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P23198 (CBX3_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 110. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Chromobox protein homolog 3
Alternative name(s):
Heterochromatin protein 1 homolog gamma
Short name=HP1 gamma
M32
Modifier 2 protein
Gene names
Name:Cbx3
OrganismMus musculus (Mouse)
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length183 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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 By similarity.

Subunit structure

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 By similarity. Interacts with LBR, INCENP, TRIM28/TIF1B and SP100. Interacts with TIF1/TIF1A. Interacts with MIS12 and DSN1 By similarity. Can interact directly with CBX5 via the chromoshadow domain By similarity. Interacts with SUV420H1 and SUV420H2. Interacts with POGZ. Interacts with CHAMP1 By similarity. Ref.5 Ref.6

Subcellular location

Nucleus. Note: May be associated with microtubules and mitotic poles during mitosis Potential. Associates with euchromatin and is largely excluded from constitutive heterochromatin. Ref.4

Post-translational modification

Phosphorylated by PIM1. Phosphorylated during interphase and possibly hyper-phosphorylated during mitosis By similarity. Ref.7 Ref.8 Ref.9

Sequence similarities

Contains 2 chromo domains.

Binary interactions

With

Entry

#Exp.

IntAct

Notes

TRIM28Q132632EBI-78162,EBI-78139From a different organism.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 183183Chromobox protein homolog 3
PRO_0000080204

Regions

Domain30 – 8859Chromo 1
Domain121 – 17959Chromo 2; shadow subtype

Amino acid modifications

Modified residue101N6-acetyllysine By similarity
Modified residue441N6-acetyllysine By similarity
Modified residue501N6-acetyllysine By similarity
Modified residue931Phosphoserine Ref.8 Ref.9
Modified residue951Phosphoserine Ref.8 Ref.9
Modified residue971Phosphoserine By similarity
Modified residue991Phosphoserine By similarity
Modified residue1761Phosphoserine Ref.7

Sequences

Sequence LengthMass (Da)Tools
P23198 [UniParc].

Last modified July 11, 2002. Version 2.
Checksum: 2FF3AD53B883E27E

FASTA18320,855
        10         20         30         40         50         60 
MASNKTTLQK MGKKQNGKSK KVEEAEPEEF VVEKVLDRRV VNGKVEYFLK WKGFTDADNT 

        70         80         90        100        110        120 
WEPEENLDCP ELIEDFLNSQ KAGKEKDGTK RKSLSDSESD DSKSKKKRDA ADKPRGFARG 

       130        140        150        160        170        180 
LDPERIIGAT DSSGELMFLM KWKDSDEADL VLAKEANMKC PQIVIAFYEE RLTWHSCPED 


EAQ 

« Hide

References

« Hide 'large scale' references
[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: 1708124] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 11-183.
Strain: C57BL/6.
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: 8751383] [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: 8978696] [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: 15145825] [Abstract]
Cited for: INTERACTION WITH SUV420H1 AND SUV420H2.
[7]"Protein phosphorylation and expression profiling by Yin-yang multidimensional liquid chromatography (Yin-yang MDLC) mass spectrometry."
Dai J., Jin W.-H., Sheng Q.-H., Shieh C.-H., Wu J.-R., Zeng R.
J. Proteome Res. 6:250-262(2007) [PubMed: 17203969] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-176, MASS SPECTROMETRY.
Tissue: Liver.
[8]"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: 18630941] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-93 AND SER-95, MASS SPECTROMETRY.
Tissue: Liver.
[9]"Solid tumor proteome and phosphoproteome analysis by high resolution mass spectrometry."
Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J., Faessler R., Mann M.
J. Proteome Res. 7:5314-5326(2008) [PubMed: 19367708] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-93 AND SER-95, MASS SPECTROMETRY.
Tissue: Melanoma.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X56683 mRNA. Translation: CAA40012.1.
AJ278617, AJ278618, AJ278619 Genomic DNA. Translation: CAC42944.1.
IPIIPI00129468.
PIRS26846.
UniGeneMm.280968.
Mm.394056.
Mm.458234.

3D structure databases

ProteinModelPortalP23198.
SMRP23198. Positions 29-81, 112-173.
ModBaseSearch...

Protein-protein interaction databases

DIPDIP-28136N.
IntActP23198. 4 interactions.
MINTMINT-191172.
STRINGP23198.

PTM databases

PhosphoSiteP23198.

2D gel databases

REPRODUCTION-2DPAGEIPI00129468.

Proteomic databases

PRIDEP23198.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Organism-specific databases

MGIMGI:108515. Cbx3.

Phylogenomic databases

eggNOGroNOG16327.
HOGENOMHBG314523.
HOVERGENHBG000400.
InParanoidP23198.
OrthoDBEOG4N30QB.

Gene expression databases

BgeeP23198.
CleanExMM_CBX3.
GenevestigatorP23198.
GermOnlineENSMUSG00000029836. Mus musculus.
ENSMUSG00000057886. Mus musculus.
ENSMUSG00000059647. Mus musculus.

Family and domain databases

InterProIPR017984. Chromo_dom_subgr.
IPR023780. Chromo_domain.
IPR000953. Chromo_domain/shadow.
IPR008251. Chromo_shadow.
IPR018125. Chromo_shadow_sbgrp.
IPR016197. Chromodomain-like.
IPR023779. Chromodomain_CS.
[Graphical view]
PfamPF00385. Chromo. 1 hit.
PF01393. Chromo_shadow. 1 hit.
[Graphical view]
PRINTSPR00504. CHROMODOMAIN.
SMARTSM00298. CHROMO. 2 hits.
SM00300. ChSh. 1 hit.
[Graphical view]
SUPFAMSSF54160. Chromodomain-like. 2 hits.
PROSITEPS00598. CHROMO_1. 1 hit.
PS50013. CHROMO_2. 2 hits.
[Graphical view]
ProtoNetSearch...

Other

SOURCESearch...

Entry information

Entry nameCBX3_MOUSE
AccessionPrimary (citable) accession number: P23198
Secondary accession number(s): Q921C4
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1991
Last sequence update: July 11, 2002
Last modified: January 25, 2012
This is version 110 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

MGD cross-references

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

SIMILARITY comments

Index of protein domains and families