CBX6_MOUSE
ID CBX6_MOUSE Reviewed; 414 AA.
AC Q9DBY5; Q8BZH5;
DT 29-AUG-2001, integrated into UniProtKB/Swiss-Prot.
DT 07-JUN-2004, sequence version 2.
DT 03-AUG-2022, entry version 147.
DE RecName: Full=Chromobox protein homolog 6;
GN Name=Cbx6;
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].
RC STRAIN=C57BL/6J; TISSUE=Lung, and Urinary bladder;
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].
RC TISSUE=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 project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [3]
RP FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH SSRNA.
RX PubMed=16537902; DOI=10.1128/mcb.26.7.2560-2569.2006;
RA Bernstein E., Duncan E.M., Masui O., Gil J., Heard E., Allis C.D.;
RT "Mouse polycomb proteins bind differentially to methylated histone H3 and
RT RNA and are enriched in facultative heterochromatin.";
RL Mol. Cell. Biol. 26:2560-2569(2006).
RN [4]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Spleen;
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 [5]
RP FUNCTION, AND TISSUE SPECIFICITY.
RX PubMed=22226355; DOI=10.1016/j.stem.2011.12.006;
RA Morey L., Pascual G., Cozzuto L., Roma G., Wutz A., Benitah S.A.,
RA Di Croce L.;
RT "Nonoverlapping functions of the Polycomb group Cbx family of proteins in
RT embryonic stem cells.";
RL Cell Stem Cell 10:47-62(2012).
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 Possibly contributes to the target selectivity of the PRC1 complex by
CC binding specific regions of chromatin (By similarity). Recruitment to
CC chromatin might occur in an H3K27me3-independent fashion
CC (PubMed:22226355, PubMed:16537902). May have a PRC1-independent
CC function in embryonic stem cells (PubMed:22226355).
CC {ECO:0000250|UniProtKB:O95503, ECO:0000269|PubMed:16537902,
CC ECO:0000269|PubMed:22226355}.
CC -!- SUBUNIT: Component of a PRC1-like complex. Distinct PRC1-like core
CC complexes are composed of a RING1 subunit (RING1B or RING1A), one of
CC the six PCGF proteins (PCGF1-6), one PHC protein (PHC1-3) and one of
CC the CBX proteins (CBX2, CBX4, CBX6, CBX7 or CBX8). Interacts with
CC PCGF1, PCGF2, PCGF3, BMI1, PCGF5, PCGF6, RING1 and RNF2. May interact
CC with H3C15 and H3C1 (By similarity). Interacts (via chromodomain) with
CC single-stranded RNA (ssRNA) (PubMed:16537902).
CC {ECO:0000250|UniProtKB:O95503, ECO:0000269|PubMed:16537902}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:16537902}. Chromosome
CC {ECO:0000269|PubMed:16537902}. Note=Localizes to the inactivated X
CC chromosome in females. {ECO:0000269|PubMed:16537902}.
CC -!- TISSUE SPECIFICITY: Expressed in mouse embryonic stem cells.
CC {ECO:0000269|PubMed:22226355}.
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DR EMBL; AK004679; BAB23467.1; -; mRNA.
DR EMBL; AK035250; BAC29001.1; -; mRNA.
DR EMBL; BC048240; AAH48240.1; -; mRNA.
DR CCDS; CCDS37142.1; -.
DR RefSeq; NP_083039.2; NM_028763.3.
DR AlphaFoldDB; Q9DBY5; -.
DR SMR; Q9DBY5; -.
DR BioGRID; 243462; 13.
DR STRING; 10090.ENSMUSP00000105255; -.
DR iPTMnet; Q9DBY5; -.
DR PhosphoSitePlus; Q9DBY5; -.
DR MaxQB; Q9DBY5; -.
DR PaxDb; Q9DBY5; -.
DR PeptideAtlas; Q9DBY5; -.
DR PRIDE; Q9DBY5; -.
DR ProteomicsDB; 281233; -.
DR Antibodypedia; 272; 258 antibodies from 33 providers.
DR DNASU; 494448; -.
DR Ensembl; ENSMUST00000109627; ENSMUSP00000105255; ENSMUSG00000089715.
DR GeneID; 494448; -.
DR KEGG; mmu:494448; -.
DR UCSC; uc007wuo.1; mouse.
DR CTD; 23466; -.
DR MGI; MGI:3512628; Cbx6.
DR VEuPathDB; HostDB:ENSMUSG00000089715; -.
DR eggNOG; KOG2748; Eukaryota.
DR GeneTree; ENSGT00940000154405; -.
DR HOGENOM; CLU_042051_2_0_1; -.
DR InParanoid; Q9DBY5; -.
DR OMA; FGAFAMY; -.
DR OrthoDB; 1628171at2759; -.
DR PhylomeDB; Q9DBY5; -.
DR TreeFam; TF106456; -.
DR BioGRID-ORCS; 494448; 6 hits in 63 CRISPR screens.
DR PRO; PR:Q9DBY5; -.
DR Proteomes; UP000000589; Chromosome 15.
DR RNAct; Q9DBY5; protein.
DR Bgee; ENSMUSG00000089715; Expressed in CA3 field of hippocampus and 242 other tissues.
DR ExpressionAtlas; Q9DBY5; baseline and differential.
DR Genevisible; Q9DBY5; MM.
DR GO; GO:0000792; C:heterochromatin; IDA:UniProtKB.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0031519; C:PcG protein complex; ISS:UniProtKB.
DR GO; GO:0003727; F:single-stranded RNA binding; IDA:UniProtKB.
DR GO; GO:0006325; P:chromatin organization; IEA:UniProtKB-KW.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; ISO:MGI.
DR InterPro; IPR033773; CBX7_C.
DR InterPro; IPR016197; Chromo-like_dom_sf.
DR InterPro; IPR000953; Chromo/chromo_shadow_dom.
DR InterPro; IPR017984; Chromo_dom_subgr.
DR InterPro; IPR023780; Chromo_domain.
DR InterPro; IPR023779; Chromodomain_CS.
DR Pfam; PF17218; CBX7_C; 1.
DR Pfam; PF00385; Chromo; 1.
DR PRINTS; PR00504; CHROMODOMAIN.
DR SMART; SM00298; CHROMO; 1.
DR SUPFAM; SSF54160; SSF54160; 1.
DR PROSITE; PS00598; CHROMO_1; 1.
DR PROSITE; PS50013; CHROMO_2; 1.
PE 1: Evidence at protein level;
KW Chromatin regulator; Chromosome; Nucleus; Phosphoprotein;
KW Reference proteome; Repressor; Transcription; Transcription regulation.
FT CHAIN 1..414
FT /note="Chromobox protein homolog 6"
FT /id="PRO_0000080211"
FT DOMAIN 11..69
FT /note="Chromo"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00053"
FT REGION 127..152
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 267..308
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 344..365
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 269..288
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 107
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O95503"
FT CONFLICT 223
FT /note="Q -> P (in Ref. 1; BAB23467)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 414 AA; 44460 MW; 299347436FC04629 CRC64;
MELSAVGERV FAAESIIKRR IRKGRIEYLV KWKGWAIKYS TWEPEENILD SRLIAAFEQK
ERERELYGPK KRGPKPKTFL LKARAQAEAL RISDVHFSVK PSASASSPKL HSSAAVHRLK
KDIRRCHRMS RRPLPRPDPQ GGSPGLRPPI SPFSETVRII NRKVKPREPK RNRIILNLKV
IDKGPGGGST AQGTGALARP KVPSRNRVIG KSKKFSESML RTQIRHMKFG TFALYKPPPA
PLAPSTAGKA DVASSGPGLL LATPAAAPFD AHSSSSSGCP SPTLQSSDPD DAPPKLLPET
LSRSVPNWRE SEVLDLSIPP EAAATGQRVP PDVTGAADQA LHTALEPTGA GSSEPEAGDW
RPEMSPCSNV VVTDVTSNLL TVTIKEFCSP EDFEKVAAGV AGATGGGGGT GPSK
