SubmitCancel

Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

P09429

- HMGB1_HUMAN

UniProt

P09429 - HMGB1_HUMAN

(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Protein

High mobility group protein B1

Gene
HMGB1, HMG1
Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

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.

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
DNA bindingi9 – 7971HMG box 1Add
BLAST
DNA bindingi95 – 16369HMG box 2Add
BLAST

GO - Molecular functioni

  1. chemoattractant activity Source: UniProtKB
  2. cytokine activity Source: UniProtKB
  3. damaged DNA binding Source: UniProtKB
  4. DNA binding, bending Source: UniProtKB
  5. double-stranded DNA binding Source: UniProtKB
  6. poly(A) RNA binding Source: UniProtKB
  7. protein binding Source: UniProtKB
  8. RAGE receptor binding Source: UniProtKB
  9. repressing transcription factor binding Source: UniProtKB
  10. sequence-specific DNA binding transcription factor activity Source: UniProtKB
  11. single-stranded DNA binding Source: UniProtKB
  12. transcription factor binding Source: UniProtKB

GO - Biological processi

  1. apoptotic DNA fragmentation Source: Reactome
  2. apoptotic process Source: Reactome
  3. base-excision repair, DNA ligation Source: UniProtKB
  4. cellular component disassembly involved in execution phase of apoptosis Source: Reactome
  5. dendritic cell chemotaxis Source: UniProtKB
  6. DNA ligation involved in DNA repair Source: UniProtKB
  7. DNA recombination Source: UniProtKB
  8. DNA topological change Source: UniProtKB
  9. inflammatory response to antigenic stimulus Source: UniProtKB
  10. innate immune response Source: Reactome
  11. myeloid dendritic cell activation Source: UniProtKB
  12. negative regulation of apoptotic cell clearance Source: Ensembl
  13. negative regulation of RNA polymerase II transcriptional preinitiation complex assembly Source: UniProtKB
  14. negative regulation of transcription from RNA polymerase II promoter Source: UniProtKB
  15. neuron projection development Source: UniProtKB
  16. positive chemotaxis Source: GOC
  17. positive regulation of apoptotic process Source: UniProtKB
  18. positive regulation of cysteine-type endopeptidase activity involved in apoptotic process Source: UniProtKB
  19. positive regulation of DNA binding Source: UniProtKB
  20. positive regulation of transcription from RNA polymerase II promoter Source: UniProtKB
  21. regulation of transcription from RNA polymerase II promoter Source: UniProtKB
  22. V(D)J recombination Source: UniProtKB
Complete GO annotation...

Keywords - Ligandi

DNA-binding

Enzyme and pathway databases

ReactomeiREACT_118563. RIP-mediated NFkB activation via ZBP1.
REACT_13462. Activation of DNA fragmentation factor.
REACT_21281. TAK1 activates NFkB by phosphorylation and activation of IKKs complex.
REACT_24969. TRAF6 mediated NF-kB activation.
REACT_25195. Advanced glycosylation endproduct receptor signaling.

Names & Taxonomyi

Protein namesi
Recommended name:
High mobility group protein B1
Alternative name(s):
High mobility group protein 1
Short name:
HMG-1
Gene namesi
Name:HMGB1
Synonyms:HMG1
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 13

Organism-specific databases

HGNCiHGNC:4983. HMGB1.

Subcellular locationi

GO - Cellular componenti

  1. cell surface Source: UniProtKB
  2. condensed chromosome Source: UniProtKB
  3. extracellular region Source: Reactome
  4. extracellular space Source: UniProtKB
  5. nucleoplasm Source: Reactome
  6. nucleus Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Chromosome, Nucleus

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA188.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed By similarity
Chaini2 – 215214High mobility group protein B1PRO_0000048526Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei30 – 301N6-acetyllysine1 Publication
Modified residuei35 – 351Phosphoserine3 Publications
Modified residuei43 – 431N6-acetyllysine By similarity
Modified residuei90 – 901N6-acetyllysine By similarity
Modified residuei100 – 1001Phosphoserine1 Publication
Cross-linki112 – 112Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)1 Publication
Modified residuei141 – 1411N6-acetyllysine By similarity

Keywords - PTMi

Acetylation, Isopeptide bond, Phosphoprotein, Ubl conjugation

Proteomic databases

MaxQBiP09429.
PaxDbiP09429.
PeptideAtlasiP09429.
PRIDEiP09429.

2D gel databases

DOSAC-COBS-2DPAGEP09429.

PTM databases

PhosphoSiteiP09429.

Expressioni

Gene expression databases

ArrayExpressiP09429.
BgeeiP09429.
CleanExiHS_HMGB1.
GenevestigatoriP09429.

Organism-specific databases

HPAiCAB005873.
HPA003506.

Interactioni

Subunit structurei

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

Protein-protein interaction databases

BioGridi109389. 63 interactions.
DIPiDIP-24195N.
IntActiP09429. 19 interactions.
MINTiMINT-153055.
STRINGi9606.ENSP00000343040.

Structurei

Secondary structure

1
215
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi6 – 83
Helixi15 – 3016
Helixi38 – 5013
Helixi54 – 7623
Beta strandi92 – 943
Helixi101 – 11616
Beta strandi118 – 1203
Helixi122 – 13514
Helixi138 – 1403
Helixi141 – 16323

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2LY4NMR-A2-84[»]
2RTUNMR-A1-84[»]
2YRQNMR-A1-166[»]
ProteinModelPortaliP09429.
SMRiP09429. Positions 5-166.

Miscellaneous databases

EvolutionaryTraceiP09429.

Family & Domainsi

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi186 – 21530Asp/Glu-rich (acidic)Add
BLAST

Sequence similaritiesi

Belongs to the HMGB family.

Keywords - Domaini

Repeat

Phylogenomic databases

eggNOGiCOG5648.
HOGENOMiHOG000197861.
HOVERGENiHBG009000.
InParanoidiP09429.
KOiK10802.
OMAiDMGKPPV.
OrthoDBiEOG7WHHBQ.
PhylomeDBiP09429.
TreeFamiTF105371.

Family and domain databases

Gene3Di1.10.30.10. 2 hits.
InterProiIPR009071. HMG_box_dom.
IPR017967. HMG_boxA_CS.
[Graphical view]
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.

P09429-1 [UniParc]FASTAAdd to Basket

« Hide

MGKGDPKKPR GKMSSYAFFV QTCREEHKKK HPDASVNFSE FSKKCSERWK    50
TMSAKEKGKF EDMAKADKAR YEREMKTYIP PKGETKKKFK DPNAPKRPPS 100
AFFLFCSEYR PKIKGEHPGL SIGDVAKKLG EMWNNTAADD KQPYEKKAAK 150
LKEKYEKDIA AYRAKGKPDA AKKGVVKAEK SKKKKEEEED EEDEEDEEEE 200
EDEEDEDEEE DDDDE 215
Length:215
Mass (Da):24,894
Last modified:January 23, 2007 - v3
Checksum:i8A868CF277D417B5
GO

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti11 – 111G → R in gastric-carcinoma cell line. 1 Publication
VAR_046451
Natural varianti149 – 1491A → E in gastric-carcinoma cell line. 1 Publication
VAR_046452
Natural varianti156 – 1561E → Q.1 Publication
VAR_046453
Natural varianti190 – 1901D → G in gastric-carcinoma cell line. 1 Publication
VAR_046454

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti143 – 1431P → H in AAI41845. 1 Publication
Sequence conflicti215 – 2151E → D in CAG33144. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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.
CCDSiCCDS9335.1.
PIRiS02826.
RefSeqiNP_002119.1. NM_002128.4.
XP_005266420.1. XM_005266363.1.
XP_005266422.1. XM_005266365.1.
UniGeneiHs.434102.
Hs.593339.
Hs.596078.

Genome annotation databases

EnsembliENST00000339872; ENSP00000343040; ENSG00000189403.
ENST00000341423; ENSP00000345347; ENSG00000189403.
ENST00000399494; ENSP00000382417; ENSG00000189403.
ENST00000405805; ENSP00000384678; ENSG00000189403.
GeneIDi3146.
KEGGihsa:3146.
UCSCiuc001usx.3. human.

Polymorphism databases

DMDMi123369.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Web resourcesi

SeattleSNPs

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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 .
CCDSi CCDS9335.1.
PIRi S02826.
RefSeqi NP_002119.1. NM_002128.4.
XP_005266420.1. XM_005266363.1.
XP_005266422.1. XM_005266365.1.
UniGenei Hs.434102.
Hs.593339.
Hs.596078.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
2LY4 NMR - A 2-84 [» ]
2RTU NMR - A 1-84 [» ]
2YRQ NMR - A 1-166 [» ]
ProteinModelPortali P09429.
SMRi P09429. Positions 5-166.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 109389. 63 interactions.
DIPi DIP-24195N.
IntActi P09429. 19 interactions.
MINTi MINT-153055.
STRINGi 9606.ENSP00000343040.

Chemistry

ChEMBLi CHEMBL2311236.

PTM databases

PhosphoSitei P09429.

Polymorphism databases

DMDMi 123369.

2D gel databases

DOSAC-COBS-2DPAGE P09429.

Proteomic databases

MaxQBi P09429.
PaxDbi P09429.
PeptideAtlasi P09429.
PRIDEi P09429.

Protocols and materials databases

DNASUi 3146.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000339872 ; ENSP00000343040 ; ENSG00000189403 .
ENST00000341423 ; ENSP00000345347 ; ENSG00000189403 .
ENST00000399494 ; ENSP00000382417 ; ENSG00000189403 .
ENST00000405805 ; ENSP00000384678 ; ENSG00000189403 .
GeneIDi 3146.
KEGGi hsa:3146.
UCSCi uc001usx.3. human.

Organism-specific databases

CTDi 3146.
GeneCardsi GC13M031032.
H-InvDB HIX0030745.
HGNCi HGNC:4983. HMGB1.
HPAi CAB005873.
HPA003506.
MIMi 163905. gene.
neXtProti NX_P09429.
PharmGKBi PA188.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG5648.
HOGENOMi HOG000197861.
HOVERGENi HBG009000.
InParanoidi P09429.
KOi K10802.
OMAi DMGKPPV.
OrthoDBi EOG7WHHBQ.
PhylomeDBi P09429.
TreeFami TF105371.

Enzyme and pathway databases

Reactomei REACT_118563. RIP-mediated NFkB activation via ZBP1.
REACT_13462. Activation of DNA fragmentation factor.
REACT_21281. TAK1 activates NFkB by phosphorylation and activation of IKKs complex.
REACT_24969. TRAF6 mediated NF-kB activation.
REACT_25195. Advanced glycosylation endproduct receptor signaling.

Miscellaneous databases

ChiTaRSi HMGB1. human.
EvolutionaryTracei P09429.
GeneWikii HMGB1.
GenomeRNAii 3146.
NextBioi 12470.
PROi P09429.
SOURCEi Search...

Gene expression databases

ArrayExpressi P09429.
Bgeei P09429.
CleanExi HS_HMGB1.
Genevestigatori P09429.

Family and domain databases

Gene3Di 1.10.30.10. 2 hits.
InterProi IPR009071. HMG_box_dom.
IPR017967. HMG_boxA_CS.
[Graphical view ]
Pfami PF00505. HMG_box. 1 hit.
PF09011. HMG_box_2. 1 hit.
[Graphical view ]
SMARTi SM00398. HMG. 2 hits.
[Graphical view ]
SUPFAMi SSF47095. SSF47095. 2 hits.
PROSITEi PS00353. HMG_BOX_1. 1 hit.
PS50118. HMG_BOX_2. 2 hits.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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. 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.
    , 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. 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.
    , 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. 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. 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. 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. 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.

Entry informationi

Entry nameiHMGB1_HUMAN
AccessioniPrimary (citable) accession number: P09429
Secondary accession number(s): A5D8W9
, Q14321, Q5T7C3, Q6IBE1
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 1, 1989
Last sequence update: January 23, 2007
Last modified: September 3, 2014
This is version 160 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (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.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 13
    Human chromosome 13: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi