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 10-MAY-2017, entry version 122.
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;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; 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.,
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 [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.,
RA Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K.,
RA Ottenwaelder B., Poustka A., 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.,
RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA 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
RT project: 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
RT PRC1 Complexes in mammalian cells.";
RL Mol. Cell. Proteomics 0:0-0(2011).
CC -!- FUNCTION: Component of a Polycomb group (PcG) multiprotein PRC1-
CC like complex, a complex class required to maintain the
CC transcriptionally repressive state of many genes, including Hox
CC genes, throughout development. PcG PRC1 complex acts via chromatin
CC remodeling and modification of histones; it mediates
CC monoubiquitination of histone H2A 'Lys-119', rendering chromatin
CC heritably changed in its expressibility.
CC -!- SUBUNIT: Component of a PRC1-like complex. Interacts with CBX6,
CC CBX7 and CBX8. {ECO:0000269|PubMed:21282530}.
CC -!- INTERACTION:
CC Q6W2J9-4:BCOR; NbExp=3; IntAct=EBI-2827999, EBI-10208579;
CC Q9HC52:CBX8; NbExp=4; IntAct=EBI-2827999, EBI-712912;
CC Q8IXK0:PHC2; NbExp=3; IntAct=EBI-2827999, EBI-713786;
CC Q96LA8:PRMT6; NbExp=2; IntAct=EBI-2827999, EBI-912440;
CC Q06587:RING1; NbExp=6; IntAct=EBI-2827999, EBI-752313;
CC Q99496:RNF2; NbExp=4; IntAct=EBI-2827999, EBI-722416;
CC Q12933:TRAF2; NbExp=3; IntAct=EBI-2827999, EBI-355744;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:21282530}.
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;
CC Note=No experimental confirmation available.;
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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 UniGene; Hs.500512; -.
DR PDB; 4S3O; X-ray; 2.00 A; C/F=1-109.
DR PDBsum; 4S3O; -.
DR ProteinModelPortal; Q86SE9; -.
DR SMR; Q86SE9; -.
DR BioGrid; 124057; 34.
DR DIP; DIP-61356N; -.
DR IntAct; Q86SE9; 48.
DR MINT; MINT-4726289; -.
DR STRING; 9606.ENSP00000337500; -.
DR PhosphoSitePlus; Q86SE9; -.
DR BioMuta; PCGF5; -.
DR DMDM; 74750353; -.
DR EPD; Q86SE9; -.
DR MaxQB; Q86SE9; -.
DR PaxDb; Q86SE9; -.
DR PeptideAtlas; Q86SE9; -.
DR PRIDE; Q86SE9; -.
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 GeneCards; PCGF5; -.
DR HGNC; HGNC:28264; PCGF5.
DR HPA; HPA038349; -.
DR neXtProt; NX_Q86SE9; -.
DR OpenTargets; ENSG00000180628; -.
DR PharmGKB; PA134929149; -.
DR eggNOG; KOG2660; Eukaryota.
DR eggNOG; ENOG410XPCN; LUCA.
DR GeneTree; ENSGT00550000074463; -.
DR HOGENOM; HOG000231946; -.
DR HOVERGEN; HBG052826; -.
DR InParanoid; Q86SE9; -.
DR KO; K11489; -.
DR OMA; FNHFITC; -.
DR OrthoDB; EOG091G0EC9; -.
DR PhylomeDB; Q86SE9; -.
DR TreeFam; TF324206; -.
DR ChiTaRS; PCGF5; human.
DR GeneWiki; PCGF5; -.
DR GenomeRNAi; 84333; -.
DR PRO; PR:Q86SE9; -.
DR Proteomes; UP000005640; Chromosome 10.
DR Bgee; ENSG00000180628; -.
DR CleanEx; HS_PCGF5; -.
DR Genevisible; Q86SE9; HS.
DR GO; GO:0005813; C:centrosome; IDA:LIFEdb.
DR GO; GO:0005730; C:nucleolus; IDA:HPA.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0031519; C:PcG protein complex; IDA:UniProtKB.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0045944; P:positive regulation of transcription from RNA polymerase II promoter; IDA:MGI.
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; 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; Complete proteome; Metal-binding;
KW Nucleus; Reference proteome; Repressor; Transcription;
KW Transcription regulation; Zinc; Zinc-finger.
FT CHAIN 1 256 Polycomb group RING finger protein 5.
FT /FTId=PRO_0000277868.
FT ZN_FING 18 57 RING-type. {ECO:0000255|PROSITE-
FT ProRule:PRU00175}.
FT VAR_SEQ 38 49 FCKTCIVQHFED -> SAESYWMSTWMS (in isoform
FT 2). {ECO:0000303|PubMed:15489334}.
FT /FTId=VSP_023118.
FT VAR_SEQ 50 256 Missing (in isoform 2).
FT {ECO:0000303|PubMed:15489334}.
FT /FTId=VSP_023119.
FT HELIX 9 12 {ECO:0000244|PDB:4S3O}.
FT HELIX 13 16 {ECO:0000244|PDB:4S3O}.
FT TURN 19 21 {ECO:0000244|PDB:4S3O}.
FT STRAND 22 24 {ECO:0000244|PDB:4S3O}.
FT STRAND 26 31 {ECO:0000244|PDB:4S3O}.
FT TURN 32 35 {ECO:0000244|PDB:4S3O}.
FT STRAND 36 39 {ECO:0000244|PDB:4S3O}.
FT HELIX 40 46 {ECO:0000244|PDB:4S3O}.
FT TURN 47 49 {ECO:0000244|PDB:4S3O}.
FT TURN 54 56 {ECO:0000244|PDB:4S3O}.
FT HELIX 65 68 {ECO:0000244|PDB:4S3O}.
FT STRAND 69 71 {ECO:0000244|PDB:4S3O}.
FT HELIX 73 82 {ECO:0000244|PDB:4S3O}.
FT HELIX 86 98 {ECO:0000244|PDB:4S3O}.
CC --------------------------------------------------------------------------
CC The following FT lines are automated annotations from the MyHits database.
CC --------------------------------------------------------------------------
FT MYHIT 18 56 ismart:RING [T]
FT MYHIT 34 43 ipat:ZF_RING_1 [T]
FT MYHIT 163 216 ipfam:RAWUL [T]
FT MYHIT 18 56 iprf:ZF_RING_2 [T]
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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