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Q9HC52

- CBX8_HUMAN

UniProt

Q9HC52 - CBX8_HUMAN

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Protein
Chromobox protein homolog 8
Gene
CBX8, PC3, RC1
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.1 Publication

GO - Molecular functioni

  1. methylated histone binding Source: UniProtKB
  2. protein binding Source: IntAct
  3. single-stranded RNA binding Source: Ensembl
  4. ubiquitin-protein transferase activity Source: Ensembl
Complete GO annotation...

GO - Biological processi

  1. histone ubiquitination Source: Ensembl
  2. negative regulation of transcription from RNA polymerase II promoter Source: UniProtKB
  3. transcription, DNA-templated Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Chromatin regulator, Repressor

Keywords - Biological processi

Transcription, Transcription regulation

Enzyme and pathway databases

ReactomeiREACT_169436. Oxidative Stress Induced Senescence.

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
ProteomesiUP000005640: Chromosome 17

Organism-specific databases

HGNCiHGNC:15962. CBX8.

Subcellular locationi

Nucleus 1 Publication

GO - Cellular componenti

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

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA26133.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 389389Chromobox protein homolog 8
PRO_0000080215Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei110 – 1101Phosphoserine2 Publications
Modified residuei130 – 1301Phosphoserine1 Publication
Modified residuei191 – 1911Phosphoserine1 Publication
Modified residuei256 – 2561Phosphoserine2 Publications
Modified residuei265 – 2651Phosphoserine1 Publication
Modified residuei311 – 3111Phosphoserine By similarity
Modified residuei352 – 3521Phosphoserine2 Publications

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiQ9HC52.
PaxDbiQ9HC52.
PeptideAtlasiQ9HC52.
PRIDEiQ9HC52.

PTM databases

PhosphoSiteiQ9HC52.

Expressioni

Gene expression databases

ArrayExpressiQ9HC52.
BgeeiQ9HC52.
CleanExiHS_CBX8.
GenevestigatoriQ9HC52.

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.4 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
BMI1P3522613EBI-712912,EBI-2341576
KAT5Q929932EBI-712912,EBI-399080
PCGF1Q9BSM12EBI-712912,EBI-749901
PCGF2P352277EBI-712912,EBI-2129767
PCGF3Q3KNV83EBI-712912,EBI-2339807
PCGF5Q86SE92EBI-712912,EBI-2827999
PCGF6Q9BYE72EBI-712912,EBI-1048026
RING1Q065873EBI-712912,EBI-752313
RNF2Q994965EBI-712912,EBI-722416
USP11P517845EBI-712912,EBI-306876
USP7Q930097EBI-712912,EBI-302474

Protein-protein interaction databases

BioGridi121487. 78 interactions.
DIPiDIP-44566N.
IntActiQ9HC52. 74 interactions.
MINTiMINT-1372508.
STRINGi9606.ENSP00000269385.

Structurei

Secondary structure

Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi10 – 2213
Beta strandi25 – 328
Helixi37 – 393
Beta strandi41 – 444
Helixi45 – 473
Helixi51 – 599

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3I91X-ray1.55A/B8-61[»]
ProteinModelPortaliQ9HC52.
SMRiQ9HC52. Positions 9-60.

Miscellaneous databases

EvolutionaryTraceiQ9HC52.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini11 – 6959Chromo
Add
BLAST

Sequence similaritiesi

Contains 1 chromo domain.

Phylogenomic databases

eggNOGiNOG304493.
HOGENOMiHOG000233642.
HOVERGENiHBG003608.
InParanoidiQ9HC52.
KOiK11455.
OMAiVQCGVTS.
PhylomeDBiQ9HC52.
TreeFamiTF106456.

Family and domain databases

InterProiIPR023780. Chromo_domain.
IPR000953. Chromo_domain/shadow.
IPR016197. Chromodomain-like.
IPR023779. Chromodomain_CS.
[Graphical view]
PfamiPF00385. 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

MELSAVGERV FAAEALLKRR IRKGRMEYLV KWKGWSQKYS TWEPEENILD    50
ARLLAAFEER EREMELYGPK KRGPKPKTFL LKAQAKAKAK TYEFRSDSAR 100
GIRIPYPGRS PQDLASTSRA REGLRNMGLS PPASSTSTSS TCRAEAPRDR 150
DRDRDRDRER DRERERERER ERERERERER GTSRVDDKPS SPGDSSKKRG 200
PKPRKELPDP SQRPLGEPSA GLGEYLKGRK LDDTPSGAGK FPAGHSVIQL 250
ARRQDSDLVQ CGVTSPSSAE ATGKLAVDTF PARVIKHRAA FLEAKGQGAL 300
DPNGTRVRHG SGPPSSGGGL YRDMGAQGGR PSLIARIPVA RILGDPEEES 350
WSPSLTNLEK VVVTDVTSNF LTVTIKESNT DQGFFKEKR 389
Length:389
Mass (Da):43,396
Last modified:May 10, 2005 - v3
Checksum:i651263C85B0ECD93
GO

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti317 – 3171G → V.2 Publications
Corresponds to variant rs4889891 [ dbSNP | Ensembl ].
VAR_014954

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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.
ENST00000570393; ENSP00000459583; ENSG00000262572.
GeneIDi57332.
KEGGihsa:57332.
UCSCiuc002jxd.2. human.

Polymorphism databases

DMDMi78099843.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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 .
CCDSi CCDS11765.1.
RefSeqi NP_065700.1. NM_020649.2.
UniGenei Hs.387258.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
3I91 X-ray 1.55 A/B 8-61 [» ]
ProteinModelPortali Q9HC52.
SMRi Q9HC52. Positions 9-60.
ModBasei Search...

Protein-protein interaction databases

BioGridi 121487. 78 interactions.
DIPi DIP-44566N.
IntActi Q9HC52. 74 interactions.
MINTi MINT-1372508.
STRINGi 9606.ENSP00000269385.

PTM databases

PhosphoSitei Q9HC52.

Polymorphism databases

DMDMi 78099843.

Proteomic databases

MaxQBi Q9HC52.
PaxDbi Q9HC52.
PeptideAtlasi Q9HC52.
PRIDEi Q9HC52.

Protocols and materials databases

DNASUi 57332.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000269385 ; ENSP00000269385 ; ENSG00000141570 .
ENST00000570393 ; ENSP00000459583 ; ENSG00000262572 .
GeneIDi 57332.
KEGGi hsa:57332.
UCSCi uc002jxd.2. human.

Organism-specific databases

CTDi 57332.
GeneCardsi GC17M077765.
HGNCi HGNC:15962. CBX8.
HPAi HPA031462.
neXtProti NX_Q9HC52.
PharmGKBi PA26133.
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG304493.
HOGENOMi HOG000233642.
HOVERGENi HBG003608.
InParanoidi Q9HC52.
KOi K11455.
OMAi VQCGVTS.
PhylomeDBi Q9HC52.
TreeFami TF106456.

Enzyme and pathway databases

Reactomei REACT_169436. Oxidative Stress Induced Senescence.

Miscellaneous databases

EvolutionaryTracei Q9HC52.
GeneWikii CBX8.
GenomeRNAii 57332.
NextBioi 63438.
PROi Q9HC52.

Gene expression databases

ArrayExpressi Q9HC52.
Bgeei Q9HC52.
CleanExi HS_CBX8.
Genevestigatori Q9HC52.

Family and domain databases

InterProi IPR023780. Chromo_domain.
IPR000953. Chromo_domain/shadow.
IPR016197. Chromodomain-like.
IPR023779. Chromodomain_CS.
[Graphical view ]
Pfami PF00385. Chromo. 1 hit.
[Graphical view ]
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. "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. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-110; SER-130; SER-256; SER-265 AND SER-352, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  12. 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, IDENTIFICATION BY MASS SPECTROMETRY, SUBCELLULAR LOCATION, IDENTIFICATION IN A PRC1-LIKE COMPLEX, INTERACTION WITH RING1; RNF2; PCGF1; PCGF2; PCGF3; BMI1; PCGF5 AND PCGF6.
  14. Cited for: X-RAY CRYSTALLOGRAPHY (1.55 ANGSTROMS) OF 8-61 IN COMPLEX WITH HISTONE H3 PEPTIDE.

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: September 3, 2014
This is version 123 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 1 Publication 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

External Data

Dasty 3

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