CPLM-013914

Genbank Nucleotide ID

Heterochromatin protein 1-binding protein 3

Protein Synonyms/Alias

Homo sapiens (Human)

Position	Peptide	Type	References
14	QGELVHPKALPLIVG	ubiquitination	[1, 2]
131	EKEKKVKKTIPSWAT	ubiquitination	[1, 2, 3]
149	SQLARAQKQTPMASS	ubiquitination	[3]
170	AILTEAIKACFQKSG	ubiquitination	[3]
175	AIKACFQKSGASVVA	ubiquitination	[3]
190	IRKYIIHKYPSLELE	acetylation	[4]
204	ERRGYLLKQALKREL	ubiquitination	[3]
258	VDPEPQVKLEDVLPL	ubiquitination	[3]
274	FTRLCEPKEASYSLI	ubiquitination	[3]
283	ASYSLIRKYVSQYYP	ubiquitination	[3]
291	YVSQYYPKLRVDIRP	ubiquitination	[1, 2, 3]
302	DIRPQLLKNALQRAV	ubiquitination	[3]
320	QLEQITGKGASGTFQ	ubiquitination	[5]
366	CSTTALKKYVLENHP	ubiquitination	[5]

[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] 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]
[3] 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]
[4] 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]
[5] 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]

Functional Description

Component of heterochromatin, may be involved in chromatin structure and function (By similarity).

DOMAIN 157 232 H15 1.
DOMAIN 255 330 H15 2.
DOMAIN 337 413 H15 3.
MOD_RES 2 2 N-acetylalanine.
MOD_RES 6 6 Phosphoserine.
MOD_RES 51 51 Phosphothreonine (By similarity).
MOD_RES 142 142 Phosphoserine.
MOD_RES 155 155 Phosphoserine.
MOD_RES 156 156 Phosphoserine.
MOD_RES 248 248 Phosphoserine.
MOD_RES 249 249 Phosphoserine.
MOD_RES 431 431 Phosphoserine (By similarity).
MOD_RES 441 441 Phosphoserine.
MOD_RES 442 442 Phosphoserine.
MOD_RES 446 446 Phosphoserine.

3D-structure; Acetylation; Alternative splicing; Chromosome; Complete proteome; Direct protein sequencing; DNA-binding; Nucleus; Phosphoprotein; Reference proteome; Repeat.

UniProt (SWISSPROT/TrEMBL); GenBank; EMBL

GO:0000786; C:nucleosome; IEA:InterPro.
GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
GO:0006334; P:nucleosome assembly; IEA:InterPro.

IPR005818; Histone_H1/H5.
IPR011991; WHTH_DNA-bd_dom.

PF00538; Linker_histone