HMGB2_HUMAN
ID HMGB2_HUMAN Reviewed; 209 AA.
AC P26583; B2R4K8; D3DP37; Q5U072;
DT 01-AUG-1992, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 212.
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 Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=1754403; DOI=10.1093/nar/19.23.6643;
RA Majumdar A., Brown D., Kerby S., Rudzinski I., Polte T., Randawa Z.,
RA Seidman M.M.;
RT "Sequence of human HMG2 cDNA.";
RL Nucleic Acids Res. 19:6643-6643(1991).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=1551873; DOI=10.1016/s0021-9258(19)50475-6;
RA Shirakawa H., Yoshida M.;
RT "Structure of a gene coding for human HMG2 protein.";
RL J. Biol. Chem. 267:6641-6645(1992).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S.,
RA Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y.,
RA Phelan M., Farmer A.;
RT "Cloning of human full-length CDSs in BD Creator(TM) system donor vector.";
RL Submitted (OCT-2004) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Placenta, and Skin;
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 NUCLEOTIDE SEQUENCE [MRNA] OF 24-209.
RX PubMed=1475204; DOI=10.1093/nar/20.23.6413;
RA Alexandre S., Li W.W., Lee A.S.;
RT "A human HMG2 cDNA with a novel 3'-untranslated region.";
RL Nucleic Acids Res. 20:6413-6413(1992).
RN [8]
RP FUNCTION.
RX PubMed=7797075; DOI=10.1101/gad.9.11.1354;
RA Shykind B.M., Kim J., Sharp P.A.;
RT "Activation of the TFIID-TFIIA complex with HMG-2.";
RL Genes Dev. 9:1354-1365(1995).
RN [9]
RP FUNCTION, SUBCELLULAR LOCATION, IDENTIFICATION IN THE SET COMPLEX, AND
RP INTERACTION WITH SET.
RX PubMed=11909973; DOI=10.1128/mcb.22.8.2810-2820.2002;
RA Fan Z., Beresford P.J., Zhang D., Lieberman J.;
RT "HMG2 interacts with the nucleosome assembly protein SET and is a target of
RT the cytotoxic T-lymphocyte protease granzyme A.";
RL Mol. Cell. Biol. 22:2810-2820(2002).
RN [10]
RP SUBCELLULAR LOCATION.
RX PubMed=12925773; DOI=10.1091/mbc.e02-09-0581;
RA Pallier C., Scaffidi P., Chopineau-Proust S., Agresti A., Nordmann P.,
RA Bianchi M.E., Marechal V.;
RT "Association of chromatin proteins high mobility group box (HMGB) 1 and
RT HMGB2 with mitotic chromosomes.";
RL Mol. Biol. Cell 14:3414-3426(2003).
RN [11]
RP FUNCTION.
RX PubMed=18413230; DOI=10.1016/j.bbrc.2008.04.024;
RA Zimmerman J., Maher L.J. III;
RT "Transient HMGB protein interactions with B-DNA duplexes and complexes.";
RL Biochem. Biophys. Res. Commun. 371:79-84(2008).
RN [12]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=19811285; DOI=10.1080/08916930902831845;
RA Pusterla T., de Marchis F., Palumbo R., Bianchi M.E.;
RT "High mobility group B2 is secreted by myeloid cells and has mitogenic and
RT chemoattractant activities similar to high mobility group B1.";
RL Autoimmunity 42:308-310(2009).
RN [13]
RP FUNCTION, AND ACETYLATION.
RX PubMed=19522541; DOI=10.1021/bi9004304;
RA Ugrinova I., Pashev I.G., Pasheva E.A.;
RT "Nucleosome binding properties and Co-remodeling activities of native and
RT in vivo acetylated HMGB-1 and HMGB-2 proteins.";
RL Biochemistry 48:6502-6507(2009).
RN [14]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-30, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19608861; DOI=10.1126/science.1175371;
RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C.,
RA Olsen J.V., Mann M.;
RT "Lysine acetylation targets protein complexes and co-regulates major
RT cellular functions.";
RL Science 325:834-840(2009).
RN [15]
RP FUNCTION.
RX PubMed=19965638; DOI=10.1182/blood-2009-06-230094;
RA Laurent B., Randrianarison-Huetz V., Marechal V., Marchal V., Mayeux P.,
RA Dusanter-Fourt I., Dumenil D.;
RT "High-mobility group protein HMGB2 regulates human erythroid
RT differentiation through trans-activation of GFI1B transcription.";
RL Blood 115:687-695(2010).
RN [16]
RP REVIEW ON FUNCTION RELATED TO DNA-BINDING.
RX PubMed=20123072; DOI=10.1016/j.bbagrm.2009.09.008;
RA Stros M.;
RT "HMGB proteins: interactions with DNA and chromatin.";
RL Biochim. Biophys. Acta 1799:101-113(2010).
RN [17]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [18]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-terminal
RT acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN [19]
RP FUNCTION, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=23877675; DOI=10.1128/aac.00805-13;
RA Kuechler R., Schroeder B.O., Jaeger S.U., Stange E.F., Wehkamp J.;
RT "Antimicrobial activity of high-mobility-group box 2: a new function to a
RT well-known protein.";
RL Antimicrob. Agents Chemother. 57:4782-4793(2013).
RN [20]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-35, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma, and Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [21]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [22]
RP NOMENCLATURE OF REDOX FORMS.
RX PubMed=24531895; DOI=10.2119/molmed.2014.00022;
RA Antoine D.J., Harris H.E., Andersson U., Tracey K.J., Bianchi M.E.;
RT "A systematic nomenclature for the redox states of high mobility group box
RT (HMGB) proteins.";
RL Mol. Med. 20:135-137(2014).
RN [23]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25944712; DOI=10.1002/pmic.201400617;
RA Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., Ayoub D.,
RA Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
RT "N-terminome analysis of the human mitochondrial proteome.";
RL Proteomics 15:2519-2524(2015).
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 (PubMed:7797075, PubMed:11909973, PubMed:19522541,
CC PubMed:18413230, PubMed:19965638, PubMed:20123072). Involved in V(D)J
CC recombination by acting as a cofactor of the RAG complex: acts by
CC stimulating cleavage and RAG protein binding at the 23 bp spacer of
CC conserved recombination signal sequences (RSS) (By similarity).
CC Proposed to be involved in the innate immune response to nucleic acids
CC by acting as a promiscuous immunogenic DNA/RNA sensor which cooperates
CC with subsequent discriminative sensing by specific pattern recognition
CC receptors (By similarity). In the extracellular compartment acts as a
CC chemokine. Promotes proliferation and migration of endothelial cells
CC implicating AGER/RAGE (PubMed:19811285). Has antimicrobial activity in
CC gastrointestinal epithelial tissues (PubMed:23877675). Involved in
CC inflammatory response to antigenic stimulus coupled with pro-
CC inflammatory activity (By similarity). Involved in modulation of
CC neurogenesis probably by regulation of neural stem proliferation (By
CC similarity). Involved in articular cartilage surface maintenance
CC implicating LEF1 and the Wnt/beta-catenin pathway (By similarity).
CC {ECO:0000250|UniProtKB:P09429, ECO:0000250|UniProtKB:P30681,
CC ECO:0000269|PubMed:11909973, ECO:0000269|PubMed:18413230,
CC ECO:0000269|PubMed:19522541, ECO:0000269|PubMed:19811285,
CC ECO:0000269|PubMed:19965638, ECO:0000269|PubMed:23877675,
CC ECO:0000269|PubMed:7797075, ECO:0000305|PubMed:20123072}.
CC -!- SUBUNIT: Interacts with POU2F2, POU2F1 and POU3F1 (By similarity).
CC Component of the RAG complex composed of core components RAG1 and RAG2,
CC and associated component HMGB1 or HMGB2 (By similarity). Component of
CC the SET complex, composed of at least ANP32A, APEX1, HMGB2, NME1, SET
CC and TREX1. Directly interacts with SET (PubMed:11909973). Interacts
CC with LEF1 (By similarity). {ECO:0000250|UniProtKB:P30681,
CC ECO:0000269|PubMed:11909973}.
CC -!- INTERACTION:
CC P26583; Q8N668: COMMD1; NbExp=3; IntAct=EBI-1057009, EBI-1550112;
CC P26583; Q9BRT3: MIEN1; NbExp=6; IntAct=EBI-1057009, EBI-6137472;
CC P26583; Q9NZM5: NOP53; NbExp=4; IntAct=EBI-1057009, EBI-720156;
CC P26583; P55347: PKNOX1; NbExp=4; IntAct=EBI-1057009, EBI-1373569;
CC P26583; Q96I87: PKNOX1; NbExp=3; IntAct=EBI-1057009, EBI-10173774;
CC P26583; Q99598: TSNAX; NbExp=3; IntAct=EBI-1057009, EBI-742638;
CC P26583; Q96B54: ZNF428; NbExp=4; IntAct=EBI-1057009, EBI-9995882;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:11909973,
CC ECO:0000269|PubMed:12925773, ECO:0000269|PubMed:23877675}. Chromosome
CC {ECO:0000269|PubMed:12925773}. Cytoplasm {ECO:0000269|PubMed:11909973,
CC ECO:0000269|PubMed:23877675}. Secreted {ECO:0000269|PubMed:19811285,
CC ECO:0000269|PubMed:23877675}. Note=In basal state predominantly
CC nuclear. {ECO:0000305}.
CC -!- TISSUE SPECIFICITY: Expressed in gastric and intestinal tissues (at
CC protein level). {ECO:0000269|PubMed:23877675}.
CC -!- DOMAIN: Both, HMG box 1 and HMG box 2, show antimicrobial activity.
CC {ECO:0000269|PubMed:23877675}.
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, ECO:0000305|PubMed:24531895}.
CC -!- PTM: Acetylation enhances nucleosome binding and chromation remodeling
CC activity. {ECO:0000269|PubMed:19522541}.
CC -!- SIMILARITY: Belongs to the HMGB family. {ECO:0000305}.
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DR EMBL; M83665; AAA58659.1; -; Genomic_DNA.
DR EMBL; X62534; CAA44395.1; -; mRNA.
DR EMBL; BT019782; AAV38585.1; -; mRNA.
DR EMBL; AK311864; BAG34805.1; -; mRNA.
DR EMBL; CH471056; EAX04758.1; -; Genomic_DNA.
DR EMBL; CH471056; EAX04759.1; -; Genomic_DNA.
DR EMBL; BC001063; AAH01063.1; -; mRNA.
DR EMBL; BC100019; AAI00020.1; -; mRNA.
DR EMBL; Z17240; CAA78938.1; -; mRNA.
DR CCDS; CCDS3816.1; -.
DR PIR; A42425; NSHUH2.
DR PIR; S30221; S30221.
DR RefSeq; NP_001124160.1; NM_001130688.1.
DR RefSeq; NP_001124161.1; NM_001130689.1.
DR RefSeq; NP_002120.1; NM_002129.3.
DR AlphaFoldDB; P26583; -.
DR SMR; P26583; -.
DR BioGRID; 109391; 131.
DR CORUM; P26583; -.
DR IntAct; P26583; 74.
DR MINT; P26583; -.
DR STRING; 9606.ENSP00000296503; -.
DR ChEMBL; CHEMBL4295734; -.
DR GlyGen; P26583; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; P26583; -.
DR MetOSite; P26583; -.
DR PhosphoSitePlus; P26583; -.
DR SwissPalm; P26583; -.
DR BioMuta; HMGB2; -.
DR DMDM; 123374; -.
DR EPD; P26583; -.
DR jPOST; P26583; -.
DR MassIVE; P26583; -.
DR MaxQB; P26583; -.
DR PaxDb; P26583; -.
DR PeptideAtlas; P26583; -.
DR PRIDE; P26583; -.
DR ProteomicsDB; 54353; -.
DR TopDownProteomics; P26583; -.
DR ABCD; P26583; 1 sequenced antibody.
DR Antibodypedia; 1112; 406 antibodies from 35 providers.
DR DNASU; 3148; -.
DR Ensembl; ENST00000296503.10; ENSP00000296503.5; ENSG00000164104.12.
DR Ensembl; ENST00000438704.6; ENSP00000404912.2; ENSG00000164104.12.
DR Ensembl; ENST00000446922.6; ENSP00000393448.2; ENSG00000164104.12.
DR GeneID; 3148; -.
DR KEGG; hsa:3148; -.
DR MANE-Select; ENST00000296503.10; ENSP00000296503.5; NM_002129.4; NP_002120.1.
DR UCSC; uc003ita.4; human.
DR CTD; 3148; -.
DR DisGeNET; 3148; -.
DR GeneCards; HMGB2; -.
DR HGNC; HGNC:5000; HMGB2.
DR HPA; ENSG00000164104; Group enriched (bone marrow, lymphoid tissue).
DR MIM; 163906; gene.
DR neXtProt; NX_P26583; -.
DR OpenTargets; ENSG00000164104; -.
DR PharmGKB; PA35091; -.
DR VEuPathDB; HostDB:ENSG00000164104; -.
DR eggNOG; KOG0381; Eukaryota.
DR GeneTree; ENSGT00940000154466; -.
DR HOGENOM; CLU_082854_0_0_1; -.
DR InParanoid; P26583; -.
DR OMA; FASAIRP; -.
DR OrthoDB; 1641977at2759; -.
DR PhylomeDB; P26583; -.
DR TreeFam; TF105371; -.
DR PathwayCommons; P26583; -.
DR Reactome; R-HSA-140342; Apoptosis induced DNA fragmentation.
DR SignaLink; P26583; -.
DR SIGNOR; P26583; -.
DR BioGRID-ORCS; 3148; 16 hits in 1109 CRISPR screens.
DR ChiTaRS; HMGB2; human.
DR GeneWiki; HMGB2; -.
DR GenomeRNAi; 3148; -.
DR Pharos; P26583; Tbio.
DR PRO; PR:P26583; -.
DR Proteomes; UP000005640; Chromosome 4.
DR RNAct; P26583; protein.
DR Bgee; ENSG00000164104; Expressed in ventricular zone and 209 other tissues.
DR ExpressionAtlas; P26583; baseline and differential.
DR Genevisible; P26583; HS.
DR GO; GO:0000785; C:chromatin; ISS:AgBase.
DR GO; GO:0000793; C:condensed chromosome; IDA:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005615; C:extracellular space; IDA:UniProtKB.
DR GO; GO:0005730; C:nucleolus; IDA:HPA.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; IDA:UniProtKB.
DR GO; GO:0032991; C:protein-containing complex; IDA:UniProtKB.
DR GO; GO:0042056; F:chemoattractant activity; IDA:UniProtKB.
DR GO; GO:0000987; F:cis-regulatory region sequence-specific DNA binding; ISS:AgBase.
DR GO; GO:0003684; F:damaged DNA binding; IDA:UniProtKB.
DR GO; GO:0003677; F:DNA binding; IMP:UniProtKB.
DR GO; GO:0008301; F:DNA binding, bending; IDA:UniProtKB.
DR GO; GO:0140297; F:DNA-binding transcription factor binding; IEA:Ensembl.
DR GO; GO:0003690; F:double-stranded DNA binding; ISS:UniProtKB.
DR GO; GO:0000400; F:four-way junction DNA binding; ISS:AgBase.
DR GO; GO:0044378; F:non-sequence-specific DNA binding, bending; ISS:AgBase.
DR GO; GO:0019904; F:protein domain specific binding; IEA:Ensembl.
DR GO; GO:0050786; F:RAGE receptor binding; IGI:UniProtKB.
DR GO; GO:0003723; F:RNA binding; HDA:UniProtKB.
DR GO; GO:0003697; F:single-stranded DNA binding; ISS:UniProtKB.
DR GO; GO:0097100; F:supercoiled DNA binding; ISS:AgBase.
DR GO; GO:0000976; F:transcription cis-regulatory region binding; IDA:UniProtKB.
DR GO; GO:0003713; F:transcription coactivator activity; IDA:UniProtKB.
DR GO; GO:0008134; F:transcription factor binding; ISS:AgBase.
DR GO; GO:0060326; P:cell chemotaxis; IDA:UniProtKB.
DR GO; GO:0071222; P:cellular response to lipopolysaccharide; IEP:UniProtKB.
DR GO; GO:0006325; P:chromatin organization; NAS:UniProtKB.
DR GO; GO:0050829; P:defense response to Gram-negative bacterium; IDA:AgBase.
DR GO; GO:0050830; P:defense response to Gram-positive bacterium; IDA:AgBase.
DR GO; GO:0032392; P:DNA geometric change; ISS:AgBase.
DR GO; GO:0006265; P:DNA topological change; ISS:UniProtKB.
DR GO; GO:0006303; P:double-strand break repair via nonhomologous end joining; ISS:UniProtKB.
DR GO; GO:0008625; P:extrinsic apoptotic signaling pathway via death domain receptors; IEA:Ensembl.
DR GO; GO:0002437; P:inflammatory response to antigenic stimulus; ISS:AgBase.
DR GO; GO:0045087; P:innate immune response; IEA:UniProtKB-KW.
DR GO; GO:0008584; P:male gonad development; IEA:Ensembl.
DR GO; GO:1902042; P:negative regulation of extrinsic apoptotic signaling pathway via death domain receptors; IEA:Ensembl.
DR GO; GO:0010629; P:negative regulation of gene expression; IEA:Ensembl.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IDA:UniProtKB.
DR GO; GO:0045892; P:negative regulation of transcription, DNA-templated; IDA:BHF-UCL.
DR GO; GO:0006334; P:nucleosome assembly; NAS:UniProtKB.
DR GO; GO:0043388; P:positive regulation of DNA binding; IDA:UniProtKB.
DR GO; GO:0001938; P:positive regulation of endothelial cell proliferation; IDA:UniProtKB.
DR GO; GO:0045648; P:positive regulation of erythrocyte differentiation; IMP:UniProtKB.
DR GO; GO:0045089; P:positive regulation of innate immune response; IEA:Ensembl.
DR GO; GO:0032728; P:positive regulation of interferon-beta production; IEA:Ensembl.
DR GO; GO:0045654; P:positive regulation of megakaryocyte differentiation; IMP:UniProtKB.
DR GO; GO:0032075; P:positive regulation of nuclease activity; IDA:UniProtKB.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IDA:UniProtKB.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IDA:UniProtKB.
DR GO; GO:0050767; P:regulation of neurogenesis; ISS:AgBase.
DR GO; GO:0072091; P:regulation of stem cell proliferation; ISS:AgBase.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IDA:UniProtKB.
DR GO; GO:0032496; P:response to lipopolysaccharide; ISS:AgBase.
DR GO; GO:0048545; P:response to steroid hormone; IEA:Ensembl.
DR GO; GO:0007289; P:spermatid nucleus differentiation; IEA:Ensembl.
DR GO; GO:0033151; P:V(D)J recombination; ISS:UniProtKB.
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..209
FT /note="High mobility group protein B2"
FT /id="PRO_0000048534"
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 52..150
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 162..209
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 165..180
FT /note="Required for chemotactic activity"
FT /evidence="ECO:0000269|PubMed:19811285"
FT COMPBIAS 52..95
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 133..150
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 188..209
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:19608861"
FT MOD_RES 35
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
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:0000250|UniProtKB:P30681"
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 163
FT /note="R -> G (in Ref. 7; CAA78938)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 209 AA; 24034 MW; 5E65292BC4AD8373 CRC64;
MGKGDPNKPR GKMSSYAFFV QTCREEHKKK HPDSSVNFAE FSKKCSERWK TMSAKEKSKF
EDMAKSDKAR YDREMKNYVP PKGDKKGKKK DPNAPKRPPS AFFLFCSEHR PKIKSEHPGL
SIGDTAKKLG EMWSEQSAKD KQPYEQKAAK LKEKYEKDIA AYRAKGKSEA GKKGPGRPTG
SKKKNEPEDE EEEEEEEDED EEEEDEDEE
