PCGF5_MOUSE
ID PCGF5_MOUSE Reviewed; 256 AA.
AC Q3UK78; B2RTD3; B7ZP23; Q9D3E5; Q9DCW8;
DT 20-FEB-2007, integrated into UniProtKB/Swiss-Prot.
DT 11-OCT-2005, sequence version 1.
DT 03-AUG-2022, entry version 127.
DE RecName: Full=Polycomb group RING finger protein 5;
DE AltName: Full=RING finger protein 159;
GN Name=Pcgf5; Synonyms=Rnf159;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC STRAIN=C57BL/6J, and DBA/2J; TISSUE=Kidney, and Thymus;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC TISSUE=Brain;
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 [3]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [4]
RP FUNCTION, INTERACTION WITH RNF2, AND TISSUE SPECIFICITY.
RX PubMed=27136092; DOI=10.1371/journal.pone.0154561;
RA Si S., Nakajima-Takagi Y., Aoyama K., Oshima M., Saraya A., Sugishita H.,
RA Nakayama M., Ishikura T., Koseki H., Iwama A.;
RT "Loss of Pcgf5 affects global H2A monoubiquitination but not the function
RT of hematopoietic stem and progenitor cells.";
RL PLoS ONE 11:E0154561-E0154561(2016).
RN [5]
RP FUNCTION, SUBCELLULAR LOCATION, SUBUNIT, INTERACTION WITH RNF2, AND
RP DISRUPTION PHENOTYPE.
RX PubMed=28596365; DOI=10.1126/science.aal2512;
RA Almeida M., Pintacuda G., Masui O., Koseki Y., Gdula M., Cerase A.,
RA Brown D., Mould A., Innocent C., Nakayama M., Schermelleh L.,
RA Nesterova T.B., Koseki H., Brockdorff N.;
RT "PCGF3/5-PRC1 initiates Polycomb recruitment in X chromosome
RT inactivation.";
RL Science 356:1081-1084(2017).
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:27136092, PubMed:28596365). Within the PRC1-like complex,
CC regulates RNF2 ubiquitin ligase activity (By similarity). Plays a
CC redundant role 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 (PubMed:28596365). {ECO:0000250|UniProtKB:Q86SE9,
CC ECO:0000269|PubMed:27136092, ECO:0000269|PubMed:28596365}.
CC -!- SUBUNIT: Component of a PRC1-like complex that contains PCGF5, RNF2 and
CC UBE2D3 (PubMed:28596365). Interacts with RNF2; the interaction is
CC direct (PubMed:27136092, PubMed:28596365). Interacts with CBX6, CBX7
CC and CBX8. Interacts with AUTS2; the interaction is direct. Identified
CC in a complex that contains AUTS2, PCGF5, CSNK2B and RNF2 (By
CC similarity). {ECO:0000250|UniProtKB:Q86SE9,
CC ECO:0000269|PubMed:27136092, ECO:0000269|PubMed:28596365}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:28596365}. Nucleus,
CC nucleoplasm {ECO:0000269|PubMed:28596365}. Note=Recruited by the non-
CC coding RNA Xist to specific nuclear foci that probably correspond to
CC the inactivated X chromosome. {ECO:0000269|PubMed:28596365}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q3UK78-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q3UK78-2; Sequence=VSP_023120;
CC -!- TISSUE SPECIFICITY: Detected in hematopoietic stem cells and
CC multipotent progenitor cells. {ECO:0000269|PubMed:27136092}.
CC -!- DISRUPTION PHENOTYPE: Combined disruption of both Pcgf3 and Pcgf5
CC causes embryonic lethality; there are no live progeny. Male embryos are
CC detected at 9.5 and 10.5 dpc, but are smaller than normal. Female
CC embryos are already extensively degraded at 9.5 dpc. Placentas from
CC male embryos have some parietal trophoblast giant cells, but fail to
CC form a labyrinth. Placentas from female embryos lack trophoblasts
CC altogether and fail to form a labyrinth. Defects can be attributed to
CC the observed lack of monoubiquitination of histone H2A 'Lys-119' and
CC lack of Xist-mediated silencing of one copy of the X chromosome.
CC {ECO:0000269|PubMed:28596365}.
CC -!- MISCELLANEOUS: Selective knockout in hematopoietic stem cells has only
CC minor effects on gene expression and hematopoiesis, probably due to
CC functional compensation by Pcgf1. {ECO:0000269|PubMed:27136092}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAB22061.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AK002387; BAB22061.1; ALT_FRAME; mRNA.
DR EMBL; AK017984; BAB31023.1; -; mRNA.
DR EMBL; AK146133; BAE26924.1; -; mRNA.
DR EMBL; BC139258; AAI39259.1; -; mRNA.
DR EMBL; BC139259; AAI39260.1; -; mRNA.
DR EMBL; BC145590; AAI45591.1; -; mRNA.
DR CCDS; CCDS29772.1; -. [Q3UK78-2]
DR CCDS; CCDS89384.1; -. [Q3UK78-1]
DR RefSeq; NP_083784.1; NM_029508.3. [Q3UK78-2]
DR RefSeq; XP_006527494.1; XM_006527431.3.
DR RefSeq; XP_006527496.1; XM_006527433.3.
DR RefSeq; XP_011245693.1; XM_011247391.2.
DR RefSeq; XP_011245694.1; XM_011247392.2. [Q3UK78-1]
DR RefSeq; XP_011245697.1; XM_011247395.2.
DR AlphaFoldDB; Q3UK78; -.
DR SMR; Q3UK78; -.
DR BioGRID; 217946; 3.
DR IntAct; Q3UK78; 1.
DR STRING; 10090.ENSMUSP00000058730; -.
DR iPTMnet; Q3UK78; -.
DR PhosphoSitePlus; Q3UK78; -.
DR EPD; Q3UK78; -.
DR MaxQB; Q3UK78; -.
DR PRIDE; Q3UK78; -.
DR ProteomicsDB; 288067; -. [Q3UK78-1]
DR ProteomicsDB; 288068; -. [Q3UK78-2]
DR Antibodypedia; 30344; 37 antibodies from 15 providers.
DR DNASU; 76073; -.
DR Ensembl; ENSMUST00000062389; ENSMUSP00000058730; ENSMUSG00000024805. [Q3UK78-2]
DR Ensembl; ENSMUST00000071267; ENSMUSP00000071245; ENSMUSG00000024805. [Q3UK78-2]
DR Ensembl; ENSMUST00000224679; ENSMUSP00000153681; ENSMUSG00000024805. [Q3UK78-1]
DR Ensembl; ENSMUST00000225411; ENSMUSP00000153464; ENSMUSG00000024805. [Q3UK78-1]
DR Ensembl; ENSMUST00000225920; ENSMUSP00000153206; ENSMUSG00000024805. [Q3UK78-2]
DR GeneID; 76073; -.
DR KEGG; mmu:76073; -.
DR UCSC; uc008hhi.1; mouse. [Q3UK78-2]
DR UCSC; uc008hhk.1; mouse. [Q3UK78-1]
DR CTD; 84333; -.
DR MGI; MGI:1923505; Pcgf5.
DR VEuPathDB; HostDB:ENSMUSG00000024805; -.
DR eggNOG; KOG2660; Eukaryota.
DR GeneTree; ENSGT00940000155896; -.
DR HOGENOM; CLU_046427_4_1_1; -.
DR InParanoid; Q3UK78; -.
DR OMA; NRELEFW; -.
DR OrthoDB; 1203951at2759; -.
DR PhylomeDB; Q3UK78; -.
DR TreeFam; TF324206; -.
DR Reactome; R-MMU-8939243; RUNX1 interacts with co-factors whose precise effect on RUNX1 targets is not known.
DR BioGRID-ORCS; 76073; 2 hits in 75 CRISPR screens.
DR ChiTaRS; Pcgf5; mouse.
DR PRO; PR:Q3UK78; -.
DR Proteomes; UP000000589; Chromosome 19.
DR RNAct; Q3UK78; protein.
DR Bgee; ENSMUSG00000024805; Expressed in spermatocyte and 217 other tissues.
DR ExpressionAtlas; Q3UK78; baseline and differential.
DR Genevisible; Q3UK78; MM.
DR GO; GO:0005813; C:centrosome; ISO:MGI.
DR GO; GO:0005794; C:Golgi apparatus; ISO:MGI.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005634; C:nucleus; ISO:MGI.
DR GO; GO:0031519; C:PcG protein complex; IDA:UniProtKB.
DR GO; GO:0035102; C:PRC1 complex; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0036353; P:histone H2A-K119 monoubiquitination; IMP:UniProtKB.
DR GO; GO:0060819; P:inactivation of X chromosome by genomic imprinting; IMP:UniProtKB.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; ISO: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 Alternative splicing; Metal-binding; Nucleus; Reference proteome;
KW Repressor; Transcription; Transcription regulation; Zinc; Zinc-finger.
FT CHAIN 1..256
FT /note="Polycomb group RING finger protein 5"
FT /id="PRO_0000277869"
FT ZN_FING 18..57
FT /note="RING-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00175"
FT REGION 102..133
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT VAR_SEQ 222..241
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334,
FT ECO:0000303|PubMed:16141072"
FT /id="VSP_023120"
SQ SEQUENCE 256 AA; 29657 MW; 053CF6DDEA3C2339 CRC64;
MATQRKHLVK DFNPYITCYI CKGYLIKPTT VTECLHTFCK TCIVQHFEDS NDCPRCGNQV
HETNPLEMLR LDNTLEEIIF KLVPGLREQE LQRELEFWKK NKPQENGQDD ISKVDKSKAD
EEGDENQDDK DYHRSDPQIA ICLDCLRNNG QSGDNVVKGL MKKFIRCSTR VTVGTIKKFL
SLKLKLPSSY ELDVLCNGEI MGKDHTMEFI YMTRWRLRGE NLCCLNCSAS QVCSQDGTLY
QSYPMVLQYR PRIDFG
