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Protein

Chromobox protein homolog 3

Gene

Cbx3

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Component of heterochromatin. Recognizes and binds histone H3 tails methylated at 'Lys-9', leading to epigenetic repression. Probably involved in the repression of many genes located in euchromatin, such as E2F1, MYC and CDC25A. Involved in the formation of functional kinetochore through interaction with MIS12 complex proteins. Contributes to the conversion of local chromatin to a heterochromatin-like repressive state through H3 'Lys-9' trimethylation, mediates the recruitment of the methyltransferases SUV39H1 and/or SUV39H2 by the PER complex to the E-box elements of the circadian target genes such as PER2 itself or PER1.1 Publication

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Chromatin regulator, Repressor

Keywords - Biological processi

Biological rhythms, Transcription, Transcription regulation

Enzyme and pathway databases

ReactomeiR-MMU-427389. ERCC6 (CSB) and EHMT2 (G9a) positively regulate rRNA expression.

Names & Taxonomyi

Protein namesi
Recommended name:
Chromobox protein homolog 3
Alternative name(s):
Heterochromatin protein 1 homolog gamma
Short name:
HP1 gamma
M32
Modifier 2 protein
Gene namesi
Name:Cbx3
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Unplaced

Organism-specific databases

MGIiMGI:108515. Cbx3.

Subcellular locationi

  • Nucleus 1 Publication

  • Note: May be associated with microtubules and mitotic poles during mitosis (Potential). Associates with euchromatin and is largely excluded from constitutive heterochromatin.Curated

GO - Cellular componenti

  • chromatin Source: MGI
  • chromocenter Source: MGI
  • chromosome, centromeric region Source: MGI
  • condensed chromosome, centromeric region Source: UniProtKB
  • nuclear chromosome, telomeric region Source: MGI
  • nuclear envelope Source: UniProtKB
  • nuclear euchromatin Source: MGI
  • nuclear heterochromatin Source: MGI
  • nuclear pericentric heterochromatin Source: UniProtKB
  • nucleoplasm Source: Reactome
  • nucleus Source: MGI
  • spindle Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methionineiRemovedCombined sources
Chaini2 – 183182Chromobox protein homolog 3PRO_0000080204Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylalanineCombined sources
Modified residuei5 – 51N6-acetyllysine; alternateCombined sources
Cross-linki5 – 5Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternateBy similarity
Modified residuei10 – 101N6-acetyllysine; alternateBy similarity
Cross-linki10 – 10Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternateBy similarity
Cross-linki21 – 21Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)By similarity
Modified residuei44 – 441N6-acetyllysineCombined sources
Modified residuei50 – 501N6-acetyllysineBy similarity
Modified residuei93 – 931PhosphoserineCombined sources
Modified residuei95 – 951PhosphoserineCombined sources
Modified residuei97 – 971PhosphoserineBy similarity
Modified residuei99 – 991PhosphoserineBy similarity
Cross-linki103 – 103Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)By similarity
Modified residuei176 – 1761PhosphoserineCombined sources

Post-translational modificationi

Phosphorylated by PIM1. Phosphorylated during interphase and possibly hyper-phosphorylated during mitosis (By similarity).By similarity

Keywords - PTMi

Acetylation, Isopeptide bond, Phosphoprotein, Ubl conjugation

Proteomic databases

EPDiP23198.
MaxQBiP23198.
PaxDbiP23198.
PeptideAtlasiP23198.
PRIDEiP23198.

2D gel databases

REPRODUCTION-2DPAGEIPI00129468.

PTM databases

iPTMnetiP23198.
PhosphoSiteiP23198.

Expressioni

Gene expression databases

CleanExiMM_CBX3.

Interactioni

Subunit structurei

Binds directly to CHAF1A. Interacts with histone H3 methylated at 'Lys-9'. Part of the E2F6.com-1 complex in G0 phase composed of E2F6, MGA, MAX, TFDP1, CBX3, BAT8, EUHMTASE1, RING1, RNF2, MBLR, L3MBTL2 and YAF2. Interacts with LBR, INCENP, TRIM28/TIF1B and SP100. Interacts with TIF1/TIF1A. Interacts with MIS12 and DSN1. Can interact directly with CBX5 via the chromoshadow domain. Interacts with KMT5B and KMT5C. Interacts with POGZ. Interacts with CHAMP1. Interacts with ASXL1. The large PER complex involved in the histone methylation is composed of at least PER2, CBX3, TRIM28, SUV39H1 and/or SUV39H2; CBX3 mediates the formation of the complex.2 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
TRIM28Q132632EBI-78162,EBI-78139From a different organism.

GO - Molecular functioni

Protein-protein interaction databases

DIPiDIP-28136N.
IntActiP23198. 8 interactions.
MINTiMINT-191172.
STRINGi10090.ENSMUSP00000080177.

Structurei

3D structure databases

ProteinModelPortaliP23198.
SMRiP23198. Positions 29-81, 112-173.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini30 – 8859Chromo 1PROSITE-ProRule annotationAdd
BLAST
Domaini121 – 17959Chromo 2; shadow subtypePROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Contains 2 chromo domains.PROSITE-ProRule annotation

Keywords - Domaini

Repeat

Phylogenomic databases

eggNOGiKOG1911. Eukaryota.
ENOG4111JKD. LUCA.
HOGENOMiHOG000220852.
HOVERGENiHBG000400.
InParanoidiP23198.

Family and domain databases

InterProiIPR000953. Chromo/shadow_dom.
IPR017984. Chromo_dom_subgr.
IPR023780. Chromo_domain.
IPR008251. Chromo_shadow_dom.
IPR016197. Chromodomain-like.
IPR023779. Chromodomain_CS.
[Graphical view]
PfamiPF00385. Chromo. 1 hit.
PF01393. Chromo_shadow. 1 hit.
[Graphical view]
PRINTSiPR00504. CHROMODOMAIN.
SMARTiSM00298. CHROMO. 2 hits.
SM00300. ChSh. 1 hit.
[Graphical view]
SUPFAMiSSF54160. SSF54160. 2 hits.
PROSITEiPS00598. CHROMO_1. 1 hit.
PS50013. CHROMO_2. 2 hits.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P23198-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MASNKTTLQK MGKKQNGKSK KVEEAEPEEF VVEKVLDRRV VNGKVEYFLK
60 70 80 90 100
WKGFTDADNT WEPEENLDCP ELIEDFLNSQ KAGKEKDGTK RKSLSDSESD
110 120 130 140 150
DSKSKKKRDA ADKPRGFARG LDPERIIGAT DSSGELMFLM KWKDSDEADL
160 170 180
VLAKEANMKC PQIVIAFYEE RLTWHSCPED EAQ
Length:183
Mass (Da):20,855
Last modified:July 11, 2002 - v2
Checksum:i2FF3AD53B883E27E
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X56683 mRNA. Translation: CAA40012.1.
AJ278617, AJ278618, AJ278619 Genomic DNA. Translation: CAC42944.1.
PIRiS26846.
UniGeneiMm.280968.
Mm.393602.
Mm.458234.
Mm.490361.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X56683 mRNA. Translation: CAA40012.1.
AJ278617, AJ278618, AJ278619 Genomic DNA. Translation: CAC42944.1.
PIRiS26846.
UniGeneiMm.280968.
Mm.393602.
Mm.458234.
Mm.490361.

3D structure databases

ProteinModelPortaliP23198.
SMRiP23198. Positions 29-81, 112-173.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

DIPiDIP-28136N.
IntActiP23198. 8 interactions.
MINTiMINT-191172.
STRINGi10090.ENSMUSP00000080177.

PTM databases

iPTMnetiP23198.
PhosphoSiteiP23198.

2D gel databases

REPRODUCTION-2DPAGEIPI00129468.

Proteomic databases

EPDiP23198.
MaxQBiP23198.
PaxDbiP23198.
PeptideAtlasiP23198.
PRIDEiP23198.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Organism-specific databases

MGIiMGI:108515. Cbx3.

Phylogenomic databases

eggNOGiKOG1911. Eukaryota.
ENOG4111JKD. LUCA.
HOGENOMiHOG000220852.
HOVERGENiHBG000400.
InParanoidiP23198.

Enzyme and pathway databases

ReactomeiR-MMU-427389. ERCC6 (CSB) and EHMT2 (G9a) positively regulate rRNA expression.

Miscellaneous databases

PROiP23198.
SOURCEiSearch...

Gene expression databases

CleanExiMM_CBX3.

Family and domain databases

InterProiIPR000953. Chromo/shadow_dom.
IPR017984. Chromo_dom_subgr.
IPR023780. Chromo_domain.
IPR008251. Chromo_shadow_dom.
IPR016197. Chromodomain-like.
IPR023779. Chromodomain_CS.
[Graphical view]
PfamiPF00385. Chromo. 1 hit.
PF01393. Chromo_shadow. 1 hit.
[Graphical view]
PRINTSiPR00504. CHROMODOMAIN.
SMARTiSM00298. CHROMO. 2 hits.
SM00300. ChSh. 1 hit.
[Graphical view]
SUPFAMiSSF54160. SSF54160. 2 hits.
PROSITEiPS00598. CHROMO_1. 1 hit.
PS50013. CHROMO_2. 2 hits.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "The gene and pseudogenes of Cbx3."
    Jones D.O., Mattei M.-G., Horsley D., Cowell I.G., Singh P.B.
    Submitted (JUN-2000) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  2. "A sequence motif found in a Drosophila heterochromatin protein is conserved in animals and plants."
    Singh P.B., Miller J.R., Pearce J., Kothary R., Burton R.D., Paro R., James T.C., Gaunt S.J.
    Nucleic Acids Res. 19:789-794(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 11-183.
    Strain: C57BL/6J.
    Tissue: Embryo.
  3. Lubec G., Yang J.W., Zigmond M.
    Submitted (JUL-2007) to UniProtKB
    Cited for: PROTEIN SEQUENCE OF 160-171.
    Tissue: Brain.
  4. "M32, a murine homologue of Drosophila heterochromatin protein 1 (HP1), localises to euchromatin within interphase nuclei and is largely excluded from constitutive heterochromatin."
    Horsley D., Hutchings A., Butcher G.W., Singh P.B.
    Cytogenet. Cell Genet. 73:308-311(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION.
  5. "A possible involvement of TIF1 alpha and TIF1 beta in the epigenetic control of transcription by nuclear receptors."
    le Douarin B., Nielsen A.L., Garnier J.-M., Ichinose H., Jeanmougin F., Losson R., Chambon P.
    EMBO J. 15:6701-6715(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH TIF1A.
  6. "A silencing pathway to induce H3-K9 and H4-K20 trimethylation at constitutive heterochromatin."
    Schotta G., Lachner M., Sarma K., Ebert A., Sengupta R., Reuter G., Reinberg D., Jenuwein T.
    Genes Dev. 18:1251-1262(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH KMT5B AND KMT5C.
  7. "Specific phosphopeptide enrichment with immobilized titanium ion affinity chromatography adsorbent for phosphoproteome analysis."
    Zhou H., Ye M., Dong J., Han G., Jiang X., Wu R., Zou H.
    J. Proteome Res. 7:3957-3967(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-95, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  8. "The phagosomal proteome in interferon-gamma-activated macrophages."
    Trost M., English L., Lemieux S., Courcelles M., Desjardins M., Thibault P.
    Immunity 30:143-154(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  9. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-93; SER-95 AND SER-176, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas, Spleen and Testis.
  10. "SIRT5-mediated lysine desuccinylation impacts diverse metabolic pathways."
    Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y., Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.
    Mol. Cell 50:919-930(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2; LYS-5 AND LYS-44, CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS], IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Embryonic fibroblast.
  11. "Temporal orchestration of repressive chromatin modifiers by circadian clock Period complexes."
    Duong H.A., Weitz C.J.
    Nat. Struct. Mol. Biol. 21:126-132(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN CIRCADIAN RHYTHMS, IDENTIFIACTION IN A LARGE PER COMPLEX.

Entry informationi

Entry nameiCBX3_MOUSE
AccessioniPrimary (citable) accession number: P23198
Secondary accession number(s): Q921C4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1991
Last sequence update: July 11, 2002
Last modified: July 6, 2016
This is version 146 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. 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.