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 27-NOV-2024, entry version 225. 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:11909973, PubMed:18413230, PubMed:19522541, CC PubMed:19965638, PubMed:20123072, PubMed:7797075). 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-21353855; 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}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- 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; 257. DR CORUM; P26583; -. DR IntAct; P26583; 156. 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 jPOST; P26583; -. DR MassIVE; P26583; -. DR PaxDb; 9606-ENSP00000296503; -. DR PeptideAtlas; P26583; -. DR ProteomicsDB; 54353; -. DR Pumba; P26583; -. DR TopDownProteomics; P26583; -. DR ABCD; P26583; 1 sequenced antibody. DR Antibodypedia; 1112; 394 antibodies from 34 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 AGR; HGNC:5000; -. 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; INTCREE; -. DR OrthoDB; 1222485at2759; -. 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; 20 hits in 1189 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 211 other cell types or tissues. DR ExpressionAtlas; P26583; baseline and differential. 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:0045892; P:negative regulation of DNA-templated transcription; IDA:BHF-UCL. 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:0006334; P:nucleosome assembly; NAS:UniProtKB. DR GO; GO:0045893; P:positive regulation of DNA-templated transcription; 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:0045944; P:positive regulation of transcription by RNA polymerase II; 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 CDD; cd21978; HMG-box_HMGB_rpt1; 1. DR CDD; cd21979; HMG-box_HMGB_rpt2; 1. DR FunFam; 1.10.30.10:FF:000006; High mobility group protein B1; 1. DR FunFam; 1.10.30.10:FF:000018; High mobility group protein B2; 1. DR Gene3D; 1.10.30.10; High mobility group box domain; 2. DR InterPro; IPR009071; HMG_box_dom. DR InterPro; IPR036910; HMG_box_dom_sf. DR InterPro; IPR017967; HMG_boxA_CS. DR InterPro; IPR050342; HMGB. DR PANTHER; PTHR48112:SF3; HIGH MOBILITY GROUP PROTEIN B2; 1. DR PANTHER; PTHR48112; HIGH MOBILITY GROUP PROTEIN DSP1; 1. DR Pfam; PF00505; HMG_box; 1. DR Pfam; PF09011; HMG_box_2; 1. DR PRINTS; PR00886; HIGHMOBLTY12. DR SMART; SM00398; HMG; 2. DR SUPFAM; SSF47095; HMG-box; 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; KW Proteomics identification; Reference proteome; Repeat; Secreted; KW 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 //