O95931 (CBX7_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Chromobox protein homolog 7

Gene names

Name:

CBX7

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	251 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. Promotes histone H3 trimethylation at 'Lys-9' (H3K9me3). Binds to trimethylated lysine residues in histones, and possibly also other proteins. Regulator of cellular lifespan by maintaining the repression of CDKN2A, but not by inducing telomerase activity. Ref.5 Ref.6 Ref.7 Ref.10
Subunit structure	Component of a PRC1-like complex. Interacts with RING1 and RNF2/RING1B, but not with BMI1, EED or EZH2. Interacts with PCGF1, PCGF2, PCGF3, PCGF5 and PCGF6. Ref.3 Ref.4 Ref.5 Ref.7 Ref.9 Ref.10
Subcellular location	Nucleus Ref.3 Ref.6 Ref.7.
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.
Sequence similarities	Contains 1 chromo domain.

Ontologies

Keywords
Biological process	Transcription Transcription regulation
Cellular component	Nucleus
Molecular function	Chromatin regulator Repressor
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	chromatin modification Inferred from electronic annotation. Source: UniProtKB-KW negative regulation of transcription from RNA polymerase II promoter Inferred from mutant phenotype Ref.5Ref.7. Source: UniProtKB transcription, DNA-dependent Inferred from electronic annotation. Source: UniProtKB-KW
Cellular_component	PRC1 complex Inferred from sequence or structural similarity. Source: UniProtKB heterochromatin Inferred from electronic annotation. Source: Compara nuclear chromatin Inferred from direct assay Ref.5. Source: UniProtKB
Molecular_function	single-stranded RNA binding Inferred from electronic annotation. Source: Compara
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
BMI1	P35226	5	EBI-3923843,EBI-2341576
PCGF2	P35227	3	EBI-3923843,EBI-2129767
PCGF3	Q3KNV8	2	EBI-3923843,EBI-2339807
PCGF6	Q9BYE7	2	EBI-3923843,EBI-1048026
RING1	Q06587	3	EBI-3923843,EBI-752313
RNF2	Q99496	3	EBI-3923843,EBI-722416

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 251

251

Chromobox protein homolog 7

PRO_0000080212

Regions

Domain

11 – 69

59

Chromo

Region

223 – 236

14

Required for cellular lifespan extension

Experimental info

Mutagenesis

31

1

K → A: Loss of cellular lifespan extension. Ref.3

Mutagenesis

32

1

W → A: Loss of cellular lifespan extension. Ref.3

Mutagenesis

234

1

F → D: Loss of interaction with RNF2. Ref.9

Mutagenesis

244

1

F → D: Reduced interaction with RNF2. Ref.9

Sequence conflict

77

1

K → R in AAH51773. Ref.2

Sequence conflict

239

1

A → P in AAH51773. Ref.2

Secondary structure

1

.

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251

Helix Strand Turn

Details...

Beta strand

14 – 22

9

Beta strand

25 – 31

7

Helix

37 – 39

3

Beta strand

42 – 44

3

Turn

45 – 47

3

Helix

51 – 58

8

Beta strand

221 – 227

7

Beta strand

230 – 238

9

Turn

241 – 243

3

Sequences

	Sequence		Length	Mass (Da)
	O95931 [UniParc]. Last modified May 1, 1999. Version 1. Checksum: A90019C1D08812B8	FASTA	251	28,341
	10 20 30 40 50 60 MELSAIGEQV FAVESIRKKR VRKGKVEYLV KWKGWPPKYS TWEPEEHILD PRLVMAYEEK 70 80 90 100 110 120 EERDRASGYR KRGPKPKRLL LQRLYSMDLR SSHKAKGKEK LCFSLTCPLG SGSPEGVVKA 130 140 150 160 170 180 GAPELVDKGP LVPTLPFPLR KPRKAHKYLR LSRKKFPPRG PNLESHSHRR ELFLQEPPAP 190 200 210 220 230 240 DVLQAAGEWE PAAQPPEEEA DADLAEGPPP WTPALPSSEV TVTDITANSI TVTFREAQAA 250 EGFFRDRSGK F

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"The DNA sequence of human chromosome 22." Dunham I., Hunt A.R., Collins J.E., Bruskiewich R., Beare D.M., Clamp M., Smink L.J., Ainscough R., Almeida J.P., Babbage A.K., Bagguley C., Bailey J., Barlow K.F., Bates K.N., Beasley O.P., Bird C.P., Blakey S.E., Bridgeman A.M. , Buck D., Burgess J., Burrill W.D., Burton J., Carder C., Carter N.P., Chen Y., Clark G., Clegg S.M., Cobley V.E., Cole C.G., Collier R.E., Connor R., Conroy D., Corby N.R., Coville G.J., Cox A.V., Davis J., Dawson E., Dhami P.D., Dockree C., Dodsworth S.J., Durbin R.M., Ellington A.G., Evans K.L., Fey J.M., Fleming K., French L., Garner A.A., Gilbert J.G.R., Goward M.E., Grafham D.V., Griffiths M.N.D., Hall C., Hall R.E., Hall-Tamlyn G., Heathcott R.W., Ho S., Holmes S., Hunt S.E., Jones M.C., Kershaw J., Kimberley A.M., King A., Laird G.K., Langford C.F., Leversha M.A., Lloyd C., Lloyd D.M., Martyn I.D., Mashreghi-Mohammadi M., Matthews L.H., Mccann O.T., Mcclay J., Mclaren S., McMurray A.A., Milne S.A., Mortimore B.J., Odell C.N., Pavitt R., Pearce A.V., Pearson D., Phillimore B.J.C.T., Phillips S.H., Plumb R.W., Ramsay H., Ramsey Y., Rogers L., Ross M.T., Scott C.E., Sehra H.K., Skuce C.D., Smalley S., Smith M.L., Soderlund C., Spragon L., Steward C.A., Sulston J.E., Swann R.M., Vaudin M., Wall M., Wallis J.M., Whiteley M.N., Willey D.L., Williams L., Williams S.A., Williamson H., Wilmer T.E., Wilming L., Wright C.L., Hubbard T., Bentley D.R., Beck S., Rogers J., Shimizu N., Minoshima S., Kawasaki K., Sasaki T., Asakawa S., Kudoh J., Shintani A., Shibuya K., Yoshizaki Y., Aoki N., Mitsuyama S., Roe B.A., Chen F., Chu L., Crabtree J., Deschamps S., Do A., Do T., Dorman A., Fang F., Fu Y., Hu P., Hua A., Kenton S., Lai H., Lao H.I., Lewis J., Lewis S., Lin S.-P., Loh P., Malaj E., Nguyen T., Pan H., Phan S., Qi S., Qian Y., Ray L., Ren Q., Shaull S., Sloan D., Song L., Wang Q., Wang Y., Wang Z., White J., Willingham D., Wu H., Yao Z., Zhan M., Zhang G., Chissoe S., Murray J., Miller N., Minx P., Fulton R., Johnson D., Bemis G., Bentley D., Bradshaw H., Bourne S., Cordes M., Du Z., Fulton L., Goela D., Graves T., Hawkins J., Hinds K., Kemp K., Latreille P., Layman D., Ozersky P., Rohlfing T., Scheet P., Walker C., Wamsley A., Wohldmann P., Pepin K., Nelson J., Korf I., Bedell J.A., Hillier L.W., Mardis E., Waterston R., Wilson R., Emanuel B.S., Shaikh T., Kurahashi H., Saitta S., Budarf M.L., McDermid H.E., Johnson A., Wong A.C.C., Morrow B.E., Edelmann L., Kim U.J., Shizuya H., Simon M.I., Dumanski J.P., Peyrard M., Kedra D., Seroussi E., Fransson I., Tapia I., Bruder C.E., O'Brien K.P., Wilkinson P., Bodenteich A., Hartman K., Hu X., Khan A.S., Lane L., Tilahun Y., Wright H. Nature 402:489-495(1999) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[2]	"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: PNS.
[3]	"Polycomb CBX7 has a unifying role in cellular lifespan." Gil J., Bernard D., Martinez D., Beach D. Nat. Cell Biol. 6:67-72(2004) [PubMed] [Europe PMC] [Abstract] Cited for: SUBCELLULAR LOCATION, INTERACTION WITH RING1, MUTAGENESIS OF LYS-31 AND TRP-32.
[4]	"Ring1B contains a ubiquitin-like docking module for interaction with Cbx proteins." Bezsonova I., Walker J.R., Bacik J.P., Duan S., Dhe-Paganon S., Arrowsmith C.H. Biochemistry 48:10542-10548(2009) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH RNF2.
[5]	"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: FUNCTION, IDENTIFICATION IN A PRC1-LIKE COMPLEX, INTERACTION WITH BMI1.
[6]	"Polycomb CBX7 directly controls trimethylation of histone H3 at lysine 9 at the p16 locus." Li Q., Wang X., Lu Z., Zhang B., Guan Z., Liu Z., Zhong Q., Gu L., Zhou J., Zhu B., Ji J., Deng D. PLoS ONE 5:E13732-E13732(2010) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, SUBCELLULAR LOCATION.
[7]	"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.
[8]	"Solution NMR structure of the chromobox protein homolog 7." Structural genomics consortium (SGC) Submitted (MAR-2008) to the PDB data bank Cited for: STRUCTURE BY NMR OF 7-62.
[9]	"Polycomb group targeting through different binding partners of RING1B C-terminal domain." Wang R., Taylor A.B., Leal B.Z., Chadwell L.V., Ilangovan U., Robinson A.K., Schirf V., Hart P.J., Lafer E.M., Demeler B., Hinck A.P., McEwen D.G., Kim C.A. Structure 18:966-975(2010) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS) OF 219-248 IN COMPLEX WITH RNF2, INTERACTION WITH RNF2, MUTAGENESIS OF PHE-234 AND PHE-244.
[10]	"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: STRUCTURE BY NMR OF 8-62, FUNCTION, INTERACTION WITH TRIMETHYLATED LYSINE RESIDUES.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

AL031846 Genomic DNA. Translation: CAB36555.1.
BC051773 mRNA. Translation: AAH51773.1.

IPI

IPI00001385.

RefSeq

NP_783640.1. NM_175709.3.

UniGene

Hs.356416.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
2K1B	NMR	-	A	7-62	[»]
2L12	NMR	-	A	7-62	[»]
2L1B	NMR	-	A	8-62	[»]
3GS2	X-ray	1.70	B/D	219-248	[»]

ProteinModelPortal

O95931.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-44565N.

IntAct

O95931. 19 interactions.

MINT

MINT-4543653.

STRING

9606.ENSP00000216133.

PTM databases

PhosphoSite

O95931.

Proteomic databases

PaxDb

O95931.

PRIDE

O95931.

Protocols and materials databases

DNASU

23492.

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000216133; ENSP00000216133; ENSG00000100307.

GeneID

23492.

KEGG

hsa:23492.

UCSC

uc003axb.3. human.

Organism-specific databases

CTD

23492.

GeneCards

GC22M039519.

HGNC

HGNC:1557. CBX7.

HPA

CAB011574.

MIM

608457. gene.

neXtProt

NX_O95931.

PharmGKB

PA26132.

GenAtlas

Search...

Phylogenomic databases

eggNOG

NOG258927.

HOGENOM

HOG000233642.

HOVERGEN

HBG019320.

InParanoid

O95931.

KO

K11454.

OMA

CFSLARP.

OrthoDB

EOG42RD8T.

PhylomeDB

O95931.

Gene expression databases

ArrayExpress

O95931.

Bgee

O95931.

CleanEx

HS_CBX7.

Genevestigator

O95931.

GermOnline

ENSG00000100307. Homo sapiens.

Family and domain databases

InterPro

IPR017984. Chromo_dom_subgr.
IPR023780. Chromo_domain.
IPR000953. Chromo_domain/shadow.
IPR016197. Chromodomain-like.
IPR023779. Chromodomain_CS.
[Graphical view]

Pfam

PF00385. Chromo. 1 hit.
[Graphical view]

PRINTS

PR00504. CHROMODOMAIN.

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

ChEMBL

CHEMBL1764946.

EvolutionaryTrace

O95931.

GenomeRNAi

23492.

NextBio

45855.

SOURCE

Search...

Entry information

Entry name

CBX7_HUMAN

Accession

Primary (citable) accession number: O95931
Secondary accession number(s): Q86T17

Entry history

Integrated into UniProtKB/Swiss-Prot:	August 29, 2001
Last sequence update:	May 1, 1999
Last modified:	May 1, 2013
This is version 109 of the entry and version 1 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.