ID HMGB2_RAT Reviewed; 210 AA. AC P52925; Q5FVP0; DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot. DT 23-JAN-2007, sequence version 2. DT 02-SEP-2026, entry version 184. 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 Rattus norvegicus (Rat). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae; OC Murinae; Rattus. OX NCBI_TaxID=10116; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RC STRAIN=Fischer; RA Yoshida M.; RT "Rat mRNA for chromosomal protein HMG2, complete cds."; RL Submitted (MAY-1996) to the EMBL/GenBank/DDBJ databases. RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Spleen, Testis, and Thymus; 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). 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 (By similarity). Binds DNA with a CC preference to non-canonical DNA structures such as single-stranded DNA. CC Can bent DNA and enhance DNA flexibility by looping thus providing a CC mechanism to promote activities on various gene promoters by enhancing CC transcription factor binding and/or bringing distant regulatory CC sequences into close proximity. Involved in V(D)J recombination by CC acting as a cofactor of the RAG complex: acts by stimulating cleavage CC and RAG protein binding at the 23 bp spacer of conserved recombination CC signal sequences (RSS). Proposed to be involved in the innate immune CC 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. In CC the extracellular compartment acts as a chemokine. Promotes CC proliferation and migration of endothelial cells implicating AGER/RAGE. CC Has antimicrobial activity in gastrointestinal epithelial tissues. CC Involved in inflammatory response to antigenic stimulus coupled with CC pro-inflammatory activity. May play a role in germ cell CC differentiation. Involved in modulation of neurogenesis probably by CC regulation of neural stem proliferation. Involved in articular CC cartilage surface maintenance implicating LEF1 and the Wnt/beta-catenin CC pathway (By similarity). {ECO:0000250|UniProtKB:P09429, CC ECO:0000250|UniProtKB:P26583, ECO:0000250|UniProtKB:P30681}. CC -!- SUBUNIT: Interacts with POU2F2, POU2F1 and POU3F1. Component of the RAG CC complex composed of core components RAG1 and RAG2, and associated CC component HMGB1 or HMGB2. Component of the SET complex, composed of at CC least ANP32A, APEX1, HMGB2, NME1, SET and TREX1. Directly interacts CC with SET. Interacts with LEF1. {ECO:0000250|UniProtKB:P26583, CC ECO:0000250|UniProtKB:P30681}. CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:P26583, CC ECO:0000255|PROSITE-ProRule:PRU00267}. Chromosome CC {ECO:0000250|UniProtKB:P26583}. Cytoplasm CC {ECO:0000250|UniProtKB:P26583, ECO:0000250|UniProtKB:P30681}. Secreted CC {ECO:0000250|UniProtKB:P26583}. 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 -!- 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; D84418; BAA12350.1; -; mRNA. DR EMBL; BC078866; AAH78866.1; -; mRNA. DR EMBL; BC089854; AAH89854.1; -; mRNA. DR EMBL; BC107455; AAI07456.1; -; mRNA. DR RefSeq; NP_001316810.1; NM_001329881.2. DR RefSeq; NP_058883.1; NM_017187.2. DR RefSeq; XP_017455541.1; XM_017600052.3. DR AlphaFoldDB; P52925; -. DR SMR; P52925; -. DR FunCoup; P52925; 881. DR STRING; 10116.ENSRNOP00000017635; -. DR iPTMnet; P52925; -. DR PhosphoSitePlus; P52925; -. DR jPOST; P52925; -. DR PaxDb; 10116-ENSRNOP00000017635; -. DR DNASU; 29395; -. DR Ensembl; ENSRNOT00000017635.8; ENSRNOP00000017635.4; ENSRNOG00000013167.8. DR Ensembl; ENSRNOT00000046874.4; ENSRNOP00000039358.2; ENSRNOG00000033321.4. DR Ensembl; ENSRNOT00055020881; ENSRNOP00055016856; ENSRNOG00055012275. DR Ensembl; ENSRNOT00060011259; ENSRNOP00060008407; ENSRNOG00060006879. DR Ensembl; ENSRNOT00065006504; ENSRNOP00065004563; ENSRNOG00065004463. DR GeneID; 29395; -. DR GeneID; 498072; -. DR KEGG; rno:29395; -. DR KEGG; rno:498072; -. DR UCSC; RGD:69291; rat. DR AGR; RGD:1564519; -. DR AGR; RGD:69291; -. DR CTD; 3148; -. DR CTD; 498072; -. DR RGD; 69291; Hmgb2. DR eggNOG; KOG0381; Eukaryota. DR GeneTree; ENSGT00940000154466; -. DR HOGENOM; CLU_082854_0_0_1; -. DR InParanoid; P52925; -. DR OMA; YAYFVAT; -. DR OrthoDB; 1919336at2759; -. DR PhylomeDB; P52925; -. DR Reactome; R-RNO-140342; Apoptosis induced DNA fragmentation. DR PRO; PR:P52925; -. DR Proteomes; UP000002494; Chromosome 11. DR Proteomes; UP000002494; Chromosome 16. DR Bgee; ENSRNOG00000013167; Expressed in thymus and 19 other cell types or tissues. DR ExpressionAtlas; P52925; baseline and differential. DR GO; GO:0000785; C:chromatin; ISS:AgBase. DR GO; GO:0005694; C:chromosome; ISO:RGD. DR GO; GO:0000793; C:condensed chromosome; ISS:UniProtKB. DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB. DR GO; GO:0005576; C:extracellular region; ISS:AgBase. DR GO; GO:0005730; C:nucleolus; ISO:RGD. DR GO; GO:0005654; C:nucleoplasm; ISO:RGD. DR GO; GO:0005634; C:nucleus; ISS:UniProtKB. DR GO; GO:0048471; C:perinuclear region of cytoplasm; ISS:UniProtKB. DR GO; GO:0032991; C:protein-containing complex; ISO:RGD. DR GO; GO:0042056; F:chemoattractant activity; ISO:RGD. DR GO; GO:0000987; F:cis-regulatory region sequence-specific DNA binding; ISS:AgBase. DR GO; GO:0003684; F:damaged DNA binding; ISO:RGD. 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; ISO:RGD. DR GO; GO:0003690; F:double-stranded DNA binding; ISS:AgBase. DR GO; GO:0008289; F:lipid binding; IDA:RGD. DR GO; GO:0044378; F:non-sequence-specific DNA binding, bending; ISS:AgBase. DR GO; GO:0019904; F:protein domain specific binding; ISO:RGD. DR GO; GO:0050786; F:RAGE receptor binding; ISO:RGD. DR GO; GO:0003697; F:single-stranded DNA binding; ISS:AgBase. DR GO; GO:0097100; F:supercoiled DNA binding; ISS:AgBase. DR GO; GO:0000976; F:transcription cis-regulatory region binding; ISO:RGD. DR GO; GO:0003713; F:transcription coactivator activity; ISO:RGD. DR GO; GO:0031100; P:animal organ regeneration; IEP:RGD. DR GO; GO:0060326; P:cell chemotaxis; ISO:RGD. DR GO; GO:0071222; P:cellular response to lipopolysaccharide; ISO:RGD. DR GO; GO:0006338; P:chromatin remodeling; IBA:GO_Central. 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:0006265; P:DNA topological change; ISS:AgBase. DR GO; GO:0006303; P:double-strand break repair via nonhomologous end joining; ISO:RGD. DR GO; GO:0002437; P:inflammatory response to antigenic stimulus; ISS:AgBase. DR GO; GO:0008584; P:male gonad development; ISO:RGD. DR GO; GO:0045892; P:negative regulation of DNA-templated transcription; ISO:RGD. DR GO; GO:1902042; P:negative regulation of extrinsic apoptotic signaling pathway via death domain receptors; ISO:RGD. DR GO; GO:0010629; P:negative regulation of gene expression; ISS:AgBase. DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; ISO:RGD. DR GO; GO:0007399; P:nervous system development; IDA:RGD. DR GO; GO:0006334; P:nucleosome assembly; ISO:RGD. DR GO; GO:0051054; P:positive regulation of DNA metabolic process; IMP:RGD. DR GO; GO:0045893; P:positive regulation of DNA-templated transcription; IMP:RGD. DR GO; GO:0001938; P:positive regulation of endothelial cell proliferation; ISO:RGD. DR GO; GO:0045648; P:positive regulation of erythrocyte differentiation; ISO:RGD. DR GO; GO:0010628; P:positive regulation of gene expression; ISS:AgBase. DR GO; GO:0045089; P:positive regulation of innate immune response; ISO:RGD. DR GO; GO:0032728; P:positive regulation of interferon-beta production; ISO:RGD. DR GO; GO:0045654; P:positive regulation of megakaryocyte differentiation; ISO:RGD. DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; ISO:RGD. 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; ISS:UniProtKB. DR GO; GO:0032496; P:response to lipopolysaccharide; ISS:AgBase. DR GO; GO:0048545; P:response to steroid hormone; ISO:RGD. DR GO; GO:0007289; P:spermatid nucleus differentiation; ISO:RGD. DR GO; GO:0007283; P:spermatogenesis; ISO:RGD. 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 2: Evidence at transcript 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_0000048537" 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 51..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 51..76 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 162..172 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 187..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:0000250|UniProtKB:P26583" 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: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" SQ SEQUENCE 210 AA; 24159 MW; 3B5CBAF61415C6F3 CRC64; MGKGDPNKPR GKMSSYAFFV QTCREEHKKK HPDSSVNFAE FSKKCSERWK TMSAKEKSKF EDLAKSDKAR YDREMKNYVP PKGDKKGKKK DPNAPKRPPS AFFLFCSEHR PKIKSEHPGL SIGDTAKKLG EMWSEQSAKD KQPYEQKAAK LKEKYEKDIA AYRAKGKSEV GKKGPGRPTG SKKKNEPEDE EEEEEEEDDE DEEEEDEDEE //