UniProt Accession

 CBX5_HUMAN; P45973; B2R8T9 

Genbank Protein ID

 S62077; L07515; AK313506; CH471054; BC006821; U26311 

Genbank Nucleotide ID

 AAB26994.1; AAA72327.1; BAG36286.1; EAW96759.1; AAH06821.1; AAC50553.1 

Protein Name

 Chromobox protein homolog 5 

Protein Synonyms/Alias

 Antigen p25; Heterochromatin protein 1 homolog alpha; HP1 alpha 

Gene Name

 CBX5 

Gene Synonyms/Alias

 HP1A 

Created Date

 July 27, 2013 

Organism

 Homo sapiens (Human) 

NCBI Taxa ID

 9606 

Lysine Modification

Position	Peptide	Type	References
32	VLDRRVVKGQVEYLL	ubiquitination	[1, 2, 3, 4, 5]
40	GQVEYLLKWKGFSEE	ubiquitination	[1, 3, 5]
69	LISEFMKKYKKMKEG	sumoylation	[6]
69	LISEFMKKYKKMKEG	ubiquitination	[4]
71	SEFMKKYKKMKEGEN	sumoylation	[6]
84	ENNKPREKSESNKRK	sumoylation	[6]
91	KSESNKRKSNFSNSA	ubiquitination	[2, 4, 7]
102	SNSADDIKSKKKREQ	ubiquitination	[2, 3, 4, 7, 8, 9]
104	SADDIKSKKKREQSN	sumoylation	[6]
105	ADDIKSKKKREQSND	ubiquitination	[4]
106	DDIKSKKKREQSNDI	sumoylation	[6]
125	ERGLEPEKIIGATDS	ubiquitination	[4, 7]
143	LMFLMKWKDTDEADL	ubiquitination	[2, 4]
154	EADLVLAKEANVKCP	ubiquitination	[1, 2, 4, 5, 7, 8, 9]
159	LAKEANVKCPQIVIA	ubiquitination	[4]
184	YPEDAENKEKETAKS	ubiquitination	[2, 4, 8, 9]
186	EDAENKEKETAKS**	ubiquitination	[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] 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]
 [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] hCKSAAP_UbSite: improved prediction of human ubiquitination sites by exploiting amino acid pattern and properties.
 Chen Z, Zhou Y, Song J, Zhang Z.
 Biochim Biophys Acta. 2013 Aug;1834(8):1461-7. [PMID: 23603789]
 [6] SUMOylation promotes de novo targeting of HP1α to pericentric heterochromatin.
 Maison C, Bailly D, Roche D, Montes de Oca R, Probst AV, Vassias I, Dingli F, Lombard B, Loew D, Quivy JP, Almouzni G.
 Nat Genet. 2011 Mar;43(3):220-7. [PMID: 21317888]
 [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]
 [8] 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]
 [9] 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] 

Functional Description

 Component of heterochromatin that recognizes and binds histone H3 tails methylated at 'Lys-9' (H3K9me), leading to epigenetic repression. In contrast, it is excluded from chromatin when 'Tyr-41' of histone H3 is phosphorylated (H3Y41ph). Can interact with lamin-B receptor (LBR). This interaction can contribute to the association of the heterochromatin with the inner nuclear membrane. Involved in the formation of functional kinetochore through interaction with MIS12 complex proteins. 

Sequence Annotation

 DOMAIN 20 78 Chromo 1.
 DOMAIN 121 179 Chromo 2; shadow subtype.
 REGION 116 191 Interaction with ASXL1.
 MOD_RES 8 8 Phosphothreonine.
 MOD_RES 11 11 Phosphoserine.
 MOD_RES 12 12 Phosphoserine.
 MOD_RES 13 13 Phosphoserine.
 MOD_RES 14 14 Phosphoserine.
 MOD_RES 92 92 Phosphoserine.
 MOD_RES 97 97 Phosphoserine.
 MOD_RES 110 110 Phosphoserine.  

Keyword

 3D-structure; Centromere; Chromosome; Complete proteome; Direct protein sequencing; Host-virus interaction; Nucleus; Phosphoprotein; Reference proteome; Repeat; Ubl conjugation. 

Sequence Source

 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 

Protein Length

 191 AA 

Protein Sequence

Gene Ontology

 GO:0010369; C:chromocenter; IEA:Compara.
 GO:0005737; C:cytoplasm; IDA:HPA.
 GO:0000118; C:histone deacetylase complex; ISS:BHF-UCL.
 GO:0035097; C:histone methyltransferase complex; ISS:BHF-UCL.
 GO:0000776; C:kinetochore; IEA:Compara.
 GO:0031618; C:nuclear centromeric heterochromatin; NAS:BHF-UCL.
 GO:0005635; C:nuclear envelope; TAS:ProtInc.
 GO:0005730; C:nucleolus; IDA:BHF-UCL.
 GO:0017053; C:transcriptional repressor complex; ISS:BHF-UCL.
 GO:0003682; F:chromatin binding; IEA:Compara.
 GO:0035064; F:methylated histone residue binding; IDA:UniProtKB.
 GO:0030674; F:protein binding, bridging; ISS:BHF-UCL.
 GO:0070491; F:repressing transcription factor binding; ISS:BHF-UCL.
 GO:0007596; P:blood coagulation; TAS:Reactome.
 GO:0045892; P:negative regulation of transcription, DNA-dependent; IDA:UniProtKB.
 GO:0019048; P:virus-host interaction; 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.