Q9HC52 (CBX8_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Chromobox protein homolog 8

Alternative name(s):
Polycomb 3 homolog
Short name=Pc3
Short name=hPc3
Rectachrome 1

Gene names

Name:	CBX8
Synonyms:	PC3, RC1

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	389 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Component of a Polycomb group (PcG) multiprotein PRC1-like complex, a complex class required to maintain the transcriptionally repressive state of many genes, including Hox genes, throughout development. PcG PRC1 complex acts via chromatin remodeling and modification of histones; it mediates monoubiquitination of histone H2A 'Lys-119', rendering chromatin heritably changed in its expressibility. Ref.13
Subunit structure	Component of a PRC1-like complex. Interacts with RING1 RNF2, PCGF1, PCGF2, PCGF3, BMI1, PCGF5 AND PCGF6. Interacts with MLLT3 and histone H3. Interacts with PHC2 By similarity. Ref.5 Ref.6 Ref.9 Ref.13
Subcellular location	Nucleus Ref.13.
Miscellaneous	The human orthologuous proteins of Drosphila Polycomb group protein Pc, CBX2, CBX4, CBX6, CBX7 and CBX8, show distinct nulear localizations, contribute differently to transcriptional repression, and appear to be part of distinct PRC1-like protein complexes. The hPRC-H complex purification reported by Ref.6 probably presents a mixture of different complexes.
Sequence similarities	Contains 1 chromo domain.

Ontologies

Keywords
Biological process	Transcription Transcription regulation
Cellular component	Nucleus
Coding sequence diversity	Polymorphism
Molecular function	Chromatin regulator Repressor
PTM	Phosphoprotein
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	histone ubiquitination Inferred from electronic annotation. Source: Compara negative regulation of transcription from RNA polymerase II promoter Inferred from mutant phenotype Ref.9Ref.13. Source: UniProtKB transcription, DNA-dependent Inferred from electronic annotation. Source: UniProtKB-KW
Cellular_component	PRC1 complex Inferred from direct assay Ref.6Ref.9. Source: UniProtKB heterochromatin Inferred from electronic annotation. Source: Compara nuclear chromatin Inferred from direct assay Ref.9. Source: UniProtKB ubiquitin ligase complex Inferred from electronic annotation. Source: Compara
Molecular_function	methylated histone residue binding Inferred from direct assay PubMed 21029866. Source: UniProtKB single-stranded RNA binding Inferred from electronic annotation. Source: Compara ubiquitin-protein ligase activity Inferred from electronic annotation. Source: Compara
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
BMI1	P35226	6	EBI-712912,EBI-2341576
KAT5	Q92993	2	EBI-712912,EBI-399080
PCGF1	Q9BSM1	2	EBI-712912,EBI-749901
PCGF2	P35227	6	EBI-712912,EBI-2129767
PCGF3	Q3KNV8	3	EBI-712912,EBI-2339807
PCGF5	Q86SE9	2	EBI-712912,EBI-2827999
PCGF6	Q9BYE7	2	EBI-712912,EBI-1048026
RING1	Q06587	3	EBI-712912,EBI-752313
RNF2	Q99496	4	EBI-712912,EBI-722416

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 389

389

Chromobox protein homolog 8

PRO_0000080215

Regions

Domain

11 – 69

59

Chromo

Amino acid modifications

Modified residue

110

1

Phosphoserine Ref.8 Ref.11

Modified residue

130

1

Phosphoserine Ref.8

Modified residue

191

1

Phosphoserine Ref.11

Modified residue

256

1

Phosphoserine Ref.8 Ref.10

Modified residue

265

1

Phosphoserine Ref.8

Modified residue

352

1

Phosphoserine Ref.8 Ref.11

Natural variations

Natural variant

317

1

G → V. Ref.2 Ref.3
Corresponds to variant rs4889891 [ dbSNP | Ensembl ].

VAR_014954

Secondary structure

1

.

.

.

.

.

.

.

.

.

.

.

.

389

Helix Strand Turn

Details...

Beta strand

10 – 22

13

Beta strand

25 – 32

8

Helix

37 – 39

3

Beta strand

41 – 44

4

Helix

45 – 47

3

Helix

51 – 59

9

Sequences

	Sequence		Length	Mass (Da)
	Q9HC52 [UniParc]. Last modified May 10, 2005. Version 3. Checksum: 651263C85B0ECD93	FASTA	389	43,396
	10 20 30 40 50 60 MELSAVGERV FAAEALLKRR IRKGRMEYLV KWKGWSQKYS TWEPEENILD ARLLAAFEER 70 80 90 100 110 120 EREMELYGPK KRGPKPKTFL LKAQAKAKAK TYEFRSDSAR GIRIPYPGRS PQDLASTSRA 130 140 150 160 170 180 REGLRNMGLS PPASSTSTSS TCRAEAPRDR DRDRDRDRER DRERERERER ERERERERER 190 200 210 220 230 240 GTSRVDDKPS SPGDSSKKRG PKPRKELPDP SQRPLGEPSA GLGEYLKGRK LDDTPSGAGK 250 260 270 280 290 300 FPAGHSVIQL ARRQDSDLVQ CGVTSPSSAE ATGKLAVDTF PARVIKHRAA FLEAKGQGAL 310 320 330 340 350 360 DPNGTRVRHG SGPPSSGGGL YRDMGAQGGR PSLIARIPVA RILGDPEEES WSPSLTNLEK 370 380 VVVTDVTSNF LTVTIKESNT DQGFFKEKR

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"HPC3 is a new human polycomb orthologue that interacts and associates with RING1 and Bmi1 and has transcriptional repression properties." Bardos J.I., Saurin A.J., Tissot C., Duprez E., Freemont P.S. J. Biol. Chem. 275:28785-28792(2000) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]	"Isolation of Polycomb and Trithorax-related genes that are expressed in human colorectal mucosa." Michael M.Z., James R.J. Submitted (DEC-2002) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA], VARIANT VAL-317. Tissue: Colon carcinoma.
[3]	"Complete sequencing and characterization of 21,243 full-length human cDNAs." Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S. Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], VARIANT VAL-317. Tissue: Embryo.
[4]	"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)." The MGC Project Team Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Lung and Muscle.
[5]	"The ENL moiety of the childhood leukemia-associated MLL-ENL oncoprotein recruits human Polycomb 3." Garcia-Cuellar M.P., Zilles O., Schreiner S.A., Birke M., Winkler T.H., Slany R.K. Oncogene 20:411-419(2001) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH MLLT3.
[6]	"The core of the polycomb repressive complex is compositionally and functionally conserved in flies and humans." Levine S.S., Weiss A., Erdjument-Bromage H., Shao Z., Tempst P., Kingston R.E. Mol. Cell. Biol. 22:6070-6078(2002) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY, IDENTIFICATION IN A PRC1-LIKE HPRC-H COMPLEX WITH BMI1; CBX2; CBX4; PHC1; PHC2; PHC3; RING1 AND RNF2.
[7]	"Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle." Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., Greff Z., Keri G., Stemmann O., Mann M. Mol. Cell 31:438-448(2008) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. Tissue: Cervix carcinoma.
[8]	"A quantitative atlas of mitotic phosphorylation." Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P. Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-110; SER-130; SER-256; SER-265 AND SER-352, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[9]	"Several distinct polycomb complexes regulate and co-localize on the INK4a tumor suppressor locus." Maertens G.N., El Messaoudi-Aubert S., Racek T., Stock J.K., Nicholls J., Rodriguez-Niedenfuhr M., Gil J., Peters G. PLoS ONE 4:E6380-E6380(2009) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION IN A PRC1-LIKE COMPLEX, INTERACTION WITH BMI1 AND PCGF2.
[10]	"Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions." Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K. Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-256, MASS SPECTROMETRY. Tissue: Leukemic T-cell.
[11]	"Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis." Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M. Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-110; SER-191 AND SER-352, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[12]	"Initial characterization of the human central proteome." Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J. BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[13]	"Interaction proteomics analysis of polycomb proteins defines distinct PRC1 Complexes in mammalian cells." Vandamme J., Volkel P., Rosnoblet C., Le Faou P., Angrand P.O. Mol. Cell. Proteomics 0:0-0(2011) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, MASS SPECTROMETRY, SUBCELLULAR LOCATION, IDENTIFICATION IN A PRC1-LIKE COMPLEX, INTERACTION WITH RING1; RNF2; PCGF1; PCGF2; PCGF3; BMI1; PCGF5 AND PCGF6.
[14]	"Recognition and specificity determinants of the human cbx chromodomains." Kaustov L., Ouyang H., Amaya M., Lemak A., Nady N., Duan S., Wasney G.A., Li Z., Vedadi M., Schapira M., Min J., Arrowsmith C.H. J. Biol. Chem. 286:521-529(2011) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.55 ANGSTROMS) OF 8-61 IN COMPLEX WITH HISTONE H3 PEPTIDE.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

AF174482 mRNA. Translation: AAG09180.1.
AF266479 mRNA. Translation: AAF76328.2.
AK074560 mRNA. Translation: BAC11061.1.
BC008937 mRNA. Translation: AAH08937.1.
BC009376 mRNA. Translation: AAH09376.1.
BC019289 mRNA. Translation: AAH19289.1.

IPI

IPI00307659.

RefSeq

NP_065700.1. NM_020649.2.

UniGene

Hs.387258.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
3I91	X-ray	1.55	A/B	8-61	[»]

ProteinModelPortal

Q9HC52.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-44566N.

IntAct

Q9HC52. 68 interactions.

MINT

MINT-1372508.

STRING

9606.ENSP00000269385.

PTM databases

PhosphoSite

Q9HC52.

Polymorphism databases

DMDM

78099843.

Proteomic databases

PaxDb

Q9HC52.

PeptideAtlas

Q9HC52.

PRIDE

Q9HC52.

Protocols and materials databases

DNASU

57332.

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000269385; ENSP00000269385; ENSG00000141570.
ENST00000570393; ENSP00000459583; ENSG00000262572.

GeneID

57332.

KEGG

hsa:57332.

UCSC

uc002jxd.2. human.

Organism-specific databases

CTD

57332.

GeneCards

GC17M077765.

HGNC

HGNC:15962. CBX8.

HPA

HPA031462.

neXtProt

NX_Q9HC52.

PharmGKB

PA26133.

GenAtlas

Search...

Phylogenomic databases

eggNOG

NOG304493.

HOGENOM

HOG000233642.

HOVERGEN

HBG003608.

InParanoid

Q9HC52.

KO

K11455.

OMA

KFPAGHS.

OrthoDB

EOG4B8JDK.

PhylomeDB

Q9HC52.

Gene expression databases

ArrayExpress

Q9HC52.

Bgee

Q9HC52.

CleanEx

HS_CBX8.

Genevestigator

Q9HC52.

GermOnline

ENSG00000141570. Homo sapiens.

Family and domain databases

InterPro

IPR023780. Chromo_domain.
IPR000953. Chromo_domain/shadow.
IPR016197. Chromodomain-like.
IPR023779. Chromodomain_CS.
[Graphical view]

Pfam

PF00385. Chromo. 1 hit.
[Graphical view]

SMART

SM00298. CHROMO. 1 hit.
[Graphical view]

SUPFAM

SSF54160. Chromodomain-like. 1 hit.

PROSITE

PS00598. CHROMO_1. 1 hit.
PS50013. CHROMO_2. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

EvolutionaryTrace

Q9HC52.

GenomeRNAi

57332.

NextBio

63438.

Entry information

Entry name

CBX8_HUMAN

Accession

Primary (citable) accession number: Q9HC52
Secondary accession number(s): Q96H39, Q9NR07

Entry history

Integrated into UniProtKB/Swiss-Prot:	August 29, 2001
Last sequence update:	May 10, 2005
Last modified:	May 1, 2013
This is version 111 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.