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P09429 (HMGB1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 156. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
High mobility group protein B1
Alternative name(s):
High mobility group protein 1
Short name=HMG-1
Gene names
Name:HMGB1
Synonyms:HMG1
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length215 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). Heparin-binding protein that has a role in the extension of neurite-type cytoplasmic processes in developing cells By similarity.

Subunit structure

Component of the RAG complex composed of core components RAG1 and RAG2, and associated component HMGB1 or HMGB2 By similarity.

Subcellular location

Nucleus. Chromosome.

Sequence similarities

Belongs to the HMGB family.

Contains 2 HMG box DNA-binding domains.

Ontologies

Keywords
   Cellular componentChromosome
Nucleus
   Coding sequence diversityPolymorphism
   DomainRepeat
   LigandDNA-binding
   PTMAcetylation
Isopeptide bond
Phosphoprotein
Ubl conjugation
   Technical term3D-structure
Complete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processDNA ligation involved in DNA repair

Inferred from sequence or structural similarity. Source: UniProtKB

DNA recombination

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 direct assay PubMed 9166431. 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

cellular component disassembly involved in execution phase of apoptosis

Traceable author statement. Source: Reactome

dendritic cell chemotaxis

Inferred from sequence or structural similarity. Source: UniProtKB

inflammatory response to antigenic stimulus

Inferred from expression pattern PubMed 19841752. Source: UniProtKB

innate immune response

Traceable author statement. Source: Reactome

myeloid dendritic cell activation

Inferred from sequence or structural similarity. Source: UniProtKB

negative regulation of RNA polymerase II transcriptional preinitiation complex assembly

Inferred from direct assay PubMed 8006019. Source: UniProtKB

negative regulation of apoptotic cell clearance

Inferred from electronic annotation. Source: Ensembl

negative regulation of transcription from RNA polymerase II promoter

Inferred from mutant phenotype PubMed 19158276. Source: UniProtKB

neuron projection development

Inferred from sequence or structural similarity. Source: UniProtKB

positive chemotaxis

Inferred from sequence or structural similarity. Source: GOC

positive regulation of DNA binding

Inferred from direct assay PubMed 11748232PubMed 19223331. Source: UniProtKB

positive regulation of apoptotic process

Inferred from direct assay PubMed 19800306. Source: UniProtKB

positive regulation of cysteine-type endopeptidase activity involved in apoptotic process

Inferred from direct assay PubMed 19800306. Source: UniProtKB

positive regulation of transcription from RNA polymerase II promoter

Inferred from direct assay PubMed 19223331. Source: UniProtKB

regulation of transcription from RNA polymerase II promoter

Inferred from direct assay PubMed 11748232. Source: UniProtKB

   Cellular_componentcell surface

Inferred from direct assay PubMed 19841752. Source: UniProtKB

condensed chromosome

Inferred from direct assay PubMed 12925773. Source: UniProtKB

extracellular region

Traceable author statement. Source: Reactome

extracellular space

Inferred from direct assay PubMed 19841752. Source: UniProtKB

nucleoplasm

Traceable author statement. Source: Reactome

nucleus

Inferred from direct assay PubMed 19223331PubMed 8339930. Source: UniProtKB

   Molecular_functionDNA binding, bending

Inferred from mutant phenotype PubMed 19223331. Source: UniProtKB

RAGE receptor binding

Inferred from sequence or structural similarity. Source: UniProtKB

chemoattractant activity

Inferred from sequence or structural similarity. Source: UniProtKB

cytokine activity

Inferred from sequence or structural similarity. Source: UniProtKB

damaged DNA binding

Inferred from sequence or structural similarity. 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

repressing transcription factor binding

Inferred from physical interaction PubMed 19223331. 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 factor binding

Inferred from physical interaction PubMed 19223331. Source: UniProtKB

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed By similarity
Chain2 – 215214High mobility group protein B1
PRO_0000048526

Regions

DNA binding9 – 7971HMG box 1
DNA binding95 – 16369HMG box 2
Compositional bias186 – 21530Asp/Glu-rich (acidic)

Amino acid modifications

Modified residue301N6-acetyllysine Ref.17
Modified residue351Phosphoserine Ref.15 Ref.18 Ref.20
Modified residue431N6-acetyllysine By similarity
Modified residue901N6-acetyllysine By similarity
Modified residue1001Phosphoserine Ref.15
Modified residue1411N6-acetyllysine By similarity
Cross-link112Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) Ref.16

Natural variations

Natural variant111G → R in gastric-carcinoma cell line. Ref.3
VAR_046451
Natural variant1491A → E in gastric-carcinoma cell line. Ref.3
VAR_046452
Natural variant1561E → Q. Ref.10
VAR_046453
Natural variant1901D → G in gastric-carcinoma cell line. Ref.3
VAR_046454

Experimental info

Sequence conflict1431P → H in AAI41845. Ref.13
Sequence conflict2151E → D in CAG33144. Ref.8

Secondary structure

.................... 215
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P09429 [UniParc].

Last modified January 23, 2007. Version 3.
Checksum: 8A868CF277D417B5

FASTA21524,894
        10         20         30         40         50         60 
MGKGDPKKPR GKMSSYAFFV QTCREEHKKK HPDASVNFSE FSKKCSERWK TMSAKEKGKF 

        70         80         90        100        110        120 
EDMAKADKAR YEREMKTYIP PKGETKKKFK DPNAPKRPPS AFFLFCSEYR PKIKGEHPGL 

       130        140        150        160        170        180 
SIGDVAKKLG EMWNNTAADD KQPYEKKAAK LKEKYEKDIA AYRAKGKPDA AKKGVVKAEK 

       190        200        210 
SKKKKEEEED EEDEEDEEEE EDEEDEDEEE DDDDE 

« Hide

References

« Hide 'large scale' references
[1]"A human placental cDNA clone that encodes nonhistone chromosomal protein HMG-1."
Wen L., Huang J.K., Johnson B.H., Reeck G.R.
Nucleic Acids Res. 17:1197-1214(1989) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]"The active gene that encodes human high mobility group 1 protein (HMG1) contains introns and maps to chromosome 13."
Ferrari S., Finelli P., Rocchi M., Bianchi M.E.
Genomics 35:367-371(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[3]"Expression of high-mobility group-1 mRNA in human gastrointestinal adenocarcinoma and corresponding non-cancerous mucosa."
Xiang Y.-Y., Wang D.-Y., Tanaka M., Suzuki M., Kiyokawa E., Igarashi H., Niato Y., Shen Q., Sugimura H.
Int. J. Cancer 74:1-6(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], VARIANTS ARG-11; GLU-149 AND GLY-190.
[4]"The genetic variation of the human HMGB1 gene."
Kornblit B., Munthe-Fog L., Petersen S., Madsen H., Vindeloev L., Garred P.
Tissue Antigens 70:151-156(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[5]He F.T., Yang Z.H., Ji Q., Li R., Peng J., Jiang Y., Zhong X.
Submitted (SEP-2003) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[6]"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: Cerebellum.
[7]"The full-ORF clone resource of the German cDNA consortium."
Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U., Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A., Wiemann S., Schupp I.
BMC Genomics 8:399-399(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Small intestine.
[8]"Cloning of human full open reading frames in Gateway(TM) system entry vector (pDONR201)."
Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.
Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[9]"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].
[10]SeattleSNPs variation discovery resource
Submitted (JUL-2007) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANT GLN-156.
[11]"The DNA sequence and analysis of human chromosome 13."
Dunham A., Matthews L.H., Burton J., Ashurst J.L., Howe K.L., Ashcroft K.J., Beare D.M., Burford D.C., Hunt S.E., Griffiths-Jones S., Jones M.C., Keenan S.J., Oliver K., Scott C.E., Ainscough R., Almeida J.P., Ambrose K.D., Andrews D.T. expand/collapse author list , Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J., Bannerjee R., Barlow K.F., Bates K., Beasley H., Bird C.P., Bray-Allen S., Brown A.J., Brown J.Y., Burrill W., Carder C., Carter N.P., Chapman J.C., Clamp M.E., Clark S.Y., Clarke G., Clee C.M., Clegg S.C., Cobley V., Collins J.E., Corby N., Coville G.J., Deloukas P., Dhami P., Dunham I., Dunn M., Earthrowl M.E., Ellington A.G., Faulkner L., Frankish A.G., Frankland J., French L., Garner P., Garnett J., Gilbert J.G.R., Gilson C.J., Ghori J., Grafham D.V., Gribble S.M., Griffiths C., Hall R.E., Hammond S., Harley J.L., Hart E.A., Heath P.D., Howden P.J., Huckle E.J., Hunt P.J., Hunt A.R., Johnson C., Johnson D., Kay M., Kimberley A.M., King A., Laird G.K., Langford C.J., Lawlor S., Leongamornlert D.A., Lloyd D.M., Lloyd C., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M., McLaren S.J., McMurray A., Milne S., Moore M.J.F., Nickerson T., Palmer S.A., Pearce A.V., Peck A.I., Pelan S., Phillimore B., Porter K.M., Rice C.M., Searle S., Sehra H.K., Shownkeen R., Skuce C.D., Smith M., Steward C.A., Sycamore N., Tester J., Thomas D.W., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M., West A.P., Whitehead S.L., Willey D.L., Wilming L., Wray P.W., Wright M.W., Young L., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Beck S., Bentley D.R., Rogers J., Ross M.T.
Nature 428:522-528(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[12]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 (JUL-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[13]"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: Brain, Cervix and Testis.
[14]"Two-dimensional electrophoretic analysis of human breast carcinoma proteins: mapping of proteins that bind to the SH3 domain of mixed lineage kinase MLK2."
Rasmussen R.K., Ji H., Eddes J.S., Moritz R.L., Reid G.E., Simpson R.J., Dorow D.S.
Electrophoresis 18:588-598(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 58-65 AND 113-127.
Tissue: Mammary carcinoma.
[15]"A quantitative atlas of mitotic phosphorylation."
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-35 AND SER-100, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[16]"Proteomic analysis of ubiquitinated proteins in normal hepatocyte cell line Chang liver cells."
Tan F., Lu L., Cai Y., Wang J., Xie Y., Wang L., Gong Y., Xu B.-E., Wu J., Luo Y., Qiang B., Yuan J., Sun X., Peng X.
Proteomics 8:2885-2896(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: UBIQUITINATION [LARGE SCALE ANALYSIS] AT LYS-112.
Tissue: Cervix carcinoma.
[17]"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].
[18]"Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-35, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[19]"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].
[20]"System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-35, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[21]"Novel role of PKR in inflammasome activation and HMGB1 release."
Lu B., Nakamura T., Inouye K., Li J., Tang Y., Lundbaeck P., Valdes-Ferrer S.I., Olofsson P.S., Kalb T., Roth J., Zou Y., Erlandsson-Harris H., Yang H., Ting J.P., Wang H., Andersson U., Antoine D.J., Chavan S.S., Hotamisligil G.S., Tracey K.J.
Nature 488:670-674(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION.
[22]"Solution structure of the tandem HMG box domain from human high mobility group protein B1."
RIKEN structural genomics initiative (RSGI)
Submitted (FEB-2008) to the PDB data bank
Cited for: STRUCTURE BY NMR OF 1-166.
+Additional computationally mapped references.

Web resources

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X12597 mRNA. Translation: CAA31110.1.
U51677 Genomic DNA. Translation: AAB08987.1.
D63874 mRNA. Translation: BAA09924.1.
EF157968 Genomic DNA. Translation: ABM47301.1.
AY377859 mRNA. Translation: AAQ91389.1.
AK291494 mRNA. Translation: BAF84183.1.
AK122825 mRNA. Translation: BAG53745.1.
CR749614 mRNA. Translation: CAH18408.1.
CR456863 mRNA. Translation: CAG33144.1.
BT006940 mRNA. Translation: AAP35586.1.
BT020159 mRNA. Translation: AAV38961.1.
EU012027 Genomic DNA. Translation: ABS29271.1.
AL353648 Genomic DNA. Translation: CAI15600.1.
CH471075 Genomic DNA. Translation: EAX08457.1.
BC003378 mRNA. Translation: AAH03378.1.
BC030981 mRNA. Translation: AAH30981.1.
BC066889 mRNA. Translation: AAH66889.1.
BC067732 mRNA. Translation: AAH67732.1.
BC141844 mRNA. Translation: AAI41845.1.
PIRS02826.
RefSeqNP_002119.1. NM_002128.4.
XP_005266420.1. XM_005266363.1.
XP_005266422.1. XM_005266365.1.
UniGeneHs.434102.
Hs.593339.
Hs.596078.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2LY4NMR-A2-84[»]
2RTUNMR-A1-84[»]
2YRQNMR-A1-166[»]
ProteinModelPortalP09429.
SMRP09429. Positions 5-166.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid109389. 61 interactions.
DIPDIP-24195N.
IntActP09429. 19 interactions.
MINTMINT-153055.
STRING9606.ENSP00000343040.

Chemistry

ChEMBLCHEMBL2311236.

PTM databases

PhosphoSiteP09429.

Polymorphism databases

DMDM123369.

2D gel databases

DOSAC-COBS-2DPAGEP09429.

Proteomic databases

PaxDbP09429.
PeptideAtlasP09429.
PRIDEP09429.

Protocols and materials databases

DNASU3146.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000339872; ENSP00000343040; ENSG00000189403.
ENST00000341423; ENSP00000345347; ENSG00000189403.
ENST00000399494; ENSP00000382417; ENSG00000189403.
ENST00000405805; ENSP00000384678; ENSG00000189403.
GeneID3146.
KEGGhsa:3146.
UCSCuc001usx.3. human.

Organism-specific databases

CTD3146.
GeneCardsGC13M031032.
H-InvDBHIX0030745.
HGNCHGNC:4983. HMGB1.
HPACAB005873.
HPA003506.
MIM163905. gene.
neXtProtNX_P09429.
PharmGKBPA188.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG5648.
HOGENOMHOG000197861.
HOVERGENHBG009000.
InParanoidP09429.
KOK10802.
OMADMGKPPV.
OrthoDBEOG7WHHBQ.
PhylomeDBP09429.
TreeFamTF105371.

Enzyme and pathway databases

ReactomeREACT_578. Apoptosis.
REACT_6900. Immune System.

Gene expression databases

ArrayExpressP09429.
BgeeP09429.
CleanExHS_HMGB1.
GenevestigatorP09429.

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

ChiTaRSHMGB1. human.
EvolutionaryTraceP09429.
GeneWikiHMGB1.
GenomeRNAi3146.
NextBio12470.
PROP09429.
SOURCESearch...

Entry information

Entry nameHMGB1_HUMAN
AccessionPrimary (citable) accession number: P09429
Secondary accession number(s): A5D8W9 expand/collapse secondary AC list , Q14321, Q5T7C3, Q6IBE1
Entry history
Integrated into UniProtKB/Swiss-Prot: July 1, 1989
Last sequence update: January 23, 2007
Last modified: April 16, 2014
This is version 156 of the entry and version 3 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

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

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

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 13

Human chromosome 13: entries, gene names and cross-references to MIM