408
    Turni241 – 2433
    Beta strandi246 – 2538

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    4HPLX-ray2.00B167-255[»]
    4HPMX-ray1.85B/D167-255[»]
    ProteinModelPortaliQ9BSM1.
    SMRiQ9BSM1. Positions 35-129, 167-254.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni86 – 247162Required for repressor activityAdd
    BLAST
    Regioni167 – 25589Sufficient for interaction with BCOR and BCORL1Add
    BLAST

    Sequence similaritiesi

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

    Zinc finger

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Zinc fingeri47 – 8640RING-typePROSITE-ProRule annotationAdd
    BLAST

    Keywords - Domaini

    Zinc-finger

    Phylogenomic databases

    eggNOGiNOG277991.
    HOGENOMiHOG000231946.
    HOVERGENiHBG052826.
    InParanoidiQ9BSM1.
    KOiK11487.
    OMAiFVRCSVR.
    OrthoDBiEOG754HQ5.
    PhylomeDBiQ9BSM1.
    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]

    Sequences (2)i

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    This entry describes 2 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: Q9BSM1-1) [UniParc]FASTAAdd to Basket

    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.

    « Hide

    MASPQGGQIA IAMRLRNQLQ SVYKMDPLRN EEEVRVKIKD LNEHIVCCLC    50
    AGYFVDATTI TECLHTFCKS CIVKYLQTSK YCPMCNIKIH ETQPLLNLKL 100
    DRVMQDIVYK LVPGLQDSEE KRIREFYQSR GLDRVTQPTG EEPALSNLGL 150
    PFSSFDHSKA HYYRYDEQLN LCLERLSSGK DKNKSVLQNK YVRCSVRAEV 200
    RHLRRVLCHR LMLNPQHVQL LFDNEVLPDH MTMKQIWLSR WFGKPSPLLL 250
    QYSVKEKRR 259
    Length:259
    Mass (Da):30,346
    Last modified:February 10, 2009 - v2
    Checksum:i456C9417E53A01B6
    GO
    Isoform 2 (identifier: Q9BSM1-3) [UniParc]FASTAAdd to Basket

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

    Show »
    Length:176
    Mass (Da):20,904
    Checksum:i18CE151AA03179E4
    GO

    Sequence cautioni

    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 sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 8383Missing in isoform 2. 1 PublicationVSP_036393Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF087884 mRNA. Translation: AAP97183.1. Different initiation.
    AC005041 Genomic DNA. No translation available.
    BC004952 mRNA. Translation: AAH04952.1. Different initiation.
    CCDSiCCDS1946.2. [Q9BSM1-1]
    RefSeqiNP_116062.2. NM_032673.2. [Q9BSM1-1]
    XP_005264675.1. XM_005264618.2. [Q9BSM1-3]
    UniGeneiHs.316750.

    Genome annotation databases

    EnsembliENST00000233630; ENSP00000233630; ENSG00000115289. [Q9BSM1-1]
    GeneIDi84759.
    KEGGihsa:84759.
    UCSCiuc002sly.3. human. [Q9BSM1-1]

    Polymorphism databases

    DMDMi223590124.

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF087884 mRNA. Translation: AAP97183.1 . Different initiation.
    AC005041 Genomic DNA. No translation available.
    BC004952 mRNA. Translation: AAH04952.1 . Different initiation.
    CCDSi CCDS1946.2. [Q9BSM1-1 ]
    RefSeqi NP_116062.2. NM_032673.2. [Q9BSM1-1 ]
    XP_005264675.1. XM_005264618.2. [Q9BSM1-3 ]
    UniGenei Hs.316750.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    4HPL X-ray 2.00 B 167-255 [» ]
    4HPM X-ray 1.85 B/D 167-255 [» ]
    ProteinModelPortali Q9BSM1.
    SMRi Q9BSM1. Positions 35-129, 167-254.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 124243. 24 interactions.
    DIPi DIP-52708N.
    IntActi Q9BSM1. 16 interactions.
    MINTi MINT-1460887.
    STRINGi 9606.ENSP00000233630.

    PTM databases

    PhosphoSitei Q9BSM1.

    Polymorphism databases

    DMDMi 223590124.

    Proteomic databases

    MaxQBi Q9BSM1.
    PaxDbi Q9BSM1.
    PRIDEi Q9BSM1.

    Protocols and materials databases

    DNASUi 84759.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000233630 ; ENSP00000233630 ; ENSG00000115289 . [Q9BSM1-1 ]
    GeneIDi 84759.
    KEGGi hsa:84759.
    UCSCi uc002sly.3. human. [Q9BSM1-1 ]

    Organism-specific databases

    CTDi 84759.
    GeneCardsi GC02M074732.
    HGNCi HGNC:17615. PCGF1.
    HPAi HPA011356.
    MIMi 610231. gene.
    neXtProti NX_Q9BSM1.
    PharmGKBi PA134976631.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG277991.
    HOGENOMi HOG000231946.
    HOVERGENi HBG052826.
    InParanoidi Q9BSM1.
    KOi K11487.
    OMAi FVRCSVR.
    OrthoDBi EOG754HQ5.
    PhylomeDBi Q9BSM1.
    TreeFami TF324206.

    Miscellaneous databases

    ChiTaRSi PCGF1. human.
    GeneWikii PCGF1.
    GenomeRNAii 84759.
    NextBioi 74901.
    PROi Q9BSM1.
    SOURCEi Search...

    Gene expression databases

    Bgeei Q9BSM1.
    CleanExi HS_PCGF1.
    Genevestigatori Q9BSM1.

    Family and domain databases

    Gene3Di 3.30.40.10. 1 hit.
    InterProi IPR018957. Znf_C3HC4_RING-type.
    IPR001841. Znf_RING.
    IPR013083. Znf_RING/FYVE/PHD.
    IPR017907. Znf_RING_CS.
    [Graphical view ]
    Pfami PF00097. zf-C3HC4. 1 hit.
    [Graphical view ]
    SMARTi SM00184. RING. 1 hit.
    [Graphical view ]
    PROSITEi PS00518. ZF_RING_1. 1 hit.
    PS50089. ZF_RING_2. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    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.
      , 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.

    Entry informationi

    Entry nameiPCGF1_HUMAN
    AccessioniPrimary (citable) accession number: Q9BSM1
    Secondary accession number(s): Q7Z506
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: February 20, 2007
    Last sequence update: February 10, 2009
    Last modified: October 1, 2014
    This is version 105 of the entry and version 2 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

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. Human chromosome 2
      Human chromosome 2: 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. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    4. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3