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Protein

High mobility group protein B2

Gene

Hmgb2

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Multifunctional protein with various roles in different cellular compartments. May act in a redox sensitive manner. In the nucleus is an abundant chromatin-associated non-histone protein involved in transcription, chromatin remodeling and V(D)J recombination and probably other processes. Binds DNA with a preference to non-canonical DNA structures such as single-stranded DNA. Can bent DNA and enhance DNA flexibility by looping thus providing a mechanism to promote activities on various gene promoters by enhancing transcription factor binding and/or bringing distant regulatory sequences into close proximity (By similarity). Involved in V(D)J recombination by acting as a cofactor of the RAG complex: acts by stimulating cleavage and RAG protein binding at the 23 bp spacer of conserved recombination signal sequences (RSS) (PubMed:9184213). Proposed to be involved in the innate immune response to nucleic acids by acting as a cytoplasmic promiscuous immunogenic DNA/RNA sensor which cooperates with subsequent discriminative sensing by specific pattern recognition receptors (PubMed:19890330). In the extracellular compartment acts as a chemokine. Promotes proliferation and migration of endothelial cells implicating AGER/RAGE (By similarity). Has antimicrobial activity in gastrointestinal epithelial tissues (By similarity). Involved in inflammatory response to antigenic stimulus coupled with proinflammatory activity (PubMed:25306442). May play a role in germ cell differentiation (PubMed:11262228). Involved in modulation of neurogenesis probably by regulation of neural stem proliferation (PubMed:24391977). Involved in articular cartilage surface maintenance implicating LEF1 and the Wnt/beta-catenin pathway (PubMed:19805379).By similarity1 Publication6 Publications

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
DNA bindingi9 – 7971HMG box 1PROSITE-ProRule annotationAdd
BLAST
DNA bindingi95 – 16369HMG box 2PROSITE-ProRule annotationAdd
BLAST

GO - Molecular functioni

GO - Biological processi

  • cell chemotaxis Source: MGI
  • cellular response to lipopolysaccharide Source: Ensembl
  • defense response to Gram-negative bacterium Source: AgBase
  • defense response to Gram-positive bacterium Source: AgBase
  • DNA recombination Source: UniProtKB-KW
  • DNA topological change Source: AgBase
  • inflammatory response to antigenic stimulus Source: AgBase
  • innate immune response Source: UniProtKB-KW
  • male gonad development Source: MGI
  • negative regulation of extrinsic apoptotic signaling pathway via death domain receptors Source: MGI
  • negative regulation of gene expression Source: AgBase
  • negative regulation of transcription, DNA-templated Source: MGI
  • positive chemotaxis Source: MGI
  • positive regulation of DNA binding Source: MGI
  • positive regulation of endothelial cell proliferation Source: MGI
  • positive regulation of erythrocyte differentiation Source: MGI
  • positive regulation of gene expression Source: AgBase
  • positive regulation of innate immune response Source: UniProtKB
  • positive regulation of interferon-beta production Source: UniProtKB
  • positive regulation of megakaryocyte differentiation Source: MGI
  • positive regulation of nuclease activity Source: MGI
  • positive regulation of transcription, DNA-templated Source: MGI
  • positive regulation of transcription from RNA polymerase II promoter Source: MGI
  • regulation of neurogenesis Source: AgBase
  • regulation of stem cell proliferation Source: AgBase
  • regulation of transcription from RNA polymerase II promoter Source: UniProtKB
  • response to lipopolysaccharide Source: AgBase
  • response to steroid hormone Source: MGI
  • spermatid nucleus differentiation Source: MGI
  • spermatogenesis Source: MGI
  • transcription, DNA-templated Source: UniProtKB-KW
Complete GO annotation...

Keywords - Biological processi

Chemotaxis, DNA recombination, Immunity, Inflammatory response, Innate immunity, Transcription, Transcription regulation

Keywords - Ligandi

DNA-binding

Enzyme and pathway databases

ReactomeiR-MMU-211227. Activation of DNA fragmentation factor.

Names & Taxonomyi

Protein namesi
Recommended name:
High mobility group protein B2
Alternative name(s):
High mobility group protein 2
Short name:
HMG-2
Gene namesi
Name:Hmgb2
Synonyms:Hmg2
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 8

Organism-specific databases

MGIiMGI:96157. Hmgb2.

Subcellular locationi

GO - Cellular componenti

  • cell Source: MGI
  • condensed chromosome Source: UniProtKB
  • cytoplasm Source: UniProtKB
  • extracellular space Source: AgBase
  • nuclear chromatin Source: AgBase
  • nucleolus Source: MGI
  • nucleus Source: UniProtKB
  • perinuclear region of cytoplasm Source: UniProtKB
  • protein complex Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Chromosome, Cytoplasm, Nucleus, Secreted

Pathology & Biotechi

Disruption phenotypei

Viable, with severe reduction of sperm production in males.1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methionineiRemovedBy similarity
Chaini2 – 210209High mobility group protein B2PRO_0000048535Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi23 ↔ 45In disulfide HMGB2By similarity
Modified residuei23 – 231Cysteine derivative; cysteine sulfonic acid (-SO(3)H) in sulfonyl HMGB2; alternateBy similarity
Modified residuei30 – 301N6-acetyllysineCombined sources
Modified residuei35 – 351PhosphoserineBy similarity
Modified residuei45 – 451Cysteine derivative; cysteine sulfonic acid (-SO(3)H) in sulfonyl HMGB2; alternateBy similarity
Modified residuei106 – 1061Cysteine derivative; cysteine sulfonic acid (-SO(3)H) in sulfonyl HMGB2By similarity
Modified residuei114 – 1141N6-acetyllysineCombined sources

Post-translational modificationi

Reduction/oxidation of cysteine residues Cys-23, Cys-45 and Cys-106 and a possible intramolecular disulfide bond involving Cys-23 and Cys-45 give rise to different redox forms with specific functional activities in various cellular compartments: 1- fully reduced HMGB2 (HMGB2C23hC45hC106h), 2- disulfide HMGB2 (HMGB2C23-C45C106h) and 3- sulfonyl HMGB2 (HMGB2C23soC45soC106so).By similarity

Keywords - PTMi

Acetylation, Disulfide bond, Phosphoprotein

Proteomic databases

EPDiP30681.
MaxQBiP30681.
PaxDbiP30681.
PeptideAtlasiP30681.
PRIDEiP30681.

PTM databases

iPTMnetiP30681.
PhosphoSiteiP30681.
SwissPalmiP30681.

Expressioni

Tissue specificityi

Widely expressed in embryo. In adult mainly expressed in lymphoid organs and testes (PubMed:11262228). Expressed in primary spermatocytes. Expressed in the superficial zone of articular cartilage (PubMed:19805379).2 Publications

Gene expression databases

BgeeiP30681.
CleanExiMM_HMGB2.
GenevisibleiP30681. MM.

Interactioni

Subunit structurei

Interacts with POU2F2, POU2F1 and POU3F1 (PubMed:7720710). Component of the RAG complex composed of core components RAG1 and RAG2, and associated component HMGB1 or HMGB2 (PubMed:9184213). Component of the SET complex, composed of at least ANP32A, APEX1, HMGB2, NME1, SET and TREX1. Directly interacts with SET (By similarity). Interacts with LEF1 (PubMed:19805379).By similarity3 Publications

GO - Molecular functioni

  • protein domain specific binding Source: MGI
  • RAGE receptor binding Source: MGI
  • transcription factor binding Source: AgBase

Protein-protein interaction databases

BioGridi220633. 3 interactions.
DIPiDIP-899N.
IntActiP30681. 4 interactions.
MINTiMINT-4097539.
STRINGi10090.ENSMUSP00000065940.

Structurei

3D structure databases

ProteinModelPortaliP30681.
SMRiP30681. Positions 1-166.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni165 – 18016Required for chemotactic activityBy similarityAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi186 – 21025Asp/Glu-rich (acidic)Add
BLAST

Domaini

Both, HMG box 1 and HMG box 2, show antimicrobial activity.By similarity

Sequence similaritiesi

Belongs to the HMGB family.Curated
Contains 2 HMG box DNA-binding domains.PROSITE-ProRule annotation

Keywords - Domaini

Repeat

Phylogenomic databases

eggNOGiKOG0381. Eukaryota.
COG5648. LUCA.
GeneTreeiENSGT00760000119164.
HOGENOMiHOG000197861.
HOVERGENiHBG009000.
InParanoidiP30681.
KOiK11295.
OMAiIKNDHPG.
OrthoDBiEOG7WHHBQ.
PhylomeDBiP30681.
TreeFamiTF105371.

Family and domain databases

Gene3Di1.10.30.10. 2 hits.
InterProiIPR009071. HMG_box_dom.
IPR017967. HMG_boxA_CS.
IPR031075. HMGB2.
[Graphical view]
PANTHERiPTHR13711:SF217. PTHR13711:SF217. 1 hit.
PfamiPF00505. HMG_box. 1 hit.
PF09011. HMG_box_2. 1 hit.
[Graphical view]
SMARTiSM00398. HMG. 2 hits.
[Graphical view]
SUPFAMiSSF47095. SSF47095. 2 hits.
PROSITEiPS00353. HMG_BOX_1. 1 hit.
PS50118. HMG_BOX_2. 2 hits.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P30681-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MGKGDPNKPR GKMSSYAFFV QTCREEHKKK HPDSSVNFAE FSKKCSERWK
60 70 80 90 100
TMSAKEKSKF EDLAKSDKAR YDREMKNYVP PKGDKKGKKK DPNAPKRPPS
110 120 130 140 150
AFFLFCSENR PKIKIEHPGL SIGDTAKKLG EMWSEQSAKD KQPYEQKAAK
160 170 180 190 200
LKEKYEKDIA AYRAKGKSEA GKKGPGRPTG SKKKNEPEDE EEEEEEEEEE
210
DDEEEEEDEE
Length:210
Mass (Da):24,162
Last modified:January 23, 2007 - v3
Checksum:i45D1F667DB4ED94D
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti7 – 71N → I in CAA47900 (PubMed:1408807).Curated
Sequence conflicti10 – 101R → L in CAA47900 (PubMed:1408807).Curated
Sequence conflicti33 – 331D → N in CAA47900 (PubMed:1408807).Curated
Sequence conflicti41 – 411F → I in CAA47900 (PubMed:1408807).Curated
Sequence conflicti47 – 471E → K in CAA47900 (PubMed:1408807).Curated
Sequence conflicti57 – 571K → N in CAA47900 (PubMed:1408807).Curated
Sequence conflicti70 – 723RYD → CYY in CAA47900 (PubMed:1408807).Curated
Sequence conflicti80 – 801P → S in CAA47900 (PubMed:1408807).Curated
Sequence conflicti103 – 1031F → C in CAA47900 (PubMed:1408807).Curated
Sequence conflicti117 – 1171H → Y in CAA47900 (PubMed:1408807).Curated
Sequence conflicti140 – 1401D → E in CAA47900 (PubMed:1408807).Curated
Sequence conflicti159 – 1591I → F in CAA47900 (PubMed:1408807).Curated
Sequence conflicti164 – 1641A → V in CAA47900 (PubMed:1408807).Curated
Sequence conflicti179 – 1791T → A in CAA47900 (PubMed:1408807).Curated
Sequence conflicti184 – 19310KNEPEDEEEE → NDSED in CAA47900 (PubMed:1408807).Curated
Sequence conflicti202 – 2021D → E in CAA47900 (PubMed:1408807).Curated
Sequence conflicti202 – 2021D → E in AAG36939 (PubMed:11262228).Curated
Sequence conflicti202 – 2021D → E in AAH02050 (PubMed:15489334).Curated
Sequence conflicti204 – 2041E → G in CAA47900 (PubMed:1408807).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X67668 mRNA. Translation: CAA47900.1.
Z46757 mRNA. Translation: CAA86727.1.
AF267733 Genomic DNA. Translation: AAG36939.1.
AK003773 mRNA. Translation: BAB22988.1.
AK008443 mRNA. Translation: BAB25672.1.
AK012568 mRNA. Translation: BAB28323.1.
AK135296 mRNA. Translation: BAE22481.1.
AK135297 mRNA. Translation: BAE22482.1.
AK146212 mRNA. Translation: BAE26982.1.
BC002050 mRNA. Translation: AAH02050.1.
BC046759 mRNA. Translation: AAH46759.1.
BC083108 mRNA. Translation: AAH83108.1.
CCDSiCCDS40343.1.
PIRiS26062.
S54774.
RefSeqiNP_032278.1. NM_008252.3.
XP_006509587.1. XM_006509524.2.
UniGeneiMm.276881.
Mm.279998.

Genome annotation databases

EnsembliENSMUST00000067925; ENSMUSP00000065940; ENSMUSG00000054717.
GeneIDi97165.
KEGGimmu:97165.
UCSCiuc009lsx.2. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X67668 mRNA. Translation: CAA47900.1.
Z46757 mRNA. Translation: CAA86727.1.
AF267733 Genomic DNA. Translation: AAG36939.1.
AK003773 mRNA. Translation: BAB22988.1.
AK008443 mRNA. Translation: BAB25672.1.
AK012568 mRNA. Translation: BAB28323.1.
AK135296 mRNA. Translation: BAE22481.1.
AK135297 mRNA. Translation: BAE22482.1.
AK146212 mRNA. Translation: BAE26982.1.
BC002050 mRNA. Translation: AAH02050.1.
BC046759 mRNA. Translation: AAH46759.1.
BC083108 mRNA. Translation: AAH83108.1.
CCDSiCCDS40343.1.
PIRiS26062.
S54774.
RefSeqiNP_032278.1. NM_008252.3.
XP_006509587.1. XM_006509524.2.
UniGeneiMm.276881.
Mm.279998.

3D structure databases

ProteinModelPortaliP30681.
SMRiP30681. Positions 1-166.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi220633. 3 interactions.
DIPiDIP-899N.
IntActiP30681. 4 interactions.
MINTiMINT-4097539.
STRINGi10090.ENSMUSP00000065940.

PTM databases

iPTMnetiP30681.
PhosphoSiteiP30681.
SwissPalmiP30681.

Proteomic databases

EPDiP30681.
MaxQBiP30681.
PaxDbiP30681.
PeptideAtlasiP30681.
PRIDEiP30681.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000067925; ENSMUSP00000065940; ENSMUSG00000054717.
GeneIDi97165.
KEGGimmu:97165.
UCSCiuc009lsx.2. mouse.

Organism-specific databases

CTDi3148.
MGIiMGI:96157. Hmgb2.

Phylogenomic databases

eggNOGiKOG0381. Eukaryota.
COG5648. LUCA.
GeneTreeiENSGT00760000119164.
HOGENOMiHOG000197861.
HOVERGENiHBG009000.
InParanoidiP30681.
KOiK11295.
OMAiIKNDHPG.
OrthoDBiEOG7WHHBQ.
PhylomeDBiP30681.
TreeFamiTF105371.

Enzyme and pathway databases

ReactomeiR-MMU-211227. Activation of DNA fragmentation factor.

Miscellaneous databases

PROiP30681.
SOURCEiSearch...

Gene expression databases

BgeeiP30681.
CleanExiMM_HMGB2.
GenevisibleiP30681. MM.

Family and domain databases

Gene3Di1.10.30.10. 2 hits.
InterProiIPR009071. HMG_box_dom.
IPR017967. HMG_boxA_CS.
IPR031075. HMGB2.
[Graphical view]
PANTHERiPTHR13711:SF217. PTHR13711:SF217. 1 hit.
PfamiPF00505. HMG_box. 1 hit.
PF09011. HMG_box_2. 1 hit.
[Graphical view]
SMARTiSM00398. HMG. 2 hits.
[Graphical view]
SUPFAMiSSF47095. SSF47095. 2 hits.
PROSITEiPS00353. HMG_BOX_1. 1 hit.
PS50118. HMG_BOX_2. 2 hits.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Nucleotide sequence of a mouse cDNA encoding the non-histone chromosomal high mobility group protein-2 (HMG-2)."
    Stolzenburg F., Dinkl E., Grummt F.
    Nucleic Acids Res. 20:4927-4927(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Strain: PCC4.
  2. Stolzenburg F.
    Submitted (SEP-1992) to the EMBL/GenBank/DDBJ databases
    Cited for: SEQUENCE REVISION.
  3. "High mobility group protein 2 functionally interacts with the POU domains of octamer transcription factors."
    Zwilling S., Koenig H., Wirth T.
    EMBO J. 14:1198-1208(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, INTERACTION WITH POU2F2; POU2F1 AND POU3F1.
  4. "Reduced fertility and spermatogenesis defects in mice lacking chromosomal protein Hmgb2."
    Ronfani L., Ferraguti M., Croci L., Ovitt C.E., Schoeler H.R., Consalez G.G., Bianchi M.E.
    Development 128:1265-1273(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE, FUNCTION, TISSUE SPECIFICITY, DISRUPTION PHENOTYPE.
    Strain: 129/Sv.
  5. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: C57BL/6J and DBA/2.
    Tissue: Small intestine and Wolffian duct.
  6. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: C57BL/6J and FVB/N.
    Tissue: Brain and Mammary gland.
  7. "Stimulation of V(D)J cleavage by high mobility group proteins."
    van Gent D.C., Hiom K., Paull T.T., Gellert M.
    EMBO J. 16:2665-2670(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, IDENTIFICATION IN THE RAG COMPLEX.
  8. Cited for: FUNCTION, SUBCELLULAR LOCATION.
  9. "Chromatin protein HMGB2 regulates articular cartilage surface maintenance via beta-catenin pathway."
    Taniguchi N., Carames B., Kawakami Y., Amendt B.A., Komiya S., Lotz M.
    Proc. Natl. Acad. Sci. U.S.A. 106:16817-16822(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH LEF1, TISSUE SPECIFICITY.
  10. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas, Spleen and Testis.
  11. "SIRT5-mediated lysine desuccinylation impacts diverse metabolic pathways."
    Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y., Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.
    Mol. Cell 50:919-930(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-30 AND LYS-114, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Embryonic fibroblast.
  12. "Aberrant neural stem cell proliferation and increased adult neurogenesis in mice lacking chromatin protein HMGB2."
    Abraham A.B., Bronstein R., Reddy A.S., Maletic-Savatic M., Aguirre A., Tsirka S.E.
    PLoS ONE 8:E84838-E84838(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  13. "Oct4 interaction with Hmgb2 regulates Akt signaling and pluripotency."
    Campbell P.A., Rudnicki M.A.
    Stem Cells 31:1107-1120(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  14. "A small molecule binding HMGB1 and HMGB2 inhibits microglia-mediated neuroinflammation."
    Lee S., Nam Y., Koo J.Y., Lim D., Park J., Ock J., Kim J., Suk K., Park S.B.
    Nat. Chem. Biol. 10:1055-1060(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.

Entry informationi

Entry nameiHMGB2_MOUSE
AccessioniPrimary (citable) accession number: P30681
Secondary accession number(s): Q3UXT1, Q9EQD5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 1, 1993
Last sequence update: January 23, 2007
Last modified: July 6, 2016
This is version 148 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.