P23198 (CBX3_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended 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

Organism

Mus musculus (Mouse)

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

Protein attributes

Sequence length	183 AA.
Sequence status	Complete.
Protein existence	Evidence 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.

Ontologies

Keywords
Biological process	Transcription Transcription regulation
Cellular component	Nucleus
Domain	Repeat
Molecular function	Chromatin regulator Repressor
PTM	Acetylation Phosphoprotein
Technical term	Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological process	chromatin modification Inferred from electronic annotation. Source: UniProtKB-KW regulation of transcription, DNA-dependent Inferred from electronic annotation. Source: UniProtKB-KW transcription, DNA-dependent Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	condensed chromosome, centromeric region Inferred from direct assay. Source: UniProtKB nuclear centromeric heterochromatin Inferred from direct assay. Source: UniProtKB nuclear envelope Inferred from direct assay. Source: UniProtKB
Molecular function	protein binding Inferred from physical interaction. Source: IntAct
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
TRIM28	Q13263	2	EBI-78162,EBI-78139	From a different organism.

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 183	183	Chromobox protein homolog 3		PRO_0000080204
Regions
	Domain	30 – 88	59	Chromo 1
	Domain	121 – 179	59	Chromo 2; shadow subtype
Amino acid modifications
	Modified residue	10	1	N6-acetyllysine By similarity
	Modified residue	44	1	N6-acetyllysine By similarity
	Modified residue	50	1	N6-acetyllysine By similarity
	Modified residue	93	1	Phosphoserine Ref.8 Ref.9
	Modified residue	95	1	Phosphoserine Ref.8 Ref.9
	Modified residue	97	1	Phosphoserine By similarity
	Modified residue	99	1	Phosphoserine By similarity
	Modified residue	176	1	Phosphoserine Ref.7

Sequences

	Sequence		Length	Mass (Da)
	P23198 [UniParc]. Last modified July 11, 2002. Version 2. Checksum: 2FF3AD53B883E27E	FASTA	183	20,855
	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

References

	« Hide 'large scale' referencesShow '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.
IPI	IPI00129468.
PIR	S26846.
UniGene	Mm.280968. Mm.394056. Mm.458234.
3D structure databases
ProteinModelPortal	P23198.
SMR	P23198. Positions 29-81, 112-173.
ModBase	Search...
Protein-protein interaction databases
DIP	DIP-28136N.
IntAct	P23198. 4 interactions.
MINT	MINT-191172.
STRING	P23198.
PTM databases
PhosphoSite	P23198.
2D gel databases
REPRODUCTION-2DPAGE	IPI00129468.
Proteomic databases
PRIDE	P23198.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Organism-specific databases
MGI	MGI:108515. Cbx3.
Phylogenomic databases
eggNOG	roNOG16327.
HOGENOM	HBG314523.
HOVERGEN	HBG000400.
InParanoid	P23198.
OrthoDB	EOG4N30QB.
Gene expression databases
Bgee	P23198.
CleanEx	MM_CBX3.
Genevestigator	P23198.
GermOnline	ENSMUSG00000029836. Mus musculus. ENSMUSG00000057886. Mus musculus. ENSMUSG00000059647. Mus musculus.
Family and domain databases
InterPro	IPR017984. 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]
Pfam	PF00385. Chromo. 1 hit. PF01393. Chromo_shadow. 1 hit. [Graphical view]
PRINTS	PR00504. CHROMODOMAIN.
SMART	SM00298. CHROMO. 2 hits. SM00300. ChSh. 1 hit. [Graphical view]
SUPFAM	SSF54160. Chromodomain-like. 2 hits.
PROSITE	PS00598. CHROMO_1. 1 hit. PS50013. CHROMO_2. 2 hits. [Graphical view]
ProtoNet	Search...
Other
SOURCE	Search...

Entry information

Entry name

CBX3_MOUSE

Accession

Primary (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 status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program