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O95931 (CBX7_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 118. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Chromobox protein homolog 7
Gene names
Name:CBX7
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length251 AA.
Sequence statusComplete.
Protein existenceEvidence 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.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 251251Chromobox protein homolog 7
PRO_0000080212

Regions

Domain11 – 6959Chromo
Region223 – 23614Required for cellular lifespan extension

Experimental info

Mutagenesis311K → A: Loss of cellular lifespan extension. Ref.3
Mutagenesis321W → A: Loss of cellular lifespan extension. Ref.3
Mutagenesis2341F → D: Loss of interaction with RNF2. Ref.9
Mutagenesis2441F → D: Reduced interaction with RNF2. Ref.9
Sequence conflict771K → R in AAH51773. Ref.2
Sequence conflict2391A → P in AAH51773. Ref.2

Secondary structure

.................. 251
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
O95931 [UniParc].

Last modified May 1, 1999. Version 1.
Checksum: A90019C1D08812B8

FASTA25128,341
        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 

« Hide

References

« Hide '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. expand/collapse author list , 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, IDENTIFICATION BY 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.
RefSeqNP_783640.1. NM_175709.3.
UniGeneHs.356416.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2K1BNMR-A7-62[»]
2L12NMR-A7-62[»]
2L1BNMR-A8-62[»]
3GS2X-ray1.70B/D219-248[»]
ProteinModelPortalO95931.
SMRO95931. Positions 1-71, 219-248.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid117044. 27 interactions.
DIPDIP-44565N.
IntActO95931. 22 interactions.
MINTMINT-4543653.
STRING9606.ENSP00000216133.

Chemistry

ChEMBLCHEMBL1764946.

PTM databases

PhosphoSiteO95931.

Proteomic databases

PaxDbO95931.
PRIDEO95931.

Protocols and materials databases

DNASU23492.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000216133; ENSP00000216133; ENSG00000100307.
GeneID23492.
KEGGhsa:23492.
UCSCuc003axb.3. human.

Organism-specific databases

CTD23492.
GeneCardsGC22M039605.
HGNCHGNC:1557. CBX7.
HPACAB011574.
HPA056480.
MIM608457. gene.
neXtProtNX_O95931.
PharmGKBPA26132.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG258927.
HOGENOMHOG000233642.
HOVERGENHBG019320.
InParanoidO95931.
KOK11454.
OMAPPPWTPV.
OrthoDBEOG77T15B.
PhylomeDBO95931.
TreeFamTF106456.

Gene expression databases

ArrayExpressO95931.
BgeeO95931.
CleanExHS_CBX7.
GenevestigatorO95931.

Family and domain databases

InterProIPR017984. Chromo_dom_subgr.
IPR023780. Chromo_domain.
IPR000953. Chromo_domain/shadow.
IPR016197. Chromodomain-like.
IPR023779. Chromodomain_CS.
[Graphical view]
PfamPF00385. Chromo. 1 hit.
[Graphical view]
PRINTSPR00504. CHROMODOMAIN.
SMARTSM00298. CHROMO. 1 hit.
[Graphical view]
SUPFAMSSF54160. SSF54160. 1 hit.
PROSITEPS00598. CHROMO_1. 1 hit.
PS50013. CHROMO_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceO95931.
GenomeRNAi23492.
NextBio45855.
PROO95931.
SOURCESearch...

Entry information

Entry nameCBX7_HUMAN
AccessionPrimary (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: April 16, 2014
This is version 118 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny 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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human chromosome 22

Human chromosome 22: entries, gene names and cross-references to MIM