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Protein Page:
CBX1 (human)
p Phosphorylation
ac Acetylation
me Methylation
m1 Mono-methylation
m2 Di-methylation
m3 Tri-methylation
ub Ubiquitination
sm Sumoylation
ne Neddylation
gl O-GlcNAc
ga O-GalNAc
pa Palmitoylation
ad Adenylylation
sn S-Nitrosylation
ca Caspase cleavage
sc Succinylation

Overview
CBX1 Component of heterochromatin. Recognizes and binds histone H3 tails methylated at 'Lys-9', leading to epigenetic repression. Interaction with lamin B receptor (LBR) can contribute to the association of the heterochromatin with the inner nuclear membrane. Homodimer. Interacts directly with CHAF1A, EMSY, LBR, TIF1/TIF1A and TRIM28/TIF1B PXVXL motif via the chromoshadow domain. Interacts directly with histone H3 methylated at 'Lys-9' via the chromo domain. Interacts with SUV39H1 and SETDB1, SUV420H1 and SUV420H2. Interacts with PRDM6. Interacts with POGZ. Interacts with CHAMP1. Interacts with ASXL1. Expressed in all adult and embryonic tissues. Note: This description may include information from UniProtKB.
Protein type: Transcription factor
Cellular Component: nucleoplasm; centric heterochromatin; male pronucleus; female pronucleus; spindle; nuclear heterochromatin; chromatin; chromosome, pericentric region; chromocenter
Molecular Function: identical protein binding; protein binding; enzyme binding; chromatin binding
Biological Process: negative regulation of transcription, DNA-dependent
Reference #:  P83916 (UniProtKB)
Alt. Names/Synonyms: CBX; CBX1; chromobox homolog 1 (HP1 beta homolog Drosophila ); Chromobox protein homolog 1; Heterochromatin protein 1 homolog beta; heterochromatin protein 1-beta; Heterochromatin protein p25; heterochromatin protein p25 beta; HP1 beta; HP1-BETA; HP1Hs-beta; HP1Hsbeta; M31; MOD1; Modifier 1 protein; p25beta
Gene Symbols: CBX1
Molecular weight: 21,418 Da
Basal Isoelectric point: 4.85  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

CBX1

Protein Structure Not Found.


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Sites Implicated In
intracellular localization: T51‑p
molecular association, regulation: T51‑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

 
0 2 K9-ac GKKQNKKkVEEVLEE
0 1 K9-m1 GKKQNKKkVEEVLEE
0 1 Y21 LEEEEEEYVVEkVLD
0 2 K25-ub EEEYVVEkVLDRRVV
0 1 K33-ac VLDRRVVkGkVEYLL
0 2 K35-ac DRRVVkGkVEYLLkW
0 1 K35-m1 DRRVVkGkVEYLLkW
0 1 K41-ac GkVEYLLkWkGFSDE
0 8 K43-ub VEYLLkWkGFSDEDN
2 0 T51-p GFSDEDNtWEPEENL
0 2 S70-p LIAEFLQsQKtAHEt
0 1 T73-p EFLQsQKtAHEtDKs
0 1 T77-p sQKtAHEtDKsEGGk
0 1 S80-p tAHEtDKsEGGkRKA
0 97 K84-ac tDKsEGGkRKADsDs
0 2 K84-ub tDKsEGGkRKADsDs
0 26 S89-p GGkRKADsDsEDKGE
0 8 S91-p kRKADsDsEDKGEEs
0 1 S98-p sEDKGEEsKPKKKkE
0 1 K104-ub EsKPKKKkEESEKPR
0 3 S128-p RIIGATDsSGELMFL
0 1 K139-ac LMFLMKWkNSDEADL
0 2 K139-ub LMFLMKWkNSDEADL
0 1 S141 FLMKWkNSDEADLVP
0 39 K150-ub EADLVPAkEANVkCP
0 3 K155-ub PAkEANVkCPQVVIS
0 3 S172-p EERLTWHsyPsEDDD
0 2 Y173-p ERLTWHsyPsEDDDk
0 6 S175-p LTWHsyPsEDDDkKD
0 4 K180-ub yPsEDDDkKDDkN__
0 1 K181 PsEDDDkKDDkN___
0 6 K184-ub DDDkKDDkN______
  mouse

 
K9-ac GKKQNKKkVEEVLEE
K9 GKKQNKKKVEEVLEE
Y21 LEEEEEEYVVEKVLD
K25 EEEYVVEKVLDRRVV
K33 VLDRRVVKGKVEYLL
K35 DRRVVKGKVEYLLKW
K35 DRRVVKGKVEYLLKW
K41 GKVEYLLKWkGFSDE
K43-ub VEYLLKWkGFSDEDN
T51-p GFSDEDNtWEPEENL
S70 LIAEFLQSQKTAHET
T73 EFLQSQKTAHETDKS
T77 SQKTAHETDKSEGGk
S80 TAHETDKSEGGkRKA
K84-ac TDKSEGGkRKADsDs
K84 TDKSEGGKRKADsDs
S89-p GGkRKADsDsEDKGE
S91-p kRKADsDsEDKGEES
S98 sEDKGEESKPKKKKE
K104 ESKPKKKKEESEKPR
S128 RIIGATDSSGELMFL
K139 LMFLMKWKNsDEADL
K139 LMFLMKWKNsDEADL
S141-p FLMKWKNsDEADLVP
K150-ub EADLVPAkEANVKCP
K155 PAkEANVKCPQVVIS
S172 EERLTWHSYPsEDDD
Y173 ERLTWHSYPsEDDDk
S175-p LTWHSYPsEDDDkkD
K180-ub YPsEDDDkkDDkN__
K181-ub PsEDDDkkDDkN___
K184-ub DDDkkDDkN______
  rat

 
K9 GKKQNKKKVEEVLEE
K9 GKKQNKKKVEEVLEE
Y21-p LEEEEEEyVVEKVLD
K25 EEEyVVEKVLDRRVV
K33 VLDRRVVKGKVEYLL
K35 DRRVVKGKVEYLLKW
K35 DRRVVKGKVEYLLKW
K41 GKVEYLLKWKGFSDE
K43 VEYLLKWKGFSDEDN
T51 GFSDEDNTWEPEENL
S70 LIAEFLQSQKTAHET
T73 EFLQSQKTAHETDKS
T77 SQKTAHETDKSDGGK
S80 TAHETDKSDGGKRKA
K84 TDKSDGGKRKADSDS
K84 TDKSDGGKRKADSDS
S89 GGKRKADSDSEDKGE
S91 KRKADSDSEDKGEES
S98 SEDKGEESKPKKKKE
K104 ESKPKKKKEESEKPR
S128 RIIGATDSSGELMFL
K139 LMFLMKWKNSDEADL
K139 LMFLMKWKNSDEADL
S141 FLMKWKNSDEADLVP
K150 EADLVPAKEANVKCP
K155 PAKEANVKCPQVVIS
S172 EERLTWHSYPSEDDD
Y173 ERLTWHSYPSEDDDK
S175 LTWHSYPSEDDDKKD
K180 YPSEDDDKKDDKN__
K181 PSEDDDKKDDKN___
K184 DDDKKDDKN______
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