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P30681 (HMGB2_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 128. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
High mobility group protein B2
Alternative name(s):
High mobility group protein 2
Short name=HMG-2
Gene names
Name:Hmgb2
Synonyms:Hmg2
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length210 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

DNA binding proteins that associates with chromatin and has the ability to bend DNA. Binds preferentially single-stranded DNA. 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). Ref.7

Subunit structure

Component of the RAG complex composed of core components RAG1 and RAG2, and associated component HMGB1 or HMGB2. Component of the SET complex, composed of at least ANP32A, APEX1, HMGB2, NME1, SET and TREX1. Directly interacts with SET. Ref.7

Subcellular location

Nucleus. Chromosome.

Sequence similarities

Belongs to the HMGB family.

Contains 2 HMG box DNA-binding domains.

Ontologies

Keywords
   Cellular componentChromosome
Nucleus
   DomainRepeat
   LigandDNA-binding
   PTMAcetylation
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processbase-excision repair, DNA ligation

Inferred from sequence or structural similarity. Source: UniProtKB

cell chemotaxis

Inferred from electronic annotation. Source: Ensembl

cellular response to lipopolysaccharide

Inferred from electronic annotation. Source: Ensembl

male gonad development

Inferred from mutant phenotype PubMed 11262228. Source: MGI

negative regulation of extrinsic apoptotic signaling pathway via death domain receptors

Inferred from mutant phenotype PubMed 19139395. Source: MGI

negative regulation of transcription, DNA-templated

Inferred from electronic annotation. Source: Ensembl

positive regulation of DNA binding

Inferred from direct assay Ref.3. Source: MGI

positive regulation of endothelial cell proliferation

Inferred from electronic annotation. Source: Ensembl

positive regulation of erythrocyte differentiation

Inferred from electronic annotation. Source: Ensembl

positive regulation of megakaryocyte differentiation

Inferred from electronic annotation. Source: Ensembl

positive regulation of nuclease activity

Inferred from electronic annotation. Source: Ensembl

positive regulation of transcription from RNA polymerase II promoter

Inferred from mutant phenotype PubMed 11262228. Source: MGI

regulation of transcription from RNA polymerase II promoter

Inferred from sequence or structural similarity. Source: UniProtKB

response to steroid hormone

Inferred from mutant phenotype PubMed 11262228. Source: MGI

spermatid nucleus differentiation

Inferred from mutant phenotype PubMed 16765935. Source: MGI

spermatogenesis

Inferred from mutant phenotype PubMed 11262228. Source: MGI

   Cellular_componentcondensed chromosome

Inferred from sequence or structural similarity. Source: UniProtKB

cytoplasm

Inferred from sequence or structural similarity. Source: UniProtKB

extracellular space

Inferred from electronic annotation. Source: Ensembl

nucleus

Inferred from sequence or structural similarity. Source: UniProtKB

perinuclear region of cytoplasm

Inferred from sequence or structural similarity. Source: UniProtKB

protein complex

Inferred from electronic annotation. Source: Ensembl

   Molecular_functionDNA binding, bending

Inferred from sequence or structural similarity. Source: UniProtKB

chemoattractant activity

Inferred from electronic annotation. Source: Ensembl

damaged DNA binding

Inferred from electronic annotation. Source: Ensembl

protein domain specific binding

Inferred from physical interaction Ref.3. Source: MGI

sequence-specific DNA binding transcription factor activity

Inferred from electronic annotation. Source: Ensembl

transcription regulatory region DNA binding

Inferred from electronic annotation. Source: Ensembl

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed By similarity
Chain2 – 210209High mobility group protein B2
PRO_0000048535

Regions

DNA binding9 – 7971HMG box 1
DNA binding95 – 16369HMG box 2
Compositional bias186 – 21025Asp/Glu-rich (acidic)

Amino acid modifications

Modified residue301N6-acetyllysine Ref.8
Modified residue1141N6-acetyllysine Ref.8

Experimental info

Sequence conflict71N → I in CAA47900. Ref.1
Sequence conflict101R → L in CAA47900. Ref.1
Sequence conflict331D → N in CAA47900. Ref.1
Sequence conflict411F → I in CAA47900. Ref.1
Sequence conflict471E → K in CAA47900. Ref.1
Sequence conflict571K → N in CAA47900. Ref.1
Sequence conflict70 – 723RYD → CYY in CAA47900. Ref.1
Sequence conflict801P → S in CAA47900. Ref.1
Sequence conflict1031F → C in CAA47900. Ref.1
Sequence conflict1171H → Y in CAA47900. Ref.1
Sequence conflict1401D → E in CAA47900. Ref.1
Sequence conflict1591I → F in CAA47900. Ref.1
Sequence conflict1641A → V in CAA47900. Ref.1
Sequence conflict1791T → A in CAA47900. Ref.1
Sequence conflict184 – 19310KNEPEDEEEE → NDSED in CAA47900. Ref.1
Sequence conflict2021D → E in CAA47900. Ref.1
Sequence conflict2021D → E in AAG36939. Ref.4
Sequence conflict2021D → E in AAH02050. Ref.6
Sequence conflict2041E → G in CAA47900. Ref.1

Sequences

Sequence LengthMass (Da)Tools
P30681 [UniParc].

Last modified January 23, 2007. Version 3.
Checksum: 45D1F667DB4ED94D

FASTA21024,162
        10         20         30         40         50         60 
MGKGDPNKPR GKMSSYAFFV QTCREEHKKK HPDSSVNFAE FSKKCSERWK TMSAKEKSKF 

        70         80         90        100        110        120 
EDLAKSDKAR YDREMKNYVP PKGDKKGKKK DPNAPKRPPS AFFLFCSENR PKIKIEHPGL 

       130        140        150        160        170        180 
SIGDTAKKLG EMWSEQSAKD KQPYEQKAAK LKEKYEKDIA AYRAKGKSEA GKKGPGRPTG 

       190        200        210 
SKKKNEPEDE EEEEEEEEEE DDEEEEEDEE 

« Hide

References

« Hide 'large scale' references
[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].
[4]"Partial male infertility in mice lacking chromosomal protein HMG2."
Ronfani L., Bianchi M.E.
Submitted (MAY-2000) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE.
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. expand/collapse author list , 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/6 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]"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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
CCDSCCDS40343.1.
PIRS26062.
S54774.
RefSeqNP_032278.1. NM_008252.3.
XP_006509587.1. XM_006509524.1.
UniGeneMm.276881.
Mm.279998.

3D structure databases

ProteinModelPortalP30681.
SMRP30681. Positions 1-166.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid220633. 3 interactions.
DIPDIP-899N.
IntActP30681. 3 interactions.
MINTMINT-4097539.

PTM databases

PhosphoSiteP30681.

Proteomic databases

MaxQBP30681.
PaxDbP30681.
PRIDEP30681.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000067925; ENSMUSP00000065940; ENSMUSG00000054717.
GeneID97165.
KEGGmmu:97165.
UCSCuc009lsx.2. mouse.

Organism-specific databases

CTD3148.
MGIMGI:96157. Hmgb2.

Phylogenomic databases

eggNOGCOG5648.
GeneTreeENSGT00730000110464.
HOGENOMHOG000197861.
HOVERGENHBG009000.
InParanoidP30681.
KOK11295.
OMAFCAEHRP.
OrthoDBEOG7WHHBQ.
PhylomeDBP30681.
TreeFamTF105371.

Gene expression databases

BgeeP30681.
CleanExMM_HMGB2.
GenevestigatorP30681.

Family and domain databases

Gene3D1.10.30.10. 2 hits.
InterProIPR009071. HMG_box_dom.
IPR017967. HMG_boxA_CS.
[Graphical view]
PfamPF00505. HMG_box. 1 hit.
PF09011. HMG_box_2. 1 hit.
[Graphical view]
SMARTSM00398. HMG. 2 hits.
[Graphical view]
SUPFAMSSF47095. SSF47095. 2 hits.
PROSITEPS00353. HMG_BOX_1. 1 hit.
PS50118. HMG_BOX_2. 2 hits.
[Graphical view]
ProtoNetSearch...

Other

NextBio352589.
PROP30681.
SOURCESearch...

Entry information

Entry nameHMGB2_MOUSE
AccessionPrimary (citable) accession number: P30681
Secondary accession number(s): Q3UXT1, Q9EQD5
Entry history
Integrated into UniProtKB/Swiss-Prot: April 1, 1993
Last sequence update: January 23, 2007
Last modified: July 9, 2014
This is version 128 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot