PCGF5_HUMAN
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 03-AUG-2022, entry version 158.
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:0007744|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=8; IntAct=EBI-2827999, EBI-752313;
CC Q86SE9; Q99496: RNF2; NbExp=9; IntAct=EBI-2827999, EBI-722416;
CC Q86SE9; Q12933: TRAF2; NbExp=3; IntAct=EBI-2827999, EBI-355744;
CC Q86SE9; Q2GHU2: ECH_0166; Xeno; NbExp=3; IntAct=EBI-2827999, EBI-26585631;
CC Q86SE9-2; P28799: GRN; NbExp=3; IntAct=EBI-25861637, EBI-747754;
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;
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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 AlphaFoldDB; Q86SE9; -.
DR SMR; Q86SE9; -.
DR BioGRID; 124057; 99.
DR DIP; DIP-61356N; -.
DR IntAct; Q86SE9; 65.
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 from 15 providers.
DR DNASU; 84333; -.
DR Ensembl; ENST00000336126.6; ENSP00000337500.5; ENSG00000180628.15. [Q86SE9-1]
DR Ensembl; ENST00000543648.5; ENSP00000445704.1; ENSG00000180628.15. [Q86SE9-1]
DR Ensembl; ENST00000614189.4; ENSP00000479492.1; ENSG00000180628.15. [Q86SE9-1]
DR GeneID; 84333; -.
DR KEGG; hsa:84333; -.
DR MANE-Select; ENST00000336126.6; ENSP00000337500.5; NM_032373.5; NP_115749.2.
DR UCSC; uc001khh.5; human. [Q86SE9-1]
DR CTD; 84333; -.
DR DisGeNET; 84333; -.
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 VEuPathDB; HostDB:ENSG00000180628; -.
DR eggNOG; KOG2660; Eukaryota.
DR GeneTree; ENSGT00940000155896; -.
DR HOGENOM; CLU_046427_4_1_1; -.
DR InParanoid; Q86SE9; -.
DR OMA; CGGYLIK; -.
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 SignaLink; Q86SE9; -.
DR BioGRID-ORCS; 84333; 15 hits in 1117 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 cardiac muscle of right atrium and 193 other tissues.
DR Genevisible; Q86SE9; HS.
DR GO; GO:0005813; C:centrosome; IDA:LIFEdb.
DR GO; GO:0005794; C:Golgi apparatus; IDA:HPA.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
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:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0036353; P:histone H2A-K119 monoubiquitination; ISS:UniProtKB.
DR GO; GO:0060819; P:inactivation of X chromosome by genomic imprinting; ISS:UniProtKB.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IDA:MGI.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
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 REGION 94..133
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 94..120
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
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:0007829|PDB:4S3O"
FT HELIX 13..16
FT /evidence="ECO:0007829|PDB:4S3O"
FT TURN 19..21
FT /evidence="ECO:0007829|PDB:4S3O"
FT STRAND 22..24
FT /evidence="ECO:0007829|PDB:4S3O"
FT STRAND 26..31
FT /evidence="ECO:0007829|PDB:4S3O"
FT TURN 32..35
FT /evidence="ECO:0007829|PDB:4S3O"
FT STRAND 36..39
FT /evidence="ECO:0007829|PDB:4S3O"
FT HELIX 40..46
FT /evidence="ECO:0007829|PDB:4S3O"
FT TURN 47..49
FT /evidence="ECO:0007829|PDB:4S3O"
FT TURN 54..56
FT /evidence="ECO:0007829|PDB:4S3O"
FT HELIX 65..68
FT /evidence="ECO:0007829|PDB:4S3O"
FT STRAND 69..71
FT /evidence="ECO:0007829|PDB:4S3O"
FT HELIX 73..82
FT /evidence="ECO:0007829|PDB:4S3O"
FT HELIX 86..98
FT /evidence="ECO:0007829|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
