HMGB2_RAT
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 03-AUG-2022, entry version 167.
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}.
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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_001329881.1.
DR RefSeq; NP_058883.1; NM_017187.2.
DR RefSeq; XP_017455541.1; XM_017600052.1.
DR AlphaFoldDB; P52925; -.
DR SMR; P52925; -.
DR STRING; 10116.ENSRNOP00000017635; -.
DR iPTMnet; P52925; -.
DR PhosphoSitePlus; P52925; -.
DR jPOST; P52925; -.
DR PaxDb; P52925; -.
DR PRIDE; P52925; -.
DR DNASU; 29395; -.
DR Ensembl; ENSRNOT00000017635; ENSRNOP00000017635; ENSRNOG00000013167.
DR Ensembl; ENSRNOT00000046874; ENSRNOP00000039358; ENSRNOG00000033321.
DR GeneID; 29395; -.
DR GeneID; 498072; -.
DR KEGG; rno:29395; -.
DR KEGG; rno:498072; -.
DR UCSC; RGD:69291; rat.
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; FASAIRP; -.
DR OrthoDB; 1641977at2759; -.
DR PhylomeDB; P52925; -.
DR TreeFam; TF105371; -.
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 tissues.
DR Genevisible; P52925; RN.
DR GO; GO:0000785; C:chromatin; ISS:AgBase.
DR GO; GO:0000793; C:condensed chromosome; ISS:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0005615; C:extracellular space; ISS:AgBase.
DR GO; GO:0005634; C:nucleus; IDA:RGD.
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:0008134; F:transcription factor binding; ISS:AgBase.
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: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: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; 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:0045892; P:negative regulation of transcription, DNA-templated; ISO:RGD.
DR GO; GO:0007399; P:nervous system development; IDA:RGD.
DR GO; GO:0043388; P:positive regulation of DNA binding; ISO:RGD.
DR GO; GO:0051054; P:positive regulation of DNA metabolic process; 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:0032075; P:positive regulation of nuclease activity; ISO:RGD.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; ISO:RGD.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IMP: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 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 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..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: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
