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

 HMGB1_MOUSE             Reviewed;         215 AA.
P63158; P07155; P27109; P27428;
01-APR-1988, integrated into UniProtKB/Swiss-Prot.
23-JAN-2007, sequence version 2.
22-NOV-2017, entry version 138.
RecName: Full=High mobility group protein B1;
AltName: Full=High mobility group protein 1;
Short=HMG-1;
Name=Hmgb1; Synonyms=Hmg-1, Hmg1;
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
STRAIN=C3H/He;
PubMed=1630928; DOI=10.1093/nar/20.13.3516;
Yotov W.V., St Arnaud R.;
"Nucleotide sequence of a mouse cDNA encoding the nonhistone
chromosomal high mobility group protein-1 (HMG1).";
Nucleic Acids Res. 20:3516-3516(1992).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=129/Sv; TISSUE=Liver;
PubMed=7961836;
Ferrari S., Ronfani L., Calogero S., Bianchi M.;
"The mouse gene coding for high mobility group 1 protein (HMG1).";
J. Biol. Chem. 269:28803-28808(1994).
[3]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=8180479; DOI=10.1007/BF00292334;
Pauken C.M., Nagle D.L., Bucan M., Lo C.W.;
"Molecular cloning, expression analysis, and chromosomal localization
of mouse Hmg1-containing sequences.";
Mamm. Genome 5:91-99(1994).
[4]
NUCLEOTIDE SEQUENCE [MRNA].
STRAIN=AKR/J;
PubMed=9047378; DOI=10.1016/S0161-5890(96)00073-9;
Marrugo J., Marsh D.G., Ghosh B.;
"The conserved lymphokine element-0 in the IL5 promoter binds to a
high mobility group-1 protein.";
Mol. Immunol. 33:1119-1125(1996).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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).
[6]
PROTEIN SEQUENCE OF 31-43 AND 113-127, AND IDENTIFICATION BY MASS
SPECTROMETRY.
STRAIN=C57BL/6J; TISSUE=Brain;
Lubec G., Kang S.U.;
Submitted (APR-2007) to UniProtKB.
[7]
SUBCELLULAR LOCATION.
PubMed=2461949; DOI=10.1083/jcb.107.6.2293;
Rauvala H., Merenmies J., Pihlaskari R., Korkolainen M., Huhtala M.L.,
Panula P.;
"The adhesive and neurite-promoting molecule p30: analysis of the
amino-terminal sequence and production of antipeptide antibodies that
detect p30 at the surface of neuroblastoma cells and of brain
neurons.";
J. Cell Biol. 107:2293-2305(1988).
[8]
FUNCTION, AND IDENTIFICATION IN THE RAG COMPLEX.
PubMed=9184213; DOI=10.1093/emboj/16.10.2665;
van Gent D.C., Hiom K., Paull T.T., Gellert M.;
"Stimulation of V(D)J cleavage by high mobility group proteins.";
EMBO J. 16:2665-2670(1997).
[9]
DISRUPTION PHENOTYPE.
PubMed=10391216; DOI=10.1038/10338;
Calogero S., Grassi F., Aguzzi A., Voigtlaender T., Ferrier P.,
Ferrari S., Bianchi M.E.;
"The lack of chromosomal protein Hmg1 does not disrupt cell growth but
causes lethal hypoglycaemia in newborn mice.";
Nat. Genet. 22:276-280(1999).
[10]
INVOLVEMENT IN SEPSIS.
PubMed=10398600; DOI=10.1126/science.285.5425.248;
Wang H., Bloom O., Zhang M., Vishnubhakat J.M., Ombrellino M., Che J.,
Frazier A., Yang H., Ivanova S., Borovikova L., Manogue K.R.,
Faist E., Abraham E., Andersson J., Andersson U., Molina P.E.,
Abumrad N.N., Sama A., Tracey K.J.;
"HMG-1 as a late mediator of endotoxin lethality in mice.";
Science 285:248-251(1999).
[11]
FUNCTION, AND SUBCELLULAR LOCATION.
PubMed=12110890; DOI=10.1038/nature00858;
Scaffidi P., Misteli T., Bianchi M.E.;
"Release of chromatin protein HMGB1 by necrotic cells triggers
inflammation.";
Nature 418:191-195(2002).
[12]
FUNCTION, AND INTERACTION WITH SREBF1.
PubMed=16040616; DOI=10.1074/jbc.M414549200\;
Najima Y., Yahagi N., Takeuchi Y., Matsuzaka T., Sekiya M.,
Nakagawa Y., Amemiya-Kudo M., Okazaki H., Okazaki S., Tamura Y.,
Iizuka Y., Ohashi K., Harada K., Gotoda T., Nagai R., Kadowaki T.,
Ishibashi S., Yamada N., Osuga J., Shimano H.;
"High mobility group protein-B1 interacts with sterol regulatory
element-binding proteins to enhance their DNA binding.";
J. Biol. Chem. 280:27523-27532(2005).
[13]
INTERACTION WITH TLR2 AND TLR4.
PubMed=16267105; DOI=10.1152/ajpcell.00401.2005;
Park J.S., Gamboni-Robertson F., He Q., Svetkauskaite D., Kim J.Y.,
Strassheim D., Sohn J.W., Yamada S., Maruyama I., Banerjee A.,
Ishizaka A., Abraham E.;
"High mobility group box 1 protein interacts with multiple Toll-like
receptors.";
Am. J. Physiol. 290:C917-C924(2006).
[14]
FUNCTION.
PubMed=16365390; DOI=10.4049/jimmunol.176.1.12;
Mitola S., Belleri M., Urbinati C., Coltrini D., Sparatore B.,
Pedrazzi M., Melloni E., Presta M.;
"Extracellular high mobility group box-1 protein is a proangiogenic
cytokine.";
J. Immunol. 176:12-15(2006).
[15]
PHOSPHORYLATION, 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).
[16]
FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH TLR9.
PubMed=17548579; DOI=10.1182/blood-2006-09-044776;
Ivanov S., Dragoi A.M., Wang X., Dallacosta C., Louten J., Musco G.,
Sitia G., Yap G.S., Wan Y., Biron C.A., Bianchi M.E., Wang H.,
Chu W.M.;
"A novel role for HMGB1 in TLR9-mediated inflammatory responses to
CpG-DNA.";
Blood 110:1970-1981(2007).
[17]
FUNCTION.
PubMed=17268551; DOI=10.1038/sj.emboj.7601552;
Orlova V.V., Choi E.Y., Xie C., Chavakis E., Bierhaus A., Ihanus E.,
Ballantyne C.M., Gahmberg C.G., Bianchi M.E., Nawroth P.P.,
Chavakis T.;
"A novel pathway of HMGB1-mediated inflammatory cell recruitment that
requires Mac-1-integrin.";
EMBO J. 26:1129-1139(2007).
[18]
FUNCTION.
PubMed=17568691; DOI=10.1016/j.imlet.2007.04.011;
El Mezayen R., El Gazzar M., Seeds M.C., McCall C.E., Dreskin S.C.,
Nicolls M.R.;
"Endogenous signals released from necrotic cells augment inflammatory
responses to bacterial endotoxin.";
Immunol. Lett. 111:36-44(2007).
[19]
FUNCTION, AND INTERACTION WITH APEX1; FEN1 AND POLB.
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).
[20]
FUNCTION, POLY-ADP-RIBOSYLATION, AND PHOSPHATIDYLSERINE-BINDING.
PubMed=18768881; DOI=10.4049/jimmunol.181.6.4240;
Liu G., Wang J., Park Y.J., Tsuruta Y., Lorne E.F., Zhao X.,
Abraham E.;
"High mobility group protein-1 inhibits phagocytosis of apoptotic
neutrophils through binding to phosphatidylserine.";
J. Immunol. 181:4240-4246(2008).
[21]
FUNCTION.
PubMed=18650382; DOI=10.1073/pnas.0803181105;
Lange S.S., Mitchell D.L., Vasquez K.M.;
"High mobility group protein B1 enhances DNA repair and chromatin
modification after DNA damage.";
Proc. Natl. Acad. Sci. U.S.A. 105:10320-10325(2008).
[22]
FUNCTION, AND SUBCELLULAR LOCATION.
PubMed=19890330; DOI=10.1038/nature08512;
Yanai H., Ban T., Wang Z., Choi M.K., Kawamura T., Negishi H.,
Nakasato M., Lu Y., Hangai S., Koshiba R., Savitsky D., Ronfani L.,
Akira S., Bianchi M.E., Honda K., Tamura T., Kodama T., Taniguchi T.;
"HMGB proteins function as universal sentinels for nucleic-acid-
mediated innate immune responses.";
Nature 462:99-103(2009).
[23]
FUNCTION, AND INTERACTION WITH CD24.
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).
[24]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung,
Pancreas, Spleen, and Testis;
PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
"A tissue-specific atlas of mouse protein phosphorylation and
expression.";
Cell 143:1174-1189(2010).
[25]
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).
[26]
ROLE OF NRLC4 AND NLRP3 INFLAMMASOMES IN HMGB1 RELEASE, AND
SUBCELLULAR LOCATION.
PubMed=20802146; DOI=10.4049/jimmunol.1000803;
Lamkanfi M., Sarkar A., Vande Walle L., Vitari A.C., Amer A.O.,
Wewers M.D., Tracey K.J., Kanneganti T.D., Dixit V.M.;
"Inflammasome-dependent release of the alarmin HMGB1 in endotoxemia.";
J. Immunol. 185:4385-4392(2010).
[27]
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).
[28]
FUNCTION.
PubMed=21641551; DOI=10.1016/j.cmet.2011.04.008;
Tang D., Kang R., Livesey K.M., Kroemer G., Billiar T.R.,
Van Houten B., Zeh H.J., Lotze M.T.;
"High-mobility group box 1 is essential for mitochondrial quality
control.";
Cell Metab. 13:701-711(2011).
[29]
FUNCTION.
PubMed=21419643; DOI=10.1016/j.cyto.2011.02.017;
Zhu X.M., Yao Y.M., Liang H.P., Xu C.T., Dong N., Yu Y., Sheng Z.Y.;
"High mobility group box-1 protein regulate immunosuppression of
regulatory T cells through toll-like receptor 4.";
Cytokine 54:296-304(2011).
[30]
SUBCELLULAR LOCATION.
PubMed=21319304; DOI=10.1002/pmic.201000491;
Vettermann C., Castor D., Mekker A., Gerrits B., Karas M., Jack H.M.;
"Proteome profiling suggests a pro-inflammatory role for plasma cells
through release of high-mobility group box 1 protein.";
Proteomics 11:1228-1237(2011).
[31]
FUNCTION, AND INTERACTION WITH TERT.
PubMed=22544226; DOI=10.1007/s00412-012-0373-x;
Polanska E., Dobsakova Z., Dvorackova M., Fajkus J., Stros M.;
"HMGB1 gene knockout in mouse embryonic fibroblasts results in reduced
telomerase activity and telomere dysfunction.";
Chromosoma 121:419-431(2012).
[32]
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).
[33]
CYSTEINE REDOX STATES, AND SUBCELLULAR LOCATION.
PubMed=22105604; DOI=10.2119/molmed.2011.00389;
Yang H., Lundback P., Ottosson L., Erlandsson-Harris H., Venereau E.,
Bianchi M.E., Al-Abed Y., Andersson U., Tracey K.J., Antoine D.J.;
"Redox modification of cysteine residues regulates the cytokine
activity of high mobility group box-1 (HMGB1).";
Mol. Med. 18:250-259(2012).
[34]
FUNCTION, AND POLY-ADP-RIBOSYLATION.
PubMed=22204001; DOI=10.2119/molmed.2011.00203;
Davis K., Banerjee S., Friggeri A., Bell C., Abraham E., Zerfaoui M.;
"Poly(ADP-ribosyl)ation of high mobility group box 1 (HMGB1) protein
enhances inhibition of efferocytosis.";
Mol. Med. 18:359-369(2012).
[35]
INTERACTION WITH HAVCR2.
PubMed=22842346; DOI=10.1038/ni.2376;
Chiba S., Baghdadi M., Akiba H., Yoshiyama H., Kinoshita I.,
Dosaka-Akita H., Fujioka Y., Ohba Y., Gorman J.V., Colgan J.D.,
Hirashima M., Uede T., Takaoka A., Yagita H., Jinushi M.;
"Tumor-infiltrating DCs suppress nucleic acid-mediated innate immune
responses through interactions between the receptor TIM-3 and the
alarmin HMGB1.";
Nat. Immunol. 13:832-842(2012).
[36]
FUNCTION.
PubMed=23108142; DOI=10.1158/0008-5472.CAN-12-2704;
He Y., Zha J., Wang Y., Liu W., Yang X., Yu P.;
"Tissue damage-associated 'danger signals' influence T-cell responses
that promote the progression of preneoplasia to cancer.";
Cancer Res. 73:629-639(2013).
[37]
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).
[38]
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).
[39]
ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-30; LYS-43; LYS-90 AND
LYS-141, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
ANALYSIS].
TISSUE=Embryonic fibroblast;
PubMed=23806337; DOI=10.1016/j.molcel.2013.06.001;
Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z.,
Zhang Y., Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.;
"SIRT5-mediated lysine desuccinylation impacts diverse metabolic
pathways.";
Mol. Cell 50:919-930(2013).
[40]
FUNCTION.
PubMed=24302768; DOI=10.1073/pnas.1320808110;
Yanai H., Matsuda A., An J., Koshiba R., Nishio J., Negishi H.,
Ikushima H., Onoe T., Ohdan H., Yoshida N., Taniguchi T.;
"Conditional ablation of HMGB1 in mice reveals its protective function
against endotoxemia and bacterial infection.";
Proc. Natl. Acad. Sci. U.S.A. 110:20699-20704(2013).
[41]
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).
[42]
FUNCTION.
PubMed=24606906; DOI=10.1016/j.cmet.2014.01.014;
Huebener P., Gwak G.Y., Pradere J.P., Quinzii C.M., Friedman R.,
Lin C.S., Trent C.M., Mederacke I., Zhao E., Dapito D.H., Lin Y.,
Goldberg I.J., Czaja M.J., Schwabe R.F.;
"High-mobility group box 1 is dispensable for autophagy, mitochondrial
quality control, and organ function in vivo.";
Cell Metab. 19:539-547(2014).
[43]
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).
[44]
FUNCTION.
PubMed=25642769; DOI=10.1172/JCI76344;
Zhu X., Messer J.S., Wang Y., Lin F., Cham C.M., Chang J.,
Billiar T.R., Lotze M.T., Boone D.L., Chang E.B.;
"Cytosolic HMGB1 controls the cellular autophagy/apoptosis checkpoint
during inflammation.";
J. Clin. Invest. 125:1098-1110(2015).
[45]
TISSUE SPECIFICITY, AND INVOLVEMENT IN AUTOIMMUNE DISEASE.
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).
[46]
FUNCTION, AND SUBCELLULAR LOCATION.
PubMed=25660970; DOI=10.1016/j.molimm.2015.01.023;
Li X., Yue Y., Zhu Y., Xiong S.;
"Extracellular, but not intracellular HMGB1, facilitates self-DNA
induced macrophage activation via promoting DNA accumulation in
endosomes and contributes to the pathogenesis of lupus nephritis.";
Mol. Immunol. 65:177-188(2015).
-!- 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.
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
proangiogenic activity (PubMed:16365390). May be involved in
platelet activation. Binds to phosphatidylserine and
phosphatidylethanolamide. Bound to RAGE mediates signaling for
neuronal outgrowth. May play a role in accumulation of expanded
polyglutamine (polyQ) proteins (By similarity).
{ECO:0000250|UniProtKB:P09429, ECO:0000250|UniProtKB:P10103,
ECO:0000250|UniProtKB:P12682, ECO:0000250|UniProtKB:P63159,
ECO:0000269|PubMed:16365390, 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. May be
involved in nucleotide excision repair (NER), mismatch repair
(MMR) and base excision repair (BER) pathways, and double strand
break repair such as non-homologous end joining (NHEJ)
(PubMed:17803946, PubMed:18650382). 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). In vitro can
displace histone H1 from highly bent DNA. 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 (PubMed:16040616).
Facilitates binding of TP53 to DNA (By similarity). Proposed to be
involved in mitochondrial quality control and autophagy in a
transcription-dependent fashion implicating HSPB1; however, this
function has been questioned (PubMed:21641551, PubMed:24606906).
Can modulate the activity of the telomerase complex and may be
involved in telomere maintenance (PubMed:22544226).
{ECO:0000250|UniProtKB:P09429, ECO:0000250|UniProtKB:P10103,
ECO:0000250|UniProtKB:P63159, ECO:0000269|PubMed:16040616,
ECO:0000269|PubMed:17803946, ECO:0000269|PubMed:18650382,
ECO:0000269|PubMed:21641551, ECO:0000269|PubMed:22544226,
ECO:0000269|PubMed:24606906}.
-!- FUNCTION: In the cytoplasm proposed to dissociate the BECN1:BCL2
complex via competitive interaction with BECN1 leading to
autophagy activation (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
(PubMed:25642769). In myeloid cells has a protective role against
endotoxemia and bacterial infection by promoting autophagy
(PubMed:24302768). Involved in endosomal translocation and
activation of TLR9 in response to CpG-DNA in macrophages
(PubMed:17548579). {ECO:0000250|UniProtKB:P09429,
ECO:0000269|PubMed:17548579, ECO:0000269|PubMed:20819940,
ECO:0000269|PubMed:21395369, ECO:0000269|PubMed:24302768,
ECO:0000269|PubMed:25642769}.
-!- 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 (PubMed:17268551). 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
(PubMed:19890330). Promotes extracellular DNA-induced AIM2
inflammasome activation implicating AGER/RAGE. Disulfide HMGB1
binds to transmembrane receptors, such as AGER/RAGE, TLR2, TLR4
and probably TREM1, thus activating their signal transduction
pathways (PubMed:17568691, PubMed:19264983, PubMed:21419643).
Mediates the release of cytokines/chemokines such as TNF, IL-1,
IL-6, IL-8, CCL2, CCL3, CCL4 and CXCL10 (PubMed:12110890,
PubMed:17548579). Promotes secretion of interferon-gamma by
macrophage-stimulated natural killer (NK) cells in concert with
other cytokines like IL-2 or IL-12. TLR4 is proposed to be the
primary receptor promoting macrophage activation and signaling
through TLR4 seems to implicate LY96/MD-2. 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 (By similarity). Contributes to tumor
proliferation by association with ACER/RAGE (By similarity). Can
bind to IL1-beta and signals through the IL1R1:IL1RAP receptor
complex (By similarity). 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 (PubMed:22204001, PubMed:18768881). In adaptive
immunity may be involved in enhancing immunity through activation
of effector T-cells and suppression of regulatory T (TReg) cells
(PubMed:21419643). 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 (PubMed:23108142). 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 (By similarity).
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 (By similarity). During
macrophage activation by activated lymphocyte-derived self
apoptotic DNA (ALD-DNA) promotes recruitment of ALD-DNA to
endosomes (PubMed:25660970). {ECO:0000250|UniProtKB:P09429,
ECO:0000250|UniProtKB:P10103, ECO:0000250|UniProtKB:P63159,
ECO:0000269|PubMed:12110890, ECO:0000269|PubMed:17268551,
ECO:0000269|PubMed:17568691, ECO:0000269|PubMed:18768881,
ECO:0000269|PubMed:19264983, ECO:0000269|PubMed:21419643,
ECO:0000269|PubMed:22204001, ECO:0000269|PubMed:22370717,
ECO:0000269|PubMed:23108142, ECO:0000269|PubMed:25660970,
ECO:0000305|PubMed:19890330}.
-!- 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
(By similarity). Component of the RAG complex composed of core
components RAG1 and RAG2, and associated component HMGB1 or HMGB2
(PubMed:9184213). 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, APEX1, FEN1, POLB, TERT
(PubMed:16040616, PubMed:16267105, PubMed:17548579,
PubMed:17803946, PubMed:22544226). Interacts with AGER, PTPRZ1,
IL1B, MSH2, XPA, XPC, HNF1A, TP53 (By similarity). 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 (By similarity). Interacts
with HAVCR2; impairs HMGB1 binding to B-DNA and likely HMGB1-
mediated innate immume response (PubMed:22842346). Interacts with
XPO1; mediating nuclear export (By similarity).
{ECO:0000250|UniProtKB:P09429, ECO:0000250|UniProtKB:P10103,
ECO:0000250|UniProtKB:P63159, ECO:0000269|PubMed:16040616,
ECO:0000269|PubMed:16267105, ECO:0000269|PubMed:17114460,
ECO:0000269|PubMed:17548579, ECO:0000269|PubMed:17803946,
ECO:0000269|PubMed:19264983, ECO:0000269|PubMed:20819940,
ECO:0000269|PubMed:22370717, ECO:0000269|PubMed:22544226,
ECO:0000269|PubMed:22842346, ECO:0000269|PubMed:9184213}.
-!- INTERACTION:
O88597:Becn1; NbExp=3; IntAct=EBI-6665811, EBI-643716;
Q8VIM0:Havcr2; NbExp=4; IntAct=EBI-6665811, EBI-6665112;
Q01860:POU5F1 (xeno); NbExp=3; IntAct=EBI-6665811, EBI-475687;
-!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:17114460,
ECO:0000269|PubMed:20819940}. Cytoplasm
{ECO:0000269|PubMed:17114460, ECO:0000269|PubMed:20819940}.
Secreted {ECO:0000269|PubMed:22105604}. Chromosome
{ECO:0000269|PubMed:12110890}. Cell membrane
{ECO:0000269|PubMed:2461949}; Peripheral membrane protein
{ECO:0000269|PubMed:2461949}; Extracellular side
{ECO:0000269|PubMed:2461949}. Endosome
{ECO:0000269|PubMed:19890330}. Endoplasmic reticulum-Golgi
intermediate compartment {ECO:0000305|PubMed:17548579}. Note=In
basal state predominantly nuclear. Shuttles between the cytoplasm
and the nucleus (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 (PubMed:20802146).
Passively released to the extracellular milieu from necrotic cells
by diffusion, involving the fully reduced form which subsequently
gets oxidized (PubMed:12110890). Also released from apoptic cells
(PubMed:25660970). Actively secreted 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, involving a nonconventional secretory process via
secretory lysosomes (PubMed:17548579). Secreted by plasma cells in
response to LPS (PubMed:21319304). Associated with the plasma
membrane of filipodia in process-growing cells, and also deposited
into the substrate-attached material (By similarity). Colocalizes
with DDX58 on endosomal membranes (PubMed:19890330).
{ECO:0000250|UniProtKB:P09429, ECO:0000269|PubMed:12110890,
ECO:0000269|PubMed:17114460, ECO:0000269|PubMed:17548579,
ECO:0000269|PubMed:19890330, ECO:0000269|PubMed:20802146,
ECO:0000269|PubMed:20819940, ECO:0000269|PubMed:21319304,
ECO:0000269|PubMed:22105604, ECO:0000269|PubMed:2461949,
ECO:0000269|PubMed:25660970}.
-!- TISSUE SPECIFICITY: Serum levels are found elevated in mice with
modeled systemic lupus erythematosus (SLE) and are correlated with
SLE disease activity (PubMed:26078984).
{ECO:0000269|PubMed:26078984}.
-!- DOMAIN: HMG box 2 mediates proinflammatory cytokine-stimulating
activity and binding to TLR4. However, not involved in mediating
immunogenic activity in the context of apoptosis-induced immune
tolerance. {ECO:0000250|UniProtKB:P09429}.
-!- 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.
{ECO:0000250|UniProtKB:P09429, ECO:0000250|UniProtKB:P63159}.
-!- PTM: Acetylated on multiple sites upon stimulation with LPS (By
similarity). Acetylation on lysine residues in the nuclear
localization signals (NLS 1 and NLS 2) leads to cytoplasmic
localization and subsequent secretion. 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}.
-!- PTM: Phosphorylated at serine residues (PubMed:17114460).
Phosphorylation in both NLS regions is required for cytoplasmic
translocation followed by secretion (By similarity).
{ECO:0000250|UniProtKB:P09429, ECO:0000269|PubMed:17114460}.
-!- 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 HGMB1 (HMGB1C23hC45hC106h), 2- Disulfide HMGB1 (HMGB1C23-
C45C106h) and 3- Sulfonyl HMGB1 (HMGB1C23soC45soC106so).
{ECO:0000269|PubMed:22105604}.
-!- PTM: Poly-ADP-ribosylated by PARP1 when secreted following
stimulation with LPS (PubMed:18768881, PubMed:22204001).
{ECO:0000269|PubMed:18768881, ECO:0000269|PubMed:22204001}.
-!- 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 (By
similarity). Can be proteolytically cleaved by a
thrombin:thrombomodulin complex; reduces binding to heparin and
proinflammatory activities. {ECO:0000250|UniProtKB:P09429,
ECO:0000250|UniProtKB:P10103}.
-!- DISRUPTION PHENOTYPE: Rapid death within 24 h following birth due
to hypoglycaemia. {ECO:0000269|PubMed:10391216}.
-!- MISCELLANEOUS: Plays a role in acute sepsis; administration of
antibodies to HMGB1 attenuates endotoxin lethality; administration
of HMGB1 itself is lethal (PubMed:10398600). Overexpression in
ALD-DNA-immunized mice significantly enhances the severity of
modeled SLE (PubMed:26078984). {ECO:0000269|PubMed:10398600,
ECO:0000269|PubMed:26078984}.
-!- SIMILARITY: Belongs to the HMGB family. {ECO:0000305}.
-----------------------------------------------------------------------
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EMBL; Z11997; CAA78042.1; -; mRNA.
EMBL; X80457; CAA56631.1; -; Genomic_DNA.
EMBL; U00431; AAA20508.1; -; mRNA.
EMBL; L38477; AAA57042.1; -; mRNA.
EMBL; BC006586; AAH06586.1; -; mRNA.
EMBL; BC008565; AAH08565.1; -; mRNA.
EMBL; BC083067; AAH83067.1; -; mRNA.
EMBL; BC085090; AAH85090.1; -; mRNA.
CCDS; CCDS19883.1; -.
PIR; I48688; I48688.
RefSeq; NP_001300823.1; NM_001313894.1.
RefSeq; NP_034569.1; NM_010439.4.
RefSeq; XP_003945388.1; XM_003945339.3.
UniGene; Mm.207047; -.
UniGene; Mm.313345; -.
DisProt; DP00384; -.
ProteinModelPortal; P63158; -.
SMR; P63158; -.
BioGrid; 200322; 1.
CORUM; P63158; -.
IntAct; P63158; 14.
MINT; MINT-225214; -.
STRING; 10090.ENSMUSP00000082682; -.
ChEMBL; CHEMBL2311237; -.
iPTMnet; P63158; -.
PhosphoSitePlus; P63158; -.
SwissPalm; P63158; -.
EPD; P63158; -.
PaxDb; P63158; -.
PeptideAtlas; P63158; -.
PRIDE; P63158; -.
Ensembl; ENSMUST00000085546; ENSMUSP00000082682; ENSMUSG00000066551.
Ensembl; ENSMUST00000093196; ENSMUSP00000106131; ENSMUSG00000066551.
Ensembl; ENSMUST00000110505; ENSMUSP00000106132; ENSMUSG00000066551.
GeneID; 100862258; -.
GeneID; 15289; -.
KEGG; mmu:100862258; -.
KEGG; mmu:15289; -.
UCSC; uc009apb.2; mouse.
CTD; 3146; -.
MGI; MGI:96113; Hmgb1.
eggNOG; KOG0381; Eukaryota.
eggNOG; COG5648; LUCA.
GeneTree; ENSGT00760000119164; -.
HOGENOM; HOG000197861; -.
HOVERGEN; HBG009000; -.
InParanoid; P63158; -.
KO; K10802; -.
OMA; YSQDKRP; -.
OrthoDB; EOG091G0P81; -.
PhylomeDB; P63158; -.
TreeFam; TF105371; -.
Reactome; R-MMU-1810476; RIP-mediated NFkB activation via ZBP1.
Reactome; R-MMU-211227; Activation of DNA fragmentation factor.
Reactome; R-MMU-3134963; DEx/H-box helicases activate type I IFN and inflammatory cytokines production.
Reactome; R-MMU-445989; TAK1 activates NFkB by phosphorylation and activation of IKKs complex.
Reactome; R-MMU-5686938; Regulation of TLR by endogenous ligand.
Reactome; R-MMU-6798695; Neutrophil degranulation.
Reactome; R-MMU-879415; Advanced glycosylation endproduct receptor signaling.
Reactome; R-MMU-933542; TRAF6 mediated NF-kB activation.
PRO; PR:P63158; -.
Proteomes; UP000000589; Chromosome 5.
Bgee; ENSMUSG00000066551; -.
CleanEx; MM_HMGB1; -.
ExpressionAtlas; P63158; baseline and differential.
Genevisible; P63158; MM.
GO; GO:0009986; C:cell surface; IEA:Ensembl.
GO; GO:0000793; C:condensed chromosome; IEA:Ensembl.
GO; GO:0005737; C:cytoplasm; IDA:MGI.
GO; GO:0005769; C:early endosome; IDA:UniProtKB.
GO; GO:0005793; C:endoplasmic reticulum-Golgi intermediate compartment; IEA:UniProtKB-SubCell.
GO; GO:0005576; C:extracellular region; TAS:BHF-UCL.
GO; GO:0005615; C:extracellular space; IDA:MGI.
GO; GO:0043005; C:neuron projection; IDA:MGI.
GO; GO:0005634; C:nucleus; IDA:MGI.
GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
GO; GO:0017053; C:transcriptional repressor complex; IEA:Ensembl.
GO; GO:0003681; F:bent DNA binding; ISO:MGI.
GO; GO:0000405; F:bubble DNA binding; ISS:AgBase.
GO; GO:0019958; F:C-X-C chemokine binding; IEA:Ensembl.
GO; GO:0010858; F:calcium-dependent protein kinase regulator activity; IDA:MGI.
GO; GO:0000402; F:crossed form four-way junction DNA binding; ISO:MGI.
GO; GO:0005125; F:cytokine activity; IDA:MGI.
GO; GO:0003684; F:damaged DNA binding; IEA:Ensembl.
GO; GO:0008301; F:DNA binding, bending; ISS:AgBase.
GO; GO:0070182; F:DNA polymerase binding; IEA:Ensembl.
GO; GO:0003690; F:double-stranded DNA binding; IDA:UniProtKB.
GO; GO:0003725; F:double-stranded RNA binding; IDA:UniProtKB.
GO; GO:0000400; F:four-way junction DNA binding; ISS:AgBase.
GO; GO:0008201; F:heparin binding; IEA:UniProtKB-KW.
GO; GO:0001530; F:lipopolysaccharide binding; IEA:Ensembl.
GO; GO:0016829; F:lyase activity; IEA:Ensembl.
GO; GO:0000401; F:open form four-way junction DNA binding; ISO:MGI.
GO; GO:0001786; F:phosphatidylserine binding; TAS:BHF-UCL.
GO; GO:0030295; F:protein kinase activator activity; IDA:MGI.
GO; GO:0070491; F:repressing transcription factor binding; IEA:Ensembl.
GO; GO:0003727; F:single-stranded RNA binding; IDA:UniProtKB.
GO; GO:0097100; F:supercoiled DNA binding; ISS:AgBase.
GO; GO:0003700; F:transcription factor activity, sequence-specific DNA binding; IEA:Ensembl.
GO; GO:0002218; P:activation of innate immune response; IEA:Ensembl.
GO; GO:0043277; P:apoptotic cell clearance; ISS:UniProtKB.
GO; GO:0006914; P:autophagy; IEA:UniProtKB-KW.
GO; GO:0006284; P:base-excision repair; IMP:UniProtKB.
GO; GO:0031497; P:chromatin assembly; IDA:UniProtKB.
GO; GO:0032392; P:DNA geometric change; ISS:AgBase.
GO; GO:0035767; P:endothelial cell chemotaxis; IDA:UniProtKB.
GO; GO:0001935; P:endothelial cell proliferation; IDA:UniProtKB.
GO; GO:0001654; P:eye development; IMP:MGI.
GO; GO:0050930; P:induction of positive chemotaxis; ISO:MGI.
GO; GO:0006954; P:inflammatory response; TAS:BHF-UCL.
GO; GO:0002437; P:inflammatory response to antigenic stimulus; IEA:Ensembl.
GO; GO:0045087; P:innate immune response; IEA:UniProtKB-KW.
GO; GO:0030324; P:lung development; IMP:MGI.
GO; GO:0002281; P:macrophage activation involved in immune response; IMP:UniProtKB.
GO; GO:0001773; P:myeloid dendritic cell activation; IMP:UniProtKB.
GO; GO:2000426; P:negative regulation of apoptotic cell clearance; IDA:BHF-UCL.
GO; GO:0043537; P:negative regulation of blood vessel endothelial cell migration; IEA:Ensembl.
GO; GO:0043371; P:negative regulation of CD4-positive, alpha-beta T cell differentiation; IEA:Ensembl.
GO; GO:0032689; P:negative regulation of interferon-gamma production; IEA:Ensembl.
GO; GO:0017055; P:negative regulation of RNA polymerase II transcriptional preinitiation complex assembly; IEA:Ensembl.
GO; GO:0097350; P:neutrophil clearance; ISS:UniProtKB.
GO; GO:0002270; P:plasmacytoid dendritic cell activation; IMP:UniProtKB.
GO; GO:0042104; P:positive regulation of activated T cell proliferation; IEA:Ensembl.
GO; GO:0030335; P:positive regulation of cell migration; ISO:MGI.
GO; GO:0043280; P:positive regulation of cysteine-type endopeptidase activity involved in apoptotic process; IEA:Ensembl.
GO; GO:0007204; P:positive regulation of cytosolic calcium ion concentration; IEA:Ensembl.
GO; GO:2001200; P:positive regulation of dendritic cell differentiation; IEA:Ensembl.
GO; GO:0043388; P:positive regulation of DNA binding; IEA:Ensembl.
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; IMP:MGI.
GO; GO:0045089; P:positive regulation of innate immune response; IMP:UniProtKB.
GO; GO:0032727; P:positive regulation of interferon-alpha production; IMP:UniProtKB.
GO; GO:0032728; P:positive regulation of interferon-beta production; IMP:UniProtKB.
GO; GO:0050718; P:positive regulation of interleukin-1 beta secretion; IMP:UniProtKB.
GO; GO:0032733; P:positive regulation of interleukin-10 production; IEA:Ensembl.
GO; GO:0032735; P:positive regulation of interleukin-12 production; IEA:Ensembl.
GO; GO:0032755; P:positive regulation of interleukin-6 production; IMP:UniProtKB.
GO; GO:2000778; P:positive regulation of interleukin-6 secretion; IEA:Ensembl.
GO; GO:0046330; P:positive regulation of JNK cascade; IEA:Ensembl.
GO; GO:0002053; P:positive regulation of mesenchymal cell proliferation; ISO:MGI.
GO; GO:0032425; P:positive regulation of mismatch repair; IEA:Ensembl.
GO; GO:0045931; P:positive regulation of mitotic cell cycle; ISO:MGI.
GO; GO:0090026; P:positive regulation of monocyte chemotaxis; IEA:Ensembl.
GO; GO:0045639; P:positive regulation of myeloid cell differentiation; IDA:MGI.
GO; GO:1901224; P:positive regulation of NIK/NF-kappaB signaling; IDA:UniProtKB.
GO; GO:0001934; P:positive regulation of protein phosphorylation; IDA:MGI.
GO; GO:1903672; P:positive regulation of sprouting angiogenesis; IDA:UniProtKB.
GO; GO:0034137; P:positive regulation of toll-like receptor 2 signaling pathway; IDA:UniProtKB.
GO; GO:0034145; P:positive regulation of toll-like receptor 4 signaling pathway; IDA:UniProtKB.
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; IMP:MGI.
GO; GO:0032760; P:positive regulation of tumor necrosis factor production; IMP:UniProtKB.
GO; GO:0090303; P:positive regulation of wound healing; IDA:UniProtKB.
GO; GO:0010506; P:regulation of autophagy; IMP:UniProtKB.
GO; GO:2000819; P:regulation of nucleotide-excision repair; IMP:UniProtKB.
GO; GO:0032072; P:regulation of restriction endodeoxyribonuclease activity; IEA:Ensembl.
GO; GO:0002840; P:regulation of T cell mediated immune response to tumor cell; IDA:UniProtKB.
GO; GO:0002643; P:regulation of tolerance induction; IMP:UniProtKB.
GO; GO:0051384; P:response to glucocorticoid; IMP:MGI.
GO; GO:0035711; P:T-helper 1 cell activation; IEA:Ensembl.
GO; GO:0045063; P:T-helper 1 cell differentiation; IEA:Ensembl.
GO; GO:1990774; P:tumor necrosis factor secretion; IEA:Ensembl.
GO; GO:0033151; P:V(D)J recombination; IEA:Ensembl.
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;
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; Heparin-binding;
Immunity; Inflammatory response; Innate immunity; Membrane; Nucleus;
Oxidation; Phosphoprotein; Reference proteome; Repeat; Secreted.
CHAIN 1 215 High mobility group protein B1.
/FTId=PRO_0000048528.
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:0000269|PubMed:22842346}.
REGION 1 10 Heparin-binding.
{ECO:0000250|UniProtKB:P10103}.
REGION 3 15 LPS binding (delipidated).
{ECO:0000250|UniProtKB:P09429}.
REGION 27 43 NLS 1. {ECO:0000250|UniProtKB:P63159}.
REGION 80 96 LPS binding (Lipid A).
{ECO:0000250|UniProtKB:P09429}.
REGION 89 108 Cytokine-stimulating activity.
{ECO:0000250|UniProtKB:P09429}.
REGION 150 183 Binding to AGER/RAGE.
{ECO:0000250|UniProtKB:P63159}.
REGION 178 184 NLS 2. {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:0000250|UniProtKB:P09429}.
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:23806337}.
MOD_RES 35 35 Phosphoserine.
{ECO:0000250|UniProtKB:P09429}.
MOD_RES 43 43 N6-acetyllysine.
{ECO:0000244|PubMed:23806337}.
MOD_RES 45 45 Cysteine sulfonic acid (-SO3H);
alternate.
{ECO:0000250|UniProtKB:P63159}.
MOD_RES 90 90 N6-acetyllysine.
{ECO:0000244|PubMed:23806337}.
MOD_RES 100 100 Phosphoserine.
{ECO:0000250|UniProtKB:P09429}.
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:0000244|PubMed:23806337}.
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:0000250|UniProtKB:P09429}.
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}.
CONFLICT 179 179 E -> V (in Ref. 4; AAA57042).
{ECO:0000305}.
CONFLICT 190 190 D -> E (in Ref. 2; CAA56631).
{ECO:0000305}.
SEQUENCE 215 AA; 24894 MW; 8A868DE266D552B5 CRC64;
MGKGDPKKPR GKMSSYAFFV QTCREEHKKK HPDASVNFSE FSKKCSERWK TMSAKEKGKF
EDMAKADKAR YEREMKTYIP PKGETKKKFK DPNAPKRPPS AFFLFCSEYR PKIKGEHPGL
SIGDVAKKLG EMWNNTAADD KQPYEKKAAK LKEKYEKDIA AYRAKGKPDA AKKGVVKAEK
SKKKKEEEDD EEDEEDEEEE EEEEDEDEEE DDDDE


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