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 27-MAR-2024, entry version 196. 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; RC 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, RC Pancreas, 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}. 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; 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; 12. DR DIP; DIP-899N; -. DR IntAct; P30681; 5. DR MINT; P30681; -. DR STRING; 10090.ENSMUSP00000065940; -. DR GlyGen; P30681; 1 site, 1 O-linked glycan (1 site). 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; 10090-ENSMUSP00000065940; -. DR PeptideAtlas; P30681; -. DR ProteomicsDB; 267052; -. DR Pumba; P30681; -. DR Antibodypedia; 1112; 452 antibodies from 35 providers. DR DNASU; 97165; -. DR Ensembl; ENSMUST00000067925.8; ENSMUSP00000065940.7; ENSMUSG00000054717.8. DR GeneID; 97165; -. DR KEGG; mmu:97165; -. DR UCSC; uc009lsx.2; mouse. DR AGR; MGI:96157; -. 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; CKHEAMR; -. DR OrthoDB; 1222485at2759; -. DR PhylomeDB; P30681; -. DR TreeFam; TF105371; -. DR Reactome; R-MMU-140342; Apoptosis induced DNA fragmentation. DR BioGRID-ORCS; 97165; 10 hits in 77 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 186 other cell types or tissues. DR ExpressionAtlas; P30681; baseline and differential. 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:0008289; F:lipid binding; ISO:MGI. 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:0045892; P:negative regulation of DNA-templated transcription; ISO: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:0045893; P:positive regulation of DNA-templated transcription; ISO: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:0045944; P:positive regulation of transcription by RNA polymerase II; IMP: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 CDD; cd21978; HMG-box_HMGB_rpt1; 1. DR CDD; cd21979; HMG-box_HMGB_rpt2; 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 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. DR Genevisible; P30681; MM. 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 //