UniProt Accession

 HMGN1_HUMAN; P05114; Q3KQR8 

Genbank Protein ID

 J02621; M21339; BT007337; AF064861; AL163279; BC000075; BC023984; BC070153; BC106080 

Genbank Nucleotide ID

 AAA52676.1; AAA52677.1; AAP36001.1; CAB90453.1; AAH00075.1; AAH23984.1; AAH70153.1; AAI06081.1 

Protein Name

 Non-histone chromosomal protein HMG-14 

Protein Synonyms/Alias

 High mobility group nucleosome-binding domain-containing protein 1 

Gene Name

 HMGN1 

Gene Synonyms/Alias

 HMG14 

Created Date

 July 27, 2013 

Organism

 Homo sapiens (Human) 

NCBI Taxa ID

 9606 

Lysine Modification

Position	Peptide	Type	References
3	*****MPKRKVSSAE	acetylation	[1]
5	***MPKRKVSSAEGA	ubiquitination	[2]
14	SSAEGAAKEEPKRRS	acetylation	[1, 3]
14	SSAEGAAKEEPKRRS	ubiquitination	[2, 4]
18	GAAKEEPKRRSARLS	acetylation	[1]
27	RSARLSAKPPAKVEA	acetylation	[1]
31	LSAKPPAKVEAKPKK	acetylation	[1]
38	KVEAKPKKAAAKDKS	acetylation	[1]
42	KPKKAAAKDKSSDKK	acetylation	[1]
48	AKDKSSDKKVQTKGK	acetylation	[1]
53	SDKKVQTKGKRGAKG	acetylation	[1]
55	KKVQTKGKRGAKGKQ	acetylation	[1]
59	TKGKRGAKGKQAEVA	acetylation	[1, 5]
61	GKRGAKGKQAEVANQ	acetylation	[1, 5]
61	GKRGAKGKQAEVANQ	ubiquitination	[4]
71	EVANQETKEDLPAEN	ubiquitination	[4, 6]
82	PAENGETKTEESPAS	acetylation	[1, 3]
82	PAENGETKTEESPAS	ubiquitination	[4, 6]
95	ASDEAGEKEAKSD**	ubiquitination	[4]

Reference

 [1] Acetylation of novel sites in the nucleosomal binding domain of chromosomal protein HMG-14 by p300 alters its interaction with nucleosomes.
 Bergel M, Herrera JE, Thatcher BJ, Prymakowska-Bosak M, Vassilev A, Nakatani Y, Martin B, Bustin M.
 J Biol Chem. 2000 Apr 14;275(15):11514-20. [PMID: 10753971]
 [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] 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]
 [5] Regulation of cellular metabolism by protein lysine acetylation.
 Zhao S, Xu W, Jiang W, Yu W, Lin Y, Zhang T, Yao J, Zhou L, Zeng Y, Li H, Li Y, Shi J, An W, Hancock SM, He F, Qin L, Chin J, Yang P, Chen X, Lei Q, Xiong Y, Guan KL.
 Science. 2010 Feb 19;327(5968):1000-4. [PMID: 20167786]
 [6] 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

 Binds to the inner side of the nucleosomal DNA thus altering the interaction between the DNA and the histone octamer. May be involved in the process which maintains transcribable genes in an unique chromatin conformation. Inhibits the phosphorylation of nucleosomal histones H3 and H2A by RPS6KA5/MSK1 and RPS6KA3/RSK2 (By similarity). 

Sequence Annotation

 MOD_RES 8 8 Phosphoserine.
 MOD_RES 14 14 N6-acetyllysine.
 MOD_RES 21 21 Phosphoserine; by RPS6KA5.
 MOD_RES 25 25 Phosphoserine; by RPS6KA5.
 MOD_RES 81 81 Phosphothreonine (By similarity).
 MOD_RES 82 82 N6-acetyllysine.
 MOD_RES 86 86 Phosphoserine.
 MOD_RES 89 89 Phosphoserine.
 MOD_RES 99 99 Phosphoserine.  

Keyword

 Acetylation; Complete proteome; Cytoplasm; Direct protein sequencing; DNA-binding; Nucleus; Phosphoprotein; Reference proteome; RNA editing. 

Sequence Source

 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 

Protein Length

 100 AA 

Protein Sequence

Gene Ontology

 GO:0000785; C:chromatin; TAS:ProtInc.
 GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
 GO:0005634; C:nucleus; IDA:UniProtKB.
 GO:0003677; F:DNA binding; TAS:ProtInc.
 GO:0031492; F:nucleosomal DNA binding; IEA:InterPro.
 GO:0006325; P:chromatin organization; IEA:Compara.
 GO:0032786; P:positive regulation of DNA-dependent transcription, elongation; TAS:ProtInc.
 GO:0048597; P:post-embryonic camera-type eye morphogenesis; IEA:Compara.
 GO:0000720; P:pyrimidine dimer repair by nucleotide-excision repair; IEA:Compara.
 GO:0040034; P:regulation of development, heterochronic; IEA:Compara.
 GO:0050678; P:regulation of epithelial cell proliferation; IEA:Compara.
 GO:0010224; P:response to UV-B; IEA:Compara.
 GO:0010225; P:response to UV-C; IEA:Compara.
 GO:0006283; P:transcription-coupled nucleotide-excision repair; IEA:Compara. 

Interpro

 IPR000079; HMGN_fam. 

Pfam

 PF01101; HMG14_17 

SMART

 SM00527; HMG17 

PROSITE

 PS00355; HMG14_17 

PRINTS

 PR00925; NONHISHMG17.