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High mobility group protein B1 (High mobility group protein 1) (HMG-1)

 HMGB1_HUMAN             Reviewed;         215 AA.
P09429; A5D8W9; Q14321; Q5T7C3; Q6IBE1;
01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
23-JAN-2007, sequence version 3.
22-NOV-2017, entry version 197.
RecName: Full=High mobility group protein B1;
AltName: Full=High mobility group protein 1;
Short=HMG-1;
Name=HMGB1; Synonyms=HMG1;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=2922262; DOI=10.1093/nar/17.3.1197;
Wen L., Huang J.K., Johnson B.H., Reeck G.R.;
"A human placental cDNA clone that encodes nonhistone chromosomal
protein HMG-1.";
Nucleic Acids Res. 17:1197-1214(1989).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=8661151; DOI=10.1006/geno.1996.0369;
Ferrari S., Finelli P., Rocchi M., Bianchi M.E.;
"The active gene that encodes human high mobility group 1 protein
(HMG1) contains introns and maps to chromosome 13.";
Genomics 35:367-371(1996).
[3]
NUCLEOTIDE SEQUENCE [MRNA], AND VARIANTS ARG-11; GLU-149 AND GLY-190.
PubMed=9036861;
DOI=10.1002/(SICI)1097-0215(19970220)74:1<1::AID-IJC1>3.0.CO;2-6;
Xiang Y.-Y., Wang D.-Y., Tanaka M., Suzuki M., Kiyokawa E.,
Igarashi H., Niato Y., Shen Q., Sugimura H.;
"Expression of high-mobility group-1 mRNA in human gastrointestinal
adenocarcinoma and corresponding non-cancerous mucosa.";
Int. J. Cancer 74:1-6(1997).
[4]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=17610420; DOI=10.1111/j.1399-0039.2007.00854.x;
Kornblit B., Munthe-Fog L., Petersen S., Madsen H., Vindeloev L.,
Garred P.;
"The genetic variation of the human HMGB1 gene.";
Tissue Antigens 70:151-156(2007).
[5]
NUCLEOTIDE SEQUENCE [MRNA].
He F.T., Yang Z.H., Ji Q., Li R., Peng J., Jiang Y., Zhong X.;
Submitted (SEP-2003) to the EMBL/GenBank/DDBJ databases.
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Cerebellum;
PubMed=14702039; DOI=10.1038/ng1285;
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Small intestine;
PubMed=17974005; DOI=10.1186/1471-2164-8-399;
Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H.,
Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K.,
Ottenwaelder B., Poustka A., Wiemann S., Schupp I.;
"The full-ORF clone resource of the German cDNA consortium.";
BMC Genomics 8:399-399(2007).
[8]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.;
"Cloning of human full open reading frames in Gateway(TM) system entry
vector (pDONR201).";
Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
[9]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S.,
Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y.,
Phelan M., Farmer A.;
"Cloning of human full-length CDSs in BD Creator(TM) system donor
vector.";
Submitted (OCT-2004) to the EMBL/GenBank/DDBJ databases.
[10]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANT GLN-156.
SeattleSNPs variation discovery resource;
Submitted (JUL-2007) to the EMBL/GenBank/DDBJ databases.
[11]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=15057823; DOI=10.1038/nature02379;
Dunham A., Matthews L.H., Burton J., Ashurst J.L., Howe K.L.,
Ashcroft K.J., Beare D.M., Burford D.C., Hunt S.E.,
Griffiths-Jones S., Jones M.C., Keenan S.J., Oliver K., Scott C.E.,
Ainscough R., Almeida J.P., Ambrose K.D., Andrews D.T.,
Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J., Bannerjee R.,
Barlow K.F., Bates K., Beasley H., Bird C.P., Bray-Allen S.,
Brown A.J., Brown J.Y., Burrill W., Carder C., Carter N.P.,
Chapman J.C., Clamp M.E., Clark S.Y., Clarke G., Clee C.M.,
Clegg S.C., Cobley V., Collins J.E., Corby N., Coville G.J.,
Deloukas P., Dhami P., Dunham I., Dunn M., Earthrowl M.E.,
Ellington A.G., Faulkner L., Frankish A.G., Frankland J., French L.,
Garner P., Garnett J., Gilbert J.G.R., Gilson C.J., Ghori J.,
Grafham D.V., Gribble S.M., Griffiths C., Hall R.E., Hammond S.,
Harley J.L., Hart E.A., Heath P.D., Howden P.J., Huckle E.J.,
Hunt P.J., Hunt A.R., Johnson C., Johnson D., Kay M., Kimberley A.M.,
King A., Laird G.K., Langford C.J., Lawlor S., Leongamornlert D.A.,
Lloyd D.M., Lloyd C., Loveland J.E., Lovell J., Martin S.,
Mashreghi-Mohammadi M., McLaren S.J., McMurray A., Milne S.,
Moore M.J.F., Nickerson T., Palmer S.A., Pearce A.V., Peck A.I.,
Pelan S., Phillimore B., Porter K.M., Rice C.M., Searle S.,
Sehra H.K., Shownkeen R., Skuce C.D., Smith M., Steward C.A.,
Sycamore N., Tester J., Thomas D.W., Tracey A., Tromans A., Tubby B.,
Wall M., Wallis J.M., West A.P., Whitehead S.L., Willey D.L.,
Wilming L., Wray P.W., Wright M.W., Young L., Coulson A., Durbin R.M.,
Hubbard T., Sulston J.E., Beck S., Bentley D.R., Rogers J., Ross M.T.;
"The DNA sequence and analysis of human chromosome 13.";
Nature 428:522-528(2004).
[12]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
[13]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Brain, Cervix, and Testis;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[14]
PROTEIN SEQUENCE OF 58-65 AND 113-127.
TISSUE=Mammary carcinoma;
PubMed=9150946; DOI=10.1002/elps.1150180342;
Rasmussen R.K., Ji H., Eddes J.S., Moritz R.L., Reid G.E.,
Simpson R.J., Dorow D.S.;
"Two-dimensional electrophoretic analysis of human breast carcinoma
proteins: mapping of proteins that bind to the SH3 domain of mixed
lineage kinase MLK2.";
Electrophoresis 18:588-598(1997).
[15]
SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
PubMed=11154118;
Rouhiainen A., Imai S., Rauvala H., Parkkinen J.;
"Occurrence of amphoterin (HMG1) as an endogenous protein of human
platelets that is exported to the cell surface upon platelet
activation.";
Thromb. Haemost. 84:1087-1094(2000).
[16]
SUBCELLULAR LOCATION.
PubMed=12231511; DOI=10.1093/embo-reports/kvf198;
Gardella S., Andrei C., Ferrera D., Lotti L.V., Torrisi M.R.,
Bianchi M.E., Rubartelli A.;
"The nuclear protein HMGB1 is secreted by monocytes via a non-
classical, vesicle-mediated secretory pathway.";
EMBO Rep. 3:995-1001(2002).
[17]
SUBCELLULAR LOCATION.
PubMed=14532127; DOI=10.1093/emboj/cdg516;
Bonaldi T., Talamo F., Scaffidi P., Ferrera D., Porto A., Bachi A.,
Rubartelli A., Agresti A., Bianchi M.E.;
"Monocytic cells hyperacetylate chromatin protein HMGB1 to redirect it
towards secretion.";
EMBO J. 22:5551-5560(2003).
[18]
FUNCTION, AND DOMAIN.
PubMed=12765338;
Li J., Kokkola R., Tabibzadeh S., Yang R., Ochani M., Qiang X.,
Harris H.E., Czura C.J., Wang H., Ulloa L., Wang H., Warren H.S.,
Moldawer L.L., Fink M.P., Andersson U., Tracey K.J., Yang H.;
"Structural basis for the proinflammatory cytokine activity of high
mobility group box 1.";
Mol. Med. 9:37-45(2003).
[19]
FUNCTION, AND INTERACTION WITH MSH2.
PubMed=15014079; DOI=10.1074/jbc.M401931200;
Yuan F., Gu L., Guo S., Wang C., Li G.M.;
"Evidence for involvement of HMGB1 protein in human DNA mismatch
repair.";
J. Biol. Chem. 279:20935-20940(2004).
[20]
INVOLVEMENT IN INFLAMMATORY DISEASES.
PubMed=14695889; DOI=10.1073/pnas.2434651100;
Yang H., Ochani M., Li J., Qiang X., Tanovic M., Harris H.E.,
Susarla S.M., Ulloa L., Wang H., DiRaimo R., Czura C.J., Wang H.,
Roth J., Warren H.S., Fink M.P., Fenton M.J., Andersson U.,
Tracey K.J.;
"Reversing established sepsis with antagonists of endogenous high-
mobility group box 1.";
Proc. Natl. Acad. Sci. U.S.A. 101:296-301(2004).
[21]
FUNCTION.
PubMed=16143102; DOI=10.1016/j.cell.2005.06.027;
Zhang Y., Yuan F., Presnell S.R., Tian K., Gao Y., Tomkinson A.E.,
Gu L., Li G.-M.;
"Reconstitution of 5'-directed human mismatch repair in a purified
system.";
Cell 122:693-705(2005).
[22]
INTERACTION WITH THBD.
PubMed=15841214; DOI=10.1172/JCI22782;
Abeyama K., Stern D.M., Ito Y., Kawahara K., Yoshimoto Y., Tanaka M.,
Uchimura T., Ida N., Yamazaki Y., Yamada S., Yamamoto Y., Yamamoto H.,
Iino S., Taniguchi N., Maruyama I.;
"The N-terminal domain of thrombomodulin sequesters high-mobility
group-B1 protein, a novel antiinflammatory mechanism.";
J. Clin. Invest. 115:1267-1274(2005).
[23]
FUNCTION, AND SUBCELLULAR LOCATION.
PubMed=15944249; DOI=10.4049/jimmunol.174.12.7506;
Dumitriu I.E., Baruah P., Valentinis B., Voll R.E., Herrmann M.,
Nawroth P.P., Arnold B., Bianchi M.E., Manfredi A.A.,
Rovere-Querini P.;
"Release of high mobility group box 1 by dendritic cells controls T
cell activation via the receptor for advanced glycation end
products.";
J. Immunol. 174:7506-7515(2005).
[24]
FUNCTION.
PubMed=15607795; DOI=10.1016/j.molimm.2004.07.023;
DeMarco R.A., Fink M.P., Lotze M.T.;
"Monocytes promote natural killer cell interferon gamma production in
response to the endogenous danger signal HMGB1.";
Mol. Immunol. 42:433-444(2005).
[25]
SUBCELLULAR LOCATION.
PubMed=16855214; DOI=10.1152/ajpcell.00616.2005;
Bell C.W., Jiang W., Reich C.F., Pisetsky D.S.;
"The extracellular release of HMGB1 during apoptotic cell death.";
Am. J. Physiol. 291:C1318-C1325(2006).
[26]
DISULFIDE BRIDGE, AND REDOX FORMS.
PubMed=16962095; DOI=10.1016/j.yexcr.2006.07.020;
Hoppe G., Talcott K.E., Bhattacharya S.K., Crabb J.W., Sears J.E.;
"Molecular basis for the redox control of nuclear transport of the
structural chromatin protein Hmgb1.";
Exp. Cell Res. 312:3526-3538(2006).
[27]
PHOSPHORYLATION, MUTAGENESIS OF SER-35; SER-39; SER-42; SER-46; SER-53
AND SER-181, SUBCELLULAR LOCATION, AND INTERACTION WITH KPNA1.
PubMed=17114460; DOI=10.4049/jimmunol.177.11.7889;
Youn J.H., Shin J.S.;
"Nucleocytoplasmic shuttling of HMGB1 is regulated by phosphorylation
that redirects it toward secretion.";
J. Immunol. 177:7889-7897(2006).
[28]
FUNCTION, SUBCELLULAR LOCATION, AND MUTAGENESIS OF CYS-106.
PubMed=18631454; DOI=10.1016/j.immuni.2008.05.013;
Kazama H., Ricci J.E., Herndon J.M., Hoppe G., Green D.R.,
Ferguson T.A.;
"Induction of immunological tolerance by apoptotic cells requires
caspase-dependent oxidation of high-mobility group box-1 protein.";
Immunity 29:21-32(2008).
[29]
FUNCTION.
PubMed=17803946; DOI=10.1016/j.molcel.2007.06.029;
Prasad R., Liu Y., Deterding L.J., Poltoratsky V.P., Kedar P.S.,
Horton J.K., Kanno S., Asagoshi K., Hou E.W., Khodyreva S.N.,
Lavrik O.I., Tomer K.B., Yasui A., Wilson S.H.;
"HMGB1 is a cofactor in mammalian base excision repair.";
Mol. Cell 27:829-841(2007).
[30]
FUNCTION, TISSUE SPECIFICITY, AND INVOLVEMENT IN AUTOIMMUNE DISEASES.
PubMed=19064698; DOI=10.1084/jem.20081165;
Urbonaviciute V., Furnrohr B.G., Meister S., Munoz L., Heyder P.,
De Marchis F., Bianchi M.E., Kirschning C., Wagner H., Manfredi A.A.,
Kalden J.R., Schett G., Rovere-Querini P., Herrmann M., Voll R.E.;
"Induction of inflammatory and immune responses by HMGB1-nucleosome
complexes: implications for the pathogenesis of SLE.";
J. Exp. Med. 205:3007-3018(2008).
[31]
FUNCTION, AND INTERACTION WITH IL1B.
PubMed=18250463; DOI=10.4049/jimmunol.180.4.2531;
Sha Y., Zmijewski J., Xu Z., Abraham E.;
"HMGB1 develops enhanced proinflammatory activity by binding to
cytokines.";
J. Immunol. 180:2531-2537(2008).
[32]
FUNCTION.
PubMed=18354232; DOI=10.4049/jimmunol.180.7.5067;
Youn J.H., Oh Y.J., Kim E.S., Choi J.E., Shin J.S.;
"High mobility group box 1 protein binding to lipopolysaccharide
facilitates transfer of lipopolysaccharide to CD14 and enhances
lipopolysaccharide-mediated TNF-alpha production in human monocytes.";
J. Immunol. 180:5067-5074(2008).
[33]
INTERACTION WITH HNF1A.
PubMed=18160415; DOI=10.1093/nar/gkm1131;
Yu M., Wang J., Li W., Yuan Y.Z., Li C.Y., Qian X.H., Xu W.X.,
Zhan Y.Q., Yang X.M.;
"Proteomic screen defines the hepatocyte nuclear factor 1alpha-binding
partners and identifies HMGB1 as a new cofactor of HNF1alpha.";
Nucleic Acids Res. 36:1209-1219(2008).
[34]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-35 AND SER-100, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18669648; DOI=10.1073/pnas.0805139105;
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
Elledge S.J., Gygi S.P.;
"A quantitative atlas of mitotic phosphorylation.";
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
[35]
REDOX FORMS, AND SUBCELLULAR LOCATION.
PubMed=19811284; DOI=10.1080/08916930902831803;
Urbonaviciute V., Meister S., Furnrohr B.G., Frey B., Guckel E.,
Schett G., Herrmann M., Voll R.E.;
"Oxidation of the alarmin high-mobility group box 1 protein (HMGB1)
during apoptosis.";
Autoimmunity 42:305-307(2009).
[36]
FUNCTION, AND INTERACTION WITH XPA AND XPC.
PubMed=19446504; DOI=10.1016/j.dnarep.2009.04.001;
Lange S.S., Reddy M.C., Vasquez K.M.;
"Human HMGB1 directly facilitates interactions between nucleotide
excision repair proteins on triplex-directed psoralen interstrand
crosslinks.";
DNA Repair 8:865-872(2009).
[37]
REVIEW ON FUNCTION RELATED TO DNA REPAIR.
PubMed=19360789; DOI=10.1002/mc.20544;
Lange S.S., Vasquez K.M.;
"HMGB1: the jack-of-all-trades protein is a master DNA repair
mechanic.";
Mol. Carcinog. 48:571-580(2009).
[38]
FUNCTION, INTERACTION WITH CD24, AND LIGAND FOR CD24:SIGLEC10 RECEPTOR
COMPLEX.
PubMed=19264983; DOI=10.1126/science.1168988;
Chen G.Y., Tang J., Zheng P., Liu Y.;
"CD24 and Siglec-10 selectively repress tissue damage-induced immune
responses.";
Science 323:1722-1725(2009).
[39]
ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-30, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19608861; DOI=10.1126/science.1175371;
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M.,
Walther T.C., Olsen J.V., Mann M.;
"Lysine acetylation targets protein complexes and co-regulates major
cellular functions.";
Science 325:834-840(2009).
[40]
REVIEW ON FUNCTION RELATED TO DNA-BINDING.
PubMed=20123072; DOI=10.1016/j.bbagrm.2009.09.008;
Stros M.;
"HMGB proteins: interactions with DNA and chromatin.";
Biochim. Biophys. Acta 1799:101-113(2010).
[41]
FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH BECN1.
PubMed=20819940; DOI=10.1083/jcb.200911078;
Tang D., Kang R., Livesey K.M., Cheh C.W., Farkas A., Loughran P.,
Hoppe G., Bianchi M.E., Tracey K.J., Zeh H.J. III, Lotze M.T.;
"Endogenous HMGB1 regulates autophagy.";
J. Cell Biol. 190:881-892(2010).
[42]
FUNCTION, LIGAND FOR TLR4:LY96 RECEPTOR COMPLEX, AND DOMAIN.
PubMed=20547845; DOI=10.1073/pnas.1003893107;
Yang H., Hreggvidsdottir H.S., Palmblad K., Wang H., Ochani M., Li J.,
Lu B., Chavan S., Rosas-Ballina M., Al-Abed Y., Akira S., Bierhaus A.,
Erlandsson-Harris H., Andersson U., Tracey K.J.;
"A critical cysteine is required for HMGB1 binding to Toll-like
receptor 4 and activation of macrophage cytokine release.";
Proc. Natl. Acad. Sci. U.S.A. 107:11942-11947(2010).
[43]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-35, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=20068231; DOI=10.1126/scisignal.2000475;
Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S.,
Mann M.;
"Quantitative phosphoproteomics reveals widespread full
phosphorylation site occupancy during mitosis.";
Sci. Signal. 3:RA3-RA3(2010).
[44]
FUNCTION.
PubMed=21395369; DOI=10.1089/ars.2010.3666;
Tang D., Kang R., Livesey K.M., Zeh H.J., Lotze M.T.;
"High mobility group box 1 (HMGB1) activates an autophagic response to
oxidative stress.";
Antioxid. Redox Signal. 15:2185-2195(2011).
[45]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21269460; DOI=10.1186/1752-0509-5-17;
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
"Initial characterization of the human central proteome.";
BMC Syst. Biol. 5:17-17(2011).
[46]
LPS-BINDING.
PubMed=21660935; DOI=10.1002/eji.201141391;
Youn J.H., Kwak M.S., Wu J., Kim E.S., Ji Y., Min H.J., Yoo J.H.,
Choi J.E., Cho H.S., Shin J.S.;
"Identification of lipopolysaccharide-binding peptide regions within
HMGB1 and their effects on subclinical endotoxemia in a mouse model.";
Eur. J. Immunol. 41:2753-2762(2011).
[47]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-35, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21406692; DOI=10.1126/scisignal.2001570;
Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J.,
Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V.,
Blagoev B.;
"System-wide temporal characterization of the proteome and
phosphoproteome of human embryonic stem cell differentiation.";
Sci. Signal. 4:RS3-RS3(2011).
[48]
FUNCTION.
PubMed=22473704; DOI=10.1093/intimm/dxs051;
Wild C.A., Bergmann C., Fritz G., Schuler P., Hoffmann T.K., Lotfi R.,
Westendorf A., Brandau S., Lang S.;
"HMGB1 conveys immunosuppressive characteristics on regulatory and
conventional T cells.";
Int. Immunol. 24:485-494(2012).
[49]
FUNCTION, AND INTERACTION WITH CXCL12.
PubMed=22370717; DOI=10.1084/jem.20111739;
Schiraldi M., Raucci A., Munoz L.M., Livoti E., Celona B.,
Venereau E., Apuzzo T., De Marchis F., Pedotti M., Bachi A.,
Thelen M., Varani L., Mellado M., Proudfoot A., Bianchi M.E.,
Uguccioni M.;
"HMGB1 promotes recruitment of inflammatory cells to damaged tissues
by forming a complex with CXCL12 and signaling via CXCR4.";
J. Exp. Med. 209:551-563(2012).
[50]
REDOX FORMS, AND SUBCELLULAR LOCATION.
PubMed=22869893; DOI=10.1084/jem.20120189;
Venereau E., Casalgrandi M., Schiraldi M., Antoine D.J., Cattaneo A.,
De Marchis F., Liu J., Antonelli A., Preti A., Raeli L., Shams S.S.,
Yang H., Varani L., Andersson U., Tracey K.J., Bachi A., Uguccioni M.,
Bianchi M.E.;
"Mutually exclusive redox forms of HMGB1 promote cell recruitment or
proinflammatory cytokine release.";
J. Exp. Med. 209:1519-1528(2012).
[51]
ACETYLATION.
PubMed=22801494; DOI=10.1038/nature11290;
Lu B., Nakamura T., Inouye K., Li J., Tang Y., Lundbaeck P.,
Valdes-Ferrer S.I., Olofsson P.S., Kalb T., Roth J., Zou Y.,
Erlandsson-Harris H., Yang H., Ting J.P., Wang H., Andersson U.,
Antoine D.J., Chavan S.S., Hotamisligil G.S., Tracey K.J.;
"Novel role of PKR in inflammasome activation and HMGB1 release.";
Nature 488:670-674(2012).
[52]
INVOLVEMENT IN CANCER THERAPY.
PubMed=23040637; DOI=10.1016/j.ejca.2012.09.016;
Luo Y., Chihara Y., Fujimoto K., Sasahira T., Kuwada M., Fujiwara R.,
Fujii K., Ohmori H., Kuniyasu H.;
"High mobility group box 1 released from necrotic cells enhances
regrowth and metastasis of cancer cells that have survived
chemotherapy.";
Eur. J. Cancer 49:741-751(2013).
[53]
REVIEW ON FUNCTION RELATED TO ADAPTIVE IMUNNITY.
PubMed=23519706; DOI=10.3389/fimmu.2013.00068;
Li G., Liang X., Lotze M.T.;
"HMGB1: The central cytokine for all lymphoid cells.";
Front. Immunol. 4:68-68(2013).
[54]
FUNCTION, AND INTERACTION WITH HTT.
PubMed=23303669; DOI=10.4049/jimmunol.1202472;
Min H.J., Ko E.A., Wu J., Kim E.S., Kwon M.K., Kwak M.S., Choi J.E.,
Lee J.E., Shin J.S.;
"Chaperone-like activity of high-mobility group box 1 protein and its
role in reducing the formation of polyglutamine aggregates.";
J. Immunol. 190:1797-1806(2013).
[55]
REVIEW ON FUNCTION RELATED TO INFLAMMATION.
PubMed=23446148; DOI=10.1189/jlb.1212662;
Yang H., Antoine D.J., Andersson U., Tracey K.J.;
"The many faces of HMGB1: molecular structure-functional activity in
inflammation, apoptosis, and chemotaxis.";
J. Leukoc. Biol. 93:865-873(2013).
[56]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-35, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma, and Erythroleukemia;
PubMed=23186163; DOI=10.1021/pr300630k;
Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
Mohammed S.;
"Toward a comprehensive characterization of a human cancer cell
phosphoproteome.";
J. Proteome Res. 12:260-271(2013).
[57]
REVIEW.
PubMed=23994764; DOI=10.1016/j.semcancer.2013.08.002;
Li G., Tang D., Lotze M.T.;
"Menage a Trois in stress: DAMPs, redox and autophagy.";
Semin. Cancer Biol. 23:380-390(2013).
[58]
FUNCTION.
PubMed=24971542; DOI=10.1016/j.bbrc.2014.06.074;
Liu L., Yang M., Kang R., Dai Y., Yu Y., Gao F., Wang H., Sun X.,
Li X., Li J., Wang H., Cao L., Tang D.;
"HMGB1-DNA complex-induced autophagy limits AIM2 inflammasome
activation through RAGE.";
Biochem. Biophys. Res. Commun. 450:851-856(2014).
[59]
FUNCTION, MUTAGENESIS OF ASP-67, INTERACTION WITH AGER, DOMAIN, AND
PROTEOLYTIC CLEAVAGE.
PubMed=24474694; DOI=10.1074/jbc.M113.541474;
LeBlanc P.M., Doggett T.A., Choi J., Hancock M.A., Durocher Y.,
Frank F., Nagar B., Ferguson T.A., Saleh M.;
"An immunogenic peptide in the A-box of HMGB1 protein reverses
apoptosis-induced tolerance through RAGE receptor.";
J. Biol. Chem. 289:7777-7786(2014).
[60]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D.,
Wang L., Ye M., Zou H.;
"An enzyme assisted RP-RPLC approach for in-depth analysis of human
liver phosphoproteome.";
J. Proteomics 96:253-262(2014).
[61]
NOMENCLATURE OF REDOX FORMS.
PubMed=24531895; DOI=10.2119/molmed.2014.00022;
Antoine D.J., Harris H.E., Andersson U., Tracey K.J., Bianchi M.E.;
"A systematic nomenclature for the redox states of high mobility group
box (HMGB) proteins.";
Mol. Med. 20:135-137(2014).
[62]
REVIEW ON INVOLVEMENT IN DISEASES AND THERAPEUTIC TARGET.
PubMed=24220159; DOI=10.1016/j.pharmthera.2013.11.001;
Musumeci D., Roviello G.N., Montesarchio D.;
"An overview on HMGB1 inhibitors as potential therapeutic agents in
HMGB1-related pathologies.";
Pharmacol. Ther. 141:347-357(2014).
[63]
FUNCTION.
PubMed=25549101; DOI=10.1371/journal.pone.0115809;
Lee L.C., Chen C.M., Wang P.R., Su M.T., Lee-Chen G.J., Chang C.Y.;
"Role of high mobility group box 1 (HMGB1) in SCA17 pathogenesis.";
PLoS ONE 9:E115809-E115809(2014).
[64]
REVIEW ON FUNCTION RELATED TO INNATE IMMUNITY.
PubMed=25048472; DOI=10.3349/ymj.2014.55.5.1165;
Lee S.A., Kwak M.S., Kim S., Shin J.S.;
"The role of high mobility group box 1 in innate immunity.";
Yonsei Med. J. 55:1165-1176(2014).
[65]
INVOLVEMENT AUTOIMMUNE DISEASES.
PubMed=26078984; DOI=10.1155/2015/946748;
Lu M., Yu S., Xu W., Gao B., Xiong S.;
"HMGB1 promotes systemic lupus erythematosus by enhancing macrophage
inflammatory response.";
J. Immunol. Res. 2015:946748-946748(2015).
[66]
FUNCTION.
PubMed=25660311; DOI=10.1159/000369972;
Kwak M.S., Lim M., Lee Y.J., Lee H.S., Kim Y.H., Youn J.H., Choi J.E.,
Shin J.S.;
"HMGB1 binds to lipoteichoic acid and enhances TNF-alpha and IL-6
production through HMGB1-mediated transfer of lipoteichoic acid to
CD14 and TLR2.";
J. Innate Immun. 7:405-416(2015).
[67]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=25944712; DOI=10.1002/pmic.201400617;
Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M.,
Ayoub D., Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
"N-terminome analysis of the human mitochondrial proteome.";
Proteomics 15:2519-2524(2015).
[68]
FUNCTION, INTERACTION WITH ADENOVIRUS PROTEIN PVII (MICROBIAL
INFECTION), AND SUBCELLULAR LOCATION.
PubMed=27362237; DOI=10.1038/nature18317;
Avgousti D.C., Herrmann C., Kulej K., Pancholi N.J., Sekulic N.,
Petrescu J., Molden R.C., Blumenthal D., Paris A.J., Reyes E.D.,
Ostapchuk P., Hearing P., Seeholzer S.H., Worthen G.S., Black B.E.,
Garcia B.A., Weitzman M.D.;
"A core viral protein binds host nucleosomes to sequester immune
danger signals.";
Nature 535:173-177(2016).
[69]
ADP-RIBOSYLATION AT SER-181.
PubMed=28190768; DOI=10.1016/j.molcel.2017.01.003;
Bonfiglio J.J., Fontana P., Zhang Q., Colby T., Gibbs-Seymour I.,
Atanassov I., Bartlett E., Zaja R., Ahel I., Matic I.;
"Serine ADP-ribosylation depends on HPF1.";
Mol. Cell 0:0-0(2017).
[70]
STRUCTURE BY NMR OF 1-166.
RIKEN structural genomics initiative (RSGI);
"Solution structure of the tandem HMG box domain from human high
mobility group protein B1.";
Submitted (FEB-2008) to the PDB data bank.
[71]
STRUCTURE BY NMR OF 2-84 IN COMPLEX WITH TP53, FUNCTION, AND DOMAIN.
PubMed=23063560; DOI=10.1016/j.str.2012.09.004;
Rowell J.P., Simpson K.L., Stott K., Watson M., Thomas J.O.;
"HMGB1-facilitated p53 DNA binding occurs via HMG-Box/p53
transactivation domain interaction, regulated by the acidic tail.";
Structure 20:2014-2024(2012).
[72]
STRUCTURE BY NMR OF 1-84.
PubMed=24513216;
Wang J., Tochio N., Takeuchi A., Uewaki J.I., Kobayashi N., Tate S.I.;
"Redox-sensitive structural change in the A-domain of HMGB1 and its
implication for the binding to cisplatin modified DNA.";
Biochem. Biophys. Res. Commun. 0:0-0(2013).
-!- FUNCTION: Multifunctional redox sensitive protein with various
roles in different cellular compartments. In the nucleus is one of
the major chromatin-associated non-histone proteins and acts as a
DNA chaperone involved in replication, transcription, chromatin
remodeling, V(D)J recombination, DNA repair and genome stability.
Proposed to be an universal biosensor for nucleic acids. Promotes
host inflammatory response to sterile and infectious signals and
is involved in the coordination and integration of innate and
adaptive immune responses. In the cytoplasm functions as sensor
and/or chaperone for immunogenic nucleic acids implicating the
activation of TLR9-mediated immune responses, and mediates
autophagy. Acts as danger associated molecular pattern (DAMP)
molecule that amplifies immune responses during tissue injury
(PubMed:27362237). Released to the extracellular environment can
bind DNA, nucleosomes, IL-1 beta, CXCL12, AGER isoform 2/sRAGE,
lipopolysaccharide (LPS) and lipoteichoic acid (LTA), and
activates cells through engagement of multiple surface receptors.
In the extracellular compartment fully reduced HMGB1 (released by
necrosis) acts as a chemokine, disulfide HMGB1 (actively secreted)
as a cytokine, and sulfonyl HMGB1 (released from apoptotic cells)
promotes immunological tolerance (PubMed:23519706,
PubMed:23446148, PubMed:23994764, PubMed:25048472). Has
proangiogdenic activity (By similarity). May be involved in
platelet activation (By similarity). Binds to phosphatidylserine
and phosphatidylethanolamide (By similarity). Bound to RAGE
mediates signaling for neuronal outgrowth (By similarity). May
play a role in accumulation of expanded polyglutamine (polyQ)
proteins such as huntingtin (HTT) or TBP (PubMed:23303669,
PubMed:25549101). {ECO:0000250|UniProtKB:P10103,
ECO:0000250|UniProtKB:P12682, ECO:0000250|UniProtKB:P63158,
ECO:0000250|UniProtKB:P63159, ECO:0000269|PubMed:23303669,
ECO:0000269|PubMed:25549101, ECO:0000269|PubMed:27362237,
ECO:0000305|PubMed:23446148, ECO:0000305|PubMed:23519706,
ECO:0000305|PubMed:23994764, ECO:0000305|PubMed:25048472}.
-!- FUNCTION: Nuclear functions are attributed to fully reduced HGMB1.
Associates with chromatin and binds DNA with a preference to non-
canonical DNA structures such as single-stranded DNA, DNA-
containing cruciforms or bent structures, supercoiled DNA and
ZDNA. Can bent DNA and enhance DNA flexibility by looping thus
providing a mechanism to promote activities on various gene
promoters by enhancing transcription factor binding and/or
bringing distant regulatory sequences into close proximity
(PubMed:20123072). May have an enhancing role in nucleotide
excision repair (NER) (By similarity). However, effects in NER
using in vitro systems have been reported conflictingly
(PubMed:19446504, PubMed:19360789). May be involved in mismatch
repair (MMR) and base excision repair (BER) pathways
(PubMed:15014079, PubMed:16143102, PubMed:17803946). May be
involved in double strand break repair such as non-homologous end
joining (NHEJ) (By similarity). 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). In vitro can
displace histone H1 from highly bent DNA (By similarity). Can
restructure the canonical nucleosome leading to relaxation of
structural constraints for transcription factor-binding (By
similarity). Enhances binding of sterol regulatory element-binding
proteins (SREBPs) such as SREBF1 to their cognate DNA sequences
and increases their transcriptional activities (By similarity).
Facilitates binding of TP53 to DNA (PubMed:23063560). Proposed to
be involved in mitochondrial quality control and autophagy in a
transcription-dependent fashion implicating HSPB1; however, this
function has been questioned (By similarity). Can modulate the
activity of the telomerase complex and may be involved in telomere
maintenance (By similarity). {ECO:0000250|UniProtKB:P10103,
ECO:0000250|UniProtKB:P63158, ECO:0000250|UniProtKB:P63159,
ECO:0000269|PubMed:15014079, ECO:0000269|PubMed:16143102,
ECO:0000269|PubMed:17803946, ECO:0000269|PubMed:19446504,
ECO:0000269|PubMed:23063560, ECO:0000305|PubMed:19360789,
ECO:0000305|PubMed:20123072}.
-!- FUNCTION: In the cytoplasm proposed to dissociate the BECN1:BCL2
complex via competitive interaction with BECN1 leading to
autophagy activation (PubMed:20819940). Involved in oxidative
stress-mediated autophagy (PubMed:21395369). Can protect BECN1 and
ATG5 from calpain-mediated cleavage and thus proposed to control
their proautophagic and proapoptotic functions and to regulate the
extent and severity of inflammation-associated cellular injury (By
similarity). In myeloid cells has a protective role against
endotoxemia and bacterial infection by promoting autophagy (By
similarity). Involved in endosomal translocation and activation of
TLR9 in response to CpG-DNA in macrophages (By similarity).
{ECO:0000250|UniProtKB:P63158, ECO:0000269|PubMed:20819940,
ECO:0000269|PubMed:21395369}.
-!- FUNCTION: In the extracellular compartment (following either
active secretion or passive release) involved in regulation of the
inflammatory response. Fully reduced HGMB1 (which subsequently
gets oxidized after release) in association with CXCL12 mediates
the recruitment of inflammatory cells during the initial phase of
tissue injury; the CXCL12:HMGB1 complex triggers CXCR4
homodimerization (PubMed:22370717). Induces the migration of
monocyte-derived immature dendritic cells and seems to regulate
adhesive and migratory functions of neutrophils implicating
AGER/RAGE and ITGAM (By similarity). Can bind to various types of
DNA and RNA including microbial unmethylated CpG-DNA to enhance
the innate immune response to nucleic acids. Proposed to act in
promiscuous DNA/RNA sensing which cooperates with subsequent
discriminative sensing by specific pattern recognition receptors
(By similarity). Promotes extracellular DNA-induced AIM2
inflammasome activation implicating AGER/RAGE (PubMed:24971542).
Disulfide HMGB1 binds to transmembrane receptors, such as
AGER/RAGE, TLR2, TLR4 and probably TREM1, thus activating their
signal transduction pathways. Mediates the release of
cytokines/chemokines such as TNF, IL-1, IL-6, IL-8, CCL2, CCL3,
CCL4 and CXCL10 (PubMed:12765338, PubMed:18354232,
PubMed:19264983, PubMed:20547845, PubMed:24474694). Promotes
secretion of interferon-gamma by macrophage-stimulated natural
killer (NK) cells in concert with other cytokines like IL-2 or IL-
12 (PubMed:15607795). TLR4 is proposed to be the primary receptor
promoting macrophage activation and signaling through TLR4 seems
to implicate LY96/MD-2 (PubMed:20547845). In bacterial LPS- or
LTA-mediated inflammatory responses binds to the endotoxins and
transfers them to CD14 for signaling to the respective TLR4:LY96
and TLR2 complexes (PubMed:18354232, PubMed:21660935,
PubMed:25660311). Contributes to tumor proliferation by
association with ACER/RAGE (By similarity). Can bind to IL1-beta
and signals through the IL1R1:IL1RAP receptor complex
(PubMed:18250463). Binding to class A CpG activates cytokine
production in plasmacytoid dendritic cells implicating TLR9, MYD88
and AGER/RAGE and can activate autoreactive B cells. Via HMGB1-
containing chromatin immune complexes may also promote B cell
responses to endogenous TLR9 ligands through a B-cell receptor
(BCR)-dependent and ACER/RAGE-independent mechanism (By
similarity). Inhibits phagocytosis of apoptotic cells by
macrophages; the function is dependent on poly-ADP-ribosylation
and involves binding to phosphatidylserine on the cell surface of
apoptotic cells (By similarity). In adaptive immunity may be
involved in enhancing immunity through activation of effector T
cells and suppression of regulatory T (TReg) cells
(PubMed:15944249, PubMed:22473704). In contrast, without
implicating effector or regulatory T-cells, required for tumor
infiltration and activation of T-cells expressing the lymphotoxin
LTA:LTB heterotrimer thus promoting tumor malignant progression
(By similarity). Also reported to limit proliferation of T-cells
(By similarity). Released HMGB1:nucleosome complexes formed during
apoptosis can signal through TLR2 to induce cytokine production
(PubMed:19064698). Involved in induction of immunological
tolerance by apoptotic cells; its pro-inflammatory activities when
released by apoptotic cells are neutralized by reactive oxygen
species (ROS)-dependent oxidation specifically on Cys-106
(PubMed:18631454). During macrophage activation by activated
lymphocyte-derived self apoptotic DNA (ALD-DNA) promotes
recruitment of ALD-DNA to endosomes (By similarity).
{ECO:0000250|UniProtKB:P10103, ECO:0000250|UniProtKB:P63158,
ECO:0000250|UniProtKB:P63159, ECO:0000269|PubMed:12765338,
ECO:0000269|PubMed:15607795, ECO:0000269|PubMed:15944249,
ECO:0000269|PubMed:18250463, ECO:0000269|PubMed:18354232,
ECO:0000269|PubMed:18631454, ECO:0000269|PubMed:19064698,
ECO:0000269|PubMed:19264983, ECO:0000269|PubMed:20547845,
ECO:0000269|PubMed:21660935, ECO:0000269|PubMed:22370717,
ECO:0000269|PubMed:22473704, ECO:0000269|PubMed:24474694,
ECO:0000269|PubMed:24971542, ECO:0000269|PubMed:25660311,
ECO:0000269|Ref.8}.
-!- SUBUNIT: Interacts (fully reduced HMGB1) with CXCL12; probably in
a 1:2 ratio involving two molecules of CXCL12, each interacting
with one HMG box of HMGB1; inhibited by glycyrrhizin
(PubMed:22370717). Associates with the TLR4:LY96 receptor complex
(PubMed:20547845). Component of the RAG complex composed of core
components RAG1 and RAG2, and associated component HMGB1 or HMGB2
(By similarity). Interacts (in cytoplasm upon starvation) with
BECN1; inhibits the interaction of BECN1 and BCL2 leading to
promotion of autophagy (PubMed:20819940). Interacts with KPNA1;
involved in nuclear import (PubMed:17114460). Interacts with
SREBF1, TLR2, TLR4, TLR9, PTPRZ1, APEX1, FEN1, POLB, TERT (By
similarity). Interacts with IL1B, AGER, MSH2, XPA, XPC, HNF1A,
TP53 (PubMed:15014079, PubMed:18250463, PubMed:18160415,
PubMed:19446504, PubMed:24474694, PubMed:23063560). Interacts with
CD24; the probable CD24:SIGLEC10 complex is proposed to inhibit
HGMB1-mediated tissue damage immune response (PubMed:19264983).
Interacts with THBD; prevents HGMB1 interaction with ACER/RAGE and
inhibits HGMB1 proinflammatory activity (PubMed:15841214).
Interacts with HAVCR2; impairs HMGB1 binding to B-DNA and likely
HMGB1-mediated innate immume response (By similarity). Interacts
with XPO1; mediating nuclear export (By similarity). Interacts
with HTT (wild-type and mutant HTT with expanded polyglutamine
repeat) (PubMed:23303669). {ECO:0000250|UniProtKB:P63158,
ECO:0000250|UniProtKB:P63159, ECO:0000269|PubMed:15014079,
ECO:0000269|PubMed:15841214, ECO:0000269|PubMed:17114460,
ECO:0000269|PubMed:17803946, ECO:0000269|PubMed:18160415,
ECO:0000269|PubMed:18250463, ECO:0000269|PubMed:19264983,
ECO:0000269|PubMed:19446504, ECO:0000269|PubMed:20547845,
ECO:0000269|PubMed:20819940, ECO:0000269|PubMed:22370717,
ECO:0000269|PubMed:23063560, ECO:0000269|PubMed:23303669,
ECO:0000269|PubMed:24474694}.
-!- SUBUNIT: (Microbial infection) Interacts with adenovirus protein
pVII; this interaction immobilizes HMGB1 on chromatin, thus
preventing its release from cell and subsequent inflammation
activation. {ECO:0000269|PubMed:27362237}.
-!- INTERACTION:
Q15109:AGER; NbExp=3; IntAct=EBI-389432, EBI-1646426;
Q6RW13:AGTRAP; NbExp=3; IntAct=EBI-389432, EBI-741181;
Q14457:BECN1; NbExp=2; IntAct=EBI-389432, EBI-949378;
P42858:HTT; NbExp=13; IntAct=EBI-389432, EBI-466029;
P43246:MSH2; NbExp=2; IntAct=EBI-389432, EBI-355888;
P04637:TP53; NbExp=9; IntAct=EBI-389432, EBI-366083;
-!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:12231511,
ECO:0000269|PubMed:17114460, ECO:0000269|PubMed:20819940,
ECO:0000269|PubMed:22869893, ECO:0000269|PubMed:27362237}.
Chromosome {ECO:0000250|UniProtKB:P10103,
ECO:0000250|UniProtKB:P63159, ECO:0000305}. Cytoplasm
{ECO:0000269|PubMed:11154118, ECO:0000269|PubMed:12231511,
ECO:0000269|PubMed:17114460, ECO:0000269|PubMed:20819940,
ECO:0000269|PubMed:22869893}. Secreted
{ECO:0000250|UniProtKB:P63158, ECO:0000269|PubMed:12231511,
ECO:0000269|PubMed:14532127, ECO:0000269|PubMed:15944249,
ECO:0000269|PubMed:19811284, ECO:0000269|PubMed:22869893}. Cell
membrane {ECO:0000250|UniProtKB:P63158,
ECO:0000250|UniProtKB:P63159, ECO:0000269|PubMed:11154118};
Peripheral membrane protein {ECO:0000250|UniProtKB:P63158,
ECO:0000250|UniProtKB:P63159, ECO:0000269|PubMed:11154118};
Extracellular side {ECO:0000250|UniProtKB:P63158,
ECO:0000250|UniProtKB:P63159, ECO:0000269|PubMed:11154118}.
Endosome {ECO:0000250|UniProtKB:P63158}. Endoplasmic reticulum-
Golgi intermediate compartment {ECO:0000250|UniProtKB:P63158}.
Note=In basal state predominantly nuclear. Shuttles between the
cytoplasm and the nucleus (PubMed:12231511, PubMed:17114460).
Translocates from the nucleus to the cytoplasm upon autophagy
stimulation (PubMed:20819940). Release from macrophages in the
extracellular milieu requires the activation of NLRC4 or NLRP3
inflammasomes (By similarity). Passively released to the
extracellular milieu from necrotic cells by diffusion, involving
the fully reduced HGMB1 which subsequently gets oxidized
(PubMed:19811284). Also released from apoptic cells
(PubMed:16855214, PubMed:18631454). Active secretion from a
variety of immune and non-immune cells such as macrophages,
monocytes, neutrophils, dendritic cells and natural killer cells
in response to various stimuli such as LPS and cytokines involves
a nonconventional secretory process via secretory lysosomes
(PubMed:12231511, PubMed:14532127, PubMed:15944249). Secreted by
plasma cells in response to LPS (By similarity). Found on the
surface of activated platelets (PubMed:11154118). An increased
chromatin association is observed when associated with the
adenovirus protein pVII (PubMed:27362237).
{ECO:0000250|UniProtKB:P63158, ECO:0000269|PubMed:11154118,
ECO:0000269|PubMed:12231511, ECO:0000269|PubMed:14532127,
ECO:0000269|PubMed:15944249, ECO:0000269|PubMed:16855214,
ECO:0000269|PubMed:17114460, ECO:0000269|PubMed:18631454,
ECO:0000269|PubMed:19811284, ECO:0000269|PubMed:20819940,
ECO:0000269|PubMed:27362237, ECO:0000305|PubMed:20123072}.
-!- TISSUE SPECIFICITY: Ubiquituous. Expressed in platelets
(PubMed:11154118). {ECO:0000269|PubMed:11154118}.
-!- DOMAIN: HMG box 2 mediates proinflammatory cytokine-stimulating
activity and binding to TLR4 (PubMed:12765338, PubMed:20547845).
However, not involved in mediating immunogenic activity in the
context of apoptosis-induced immune tolerance (PubMed:24474694).
{ECO:0000269|PubMed:12765338, ECO:0000269|PubMed:20547845,
ECO:0000269|PubMed:24474694}.
-!- DOMAIN: The acidic C-terminal domain forms a flexible structure
which can reversibly interact intramolecularily with the HMG boxes
and modulate binding to DNA and other proteins (PubMed:23063560).
{ECO:0000250|UniProtKB:P63159, ECO:0000305|PubMed:23063560}.
-!- PTM: Phosphorylated at serine residues. Phosphorylation in both
NLS regions is required for cytoplasmic translocation followed by
secretion (PubMed:17114460). {ECO:0000269|PubMed:17114460}.
-!- PTM: Acetylated on multiple sites upon stimulation with LPS
(PubMed:22801494). Acetylation on lysine residues in the nuclear
localization signals (NLS 1 and NLS 2) leads to cytoplasmic
localization and subsequent secretion (By similarity). Acetylation
on Lys-3 results in preferential binding to DNA ends and impairs
DNA bending activity (By similarity).
{ECO:0000250|UniProtKB:P10103, ECO:0000250|UniProtKB:P63159,
ECO:0000269|PubMed:22801494}.
-!- PTM: Reduction/oxidation of cysteine residues Cys-23, Cys-45 and
Cys-106 and a possible intramolecular disulfide bond involving
Cys-23 and Cys-45 give rise to different redox forms with specific
functional activities in various cellular compartments: 1- fully
reduced HMGB1 (HMGB1C23hC45hC106h), 2- disulfide HMGB1 (HMGB1C23-
C45C106h) and 3- sulfonyl HMGB1 (HMGB1C23soC45soC106so).
{ECO:0000269|PubMed:16962095, ECO:0000269|PubMed:19811284,
ECO:0000269|PubMed:22869893, ECO:0000305|PubMed:24531895}.
-!- PTM: Poly-ADP-ribosylated by PARP1 when secreted following
stimulation with LPS (By similarity).
{ECO:0000250|UniProtKB:P63158}.
-!- PTM: In vitro cleavage by CASP1 is liberating a HMG box 1-
containing peptide which may mediate immunogenic activity; the
peptide antagonizes apoptosis-induced immune tolerance
(PubMed:24474694). Can be proteolytically cleaved by a
thrombin:thrombomodulin complex; reduces binding to heparin and
proinflammatory activities (By similarity).
{ECO:0000250|UniProtKB:P10103, ECO:0000269|PubMed:24474694}.
-!- MISCELLANEOUS: Proposed to contribute to the pathogenesis of
various chronic inflammatory and autoimmune diseases, and cancer.
High serum levels are found in several inflammatory events
including sepsis, rheumatoid arthritis, artherosclerosis chronic
kidney disease, systemic lupus erythematosus (SLE). Seems to be
implicated in other diseases characterized by cell death and
damage, including diabetes and Alzheimer's disease. Its
nucleosome-associated release during secondory necrosis may play a
role in SLE (PubMed:19064698). During chemotherapy can mediate
regrowth and metastasis of remaining cells in a AGER/RAGE-
depenedent manner (PubMed:23040637). Purified HMG box 1 acts as a
specific antogonist to HGMB1 pro-imflammatory activities
(PubMed:14695889). {ECO:0000269|PubMed:14695889,
ECO:0000269|PubMed:23040637, ECO:0000305,
ECO:0000305|PubMed:19064698, ECO:0000305|PubMed:24220159,
ECO:0000305|PubMed:26078984}.
-!- SIMILARITY: Belongs to the HMGB family. {ECO:0000305}.
-!- CAUTION: Inconsistent experimental results may reflect the use of
inconsistently defined redox forms. A recombinant fully reduced
form has been used in a number of experiments. However, the redox
states of HMGB1 administered in vivo, may interconvert among each
other. Purified HMGB1 by itself has only weak pro-inflammatory
activity. {ECO:0000305}.
-!- WEB RESOURCE: Name=SeattleSNPs;
URL="http://pga.gs.washington.edu/data/hmgb1/";
-----------------------------------------------------------------------
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EMBL; X12597; CAA31110.1; -; mRNA.
EMBL; U51677; AAB08987.1; -; Genomic_DNA.
EMBL; D63874; BAA09924.1; -; mRNA.
EMBL; EF157968; ABM47301.1; -; Genomic_DNA.
EMBL; AY377859; AAQ91389.1; -; mRNA.
EMBL; AK291494; BAF84183.1; -; mRNA.
EMBL; AK122825; BAG53745.1; -; mRNA.
EMBL; CR749614; CAH18408.1; -; mRNA.
EMBL; CR456863; CAG33144.1; -; mRNA.
EMBL; BT006940; AAP35586.1; -; mRNA.
EMBL; BT020159; AAV38961.1; -; mRNA.
EMBL; EU012027; ABS29271.1; -; Genomic_DNA.
EMBL; AL353648; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; CH471075; EAX08457.1; -; Genomic_DNA.
EMBL; BC003378; AAH03378.1; -; mRNA.
EMBL; BC030981; AAH30981.1; -; mRNA.
EMBL; BC066889; AAH66889.1; -; mRNA.
EMBL; BC067732; AAH67732.1; -; mRNA.
EMBL; BC141844; AAI41845.1; -; mRNA.
CCDS; CCDS9335.1; -.
PIR; S02826; S02826.
RefSeq; NP_001300821.1; NM_001313892.1.
RefSeq; NP_001300822.1; NM_001313893.1.
RefSeq; NP_002119.1; NM_002128.5.
UniGene; Hs.434102; -.
UniGene; Hs.593339; -.
UniGene; Hs.596078; -.
PDB; 2LY4; NMR; -; A=2-84.
PDB; 2RTU; NMR; -; A=1-84.
PDB; 2YRQ; NMR; -; A=1-166.
PDBsum; 2LY4; -.
PDBsum; 2RTU; -.
PDBsum; 2YRQ; -.
ProteinModelPortal; P09429; -.
SMR; P09429; -.
BioGrid; 109389; 88.
CORUM; P09429; -.
DIP; DIP-24195N; -.
IntAct; P09429; 38.
MINT; MINT-153055; -.
STRING; 9606.ENSP00000343040; -.
BindingDB; P09429; -.
ChEMBL; CHEMBL2311236; -.
DrugBank; DB05869; CTI-01.
iPTMnet; P09429; -.
PhosphoSitePlus; P09429; -.
SwissPalm; P09429; -.
BioMuta; HMGB1; -.
DMDM; 123369; -.
DOSAC-COBS-2DPAGE; P09429; -.
EPD; P09429; -.
MaxQB; P09429; -.
PaxDb; P09429; -.
PeptideAtlas; P09429; -.
PRIDE; P09429; -.
TopDownProteomics; P09429; -.
DNASU; 3146; -.
Ensembl; ENST00000339872; ENSP00000343040; ENSG00000189403.
Ensembl; ENST00000341423; ENSP00000345347; ENSG00000189403.
Ensembl; ENST00000399494; ENSP00000382417; ENSG00000189403.
Ensembl; ENST00000405805; ENSP00000384678; ENSG00000189403.
GeneID; 3146; -.
KEGG; hsa:3146; -.
UCSC; uc001usx.5; human.
CTD; 3146; -.
DisGeNET; 3146; -.
EuPathDB; HostDB:ENSG00000189403.14; -.
GeneCards; HMGB1; -.
H-InvDB; HIX0030745; -.
HGNC; HGNC:4983; HMGB1.
HPA; CAB005873; -.
HPA; HPA003506; -.
MIM; 163905; gene.
neXtProt; NX_P09429; -.
OpenTargets; ENSG00000189403; -.
PharmGKB; PA188; -.
eggNOG; KOG0381; Eukaryota.
eggNOG; COG5648; LUCA.
GeneTree; ENSGT00760000119164; -.
HOGENOM; HOG000197861; -.
HOVERGEN; HBG009000; -.
InParanoid; P09429; -.
KO; K10802; -.
OMA; YSQDKRP; -.
OrthoDB; EOG091G0P81; -.
PhylomeDB; P09429; -.
TreeFam; TF105371; -.
Reactome; R-HSA-1810476; RIP-mediated NFkB activation via ZBP1.
Reactome; R-HSA-211227; Activation of DNA fragmentation factor.
Reactome; R-HSA-3134963; DEx/H-box helicases activate type I IFN and inflammatory cytokines production.
Reactome; R-HSA-445989; TAK1 activates NFkB by phosphorylation and activation of IKKs complex.
Reactome; R-HSA-5686938; Regulation of TLR by endogenous ligand.
Reactome; R-HSA-6798695; Neutrophil degranulation.
Reactome; R-HSA-879415; Advanced glycosylation endproduct receptor signaling.
Reactome; R-HSA-933542; TRAF6 mediated NF-kB activation.
SIGNOR; P09429; -.
ChiTaRS; HMGB1; human.
EvolutionaryTrace; P09429; -.
GeneWiki; HMGB1; -.
GenomeRNAi; 3146; -.
PRO; PR:P09429; -.
Proteomes; UP000005640; Chromosome 13.
Bgee; ENSG00000189403; -.
CleanEx; HS_HMGB1; -.
ExpressionAtlas; P09429; baseline and differential.
Genevisible; P09429; HS.
GO; GO:0009986; C:cell surface; IDA:UniProtKB.
GO; GO:0000793; C:condensed chromosome; IDA:UniProtKB.
GO; GO:0005769; C:early endosome; IEA:Ensembl.
GO; GO:0005793; C:endoplasmic reticulum-Golgi intermediate compartment; IEA:UniProtKB-SubCell.
GO; GO:0005576; C:extracellular region; TAS:Reactome.
GO; GO:0005615; C:extracellular space; IDA:UniProtKB.
GO; GO:1904813; C:ficolin-1-rich granule lumen; TAS:Reactome.
GO; GO:0043005; C:neuron projection; IEA:Ensembl.
GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
GO; GO:0005634; C:nucleus; IDA:UniProtKB.
GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
GO; GO:0034774; C:secretory granule lumen; TAS:Reactome.
GO; GO:0000405; F:bubble DNA binding; ISS:AgBase.
GO; GO:0019958; F:C-X-C chemokine binding; IDA:UniProtKB.
GO; GO:0010858; F:calcium-dependent protein kinase regulator activity; IEA:Ensembl.
GO; GO:0042056; F:chemoattractant activity; ISS:UniProtKB.
GO; GO:0005125; F:cytokine activity; ISS:UniProtKB.
GO; GO:0003684; F:damaged DNA binding; IDA:UniProtKB.
GO; GO:0008301; F:DNA binding, bending; IMP:UniProtKB.
GO; GO:0070182; F:DNA polymerase binding; IDA:UniProtKB.
GO; GO:0003690; F:double-stranded DNA binding; ISS:UniProtKB.
GO; GO:0003725; F:double-stranded RNA binding; IEA:Ensembl.
GO; GO:0000400; F:four-way junction DNA binding; ISS:AgBase.
GO; GO:0001530; F:lipopolysaccharide binding; IDA:UniProtKB.
GO; GO:0016829; F:lyase activity; IDA:UniProtKB.
GO; GO:0001786; F:phosphatidylserine binding; IDA:UniProtKB.
GO; GO:0030295; F:protein kinase activator activity; IEA:Ensembl.
GO; GO:0050786; F:RAGE receptor binding; ISS:UniProtKB.
GO; GO:0070491; F:repressing transcription factor binding; IPI:UniProtKB.
GO; GO:0003723; F:RNA binding; IDA:UniProtKB.
GO; GO:0003697; F:single-stranded DNA binding; ISS:UniProtKB.
GO; GO:0003727; F:single-stranded RNA binding; IEA:Ensembl.
GO; GO:0097100; F:supercoiled DNA binding; ISS:AgBase.
GO; GO:0003700; F:transcription factor activity, sequence-specific DNA binding; IDA:UniProtKB.
GO; GO:0008134; F:transcription factor binding; IPI:UniProtKB.
GO; GO:0002218; P:activation of innate immune response; IDA:UniProtKB.
GO; GO:0043277; P:apoptotic cell clearance; IDA:UniProtKB.
GO; GO:0006309; P:apoptotic DNA fragmentation; TAS:Reactome.
GO; GO:0006914; P:autophagy; IEA:UniProtKB-KW.
GO; GO:0006284; P:base-excision repair; IEA:Ensembl.
GO; GO:0031497; P:chromatin assembly; IEA:Ensembl.
GO; GO:0002407; P:dendritic cell chemotaxis; ISS:UniProtKB.
GO; GO:0032392; P:DNA geometric change; ISS:AgBase.
GO; GO:0051103; P:DNA ligation involved in DNA repair; ISS:UniProtKB.
GO; GO:0006310; P:DNA recombination; ISS:UniProtKB.
GO; GO:0006265; P:DNA topological change; ISS:UniProtKB.
GO; GO:0035767; P:endothelial cell chemotaxis; IEA:Ensembl.
GO; GO:0001935; P:endothelial cell proliferation; IEA:Ensembl.
GO; GO:0001654; P:eye development; IEA:Ensembl.
GO; GO:0006954; P:inflammatory response; IDA:CACAO.
GO; GO:0002437; P:inflammatory response to antigenic stimulus; IEP:UniProtKB.
GO; GO:0045087; P:innate immune response; TAS:Reactome.
GO; GO:0030324; P:lung development; IEA:Ensembl.
GO; GO:0002281; P:macrophage activation involved in immune response; IEA:Ensembl.
GO; GO:0001773; P:myeloid dendritic cell activation; ISS:UniProtKB.
GO; GO:2000426; P:negative regulation of apoptotic cell clearance; IEA:Ensembl.
GO; GO:0043537; P:negative regulation of blood vessel endothelial cell migration; IDA:CACAO.
GO; GO:0043371; P:negative regulation of CD4-positive, alpha-beta T cell differentiation; IDA:UniProtKB.
GO; GO:0032689; P:negative regulation of interferon-gamma production; IDA:UniProtKB.
GO; GO:0017055; P:negative regulation of RNA polymerase II transcriptional preinitiation complex assembly; IDA:UniProtKB.
GO; GO:0000122; P:negative regulation of transcription from RNA polymerase II promoter; IMP:UniProtKB.
GO; GO:0031175; P:neuron projection development; ISS:UniProtKB.
GO; GO:0097350; P:neutrophil clearance; IDA:UniProtKB.
GO; GO:0043312; P:neutrophil degranulation; TAS:Reactome.
GO; GO:0002270; P:plasmacytoid dendritic cell activation; IEA:Ensembl.
GO; GO:0042104; P:positive regulation of activated T cell proliferation; IMP:UniProtKB.
GO; GO:0043065; P:positive regulation of apoptotic process; IDA:UniProtKB.
GO; GO:0043280; P:positive regulation of cysteine-type endopeptidase activity involved in apoptotic process; IDA:UniProtKB.
GO; GO:0007204; P:positive regulation of cytosolic calcium ion concentration; IDA:UniProtKB.
GO; GO:2001200; P:positive regulation of dendritic cell differentiation; IMP:UniProtKB.
GO; GO:0043388; P:positive regulation of DNA binding; IDA:UniProtKB.
GO; GO:0051106; P:positive regulation of DNA ligation; ISS:UniProtKB.
GO; GO:0070374; P:positive regulation of ERK1 and ERK2 cascade; IDA:UniProtKB.
GO; GO:0045819; P:positive regulation of glycogen catabolic process; IEA:Ensembl.
GO; GO:0032727; P:positive regulation of interferon-alpha production; IEA:Ensembl.
GO; GO:0032728; P:positive regulation of interferon-beta production; IEA:Ensembl.
GO; GO:0050718; P:positive regulation of interleukin-1 beta secretion; IEA:Ensembl.
GO; GO:0050716; P:positive regulation of interleukin-1 secretion; IDA:UniProtKB.
GO; GO:0032733; P:positive regulation of interleukin-10 production; IDA:UniProtKB.
GO; GO:0032735; P:positive regulation of interleukin-12 production; IMP:UniProtKB.
GO; GO:2000778; P:positive regulation of interleukin-6 secretion; IDA:UniProtKB.
GO; GO:0046330; P:positive regulation of JNK cascade; IDA:UniProtKB.
GO; GO:0043410; P:positive regulation of MAPK cascade; IDA:UniProtKB.
GO; GO:0032425; P:positive regulation of mismatch repair; IDA:UniProtKB.
GO; GO:0090026; P:positive regulation of monocyte chemotaxis; IDA:UniProtKB.
GO; GO:0045639; P:positive regulation of myeloid cell differentiation; IEA:Ensembl.
GO; GO:1901224; P:positive regulation of NIK/NF-kappaB signaling; IEA:Ensembl.
GO; GO:1903672; P:positive regulation of sprouting angiogenesis; IEA:Ensembl.
GO; GO:0034137; P:positive regulation of toll-like receptor 2 signaling pathway; IEA:Ensembl.
GO; GO:0034145; P:positive regulation of toll-like receptor 4 signaling pathway; IEA:Ensembl.
GO; GO:0034165; P:positive regulation of toll-like receptor 9 signaling pathway; ISS:UniProtKB.
GO; GO:0045944; P:positive regulation of transcription from RNA polymerase II promoter; IDA:UniProtKB.
GO; GO:0032760; P:positive regulation of tumor necrosis factor production; IEA:Ensembl.
GO; GO:0090303; P:positive regulation of wound healing; IEA:Ensembl.
GO; GO:0010506; P:regulation of autophagy; IMP:UniProtKB.
GO; GO:2000819; P:regulation of nucleotide-excision repair; IEA:Ensembl.
GO; GO:0032072; P:regulation of restriction endodeoxyribonuclease activity; IDA:UniProtKB.
GO; GO:0002840; P:regulation of T cell mediated immune response to tumor cell; ISS:UniProtKB.
GO; GO:0002643; P:regulation of tolerance induction; IDA:UniProtKB.
GO; GO:0006357; P:regulation of transcription from RNA polymerase II promoter; IDA:UniProtKB.
GO; GO:0051384; P:response to glucocorticoid; IEA:Ensembl.
GO; GO:0035711; P:T-helper 1 cell activation; IDA:UniProtKB.
GO; GO:0045063; P:T-helper 1 cell differentiation; IMP:UniProtKB.
GO; GO:0002224; P:toll-like receptor signaling pathway; TAS:Reactome.
GO; GO:1990774; P:tumor necrosis factor secretion; IDA:UniProtKB.
GO; GO:0033151; P:V(D)J recombination; IDA:UniProtKB.
Gene3D; 1.10.30.10; -; 2.
InterPro; IPR009071; HMG_box_dom.
InterPro; IPR036910; HMG_box_dom_sf.
InterPro; IPR017967; HMG_boxA_CS.
Pfam; PF00505; HMG_box; 1.
Pfam; PF09011; HMG_box_2; 1.
SMART; SM00398; HMG; 2.
SUPFAM; SSF47095; SSF47095; 2.
PROSITE; PS00353; HMG_BOX_1; 1.
PROSITE; PS50118; HMG_BOX_2; 2.
1: Evidence at protein level;
3D-structure; Acetylation; Adaptive immunity; ADP-ribosylation;
Autophagy; Cell membrane; Chemotaxis; Chromosome; Complete proteome;
Cytoplasm; Direct protein sequencing; Disulfide bond; DNA damage;
DNA recombination; DNA repair; DNA-binding; Endosome; Immunity;
Inflammatory response; Innate immunity; Membrane; Nucleus; Oxidation;
Phosphoprotein; Polymorphism; Reference proteome; Repeat; Secreted.
CHAIN 1 215 High mobility group protein B1.
/FTId=PRO_0000048526.
DNA_BIND 9 79 HMG box 1. {ECO:0000255|PROSITE-
ProRule:PRU00267}.
DNA_BIND 95 163 HMG box 2. {ECO:0000255|PROSITE-
ProRule:PRU00267}.
REGION 1 97 Sufficient for interaction with HAVCR2.
{ECO:0000250|UniProtKB:P63158}.
REGION 1 10 Heparin-binding.
{ECO:0000250|UniProtKB:P10103}.
REGION 3 15 LPS binding (delipidated).
{ECO:0000269|PubMed:21660935}.
REGION 80 96 LPS binding (Lipid A).
{ECO:0000269|PubMed:21660935}.
REGION 89 108 Cytokine-stimulating activity.
{ECO:0000269|PubMed:12765338}.
REGION 150 183 Binding to AGER/RAGE.
{ECO:0000250|UniProtKB:P63159}.
MOTIF 27 43 Nuclear localization signal (NLS) 1.
{ECO:0000250|UniProtKB:P63159}.
MOTIF 178 184 Nuclear localization signal (NLS) 2.
{ECO:0000250|UniProtKB:P63159}.
COMPBIAS 186 215 Asp/Glu-rich (acidic).
SITE 10 11 Cleavage; by thrombin:thrombomodulin.
{ECO:0000250|UniProtKB:P10103}.
SITE 67 68 Cleavage; by CASP1.
{ECO:0000269|PubMed:24474694}.
MOD_RES 3 3 N6-acetyllysine.
{ECO:0000250|UniProtKB:P10103}.
MOD_RES 7 7 N6-acetyllysine.
{ECO:0000250|UniProtKB:P10103}.
MOD_RES 8 8 N6-acetyllysine.
{ECO:0000250|UniProtKB:P10103}.
MOD_RES 12 12 N6-acetyllysine.
{ECO:0000250|UniProtKB:P10103}.
MOD_RES 23 23 Cysteine sulfonic acid (-SO3H);
alternate.
{ECO:0000250|UniProtKB:P63159}.
MOD_RES 28 28 N6-acetyllysine.
{ECO:0000250|UniProtKB:P10103}.
MOD_RES 29 29 N6-acetyllysine.
{ECO:0000250|UniProtKB:P10103}.
MOD_RES 30 30 N6-acetyllysine.
{ECO:0000244|PubMed:19608861}.
MOD_RES 35 35 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:21406692,
ECO:0000244|PubMed:23186163}.
MOD_RES 43 43 N6-acetyllysine.
{ECO:0000250|UniProtKB:P63158}.
MOD_RES 45 45 Cysteine sulfonic acid (-SO3H);
alternate.
{ECO:0000250|UniProtKB:P63159}.
MOD_RES 90 90 N6-acetyllysine.
{ECO:0000250|UniProtKB:P63158}.
MOD_RES 100 100 Phosphoserine.
{ECO:0000244|PubMed:18669648}.
MOD_RES 106 106 Cysteine sulfonic acid (-SO3H).
{ECO:0000250|UniProtKB:P63159}.
MOD_RES 127 127 N6-acetyllysine.
{ECO:0000250|UniProtKB:P10103}.
MOD_RES 128 128 N6-acetyllysine.
{ECO:0000250|UniProtKB:P10103}.
MOD_RES 141 141 N6-acetyllysine.
{ECO:0000250|UniProtKB:P63158}.
MOD_RES 172 172 N6-acetyllysine.
{ECO:0000250|UniProtKB:P10103}.
MOD_RES 173 173 N6-acetyllysine.
{ECO:0000250|UniProtKB:P10103}.
MOD_RES 177 177 N6-acetyllysine.
{ECO:0000250|UniProtKB:P10103}.
MOD_RES 180 180 N6-acetyllysine.
{ECO:0000250|UniProtKB:P10103}.
MOD_RES 181 181 ADP-ribosylserine.
{ECO:0000269|PubMed:28190768}.
MOD_RES 182 182 N6-acetyllysine.
{ECO:0000250|UniProtKB:P10103}.
MOD_RES 183 183 N6-acetyllysine.
{ECO:0000250|UniProtKB:P10103}.
MOD_RES 184 184 N6-acetyllysine.
{ECO:0000250|UniProtKB:P10103}.
MOD_RES 185 185 N6-acetyllysine.
{ECO:0000250|UniProtKB:P10103}.
DISULFID 23 45 In disulfide HMGB1; alternate.
{ECO:0000250|UniProtKB:P63159}.
VARIANT 11 11 G -> R (in gastric-carcinoma cell line).
{ECO:0000269|PubMed:9036861}.
/FTId=VAR_046451.
VARIANT 149 149 A -> E (in gastric-carcinoma cell line).
{ECO:0000269|PubMed:9036861}.
/FTId=VAR_046452.
VARIANT 156 156 E -> Q. {ECO:0000269|Ref.10}.
/FTId=VAR_046453.
VARIANT 190 190 D -> G (in gastric-carcinoma cell line).
{ECO:0000269|PubMed:9036861}.
/FTId=VAR_046454.
MUTAGEN 35 35 S->A: Greatly reduces phosphorylation,
nuclear localization; when associated
with A-39; A-42; A-46; A-53 and A-181.
{ECO:0000269|PubMed:17114460}.
MUTAGEN 35 35 S->E: Cytoplasmic localization
(phosphorylation mimicking); when
associated with E-39; E-42; E-46; E-53
and E-181. {ECO:0000269|PubMed:17114460}.
MUTAGEN 39 39 S->A: Greatly reduces phosphorylation,
nuclear localization; when associated
with A-35; A-42; A-46; A-53 and A-181.
{ECO:0000269|PubMed:17114460}.
MUTAGEN 39 39 S->E: Cytoplasmic localization
(phosphorylation mimicking); when
associated with E-35; E-42; E-46; E-53
and E-181. {ECO:0000269|PubMed:17114460}.
MUTAGEN 42 42 S->A: Greatly reduces phosphorylation,
nuclear localization; when associated
with A-35; A-39; A-46; A-53 and A-181.
{ECO:0000269|PubMed:17114460}.
MUTAGEN 42 42 S->E: Cytoplasmic localization
(phosphorylation mimicking); when
associated with E-35; E-39; E-46; E-53
and E-181. {ECO:0000269|PubMed:17114460}.
MUTAGEN 46 46 S->A: Greatly reduces phosphorylation,
nuclear localization; when associated
with A-35; A-39; A-42; A-53 and A-181.
{ECO:0000269|PubMed:17114460}.
MUTAGEN 46 46 S->E: Cytoplasmic localization
(phosphorylation mimicking); when
associated with E-35; E-39; E-42; E-53
and E-181. {ECO:0000269|PubMed:17114460}.
MUTAGEN 53 53 S->A: Greatly reduces phosphorylation,
nuclear localization; when associated
with A-35; A-39; A-42; A-46 and A-181.
{ECO:0000269|PubMed:17114460}.
MUTAGEN 53 53 S->E: Cytoplasmic localization
(phosphorylation mimicking); when
associated with E-35; E-39; E-42; E-46
and E-181. {ECO:0000269|PubMed:17114460}.
MUTAGEN 67 67 D->A: Abolishes cleavage by CASP1 and
impairs ability to antagonize apoptosis-
induced immune tolerance.
{ECO:0000269|PubMed:24474694}.
MUTAGEN 106 106 C->S: Inhibits oxidation-dependent
inactivation of immunostimmulatory
activity in apoptotic cells.
{ECO:0000269|PubMed:18631454}.
MUTAGEN 181 181 S->A: Greatly reduces phosphorylation,
nuclear localization; when associated
with A-35; A-39; A-42; A-46 and A-53.
{ECO:0000269|PubMed:17114460}.
MUTAGEN 181 181 S->E: Cytoplasmic localization
(phosphorylation mimicking); when
associated with E-35; E-39; E-42; E-46
and E-53. {ECO:0000269|PubMed:17114460}.
CONFLICT 143 143 P -> H (in Ref. 13; AAI41845).
{ECO:0000305}.
CONFLICT 215 215 E -> D (in Ref. 8; CAG33144).
{ECO:0000305}.
STRAND 1 3 {ECO:0000244|PDB:2YRQ}.
STRAND 6 8 {ECO:0000244|PDB:2YRQ}.
HELIX 15 30 {ECO:0000244|PDB:2LY4}.
HELIX 38 50 {ECO:0000244|PDB:2LY4}.
HELIX 54 76 {ECO:0000244|PDB:2LY4}.
STRAND 92 94 {ECO:0000244|PDB:2YRQ}.
HELIX 101 116 {ECO:0000244|PDB:2YRQ}.
STRAND 118 120 {ECO:0000244|PDB:2YRQ}.
HELIX 122 135 {ECO:0000244|PDB:2YRQ}.
HELIX 138 140 {ECO:0000244|PDB:2YRQ}.
HELIX 141 163 {ECO:0000244|PDB:2YRQ}.
SEQUENCE 215 AA; 24894 MW; 8A868CF277D417B5 CRC64;
MGKGDPKKPR GKMSSYAFFV QTCREEHKKK HPDASVNFSE FSKKCSERWK TMSAKEKGKF
EDMAKADKAR YEREMKTYIP PKGETKKKFK DPNAPKRPPS AFFLFCSEYR PKIKGEHPGL
SIGDVAKKLG EMWNNTAADD KQPYEKKAAK LKEKYEKDIA AYRAKGKPDA AKKGVVKAEK
SKKKKEEEED EEDEEDEEEE EDEEDEDEEE DDDDE


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