GenomeNet

Database: UniProt
Entry: Q86SE9
LinkDB: Q86SE9
Original site: Q86SE9 
ID   PCGF5_HUMAN             Reviewed;         256 AA.
AC   Q86SE9; B7Z892; D3DR33; Q6PK47; Q86TD0;
DT   20-FEB-2007, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2003, sequence version 1.
DT   12-AUG-2020, entry version 150.
DE   RecName: Full=Polycomb group RING finger protein 5;
DE   AltName: Full=RING finger protein 159;
GN   Name=PCGF5; Synonyms=RNF159;
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Homo.
OX   NCBI_TaxID=9606;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   TISSUE=Testis;
RX   PubMed=14702039; DOI=10.1038/ng1285;
RA   Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA   Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA   Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA   Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA   Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA   Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA   Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA   Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA   Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA   Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA   Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA   Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA   Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA   Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA   Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA   Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA   Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA   Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA   Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA   Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA   Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA   Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA   Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA   Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA   Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA   Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA   Isogai T., Sugano S.;
RT   "Complete sequencing and characterization of 21,243 full-length human
RT   cDNAs.";
RL   Nat. Genet. 36:40-45(2004).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   TISSUE=Endometrial adenocarcinoma, and Skeletal muscle;
RX   PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA   Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA   Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D.,
RA   Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A.,
RA   Wiemann S., Schupp I.;
RT   "The full-ORF clone resource of the German cDNA consortium.";
RL   BMC Genomics 8:399-399(2007).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA   Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA   Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA   Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA   Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA   Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA   Hunkapiller M.W., Myers E.W., Venter J.C.;
RL   Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC   TISSUE=Brain, and Pancreas;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA project:
RT   the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [5]
RP   IDENTIFICATION IN A PRC1-LIKE COMPLEX, INTERACTION WITH CBX6; CBX7 AND
RP   CBX8, AND SUBCELLULAR LOCATION.
RX   PubMed=21282530; DOI=10.1074/mcp.m110.002642;
RA   Vandamme J., Volkel P., Rosnoblet C., Le Faou P., Angrand P.O.;
RT   "Interaction proteomics analysis of polycomb proteins defines distinct PRC1
RT   Complexes in mammalian cells.";
RL   Mol. Cell. Proteomics 0:0-0(2011).
RN   [6]
RP   IDENTIFICATION IN A COMPLEX WITH AUTS2; RNF2; CSNK2B AND RYBP, AND
RP   SUBCELLULAR LOCATION.
RX   PubMed=25519132; DOI=10.1038/nature13921;
RA   Gao Z., Lee P., Stafford J.M., von Schimmelmann M., Schaefer A.,
RA   Reinberg D.;
RT   "An AUTS2-polycomb complex activates gene expression in the CNS.";
RL   Nature 516:349-354(2014).
RN   [7] {ECO:0000244|PDB:4S3O}
RP   X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS) OF 1-109 IN COMPLEX WITH ZINC IONS;
RP   UBE2D3 AND RNF2, SUBUNIT, AND FUNCTION.
RX   PubMed=26151332; DOI=10.1038/ncomms8621;
RA   Taherbhoy A.M., Huang O.W., Cochran A.G.;
RT   "BMI1-RING1B is an autoinhibited RING E3 ubiquitin ligase.";
RL   Nat. Commun. 6:7621-7621(2015).
CC   -!- FUNCTION: Component of a Polycomb group (PcG) multiprotein PRC1-like
CC       complex, a complex class required to maintain the transcriptionally
CC       repressive state of many genes, including Hox genes, throughout
CC       development. PcG PRC1 complex acts via chromatin remodeling and
CC       modification of histones; it mediates monoubiquitination of histone H2A
CC       'Lys-119', rendering chromatin heritably changed in its expressibility
CC       (PubMed:26151332). Within the PRC1-like complex, regulates RNF2
CC       ubiquitin ligase activity (PubMed:26151332). Plays a redundant role
CC       with PCGF3 as part of a PRC1-like complex that mediates
CC       monoubiquitination of histone H2A 'Lys-119' on the X chromosome and is
CC       required for normal silencing of one copy of the X chromosome in XX
CC       females (By similarity). {ECO:0000250|UniProtKB:Q3UK78,
CC       ECO:0000269|PubMed:26151332}.
CC   -!- SUBUNIT: Component of a PRC1-like complex that contains PCGF5, RNF2 and
CC       UBE2D3 (PubMed:21282530, PubMed:26151332). Interacts with RNF2; the
CC       interaction is direct (PubMed:26151332). Interacts with CBX6, CBX7 and
CC       CBX8 (PubMed:21282530). Interacts with AUTS2; the interaction is direct
CC       (PubMed:25519132). Identified in a complex that contains AUTS2, PCGF5,
CC       CSNK2B and RNF2 (PubMed:25519132). {ECO:0000269|PubMed:21282530,
CC       ECO:0000269|PubMed:25519132}.
CC   -!- INTERACTION:
CC       Q86SE9; Q8WXX7: AUTS2; NbExp=7; IntAct=EBI-2827999, EBI-2875359;
CC       Q86SE9; Q6W2J9-4: BCOR; NbExp=3; IntAct=EBI-2827999, EBI-10208579;
CC       Q86SE9; Q9HC52: CBX8; NbExp=4; IntAct=EBI-2827999, EBI-712912;
CC       Q86SE9; Q8IXK0: PHC2; NbExp=3; IntAct=EBI-2827999, EBI-713786;
CC       Q86SE9; Q96LA8: PRMT6; NbExp=2; IntAct=EBI-2827999, EBI-912440;
CC       Q86SE9; Q06587: RING1; NbExp=7; IntAct=EBI-2827999, EBI-752313;
CC       Q86SE9; Q99496: RNF2; NbExp=8; IntAct=EBI-2827999, EBI-722416;
CC       Q86SE9; Q12933: TRAF2; NbExp=3; IntAct=EBI-2827999, EBI-355744;
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:21282530,
CC       ECO:0000269|PubMed:25519132}. Nucleus, nucleoplasm
CC       {ECO:0000250|UniProtKB:Q3UK78}. Note=Recruited by the non-coding RNA
CC       Xist to specific nuclear foci that probably correspond to the
CC       inactivated X chromosome. {ECO:0000250|UniProtKB:Q3UK78}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q86SE9-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q86SE9-2; Sequence=VSP_023118, VSP_023119;
DR   EMBL; AK303014; BAH13878.1; -; mRNA.
DR   EMBL; AL832003; CAD89905.1; -; mRNA.
DR   EMBL; AL832496; CAD91165.1; -; mRNA.
DR   EMBL; CH471066; EAW50112.1; -; Genomic_DNA.
DR   EMBL; CH471066; EAW50113.1; -; Genomic_DNA.
DR   EMBL; BC007377; AAH07377.1; -; mRNA.
DR   EMBL; BC051845; AAH51845.1; -; mRNA.
DR   CCDS; CCDS7413.1; -. [Q86SE9-1]
DR   RefSeq; NP_001243478.1; NM_001256549.1. [Q86SE9-1]
DR   RefSeq; NP_001244030.1; NM_001257101.1. [Q86SE9-1]
DR   RefSeq; NP_115749.2; NM_032373.4. [Q86SE9-1]
DR   RefSeq; XP_011538573.1; XM_011540271.2. [Q86SE9-1]
DR   RefSeq; XP_016872265.1; XM_017016776.1. [Q86SE9-1]
DR   PDB; 4S3O; X-ray; 2.00 A; C/F=1-109.
DR   PDBsum; 4S3O; -.
DR   SMR; Q86SE9; -.
DR   BioGRID; 124057; 62.
DR   DIP; DIP-61356N; -.
DR   IntAct; Q86SE9; 48.
DR   MINT; Q86SE9; -.
DR   STRING; 9606.ENSP00000445704; -.
DR   PhosphoSitePlus; Q86SE9; -.
DR   BioMuta; PCGF5; -.
DR   DMDM; 74750353; -.
DR   EPD; Q86SE9; -.
DR   jPOST; Q86SE9; -.
DR   MassIVE; Q86SE9; -.
DR   MaxQB; Q86SE9; -.
DR   PaxDb; Q86SE9; -.
DR   PeptideAtlas; Q86SE9; -.
DR   PRIDE; Q86SE9; -.
DR   ProteomicsDB; 69577; -. [Q86SE9-1]
DR   ProteomicsDB; 69578; -. [Q86SE9-2]
DR   Antibodypedia; 30344; 37 antibodies.
DR   DNASU; 84333; -.
DR   Ensembl; ENST00000336126; ENSP00000337500; ENSG00000180628. [Q86SE9-1]
DR   Ensembl; ENST00000543648; ENSP00000445704; ENSG00000180628. [Q86SE9-1]
DR   Ensembl; ENST00000614189; ENSP00000479492; ENSG00000180628. [Q86SE9-1]
DR   GeneID; 84333; -.
DR   KEGG; hsa:84333; -.
DR   UCSC; uc001khh.5; human. [Q86SE9-1]
DR   CTD; 84333; -.
DR   DisGeNET; 84333; -.
DR   EuPathDB; HostDB:ENSG00000180628.14; -.
DR   GeneCards; PCGF5; -.
DR   HGNC; HGNC:28264; PCGF5.
DR   HPA; ENSG00000180628; Low tissue specificity.
DR   MIM; 617407; gene.
DR   neXtProt; NX_Q86SE9; -.
DR   OpenTargets; ENSG00000180628; -.
DR   PharmGKB; PA134929149; -.
DR   eggNOG; KOG2660; Eukaryota.
DR   GeneTree; ENSGT00940000155896; -.
DR   HOGENOM; CLU_046427_4_1_1; -.
DR   InParanoid; Q86SE9; -.
DR   KO; K11489; -.
DR   OMA; ICLDCLH; -.
DR   OrthoDB; 1203951at2759; -.
DR   PhylomeDB; Q86SE9; -.
DR   TreeFam; TF324206; -.
DR   PathwayCommons; Q86SE9; -.
DR   Reactome; R-HSA-8939243; RUNX1 interacts with co-factors whose precise effect on RUNX1 targets is not known.
DR   BioGRID-ORCS; 84333; 3 hits in 872 CRISPR screens.
DR   ChiTaRS; PCGF5; human.
DR   GeneWiki; PCGF5; -.
DR   GenomeRNAi; 84333; -.
DR   Pharos; Q86SE9; Tdark.
DR   PRO; PR:Q86SE9; -.
DR   Proteomes; UP000005640; Chromosome 10.
DR   RNAct; Q86SE9; protein.
DR   Bgee; ENSG00000180628; Expressed in substantia nigra and 223 other tissues.
DR   Genevisible; Q86SE9; HS.
DR   GO; GO:0005813; C:centrosome; IDA:LIFEdb.
DR   GO; GO:0005654; C:nucleoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR   GO; GO:0031519; C:PcG protein complex; IDA:UniProtKB.
DR   GO; GO:0035102; C:PRC1 complex; IBA:GO_Central.
DR   GO; GO:0000805; C:X chromosome; IEA:Ensembl.
DR   GO; GO:0003700; F:DNA-binding transcription factor activity; IBA:GO_Central.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0000977; F:RNA polymerase II transcription regulatory region sequence-specific DNA binding; IBA:GO_Central.
DR   GO; GO:0036353; P:histone H2A-K119 monoubiquitination; ISS:UniProtKB.
DR   GO; GO:0060819; P:inactivation of X chromosome by genetic imprinting; ISS:UniProtKB.
DR   GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IDA:MGI.
DR   Gene3D; 3.30.40.10; -; 1.
DR   InterPro; IPR032443; RAWUL.
DR   InterPro; IPR001841; Znf_RING.
DR   InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR   InterPro; IPR017907; Znf_RING_CS.
DR   Pfam; PF16207; RAWUL; 1.
DR   SMART; SM00184; RING; 1.
DR   PROSITE; PS00518; ZF_RING_1; 1.
DR   PROSITE; PS50089; ZF_RING_2; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Alternative splicing; Metal-binding; Nucleus;
KW   Reference proteome; Repressor; Transcription; Transcription regulation;
KW   Zinc; Zinc-finger.
FT   CHAIN           1..256
FT                   /note="Polycomb group RING finger protein 5"
FT                   /id="PRO_0000277868"
FT   ZN_FING         18..57
FT                   /note="RING-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00175,
FT                   ECO:0000269|PubMed:26151332"
FT   VAR_SEQ         38..49
FT                   /note="FCKTCIVQHFED -> SAESYWMSTWMS (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:15489334"
FT                   /id="VSP_023118"
FT   VAR_SEQ         50..256
FT                   /note="Missing (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:15489334"
FT                   /id="VSP_023119"
FT   HELIX           9..12
FT                   /evidence="ECO:0000244|PDB:4S3O"
FT   HELIX           13..16
FT                   /evidence="ECO:0000244|PDB:4S3O"
FT   TURN            19..21
FT                   /evidence="ECO:0000244|PDB:4S3O"
FT   STRAND          22..24
FT                   /evidence="ECO:0000244|PDB:4S3O"
FT   STRAND          26..31
FT                   /evidence="ECO:0000244|PDB:4S3O"
FT   TURN            32..35
FT                   /evidence="ECO:0000244|PDB:4S3O"
FT   STRAND          36..39
FT                   /evidence="ECO:0000244|PDB:4S3O"
FT   HELIX           40..46
FT                   /evidence="ECO:0000244|PDB:4S3O"
FT   TURN            47..49
FT                   /evidence="ECO:0000244|PDB:4S3O"
FT   TURN            54..56
FT                   /evidence="ECO:0000244|PDB:4S3O"
FT   HELIX           65..68
FT                   /evidence="ECO:0000244|PDB:4S3O"
FT   STRAND          69..71
FT                   /evidence="ECO:0000244|PDB:4S3O"
FT   HELIX           73..82
FT                   /evidence="ECO:0000244|PDB:4S3O"
FT   HELIX           86..98
FT                   /evidence="ECO:0000244|PDB:4S3O"
SQ   SEQUENCE   256 AA;  29714 MW;  E5AC78F2A3BBBED5 CRC64;
     MATQRKHLVK DFNPYITCYI CKGYLIKPTT VTECLHTFCK TCIVQHFEDS NDCPRCGNQV
     HETNPLEMLR LDNTLEEIIF KLVPGLREQE LERESEFWKK NKPQENGQDD TSKADKPKVD
     EEGDENEDDK DYHRSDPQIA ICLDCLRNNG QSGDNVVKGL MKKFIRCSTR VTVGTIKKFL
     SLKLKLPSSY ELDVLCNGEI MGKDHTMEFI YMTRWRLRGE NFRCLNCSAS QVCSQDGPLY
     QSYPMVLQYR PRIDFG
//
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