HMGB1_PAPAN
ID HMGB1_PAPAN Reviewed; 215 AA.
AC A9RA84;
DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT 05-FEB-2008, sequence version 1.
DT 03-AUG-2022, entry version 87.
DE RecName: Full=High mobility group protein B1;
DE AltName: Full=High mobility group protein 1;
DE Short=HMG-1;
GN Name=HMGB1;
OS Papio anubis (Olive baboon).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC Cercopithecidae; Cercopithecinae; Papio.
OX NCBI_TaxID=9555;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Antonellis A., Benjamin B., Blakesley R.W., Bouffard G.G., Brinkley C.,
RA Brooks S., Chu G., Chub I., Coleman H., Fuksenko T., Gestole M.,
RA Gregory M., Guan X., Gupta J., Gurson N., Han E., Han J., Hansen N.,
RA Hargrove A., Hines-Harris K., Ho S.-L., Hu P., Hunter G., Hurle B.,
RA Idol J.R., Johnson T., Knight E., Kwong P., Lee-Lin S.-Q., Legaspi R.,
RA Madden M., Maduro Q.L., Maduro V.B., Margulies E.H., Masiello C.,
RA Maskeri B., McDowell J., Merkulov G., Montemayor C., Mullikin J.C.,
RA Park M., Prasad A., Ramsahoye C., Reddix-Dugue N., Riebow N., Schandler K.,
RA Schueler M.G., Sison C., Smith L., Stantripop S., Thomas J.W., Thomas P.J.,
RA Tsipouri V., Young A., Green E.D.;
RT "NISC comparative sequencing initiative.";
RL Submitted (DEC-2007) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Multifunctional redox sensitive protein with various roles in
CC different cellular compartments. In the nucleus is one of the major
CC chromatin-associated non-histone proteins and acts as a DNA chaperone
CC involved in replication, transcription, chromatin remodeling, V(D)J
CC recombination, DNA repair and genome stability. Proposed to be an
CC universal biosensor for nucleic acids. Promotes host inflammatory
CC response to sterile and infectious signals and is involved in the
CC coordination and integration of innate and adaptive immune responses.
CC In the cytoplasm functions as sensor and/or chaperone for immunogenic
CC nucleic acids implicating the activation of TLR9-mediated immune
CC responses, and mediates autophagy. Acts as danger associated molecular
CC pattern (DAMP) molecule that amplifies immune responses during tissue
CC injury. Released to the extracellular environment can bind DNA,
CC nucleosomes, IL-1 beta, CXCL12, AGER isoform 2/sRAGE,
CC lipopolysaccharide (LPS) and lipoteichoic acid (LTA), and activates
CC cells through engagement of multiple surface receptors. In the
CC extracellular compartment fully reduced HMGB1 (released by necrosis)
CC acts as a chemokine, disulfide HMGB1 (actively secreted) as a cytokine,
CC and sulfonyl HMGB1 (released from apoptotic cells) promotes
CC immunological tolerance. Has proangiogenic activity. May be involved in
CC platelet activation. Binds to phosphatidylserine and
CC phosphatidylethanolamide. Bound to RAGE mediates signaling for neuronal
CC outgrowth. May play a role in accumulation of expanded polyglutamine
CC (polyQ) proteins. {ECO:0000250|UniProtKB:P09429,
CC ECO:0000250|UniProtKB:P10103, ECO:0000250|UniProtKB:P63159}.
CC -!- FUNCTION: Nuclear functions are attributed to fully reduced HGMB1.
CC Associates with chromatin and binds DNA with a preference to non-
CC canonical DNA structures such as single-stranded DNA, DNA-containing
CC cruciforms or bent structures, supercoiled DNA and ZDNA. Can bent DNA
CC and enhance DNA flexibility by looping thus providing a mechanism to
CC promote activities on various gene promoters by enhancing transcription
CC factor binding and/or bringing distant regulatory sequences into close
CC proximity. May be involved in nucleotide excision repair (NER),
CC mismatch repair (MMR) and base excision repair (BER) pathways, and
CC double strand break repair such as non-homologous end joining (NHEJ).
CC Involved in V(D)J recombination by acting as a cofactor of the RAG
CC complex: acts by stimulating cleavage and RAG protein binding at the 23
CC bp spacer of conserved recombination signal sequences (RSS). In vitro
CC can displace histone H1 from highly bent DNA. Can restructure the
CC canonical nucleosome leading to relaxation of structural constraints
CC for transcription factor-binding. Enhances binding of sterol regulatory
CC element-binding proteins (SREBPs) such as SREBF1 to their cognate DNA
CC sequences and increases their transcriptional activities. Facilitates
CC binding of TP53 to DNA. May be involved in mitochondrial quality
CC control and autophagy in a transcription-dependent fashion implicating
CC HSPB1. Can modulate the activity of the telomerase complex and may be
CC involved in telomere maintenance. {ECO:0000250|UniProtKB:P09429,
CC ECO:0000250|UniProtKB:P10103, ECO:0000250|UniProtKB:P63158,
CC ECO:0000250|UniProtKB:P63159}.
CC -!- FUNCTION: In the cytoplasm proposed to dissociate the BECN1:BCL2
CC complex via competitive interaction with BECN1 leading to autophagy
CC activation. Can protect BECN1 and ATG5 from calpain-mediated cleavage
CC and thus proposed to control their proautophagic and proapoptotic
CC functions and to regulate the extent and severity of inflammation-
CC associated cellular injury. In myeloid cells has a protective role
CC against endotoxemia and bacterial infection by promoting autophagy.
CC Involved in endosomal translocation and activation of TLR9 in response
CC to CpG-DNA in macrophages. {ECO:0000250|UniProtKB:P09429,
CC ECO:0000250|UniProtKB:P63158}.
CC -!- FUNCTION: In the extracellular compartment (following either active
CC secretion or passive release) involved in regulation of the
CC inflammatory response. Fully reduced HGMB1 (which subsequently gets
CC oxidized after release) in association with CXCL12 mediates the
CC recruitment of inflammatory cells during the initial phase of tissue
CC injury; the CXCL12:HMGB1 complex triggers CXCR4 homodimerization.
CC Induces the migration of monocyte-derived immature dendritic cells and
CC seems to regulate adhesive and migratory functions of neutrophils
CC implicating AGER/RAGE and ITGAM. Can bind to various types of DNA and
CC RNA including microbial unmethylated CpG-DNA to enhance the innate
CC immune response to nucleic acids. Proposed to act in promiscuous
CC DNA/RNA sensing which cooperates with subsequent discriminative sensing
CC by specific pattern recognition receptors. Promotes extracellular DNA-
CC induced AIM2 inflammasome activation implicating AGER/RAGE. Disulfide
CC HMGB1 binds to transmembrane receptors, such as AGER/RAGE, TLR2, TLR4
CC and probably TREM1, thus activating their signal transduction pathways.
CC Mediates the release of cytokines/chemokines such as TNF, IL-1, IL-6,
CC IL-8, CCL2, CCL3, CCL4 and CXCL10. Promotes secretion of interferon-
CC gamma by macrophage-stimulated natural killer (NK) cells in concert
CC with other cytokines like IL-2 or IL-12. TLR4 is proposed to be the
CC primary receptor promoting macrophage activation and signaling through
CC TLR4 seems to implicate LY96/MD-2. In bacterial LPS- or LTA-mediated
CC inflammatory responses binds to the endotoxins and transfers them to
CC CD14 for signaling to the respective TLR4:LY96 and TLR2 complexes.
CC Contributes to tumor proliferation by association with ACER/RAGE. Can
CC bind to IL1-beta and signals through the IL1R1:IL1RAP receptor complex.
CC Binding to class A CpG activates cytokine production in plasmacytoid
CC dendritic cells implicating TLR9, MYD88 and AGER/RAGE and can activate
CC autoreactive B cells. Via HMGB1-containing chromatin immune complexes
CC may also promote B cell responses to endogenous TLR9 ligands through a
CC B-cell receptor (BCR)-dependent and ACER/RAGE-independent mechanism.
CC Inhibits phagocytosis of apoptotic cells by macrophages; the function
CC is dependent on poly-ADP-ribosylation and involves binding to
CC phosphatidylserine on the cell surface of apoptotic cells. In adaptive
CC immunity may be involved in enhancing immunity through activation of
CC effector T-cells and suppression of regulatory T (TReg) cells. In
CC contrast, without implicating effector or regulatory T-cells, required
CC for tumor infiltration and activation of T-cells expressing the
CC lymphotoxin LTA:LTB heterotrimer thus promoting tumor malignant
CC progression. Also reported to limit proliferation of T-cells. Released
CC HMGB1:nucleosome complexes formed during apoptosis can signal through
CC TLR2 to induce cytokine production. Involved in induction of
CC immunological tolerance by apoptotic cells; its pro-inflammatory
CC activities when released by apoptotic cells are neutralized by reactive
CC oxygen species (ROS)-dependent oxidation specifically on Cys-106.
CC During macrophage activation by activated lymphocyte-derived self
CC apoptotic DNA (ALD-DNA) promotes recruitment of ALD-DNA to endosomes.
CC {ECO:0000250|UniProtKB:P09429, ECO:0000250|UniProtKB:P10103,
CC ECO:0000250|UniProtKB:P63158, ECO:0000250|UniProtKB:P63159}.
CC -!- SUBUNIT: Interacts (fully reduced HMGB1) with CXCL12; probably in a 1:2
CC ratio involving two molecules of CXCL12, each interacting with one HMG
CC box of HMGB1; inhibited by Glycyrrhizin. Associates with the TLR4:LY96
CC receptor complex. Component of the RAG complex composed of core
CC components RAG1 and RAG2, and associated component HMGB1 or HMGB2.
CC Interacts (in cytoplasm upon starvation) with BECN1; inhibits the
CC interaction of BECN1 and BCL2 leading to promotion of autophagy.
CC Interacts with KPNA1; involved in nuclear import. Interacts with
CC SREBF1, TLR2, TLR4, TLR9, PTPRZ1, APEX1, FEN1, POLB, TERT. Interacts
CC with IL1B, AGER, MSH2, XPA, XPC, HNF1A, TP53. Interacts with CD24; the
CC probable CD24:SIGLEC10 complex is proposed to inhibit HGMB1-mediated
CC tissue damage immune response. Interacts with THBD; prevents HGMB1
CC interaction with ACER/RAGE and inhibits HGMB1 pro-inflammatory
CC activity. Interacts with HAVCR2; impairs HMGB1 binding to B-DNA and
CC likely HMGB1-mediated innate immune response. Interacts with XPO1;
CC mediating nuclear export. {ECO:0000250|UniProtKB:P09429,
CC ECO:0000250|UniProtKB:P63158, ECO:0000250|UniProtKB:P63159}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:P09429}.
CC Chromosome {ECO:0000250|UniProtKB:P10103,
CC ECO:0000250|UniProtKB:P63159}. Cytoplasm
CC {ECO:0000250|UniProtKB:P09429}. Secreted {ECO:0000250|UniProtKB:P09429,
CC ECO:0000250|UniProtKB:P63158}. Cell membrane
CC {ECO:0000250|UniProtKB:P09429, ECO:0000250|UniProtKB:P63158,
CC ECO:0000250|UniProtKB:P63159}; Peripheral membrane protein
CC {ECO:0000250|UniProtKB:P09429, ECO:0000250|UniProtKB:P63158,
CC ECO:0000250|UniProtKB:P63159}; Extracellular side
CC {ECO:0000250|UniProtKB:P09429, ECO:0000250|UniProtKB:P63158,
CC ECO:0000250|UniProtKB:P63159}. Endosome {ECO:0000250|UniProtKB:P63158}.
CC Endoplasmic reticulum-Golgi intermediate compartment
CC {ECO:0000250|UniProtKB:P63158}. Note=In basal state predominantly
CC nuclear. Shuttles between the cytoplasm and the nucleus. Translocates
CC from the nucleus to the cytoplasm upon autophagy stimulation. Release
CC from macrophages in the extracellular milieu requires the activation of
CC NLRC4 or NLRP3 inflammasomes (By similarity). Passively released to the
CC extracellular milieu from necrotic cells by diffusion, involving the
CC fully reduced HGMB1 which subsequently gets oxidized. Also released
CC from apoptotic cells. Active secretion from a variety of immune and
CC non-immune cells such as macrophages, monocytes, neutrophils, dendritic
CC cells, natural killer cells and plasma cells in response to various
CC stimuli such as LPS and cytokines involves a nonconventional secretory
CC process via secretory lysosomes. Found on the surface of activated
CC platelets. {ECO:0000250|UniProtKB:P09429,
CC ECO:0000250|UniProtKB:P63158}.
CC -!- DOMAIN: HMG box 2 mediates pro-inflammatory cytokine-stimulating
CC activity and binding to TLR4. However, not involved in mediating
CC immunogenic activity in the context of apoptosis-induced immune
CC tolerance. {ECO:0000250|UniProtKB:P09429}.
CC -!- DOMAIN: The acidic C-terminal domain forms a flexible structure which
CC can reversibly interact intramolecularily with the HMG boxes and
CC modulate binding to DNA and other proteins.
CC {ECO:0000250|UniProtKB:P09429, ECO:0000250|UniProtKB:P63159}.
CC -!- PTM: Phosphorylated at serine residues. Phosphorylation in both NLS
CC regions is required for cytoplasmic translocation followed by
CC secretion. {ECO:0000250|UniProtKB:P09429}.
CC -!- PTM: Acetylated on multiple sites upon stimulation with LPS (By
CC similarity). Acetylation on lysine residues in the nuclear localization
CC signals (NLS 1 and NLS 2) leads to cytoplasmic localization and
CC subsequent secretion. Acetylation on Lys-3 results in preferential
CC binding to DNA ends and impairs DNA bending activity (By similarity).
CC {ECO:0000250|UniProtKB:P09429, ECO:0000250|UniProtKB:P10103,
CC ECO:0000250|UniProtKB:P63159}.
CC -!- PTM: Reduction/oxidation of cysteine residues Cys-23, Cys-45 and Cys-
CC 106 and a possible intramolecular disulfide bond involving Cys-23 and
CC Cys-45 give rise to different redox forms with specific functional
CC activities in various cellular compartments: 1- fully reduced HMGB1
CC (HMGB1C23hC45hC106h), 2- disulfide HMGB1 (HMGB1C23-C45C106h) and
CC 3- sulfonyl HMGB1 (HMGB1C23soC45soC106so).
CC {ECO:0000250|UniProtKB:P09429}.
CC -!- PTM: Poly-ADP-ribosylated by PARP1 when secreted following stimulation
CC with LPS (By similarity). {ECO:0000250|UniProtKB:P63158}.
CC -!- PTM: In vitro cleavage by CASP1 is liberating a HMG box 1-containing
CC peptide which may mediate immunogenic activity; the peptide antagonizes
CC apoptosis-induced immune tolerance. Can be proteolytically cleaved by a
CC thrombin:thrombomodulin complex; reduces binding to heparin and pro-
CC inflammatory activities (By similarity). {ECO:0000250|UniProtKB:P09429,
CC ECO:0000250|UniProtKB:P10103}.
CC -!- PTM: Forms covalent cross-links mediated by transglutaminase TGM2,
CC between a glutamine and the epsilon-amino group of a lysine residue,
CC forming homopolymers and heteropolymers.
CC {ECO:0000250|UniProtKB:P09429}.
CC -!- SIMILARITY: Belongs to the HMGB family. {ECO:0000305}.
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DR EMBL; DP000511; ABX89266.1; -; Genomic_DNA.
DR RefSeq; NP_001162380.1; NM_001168909.1.
DR RefSeq; XP_009189984.1; XM_009191720.1.
DR RefSeq; XP_009189985.1; XM_009191721.2.
DR RefSeq; XP_009189986.1; XM_009191722.1.
DR AlphaFoldDB; A9RA84; -.
DR BMRB; A9RA84; -.
DR SMR; A9RA84; -.
DR STRING; 9555.ENSPANP00000006640; -.
DR Ensembl; ENSPANT00000005593; ENSPANP00000013674; ENSPANG00000011105.
DR GeneID; 100137373; -.
DR KEGG; panu:100137373; -.
DR CTD; 3146; -.
DR eggNOG; KOG0381; Eukaryota.
DR GeneTree; ENSGT00950000183120; -.
DR HOGENOM; CLU_082854_0_0_1; -.
DR OMA; CREEHTK; -.
DR OrthoDB; 1641977at2759; -.
DR Proteomes; UP000028761; Chromosome 6.
DR Bgee; ENSPANG00000007200; Expressed in duodenum and 66 other tissues.
DR ExpressionAtlas; A9RA84; baseline.
DR GO; GO:0005694; C:chromosome; IEA:UniProtKB-SubCell.
DR GO; GO:0005793; C:endoplasmic reticulum-Golgi intermediate compartment; IEA:UniProtKB-SubCell.
DR GO; GO:0005768; C:endosome; IEA:UniProtKB-SubCell.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0000405; F:bubble DNA binding; ISS:AgBase.
DR GO; GO:0008301; F:DNA binding, bending; ISS:AgBase.
DR GO; GO:0000400; F:four-way junction DNA binding; ISS:AgBase.
DR GO; GO:0097100; F:supercoiled DNA binding; ISS:AgBase.
DR GO; GO:0002250; P:adaptive immune response; IEA:UniProtKB-KW.
DR GO; GO:0006914; P:autophagy; IEA:UniProtKB-KW.
DR GO; GO:0006935; P:chemotaxis; IEA:UniProtKB-KW.
DR GO; GO:0032392; P:DNA geometric change; ISS:AgBase.
DR GO; GO:0006310; P:DNA recombination; IEA:UniProtKB-KW.
DR GO; GO:0006281; P:DNA repair; IEA:UniProtKB-KW.
DR GO; GO:0006954; P:inflammatory response; IEA:UniProtKB-KW.
DR GO; GO:0045087; P:innate immune response; IEA:UniProtKB-KW.
DR GO; GO:0048584; P:positive regulation of response to stimulus; IEA:UniProt.
DR Gene3D; 1.10.30.10; -; 2.
DR InterPro; IPR009071; HMG_box_dom.
DR InterPro; IPR036910; HMG_box_dom_sf.
DR InterPro; IPR017967; HMG_boxA_CS.
DR InterPro; IPR031076; HMGB1.
DR PANTHER; PTHR48112:SF4; PTHR48112:SF4; 1.
DR Pfam; PF00505; HMG_box; 1.
DR Pfam; PF09011; HMG_box_2; 1.
DR SMART; SM00398; HMG; 2.
DR SUPFAM; SSF47095; SSF47095; 2.
DR PROSITE; PS00353; HMG_BOX_1; 1.
DR PROSITE; PS50118; HMG_BOX_2; 2.
PE 3: Inferred from homology;
KW Acetylation; Adaptive immunity; ADP-ribosylation; Autophagy; Cell membrane;
KW Chemotaxis; Chromosome; Cytoplasm; Disulfide bond; DNA damage;
KW DNA recombination; DNA repair; DNA-binding; Endosome; Immunity;
KW Inflammatory response; Innate immunity; Isopeptide bond; Membrane; Nucleus;
KW Oxidation; Phosphoprotein; Reference proteome; Repeat; Secreted.
FT CHAIN 1..215
FT /note="High mobility group protein B1"
FT /id="PRO_0000333885"
FT DNA_BIND 9..79
FT /note="HMG box 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00267"
FT DNA_BIND 95..163
FT /note="HMG box 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00267"
FT REGION 1..97
FT /note="Sufficient for interaction with HAVCR2"
FT /evidence="ECO:0000250|UniProtKB:P63158"
FT REGION 3..15
FT /note="LPS binding (delipidated)"
FT /evidence="ECO:0000250|UniProtKB:P09429"
FT REGION 27..43
FT /note="NLS 1"
FT /evidence="ECO:0000250|UniProtKB:P63159"
FT REGION 76..95
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 80..96
FT /note="LPS binding (Lipid A)"
FT /evidence="ECO:0000250|UniProtKB:P09429"
FT REGION 89..108
FT /note="Cytokine-stimulating activity"
FT /evidence="ECO:0000250|UniProtKB:P09429"
FT REGION 150..183
FT /note="Binding to AGER/RAGE"
FT /evidence="ECO:0000250|UniProtKB:P63159"
FT REGION 161..215
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 178..184
FT /note="NLS 2"
FT /evidence="ECO:0000250|UniProtKB:P63159"
FT MOTIF 27..43
FT /note="Nuclear localization signal (NLS) 1"
FT /evidence="ECO:0000250|UniProtKB:P63159"
FT MOTIF 178..184
FT /note="Nuclear localization signal (NLS) 2"
FT /evidence="ECO:0000250|UniProtKB:P63159"
FT COMPBIAS 76..94
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 161..187
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 188..215
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 1..10
FT /ligand="heparin"
FT /ligand_id="ChEBI:CHEBI:28304"
FT /evidence="ECO:0000250|UniProtKB:P10103"
FT SITE 10..11
FT /note="Cleavage; by thrombin:thrombomodulin"
FT /evidence="ECO:0000250|UniProtKB:P10103"
FT SITE 67..68
FT /note="Cleavage; by CASP1"
FT /evidence="ECO:0000250|UniProtKB:P09429"
FT MOD_RES 3
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P10103"
FT MOD_RES 7
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P10103"
FT MOD_RES 8
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P10103"
FT MOD_RES 12
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P10103"
FT MOD_RES 23
FT /note="Cysteine sulfonic acid (-SO3H); alternate"
FT /evidence="ECO:0000250|UniProtKB:P63159"
FT MOD_RES 28
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P10103"
FT MOD_RES 29
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P10103"
FT MOD_RES 30
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P10103"
FT MOD_RES 35
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P09429"
FT MOD_RES 43
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P63158"
FT MOD_RES 45
FT /note="Cysteine sulfonic acid (-SO3H); alternate"
FT /evidence="ECO:0000250|UniProtKB:P63159"
FT MOD_RES 90
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P63158"
FT MOD_RES 100
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P09429"
FT MOD_RES 106
FT /note="Cysteine sulfonic acid (-SO3H)"
FT /evidence="ECO:0000250|UniProtKB:P63159"
FT MOD_RES 127
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P10103"
FT MOD_RES 128
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P10103"
FT MOD_RES 141
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P63158"
FT MOD_RES 172
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P10103"
FT MOD_RES 173
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P10103"
FT MOD_RES 177
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P10103"
FT MOD_RES 180
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P10103"
FT MOD_RES 181
FT /note="ADP-ribosylserine"
FT /evidence="ECO:0000250|UniProtKB:P09429"
FT MOD_RES 182
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P10103"
FT MOD_RES 183
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P10103"
FT MOD_RES 184
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P10103"
FT MOD_RES 185
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P10103"
FT DISULFID 23..45
FT /note="In disulfide HMGB1; alternate"
FT /evidence="ECO:0000250|UniProtKB:P63159"
FT CROSSLNK 28
FT /note="Isoglutamyl lysine isopeptide (Lys-Gln) (interchain
FT with Q-?)"
FT /evidence="ECO:0000250|UniProtKB:P09429"
FT CROSSLNK 43
FT /note="Isoglutamyl lysine isopeptide (Lys-Gln) (interchain
FT with Q-?)"
FT /evidence="ECO:0000250|UniProtKB:P09429"
FT CROSSLNK 44
FT /note="Isoglutamyl lysine isopeptide (Lys-Gln) (interchain
FT with Q-?)"
FT /evidence="ECO:0000250|UniProtKB:P09429"
FT CROSSLNK 68
FT /note="Isoglutamyl lysine isopeptide (Lys-Gln) (interchain
FT with Q-?)"
FT /evidence="ECO:0000250|UniProtKB:P09429"
FT CROSSLNK 180
FT /note="Isoglutamyl lysine isopeptide (Lys-Gln) (interchain
FT with Q-?)"
FT /evidence="ECO:0000250|UniProtKB:P09429"
FT CROSSLNK 182
FT /note="Isoglutamyl lysine isopeptide (Lys-Gln) (interchain
FT with Q-?)"
FT /evidence="ECO:0000250|UniProtKB:P09429"
FT CROSSLNK 183
FT /note="Isoglutamyl lysine isopeptide (Lys-Gln) (interchain
FT with Q-?)"
FT /evidence="ECO:0000250|UniProtKB:P09429"
FT CROSSLNK 184
FT /note="Isoglutamyl lysine isopeptide (Lys-Gln) (interchain
FT with Q-?)"
FT /evidence="ECO:0000250|UniProtKB:P09429"
SQ SEQUENCE 215 AA; 24894 MW; 8A868CF277D417B5 CRC64;
MGKGDPKKPR GKMSSYAFFV QTCREEHKKK HPDASVNFSE FSKKCSERWK TMSAKEKGKF
EDMAKADKAR YEREMKTYIP PKGETKKKFK DPNAPKRPPS AFFLFCSEYR PKIKGEHPGL
SIGDVAKKLG EMWNNTAADD KQPYEKKAAK LKEKYEKDIA AYRAKGKPDA AKKGVVKAEK
SKKKKEEEED EEDEEDEEEE EDEEDEDEEE DDDDE
