ID PCGF6_HUMAN Reviewed; 350 AA.
AC Q9BYE7; A8K3R4; Q5SYD1; Q5SYD6; Q96ID9; Q96SJ1;
DT 11-OCT-2005, integrated into UniProtKB/Swiss-Prot.
DT 17-OCT-2006, sequence version 2.
DT 10-MAY-2017, entry version 146.
DE RecName: Full=Polycomb group RING finger protein 6;
DE AltName: Full=Mel18 and Bmi1-like RING finger;
DE AltName: Full=RING finger protein 134;
GN Name=PCGF6; Synonyms=MBLR, RNF134;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION IN TRANSCRIPTIONAL
RP REPRESSION, INTERACTION WITH BMI1; RING1 AND RNF2, PHOSPHORYLATION AT
RP SER-30, MUTAGENESIS OF SER-30; SER-57; SER-59 AND SER-69, VARIANT
RP PRO-PRO-23 INS, AND SUBCELLULAR LOCATION.
RC TISSUE=Testis;
RX PubMed=12167161; DOI=10.1046/j.1365-2443.2002.00565.x;
RA Akasaka T., Takahashi N., Suzuki M., Koseki H., Bodmer R., Koga H.;
RT "MBLR, a new RING finger protein resembling mammalian Polycomb gene
RT products, is regulated by cell cycle-dependent phosphorylation.";
RL Genes Cells 7:835-850(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
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.,
RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA 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.,
RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA Nakai K., Yada T., Nakamura Y., Ohara O., 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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15164054; DOI=10.1038/nature02462;
RA Deloukas P., Earthrowl M.E., Grafham D.V., Rubenfield M., French L.,
RA Steward C.A., Sims S.K., Jones M.C., Searle S., Scott C., Howe K.,
RA Hunt S.E., Andrews T.D., Gilbert J.G.R., Swarbreck D., Ashurst J.L.,
RA Taylor A., Battles J., Bird C.P., Ainscough R., Almeida J.P.,
RA Ashwell R.I.S., Ambrose K.D., Babbage A.K., Bagguley C.L., Bailey J.,
RA Banerjee R., Bates K., Beasley H., Bray-Allen S., Brown A.J.,
RA Brown J.Y., Burford D.C., Burrill W., Burton J., Cahill P., Camire D.,
RA Carter N.P., Chapman J.C., Clark S.Y., Clarke G., Clee C.M., Clegg S.,
RA Corby N., Coulson A., Dhami P., Dutta I., Dunn M., Faulkner L.,
RA Frankish A., Frankland J.A., Garner P., Garnett J., Gribble S.,
RA Griffiths C., Grocock R., Gustafson E., Hammond S., Harley J.L.,
RA Hart E., Heath P.D., Ho T.P., Hopkins B., Horne J., Howden P.J.,
RA Huckle E., Hynds C., Johnson C., Johnson D., Kana A., Kay M.,
RA Kimberley A.M., Kershaw J.K., Kokkinaki M., Laird G.K., Lawlor S.,
RA Lee H.M., Leongamornlert D.A., Laird G., Lloyd C., Lloyd D.M.,
RA Loveland J., Lovell J., McLaren S., McLay K.E., McMurray A.,
RA Mashreghi-Mohammadi M., Matthews L., Milne S., Nickerson T.,
RA Nguyen M., Overton-Larty E., Palmer S.A., Pearce A.V., Peck A.I.,
RA Pelan S., Phillimore B., Porter K., Rice C.M., Rogosin A., Ross M.T.,
RA Sarafidou T., Sehra H.K., Shownkeen R., Skuce C.D., Smith M.,
RA Standring L., Sycamore N., Tester J., Thorpe A., Torcasso W.,
RA Tracey A., Tromans A., Tsolas J., Wall M., Walsh J., Wang H.,
RA Weinstock K., West A.P., Willey D.L., Whitehead S.L., Wilming L.,
RA Wray P.W., Young L., Chen Y., Lovering R.C., Moschonas N.K.,
RA Siebert R., Fechtel K., Bentley D., Durbin R.M., Hubbard T.,
RA Doucette-Stamm L., Beck S., Smith D.R., Rogers J.;
RT "The DNA sequence and comparative analysis of human chromosome 10.";
RL Nature 429:375-381(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 3), AND VARIANT
RP PRO-PRO-23 INS.
RC TISSUE=Cervix, and Eye;
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
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [5]
RP FUNCTION, INTERACTION WITH KDM5D, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RX PubMed=17320162; DOI=10.1016/j.cell.2007.02.004;
RA Lee M.G., Norman J., Shilatifard A., Shiekhattar R.;
RT "Physical and functional association of a trimethyl H3K4 demethylase
RT and Ring6a/MBLR, a polycomb-like protein.";
RL Cell 128:877-887(2007).
RN [6]
RP IDENTIFICATION IN A PRC1-LIKE COMPLEX.
RX PubMed=19636380; DOI=10.1371/journal.pone.0006380;
RA Maertens G.N., El Messaoudi-Aubert S., Racek T., Stock J.K.,
RA Nicholls J., Rodriguez-Niedenfuhr M., Gil J., Peters G.;
RT "Several distinct polycomb complexes regulate and co-localize on the
RT INK4a tumor suppressor locus.";
RL PLoS ONE 4:E6380-E6380(2009).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-115, AND IDENTIFICATION
RP BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S.,
RA Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full
RT phosphorylation site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [8]
RP IDENTIFICATION IN A PRC1-LIKE COMPLEX, INTERACTION WITH CBX4; CBX6;
RP CBX7 AND 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
RT PRC1 Complexes in mammalian cells.";
RL Mol. Cell. Proteomics 0:0-0(2011).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-115, AND IDENTIFICATION
RP BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J.,
RA Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V.,
RA Blagoev B.;
RT "System-wide temporal characterization of the proteome and
RT phosphoproteome of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-115, AND IDENTIFICATION
RP BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma, and Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-115, AND IDENTIFICATION
RP BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D.,
RA Wang L., Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human
RT liver phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [12]
RP STRUCTURE BY NMR OF 124-182.
RG RIKEN structural genomics initiative (RSGI);
RT "Solution structure of the RING domain of the human polycomb group
RT RING finger protein 6.";
RL Submitted (MAR-2007) to the PDB data bank.
CC -!- FUNCTION: Transcriptional repressor. May modulate the levels of
CC histone H3K4Me3 by activating KDM5D histone demethylase. Component
CC of a Polycomb group (PcG) multiprotein PRC1-like complex, a
CC 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
CC histone H2A 'Lys-119', rendering chromatin heritably changed in
CC its expressibility. {ECO:0000269|PubMed:12167161,
CC ECO:0000269|PubMed:17320162}.
CC -!- SUBUNIT: Component of a PRC1-like complex. Interacts with
CC BMI1/PCGF4, RING1 and RNF2. Interacts with KDM5D. Interacts with
CC CBX4, CBX6, CBX7 and CBX8. {ECO:0000269|PubMed:12167161,
CC ECO:0000269|PubMed:17320162, ECO:0000269|PubMed:19636380,
CC ECO:0000269|PubMed:21282530}.
CC -!- INTERACTION:
CC O00257-3:CBX4; NbExp=2; IntAct=EBI-1048026, EBI-4392727;
CC O95931:CBX7; NbExp=3; IntAct=EBI-1048026, EBI-3923843;
CC Q9HC52:CBX8; NbExp=3; IntAct=EBI-1048026, EBI-712912;
CC Q06587:RING1; NbExp=3; IntAct=EBI-1048026, EBI-752313;
CC Q99496:RNF2; NbExp=4; IntAct=EBI-1048026, EBI-722416;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:12167161,
CC ECO:0000269|PubMed:21282530}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9BYE7-1; Sequence=Displayed;
CC Name=3;
CC IsoId=Q9BYE7-3; Sequence=VSP_042007, VSP_042008;
CC -!- TISSUE SPECIFICITY: Ubiquitous.
CC -!- PTM: Phosphorylated during mitosis. Phosphorylated on Ser-30 by
CC CDK7 in vitro. {ECO:0000269|PubMed:12167161}.
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DR EMBL; AB047006; BAB40779.1; -; mRNA.
DR EMBL; AK027885; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; AK290679; BAF83368.1; -; mRNA.
DR EMBL; AL591408; CAI16745.1; -; Genomic_DNA.
DR EMBL; AL591408; CAI16746.1; -; Genomic_DNA.
DR EMBL; BC007602; AAH07602.1; -; mRNA.
DR EMBL; BC010235; AAH10235.1; -; mRNA.
DR CCDS; CCDS31275.1; -. [Q9BYE7-1]
DR CCDS; CCDS7546.1; -. [Q9BYE7-3]
DR RefSeq; NP_001011663.1; NM_001011663.1. [Q9BYE7-1]
DR RefSeq; NP_115530.2; NM_032154.3. [Q9BYE7-3]
DR UniGene; Hs.335808; -.
DR PDB; 2DJB; NMR; -; A=124-182.
DR PDBsum; 2DJB; -.
DR ProteinModelPortal; Q9BYE7; -.
DR SMR; Q9BYE7; -.
DR BioGrid; 123896; 71.
DR DIP; DIP-50946N; -.
DR IntAct; Q9BYE7; 48.
DR STRING; 9606.ENSP00000358862; -.
DR iPTMnet; Q9BYE7; -.
DR PhosphoSitePlus; Q9BYE7; -.
DR BioMuta; PCGF6; -.
DR DMDM; 116242703; -.
DR EPD; Q9BYE7; -.
DR MaxQB; Q9BYE7; -.
DR PaxDb; Q9BYE7; -.
DR PeptideAtlas; Q9BYE7; -.
DR PRIDE; Q9BYE7; -.
DR DNASU; 84108; -.
DR Ensembl; ENST00000337211; ENSP00000338845; ENSG00000156374. [Q9BYE7-3]
DR Ensembl; ENST00000369847; ENSP00000358862; ENSG00000156374. [Q9BYE7-1]
DR GeneID; 84108; -.
DR KEGG; hsa:84108; -.
DR UCSC; uc001kwt.3; human. [Q9BYE7-1]
DR CTD; 84108; -.
DR DisGeNET; 84108; -.
DR GeneCards; PCGF6; -.
DR H-InvDB; HIX0014963; -.
DR HGNC; HGNC:21156; PCGF6.
DR MIM; 607816; gene.
DR neXtProt; NX_Q9BYE7; -.
DR OpenTargets; ENSG00000156374; -.
DR PharmGKB; PA134887110; -.
DR eggNOG; KOG2660; Eukaryota.
DR eggNOG; ENOG410XPCN; LUCA.
DR GeneTree; ENSGT00550000074463; -.
DR HOGENOM; HOG000231946; -.
DR HOVERGEN; HBG052826; -.
DR InParanoid; Q9BYE7; -.
DR KO; K11470; -.
DR OMA; IGANEDT; -.
DR OrthoDB; EOG091G0EC9; -.
DR PhylomeDB; Q9BYE7; -.
DR TreeFam; TF324206; -.
DR SIGNOR; Q9BYE7; -.
DR ChiTaRS; PCGF6; human.
DR EvolutionaryTrace; Q9BYE7; -.
DR GeneWiki; PCGF6; -.
DR GenomeRNAi; 84108; -.
DR PRO; PR:Q9BYE7; -.
DR Proteomes; UP000005640; Chromosome 10.
DR Bgee; ENSG00000156374; -.
DR CleanEx; HS_PCGF6; -.
DR Genevisible; Q9BYE7; HS.
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; IDA:UniProtKB.
DR GO; GO:0003677; F:DNA binding; IDA:UniProtKB.
DR GO; GO:0000977; F:RNA polymerase II regulatory region sequence-specific DNA binding; IEA:Ensembl.
DR GO; GO:0003700; F:transcription factor activity, sequence-specific DNA binding; IDA:UniProtKB.
DR GO; GO:0001227; F:transcriptional repressor activity, RNA polymerase II transcription regulatory region sequence-specific binding; IEA:Ensembl.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0045892; P:negative regulation of transcription, DNA-templated; IDA:UniProtKB.
DR GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-KW.
DR CDD; cd00162; RING; 1.
DR Gene3D; 3.30.40.10; -; 1.
DR InterPro; IPR029071; Ubiquitin-rel_dom.
DR InterPro; IPR001841; Znf_RING.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR InterPro; IPR017907; Znf_RING_CS.
DR SMART; SM00184; RING; 1.
DR SUPFAM; SSF54236; SSF54236; 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; Coiled coil; Complete proteome;
KW Metal-binding; Nucleus; Phosphoprotein; Polymorphism;
KW Reference proteome; Repressor; Transcription;
KW Transcription regulation; Zinc; Zinc-finger.
FT CHAIN 1 350 Polycomb group RING finger protein 6.
FT /FTId=PRO_0000055989.
FT ZN_FING 134 173 RING-type. {ECO:0000255|PROSITE-
FT ProRule:PRU00175}.
FT COILED 72 110 {ECO:0000255}.
FT COMPBIAS 22 66 Pro-rich.
FT COMPBIAS 63 120 Glu-rich.
FT MOD_RES 30 30 Phosphoserine.
FT {ECO:0000269|PubMed:12167161}.
FT MOD_RES 115 115 Phosphoserine.
FT {ECO:0000244|PubMed:20068231,
FT ECO:0000244|PubMed:21406692,
FT ECO:0000244|PubMed:23186163,
FT ECO:0000244|PubMed:24275569}.
FT VAR_SEQ 186 186 R -> S (in isoform 3).
FT {ECO:0000303|PubMed:15489334}.
FT /FTId=VSP_042007.
FT VAR_SEQ 187 261 Missing (in isoform 3).
FT {ECO:0000303|PubMed:15489334}.
FT /FTId=VSP_042008.
FT VARIANT 23 23 L -> LPP. {ECO:0000269|PubMed:12167161,
FT ECO:0000269|PubMed:15489334}.
FT /FTId=VAR_054312.
FT MUTAGEN 30 30 S->A: Abolishes phosphorylation.
FT {ECO:0000269|PubMed:12167161}.
FT MUTAGEN 57 57 S->A: Does not abolish phosphorylation.
FT {ECO:0000269|PubMed:12167161}.
FT MUTAGEN 59 59 S->A: Does not abolish phosphorylation.
FT {ECO:0000269|PubMed:12167161}.
FT MUTAGEN 69 69 S->A: Does not abolish phosphorylation.
FT {ECO:0000269|PubMed:12167161}.
FT CONFLICT 257 257 L -> P (in Ref. 2; BAF83368).
FT {ECO:0000305}.
FT CONFLICT 261 261 G -> S (in Ref. 4; AAH07602).
FT {ECO:0000305}.
FT HELIX 130 132 {ECO:0000244|PDB:2DJB}.
FT TURN 135 137 {ECO:0000244|PDB:2DJB}.
FT STRAND 148 150 {ECO:0000244|PDB:2DJB}.
FT HELIX 156 165 {ECO:0000244|PDB:2DJB}.
FT TURN 170 172 {ECO:0000244|PDB:2DJB}.
CC --------------------------------------------------------------------------
CC The following FT lines are automated annotations from the MyHits database.
CC --------------------------------------------------------------------------
FT MYHIT 134 172 ismart:RING [T]
FT MYHIT 134 173 iprf:ZF_RING_2 [T]
FT MYHIT 150 159 ipat:ZF_RING_1 [T]
SQ SEQUENCE 350 AA; 39047 MW; 05977FE6F14972DE CRC64;
MEGVAVVTAG SVGAAKTEGA AALPPPPPVS PPALTPAPAA GEEGPAPLSE TGAPGCSGSR
PPELEPERSL GRFRGRFEDE DEELEEEEEL EEEEEEEEED MSHFSLRLEG GRQDSEDEEE
RLINLSELTP YILCSICKGY LIDATTITEC LHTFCKSCIV RHFYYSNRCP KCNIVVHQTQ
PLYNIRLDRQ LQDIVYKLVI NLEEREKKQM HDFYKERGLE VPKPAVPQPV PSSKGRSKKV
LESVFRIPPE LDMSLLLEFI GANEGTGHFK PLEKKFVRVS GEATIGHVEK FLRRKMGLDP
ACQVDIICGD HLLEQYQTLR EIRRAIGDAA MQDGLLVLHY GLVVSPLKIT
//
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