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High mobility group protein B2 (High mobility group protein 2) (HMG-2)

 HMGB2_MOUSE             Reviewed;         210 AA.
P30681; Q3UXT1; Q9EQD5;
01-APR-1993, integrated into UniProtKB/Swiss-Prot.
23-JAN-2007, sequence version 3.
25-OCT-2017, entry version 157.
RecName: Full=High mobility group protein B2;
AltName: Full=High mobility group protein 2;
Short=HMG-2;
Name=Hmgb2; Synonyms=Hmg2;
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=PCC4;
PubMed=1408807; DOI=10.1093/nar/20.18.4927;
Stolzenburg F., Dinkl E., Grummt F.;
"Nucleotide sequence of a mouse cDNA encoding the non-histone
chromosomal high mobility group protein-2 (HMG-2).";
Nucleic Acids Res. 20:4927-4927(1992).
[2]
SEQUENCE REVISION.
Stolzenburg F.;
Submitted (SEP-1992) to the EMBL/GenBank/DDBJ databases.
[3]
NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND INTERACTION WITH POU2F2;
POU2F1 AND POU3F1.
PubMed=7720710;
Zwilling S., Koenig H., Wirth T.;
"High mobility group protein 2 functionally interacts with the POU
domains of octamer transcription factors.";
EMBO J. 14:1198-1208(1995).
[4]
NUCLEOTIDE SEQUENCE, FUNCTION, TISSUE SPECIFICITY, AND DISRUPTION
PHENOTYPE.
STRAIN=129/Sv;
PubMed=11262228;
Ronfani L., Ferraguti M., Croci L., Ovitt C.E., Schoeler H.R.,
Consalez G.G., Bianchi M.E.;
"Reduced fertility and spermatogenesis defects in mice lacking
chromosomal protein Hmgb2.";
Development 128:1265-1273(2001).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=C57BL/6J, and DBA/2J;
TISSUE=Small intestine, and Wolffian duct;
PubMed=16141072; DOI=10.1126/science.1112014;
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
Hayashizaki Y.;
"The transcriptional landscape of the mammalian genome.";
Science 309:1559-1563(2005).
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=C57BL/6J, and FVB/N; TISSUE=Brain, and Mammary gland;
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).
[7]
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).
[8]
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).
[9]
FUNCTION, INTERACTION WITH LEF1, AND TISSUE SPECIFICITY.
PubMed=19805379; DOI=10.1073/pnas.0904414106;
Taniguchi N., Carames B., Kawakami Y., Amendt B.A., Komiya S.,
Lotz M.;
"Chromatin protein HMGB2 regulates articular cartilage surface
maintenance via beta-catenin pathway.";
Proc. Natl. Acad. Sci. U.S.A. 106:16817-16822(2009).
[10]
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).
[11]
ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-30 AND LYS-114, 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).
[12]
FUNCTION.
PubMed=24391977; DOI=10.1371/journal.pone.0084838;
Abraham A.B., Bronstein R., Reddy A.S., Maletic-Savatic M.,
Aguirre A., Tsirka S.E.;
"Aberrant neural stem cell proliferation and increased adult
neurogenesis in mice lacking chromatin protein HMGB2.";
PLoS ONE 8:E84838-E84838(2013).
[13]
FUNCTION.
PubMed=23495099; DOI=10.1002/stem.1365;
Campbell P.A., Rudnicki M.A.;
"Oct4 interaction with Hmgb2 regulates Akt signaling and
pluripotency.";
Stem Cells 31:1107-1120(2013).
[14]
FUNCTION.
PubMed=25306442; DOI=10.1038/nchembio.1669;
Lee S., Nam Y., Koo J.Y., Lim D., Park J., Ock J., Kim J., Suk K.,
Park S.B.;
"A small molecule binding HMGB1 and HMGB2 inhibits microglia-mediated
neuroinflammation.";
Nat. Chem. Biol. 10:1055-1060(2014).
-!- FUNCTION: Multifunctional protein with various roles in different
cellular compartments. May act in a redox sensitive manner. In the
nucleus is an abundant chromatin-associated non-histone protein
involved in transcription, chromatin remodeling and V(D)J
recombination and probably other processes. Binds DNA with a
preference to non-canonical DNA structures such as single-stranded
DNA. 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 (By
similarity). Involved in V(D)J recombination by acting as a
cofactor of the RAG complex: acts by stimulating cleavage and RAG
protein binding at the 23 bp spacer of conserved recombination
signal sequences (RSS) (PubMed:9184213). Proposed to be involved
in the innate immune response to nucleic acids by acting as a
cytoplasmic promiscuous immunogenic DNA/RNA sensor which
cooperates with subsequent discriminative sensing by specific
pattern recognition receptors (PubMed:19890330). In the
extracellular compartment acts as a chemokine. Promotes
proliferation and migration of endothelial cells implicating
AGER/RAGE (By similarity). Has antimicrobial activity in
gastrointestinal epithelial tissues (By similarity). Involved in
inflammatory response to antigenic stimulus coupled with
proinflammatory activity (PubMed:25306442). May play a role in
germ cell differentiation (PubMed:11262228). Involved in
modulation of neurogenesis probably by regulation of neural stem
proliferation (PubMed:24391977). Involved in articular cartilage
surface maintenance implicating LEF1 and the Wnt/beta-catenin
pathway (PubMed:19805379). {ECO:0000250|UniProtKB:P09429,
ECO:0000250|UniProtKB:P26583, ECO:0000269|PubMed:19805379,
ECO:0000269|PubMed:19890330, ECO:0000269|PubMed:23495099,
ECO:0000269|PubMed:24391977, ECO:0000269|PubMed:25306442,
ECO:0000269|PubMed:9184213, ECO:0000305|PubMed:11262228}.
-!- SUBUNIT: Interacts with POU2F2, POU2F1 and POU3F1
(PubMed:7720710). Component of the RAG complex composed of core
components RAG1 and RAG2, and associated component HMGB1 or HMGB2
(PubMed:9184213). Component of the SET complex, composed of at
least ANP32A, APEX1, HMGB2, NME1, SET and TREX1. Directly
interacts with SET (By similarity). Interacts with LEF1
(PubMed:19805379). {ECO:0000250|UniProtKB:P26583,
ECO:0000269|PubMed:19805379, ECO:0000269|PubMed:7720710,
ECO:0000269|PubMed:9184213}.
-!- INTERACTION:
P27782:Lef1; NbExp=2; IntAct=EBI-6910056, EBI-984464;
-!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:P09429}.
Chromosome {ECO:0000250|UniProtKB:P26583}. Cytoplasm
{ECO:0000269|PubMed:19890330}. Secreted
{ECO:0000250|UniProtKB:P26583}.
-!- TISSUE SPECIFICITY: Widely expressed in embryo. In adult mainly
expressed in lymphoid organs and testes (PubMed:11262228).
Expressed in primary spermatocytes. Expressed in the superficial
zone of articular cartilage (PubMed:19805379).
{ECO:0000269|PubMed:11262228, ECO:0000269|PubMed:19805379}.
-!- DOMAIN: Both, HMG box 1 and HMG box 2, show antimicrobial
activity. {ECO:0000250|UniProtKB:P26583}.
-!- 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 HMGB2 (HMGB2C23hC45hC106h), 2- disulfide HMGB2 (HMGB2C23-
C45C106h) and 3- sulfonyl HMGB2 (HMGB2C23soC45soC106so).
{ECO:0000250|UniProtKB:P09429}.
-!- DISRUPTION PHENOTYPE: Viable, with severe reduction of sperm
production in males. {ECO:0000269|PubMed:11262228}.
-!- SIMILARITY: Belongs to the HMGB family. {ECO:0000305}.
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EMBL; X67668; CAA47900.1; -; mRNA.
EMBL; Z46757; CAA86727.1; -; mRNA.
EMBL; AF267733; AAG36939.1; -; Genomic_DNA.
EMBL; AK003773; BAB22988.1; -; mRNA.
EMBL; AK008443; BAB25672.1; -; mRNA.
EMBL; AK012568; BAB28323.1; -; mRNA.
EMBL; AK135296; BAE22481.1; -; mRNA.
EMBL; AK135297; BAE22482.1; -; mRNA.
EMBL; AK146212; BAE26982.1; -; mRNA.
EMBL; BC002050; AAH02050.1; -; mRNA.
EMBL; BC046759; AAH46759.1; -; mRNA.
EMBL; BC083108; AAH83108.1; -; mRNA.
CCDS; CCDS40343.1; -.
PIR; S26062; S26062.
PIR; S54774; S54774.
RefSeq; NP_032278.1; NM_008252.3.
RefSeq; XP_006509587.1; XM_006509524.2.
UniGene; Mm.276881; -.
UniGene; Mm.279998; -.
ProteinModelPortal; P30681; -.
SMR; P30681; -.
BioGrid; 220633; 3.
DIP; DIP-899N; -.
IntAct; P30681; 7.
MINT; MINT-4097539; -.
STRING; 10090.ENSMUSP00000065940; -.
iPTMnet; P30681; -.
PhosphoSitePlus; P30681; -.
SwissPalm; P30681; -.
EPD; P30681; -.
MaxQB; P30681; -.
PaxDb; P30681; -.
PeptideAtlas; P30681; -.
PRIDE; P30681; -.
Ensembl; ENSMUST00000067925; ENSMUSP00000065940; ENSMUSG00000054717.
GeneID; 97165; -.
KEGG; mmu:97165; -.
UCSC; uc009lsx.2; mouse.
CTD; 3148; -.
MGI; MGI:96157; Hmgb2.
eggNOG; KOG0381; Eukaryota.
eggNOG; COG5648; LUCA.
GeneTree; ENSGT00760000119164; -.
HOGENOM; HOG000197861; -.
HOVERGEN; HBG009000; -.
InParanoid; P30681; -.
KO; K11295; -.
OMA; EFTKKCA; -.
OrthoDB; EOG091G0P81; -.
PhylomeDB; P30681; -.
TreeFam; TF105371; -.
Reactome; R-MMU-211227; Activation of DNA fragmentation factor.
PRO; PR:P30681; -.
Proteomes; UP000000589; Chromosome 8.
Bgee; ENSMUSG00000054717; -.
CleanEx; MM_HMGB2; -.
ExpressionAtlas; P30681; baseline and differential.
Genevisible; P30681; MM.
GO; GO:0005623; C:cell; ISO:MGI.
GO; GO:0000793; C:condensed chromosome; ISS:UniProtKB.
GO; GO:0005737; C:cytoplasm; IDA:AgBase.
GO; GO:0005615; C:extracellular space; IDA:AgBase.
GO; GO:0000790; C:nuclear chromatin; IDA:AgBase.
GO; GO:0005730; C:nucleolus; ISO:MGI.
GO; GO:0005634; C:nucleus; IDA:AgBase.
GO; GO:0048471; C:perinuclear region of cytoplasm; ISS:UniProtKB.
GO; GO:0043234; C:protein complex; ISO:MGI.
GO; GO:0042056; F:chemoattractant activity; ISO:MGI.
GO; GO:0003684; F:damaged DNA binding; ISO:MGI.
GO; GO:0003677; F:DNA binding; ISS:AgBase.
GO; GO:0008301; F:DNA binding, bending; ISS:UniProtKB.
GO; GO:0003690; F:double-stranded DNA binding; IDA:UniProtKB.
GO; GO:0001158; F:enhancer sequence-specific DNA binding; IDA:AgBase.
GO; GO:0044378; F:non-sequence-specific DNA binding, bending; ISS:AgBase.
GO; GO:0019904; F:protein domain specific binding; IPI:MGI.
GO; GO:0050786; F:RAGE receptor binding; ISO:MGI.
GO; GO:0003723; F:RNA binding; ISO:MGI.
GO; GO:0097100; F:supercoiled DNA binding; ISS:AgBase.
GO; GO:0003700; F:transcription factor activity, sequence-specific DNA binding; ISO:MGI.
GO; GO:0008134; F:transcription factor binding; IDA:AgBase.
GO; GO:0044212; F:transcription regulatory region DNA binding; ISO:MGI.
GO; GO:0060326; P:cell chemotaxis; ISO:MGI.
GO; GO:0071222; P:cellular response to lipopolysaccharide; IEA:Ensembl.
GO; GO:0050829; P:defense response to Gram-negative bacterium; ISS:AgBase.
GO; GO:0050830; P:defense response to Gram-positive bacterium; ISS:AgBase.
GO; GO:0006310; P:DNA recombination; IEA:UniProtKB-KW.
GO; GO:0006265; P:DNA topological change; ISS:AgBase.
GO; GO:0002437; P:inflammatory response to antigenic stimulus; IMP:AgBase.
GO; GO:0045087; P:innate immune response; IEA:UniProtKB-KW.
GO; GO:0008584; P:male gonad development; IMP:MGI.
GO; GO:1902042; P:negative regulation of extrinsic apoptotic signaling pathway via death domain receptors; IMP:MGI.
GO; GO:0010629; P:negative regulation of gene expression; IDA:AgBase.
GO; GO:0045892; P:negative regulation of transcription, DNA-templated; ISO:MGI.
GO; GO:0043388; P:positive regulation of DNA binding; IDA:MGI.
GO; GO:0001938; P:positive regulation of endothelial cell proliferation; ISO:MGI.
GO; GO:0045648; P:positive regulation of erythrocyte differentiation; ISO:MGI.
GO; GO:0010628; P:positive regulation of gene expression; IDA:AgBase.
GO; GO:0045089; P:positive regulation of innate immune response; IMP:UniProtKB.
GO; GO:0032728; P:positive regulation of interferon-beta production; IMP:UniProtKB.
GO; GO:0045654; P:positive regulation of megakaryocyte differentiation; ISO:MGI.
GO; GO:0032075; P:positive regulation of nuclease activity; ISO:MGI.
GO; GO:0045944; P:positive regulation of transcription from RNA polymerase II promoter; IMP:MGI.
GO; GO:0045893; P:positive regulation of transcription, DNA-templated; ISO:MGI.
GO; GO:0050767; P:regulation of neurogenesis; IMP:AgBase.
GO; GO:0072091; P:regulation of stem cell proliferation; IMP:AgBase.
GO; GO:0006357; P:regulation of transcription from RNA polymerase II promoter; IDA:MGI.
GO; GO:0032496; P:response to lipopolysaccharide; IMP:AgBase.
GO; GO:0048545; P:response to steroid hormone; IMP:MGI.
GO; GO:0007289; P:spermatid nucleus differentiation; IMP:MGI.
GO; GO:0007283; P:spermatogenesis; IMP:MGI.
GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-KW.
Gene3D; 1.10.30.10; -; 2.
InterPro; IPR009071; HMG_box_dom.
InterPro; IPR036910; HMG_box_dom_sf.
InterPro; IPR017967; HMG_boxA_CS.
InterPro; IPR031075; HMGB2.
PANTHER; PTHR13711:SF181; PTHR13711:SF181; 1.
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; Chemotaxis; Chromosome; Complete proteome; Cytoplasm;
Disulfide bond; DNA recombination; DNA-binding; Immunity;
Inflammatory response; Innate immunity; Nucleus; Oxidation;
Phosphoprotein; Reference proteome; Repeat; Secreted; Transcription;
Transcription regulation.
CHAIN 1 210 High mobility group protein B2.
/FTId=PRO_0000048535.
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 165 180 Required for chemotactic activity.
{ECO:0000250|UniProtKB:P26583}.
COMPBIAS 186 210 Asp/Glu-rich (acidic).
MOD_RES 3 3 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:P26583}.
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 114 114 N6-acetyllysine.
{ECO:0000244|PubMed:23806337}.
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 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}.
DISULFID 23 45 In disulfide HMGB2; alternate.
{ECO:0000250|UniProtKB:P63159}.
CONFLICT 7 7 N -> I (in Ref. 1; CAA47900).
{ECO:0000305}.
CONFLICT 10 10 R -> L (in Ref. 1; CAA47900).
{ECO:0000305}.
CONFLICT 33 33 D -> N (in Ref. 1; CAA47900).
{ECO:0000305}.
CONFLICT 41 41 F -> I (in Ref. 1; CAA47900).
{ECO:0000305}.
CONFLICT 47 47 E -> K (in Ref. 1; CAA47900).
{ECO:0000305}.
CONFLICT 57 57 K -> N (in Ref. 1; CAA47900).
{ECO:0000305}.
CONFLICT 70 72 RYD -> CYY (in Ref. 1; CAA47900).
{ECO:0000305}.
CONFLICT 80 80 P -> S (in Ref. 1; CAA47900).
{ECO:0000305}.
CONFLICT 103 103 F -> C (in Ref. 1; CAA47900).
{ECO:0000305}.
CONFLICT 117 117 H -> Y (in Ref. 1; CAA47900).
{ECO:0000305}.
CONFLICT 140 140 D -> E (in Ref. 1; CAA47900).
{ECO:0000305}.
CONFLICT 159 159 I -> F (in Ref. 1; CAA47900).
{ECO:0000305}.
CONFLICT 164 164 A -> V (in Ref. 1; CAA47900).
{ECO:0000305}.
CONFLICT 179 179 T -> A (in Ref. 1; CAA47900).
{ECO:0000305}.
CONFLICT 184 193 KNEPEDEEEE -> NDSED (in Ref. 1;
CAA47900). {ECO:0000305}.
CONFLICT 202 202 D -> E (in Ref. 1; CAA47900, 4; AAG36939
and 6; AAH02050). {ECO:0000305}.
CONFLICT 204 204 E -> G (in Ref. 1; CAA47900).
{ECO:0000305}.
SEQUENCE 210 AA; 24162 MW; 45D1F667DB4ED94D CRC64;
MGKGDPNKPR GKMSSYAFFV QTCREEHKKK HPDSSVNFAE FSKKCSERWK TMSAKEKSKF
EDLAKSDKAR YDREMKNYVP PKGDKKGKKK DPNAPKRPPS AFFLFCSENR PKIKIEHPGL
SIGDTAKKLG EMWSEQSAKD KQPYEQKAAK LKEKYEKDIA AYRAKGKSEA GKKGPGRPTG
SKKKNEPEDE EEEEEEEEEE DDEEEEEDEE


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