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

 HMGB1_BOVIN             Reviewed;         215 AA.
P10103; A5D9G8; Q3ZC39;
01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
23-JAN-2007, sequence version 3.
30-AUG-2017, entry version 162.
RecName: Full=High mobility group protein B1;
AltName: Full=High mobility group protein 1;
Short=HMG-1;
Name=HMGB1; Synonyms=HMG1;
Bos taurus (Bovine).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Laurasiatheria; Cetartiodactyla; Ruminantia;
Pecora; Bovidae; Bovinae; Bos.
NCBI_TaxID=9913;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
STRAIN=Holstein; TISSUE=Fetal thymus;
PubMed=3194213; DOI=10.1093/nar/16.21.10375;
Kaplan D.J., Duncan C.H.;
"Full length cDNA sequence for bovine high mobility group 1 (HMG1)
protein.";
Nucleic Acids Res. 16:10375-10375(1988).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
PubMed=16305752; DOI=10.1186/1471-2164-6-166;
Harhay G.P., Sonstegard T.S., Keele J.W., Heaton M.P., Clawson M.L.,
Snelling W.M., Wiedmann R.T., Van Tassell C.P., Smith T.P.L.;
"Characterization of 954 bovine full-CDS cDNA sequences.";
BMC Genomics 6:166-166(2005).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=Hereford; TISSUE=Thymus;
NIH - Mammalian Gene Collection (MGC) project;
Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases.
[4]
NUCLEOTIDE SEQUENCE [MRNA] OF 116-215.
PubMed=6141822; DOI=10.1007/BF01120823;
Pentecost B., Dixon G.H.;
"Isolation and partial sequence of bovine cDNA clones for the high-
mobility-group protein (HMG-1).";
Biosci. Rep. 4:49-57(1984).
[5]
PROTEIN SEQUENCE OF 2-38; 46-157 AND 159-195.
PubMed=7202717; DOI=10.1016/0014-5793(80)80453-4;
Walker J.M., Gooderham K., Hastings J.R., Mayes E., Johns E.W.;
"The primary structures of non-histone chromosomal proteins HMG 1 and
2.";
FEBS Lett. 122:264-270(1980).
[6]
PROTEIN SEQUENCE OF 2-37.
PubMed=2365081; DOI=10.1016/0014-5793(90)80308-6;
Christen T., Bischoff M., Hobi R., Kuenzle C.C.;
"High mobility group proteins 1 and 2 bind preferentially to
brominated poly(dG-dC).poly(dG-dC) in the Z-DNA conformation but not
to other types of Z-DNA.";
FEBS Lett. 267:139-141(1990).
[7]
SUBCELLULAR LOCATION.
PubMed=7409193; DOI=10.1016/0014-5793(80)81219-1;
Itkes A.V., Glotov B.O., Nikolaev L.G., Severin E.S.;
"Clusters of nonhistone chromosomal protein HMG1 molecules in intact
chromatin.";
FEBS Lett. 118:63-66(1980).
[8]
ACETYLATION AT LYS-3; LYS-7; LYS-8; LYS-12; LYS-28; LYS-29; LYS-30;
LYS-127; LYS-128; LYS-172; LYS-173; LYS-177; LYS-180; LYS-182;
LYS-183; LYS-184 AND LYS-185.
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).
[9]
FUNCTION.
PubMed=16966386; DOI=10.1189/jlb.0306180;
Yang D., Chen Q., Yang H., Tracey K.J., Bustin M., Oppenheim J.J.;
"High mobility group box-1 protein induces the migration and
activation of human dendritic cells and acts as an alarmin.";
J. Leukoc. Biol. 81:59-66(2007).
[10]
FUNCTION, AND INTERACTION WITH AGER.
PubMed=17417641; DOI=10.1038/ni1457;
Tian J., Avalos A.M., Mao S.Y., Chen B., Senthil K., Wu H.,
Parroche P., Drabic S., Golenbock D., Sirois C., Hua J., An L.L.,
Audoly L., La Rosa G., Bierhaus A., Naworth P., Marshak-Rothstein A.,
Crow M.K., Fitzgerald K.A., Latz E., Kiener P.A., Coyle A.J.;
"Toll-like receptor 9-dependent activation by DNA-containing immune
complexes is mediated by HMGB1 and RAGE.";
Nat. Immunol. 8:487-496(2007).
[11]
FUNCTION.
PubMed=20014975; DOI=10.3109/08916930903384591;
Avalos A.M., Kiefer K., Tian J., Christensen S., Shlomchik M.,
Coyle A.J., Marshak-Rothstein A.;
"RAGE-independent autoreactive B cell activation in response to
chromatin and HMGB1/DNA immune complexes.";
Autoimmunity 43:103-110(2010).
[12]
HEPARIN-BINDING, AND CLEAVAGE BY THROMBIN:THROMBOMODULIN.
PubMed=18599803; DOI=10.1161/ATVBAHA.107.150631;
Ito T., Kawahara K., Okamoto K., Yamada S., Yasuda M., Imaizumi H.,
Nawa Y., Meng X., Shrestha B., Hashiguchi T., Maruyama I.;
"Proteolytic cleavage of high mobility group box 1 protein by
thrombin-thrombomodulin complexes.";
Arterioscler. Thromb. Vasc. Biol. 28:1825-1830(2008).
[13]
FUNCTION.
PubMed=22941653; DOI=10.1093/nar/gks815;
Joshi S.R., Sarpong Y.C., Peterson R.C., Scovell W.M.;
"Nucleosome dynamics: HMGB1 relaxes canonical nucleosome structure to
facilitate estrogen receptor binding.";
Nucleic Acids Res. 40:10161-10171(2012).
[14]
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).
[15]
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).
[16]
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).
[17]
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).
-!- 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. 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:P63158, ECO:0000250|UniProtKB:P63159,
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). 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. Can restructure the canonical nucleosome leading to
relaxation of structural constraints for transcription factor-
binding (PubMed:22941653). Enhances binding of sterol regulatory
element-binding proteins (SREBPs) such as SREBF1 to their cognate
DNA sequences and increases their transcriptional activities.
Facilitates binding of TP53 to DNA. May be involved in
mitochondrial quality control and autophagy in a transcription-
dependent fashion implicating HSPB1. Can modulate the activity of
the telomerase complex and may be involved in telomere maintenance
(By similarity). {ECO:0000250|UniProtKB:P09429,
ECO:0000250|UniProtKB:P63158, ECO:0000250|UniProtKB:P63159,
ECO:0000269|PubMed:22941653}.
-!- FUNCTION: In the cytoplasm proposed to dissociate the BECN1:BCL2
complex via competitive interaction with BECN1 leading to
autophagy activation. Involved in oxidative stress-mediated
autophagy. 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. In myeloid cells has a
protective role against endotoxemia and bacterial infection by
promoting autophagy. 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 (By similarity). 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:16966386). 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
(PubMed:17417641). Mediates the release of cytokines/chemokines
such as TNF, IL-1, IL-6, IL-8, CCL2, CCL3, CCL4 and CXCL10.
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. Contributes to tumor proliferation by association with
ACER/RAGE. 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 (PubMed:17417641). 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 (PubMed:20014975). 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. In
adaptive immunity may be involved in enhancing immunity through
activation of effector T-cells and suppression of regulatory T
(TReg) cells. 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. Also reported to limit
proliferation of T-cells. 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. 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:P63158, ECO:0000250|UniProtKB:P63159,
ECO:0000269|PubMed:16966386, ECO:0000269|PubMed:17417641,
ECO:0000269|PubMed:20014975}.
-!- 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. Associates
with the TLR4:LY96 receptor complex. Component of the RAG complex
composed of core components RAG1 and RAG2, and associated
component HMGB1 or HMGB2. Interacts (in cytoplasm upon starvation)
with BECN1; inhibits the interaction of BECN1 and BCL2 leading to
promotion of autophagy. Interacts with KPNA1; involved in nuclear
import (By similarity). Interacts with AGER (PubMed:17417641).
Interacts with SREBF1, TLR2, TLR4, TLR9, PTPRZ1, APEX1, FEN1,
POLB, TERT. Interacts with IL1B, MSH2, XPA, XPC, HNF1A, TP53.
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. Interacts with XPO1; mediating nuclear export (By
similarity). {ECO:0000250|UniProtKB:P09429,
ECO:0000250|UniProtKB:P63158, ECO:0000250|UniProtKB:P63159}.
-!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:7409193}.
Chromosome {ECO:0000269|PubMed:7409193}. Cytoplasm
{ECO:0000250|UniProtKB:P09429}. Secreted
{ECO:0000250|UniProtKB:P09429, ECO:0000250|UniProtKB:P63158}. Cell
membrane {ECO:0000250|UniProtKB:P09429,
ECO:0000250|UniProtKB:P63158, ECO:0000250|UniProtKB:P63159};
Peripheral membrane protein {ECO:0000250|UniProtKB:P09429,
ECO:0000250|UniProtKB:P63158, ECO:0000250|UniProtKB:P63159};
Extracellular side {ECO:0000250|UniProtKB:P09429,
ECO:0000250|UniProtKB:P63158, ECO:0000250|UniProtKB:P63159}.
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. Translocates from the nucleus to the
cytoplasm upon autophagy stimulation. 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. Also
released from apoptic cells. Active secretion from a variety of
immune and non-immune cells such as macrophages, monocytes,
neutrophils, dendritic cells, natural killer cells and plasma
cells in response to various stimuli such as LPS and cytokines
involves a nonconventional secretory process via secretory
lysosomes. Found on the surface of activated platelets.
{ECO:0000250|UniProtKB:P09429, ECO:0000250|UniProtKB:P63158}.
-!- 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: 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.
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
(By similarity). {ECO:0000250|UniProtKB:P63159,
ECO:0000269|PubMed:14532127}.
-!- 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:0000250|UniProtKB:P09429}.
-!- 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 (By
similarity). Can be proteolytically cleaved by a
thrombin:thrombomodulin complex; reduces binding to heparin and
proinflammatory activities. {ECO:0000250|UniProtKB:P09429,
ECO:0000269|PubMed:18599803}.
-!- SIMILARITY: Belongs to the HMGB family. {ECO:0000305}.
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EMBL; X12796; CAA31284.1; -; mRNA.
EMBL; BT030587; ABQ13027.1; -; mRNA.
EMBL; BC102929; AAI02930.1; -; mRNA.
EMBL; M26110; AAA30567.1; -; mRNA.
PIR; S01947; S01947.
RefSeq; NP_788785.1; NM_176612.1.
RefSeq; XP_005213615.1; XM_005213558.1.
RefSeq; XP_010808966.1; XM_010810664.2.
UniGene; Bt.49650; -.
ProteinModelPortal; P10103; -.
SMR; P10103; -.
STRING; 9913.ENSBTAP00000024094; -.
iPTMnet; P10103; -.
PaxDb; P10103; -.
PeptideAtlas; P10103; -.
PRIDE; P10103; -.
Ensembl; ENSBTAT00000024094; ENSBTAP00000024094; ENSBTAG00000018103.
GeneID; 282691; -.
KEGG; bta:282691; -.
CTD; 3146; -.
eggNOG; KOG0381; Eukaryota.
eggNOG; COG5648; LUCA.
GeneTree; ENSGT00760000119164; -.
HOGENOM; HOG000197861; -.
HOVERGEN; HBG009000; -.
InParanoid; P10103; -.
KO; K10802; -.
OMA; YSQDKRP; -.
OrthoDB; EOG091G0P81; -.
TreeFam; TF105371; -.
Reactome; R-BTA-1810476; RIP-mediated NFkB activation via ZBP1.
Reactome; R-BTA-211227; Activation of DNA fragmentation factor.
Reactome; R-BTA-3134963; DEx/H-box helicases activate type I IFN and inflammatory cytokines production.
Reactome; R-BTA-445989; TAK1 activates NFkB by phosphorylation and activation of IKKs complex.
Reactome; R-BTA-5686938; Regulation of TLR by endogenous ligand.
Reactome; R-BTA-6798695; Neutrophil degranulation.
Reactome; R-BTA-879415; Advanced glycosylation endproduct receptor signaling.
Reactome; R-BTA-933542; TRAF6 mediated NF-kB activation.
Proteomes; UP000009136; Chromosome 12.
Bgee; ENSBTAG00000018103; -.
GO; GO:0005623; C:cell; ISS:AgBase.
GO; GO:0000793; C:condensed chromosome; ISS:AgBase.
GO; GO:0005793; C:endoplasmic reticulum-Golgi intermediate compartment; IEA:UniProtKB-SubCell.
GO; GO:0005768; C:endosome; IEA:UniProtKB-SubCell.
GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
GO; GO:0000790; C:nuclear chromatin; ISS:AgBase.
GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
GO; GO:0000405; F:bubble DNA binding; ISS:AgBase.
GO; GO:0042056; F:chemoattractant activity; IDA:UniProtKB.
GO; GO:0003684; F:damaged DNA binding; IDA:UniProtKB.
GO; GO:0008301; F:DNA binding, bending; IDA:UniProtKB.
GO; GO:0003690; F:double-stranded DNA binding; IDA:UniProtKB.
GO; GO:0000400; F:four-way junction DNA binding; ISS:AgBase.
GO; GO:0042393; F:histone binding; IDA:UniProtKB.
GO; GO:0044378; F:non-sequence-specific DNA binding, bending; ISS:AgBase.
GO; GO:0050786; F:RAGE receptor binding; IDA:UniProtKB.
GO; GO:0003697; F:single-stranded DNA binding; IDA:UniProtKB.
GO; GO:0097100; F:supercoiled DNA binding; ISS:AgBase.
GO; GO:0045322; F:unmethylated CpG binding; IDA:UniProtKB.
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:0002322; P:B cell proliferation involved in immune response; IDA:UniProtKB.
GO; GO:0006338; P:chromatin remodeling; NAS:UniProtKB.
GO; GO:0002407; P:dendritic cell chemotaxis; IDA:UniProtKB.
GO; GO:0032392; P:DNA geometric change; ISS:AgBase.
GO; GO:0051103; P:DNA ligation involved in DNA repair; ISS:AgBase.
GO; GO:0006310; P:DNA recombination; IDA:UniProtKB.
GO; GO:0006265; P:DNA topological change; IDA:UniProtKB.
GO; GO:0006954; P:inflammatory response; IEA:UniProtKB-KW.
GO; GO:0045087; P:innate immune response; IEA:UniProtKB-KW.
GO; GO:0001773; P:myeloid dendritic cell activation; IDA:UniProtKB.
GO; GO:0017055; P:negative regulation of RNA polymerase II transcriptional preinitiation complex assembly; ISS:AgBase.
GO; GO:0097350; P:neutrophil clearance; ISS:UniProtKB.
GO; GO:0006334; P:nucleosome assembly; ISS:AgBase.
GO; GO:0002270; P:plasmacytoid dendritic cell activation; IDA:UniProtKB.
GO; GO:0051106; P:positive regulation of DNA ligation; ISS:UniProtKB.
GO; GO:1902741; P:positive regulation of interferon-alpha secretion; IDA:UniProtKB.
GO; GO:0034165; P:positive regulation of toll-like receptor 9 signaling pathway; IMP:UniProtKB.
GO; GO:0002840; P:regulation of T cell mediated immune response to tumor cell; ISS:UniProtKB.
GO; GO:0006357; P:regulation of transcription from RNA polymerase II promoter; ISS:UniProtKB.
GO; GO:0034162; P:toll-like receptor 9 signaling pathway; IDA:UniProtKB.
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; 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; Immunity;
Inflammatory response; Innate immunity; Membrane; Nucleus; Oxidation;
Phosphoprotein; Reference proteome; Repeat; Secreted.
INIT_MET 1 1 Removed. {ECO:0000269|PubMed:2365081,
ECO:0000269|PubMed:7202717}.
CHAIN 2 215 High mobility group protein B1.
/FTId=PRO_0000048523.
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:0000269|PubMed:18599803}.
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: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:0000269|PubMed:18599803}.
SITE 67 68 Cleavage; by CASP1.
{ECO:0000250|UniProtKB:P09429}.
MOD_RES 3 3 N6-acetyllysine.
{ECO:0000269|PubMed:14532127}.
MOD_RES 7 7 N6-acetyllysine.
{ECO:0000269|PubMed:14532127}.
MOD_RES 8 8 N6-acetyllysine.
{ECO:0000269|PubMed:14532127}.
MOD_RES 12 12 N6-acetyllysine.
{ECO:0000269|PubMed:14532127}.
MOD_RES 23 23 Cysteine sulfonic acid (-SO3H);
alternate.
{ECO:0000250|UniProtKB:P63159}.
MOD_RES 28 28 N6-acetyllysine.
{ECO:0000269|PubMed:14532127}.
MOD_RES 29 29 N6-acetyllysine.
{ECO:0000269|PubMed:14532127}.
MOD_RES 30 30 N6-acetyllysine.
{ECO:0000269|PubMed:14532127}.
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:0000250|UniProtKB:P63159}.
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:0000250|UniProtKB:P63159}.
MOD_RES 127 127 N6-acetyllysine.
{ECO:0000269|PubMed:14532127}.
MOD_RES 128 128 N6-acetyllysine.
{ECO:0000269|PubMed:14532127}.
MOD_RES 141 141 N6-acetyllysine.
{ECO:0000250|UniProtKB:P63158}.
MOD_RES 172 172 N6-acetyllysine.
{ECO:0000269|PubMed:14532127}.
MOD_RES 173 173 N6-acetyllysine.
{ECO:0000269|PubMed:14532127}.
MOD_RES 177 177 N6-acetyllysine.
{ECO:0000269|PubMed:14532127}.
MOD_RES 180 180 N6-acetyllysine.
{ECO:0000269|PubMed:14532127}.
MOD_RES 181 181 ADP-ribosylserine.
{ECO:0000250|UniProtKB:P09429}.
MOD_RES 182 182 N6-acetyllysine.
{ECO:0000269|PubMed:14532127}.
MOD_RES 183 183 N6-acetyllysine.
{ECO:0000269|PubMed:14532127}.
MOD_RES 184 184 N6-acetyllysine.
{ECO:0000269|PubMed:14532127}.
MOD_RES 185 185 N6-acetyllysine.
{ECO:0000269|PubMed:14532127}.
DISULFID 23 45 In disulfide HMGB1; alternate.
{ECO:0000250|UniProtKB:P63159}.
CONFLICT 23 23 C -> S (in Ref. 5; AA sequence).
{ECO:0000305}.
CONFLICT 106 106 C -> A (in Ref. 5; AA sequence).
{ECO:0000305}.
CONFLICT 116 120 EHPGL -> PGGGV (in Ref. 4; AAA30567).
{ECO:0000305}.
CONFLICT 194 194 E -> D (in Ref. 5; AA sequence).
{ECO:0000305}.
SEQUENCE 215 AA; 24908 MW; 8BC38CF277D417B5 CRC64;
MGKGDPKKPR GKMSSYAFFV QTCREEHKKK HPDASVNFSE FSKKCSERWK TMSAKEKGKF
EDMAKADKAR YEREMKTYIP PKGETKKKFK DPNAPKRPPS AFFLFCSEYR PKIKGEHPGL
SIGDVAKKLG EMWNNTAADD KQPYEKKAAK LKEKYEKDIA AYRAKGKPDA AKKGVVKAEK
SKKKKEEEED EEDEEDEEEE EDEEDEEEEE DDDDE


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