UniProt Accession

 HMGB2_HUMAN; P26583; B2R4K8; D3DP37; Q5U072 

Genbank Protein ID

 M83665; X62534; BT019782; AK311864; CH471056; CH471056; BC001063; BC100019; Z17240 

Genbank Nucleotide ID

 AAA58659.1; CAA44395.1; AAV38585.1; BAG34805.1; EAX04758.1; EAX04759.1; AAH01063.1; AAI00020.1; CAA78938.1 

Protein Name

 High mobility group protein B2 

Protein Synonyms/Alias

 High mobility group protein 2; HMG-2 

Gene Name

 HMGB2 

Gene Synonyms/Alias

 HMG2 

Created Date

 July 27, 2013 

Organism

 Homo sapiens (Human) 

NCBI Taxa ID

 9606 

Lysine Modification

Position	Peptide	Type	References
3	*****MGKGDPNKPR	acetylation	[1]
12	DPNKPRGKMSSYAFF	acetylation	[2]
12	DPNKPRGKMSSYAFF	ubiquitination	[3, 4]
30	CREEHKKKHPDSSVN	acetylation	[2]
43	VNFAEFSKKCSERWK	acetylation	[2]
43	VNFAEFSKKCSERWK	ubiquitination	[5, 6]
59	MSAKEKSKFEDMAKS	acetylation	[2]
82	MKNYVPPKGDKKGKK	acetylation	[1]
114	SEHRPKIKSEHPGLS	ubiquitination	[5, 7, 8]
127	LSIGDTAKKLGEMWS	ubiquitination	[8]
128	SIGDTAKKLGEMWSE	ubiquitination	[7, 9]
139	MWSEQSAKDKQPYEQ	ubiquitination	[5, 6, 8]
141	SEQSAKDKQPYEQKA	ubiquitination	[5, 6, 7]
147	DKQPYEQKAAKLKEK	acetylation	[9]
147	DKQPYEQKAAKLKEK	ubiquitination	[4, 5, 6, 7, 8, 10]
154	KAAKLKEKYEKDIAA	ubiquitination	[3]
157	KLKEKYEKDIAAYRA	ubiquitination	[3, 4]
172	KGKSEAGKKGPGRPT	acetylation	[2]
173	GKSEAGKKGPGRPTG	acetylation	[2]

Reference

 [1] In vitro acetylation of HMGB-1 and -2 proteins by CBP: the role of the acidic tail.
 Pasheva E, Sarov M, Bidjekov K, Ugrinova I, Sarg B, Lindner H, Pashev IG.
 Biochemistry. 2004 Mar 16;43(10):2935-40. [PMID: 15005629]
 [2] 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]
 [3] 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]
 [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] 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] 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]
 [7] 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]
 [8] 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]
 [9] 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]
 [10] 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

 DNA binding proteins that associates with chromatin and has the ability to bend DNA. Binds preferentially single-stranded DNA. Involved in V(D)J recombination by acting as a cofactor of the RAG complex. Acts by stimulating cleavage and RAG protein binding at the 23 bp spacer of conserved recombination signal sequences (RSS) (By similarity). 

Sequence Annotation

 DNA_BIND 9 79 HMG box 1.
 DNA_BIND 95 163 HMG box 2.
 MOD_RES 30 30 N6-acetyllysine.
 MOD_RES 35 35 Phosphoserine (By similarity).  

Keyword

 Acetylation; Chromosome; Complete proteome; DNA-binding; Nucleus; Phosphoprotein; Reference proteome; Repeat. 

Sequence Source

 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 

Protein Length

 209 AA 

Protein Sequence

Gene Ontology

 GO:0000793; C:condensed chromosome; IDA:UniProtKB.
 GO:0005615; C:extracellular space; IDA:UniProtKB.
 GO:0005654; C:nucleoplasm; TAS:Reactome.
 GO:0048471; C:perinuclear region of cytoplasm; IDA:UniProtKB.
 GO:0043234; C:protein complex; IDA:UniProtKB.
 GO:0042056; F:chemoattractant activity; IDA:UniProtKB.
 GO:0003684; F:damaged DNA binding; IDA:UniProtKB.
 GO:0008301; F:DNA binding, bending; IDA:UniProtKB.
 GO:0003690; F:double-stranded DNA binding; ISS:UniProtKB.
 GO:0050786; F:RAGE receptor binding; IGI:UniProtKB.
 GO:0003700; F:sequence-specific DNA binding transcription factor activity; IDA:UniProtKB.
 GO:0003697; F:single-stranded DNA binding; ISS:UniProtKB.
 GO:0044212; F:transcription regulatory region DNA binding; IDA:UniProtKB.
 GO:0006309; P:apoptotic DNA fragmentation; TAS:Reactome.
 GO:0006288; P:base-excision repair, DNA ligation; IDA:UniProtKB.
 GO:0060326; P:cell chemotaxis; IDA:UniProtKB.
 GO:0071222; P:cellular response to lipopolysaccharide; IEP:UniProtKB.
 GO:0006265; P:DNA topological change; ISS:UniProtKB.
 GO:0008584; P:male gonad development; IEA:Compara.
 GO:0045892; P:negative regulation of transcription, DNA-dependent; IDA:BHF-UCL.
 GO:0006334; P:nucleosome assembly; NAS:UniProtKB.
 GO:0048015; P:phosphatidylinositol-mediated signaling; NAS:UniProtKB.
 GO:0043388; P:positive regulation of DNA binding; IDA:UniProtKB.
 GO:0001938; P:positive regulation of endothelial cell proliferation; IDA:UniProtKB.
 GO:0045648; P:positive regulation of erythrocyte differentiation; IMP:UniProtKB.
 GO:0045654; P:positive regulation of megakaryocyte differentiation; IMP:UniProtKB.
 GO:0032075; P:positive regulation of nuclease activity; IDA:UniProtKB.
 GO:0045944; P:positive regulation of transcription from RNA polymerase II promoter; IDA:UniProtKB.
 GO:0048545; P:response to steroid hormone stimulus; IEA:Compara.
 GO:0007289; P:spermatid nucleus differentiation; IEA:Compara.
 GO:0033151; P:V(D)J recombination; ISS:UniProtKB. 

Interpro

 IPR009071; HMG_box_dom.
 IPR017967; HMG_boxA_CS. 

Pfam

 PF09011; DUF1898
 PF00505; HMG_box 

SMART

 SM00398; HMG 

PROSITE

 PS00353; HMG_BOX_1
 PS50118; HMG_BOX_2 

PRINTS