HMGB3_MOUSE
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 03-AUG-2022, entry version 168.
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, Spleen,
RC 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 to non-canonical DNA
CC structures such as single-stranded DNA. Can bent 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}.
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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; 4.
DR STRING; 10090.ENSMUSP00000110229; -.
DR iPTMnet; O54879; -.
DR PhosphoSitePlus; O54879; -.
DR EPD; O54879; -.
DR jPOST; O54879; -.
DR PaxDb; O54879; -.
DR PeptideAtlas; O54879; -.
DR PRIDE; O54879; -.
DR ProteomicsDB; 273116; -.
DR Antibodypedia; 17019; 306 antibodies from 36 providers.
DR DNASU; 15354; -.
DR Ensembl; ENSMUST00000015361; ENSMUSP00000015361; ENSMUSG00000015217.
DR Ensembl; ENSMUST00000072699; ENSMUSP00000110232; ENSMUSG00000015217.
DR Ensembl; ENSMUST00000088874; ENSMUSP00000086260; ENSMUSG00000015217.
DR Ensembl; ENSMUST00000114582; ENSMUSP00000110229; ENSMUSG00000015217.
DR GeneID; 15354; -.
DR KEGG; mmu:15354; -.
DR UCSC; uc009tkb.2; mouse.
DR CTD; 3149; -.
DR MGI; MGI:1098219; Hmgb3.
DR VEuPathDB; HostDB:ENSMUSG00000015217; -.
DR eggNOG; KOG0381; Eukaryota.
DR GeneTree; ENSGT00940000153299; -.
DR InParanoid; O54879; -.
DR OMA; DMKNTEL; -.
DR OrthoDB; 1641977at2759; -.
DR PhylomeDB; O54879; -.
DR TreeFam; TF105371; -.
DR BioGRID-ORCS; 15354; 9 hits in 40 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 85 other tissues.
DR ExpressionAtlas; O54879; baseline and differential.
DR Genevisible; O54879; MM.
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 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 InterPro; IPR031077; HMGB3.
DR PANTHER; PTHR48112:SF14; PTHR48112:SF14; 1.
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 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
