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Protein

Chromobox protein homolog 8

Gene

CBX8

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: 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.1 Publication

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Chromatin regulator, Repressor

Keywords - Biological processi

Transcription, Transcription regulation

Enzyme and pathway databases

BioCyciZFISH:ENSG00000141570-MONOMER.
ReactomeiR-HSA-2559580. Oxidative Stress Induced Senescence.
R-HSA-3108214. SUMOylation of DNA damage response and repair proteins.
R-HSA-4570464. SUMOylation of RNA binding proteins.

Names & Taxonomyi

Protein namesi
Recommended name:
Chromobox protein homolog 8
Alternative name(s):
Polycomb 3 homolog
Short name:
Pc3
Short name:
hPc3
Rectachrome 1
Gene namesi
Name:CBX8
Synonyms:PC3, RC1
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 17

Organism-specific databases

HGNCiHGNC:15962. CBX8.

Subcellular locationi

  • Nucleus 1 Publication

GO - Cellular componenti

  • heterochromatin Source: Ensembl
  • nuclear chromatin Source: UniProtKB
  • nucleoplasm Source: HPA
  • nucleus Source: UniProtKB
  • PcG protein complex Source: UniProtKB
  • PRC1 complex Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Organism-specific databases

DisGeNETi57332.
OpenTargetsiENSG00000141570.
PharmGKBiPA26133.

Chemistry databases

ChEMBLiCHEMBL3232684.

Polymorphism and mutation databases

BioMutaiCBX8.
DMDMi78099843.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000802151 – 389Chromobox protein homolog 8Add BLAST389

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei110PhosphoserineCombined sources1
Modified residuei130PhosphoserineCombined sources1
Modified residuei191PhosphoserineCombined sources1
Modified residuei256PhosphoserineCombined sources1
Modified residuei265PhosphoserineCombined sources1
Modified residuei311PhosphoserineCombined sources1
Modified residuei332PhosphoserineCombined sources1
Modified residuei352PhosphoserineCombined sources1

Keywords - PTMi

Phosphoprotein

Proteomic databases

EPDiQ9HC52.
MaxQBiQ9HC52.
PaxDbiQ9HC52.
PeptideAtlasiQ9HC52.
PRIDEiQ9HC52.

PTM databases

iPTMnetiQ9HC52.
PhosphoSitePlusiQ9HC52.

Expressioni

Gene expression databases

BgeeiENSG00000141570.
CleanExiHS_CBX8.
ExpressionAtlasiQ9HC52. baseline and differential.
GenevisibleiQ9HC52. HS.

Organism-specific databases

HPAiHPA031462.

Interactioni

Subunit structurei

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).By similarity

Binary interactionsi

WithEntry#Exp.IntActNotes
BMI1P3522616EBI-712912,EBI-2341576
CALCOCO2Q131375EBI-712912,EBI-739580
CBX4O002573EBI-712912,EBI-722425
CCDC136Q96JN2-23EBI-712912,EBI-10171416
CCDC57Q2TAC23EBI-712912,EBI-2808286
FSD2A1L4K15EBI-712912,EBI-5661036
GOLGA2Q083793EBI-712912,EBI-618309
GPRASP2Q96D093EBI-712912,EBI-473189
HMBOX1Q6NT765EBI-712912,EBI-2549423
IKZF1Q134223EBI-712912,EBI-745305
KAT5Q929932EBI-712912,EBI-399080
KCTD9Q7L2735EBI-712912,EBI-4397613
KIFC3Q9BVG83EBI-712912,EBI-2125614
KRT40Q6A1625EBI-712912,EBI-10171697
LZTS2Q9BRK45EBI-712912,EBI-741037
MID2Q9UJV3-25EBI-712912,EBI-10172526
MTUS2Q5JR593EBI-712912,EBI-742948
PCGF1Q9BSM14EBI-712912,EBI-749901
PCGF2P352279EBI-712912,EBI-2129767
PCGF3Q3KNV84EBI-712912,EBI-2339807
PCGF5Q86SE94EBI-712912,EBI-2827999
PCGF6Q9BYE73EBI-712912,EBI-1048026
PHC2Q8IXK07EBI-712912,EBI-713786
PNMA2Q9UL425EBI-712912,EBI-302355
RING1Q0658711EBI-712912,EBI-752313
RNF2Q994969EBI-712912,EBI-722416
RPGRIP1Q96KN73EBI-712912,EBI-1050213
SOX5P357113EBI-712912,EBI-3505701
TFCP2Q128003EBI-712912,EBI-717422
TRAF2Q129335EBI-712912,EBI-355744
TSGA10Q9BZW73EBI-712912,EBI-744794
USP11P517845EBI-712912,EBI-306876
USP7Q930097EBI-712912,EBI-302474
ZBTB14O438295EBI-712912,EBI-10176632

GO - Molecular functioni

  • methylated histone binding Source: UniProtKB

Protein-protein interaction databases

BioGridi121487. 135 interactors.
DIPiDIP-44566N.
IntActiQ9HC52. 169 interactors.
MINTiMINT-1372508.
STRINGi9606.ENSP00000269385.

Chemistry databases

BindingDBiQ9HC52.

Structurei

Secondary structure

1389
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi9 – 11Combined sources3
Beta strandi13 – 22Combined sources10
Beta strandi25 – 32Combined sources8
Helixi37 – 39Combined sources3
Beta strandi41 – 44Combined sources4
Helixi45 – 47Combined sources3
Helixi51 – 59Combined sources9
Beta strandi334 – 336Combined sources3
Helixi339 – 342Combined sources4

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2N4QNMR-A327-349[»]
3I91X-ray1.55A/B8-61[»]
5EQ0X-ray1.18A7-61[»]
ProteinModelPortaliQ9HC52.
SMRiQ9HC52.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ9HC52.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini11 – 69ChromoPROSITE-ProRule annotationAdd BLAST59

Sequence similaritiesi

Contains 1 chromo domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiENOG410IPQ7. Eukaryota.
ENOG410XRRX. LUCA.
GeneTreeiENSGT00530000063056.
HOGENOMiHOG000233642.
HOVERGENiHBG003608.
InParanoidiQ9HC52.
KOiK11455.
OMAiTGKFPAG.
OrthoDBiEOG091G0MFV.
PhylomeDBiQ9HC52.
TreeFamiTF106456.

Family and domain databases

InterProiIPR033773. CBX7_C.
IPR000953. Chromo/shadow_dom.
IPR023780. Chromo_domain.
IPR016197. Chromodomain-like.
IPR023779. Chromodomain_CS.
[Graphical view]
PfamiPF17218. CBX7_C. 1 hit.
PF00385. Chromo. 1 hit.
[Graphical view]
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.

Q9HC52-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MELSAVGERV FAAEALLKRR IRKGRMEYLV KWKGWSQKYS TWEPEENILD
60 70 80 90 100
ARLLAAFEER EREMELYGPK KRGPKPKTFL LKAQAKAKAK TYEFRSDSAR
110 120 130 140 150
GIRIPYPGRS PQDLASTSRA REGLRNMGLS PPASSTSTSS TCRAEAPRDR
160 170 180 190 200
DRDRDRDRER DRERERERER ERERERERER GTSRVDDKPS SPGDSSKKRG
210 220 230 240 250
PKPRKELPDP SQRPLGEPSA GLGEYLKGRK LDDTPSGAGK FPAGHSVIQL
260 270 280 290 300
ARRQDSDLVQ CGVTSPSSAE ATGKLAVDTF PARVIKHRAA FLEAKGQGAL
310 320 330 340 350
DPNGTRVRHG SGPPSSGGGL YRDMGAQGGR PSLIARIPVA RILGDPEEES
360 370 380
WSPSLTNLEK VVVTDVTSNF LTVTIKESNT DQGFFKEKR
Length:389
Mass (Da):43,396
Last modified:May 10, 2005 - v3
Checksum:i651263C85B0ECD93
GO

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_014954317G → V.2 PublicationsCorresponds to variant rs4889891dbSNPEnsembl.1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS11765.1.
RefSeqiNP_065700.1. NM_020649.2.
UniGeneiHs.387258.

Genome annotation databases

EnsembliENST00000269385; ENSP00000269385; ENSG00000141570.
GeneIDi57332.
KEGGihsa:57332.
UCSCiuc002jxd.3. human.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS11765.1.
RefSeqiNP_065700.1. NM_020649.2.
UniGeneiHs.387258.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2N4QNMR-A327-349[»]
3I91X-ray1.55A/B8-61[»]
5EQ0X-ray1.18A7-61[»]
ProteinModelPortaliQ9HC52.
SMRiQ9HC52.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi121487. 135 interactors.
DIPiDIP-44566N.
IntActiQ9HC52. 169 interactors.
MINTiMINT-1372508.
STRINGi9606.ENSP00000269385.

Chemistry databases

BindingDBiQ9HC52.
ChEMBLiCHEMBL3232684.

PTM databases

iPTMnetiQ9HC52.
PhosphoSitePlusiQ9HC52.

Polymorphism and mutation databases

BioMutaiCBX8.
DMDMi78099843.

Proteomic databases

EPDiQ9HC52.
MaxQBiQ9HC52.
PaxDbiQ9HC52.
PeptideAtlasiQ9HC52.
PRIDEiQ9HC52.

Protocols and materials databases

DNASUi57332.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000269385; ENSP00000269385; ENSG00000141570.
GeneIDi57332.
KEGGihsa:57332.
UCSCiuc002jxd.3. human.

Organism-specific databases

CTDi57332.
DisGeNETi57332.
GeneCardsiCBX8.
HGNCiHGNC:15962. CBX8.
HPAiHPA031462.
neXtProtiNX_Q9HC52.
OpenTargetsiENSG00000141570.
PharmGKBiPA26133.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiENOG410IPQ7. Eukaryota.
ENOG410XRRX. LUCA.
GeneTreeiENSGT00530000063056.
HOGENOMiHOG000233642.
HOVERGENiHBG003608.
InParanoidiQ9HC52.
KOiK11455.
OMAiTGKFPAG.
OrthoDBiEOG091G0MFV.
PhylomeDBiQ9HC52.
TreeFamiTF106456.

Enzyme and pathway databases

BioCyciZFISH:ENSG00000141570-MONOMER.
ReactomeiR-HSA-2559580. Oxidative Stress Induced Senescence.
R-HSA-3108214. SUMOylation of DNA damage response and repair proteins.
R-HSA-4570464. SUMOylation of RNA binding proteins.

Miscellaneous databases

EvolutionaryTraceiQ9HC52.
GeneWikiiCBX8.
GenomeRNAii57332.
PROiQ9HC52.

Gene expression databases

BgeeiENSG00000141570.
CleanExiHS_CBX8.
ExpressionAtlasiQ9HC52. baseline and differential.
GenevisibleiQ9HC52. HS.

Family and domain databases

InterProiIPR033773. CBX7_C.
IPR000953. Chromo/shadow_dom.
IPR023780. Chromo_domain.
IPR016197. Chromodomain-like.
IPR023779. Chromodomain_CS.
[Graphical view]
PfamiPF17218. CBX7_C. 1 hit.
PF00385. Chromo. 1 hit.
[Graphical view]
SMARTiSM00298. CHROMO. 1 hit.
[Graphical view]
SUPFAMiSSF54160. SSF54160. 1 hit.
PROSITEiPS00598. CHROMO_1. 1 hit.
PS50013. CHROMO_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiCBX8_HUMAN
AccessioniPrimary (citable) accession number: Q9HC52
Secondary accession number(s): Q96H39, Q9NR07
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 29, 2001
Last sequence update: May 10, 2005
Last modified: November 30, 2016
This is version 148 of the entry and version 3 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. The hPRC-H complex purification reported by PubMed:12167701 probably presents a mixture of different complexes.

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 17
    Human chromosome 17: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  5. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.