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P09429

- HMGB1_HUMAN

UniProt

P09429 - HMGB1_HUMAN

Protein

High mobility group protein B1

Gene

HMGB1

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 161 (01 Oct 2014)
      Sequence version 3 (23 Jan 2007)
      Previous versions | rss
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    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.By similarity

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    DNA bindingi9 – 7971HMG box 1PROSITE-ProRule annotationAdd
    BLAST
    DNA bindingi95 – 16369HMG box 2PROSITE-ProRule annotationAdd
    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

    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

    Keywords - Cellular componenti

    Chromosome, Nucleus

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA188.

    PTM / Processingi

    Molecule processing

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

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei30 – 301N6-acetyllysine2 Publications
    Modified residuei35 – 351Phosphoserine3 Publications
    Modified residuei43 – 431N6-acetyllysineBy similarity
    Modified residuei90 – 901N6-acetyllysineBy similarity
    Modified residuei100 – 1001Phosphoserine1 Publication
    Cross-linki112 – 112Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)1 Publication
    Modified residuei141 – 1411N6-acetyllysineBy 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.
    ModBaseiSearch...
    MobiDBiSearch...

    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.Curated
    Contains 2 HMG box DNA-binding domains.PROSITE-ProRule annotation

    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

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti143 – 1431P → H in AAI41845. (PubMed:15489334)Curated
    Sequence conflicti215 – 2151E → D in CAG33144. 1 PublicationCurated

    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 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

    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: October 1, 2014
    This is version 161 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