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P26583 (HMGB2_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 148. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | 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
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length209 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) By similarity.

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.8

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_processDNA ligation involved in DNA repair

Inferred from sequence or structural similarity. Source: UniProtKB

DNA topological change

Inferred from sequence or structural similarity. Source: UniProtKB

V(D)J recombination

Inferred from sequence or structural similarity. Source: UniProtKB

apoptotic DNA fragmentation

Traceable author statement. Source: Reactome

apoptotic process

Traceable author statement. Source: Reactome

base-excision repair, DNA ligation

Inferred from direct assay PubMed 9600082. Source: UniProtKB

cell chemotaxis

Inferred from direct assay PubMed 19811285. Source: UniProtKB

cellular component disassembly involved in execution phase of apoptosis

Traceable author statement. Source: Reactome

cellular response to lipopolysaccharide

Inferred from expression pattern PubMed 19811285. Source: UniProtKB

chromatin organization

Non-traceable author statement Ref.8PubMed 15504738. Source: UniProtKB

male gonad development

Inferred from electronic annotation. Source: Ensembl

negative regulation of extrinsic apoptotic signaling pathway via death domain receptors

Inferred from electronic annotation. Source: Ensembl

negative regulation of transcription, DNA-templated

Inferred from direct assay PubMed 9636147. Source: BHF-UCL

nucleosome assembly

Non-traceable author statement Ref.8. Source: UniProtKB

phosphatidylinositol-mediated signaling

Non-traceable author statement PubMed 15504738. Source: UniProtKB

positive chemotaxis

Inferred from direct assay PubMed 19811285. Source: GOC

positive regulation of DNA binding

Inferred from direct assay PubMed 19965638. Source: UniProtKB

positive regulation of endothelial cell proliferation

Inferred from direct assay PubMed 19811285. Source: UniProtKB

positive regulation of erythrocyte differentiation

Inferred from mutant phenotype PubMed 19965638. Source: UniProtKB

positive regulation of megakaryocyte differentiation

Inferred from mutant phenotype PubMed 19965638. Source: UniProtKB

positive regulation of nuclease activity

Inferred from direct assay PubMed 978439. Source: UniProtKB

positive regulation of transcription from RNA polymerase II promoter

Inferred from direct assay PubMed 19223331PubMed 19965638. Source: UniProtKB

positive regulation of transcription, DNA-templated

Inferred from direct assay PubMed 19965638. Source: UniProtKB

regulation of transcription from RNA polymerase II promoter

Inferred from direct assay PubMed 7797075. Source: UniProtKB

response to steroid hormone

Inferred from electronic annotation. Source: Ensembl

spermatid nucleus differentiation

Inferred from electronic annotation. Source: Ensembl

   Cellular_componentcondensed chromosome

Inferred from direct assay PubMed 12925773. Source: UniProtKB

cytoplasm

Inferred from direct assay Ref.8. Source: UniProtKB

extracellular space

Inferred from direct assay PubMed 19811285. Source: UniProtKB

nucleoplasm

Traceable author statement. Source: Reactome

nucleus

Inferred from direct assay Ref.8PubMed 8339930. Source: UniProtKB

perinuclear region of cytoplasm

Inferred from direct assay Ref.8. Source: UniProtKB

protein complex

Inferred from direct assay Ref.8. Source: UniProtKB

   Molecular_functionDNA binding

Inferred from mutant phenotype Ref.8. Source: UniProtKB

DNA binding, bending

Inferred from direct assay Ref.8PubMed 8339930. Source: UniProtKB

RAGE receptor binding

Inferred from genetic interaction PubMed 19811285. Source: UniProtKB

chemoattractant activity

Inferred from direct assay PubMed 19811285. Source: UniProtKB

damaged DNA binding

Inferred from direct assay PubMed 8226934. Source: UniProtKB

double-stranded DNA binding

Inferred from sequence or structural similarity. Source: UniProtKB

poly(A) RNA binding

Inferred from direct assay PubMed 22658674PubMed 22681889. Source: UniProtKB

protein binding

Inferred from physical interaction Ref.8. Source: UniProtKB

sequence-specific DNA binding transcription factor activity

Inferred from direct assay PubMed 19223331. Source: UniProtKB

single-stranded DNA binding

Inferred from sequence or structural similarity. Source: UniProtKB

transcription regulatory region DNA binding

Inferred from direct assay PubMed 19965638. Source: UniProtKB

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed By similarity
Chain2 – 209208High mobility group protein B2
PRO_0000048534

Regions

DNA binding9 – 7971HMG box 1
DNA binding95 – 16369HMG box 2
Compositional bias186 – 20924Asp/Glu-rich (acidic)

Amino acid modifications

Modified residue301N6-acetyllysine Ref.9
Modified residue1141N6-acetyllysine By similarity

Experimental info

Sequence conflict1631R → G in CAA78938. Ref.7

Sequences

Sequence LengthMass (Da)Tools
P26583 [UniParc].

Last modified January 23, 2007. Version 2.
Checksum: 5E65292BC4AD8373

FASTA20924,034
        10         20         30         40         50         60 
MGKGDPNKPR GKMSSYAFFV QTCREEHKKK HPDSSVNFAE FSKKCSERWK TMSAKEKSKF 

        70         80         90        100        110        120 
EDMAKSDKAR YDREMKNYVP PKGDKKGKKK DPNAPKRPPS AFFLFCSEHR PKIKSEHPGL 

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

       190        200 
SKKKNEPEDE EEEEEEEDED EEEEDEDEE 

« Hide

References

« Hide 'large scale' references
[1]"Sequence of human HMG2 cDNA."
Majumdar A., Brown D., Kerby S., Rudzinski I., Polte T., Randawa Z., Seidman M.M.
Nucleic Acids Res. 19:6643-6643(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]"Structure of a gene coding for human HMG2 protein."
Shirakawa H., Yoshida M.
J. Biol. Chem. 267:6641-6645(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[3]"Cloning of human full-length CDSs in BD Creator(TM) system donor vector."
Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., Phelan M., Farmer A.
Submitted (OCT-2004) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[4]"Complete sequencing and characterization of 21,243 full-length human cDNAs."
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. expand/collapse author list , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Brain.
[5]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[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].
Tissue: Placenta and Skin.
[7]"A human HMG2 cDNA with a novel 3'-untranslated region."
Alexandre S., Li W.W., Lee A.S.
Nucleic Acids Res. 20:6413-6413(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 24-209.
[8]"HMG2 interacts with the nucleosome assembly protein SET and is a target of the cytotoxic T-lymphocyte protease granzyme A."
Fan Z., Beresford P.J., Zhang D., Lieberman J.
Mol. Cell. Biol. 22:2810-2820(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION IN THE SET COMPLEX, INTERACTION WITH SET.
[9]"Lysine acetylation targets protein complexes and co-regulates major cellular functions."
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M.
Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-30, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[10]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[11]"N-terminal acetylome analyses and functional insights of the N-terminal acetyltransferase NatB."
Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A., Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M83665 Genomic DNA. Translation: AAA58659.1.
X62534 mRNA. Translation: CAA44395.1.
BT019782 mRNA. Translation: AAV38585.1.
AK311864 mRNA. Translation: BAG34805.1.
CH471056 Genomic DNA. Translation: EAX04758.1.
CH471056 Genomic DNA. Translation: EAX04759.1.
BC001063 mRNA. Translation: AAH01063.1.
BC100019 mRNA. Translation: AAI00020.1.
Z17240 mRNA. Translation: CAA78938.1.
CCDSCCDS3816.1.
PIRNSHUH2. A42425.
S30221.
RefSeqNP_001124160.1. NM_001130688.1.
NP_001124161.1. NM_001130689.1.
NP_002120.1. NM_002129.3.
UniGeneHs.434953.

3D structure databases

ProteinModelPortalP26583.
SMRP26583. Positions 1-166.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid109391. 29 interactions.
IntActP26583. 6 interactions.
MINTMINT-240190.
STRING9606.ENSP00000296503.

PTM databases

PhosphoSiteP26583.

Polymorphism databases

DMDM123374.

Proteomic databases

MaxQBP26583.
PaxDbP26583.
PeptideAtlasP26583.
PRIDEP26583.

Protocols and materials databases

DNASU3148.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000296503; ENSP00000296503; ENSG00000164104.
ENST00000438704; ENSP00000404912; ENSG00000164104.
ENST00000446922; ENSP00000393448; ENSG00000164104.
GeneID3148.
KEGGhsa:3148.
UCSCuc003ita.3. human.

Organism-specific databases

CTD3148.
GeneCardsGC04M174252.
HGNCHGNC:5000. HMGB2.
HPAHPA003506.
MIM163906. gene.
neXtProtNX_P26583.
PharmGKBPA35091.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG5648.
HOGENOMHOG000197861.
HOVERGENHBG009000.
InParanoidP26583.
KOK11295.
OMAFCAEHRP.
OrthoDBEOG7WHHBQ.
PhylomeDBP26583.
TreeFamTF105371.

Enzyme and pathway databases

ReactomeREACT_578. Apoptosis.

Gene expression databases

ArrayExpressP26583.
BgeeP26583.
CleanExHS_HMGB2.
GenevestigatorP26583.

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

ChiTaRSHMGB2. human.
GeneWikiHMGB2.
GenomeRNAi3148.
NextBio12476.
PMAP-CutDBP26583.
PROP26583.
SOURCESearch...

Entry information

Entry nameHMGB2_HUMAN
AccessionPrimary (citable) accession number: P26583
Secondary accession number(s): B2R4K8, D3DP37, Q5U072
Entry history
Integrated into UniProtKB/Swiss-Prot: August 1, 1992
Last sequence update: January 23, 2007
Last modified: July 9, 2014
This is version 148 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Relevant documents

SIMILARITY comments

Index of protein domains and families

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human chromosome 4

Human chromosome 4: entries, gene names and cross-references to MIM