ID HMGB3_MOUSE Reviewed; 200 AA. AC O54879; DT 27-MAR-2002, integrated into UniProtKB/Swiss-Prot. DT 23-JAN-2007, sequence version 3. DT 27-MAR-2024, entry version 177. DE RecName: Full=High mobility group protein B3; DE AltName: Full=High mobility group protein 2a; DE Short=HMG-2a; DE AltName: Full=High mobility group protein 4; DE Short=HMG-4; GN Name=Hmgb3; Synonyms=Hmg2a, Hmg4; 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=129/Sv; RX PubMed=9598312; DOI=10.1006/geno.1998.5214; RA Vaccari T., Beltrame M., Ferrari S., Bianchi M.E.; RT "Hmg4, a new member of the Hmg1/2 gene family."; RL Genomics 49:247-252(1998). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=C57BL/6J; TISSUE=Eye; 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 [3] RP FUNCTION, AND TISSUE SPECIFICITY. RX PubMed=12714519; DOI=10.1182/blood-2002-11-3541; RA Nemeth M.J., Curtis D.J., Kirby M.R., Garrett-Beal L.J., Seidel N.E., RA Cline A.P., Bodine D.M.; RT "Hmgb3: an HMG-box family member expressed in primitive hematopoietic cells RT that inhibits myeloid and B-cell differentiation."; RL Blood 102:1298-1306(2003). RN [4] RP FUNCTION. RX PubMed=15358624; DOI=10.1182/blood-2004-07-2551; RA Nemeth M.J., Cline A.P., Anderson S.M., Garrett-Beal L.J., Bodine D.M.; RT "Hmgb3 deficiency deregulates proliferation and differentiation of common RT lymphoid and myeloid progenitors."; RL Blood 105:627-634(2005). RN [5] 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 [6] RP FUNCTION. RX PubMed=16945912; DOI=10.1073/pnas.0604006103; RA Nemeth M.J., Kirby M.R., Bodine D.M.; RT "Hmgb3 regulates the balance between hematopoietic stem cell self-renewal RT and differentiation."; RL Proc. Natl. Acad. Sci. U.S.A. 103:13783-13788(2006). RN [7] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Lung, Pancreas, RC 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). CC -!- FUNCTION: Multifunctional protein with various roles in different CC cellular compartments. May act in a redox sensitive manner. Associates CC with chromatin and binds DNA with a preference for non-canonical DNA CC structures such as single-stranded DNA. Can bend DNA and enhance DNA CC flexibility by looping thus providing a mechanism to promote activities CC on various gene promoters (By similarity). Proposed to be involved in CC the innate immune response to nucleic acids by acting as a cytoplasmic CC promiscuous immunogenic DNA/RNA sensor (PubMed:19890330). Negatively CC regulates B-cell and myeloid cell differentiation. In hematopoietic CC stem cells may regulate the balance between self-renewal and CC differentiation. Involved in negative regulation of canonical Wnt CC signaling (PubMed:12714519, PubMed:15358624, PubMed:16945912). CC {ECO:0000250|UniProtKB:P09429, ECO:0000250|UniProtKB:P40618, CC ECO:0000269|PubMed:12714519, ECO:0000269|PubMed:15358624, CC ECO:0000269|PubMed:16945912, ECO:0000269|PubMed:19890330}. CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:P40618, CC ECO:0000255|PROSITE-ProRule:PRU00267}. Chromosome {ECO:0000305}. CC Cytoplasm {ECO:0000269|PubMed:19890330}. CC -!- TISSUE SPECIFICITY: Expressed in bone marrow cells, specifically in CC primitive Lin-, c-kit+, Sca-1+, IL-7Ralpha- cells, and Ter119+ CC erythroid cells (PubMed:12714519). {ECO:0000269|PubMed:12714519}. CC -!- DEVELOPMENTAL STAGE: Highly expressed in the embryo; barely detectable CC in the adult stage. CC -!- PTM: Reduction/oxidation of cysteine residues Cys-23, Cys-45 and Cys- CC 104 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 HMGB3 CC (HMGB3C23hC45hC104h), 2- disulfide HMGB3 (HMGB3C23-C45C104h) and CC 3- sulfonyl HMGB3 (HMGB3C23soC45soC104so). 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; AF022465; AAC16925.1; -; mRNA. DR EMBL; BC011276; AAH11276.1; -; mRNA. DR EMBL; BC083352; AAH83352.1; -; mRNA. DR CCDS; CCDS30180.1; -. DR RefSeq; NP_001280552.1; NM_001293623.1. DR RefSeq; NP_001280553.1; NM_001293624.1. DR RefSeq; NP_001280554.1; NM_001293625.1. DR RefSeq; NP_032279.1; NM_008253.4. DR RefSeq; XP_006527905.1; XM_006527842.3. DR AlphaFoldDB; O54879; -. DR SMR; O54879; -. DR BioGRID; 200336; 5. DR STRING; 10090.ENSMUSP00000110229; -. DR iPTMnet; O54879; -. DR PhosphoSitePlus; O54879; -. DR EPD; O54879; -. DR jPOST; O54879; -. DR PaxDb; 10090-ENSMUSP00000110229; -. DR PeptideAtlas; O54879; -. DR ProteomicsDB; 273116; -. DR Pumba; O54879; -. DR Antibodypedia; 17019; 343 antibodies from 36 providers. DR DNASU; 15354; -. DR Ensembl; ENSMUST00000015361.11; ENSMUSP00000015361.5; ENSMUSG00000015217.12. DR Ensembl; ENSMUST00000072699.13; ENSMUSP00000110232.3; ENSMUSG00000015217.12. DR Ensembl; ENSMUST00000088874.10; ENSMUSP00000086260.4; ENSMUSG00000015217.12. DR Ensembl; ENSMUST00000114582.9; ENSMUSP00000110229.3; ENSMUSG00000015217.12. DR GeneID; 15354; -. DR KEGG; mmu:15354; -. DR UCSC; uc009tkb.2; mouse. DR AGR; MGI:1098219; -. DR CTD; 3149; -. DR MGI; MGI:1098219; Hmgb3. DR VEuPathDB; HostDB:ENSMUSG00000015217; -. DR eggNOG; KOG0381; Eukaryota. DR GeneTree; ENSGT00940000153299; -. DR InParanoid; O54879; -. DR OMA; HEKERFN; -. DR OrthoDB; 1222485at2759; -. DR PhylomeDB; O54879; -. DR TreeFam; TF105371; -. DR BioGRID-ORCS; 15354; 9 hits in 46 CRISPR screens. DR ChiTaRS; Hmgb3; mouse. DR PRO; PR:O54879; -. DR Proteomes; UP000000589; Chromosome X. DR RNAct; O54879; Protein. DR Bgee; ENSMUSG00000015217; Expressed in ventricular zone and 87 other cell types or tissues. DR ExpressionAtlas; O54879; baseline and differential. DR GO; GO:0005694; C:chromosome; IEA:UniProtKB-SubCell. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005634; C:nucleus; IDA:MGI. DR GO; GO:0003677; F:DNA binding; IDA:UniProtKB. DR GO; GO:0008301; F:DNA binding, bending; ISS:AgBase. DR GO; GO:0000400; F:four-way junction DNA binding; ISS:AgBase. DR GO; GO:0003723; F:RNA binding; IDA:UniProtKB. DR GO; GO:0032392; P:DNA geometric change; ISS:AgBase. DR GO; GO:0045087; P:innate immune response; IEA:UniProtKB-KW. DR GO; GO:0045578; P:negative regulation of B cell differentiation; IDA:MGI. DR GO; GO:0045638; P:negative regulation of myeloid cell differentiation; IDA:MGI. DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central. 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:SF14; HIGH MOBILITY GROUP PROTEIN B3; 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; O54879; MM. PE 1: Evidence at protein level; KW Acetylation; Chromosome; Cytoplasm; Disulfide bond; DNA-binding; Immunity; KW Innate immunity; Nucleus; Oxidation; Phosphoprotein; Reference proteome; KW Repeat; Transcription; Transcription regulation. FT CHAIN 1..200 FT /note="High mobility group protein B3" FT /id="PRO_0000048540" FT DNA_BIND 9..79 FT /note="HMG box 1" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00267" FT DNA_BIND 93..161 FT /note="HMG box 2" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00267" FT REGION 71..97 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 161..200 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 71..93 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 161..181 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 182..200 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:P09429" 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 98 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:P09429" FT MOD_RES 104 FT /note="Cysteine sulfonic acid (-SO3H)" FT /evidence="ECO:0000250|UniProtKB:P63159" FT MOD_RES 112 FT /note="N6-acetyllysine" FT /evidence="ECO:0000250|UniProtKB:P30681" FT MOD_RES 139 FT /note="N6-acetyllysine" FT /evidence="ECO:0000250|UniProtKB:P63158" FT DISULFID 23..45 FT /note="In disulfide HMGB3; alternate" FT /evidence="ECO:0000250|UniProtKB:P63159" SQ SEQUENCE 200 AA; 23010 MW; 34A45470D4F1B1FB CRC64; MAKGDPKKPK GKMSAYAFFV QTCREEHKKK NPEVPVNFAE FSKKCSERWK TMSSKEKSKF DEMAKADKVR YDREMKDYGP AKGGKKKKDP NAPKRPPSGF FLFCSEFRPK IKSTNPGISI GDVAKKLGEM WNNLSDNEKQ PYVTKAAKLK EKYEKDVADY KSKGKFDGAK GPAKVARKKV EEEEEEEEEE EEEEEEEEDE //