UniProt Accession

 HMGB1_HUMAN; P09429; A5D8W9; Q14321; Q5T7C3; Q6IBE1 

Genbank Protein ID

 X12597; U51677; D63874; EF157968; AY377859; AK291494; AK122825; CR749614; CR456863; BT006940; BT020159; EU012027; AL353648; CH471075; BC003378; BC030981; BC066889; BC067732; BC141844 

Genbank Nucleotide ID

 CAA31110.1; AAB08987.1; BAA09924.1; ABM47301.1; AAQ91389.1; BAF84183.1; BAG53745.1; CAH18408.1; CAG33144.1; AAP35586.1; AAV38961.1; ABS29271.1; CAI15600.1; EAX08457.1; AAH03378.1; AAH30981.1; AAH66889.1; AAH67732.1; AAI41845.1 

Protein Name

 High mobility group protein B1 

Protein Synonyms/Alias

 High mobility group protein 1; HMG-1 

Gene Name

 HMGB1 

Gene Synonyms/Alias

 HMG1 

Created Date

 July 27, 2013 

Organism

 Homo sapiens (Human) 

NCBI Taxa ID

 9606 

Lysine Modification

Position	Peptide	Type	References
3	*****MGKGDPKKPR	acetylation	[1, 2]
12	DPKKPRGKMSSYAFF	acetylation	[3]
12	DPKKPRGKMSSYAFF	ubiquitination	[4, 5, 6]
28	QTCREEHKKKHPDAS	acetylation	[7]
30	CREEHKKKHPDASVN	acetylation	[3, 8, 9, 10]
30	CREEHKKKHPDASVN	ubiquitination	[4, 5, 11]
43	VNFSEFSKKCSERWK	acetylation	[3, 10, 12]
43	VNFSEFSKKCSERWK	methylation	[13]
43	VNFSEFSKKCSERWK	ubiquitination	[6, 11, 14, 15]
50	KKCSERWKTMSAKEK	ubiquitination	[5]
55	RWKTMSAKEKGKFED	ubiquitination	[11]
59	MSAKEKGKFEDMAKA	ubiquitination	[4, 5, 14]
65	GKFEDMAKADKARYE	ubiquitination	[5, 11]
76	ARYEREMKTYIPPKG	acetylation	[16]
82	MKTYIPPKGETKKKF	acetylation	[1, 2, 16]
82	MKTYIPPKGETKKKF	ubiquitination	[4]
90	GETKKKFKDPNAPKR	ubiquitination	[5]
112	FCSEYRPKIKGEHPG	ubiquitination	[6, 17]
114	SEYRPKIKGEHPGLS	ubiquitination	[4, 5, 6, 11, 14, 15, 18, 19]
127	LSIGDVAKKLGEMWN	ubiquitination	[11, 15]
128	SIGDVAKKLGEMWNN	ubiquitination	[4, 5, 6, 10, 11, 14, 15, 19]
141	NNTAADDKQPYEKKA	ubiquitination	[15]
146	DDKQPYEKKAAKLKE	acetylation	[3, 12]
146	DDKQPYEKKAAKLKE	ubiquitination	[11, 15, 20]
147	DKQPYEKKAAKLKEK	ubiquitination	[5]
154	KAAKLKEKYEKDIAA	acetylation	[3, 9]
154	KAAKLKEKYEKDIAA	ubiquitination	[6, 14, 19]
157	KLKEKYEKDIAAYRA	acetylation	[3, 9, 10, 12]
157	KLKEKYEKDIAAYRA	ubiquitination	[4, 5, 6, 10, 11, 14, 19]

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] Interplay between in vitro acetylation and phosphorylation of tailless HMGB1 protein.
 Pelovsky P, Pashev IG, Pasheva E.
 Biochem Biophys Res Commun. 2009 Feb 27;380(1):138-42. [PMID: 19166815]
 [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] 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] 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]
 [6] 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]
 [7] Proteome-wide prediction of acetylation substrates.
 Basu A, Rose KL, Zhang J, Beavis RC, Ueberheide B, Garcia BA, Chait B, Zhao Y, Hunt DF, Segal E, Allis CD, Hake SB.
 Proc Natl Acad Sci U S A. 2009 Aug 18;106(33):13785-90. [PMID: 19666589]
 [8] Substrate and functional diversity of lysine acetylation revealed by a proteomics survey.
 Kim SC, Sprung R, Chen Y, Xu Y, Ball H, Pei J, Cheng T, Kho Y, Xiao H, Xiao L, Grishin NV, White M, Yang XJ, Zhao Y.
 Mol Cell. 2006 Aug;23(4):607-18. [PMID: 16916647]
 [9] Proteomic investigations reveal a role for RNA processing factor THRAP3 in the DNA damage response.
 Beli P, Lukashchuk N, Wagner SA, Weinert BT, Olsen JV, Baskcomb L, Mann M, Jackson SP, Choudhary C.
 Mol Cell. 2012 Apr 27;46(2):212-25. [PMID: 22424773]
 [10] 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]
 [11] 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]
 [12] 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]
 [13] High mobility group proteins and their post-translational modifications.
 Zhang Q, Wang Y.
 Biochim Biophys Acta. 2008 Sep;1784(9):1159-66. [PMID: 18513496]
 [14] 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]
 [15] 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]
 [16] 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]
 [17] Proteomic analysis of ubiquitinated proteins in normal hepatocyte cell line Chang liver cells.
 Tan F, Lu L, Cai Y, Wang J, Xie Y, Wang L, Gong Y, Xu BE, Wu J, Luo Y, Qiang B, Yuan J, Sun X, Peng X.
 Proteomics. 2008 Jul;8(14):2885-96. [PMID: 18655026]
 [18] 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]
 [19] 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]
 [20] 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] 

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). Heparin-binding protein that has a role in the extension of neurite-type cytoplasmic processes in developing cells (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.
 MOD_RES 100 100 Phosphoserine.
 CROSSLNK 112 112 Glycyl lysine isopeptide (Lys-Gly)  

Keyword

 3D-structure; Acetylation; Chromosome; Complete proteome; Direct protein sequencing; DNA-binding; Isopeptide bond; Nucleus; Phosphoprotein; Polymorphism; Reference proteome; Repeat; Ubl conjugation. 

Sequence Source

 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 

Protein Length

 215 AA 

Protein Sequence

Gene Ontology

 GO:0009986; C:cell surface; IDA:UniProtKB.
 GO:0000793; C:condensed chromosome; IDA:UniProtKB.
 GO:0005737; C:cytoplasm; IEA:Compara.
 GO:0005615; C:extracellular space; IDA:UniProtKB.
 GO:0043005; C:neuron projection; IEA:Compara.
 GO:0005654; C:nucleoplasm; TAS:Reactome.
 GO:0010858; F:calcium-dependent protein kinase regulator activity; IEA:Compara.
 GO:0042056; F:chemoattractant activity; ISS:UniProtKB.
 GO:0005125; F:cytokine activity; ISS:UniProtKB.
 GO:0003684; F:damaged DNA binding; ISS:UniProtKB.
 GO:0008301; F:DNA binding, bending; IMP:UniProtKB.
 GO:0003690; F:double-stranded DNA binding; ISS:UniProtKB.
 GO:0030295; F:protein kinase activator activity; IEA:Compara.
 GO:0050786; F:RAGE receptor binding; ISS:UniProtKB.
 GO:0003700; F:sequence-specific DNA binding transcription factor activity; IDA:UniProtKB.
 GO:0003697; F:single-stranded DNA binding; ISS:UniProtKB.
 GO:0006309; P:apoptotic DNA fragmentation; TAS:Reactome.
 GO:0006288; P:base-excision repair, DNA ligation; IDA:UniProtKB.
 GO:0002407; P:dendritic cell chemotaxis; ISS:UniProtKB.
 GO:0006265; P:DNA topological change; ISS:UniProtKB.
 GO:0001654; P:eye development; IEA:Compara.
 GO:0002437; P:inflammatory response to antigenic stimulus; IEP:UniProtKB.
 GO:0045087; P:innate immune response; TAS:Reactome.
 GO:0030324; P:lung development; IEA:Compara.
 GO:0001773; P:myeloid dendritic cell activation; ISS:UniProtKB.
 GO:2000426; P:negative regulation of apoptotic cell clearance; IEA:Compara.
 GO:0017055; P:negative regulation of RNA polymerase II transcriptional preinitiation complex assembly; IDA:UniProtKB.
 GO:0031175; P:neuron projection development; ISS:UniProtKB.
 GO:0043065; P:positive regulation of apoptotic process; IDA:UniProtKB.
 GO:0043280; P:positive regulation of cysteine-type endopeptidase activity involved in apoptotic process; IDA:UniProtKB.
 GO:0043388; P:positive regulation of DNA binding; IDA:UniProtKB.
 GO:0045819; P:positive regulation of glycogen catabolic process; IEA:Compara.
 GO:0045639; P:positive regulation of myeloid cell differentiation; IEA:Compara.
 GO:0045944; P:positive regulation of transcription from RNA polymerase II promoter; IDA:UniProtKB.
 GO:0051384; P:response to glucocorticoid stimulus; IEA:Compara.
 GO:0033151; P:V(D)J recombination; IDA: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