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High mobility group protein B1 (Amphoterin) (Heparin-binding protein p30) (High mobility group protein 1) (HMG-1)

 HMGB1_RAT               Reviewed;         215 AA.
P63159; P07155; P27109; P27428; Q548R9;
01-APR-1988, integrated into UniProtKB/Swiss-Prot.
23-JAN-2007, sequence version 2.
30-AUG-2017, entry version 130.
RecName: Full=High mobility group protein B1;
AltName: Full=Amphoterin;
AltName: Full=Heparin-binding protein p30;
AltName: Full=High mobility group protein 1;
Short=HMG-1;
Name=Hmgb1; Synonyms=Hmg-1, Hmg1;
Rattus norvegicus (Rat).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Rattus.
NCBI_TaxID=10116;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
STRAIN=Sprague-Dawley; TISSUE=Liver;
PubMed=3684582; DOI=10.1093/nar/15.21.9077;
Paonessa G., Frank R., Cortese R.;
"Nucleotide sequence of rat liver HMG1 cDNA.";
Nucleic Acids Res. 15:9077-9077(1987).
[2]
SEQUENCE REVISION.
Bianchi M.;
Submitted (DEC-1988) to the EMBL/GenBank/DDBJ databases.
[3]
NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE, SUBCELLULAR
LOCATION, AND FUNCTION.
PubMed=1885601;
Merenmies J., Pihlaskari R., Laitinen J., Wartiovaara J., Rauvala H.;
"30-kDa heparin-binding protein of brain (amphoterin) involved in
neurite outgrowth. Amino acid sequence and localization in the
filopodia of the advancing plasma membrane.";
J. Biol. Chem. 266:16722-16729(1991).
[4]
NUCLEOTIDE SEQUENCE [MRNA].
STRAIN=Sprague-Dawley; TISSUE=Kidney;
Ito T., Suzuki A., Horimoto N., Imai E., Hori M.;
"Amphoterin is associated with the development of the kidney.";
Submitted (JUN-2000) to the EMBL/GenBank/DDBJ databases.
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Kidney, Prostate, 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).
[6]
PROTEIN SEQUENCE OF 2-21, SUBCELLULAR LOCATION, AND FUNCTION.
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).
[7]
DNA-BINDING.
PubMed=2922595; DOI=10.1126/science.2922595;
Bianchi M.E., Beltrame M., Paonessa G.;
"Specific recognition of cruciform DNA by nuclear protein HMG1.";
Science 243:1056-1059(1989).
[8]
FUNCTION.
PubMed=7592757; DOI=10.1074/jbc.270.43.25752;
Hori O., Brett J., Slattery T., Cao R., Zhang J., Chen J.X.,
Nagashima M., Lundh E.R., Vijay S., Nitecki D.;
"The receptor for advanced glycation end products (RAGE) is a cellular
binding site for amphoterin. Mediation of neurite outgrowth and co-
expression of rage and amphoterin in the developing nervous system.";
J. Biol. Chem. 270:25752-25761(1995).
[9]
INTERACTION WITH PTPRZ1.
PubMed=9507007; DOI=10.1074/jbc.273.12.6998;
Milev P., Chiba A., Haring M., Rauvala H., Schachner M., Ranscht B.,
Margolis R.K., Margolis R.U.;
"High affinity binding and overlapping localization of neurocan and
phosphacan/protein-tyrosine phosphatase-zeta/beta with tenascin-R,
amphoterin, and the heparin-binding growth-associated molecule.";
J. Biol. Chem. 273:6998-7005(1998).
[10]
FUNCTION.
PubMed=10866811; DOI=10.1046/j.1432-1327.2000.01450.x;
Stros M., Cherny D., Jovin T.M.;
"HMG1 protein stimulates DNA end joining by promoting association of
DNA molecules via their ends.";
Eur. J. Biochem. 267:4088-4097(2000).
[11]
FUNCTION.
PubMed=10952726; DOI=10.1084/jem.192.4.565;
Andersson U., Wang H., Palmblad K., Aveberger A.C., Bloom O.,
Erlandsson-Harris H., Janson A., Kokkola R., Zhang M., Yang H.,
Tracey K.J.;
"High mobility group 1 protein (HMG-1) stimulates proinflammatory
cytokine synthesis in human monocytes.";
J. Exp. Med. 192:565-570(2000).
[12]
FUNCTION.
PubMed=10830965; DOI=10.1038/35012626;
Taguchi A., Blood D.C., del Toro G., Canet A., Lee D.C., Qu W.,
Tanji N., Lu Y., Lalla E., Fu C., Hofmann M.A., Kislinger T.,
Ingram M., Lu A., Tanaka H., Hori O., Ogawa S., Stern D.M.,
Schmidt A.M.;
"Blockade of RAGE-amphoterin signalling suppresses tumour growth and
metastases.";
Nature 405:354-360(2000).
[13]
PHOSPHOLIPID-BINDING.
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).
[14]
DNA-BINDING, AND DOMAIN.
PubMed=11513603; DOI=10.1021/bi0100900;
Mueller S., Bianchi M.E., Knapp S.;
"Thermodynamics of HMGB1 interaction with duplex DNA.";
Biochemistry 40:10254-10261(2001).
[15]
FUNCTION, AND LIGAND FOR AGER RECEPTOR.
PubMed=12183440;
Huttunen H.J., Fages C., Kuja-Panula J., Ridley A.J., Rauvala H.;
"Receptor for advanced glycation end products-binding COOH-terminal
motif of amphoterin inhibits invasive migration and metastasis.";
Cancer Res. 62:4805-4811(2002).
[16]
FUNCTION.
PubMed=12486007; DOI=10.1093/emboj/cdf692;
Bonaldi T., Langst G., Strohner R., Becker P.B., Bianchi M.E.;
"The DNA chaperone HMGB1 facilitates ACF/CHRAC-dependent nucleosome
sliding.";
EMBO J. 21:6865-6873(2002).
[17]
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).
[18]
SUBCELLULAR LOCATION, MUTAGENESIS OF 28-LYS--LYS-30 AND
182-LYS--LYS-184, AND INTERACTION WITH XPO1.
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).
[19]
DOMAIN.
PubMed=15379539; DOI=10.1021/bi049364k;
Knapp S., Mueller S., Digilio G., Bonaldi T., Bianchi M.E., Musco G.;
"The long acidic tail of high mobility group box 1 (HMGB1) protein
forms an extended and flexible structure that interacts with specific
residues within and between the HMG boxes.";
Biochemistry 43:11992-11997(2004).
[20]
SUBCELLULAR LOCATION, CHROMATIN-BINDING, AND MUTAGENESIS OF PHE-38;
PHE-103 AND ILE-122.
PubMed=15808513; DOI=10.1016/j.molcel.2005.03.005;
Agresti A., Scaffidi P., Riva A., Caiolfa V.R., Bianchi M.E.;
"GR and HMGB1 interact only within chromatin and influence each
other's residence time.";
Mol. Cell 18:109-121(2005).
[21]
DISULFIDE BRIDGE, REDOX FORMS, AND MUTAGENESIS OF CYS-23; CYS-45 AND
CYS-106.
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).
[22]
ACETYLATION AT LYS-3.
PubMed=17269659; DOI=10.1021/bi0614479;
Ugrinova I., Mitkova E., Moskalenko C., Pashev I., Pasheva E.;
"DNA bending versus DNA end joining activity of HMGB1 protein is
modulated in vitro by acetylation.";
Biochemistry 46:2111-2117(2007).
[23]
FUNCTION.
PubMed=18277947; DOI=10.1097/SHK.0b013e3181672495;
Zhang L.T., Yao Y.M., Dong Y.Q., Dong N., Yu Y., Sheng Z.Y.;
"Relationship between high-mobility group box 1 protein release and T-
cell suppression in rats after thermal injury.";
Shock 30:449-455(2008).
[24]
INTERACTION WITH BECN1, AND MUTAGENESIS OF CYS-23; CYS-45 AND CYS-106.
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).
[25]
FUNCTION, LIGAND FOR TLR4:LY96 RECEPTOR COMPLEX, AND MUTAGENESIS OF
CYS-106.
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).
[26]
REDOX FORMS, FUNCTION, INTERACTION WITH CXCL12, 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).
[27]
REDOX FORMS, AND MUTAGENESIS OF CYS-45.
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).
[28]
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).
[29]
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).
[30]
FUNCTION.
PubMed=23508573; DOI=10.2119/molmed.2012.00306;
Kim S., Kim S.Y., Pribis J.P., Lotze M., Mollen K.P., Shapiro R.,
Loughran P., Scott M.J., Billiar T.R.;
"Signaling of high mobility group box 1 (HMGB1) through toll-like
receptor 4 in macrophages requires CD14.";
Mol. Med. 19:88-98(2013).
[31]
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).
[32]
FUNCTION, AND REDOX FORMS.
PubMed=24551219; DOI=10.1371/journal.pone.0089070;
Polanska E., Pospisilova S., Stros M.;
"Binding of histone H1 to DNA is differentially modulated by redox
state of HMGB1.";
PLoS ONE 9:E89070-E89070(2014).
[33]
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).
[34]
STRUCTURE BY NMR OF 88-165.
PubMed=8467791;
Weir H.M., Kraulis P.J., Hill C.S., Raine A.R.C., Laue E.D.,
Thomas J.O.;
"Structure of the HMG box motif in the B-domain of HMG1.";
EMBO J. 12:1311-1319(1993).
[35]
STRUCTURE BY NMR OF 1-84.
STRAIN=Sprague-Dawley;
PubMed=8527432; DOI=10.1021/bi00051a007;
Hardman C.H., Broadhurst R.W., Raine A.R.C., Grasser K.D.,
Thomas J.O., Laue E.D.;
"Structure of the A-domain of HMG1 and its interaction with DNA as
studied by heteronuclear three- and four-dimensional NMR
spectroscopy.";
Biochemistry 34:16596-16607(1995).
-!- 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. May be involved in platelet activation.
Binds to phosphatidylserine and phosphatidylethanolamide
(PubMed:11154118). Bound to RAGE mediates signaling for neuronal
outgrowth (PubMed:1885601, PubMed:2461949, PubMed:7592757,
PubMed:12183440). May play a role in accumulation of expanded
polyglutamine (polyQ) proteins. {ECO:0000250|UniProtKB:P09429,
ECO:0000250|UniProtKB:P10103, ECO:0000250|UniProtKB:P63158,
ECO:0000269|PubMed:11154118, ECO:0000269|PubMed:12183440,
ECO:0000269|PubMed:1885601, ECO:0000269|PubMed:2461949,
ECO:0000269|PubMed:7592757, 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
(PubMed:2922595, PubMed:11513603). 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:12486007). 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:10866811). 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
(PubMed:24551219). 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 (By
similarity). May be involved in mitochondrial quality control and
autophagy in a transcription-dependent fashion implicating HSPB1
(By similarity). Can modulate the activity of the telomerase
complex and may be involved in telomere maintenance (By
similarity). {ECO:0000250|UniProtKB:P09429,
ECO:0000250|UniProtKB:P10103, ECO:0000250|UniProtKB:P63158,
ECO:0000269|PubMed:10866811, ECO:0000269|PubMed:11513603,
ECO:0000269|PubMed:12486007, ECO:0000269|PubMed:24551219,
ECO:0000269|PubMed:2922595}.
-!- FUNCTION: In the cytoplasm proposed to dissociate the BECN1:BCL2
complex via competitive interaction with BECN1 leading to
autophagy activation (By similarity). 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:P09429, ECO:0000250|UniProtKB:P63158}.
-!- 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:22869893). 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.
Promotes extracellular DNA-induced AIM2 inflammasome activation
implicating AGER/RAGE (By similarity). 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:10952726, PubMed:20547845, PubMed:22869893). 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 (By similarity). 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:23508573). Contributes to tumor
proliferation by association with ACER/RAGE (PubMed:10830965). 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 (By
similarity). 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
(By similarity). 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 (PubMed:18277947).
Released HMGB1:nucleosome complexes formed during apoptosis can
signal through TLR2 to induce cytokine production. 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 (By
similarity). {ECO:0000250|UniProtKB:P09429,
ECO:0000250|UniProtKB:P10103, ECO:0000250|UniProtKB:P63158,
ECO:0000269|PubMed:10830965, ECO:0000269|PubMed:10952726,
ECO:0000269|PubMed:18277947, ECO:0000269|PubMed:22869893}.
-!- 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:22869893). 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 (By similarity). Interacts with AGER
(PubMed:12183440). Interacts with PTPRZ1 isoform 3/phosphacan
(PubMed:9507007). Interacts with SREBF1, TLR2, TLR4, TLR9, APEX1,
FEN1, POLB, TERT, 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. Interacts with THBD; prevents HGMB1 interaction with
ACER/RAGE and inhibits HGMB1 proinflammatory activity. Interacts
with HAVCR2; impairs HMGB1 binding to B-DNA and likely HMGB1-
mediated innate immume response (By similarity). Interacts with
XPO1; mediating nuclear export (PubMed:14532127).
{ECO:0000250|UniProtKB:P09429, ECO:0000250|UniProtKB:P63158,
ECO:0000269|PubMed:12183440, ECO:0000269|PubMed:14532127,
ECO:0000269|PubMed:20547845, ECO:0000269|PubMed:20819940,
ECO:0000269|PubMed:22869893}.
-!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:22869893}.
Cytoplasm {ECO:0000269|PubMed:22869893}. Secreted
{ECO:0000250|UniProtKB:P63158, ECO:0000269|PubMed:1885601,
ECO:0000269|PubMed:22869893}. Chromosome
{ECO:0000269|PubMed:12110890, ECO:0000269|PubMed:15808513}. Cell
membrane {ECO:0000269|PubMed:1885601, ECO:0000269|PubMed:2461949};
Peripheral membrane protein {ECO:0000269|PubMed:1885601,
ECO:0000269|PubMed:2461949}; Extracellular side
{ECO:0000269|PubMed:2461949}. 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. Nuclear export is in part XPO1-dependent
implicating NES contained in both HMG boxes 1 and 2
(PubMed:14532127). 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 form
which subsequently gets oxidized (PubMed:22869893). 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.
Secreted by plasma cells in response to LPS (By similarity).
Associated with the plasma membrane of filipodia in process-
growing cells, and also deposited into the substrate-attached
material (PubMed:1885601). {ECO:0000250|UniProtKB:P63158,
ECO:0000269|PubMed:14532127, ECO:0000269|PubMed:15808513,
ECO:0000269|PubMed:1885601, ECO:0000269|PubMed:22869893}.
-!- 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:0000269|PubMed:11513603, ECO:0000269|PubMed:15379539}.
-!- PTM: Phosphorylated at serine residues. Phosphorylation in both
NLS regions is required for cytoplasmic translocation followed by
secretion. {ECO:0000250|UniProtKB:P09429}.
-!- 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 (PubMed:14532127).
Acetylation on Lys-3 results in preferential binding to DNA ends
and impairs DNA bending activity (PubMed:17269659).
{ECO:0000250|UniProtKB:P10103, ECO:0000269|PubMed:14532127,
ECO:0000269|PubMed:17269659}.
-!- 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:22105604,
ECO:0000269|PubMed:22869893, ECO:0000269|PubMed:24551219,
ECO:0000305}.
-!- PTM: Poly-ADP-ribosylated by PARP1 when secreted following
stimulation with LPS. {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. Can be
proteolytically cleaved by a thrombin:thrombomodulin complex;
reduces binding to heparin and proinflammatory activities (By
similarity). {ECO:0000250|UniProtKB:P09429,
ECO:0000250|UniProtKB:P10103}.
-!- SIMILARITY: Belongs to the HMGB family. {ECO:0000305}.
-----------------------------------------------------------------------
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
Distributed under the Creative Commons Attribution-NoDerivs License
-----------------------------------------------------------------------
EMBL; M64986; AAA40729.1; -; mRNA.
EMBL; Y00463; CAA68526.1; -; mRNA.
EMBL; AF275734; AAF82799.1; -; mRNA.
EMBL; BC061779; AAH61779.1; -; mRNA.
EMBL; BC081839; AAH81839.1; -; mRNA.
EMBL; BC088402; AAH88402.1; -; mRNA.
PIR; A41175; NSRTH1.
RefSeq; NP_037095.1; NM_012963.2.
UniGene; Rn.144565; -.
UniGene; Rn.151172; -.
UniGene; Rn.165951; -.
UniGene; Rn.4121; -.
PDB; 1AAB; NMR; -; A=2-84.
PDB; 1CKT; X-ray; 2.50 A; A=8-78.
PDB; 1HME; NMR; -; A=89-165.
PDB; 1HMF; NMR; -; A=89-165.
PDB; 2GZK; NMR; -; A=82-165.
PDB; 4QR9; X-ray; 2.00 A; A/B=8-81.
PDBsum; 1AAB; -.
PDBsum; 1CKT; -.
PDBsum; 1HME; -.
PDBsum; 1HMF; -.
PDBsum; 2GZK; -.
PDBsum; 4QR9; -.
ProteinModelPortal; P63159; -.
SMR; P63159; -.
BioGrid; 247493; 7.
IntAct; P63159; 2.
STRING; 10116.ENSRNOP00000040874; -.
PaxDb; P63159; -.
PRIDE; P63159; -.
GeneID; 25459; -.
KEGG; rno:25459; -.
CTD; 3146; -.
RGD; 2802; Hmgb1.
eggNOG; KOG0381; Eukaryota.
eggNOG; COG5648; LUCA.
HOGENOM; HOG000197861; -.
HOVERGEN; HBG009000; -.
InParanoid; P63159; -.
KO; K10802; -.
PhylomeDB; P63159; -.
EvolutionaryTrace; P63159; -.
PRO; PR:P63159; -.
Proteomes; UP000002494; Unplaced.
GO; GO:0005694; C:chromosome; IEA:UniProtKB-SubCell.
GO; GO:0005737; C:cytoplasm; IDA:RGD.
GO; GO:0005829; C:cytosol; IDA:CAFA.
GO; GO:0005793; C:endoplasmic reticulum-Golgi intermediate compartment; IEA:UniProtKB-SubCell.
GO; GO:0005768; C:endosome; IEA:UniProtKB-SubCell.
GO; GO:0005615; C:extracellular space; IDA:RGD.
GO; GO:0045121; C:membrane raft; IDA:CAFA.
GO; GO:0005634; C:nucleus; IDA:RGD.
GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
GO; GO:0008097; F:5S rRNA binding; IDA:RGD.
GO; GO:0003681; F:bent DNA binding; IDA:MGI.
GO; GO:0000405; F:bubble DNA binding; ISS:AgBase.
GO; GO:0000402; F:crossed form four-way junction DNA binding; IDA:MGI.
GO; GO:0005125; F:cytokine activity; IDA:UniProtKB.
GO; GO:0008301; F:DNA binding, bending; IDA:RGD.
GO; GO:0003690; F:double-stranded DNA binding; IDA:RGD.
GO; GO:0000400; F:four-way junction DNA binding; IDA:RGD.
GO; GO:0051861; F:glycolipid binding; IDA:RGD.
GO; GO:0008201; F:heparin binding; IDA:RGD.
GO; GO:0000401; F:open form four-way junction DNA binding; IDA:MGI.
GO; GO:0042277; F:peptide binding; IDA:RGD.
GO; GO:0046983; F:protein dimerization activity; IDA:RGD.
GO; GO:0050786; F:RAGE receptor binding; IMP:RGD.
GO; GO:0003697; F:single-stranded DNA binding; IDA:RGD.
GO; GO:0097100; F:supercoiled DNA binding; ISS:AgBase.
GO; GO:0008134; F:transcription factor binding; IDA:RGD.
GO; GO:0031532; P:actin cytoskeleton reorganization; IMP:RGD.
GO; GO:0002250; P:adaptive immune response; IEA:UniProtKB-KW.
GO; GO:0043277; P:apoptotic cell clearance; ISS:UniProtKB.
GO; GO:0006914; P:autophagy; IEA:UniProtKB-KW.
GO; GO:0000902; P:cell morphogenesis; IMP:RGD.
GO; GO:0071347; P:cellular response to interleukin-1; IEP:RGD.
GO; GO:0006935; P:chemotaxis; IDA:RGD.
GO; GO:0007623; P:circadian rhythm; IEP:RGD.
GO; GO:0032392; P:DNA geometric change; IDA:MGI.
GO; GO:0006310; P:DNA recombination; IEA:UniProtKB-KW.
GO; GO:0006281; P:DNA repair; IEA:UniProtKB-KW.
GO; GO:0050930; P:induction of positive chemotaxis; IDA:MGI.
GO; GO:0006954; P:inflammatory response; IEA:UniProtKB-KW.
GO; GO:0050831; P:male-specific defense response to bacterium; IDA:RGD.
GO; GO:0051450; P:myoblast proliferation; IMP:RGD.
GO; GO:0008156; P:negative regulation of DNA replication; IDA:RGD.
GO; GO:0007399; P:nervous system development; IMP:RGD.
GO; GO:0031175; P:neuron projection development; IGI:UniProtKB.
GO; GO:0097350; P:neutrophil clearance; ISS:UniProtKB.
GO; GO:0043065; P:positive regulation of apoptotic process; IMP:RGD.
GO; GO:0010508; P:positive regulation of autophagy; IMP:RGD.
GO; GO:0010942; P:positive regulation of cell death; IMP:RGD.
GO; GO:0030335; P:positive regulation of cell migration; IDA:MGI.
GO; GO:0008284; P:positive regulation of cell proliferation; IDA:RGD.
GO; GO:0051106; P:positive regulation of DNA ligation; IDA:UniProtKB.
GO; GO:0032732; P:positive regulation of interleukin-1 production; IDA:UniProtKB.
GO; GO:0032755; P:positive regulation of interleukin-6 production; IDA:UniProtKB.
GO; GO:0032757; P:positive regulation of interleukin-8 production; IDA:UniProtKB.
GO; GO:0071642; P:positive regulation of macrophage inflammatory protein 1 alpha production; IDA:UniProtKB.
GO; GO:0002053; P:positive regulation of mesenchymal cell proliferation; IDA:MGI.
GO; GO:0045931; P:positive regulation of mitotic cell cycle; IDA:MGI.
GO; GO:0033034; P:positive regulation of myeloid cell apoptotic process; IDA:RGD.
GO; GO:0045663; P:positive regulation of myoblast differentiation; IMP:RGD.
GO; GO:0010976; P:positive regulation of neuron projection development; IMP:RGD.
GO; GO:0014911; P:positive regulation of smooth muscle cell migration; IMP:RGD.
GO; GO:0034165; P:positive regulation of toll-like receptor 9 signaling pathway; ISS:UniProtKB.
GO; GO:0032760; P:positive regulation of tumor necrosis factor production; IDA:UniProtKB.
GO; GO:0050727; P:regulation of inflammatory response; IDA:RGD.
GO; GO:0002840; P:regulation of T cell mediated immune response to tumor cell; ISS:UniProtKB.
GO; GO:0042493; P:response to drug; IEP:RGD.
GO; GO:0009749; P:response to glucose; IEP:RGD.
GO; GO:0009408; P:response to heat; IEP:RGD.
GO; GO:0032868; P:response to insulin; IEP:RGD.
GO; GO:0034341; P:response to interferon-gamma; IMP:RGD.
GO; GO:0032496; P:response to lipopolysaccharide; IEP:RGD.
Gene3D; 1.10.30.10; -; 2.
InterPro; IPR009071; HMG_box_dom.
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; Heparin-binding;
Immunity; Inflammatory response; Innate immunity; Membrane; Nucleus;
Oxidation; Phosphoprotein; Reference proteome; Repeat; Secreted.
INIT_MET 1 1 Removed. {ECO:0000269|PubMed:2461949}.
CHAIN 2 215 High mobility group protein B1.
/FTId=PRO_0000048530.
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 2 97 Sufficient for interaction with HAVCR2.
{ECO:0000250|UniProtKB:P63158}.
REGION 2 10 Heparin-binding.
{ECO:0000250|UniProtKB:P10103}.
REGION 3 15 LPS binding (delipidated).
{ECO:0000250|UniProtKB:P09429}.
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:0000269|PubMed:12183440}.
MOTIF 27 43 Nuclear localization signal (NLS) 1.
{ECO:0000269|PubMed:14532127}.
MOTIF 178 184 Nuclear localization signal (NLS) 2.
{ECO:0000269|PubMed:14532127}.
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:0000269|PubMed:17269659}.
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:0000305|PubMed:22869893}.
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:0000250|UniProtKB:P10103}.
MOD_RES 35 35 Phosphoserine.
{ECO:0000250|UniProtKB:P09429}.
MOD_RES 43 43 N6-acetyllysine.
{ECO:0000250|UniProtKB:P63158}.
MOD_RES 45 45 Cysteine sulfonic acid (-SO3H);
alternate. {ECO:0000305|PubMed:22869893}.
MOD_RES 90 90 N6-acetyllysine.
{ECO:0000250|UniProtKB:P63158}.
MOD_RES 100 100 Phosphoserine.
{ECO:0000250|UniProtKB:P09429}.
MOD_RES 106 106 Cysteine sulfonic acid (-SO3H).
{ECO:0000305|PubMed:22869893}.
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: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:0000269|PubMed:16962095,
ECO:0000269|PubMed:22869893,
ECO:0000269|PubMed:24551219}.
MUTAGEN 23 23 C->S: No effect on nuclear localization.
Decreases interaction with BCN1 and
impairs in autophagy induction. Abolishes
cytokine-stimulating activity and no
effect on chemoattractant activity; when
associated with S-45.
{ECO:0000269|PubMed:16962095,
ECO:0000269|PubMed:20819940,
ECO:0000269|PubMed:22869893}.
MUTAGEN 28 30 KKK->AAA: Partial cytoplasmic
localization; when associated with 181-
A--A-183. {ECO:0000269|PubMed:14532127}.
MUTAGEN 28 30 KKK->QQQ: Partial cytoplasmic
localization (mimicks acetylation); when
associated with 181-Q--Q-183.
{ECO:0000269|PubMed:14532127}.
MUTAGEN 38 38 F->A: Disrupts association with
chromatin; when associated A-103 and A-
122. {ECO:0000269|PubMed:15808513}.
MUTAGEN 45 45 C->A: Reduces TNF-stimulating activity.
{ECO:0000269|PubMed:22105604}.
MUTAGEN 45 45 C->S: No effect on nuclear localization.
Decreases interaction with BCN1 and
impairs autophagy induction. Abolishes
cytokine-stimulating activity and no
effect on chemoattractant activity; when
associated with S-23.
{ECO:0000269|PubMed:16962095,
ECO:0000269|PubMed:20819940,
ECO:0000269|PubMed:22869893}.
MUTAGEN 103 103 F->A: Disrupts association with
chromatin; when associated A-38 and A-
122. {ECO:0000269|PubMed:15808513}.
MUTAGEN 106 106 C->A: Disrupts interaction with TLR4:LY96
receptor complex and abolishes TNF
release from macrophages.
{ECO:0000269|PubMed:20547845}.
MUTAGEN 106 106 C->S: Abolishes cytokine-stimulating
activity; no effect on chemoattractant
activity; impaired nuclear and enhanced
cytoplasmic localization, retained
activity in autophagy regulation.
{ECO:0000269|PubMed:16962095,
ECO:0000269|PubMed:20819940,
ECO:0000269|PubMed:22869893}.
MUTAGEN 122 122 I->A: Disrupts association with
chromatin; when associated A-38 and A-
103. {ECO:0000269|PubMed:15808513}.
MUTAGEN 182 184 KKK->AAA: Partial cytoplasmic
localization; when associated with 27-A--
A-29. {ECO:0000269|PubMed:14532127}.
MUTAGEN 182 184 KKK->QQQ: Partial cytoplasmic
localization (mimicks acetylation); when
associated with 27-Q--Q-29.
{ECO:0000269|PubMed:14532127}.
HELIX 15 30 {ECO:0000244|PDB:4QR9}.
TURN 32 34 {ECO:0000244|PDB:1AAB}.
HELIX 38 51 {ECO:0000244|PDB:4QR9}.
HELIX 54 76 {ECO:0000244|PDB:4QR9}.
HELIX 86 88 {ECO:0000244|PDB:2GZK}.
HELIX 103 116 {ECO:0000244|PDB:1HME}.
HELIX 122 135 {ECO:0000244|PDB:1HME}.
HELIX 138 140 {ECO:0000244|PDB:1HME}.
HELIX 142 159 {ECO:0000244|PDB:1HME}.
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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