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O95931

- CBX7_HUMAN

UniProt

O95931 - CBX7_HUMAN

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Protein

Chromobox protein homolog 7

Gene

CBX7

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

Functioni

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.4 Publications

GO - Molecular functioni

  1. chromatin binding Source: Ensembl
  2. single-stranded RNA binding Source: Ensembl

GO - Biological processi

  1. chromatin modification Source: UniProtKB-KW
  2. negative regulation of transcription from RNA polymerase II promoter Source: UniProtKB
  3. sebaceous gland development Source: Ensembl
  4. transcription, DNA-templated Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Chromatin regulator, Repressor

Keywords - Biological processi

Transcription, Transcription regulation

Names & Taxonomyi

Protein namesi
Recommended name:
Chromobox protein homolog 7
Gene namesi
Name:CBX7
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 22

Organism-specific databases

HGNCiHGNC:1557. CBX7.

Subcellular locationi

Nucleus 3 Publications

GO - Cellular componenti

  1. cytoplasm Source: HPA
  2. heterochromatin Source: Ensembl
  3. nuclear chromatin Source: UniProtKB
  4. nucleus Source: UniProtKB
  5. PcG protein complex Source: UniProtKB
  6. PRC1 complex Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi31 – 311K → A: Loss of cellular lifespan extension. 1 Publication
Mutagenesisi32 – 321W → A: Loss of cellular lifespan extension. 1 Publication
Mutagenesisi234 – 2341F → D: Loss of interaction with RNF2. 1 Publication
Mutagenesisi244 – 2441F → D: Reduced interaction with RNF2. 1 Publication

Organism-specific databases

PharmGKBiPA26132.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 251251Chromobox protein homolog 7PRO_0000080212Add
BLAST

Proteomic databases

MaxQBiO95931.
PaxDbiO95931.
PRIDEiO95931.

PTM databases

PhosphoSiteiO95931.

Expressioni

Gene expression databases

BgeeiO95931.
CleanExiHS_CBX7.
ExpressionAtlasiO95931. baseline and differential.
GenevestigatoriO95931.

Organism-specific databases

HPAiCAB011574.
HPA056480.

Interactioni

Subunit structurei

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 PCGF6.6 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
BMI1P352267EBI-3923843,EBI-2341576
PCGF2P352273EBI-3923843,EBI-2129767
PCGF3Q3KNV82EBI-3923843,EBI-2339807
PCGF6Q9BYE72EBI-3923843,EBI-1048026
RING1Q065873EBI-3923843,EBI-752313
RNF2Q994963EBI-3923843,EBI-722416

Protein-protein interaction databases

BioGridi117044. 31 interactions.
DIPiDIP-44565N.
IntActiO95931. 22 interactions.
MINTiMINT-4543653.
STRINGi9606.ENSP00000216133.

Structurei

Secondary structure

1
251
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi13 – 2210Combined sources
Beta strandi25 – 328Combined sources
Helixi37 – 393Combined sources
Beta strandi41 – 444Combined sources
Helixi45 – 473Combined sources
Helixi51 – 6010Combined sources
Beta strandi221 – 2277Combined sources
Beta strandi230 – 2389Combined sources
Turni241 – 2433Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2K1BNMR-A7-62[»]
2L12NMR-A7-62[»]
2L1BNMR-A8-62[»]
3GS2X-ray1.70B/D219-248[»]
4MN3X-ray1.54A7-62[»]
ProteinModelPortaliO95931.
SMRiO95931. Positions 7-62, 219-248.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiO95931.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini11 – 6959ChromoPROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni223 – 23614Required for cellular lifespan extensionAdd
BLAST

Sequence similaritiesi

Contains 1 chromo domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiNOG258927.
GeneTreeiENSGT00530000063056.
HOGENOMiHOG000233642.
HOVERGENiHBG019320.
InParanoidiO95931.
KOiK11454.
OMAiPPPWTPV.
OrthoDBiEOG77T15B.
PhylomeDBiO95931.
TreeFamiTF106456.

Family and domain databases

InterProiIPR017984. Chromo_dom_subgr.
IPR023780. Chromo_domain.
IPR000953. Chromo_domain/shadow.
IPR016197. Chromodomain-like.
IPR023779. Chromodomain_CS.
[Graphical view]
PfamiPF00385. Chromo. 1 hit.
[Graphical view]
PRINTSiPR00504. CHROMODOMAIN.
SMARTiSM00298. CHROMO. 1 hit.
[Graphical view]
SUPFAMiSSF54160. SSF54160. 1 hit.
PROSITEiPS00598. CHROMO_1. 1 hit.
PS50013. CHROMO_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

O95931-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MELSAIGEQV FAVESIRKKR VRKGKVEYLV KWKGWPPKYS TWEPEEHILD
60 70 80 90 100
PRLVMAYEEK EERDRASGYR KRGPKPKRLL LQRLYSMDLR SSHKAKGKEK
110 120 130 140 150
LCFSLTCPLG SGSPEGVVKA GAPELVDKGP LVPTLPFPLR KPRKAHKYLR
160 170 180 190 200
LSRKKFPPRG PNLESHSHRR ELFLQEPPAP DVLQAAGEWE PAAQPPEEEA
210 220 230 240 250
DADLAEGPPP WTPALPSSEV TVTDITANSI TVTFREAQAA EGFFRDRSGK

F
Length:251
Mass (Da):28,341
Last modified:May 1, 1999 - v1
Checksum:iA90019C1D08812B8
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti77 – 771K → R in AAH51773. (PubMed:15489334)Curated
Sequence conflicti239 – 2391A → P in AAH51773. (PubMed:15489334)Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AL031846 Genomic DNA. Translation: CAB36555.1.
BC051773 mRNA. Translation: AAH51773.1.
CCDSiCCDS13986.1.
RefSeqiNP_783640.1. NM_175709.3.
UniGeneiHs.356416.

Genome annotation databases

EnsembliENST00000216133; ENSP00000216133; ENSG00000100307.
GeneIDi23492.
KEGGihsa:23492.
UCSCiuc003axb.3. human.

Cross-referencesi

Web resourcesi

Atlas of Genetics and Cytogenetics in Oncology and Haematology

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AL031846 Genomic DNA. Translation: CAB36555.1 .
BC051773 mRNA. Translation: AAH51773.1 .
CCDSi CCDS13986.1.
RefSeqi NP_783640.1. NM_175709.3.
UniGenei Hs.356416.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
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 [» ]
4MN3 X-ray 1.54 A 7-62 [» ]
ProteinModelPortali O95931.
SMRi O95931. Positions 7-62, 219-248.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 117044. 31 interactions.
DIPi DIP-44565N.
IntActi O95931. 22 interactions.
MINTi MINT-4543653.
STRINGi 9606.ENSP00000216133.

Chemistry

BindingDBi O95931.
ChEMBLi CHEMBL1764946.

PTM databases

PhosphoSitei O95931.

Proteomic databases

MaxQBi O95931.
PaxDbi O95931.
PRIDEi O95931.

Protocols and materials databases

DNASUi 23492.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000216133 ; ENSP00000216133 ; ENSG00000100307 .
GeneIDi 23492.
KEGGi hsa:23492.
UCSCi uc003axb.3. human.

Organism-specific databases

CTDi 23492.
GeneCardsi GC22M040104.
HGNCi HGNC:1557. CBX7.
HPAi CAB011574.
HPA056480.
MIMi 608457. gene.
neXtProti NX_O95931.
PharmGKBi PA26132.
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG258927.
GeneTreei ENSGT00530000063056.
HOGENOMi HOG000233642.
HOVERGENi HBG019320.
InParanoidi O95931.
KOi K11454.
OMAi PPPWTPV.
OrthoDBi EOG77T15B.
PhylomeDBi O95931.
TreeFami TF106456.

Miscellaneous databases

EvolutionaryTracei O95931.
GenomeRNAii 23492.
NextBioi 45855.
PROi O95931.
SOURCEi Search...

Gene expression databases

Bgeei O95931.
CleanExi HS_CBX7.
ExpressionAtlasi O95931. baseline and differential.
Genevestigatori O95931.

Family and domain databases

InterProi IPR017984. Chromo_dom_subgr.
IPR023780. Chromo_domain.
IPR000953. Chromo_domain/shadow.
IPR016197. Chromodomain-like.
IPR023779. Chromodomain_CS.
[Graphical view ]
Pfami PF00385. Chromo. 1 hit.
[Graphical view ]
PRINTSi PR00504. CHROMODOMAIN.
SMARTi SM00298. CHROMO. 1 hit.
[Graphical view ]
SUPFAMi SSF54160. SSF54160. 1 hit.
PROSITEi PS00598. CHROMO_1. 1 hit.
PS50013. CHROMO_2. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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, 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. Cited for: STRUCTURE BY NMR OF 8-62, FUNCTION, INTERACTION WITH TRIMETHYLATED LYSINE RESIDUES.

Entry informationi

Entry nameiCBX7_HUMAN
AccessioniPrimary (citable) accession number: O95931
Secondary accession number(s): Q86T17
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 29, 2001
Last sequence update: May 1, 1999
Last modified: November 26, 2014
This is version 124 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (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.

Miscellaneousi

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.

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 22
    Human chromosome 22: entries, gene names and cross-references to MIM
  2. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3