P26583 (HMGB2_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
High mobility group protein B2

Alternative name(s):
High mobility group protein 2
Short name=HMG-2

Gene names

Name:	HMGB2
Synonyms:	HMG2

Organism

Homo sapiens (Human)

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length	209 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence 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 By similarity. Component of the SET complex, which also contains SET, ANP32A, APEX1 and NME1. 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 component	Chromosome Nucleus
Domain	Repeat
Ligand	DNA-binding
PTM	Acetylation Phosphoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological process	DNA fragmentation involved in apoptotic nuclear change Traceable author statement. Source: Reactome DNA topological change Inferred from sequence or structural similarity. Source: UniProtKB V(D)J recombination Inferred from sequence or structural similarity. Source: UniProtKB base-excision repair, DNA ligation Inferred from direct assay. Source: UniProtKB cell chemotaxis Inferred from direct assay. Source: UniProtKB cellular response to lipopolysaccharide Inferred from expression pattern. Source: UniProtKB negative regulation of transcription, DNA-dependent Inferred from direct assay. Source: BHF-UCL nucleosome assembly Non-traceable author statement Ref.8. Source: UniProtKB phosphatidylinositol-mediated signaling Non-traceable author statement. Source: UniProtKB positive regulation of DNA binding Inferred from direct assay. Source: UniProtKB positive regulation of endothelial cell proliferation Inferred from direct assay. Source: UniProtKB positive regulation of erythrocyte differentiation Inferred from mutant phenotype. Source: UniProtKB positive regulation of megakaryocyte differentiation Inferred from mutant phenotype. Source: UniProtKB positive regulation of nuclease activity Inferred from direct assay. Source: UniProtKB positive regulation of transcription from RNA polymerase II promoter Inferred from direct assay. Source: UniProtKB
Cellular component	condensed chromosome Inferred from direct assay. Source: UniProtKB extracellular space Inferred from direct assay. Source: UniProtKB nucleolus Inferred from direct assay. Source: HPA nucleoplasm Traceable author statement. Source: Reactome perinuclear region of cytoplasm Inferred from direct assay Ref.8. Source: UniProtKB protein complex Inferred from direct assay Ref.8. Source: UniProtKB
Molecular function	DNA binding, bending Inferred from direct assay Ref.8. Source: UniProtKB RAGE receptor binding Inferred from genetic interaction. Source: UniProtKB chemoattractant activity Inferred from direct assay. Source: UniProtKB damaged DNA binding Inferred from direct assay. Source: UniProtKB double-stranded DNA binding Inferred from sequence or structural similarity. Source: UniProtKB sequence-specific DNA binding transcription factor activity Inferred from direct assay. Source: UniProtKB single-stranded DNA binding Inferred from sequence or structural similarity. Source: UniProtKB transcription regulatory region DNA binding Inferred from direct assay. Source: UniProtKB
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Initiator methionine	1	1	Removed By similarity
	Chain	2 – 209	208	High mobility group protein B2		PRO_0000048534
Regions
	DNA binding	9 – 79	71	HMG box 1
	DNA binding	95 – 163	69	HMG box 2
	Compositional bias	186 – 209	24	Asp/Glu-rich (acidic)
Amino acid modifications
	Modified residue	30	1	N6-acetyllysine Ref.10
	Modified residue	35	1	Phosphoserine Ref.9
	Modified residue	59	1	N6-acetyllysine Ref.10
	Modified residue	155	1	Phosphotyrosine Ref.9
	Modified residue	162	1	Phosphotyrosine Ref.9
	Modified residue	172	1	N6-acetyllysine Ref.10
	Modified residue	173	1	N6-acetyllysine Ref.10
Experimental info
	Sequence conflict	163	1	R → G in CAA78938. Ref.7

Sequences

	Sequence		Length	Mass (Da)
	P26583 [UniParc]. Last modified January 23, 2007. Version 2. Checksum: 5E65292BC4AD8373	FASTA	209	24,034
	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

References

	« Hide 'large scale' referencesShow '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: 1754403] [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: 1551873] [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. , 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: 14702039] [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. , 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: 15489334] [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: 1475204] [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: 11909973] [Abstract] Cited for: IDENTIFICATION IN THE SET COMPLEX, INTERACTION WITH SET.
[9]	"Global proteomic profiling of phosphopeptides using electron transfer dissociation tandem mass spectrometry." Molina H., Horn D.M., Tang N., Mathivanan S., Pandey A. Proc. Natl. Acad. Sci. U.S.A. 104:2199-2204(2007) [PubMed: 17287340] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-35; TYR-155 AND TYR-162, MASS SPECTROMETRY. Tissue: Embryonic kidney.
[10]	"Lysine acetylation targets protein complexes and co-regulates major cellular functions." Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T., Olsen J.V., Mann M. Science 325:834-840(2009) [PubMed: 19608861] [Abstract] Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-30; LYS-59; LYS-172 AND LYS-173, MASS SPECTROMETRY.
[11]	"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: 21269460] [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.
IPI	IPI00219097.
PIR	NSHUH2. A42425. S30221.
RefSeq	NP_001124160.1. NM_001130688.1. NP_001124161.1. NM_001130689.1. NP_002120.1. NM_002129.3.
UniGene	Hs.434953.
3D structure databases
ProteinModelPortal	P26583.
SMR	P26583. Positions 1-166.
ModBase	Search...
Protein-protein interaction databases
IntAct	P26583. 3 interactions.
MINT	MINT-240190.
STRING	P26583.
PTM databases
PhosphoSite	P26583.
Polymorphism databases
DMDM	123374.
Proteomic databases
PeptideAtlas	P26583.
PRIDE	P26583.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000296503; ENSP00000296503; ENSG00000164104. ENST00000438704; ENSP00000404912; ENSG00000164104. ENST00000446922; ENSP00000393448; ENSG00000164104.
GeneID	3148.
KEGG	hsa:3148.
UCSC	uc003ita.2. human.
Organism-specific databases
CTD	3148.
GeneCards	GC04M174252.
H-InvDB	HIX0004637.
HGNC	HGNC:5000. HMGB2.
HPA	HPA003506.
MIM	163906. gene.
neXtProt	NX_P26583.
PharmGKB	PA35091.
GenAtlas	Search...
Phylogenomic databases
eggNOG	prNOG10248.
HOGENOM	HBG738370.
HOVERGEN	HBG009000.
InParanoid	P26583.
OMA	KGDKARY.
OrthoDB	EOG4TTGK2.
PhylomeDB	P26583.
Enzyme and pathway databases
Reactome	REACT_578. Apoptosis.
Gene expression databases
ArrayExpress	P26583.
Bgee	P26583.
CleanEx	HS_HMGB2.
Genevestigator	P26583.
GermOnline	ENSG00000164104. Homo sapiens.
Family and domain databases
InterPro	IPR017967. HMG_boxA_CS. IPR000910. HMG_HMG1/HMG2. IPR000135. HMG_HMG1/HMG2_subgr. IPR009071. HMG_superfamily. [Graphical view]
Gene3D	G3DSA:1.10.30.10. HMG-box. 2 hits.
KO	K11295.
Pfam	PF00505. HMG_box. 2 hits. [Graphical view]
PRINTS	PR00886. HIGHMOBLTY12.
SMART	SM00398. HMG. 2 hits. [Graphical view]
SUPFAM	SSF47095. HMG-box. 2 hits.
PROSITE	PS00353. HMG_BOX_1. 1 hit. PS50118. HMG_BOX_2. 2 hits. [Graphical view]
ProtoNet	Search...
Other
NextBio	12476.
PMAP-CutDB	P26583.
SOURCE	Search...

Entry information

Entry name

HMGB2_HUMAN

Accession

Primary (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:	January 25, 2012
This is version 123 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.