UniProt Accession

 CBX3_HUMAN; Q13185; Q96CD7; Q99409; Q9BVS3; Q9P0Z6 

Genbank Protein ID

 U26312; AB030905; AF136630; BC000954; BC014380 

Genbank Nucleotide ID

 AAB48101.1; BAA83340.1; AAF62370.1; AAH00954.1; AAH14380.1 

Protein Name

 Chromobox protein homolog 3 

Protein Synonyms/Alias

 HECH; Heterochromatin protein 1 homolog gamma; HP1 gamma; Modifier 2 protein 

Gene Name

 CBX3 

Gene Synonyms/Alias

  

Created Date

 July 27, 2013 

Organism

 Homo sapiens (Human) 

NCBI Taxa ID

 9606 

Lysine Modification

Position	Peptide	Type	References
5	***MASNKTTLQKMG	ubiquitination	[1, 2]
10	SNKTTLQKMGKKQNG	acetylation	[3]
20	KKQNGKSKKVEEAEP	ubiquitination	[2, 4]
21	KQNGKSKKVEEAEPE	ubiquitination	[2, 5]
34	PEEFVVEKVLDRRVV	ubiquitination	[2, 4, 5, 6]
44	DRRVVNGKVEYFLKW	acetylation	[3]
44	DRRVVNGKVEYFLKW	ubiquitination	[2]
50	GKVEYFLKWKGFTDA	acetylation	[3]
50	GKVEYFLKWKGFTDA	ubiquitination	[6]
52	VEYFLKWKGFTDADN	ubiquitination	[7]
81	EAFLNSQKAGKEKDG	ubiquitination	[7]
92	EKDGTKRKSLSDSES	ubiquitination	[4, 5]
103	DSESDDSKSKKKRDA	ubiquitination	[4, 5]
113	KKRDAADKPRGFARG	ubiquitination	[5]
141	GELMFLMKWKDSDEA	ubiquitination	[4]
143	LMFLMKWKDSDEADL	ubiquitination	[2, 4, 5, 8]
154	EADLVLAKEANMKCP	ubiquitination	[1, 2, 4, 5, 6, 7, 8, 9]

Reference

 [1] Methods for quantification of in vivo changes in protein ubiquitination following proteasome and deubiquitinase inhibition.
 Udeshi ND, Mani DR, Eisenhaure T, Mertins P, Jaffe JD, Clauser KR, Hacohen N, Carr SA.
 Mol Cell Proteomics. 2012 May;11(5):148-59. [PMID: 22505724]
 [2] 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]
 [3] Lysine acetylation targets protein complexes and co-regulates major cellular functions.
 Choudhary C, Kumar C, Gnad F, Nielsen ML, Rehman M, Walther TC, Olsen JV, Mann M.
 Science. 2009 Aug 14;325(5942):834-40. [PMID: 19608861]
 [4] 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]
 [5] Systematic and quantitative assessment of the ubiquitin-modified proteome.
 Kim W, Bennett EJ, Huttlin EL, Guo A, Li J, Possemato A, Sowa ME, Rad R, Rush J, Comb MJ, Harper JW, Gygi SP.
 Mol Cell. 2011 Oct 21;44(2):325-40. [PMID: 21906983]
 [6] 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]
 [7] Global identification of modular cullin-RING ligase substrates.
 Emanuele MJ, Elia AE, Xu Q, Thoma CR, Izhar L, Leng Y, Guo A, Chen YN, Rush J, Hsu PW, Yen HC, Elledge SJ.
 Cell. 2011 Oct 14;147(2):459-74. [PMID: 21963094]
 [8] 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]
 [9] 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] 

Functional Description

 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. 

Sequence Annotation

 DOMAIN 30 88 Chromo 1.
 DOMAIN 121 179 Chromo 2; shadow subtype.
 MOD_RES 10 10 N6-acetyllysine.
 MOD_RES 44 44 N6-acetyllysine.
 MOD_RES 50 50 N6-acetyllysine.
 MOD_RES 93 93 Phosphoserine.
 MOD_RES 95 95 Phosphoserine.
 MOD_RES 97 97 Phosphoserine.
 MOD_RES 99 99 Phosphoserine.
 MOD_RES 176 176 Phosphoserine.  

Keyword

 3D-structure; Acetylation; Chromatin regulator; Complete proteome; Direct protein sequencing; Nucleus; Phosphoprotein; Reference proteome; Repeat; Repressor; Transcription; Transcription regulation. 

Sequence Source

 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 

Protein Length

 183 AA 

Protein Sequence

Gene Ontology

 GO:0000779; C:condensed chromosome, centromeric region; ISS:UniProtKB.
 GO:0031618; C:nuclear centromeric heterochromatin; ISS:UniProtKB.
 GO:0005719; C:nuclear euchromatin; IDA:UniProtKB.
 GO:0005637; C:nuclear inner membrane; NAS:UniProtKB.
 GO:0005819; C:spindle; IDA:UniProtKB.
 GO:0006338; P:chromatin remodeling; NAS:UniProtKB.
 GO:0045892; P:negative regulation of transcription, DNA-dependent; IDA:UniProtKB.
 GO:0006351; P:transcription, DNA-dependent; IEA:UniProtKB-KW. 

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.