CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-010534
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Chromobox protein homolog 1 
Protein Synonyms/Alias
 HP1Hsbeta; Heterochromatin protein 1 homolog beta; HP1 beta; Heterochromatin protein p25; M31; Modifier 1 protein; p25beta 
Gene Name
 CBX1 
Gene Synonyms/Alias
 CBX 
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
25EEEYVVEKVLDRRVVubiquitination[1, 2]
41GKVEYLLKWKGFSDEubiquitination[1, 3]
139LMFLMKWKNSDEADLubiquitination[1, 2, 3, 4]
150EADLVPAKEANVKCPubiquitination[1, 2, 5]
180YPSEDDDKKDDKN**ubiquitination[4, 6, 7]
181PSEDDDKKDDKN***ubiquitination[4, 7]
184DDDKKDDKN******ubiquitination[2, 7]
Reference
 [1] A proteome-wide, quantitative survey of in vivo ubiquitylation sites reveals widespread regulatory roles.
 Wagner SA, Beli P, Weinert BT, Nielsen ML, Cox J, Mann M, Choudhary C.
 Mol Cell Proteomics. 2011 Oct;10(10):M111.013284. [PMID: 21890473]
 [2] Landscape of the PARKIN-dependent ubiquitylome in response to mitochondrial depolarization.
 Sarraf SA, Raman M, Guarani-Pereira V, Sowa ME, Huttlin EL, Gygi SP, Harper JW.
 Nature. 2013 Apr 18;496(7445):372-6. [PMID: 23503661]
 [3] Systems-wide analysis of ubiquitylation dynamics reveals a key role for PAF15 ubiquitylation in DNA-damage bypass.
 Povlsen LK, Beli P, Wagner SA, Poulsen SL, Sylvestersen KB, Poulsen JW, Nielsen ML, Bekker-Jensen S, Mailand N, Choudhary C.
 Nat Cell Biol. 2012 Oct;14(10):1089-98. [PMID: 23000965]
 [4] Refined preparation and use of anti-diglycine remnant (K-ε-GG) antibody enables routine quantification of 10,000s of ubiquitination sites in single proteomics experiments.
 Udeshi ND, Svinkina T, Mertins P, Kuhn E, Mani DR, Qiao JW, Carr SA.
 Mol Cell Proteomics. 2013 Mar;12(3):825-31. [PMID: 23266961]
 [5] Proteomic analyses reveal divergent ubiquitylation site patterns in murine tissues.
 Wagner SA, Beli P, Weinert BT, Schölz C, Kelstrup CD, Young C, Nielsen ML, Olsen JV, Brakebusch C, Choudhary C.
 Mol Cell Proteomics. 2012 Dec;11(12):1578-85. [PMID: 22790023]
 [6] Mass spectrometric analysis of lysine ubiquitylation reveals promiscuity at site level.
 Danielsen JM, Sylvestersen KB, Bekker-Jensen S, Szklarczyk D, Poulsen JW, Horn H, Jensen LJ, Mailand N, Nielsen ML.
 Mol Cell Proteomics. 2011 Mar;10(3):M110.003590. [PMID: 21139048]
 [7] Integrated proteomic analysis of post-translational modifications by serial enrichment.
 Mertins P, Qiao JW, Patel J, Udeshi ND, Clauser KR, Mani DR, Burgess MW, Gillette MA, Jaffe JD, Carr SA.
 Nat Methods. 2013 Jul;10(7):634-7. [PMID: 23749302
Functional Description
 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. 
Sequence Annotation
 DOMAIN 21 79 Chromo 1.
 DOMAIN 117 175 Chromo 2; shadow subtype.
 BINDING 21 21 Histone H3K9me2 (By similarity).
 BINDING 23 23 Histone H3A7 (By similarity).
 BINDING 40 40 Histone H3A7 (By similarity).
 BINDING 42 42 Histone H3A7 (By similarity).
 BINDING 42 42 Histone H3K9me2 (By similarity).
 BINDING 45 45 Histone H3K9me2 (By similarity).
 BINDING 58 58 Histone H3A7 (By similarity).
 BINDING 60 60 Histone H3A7 (By similarity).
 BINDING 125 125 PxVxL motif (By similarity).
 BINDING 126 126 PxVxL motif (By similarity).
 BINDING 135 135 PxVxL motif (By similarity).
 BINDING 146 146 PxVxL motif (By similarity).
 BINDING 163 163 PxVxL motif (By similarity).
 BINDING 167 167 PxVxL motif (By similarity).
 BINDING 168 168 PxVxL motif (By similarity).
 BINDING 170 170 PxVxL motif (By similarity).
 MOD_RES 89 89 Phosphoserine.
 MOD_RES 91 91 Phosphoserine.
 MOD_RES 175 175 Phosphoserine.  
Keyword
 3D-structure; Complete proteome; Direct protein sequencing; Nucleus; Phosphoprotein; Reference proteome; Repeat; Ubl conjugation. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 185 AA 
Protein Sequence
MGKKQNKKKV EEVLEEEEEE YVVEKVLDRR VVKGKVEYLL KWKGFSDEDN TWEPEENLDC 60
PDLIAEFLQS QKTAHETDKS EGGKRKADSD SEDKGEESKP KKKKEESEKP RGFARGLEPE 120
RIIGATDSSG ELMFLMKWKN SDEADLVPAK EANVKCPQVV ISFYEERLTW HSYPSEDDDK 180
KDDKN 185 
Gene Ontology
 GO:0005721; C:centromeric heterochromatin; IEA:Compara.
 GO:0010369; C:chromocenter; IEA:Compara.
 GO:0000775; C:chromosome, centromeric region; IDA:UniProtKB.
 GO:0001939; C:female pronucleus; IEA:Compara.
 GO:0001940; C:male pronucleus; IEA:Compara.
 GO:0005720; C:nuclear heterochromatin; TAS:ProtInc.
 GO:0005654; C:nucleoplasm; TAS:ProtInc.
 GO:0005819; C:spindle; IDA:UniProtKB.
 GO:0003682; F:chromatin binding; TAS:ProtInc.
 GO:0045892; P:negative regulation of transcription, DNA-dependent; IEA:Compara. 
Interpro
 IPR017984; Chromo_dom_subgr.
 IPR023780; Chromo_domain.
 IPR000953; Chromo_domain/shadow.
 IPR008251; Chromo_shadow_dom.
 IPR016197; Chromodomain-like.
 IPR023779; Chromodomain_CS. 
Pfam
 PF00385; Chromo
 PF01393; Chromo_shadow 
SMART
 SM00298; CHROMO
 SM00300; ChSh 
PROSITE
 PS00598; CHROMO_1
 PS50013; CHROMO_2 
PRINTS
 PR00504; CHROMODOMAIN.