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Protein Page:
CBX3 (human)
p Phosphorylation
a Acetylation
m Methylation
m1 Mono-methylation
m2 Di-methylation
m3 Tri-methylation
u Ubiquitination
s Sumoylation
n Neddylation
gl O-GlcNAc
ga O-GalNAc
h Palmitoylation
ad Adenylylation
sn S-Nitrosylation
ca Caspase cleavage

Overview
CBX3 Seems to be involved in transcriptional silencing in heterochromatin-like complexes. Recognizes and binds histone H3 tails methylated at 'Lys-9', leading to epigenetic repression. May contribute to the association of the heterochromatin with the inner nuclear membrane through its interaction with lamin B receptor (LBR). Involved in the formation of functional kinetochore through interaction with MIS12 complex proteins. 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, SUV420H1, SUV420H2 and SP100. Interacts with TIF1A. Interacts with MIS12 and DSN1. Can interact directly with CBX5 via the chromoshadow domain. Interacts with POGZ. Interacts with CHAMP1. Interacts with ASXL1. Note: This description may include information from UniProtKB.
Protein type: DNA binding protein
Cellular Component: nuclear inner membrane; spindle; nuclear envelope; nuclear heterochromatin; chromatin; nucleus
Molecular Function: identical protein binding; protein domain specific binding; protein binding; enzyme binding
Biological Process: chromatin remodeling; transcription, DNA-dependent; negative regulation of transcription, DNA-dependent
Reference #:  Q13185 (UniProtKB)
Alt. Names/Synonyms: CBX3; chromobox homolog 3 (HP1 gamma homolog, Drosophila); Chromobox protein homolog 3; HECH; Heterochromatin protein 1 homolog gamma; heterochromatin protein HP1 gamma; heterochromatin-like protein 1; HP1 gamma; HP1 gamma homolog; HP1-GAMMA; HP1Hs-gamma; Modifier 2 protein
Gene Symbols: CBX3
Molecular weight: 20,811 Da
Basal Isoelectric point: 5.23  Predict pI for various phosphorylation states
CST Pathways:  Crosstalk between PTMs  |  Histone Methylation
Protein-Specific Antibodies or siRNAs from Cell Signaling Technology® Total Proteins
Select Structure to View Below

CBX3
Protein Structure Not Found.


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Sites Implicated In
intracellular localization: S93‑p
molecular association, regulation: S93‑p

Modification Sites and Domains Show Modification Legend
Click here to view phosphorylation modifications only

Modification Sites in Parent Protein, Orthologs, and Isoforms Show Modification Legend
 

Show Multiple Sequence Alignment


 SS 

SS: The number of records in which this modification site was determined using site-specific methods. SS methods include amino acid sequencing, site-directed mutagenesis, modification site-specific antibodies, specific MS strategies, etc.


  MS 

MS: The number of records in which this modification site was assigned using ONLY proteomic discovery-mode mass spectrometry.


        human

► Hide Isoforms 		 
0 1 K10-a SNKTTLQkMGKKQNG
0 2 K21-a KQNGKSKkVEEAEPE
0 1 K21-m1 KQNGKSKkVEEAEPE
0 1 K21-u KQNGKSKkVEEAEPE
0 1 K34-a PEEFVVEkVLDRRVV
0 12 K34-u PEEFVVEkVLDRRVV
0 17 K44-a DRRVVNGkVEYFLkW
0 1 K44-m1 DRRVVNGkVEYFLkW
0 1 K50-a GkVEYFLkWkGFTDA
0 1 K50-u GkVEYFLkWkGFTDA
0 13 K52-u VEYFLkWkGFTDADN
0 2 T60-p GFTDADNtWEPEENL
0 14 S79-p LIEAFLNsQkAGkEk
0 6 K81-u EAFLNsQkAGkEkDG
0 1 K84-a LNsQkAGkEkDGTKR
0 6 K84-u LNsQkAGkEkDGTKR
0 1 K86-u sQkAGkEkDGTKRks
0 2 K92-u EkDGTKRksLsDsEs
2 72 S93-p kDGTKRksLsDsEsD
0 54 S95-p GTKRksLsDsEsDDS
0 27 S97-p KRksLsDsEsDDSkS
0 17 S99-p ksLsDsEsDDSkSkK
0 2 S102 sDsEsDDSkSkKKRD
0 1 K103-a DsEsDDSkSkKKRDA
0 5 K103-u DsEsDDSkSkKKRDA
0 3 K105-u EsDDSkSkKKRDAAD
0 3 K113 KKRDAADKPRGFARG
0 1 K113-u KKRDAADkPRGFARG
0 1 S132-p RIIGATDsSGELMFL
0 2 K143-a LMFLMKWkDSDEADL
0 1 K143-m1 LMFLMKWkDSDEADL
0 1 K143-u LMFLMKWkDSDEADL
0 29 K154-u EADLVLAkEANMkCP
0 22 K159-u LAkEANMkCPQIVIA
0 11 T173-p AFYEERLtWHsCPED
0 58 S176-p EERLtWHsCPEDEAQ
0 1 - gap
2600 : Phospho-HP1-gamma (Ser83) Antibody
  CBX3 iso3  
K10 SNKTTLQKMGKKQNG
K21 KQNGKSKKVEEAEPE
K21 KQNGKSKKVEEAEPE
K21 KQNGKSKKVEEAEPE
K34 PEEFVVEKVLDRRVV
K34 PEEFVVEKVLDRRVV
K44 DRRVVNGKVEYFLKW
K44 DRRVVNGKVEYFLKW
K50 GKVEYFLKWKGFTEK
K50 GKVEYFLKWKGFTEK
K52 VEYFLKWKGFTEKLA
- gap
- gap
- gap
- gap
- gap
- gap
- gap
- gap
- gap
- gap
- gap
- gap
- gap
- gap
- gap
- gap
- gap
- gap
- gap
- gap
- gap
- gap
- gap
- gap
- gap
K100-u LPEVLILkE______
  mouse

 
K10 SNKTTLQKMGKKQNG
K21 KQNGKSKKVEEAEPE
K21 KQNGKSKKVEEAEPE
K21 KQNGKSKKVEEAEPE
K34 PEEFVVEKVLDRRVV
K34-u PEEFVVEkVLDRRVV
K44-a DRRVVNGkVEYFLKW
K44 DRRVVNGKVEYFLKW
K50 GkVEYFLKWkGFTDA
K50 GkVEYFLKWkGFTDA
K52-u VEYFLKWkGFTDADN
T60 GFTDADNTWEPEENL
S79 LIEDFLNSQKAGKEK
K81 EDFLNSQKAGKEKDG
K84 LNSQKAGKEKDGTKR
K84 LNSQKAGKEKDGTKR
K86 SQKAGKEKDGTKRKs
K92 EKDGTKRKsLsDsEs
S93-p KDGTKRKsLsDsEsD
S95-p GTKRKsLsDsEsDDs
S97-p KRKsLsDsEsDDsKS
S99-p KsLsDsEsDDsKSKK
S102-p sDsEsDDsKSKKKRD
K103 DsEsDDsKSKKKRDA
K103 DsEsDDsKSKKKRDA
K105 EsDDsKSKKKRDAAD
K113-a KKRDAADkPRGFARG
K113 KKRDAADKPRGFARG
S132 RIIGATDSSGELMFL
K143 LMFLMKWKDSDEADL
K143 LMFLMKWKDSDEADL
K143 LMFLMKWKDSDEADL
K154-u EADLVLAkEANMkCP
K159-u LAkEANMkCPQIVIA
T173 AFYEERLTWHsCPED
S176-p EERLTWHsCPEDEAQ
- gap
2600 : Phospho-HP1-gamma (Ser83) Antibody
  rat

 
K10 SNKTTLQKMGKKQNG
K21 KQNGKSKKVEEAEPE
K21 KQNGKSKKVEEAEPE
K21 KQNGKSKKVEEAEPE
K34 PEEFVVEKVLDRRVV
K34 PEEFVVEKVLDRRVV
K44 DRRVVNGKVEYFLKW
K44 DRRVVNGKVEYFLKW
K50 GKVEYFLKWKGFTDA
K50 GKVEYFLKWKGFTDA
K52 VEYFLKWKGFTDADN
T60 GFTDADNTWEPEENL
S79 LIEAFLNSQKAGKEK
K81 EAFLNSQKAGKEKDG
K84 LNSQKAGKEKDGTKR
K84 LNSQKAGKEKDGTKR
K86 SQKAGKEKDGTKRKS
K92 EKDGTKRKSLSDSES
S93 KDGTKRKSLSDSESD
S95 GTKRKSLSDSESDDS
S97 KRKSLSDSESDDSKS
S99 KSLSDSESDDSKSKK
S102 SDSESDDSKSKKKRD
K103 DSESDDSKSKKKRDA
K103 DSESDDSKSKKKRDA
K105 ESDDSKSKKKRDAAD
K113 KKRDAADKPRGFARG
K113 KKRDAADKPRGFARG
S132 RIIGATDSSGELMFL
K143 LMFLMKWKDSDEADL
K143 LMFLMKWKDSDEADL
K143 LMFLMKWKDSDEADL
K154 EADLVLAKEANMKCP
K159 LAKEANMKCPQIVIA
T173 AFYEERLTWHSCPED
S176 EERLTWHSCPEDEAQ
- gap
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