HMGB2_MOUSE
ID HMGB2_MOUSE Reviewed; 210 AA.
AC P30681; Q3UXT1; Q9EQD5;
DT 01-APR-1993, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 187.
DE RecName: Full=High mobility group protein B2;
DE AltName: Full=High mobility group protein 2;
DE Short=HMG-2;
GN Name=Hmgb2; Synonyms=Hmg2;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=PCC4;
RX PubMed=1408807; DOI=10.1093/nar/20.18.4927;
RA Stolzenburg F., Dinkl E., Grummt F.;
RT "Nucleotide sequence of a mouse cDNA encoding the non-histone chromosomal
RT high mobility group protein-2 (HMG-2).";
RL Nucleic Acids Res. 20:4927-4927(1992).
RN [2]
RP SEQUENCE REVISION.
RA Stolzenburg F.;
RL Submitted (SEP-1992) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND INTERACTION WITH POU2F2; POU2F1
RP AND POU3F1.
RX PubMed=7720710; DOI=10.1002/j.1460-2075.1995.tb07103.x;
RA Zwilling S., Koenig H., Wirth T.;
RT "High mobility group protein 2 functionally interacts with the POU domains
RT of octamer transcription factors.";
RL EMBO J. 14:1198-1208(1995).
RN [4]
RP NUCLEOTIDE SEQUENCE, FUNCTION, TISSUE SPECIFICITY, AND DISRUPTION
RP PHENOTYPE.
RC STRAIN=129/Sv;
RX PubMed=11262228; DOI=10.1242/dev.128.8.1265;
RA Ronfani L., Ferraguti M., Croci L., Ovitt C.E., Schoeler H.R.,
RA Consalez G.G., Bianchi M.E.;
RT "Reduced fertility and spermatogenesis defects in mice lacking chromosomal
RT protein Hmgb2.";
RL Development 128:1265-1273(2001).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J, and DBA/2J; TISSUE=Small intestine, and Wolffian duct;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J, and FVB/N; TISSUE=Brain, and Mammary gland;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [7]
RP FUNCTION, AND IDENTIFICATION IN THE RAG COMPLEX.
RX PubMed=9184213; DOI=10.1093/emboj/16.10.2665;
RA van Gent D.C., Hiom K., Paull T.T., Gellert M.;
RT "Stimulation of V(D)J cleavage by high mobility group proteins.";
RL EMBO J. 16:2665-2670(1997).
RN [8]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=19890330; DOI=10.1038/nature08512;
RA Yanai H., Ban T., Wang Z., Choi M.K., Kawamura T., Negishi H., Nakasato M.,
RA Lu Y., Hangai S., Koshiba R., Savitsky D., Ronfani L., Akira S.,
RA Bianchi M.E., Honda K., Tamura T., Kodama T., Taniguchi T.;
RT "HMGB proteins function as universal sentinels for nucleic-acid-mediated
RT innate immune responses.";
RL Nature 462:99-103(2009).
RN [9]
RP FUNCTION, INTERACTION WITH LEF1, AND TISSUE SPECIFICITY.
RX PubMed=19805379; DOI=10.1073/pnas.0904414106;
RA Taniguchi N., Carames B., Kawakami Y., Amendt B.A., Komiya S., Lotz M.;
RT "Chromatin protein HMGB2 regulates articular cartilage surface maintenance
RT via beta-catenin pathway.";
RL Proc. Natl. Acad. Sci. U.S.A. 106:16817-16822(2009).
RN [10]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
RC Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [11]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-30 AND LYS-114, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic fibroblast;
RX PubMed=23806337; DOI=10.1016/j.molcel.2013.06.001;
RA Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y.,
RA Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.;
RT "SIRT5-mediated lysine desuccinylation impacts diverse metabolic
RT pathways.";
RL Mol. Cell 50:919-930(2013).
RN [12]
RP FUNCTION.
RX PubMed=24391977; DOI=10.1371/journal.pone.0084838;
RA Abraham A.B., Bronstein R., Reddy A.S., Maletic-Savatic M., Aguirre A.,
RA Tsirka S.E.;
RT "Aberrant neural stem cell proliferation and increased adult neurogenesis
RT in mice lacking chromatin protein HMGB2.";
RL PLoS ONE 8:E84838-E84838(2013).
RN [13]
RP FUNCTION.
RX PubMed=23495099; DOI=10.1002/stem.1365;
RA Campbell P.A., Rudnicki M.A.;
RT "Oct4 interaction with Hmgb2 regulates Akt signaling and pluripotency.";
RL Stem Cells 31:1107-1120(2013).
RN [14]
RP FUNCTION.
RX PubMed=25306442; DOI=10.1038/nchembio.1669;
RA Lee S., Nam Y., Koo J.Y., Lim D., Park J., Ock J., Kim J., Suk K.,
RA Park S.B.;
RT "A small molecule binding HMGB1 and HMGB2 inhibits microglia-mediated
RT neuroinflammation.";
RL Nat. Chem. Biol. 10:1055-1060(2014).
CC -!- FUNCTION: Multifunctional protein with various roles in different
CC cellular compartments. May act in a redox sensitive manner. In the
CC nucleus is an abundant chromatin-associated non-histone protein
CC involved in transcription, chromatin remodeling and V(D)J recombination
CC and probably other processes. Binds DNA with a preference to non-
CC canonical DNA structures such as single-stranded DNA. Can bent DNA and
CC 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 (By similarity). Involved in V(D)J recombination by acting as
CC a cofactor of the RAG complex: acts by stimulating cleavage and RAG
CC protein binding at the 23 bp spacer of conserved recombination signal
CC sequences (RSS) (PubMed:9184213). Proposed to be involved in the innate
CC immune response to nucleic acids by acting as a cytoplasmic promiscuous
CC immunogenic DNA/RNA sensor which cooperates with subsequent
CC discriminative sensing by specific pattern recognition receptors
CC (PubMed:19890330). In the extracellular compartment acts as a
CC chemokine. Promotes proliferation and migration of endothelial cells
CC implicating AGER/RAGE (By similarity). Has antimicrobial activity in
CC gastrointestinal epithelial tissues (By similarity). Involved in
CC inflammatory response to antigenic stimulus coupled with pro-
CC inflammatory activity (PubMed:25306442). May play a role in germ cell
CC differentiation (PubMed:11262228). Involved in modulation of
CC neurogenesis probably by regulation of neural stem proliferation
CC (PubMed:24391977). Involved in articular cartilage surface maintenance
CC implicating LEF1 and the Wnt/beta-catenin pathway (PubMed:19805379).
CC {ECO:0000250|UniProtKB:P09429, ECO:0000250|UniProtKB:P26583,
CC ECO:0000269|PubMed:19805379, ECO:0000269|PubMed:19890330,
CC ECO:0000269|PubMed:23495099, ECO:0000269|PubMed:24391977,
CC ECO:0000269|PubMed:25306442, ECO:0000269|PubMed:9184213,
CC ECO:0000305|PubMed:11262228}.
CC -!- SUBUNIT: Interacts with POU2F2, POU2F1 and POU3F1 (PubMed:7720710).
CC Component of the RAG complex composed of core components RAG1 and RAG2,
CC and associated component HMGB1 or HMGB2 (PubMed:9184213). Component of
CC the SET complex, composed of at least ANP32A, APEX1, HMGB2, NME1, SET
CC and TREX1. Directly interacts with SET (By similarity). Interacts with
CC LEF1 (PubMed:19805379). {ECO:0000250|UniProtKB:P26583,
CC ECO:0000269|PubMed:19805379, ECO:0000269|PubMed:7720710,
CC ECO:0000269|PubMed:9184213}.
CC -!- INTERACTION:
CC P30681; P27782: Lef1; NbExp=2; IntAct=EBI-6910056, EBI-984464;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:P09429}.
CC Chromosome {ECO:0000250|UniProtKB:P26583}. Cytoplasm
CC {ECO:0000269|PubMed:19890330}. Secreted {ECO:0000250|UniProtKB:P26583}.
CC -!- TISSUE SPECIFICITY: Widely expressed in embryo. In adult mainly
CC expressed in lymphoid organs and testes (PubMed:11262228). Expressed in
CC primary spermatocytes. Expressed in the superficial zone of articular
CC cartilage (PubMed:19805379). {ECO:0000269|PubMed:11262228,
CC ECO:0000269|PubMed:19805379}.
CC -!- DOMAIN: Both, HMG box 1 and HMG box 2, show antimicrobial activity.
CC {ECO:0000250|UniProtKB:P26583}.
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 HMGB2
CC (HMGB2C23hC45hC106h), 2- disulfide HMGB2 (HMGB2C23-C45C106h) and
CC 3- sulfonyl HMGB2 (HMGB2C23soC45soC106so).
CC {ECO:0000250|UniProtKB:P09429}.
CC -!- DISRUPTION PHENOTYPE: Viable, with severe reduction of sperm production
CC in males. {ECO:0000269|PubMed:11262228}.
CC -!- SIMILARITY: Belongs to the HMGB family. {ECO:0000305}.
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DR EMBL; X67668; CAA47900.1; -; mRNA.
DR EMBL; Z46757; CAA86727.1; -; mRNA.
DR EMBL; AF267733; AAG36939.1; -; Genomic_DNA.
DR EMBL; AK003773; BAB22988.1; -; mRNA.
DR EMBL; AK008443; BAB25672.1; -; mRNA.
DR EMBL; AK012568; BAB28323.1; -; mRNA.
DR EMBL; AK135296; BAE22481.1; -; mRNA.
DR EMBL; AK135297; BAE22482.1; -; mRNA.
DR EMBL; AK146212; BAE26982.1; -; mRNA.
DR EMBL; BC002050; AAH02050.1; -; mRNA.
DR EMBL; BC046759; AAH46759.1; -; mRNA.
DR EMBL; BC083108; AAH83108.1; -; mRNA.
DR CCDS; CCDS40343.1; -.
DR PIR; S26062; S26062.
DR PIR; S54774; S54774.
DR RefSeq; NP_032278.1; NM_008252.3.
DR RefSeq; XP_006509587.1; XM_006509524.2.
DR AlphaFoldDB; P30681; -.
DR SMR; P30681; -.
DR BioGRID; 220633; 9.
DR DIP; DIP-899N; -.
DR IntAct; P30681; 5.
DR MINT; P30681; -.
DR STRING; 10090.ENSMUSP00000065940; -.
DR iPTMnet; P30681; -.
DR PhosphoSitePlus; P30681; -.
DR SwissPalm; P30681; -.
DR CPTAC; non-CPTAC-3820; -.
DR EPD; P30681; -.
DR jPOST; P30681; -.
DR MaxQB; P30681; -.
DR PaxDb; P30681; -.
DR PeptideAtlas; P30681; -.
DR PRIDE; P30681; -.
DR ProteomicsDB; 267052; -.
DR Antibodypedia; 1112; 406 antibodies from 35 providers.
DR DNASU; 97165; -.
DR Ensembl; ENSMUST00000067925; ENSMUSP00000065940; ENSMUSG00000054717.
DR GeneID; 97165; -.
DR KEGG; mmu:97165; -.
DR UCSC; uc009lsx.2; mouse.
DR CTD; 3148; -.
DR MGI; MGI:96157; Hmgb2.
DR VEuPathDB; HostDB:ENSMUSG00000054717; -.
DR eggNOG; KOG0381; Eukaryota.
DR GeneTree; ENSGT00940000154466; -.
DR HOGENOM; CLU_082854_0_0_1; -.
DR InParanoid; P30681; -.
DR OMA; YAYFVAT; -.
DR OrthoDB; 1641977at2759; -.
DR PhylomeDB; P30681; -.
DR TreeFam; TF105371; -.
DR Reactome; R-MMU-140342; Apoptosis induced DNA fragmentation.
DR BioGRID-ORCS; 97165; 10 hits in 72 CRISPR screens.
DR ChiTaRS; Hmgb2; mouse.
DR PRO; PR:P30681; -.
DR Proteomes; UP000000589; Chromosome 8.
DR RNAct; P30681; protein.
DR Bgee; ENSMUSG00000054717; Expressed in embryonic post-anal tail and 184 other tissues.
DR ExpressionAtlas; P30681; baseline and differential.
DR Genevisible; P30681; MM.
DR GO; GO:0000785; C:chromatin; IDA:AgBase.
DR GO; GO:0000793; C:condensed chromosome; ISS:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; IDA:AgBase.
DR GO; GO:0005615; C:extracellular space; IDA:AgBase.
DR GO; GO:0005730; C:nucleolus; ISO:MGI.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005634; C:nucleus; IDA:AgBase.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; ISS:UniProtKB.
DR GO; GO:0032991; C:protein-containing complex; ISO:MGI.
DR GO; GO:0042056; F:chemoattractant activity; ISO:MGI.
DR GO; GO:0000987; F:cis-regulatory region sequence-specific DNA binding; IDA:AgBase.
DR GO; GO:0003684; F:damaged DNA binding; ISO:MGI.
DR GO; GO:0003677; F:DNA binding; ISS:AgBase.
DR GO; GO:0008301; F:DNA binding, bending; ISS:UniProtKB.
DR GO; GO:0140297; F:DNA-binding transcription factor binding; IPI:UniProtKB.
DR GO; GO:0003690; F:double-stranded DNA binding; IDA:UniProtKB.
DR GO; GO:0044378; F:non-sequence-specific DNA binding, bending; ISS:AgBase.
DR GO; GO:0019904; F:protein domain specific binding; IPI:MGI.
DR GO; GO:0050786; F:RAGE receptor binding; ISO:MGI.
DR GO; GO:0097100; F:supercoiled DNA binding; ISS:AgBase.
DR GO; GO:0000976; F:transcription cis-regulatory region binding; ISO:MGI.
DR GO; GO:0003713; F:transcription coactivator activity; ISO:MGI.
DR GO; GO:0008134; F:transcription factor binding; IDA:AgBase.
DR GO; GO:0060326; P:cell chemotaxis; ISO:MGI.
DR GO; GO:0071222; P:cellular response to lipopolysaccharide; IEA:Ensembl.
DR GO; GO:0050829; P:defense response to Gram-negative bacterium; ISS:AgBase.
DR GO; GO:0050830; P:defense response to Gram-positive bacterium; ISS:AgBase.
DR GO; GO:0006310; P:DNA recombination; IEA:UniProtKB-KW.
DR GO; GO:0006265; P:DNA topological change; ISS:AgBase.
DR GO; GO:0008625; P:extrinsic apoptotic signaling pathway via death domain receptors; IMP:MGI.
DR GO; GO:0002437; P:inflammatory response to antigenic stimulus; IMP:AgBase.
DR GO; GO:0045087; P:innate immune response; IEA:UniProtKB-KW.
DR GO; GO:0008584; P:male gonad development; IMP:MGI.
DR GO; GO:1902042; P:negative regulation of extrinsic apoptotic signaling pathway via death domain receptors; IMP:MGI.
DR GO; GO:0010629; P:negative regulation of gene expression; IDA:AgBase.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; ISO:MGI.
DR GO; GO:0045892; P:negative regulation of transcription, DNA-templated; ISO:MGI.
DR GO; GO:0043388; P:positive regulation of DNA binding; IDA:MGI.
DR GO; GO:0001938; P:positive regulation of endothelial cell proliferation; ISO:MGI.
DR GO; GO:0045648; P:positive regulation of erythrocyte differentiation; ISO:MGI.
DR GO; GO:0010628; P:positive regulation of gene expression; IDA:AgBase.
DR GO; GO:0045089; P:positive regulation of innate immune response; IMP:UniProtKB.
DR GO; GO:0032728; P:positive regulation of interferon-beta production; IMP:UniProtKB.
DR GO; GO:0045654; P:positive regulation of megakaryocyte differentiation; ISO:MGI.
DR GO; GO:0032075; P:positive regulation of nuclease activity; ISO:MGI.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IMP:MGI.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; ISO:MGI.
DR GO; GO:0050767; P:regulation of neurogenesis; IMP:AgBase.
DR GO; GO:0072091; P:regulation of stem cell proliferation; IMP:AgBase.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IDA:MGI.
DR GO; GO:0032496; P:response to lipopolysaccharide; IMP:AgBase.
DR GO; GO:0048545; P:response to steroid hormone; IMP:MGI.
DR GO; GO:0007289; P:spermatid nucleus differentiation; IMP:MGI.
DR GO; GO:0007283; P:spermatogenesis; IMP:MGI.
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 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 1: Evidence at protein level;
KW Acetylation; Chemotaxis; Chromosome; Cytoplasm; Disulfide bond;
KW DNA recombination; DNA-binding; Immunity; Inflammatory response;
KW Innate immunity; Nucleus; Oxidation; Phosphoprotein; Reference proteome;
KW Repeat; Secreted; Transcription; Transcription regulation.
FT CHAIN 1..210
FT /note="High mobility group protein B2"
FT /id="PRO_0000048535"
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 71..102
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 162..210
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 165..180
FT /note="Required for chemotactic activity"
FT /evidence="ECO:0000250|UniProtKB:P26583"
FT COMPBIAS 71..95
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 188..210
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 3
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P63159"
FT MOD_RES 23
FT /note="Cysteine sulfonic acid (-SO3H); alternate"
FT /evidence="ECO:0000250|UniProtKB:P63159"
FT MOD_RES 30
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:23806337"
FT MOD_RES 35
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P26583"
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 114
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:23806337"
FT MOD_RES 141
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P63158"
FT DISULFID 23..45
FT /note="In disulfide HMGB2; alternate"
FT /evidence="ECO:0000250|UniProtKB:P63159"
FT CONFLICT 7
FT /note="N -> I (in Ref. 1; CAA47900)"
FT /evidence="ECO:0000305"
FT CONFLICT 10
FT /note="R -> L (in Ref. 1; CAA47900)"
FT /evidence="ECO:0000305"
FT CONFLICT 33
FT /note="D -> N (in Ref. 1; CAA47900)"
FT /evidence="ECO:0000305"
FT CONFLICT 41
FT /note="F -> I (in Ref. 1; CAA47900)"
FT /evidence="ECO:0000305"
FT CONFLICT 47
FT /note="E -> K (in Ref. 1; CAA47900)"
FT /evidence="ECO:0000305"
FT CONFLICT 57
FT /note="K -> N (in Ref. 1; CAA47900)"
FT /evidence="ECO:0000305"
FT CONFLICT 70..72
FT /note="RYD -> CYY (in Ref. 1; CAA47900)"
FT /evidence="ECO:0000305"
FT CONFLICT 80
FT /note="P -> S (in Ref. 1; CAA47900)"
FT /evidence="ECO:0000305"
FT CONFLICT 103
FT /note="F -> C (in Ref. 1; CAA47900)"
FT /evidence="ECO:0000305"
FT CONFLICT 117
FT /note="H -> Y (in Ref. 1; CAA47900)"
FT /evidence="ECO:0000305"
FT CONFLICT 140
FT /note="D -> E (in Ref. 1; CAA47900)"
FT /evidence="ECO:0000305"
FT CONFLICT 159
FT /note="I -> F (in Ref. 1; CAA47900)"
FT /evidence="ECO:0000305"
FT CONFLICT 164
FT /note="A -> V (in Ref. 1; CAA47900)"
FT /evidence="ECO:0000305"
FT CONFLICT 179
FT /note="T -> A (in Ref. 1; CAA47900)"
FT /evidence="ECO:0000305"
FT CONFLICT 184..193
FT /note="KNEPEDEEEE -> NDSED (in Ref. 1; CAA47900)"
FT /evidence="ECO:0000305"
FT CONFLICT 202
FT /note="D -> E (in Ref. 1; CAA47900, 4; AAG36939 and 6;
FT AAH02050)"
FT /evidence="ECO:0000305"
FT CONFLICT 204
FT /note="E -> G (in Ref. 1; CAA47900)"
FT /evidence="ECO:0000305"
SQ 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
