HMGB2_PIG
ID HMGB2_PIG Reviewed; 210 AA.
AC P17741;
DT 01-AUG-1990, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 25-MAY-2022, entry version 144.
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 Sus scrofa (Pig).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Suina; Suidae; Sus.
OX NCBI_TaxID=9823;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Thymus;
RX PubMed=2350545; DOI=10.1021/bi00470a022;
RA Shirakawa H., Tsuda K., Yoshida M.;
RT "Primary structure of non-histone chromosomal protein HMG2 revealed by the
RT nucleotide sequence.";
RL Biochemistry 29:4419-4423(1990).
RN [2]
RP FUNCTION.
RX PubMed=11275566; DOI=10.1093/oxfordjournals.jbchem.a002902;
RA Nakamura Y., Yoshioka K., Shirakawa H., Yoshida M.;
RT "HMG box A in HMG2 protein functions as a mediator of DNA structural
RT alteration together with box B.";
RL J. Biochem. 129:643-651(2001).
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 (PubMed:11275566). Involved in V(D)J
CC recombination by acting as a cofactor of the RAG complex: acts by
CC stimulating cleavage and RAG protein binding at the 23 bp spacer of
CC conserved recombination signal sequences (RSS). Proposed to be involved
CC in the innate immune response to nucleic acids by acting as a
CC cytoplasmic promiscuous immunogenic DNA/RNA sensor which cooperates
CC with subsequent discriminative sensing by specific pattern recognition
CC receptors. In the extracellular compartment acts as a chemokine.
CC Promotes proliferation and migration of endothelial cells implicating
CC AGER/RAGE. Has antimicrobial activity in gastrointestinal epithelial
CC tissues. Involved in inflammatory response to antigenic stimulus
CC coupled with 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:P26583,
CC ECO:0000250|UniProtKB:P30681, ECO:0000269|PubMed:11275566}.
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:P09429,
CC ECO:0000250|UniProtKB:P26583, 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; J02895; AAA31051.1; -; mRNA.
DR PIR; A34719; A34719.
DR RefSeq; NP_999228.1; NM_214063.1.
DR PDB; 1J3C; NMR; -; A=88-165.
DR PDB; 1J3D; NMR; -; A=89-165.
DR PDB; 1J3X; NMR; -; A=1-77.
DR PDBsum; 1J3C; -.
DR PDBsum; 1J3D; -.
DR PDBsum; 1J3X; -.
DR AlphaFoldDB; P17741; -.
DR SMR; P17741; -.
DR STRING; 9823.ENSSSCP00000010363; -.
DR PaxDb; P17741; -.
DR PeptideAtlas; P17741; -.
DR PRIDE; P17741; -.
DR Ensembl; ENSSSCT00005038939; ENSSSCP00005023920; ENSSSCG00005024507.
DR Ensembl; ENSSSCT00015106777; ENSSSCP00015044973; ENSSSCG00015078793.
DR Ensembl; ENSSSCT00025013234; ENSSSCP00025005192; ENSSSCG00025010028.
DR Ensembl; ENSSSCT00030042028; ENSSSCP00030019114; ENSSSCG00030030250.
DR Ensembl; ENSSSCT00035057720; ENSSSCP00035023187; ENSSSCG00035043445.
DR Ensembl; ENSSSCT00040042850; ENSSSCP00040017965; ENSSSCG00040031799.
DR Ensembl; ENSSSCT00045000909; ENSSSCP00045000488; ENSSSCG00045000634.
DR Ensembl; ENSSSCT00050042906; ENSSSCP00050017741; ENSSSCG00050031940.
DR Ensembl; ENSSSCT00060057384; ENSSSCP00060024552; ENSSSCG00060042319.
DR Ensembl; ENSSSCT00065031170; ENSSSCP00065012753; ENSSSCG00065023423.
DR Ensembl; ENSSSCT00070044114; ENSSSCP00070037156; ENSSSCG00070022186.
DR GeneID; 397130; -.
DR KEGG; ssc:397130; -.
DR CTD; 3148; -.
DR eggNOG; KOG0381; Eukaryota.
DR InParanoid; P17741; -.
DR EvolutionaryTrace; P17741; -.
DR Proteomes; UP000008227; Unplaced.
DR Proteomes; UP000314985; Chromosome 14.
DR GO; GO:0000785; C:chromatin; IDA: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; ISS:UniProtKB.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; ISS:UniProtKB.
DR GO; GO:0000987; F:cis-regulatory region sequence-specific DNA binding; ISS:AgBase.
DR GO; GO:0003677; F:DNA binding; IDA:UniProtKB.
DR GO; GO:0008301; F:DNA binding, bending; IDA:UniProtKB.
DR GO; GO:0003690; F:double-stranded DNA binding; IDA:AgBase.
DR GO; GO:0000400; F:four-way junction DNA binding; ISS:AgBase.
DR GO; GO:0044378; F:non-sequence-specific DNA binding, bending; IDA:AgBase.
DR GO; GO:0019904; F:protein domain specific binding; ISS:AgBase.
DR GO; GO:0003697; F:single-stranded DNA binding; IMP:AgBase.
DR GO; GO:0097100; F:supercoiled DNA binding; IDA:AgBase.
DR GO; GO:0008134; F:transcription factor binding; ISS:AgBase.
DR GO; GO:0006935; P:chemotaxis; IEA:UniProtKB-KW.
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:0032392; P:DNA geometric change; ISS:AgBase.
DR GO; GO:0006310; P:DNA recombination; IEA:UniProtKB-KW.
DR GO; GO:0006265; P:DNA topological change; IDA:UniProtKB.
DR GO; GO:0006303; P:double-strand break repair via nonhomologous end joining; IDA:GO_Central.
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; ISS:AgBase.
DR GO; GO:1902042; P:negative regulation of extrinsic apoptotic signaling pathway via death domain receptors; ISS:AgBase.
DR GO; GO:0010629; P:negative regulation of gene expression; ISS:AgBase.
DR GO; GO:0006334; P:nucleosome assembly; IDA:AgBase.
DR GO; GO:0043388; P:positive regulation of DNA binding; ISS:AgBase.
DR GO; GO:1904877; P:positive regulation of DNA ligase activity; IDA:CACAO.
DR GO; GO:0010628; P:positive regulation of gene expression; ISS:AgBase.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; ISS:AgBase.
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; ISS:AgBase.
DR GO; GO:0007289; P:spermatid nucleus differentiation; ISS:AgBase.
DR GO; GO:0007283; P:spermatogenesis; ISS:AgBase.
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 1: Evidence at protein level;
KW 3D-structure; Acetylation; Chemotaxis; Chromosome; Cytoplasm;
KW Disulfide bond; DNA recombination; DNA-binding; Immunity;
KW Inflammatory response; Innate immunity; Nucleus; Oxidation; Phosphoprotein;
KW Reference proteome; Repeat; Secreted; Transcription;
KW Transcription regulation.
FT CHAIN 1..210
FT /note="High mobility group protein B2"
FT /id="PRO_0000048536"
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 52..150
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 52..95
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 133..150
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"
FT STRAND 6..8
FT /evidence="ECO:0007829|PDB:1J3X"
FT HELIX 15..25
FT /evidence="ECO:0007829|PDB:1J3X"
FT HELIX 28..30
FT /evidence="ECO:0007829|PDB:1J3X"
FT HELIX 38..51
FT /evidence="ECO:0007829|PDB:1J3X"
FT HELIX 54..70
FT /evidence="ECO:0007829|PDB:1J3X"
FT TURN 71..74
FT /evidence="ECO:0007829|PDB:1J3X"
FT STRAND 92..94
FT /evidence="ECO:0007829|PDB:1J3C"
FT HELIX 102..116
FT /evidence="ECO:0007829|PDB:1J3C"
FT HELIX 122..135
FT /evidence="ECO:0007829|PDB:1J3C"
FT TURN 139..141
FT /evidence="ECO:0007829|PDB:1J3D"
FT HELIX 147..149
FT /evidence="ECO:0007829|PDB:1J3C"
FT HELIX 152..163
FT /evidence="ECO:0007829|PDB:1J3C"
SQ SEQUENCE 210 AA; 24133 MW; 28FF308D9B341D83 CRC64;
MGKGDPNKPR GKMSSYAFFV QTCREEHKKK HPDSSVNFAE FSKKCSERWK TMSAKEKSKF
EDMAKSDKAR YDREMKNYVP PKGDKKGKKK DPNAPKRPPS AFFLFCSEHR PKIKSEHPGL
SIGDTAKKLG EMWSEQSAKD KQPYEQKAAK LKEKYEKDIA AYRAKGKGEA GKKGPGRPTG
SKKKNEPEDE EEEEEEEEDE DEEEEDEDEE
