CPLM-012607

Genbank Nucleotide ID

High mobility group nucleosome-binding domain-containing protein 3

Protein Synonyms/Alias

Thyroid receptor-interacting protein 7; TR-interacting protein 7; TRIP-7

Homo sapiens (Human)

Position	Peptide	Type	References
13	SPENTEGKDGSKVTK	acetylation	[1, 2]
13	SPENTEGKDGSKVTK	ubiquitination	[3]
33	RSARLSAKPAPPKPE	ubiquitination	[4]
38	SAKPAPPKPEPKPRK	ubiquitination	[4]
55	AKKEPGAKISRGAKG	ubiquitination	[3]
84	PSENGETKAEEAQKT	ubiquitination	[5]
90	TKAEEAQKTESVDNE	acetylation	[6]
90	TKAEEAQKTESVDNE	ubiquitination	[3]

[1] Spermidine and resveratrol induce autophagy by distinct pathways converging on the acetylproteome.
Morselli E, Mariño G, Bennetzen MV, Eisenberg T, Megalou E, Schroeder S, Cabrera S, Bénit P, Rustin P, Criollo A, Kepp O, Galluzzi L, Shen S, Malik SA, Maiuri MC, Horio Y, López-Otín C, Andersen JS, Tavernarakis N, Madeo F, Kroemer G.
J Cell Biol. 2011 Feb 21;192(4):615-29. [PMID: 21339330]
[2] Proteomic investigations of lysine acetylation identify diverse substrates of mitochondrial deacetylase sirt3.
Sol EM, Wagner SA, Weinert BT, Kumar A, Kim HS, Deng CX, Choudhary C.
PLoS One. 2012;7(12):e50545. [PMID: 23236377]
[3] 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]
[4] 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]
[5] 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]
[6] 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]

Functional Description

Binds to nucleosomes, regulating chromatin structure and consequently, chromatin-dependent processes such as transcription, DNA replication and DNA repair. Affects both insulin and glucagon levels and modulates the expression of pancreatic genes involved in insulin secretion. Regulates the expression of the glucose transporter SLC2A2 by binding specifically to its promoter region and recruiting PDX1 and additional transcription factors. Regulates the expression of SLC6A9, a glycine transporter which regulates the glycine concentration in synaptic junctions in the central nervous system, by binding to its transcription start site. May play a role in ocular development and astrocyte function (By similarity).

MOD_RES 6 6 Phosphoserine.
MOD_RES 10 10 Phosphothreonine.
MOD_RES 78 78 Phosphoserine.
MOD_RES 93 93 Phosphoserine.

Alternative splicing; Chromatin regulator; Complete proteome; DNA-binding; Nucleus; Phosphoprotein; Reference proteome.

UniProt (SWISSPROT/TrEMBL); GenBank; EMBL

GO:0000785; C:chromatin; IEA:InterPro.
GO:0005737; C:cytoplasm; IDA:HPA.
GO:0005634; C:nucleus; NAS:UniProtKB.
GO:0031492; F:nucleosomal DNA binding; IEA:InterPro.
GO:0046966; F:thyroid hormone receptor binding; NAS:UniProtKB.
GO:0016568; P:chromatin modification; IEA:UniProtKB-KW.
GO:0051091; P:positive regulation of sequence-specific DNA binding transcription factor activity; IEA:Compara.
GO:0045944; P:positive regulation of transcription from RNA polymerase II promoter; IEA:Compara.
GO:0061178; P:regulation of insulin secretion involved in cellular response to glucose stimulus; IEA:Compara.

IPR000079; HMGN_fam.

PR00925; NONHISHMG17.