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P17096

- HMGA1_HUMAN

UniProt

P17096 - HMGA1_HUMAN

Protein

High mobility group protein HMG-I/HMG-Y

Gene

HMGA1

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
  1. Functioni

    HMG-I/Y bind preferentially to the minor groove of A+T rich regions in double-stranded DNA. It is suggested that these proteins could function in nucleosome phasing and in the 3'-end processing of mRNA transcripts. They are also involved in the transcription regulation of genes containing, or in close proximity to A+T-rich regions.

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    DNA bindingi21 – 3111A.T hook 1Add
    BLAST
    DNA bindingi53 – 6311A.T hook 2Add
    BLAST
    DNA bindingi78 – 8912A.T hook 3Add
    BLAST

    GO - Molecular functioni

    1. 5'-deoxyribose-5-phosphate lyase activity Source: UniProtKB
    2. AT DNA binding Source: UniProtKB
    3. DNA-(apurinic or apyrimidinic site) lyase activity Source: UniProtKB
    4. DNA binding Source: ProtInc
    5. enzyme binding Source: UniProtKB
    6. ligand-dependent nuclear receptor transcription coactivator activity Source: UniProtKB
    7. peroxisome proliferator activated receptor binding Source: UniProtKB
    8. protein binding Source: IntAct
    9. retinoic acid receptor binding Source: UniProtKB
    10. retinoid X receptor binding Source: UniProtKB
    11. sequence-specific DNA binding transcription factor activity Source: UniProtKB
    12. transcription factor binding Source: UniProtKB

    GO - Biological processi

    1. base-excision repair Source: UniProtKB
    2. DNA catabolic process, endonucleolytic Source: GOC
    3. DNA unwinding involved in DNA replication Source: UniProtKB
    4. establishment of integrated proviral latency Source: Reactome
    5. negative regulation of cell proliferation Source: UniProtKB
    6. negative regulation of chromatin silencing Source: UniProtKB
    7. negative regulation of transcription, DNA-templated Source: UniProtKB
    8. nucleosome disassembly Source: UniProtKB
    9. oncogene-induced cell senescence Source: UniProtKB
    10. positive regulation of cellular senescence Source: UniProtKB
    11. positive regulation of transcription, DNA-templated Source: UniProtKB
    12. protein complex assembly Source: UniProtKB
    13. regulation of transcription, DNA-templated Source: ProtInc
    14. response to virus Source: UniProtKB
    15. senescence-associated heterochromatin focus assembly Source: UniProtKB
    16. transcription, DNA-templated Source: UniProtKB-KW
    17. viral process Source: Reactome

    Keywords - Biological processi

    Host-virus interaction, Transcription, Transcription regulation

    Keywords - Ligandi

    DNA-binding

    Enzyme and pathway databases

    ReactomeiREACT_169121. Formation of Senescence-Associated Heterochromatin Foci (SAHF).
    REACT_6866. Autointegration results in viral DNA circles.
    REACT_6918. Integration of provirus.
    REACT_7991. Vpr-mediated nuclear import of PICs.
    REACT_8990. Integration of viral DNA into host genomic DNA.
    REACT_9058. 2-LTR circle formation.
    REACT_9406. APOBEC3G mediated resistance to HIV-1 infection.
    SignaLinkiP17096.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    High mobility group protein HMG-I/HMG-Y
    Short name:
    HMG-I(Y)
    Alternative name(s):
    High mobility group AT-hook protein 1
    Short name:
    High mobility group protein A1
    High mobility group protein R
    Gene namesi
    Name:HMGA1
    Synonyms:HMGIY
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 6

    Organism-specific databases

    HGNCiHGNC:5010. HMGA1.

    Subcellular locationi

    GO - Cellular componenti

    1. cytosol Source: Reactome
    2. nucleoplasm Source: Reactome
    3. nucleus Source: UniProtKB
    4. senescence-associated heterochromatin focus Source: UniProtKB
    5. transcription factor complex Source: UniProtKB

    Keywords - Cellular componenti

    Chromosome, Nucleus

    Pathology & Biotechi

    Involvement in diseasei

    A chromosomal aberration involving HMGA1 is found in pulmonary chondroid hamartoma. Translocation t(6;14)(p21;q23-24) with RAD51B.

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi26 – 261R → A: Does not affect methylation by PRMT6. 1 Publication
    Mutagenesisi58 – 581R → A: Decreases methylation by PRMT6. Abolishes methylation by PRMT6; when associated with A-60. 1 Publication
    Mutagenesisi60 – 601R → A: Decreases methylation by PRMT6. Abolishes methylation by PRMT6; when associated with A-58. 1 Publication

    Organism-specific databases

    PharmGKBiPA35094.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11RemovedBy similarity
    Chaini2 – 107106High mobility group protein HMG-I/HMG-YPRO_0000206708Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei2 – 21N-acetylserineBy similarity
    Modified residuei7 – 71N6-acetyllysineBy similarity
    Modified residuei15 – 151N6-acetyllysine1 Publication
    Modified residuei26 – 261Asymmetric dimethylarginine; alternate3 Publications
    Modified residuei26 – 261Omega-N-methylarginine; alternate3 Publications
    Modified residuei26 – 261Symmetric dimethylarginine; alternate3 Publications
    Modified residuei36 – 361Phosphoserine; by HIPK2 and CDC26 Publications
    Modified residuei39 – 391Phosphothreonine2 Publications
    Modified residuei44 – 441Phosphoserine3 Publications
    Modified residuei49 – 491Phosphoserine2 Publications
    Modified residuei53 – 531Phosphothreonine; by HIPK2 and CDC25 Publications
    Modified residuei58 – 581Asymmetric dimethylarginine; by PRMT6; alternate2 Publications
    Modified residuei58 – 581Omega-N-methylarginine; by PRMT6; alternate2 Publications
    Modified residuei60 – 601Asymmetric dimethylarginine; by PRMT6; alternate2 Publications
    Modified residuei60 – 601Omega-N-methylarginine; by PRMT6; alternate2 Publications
    Modified residuei78 – 781Phosphothreonine; by HIPK2 and CDC21 Publication
    Modified residuei99 – 991Phosphoserine7 Publications
    Modified residuei102 – 1021Phosphoserine; by CK7 Publications
    Modified residuei103 – 1031Phosphoserine; by CK6 Publications

    Post-translational modificationi

    Constitutively phosphorylated on two or three sites. Hyperphosphorylated at early stages of apoptosis, followed by dephosphorylation and methylation, which coincides with chromatin condensation. Isoforms HMG-I and HMG-Y can be phosphorylated by HIPK2. Phosphorylation of HMG-I at Ser-36, Thr-53 and Thr-78 and of HMG-Y at Thr-42 and Thr-67 by HIPK2 modulates DNA-binding affinity.9 Publications
    HMG-Y is not methylated.
    Methylation at Arg-58 is mutually exclusive with methylation at Arg-60.1 Publication

    Keywords - PTMi

    Acetylation, Methylation, Phosphoprotein

    Proteomic databases

    MaxQBiP17096.
    PaxDbiP17096.
    PRIDEiP17096.

    PTM databases

    PhosphoSiteiP17096.

    Expressioni

    Gene expression databases

    ArrayExpressiP17096.
    BgeeiP17096.
    CleanExiHS_HMGA1.
    GenevestigatoriP17096.

    Organism-specific databases

    HPAiCAB032200.

    Interactioni

    Subunit structurei

    Interacts with HIPK2 By similarity. Interacts with HIV-1 pre-integration complex.By similarity

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    PRMT6Q96LA84EBI-746854,EBI-912440

    Protein-protein interaction databases

    BioGridi109402. 70 interactions.
    DIPiDIP-29687N.
    IntActiP17096. 39 interactions.
    MINTiMINT-262941.
    STRINGi9606.ENSP00000308227.

    Structurei

    Secondary structure

    1
    107
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi53 – 553

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2EZDNMR-A51-71[»]
    2EZENMR-A51-75[»]
    2EZFNMR-A80-89[»]
    2EZGNMR-A80-89[»]
    DisProtiDP00040.
    ProteinModelPortaliP17096.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni53 – 7725Interaction with HIPK2By similarityAdd
    BLAST

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi91 – 10616Glu-rich (acidic)Add
    BLAST

    Sequence similaritiesi

    Belongs to the HMGA family.Curated
    Contains 3 A.T hook DNA-binding domains.Curated

    Keywords - Domaini

    Repeat

    Phylogenomic databases

    eggNOGiNOG41800.
    HOGENOMiHOG000076308.
    HOVERGENiHBG063451.
    KOiK09282.
    OMAiQQEPSEA.
    TreeFamiTF351623.

    Family and domain databases

    InterProiIPR020478. AT_hook-like.
    IPR017956. AT_hook_DNA-bd_motif.
    IPR000116. HMGI/HMGY.
    IPR000637. HMGI/Y_DNA-bd_CS.
    [Graphical view]
    PfamiPF02178. AT_hook. 3 hits.
    [Graphical view]
    PRINTSiPR00929. ATHOOK.
    PR00930. HIGHMOBLTYIY.
    SMARTiSM00384. AT_hook. 3 hits.
    [Graphical view]
    PROSITEiPS00354. HMGI_Y. 3 hits.
    [Graphical view]

    Sequences (3)i

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    This entry describes 3 isoformsi produced by alternative splicing. Align

    Isoform HMG-I (identifier: P17096-1) [UniParc]FASTAAdd to Basket

    Also known as: HMGA1a

    This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

    « Hide

    MSESSSKSSQ PLASKQEKDG TEKRGRGRPR KQPPVSPGTA LVGSQKEPSE    50
    VPTPKRPRGR PKGSKNKGAA KTRKTTTTPG RKPRGRPKKL EKEEEEGISQ 100
    ESSEEEQ 107
    Length:107
    Mass (Da):11,676
    Last modified:January 23, 2007 - v3
    Checksum:iE9C4E3F2200914B8
    GO
    Isoform HMG-Y (identifier: P17096-2) [UniParc]FASTAAdd to Basket

    Also known as: HMGA1b

    The sequence of this isoform differs from the canonical sequence as follows:
         35-45: Missing.

    Note: Contains a phosphothreonine at position 42. Contains a phosphothreonine at position 67.

    Show »
    Length:96
    Mass (Da):10,679
    Checksum:iB82DCAA29E6D18FD
    GO
    Isoform HMG-R (identifier: P17096-3) [UniParc]FASTAAdd to Basket

    Also known as: HMGA1c

    The sequence of this isoform differs from the canonical sequence as follows:
         66-107: NKGAAKTRKT...ISQESSEEEQ → KNWRRRKRRA...RIHTCPPGQG

    Show »
    Length:179
    Mass (Da):19,694
    Checksum:i91E56E235C504AAA
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti107 – 1071Q → QQQ AA sequence (PubMed:2920035)Curated

    Mass spectrometryi

    Isoform HMG-I : Molecular mass is 11750±12 Da from positions 2 - 107. Determined by MALDI. With 1 acetyl and 2 phosphate groups.1 Publication
    Isoform HMG-I : Molecular mass is 11828±12 Da from positions 2 - 107. Determined by MALDI. With 1 acetyl and 3 phosphate groups.1 Publication
    Isoform HMG-I : Molecular mass is 11765±12 Da from positions 2 - 107. Determined by MALDI. With 1 acetyl, 1 methyl and 2 phosphate groups.1 Publication
    Isoform HMG-I : Molecular mass is 11844±12 Da from positions 2 - 107. Determined by MALDI. With 1 acetyl, 1 methyl and 3 phosphate groups.1 Publication
    Isoform HMG-I : Molecular mass is 11780±12 Da from positions 2 - 107. Determined by MALDI. With 1 acetyl, 2 methyl and 2 phosphate groups.1 Publication
    Isoform HMG-I : Molecular mass is 11858±12 Da from positions 2 - 107. Determined by MALDI. With 1 acetyl, 2 methyl and 3 phosphate groups.1 Publication

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei35 – 4511Missing in isoform HMG-Y. 3 PublicationsVSP_002182Add
    BLAST
    Alternative sequencei66 – 10742NKGAA…SEEEQ → KNWRRRKRRASRRSPRRRSS DPCVPPAPHWRSSFLLGLDS FAPLPPPPPLPQAHHHHRLW PPPPSSTCALTTTLHSTPAA AGLPWAEWGAVFPWPQFPAP PAHPRIHTCPPGQG in isoform HMG-R. 1 PublicationVSP_018084Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X14957 mRNA. Translation: CAA33080.1.
    X14958 mRNA. Translation: CAA33081.1.
    M23614 mRNA. Translation: AAA88072.1.
    M23615 mRNA. Translation: AAA88073.1.
    M23616 mRNA. Translation: AAA88074.1.
    M23617 mRNA. Translation: AAA88075.1.
    M23618 mRNA. Translation: AAA88076.1.
    M23619 mRNA. Translation: AAA35998.1.
    L17131 Genomic DNA. Translation: AAB00145.1.
    AF176039 mRNA. Translation: AAD53889.1.
    AL354740 Genomic DNA. Translation: CAI14991.1.
    BC004924 mRNA. Translation: AAH04924.1.
    BC008832 mRNA. Translation: AAH08832.1.
    BC063434 mRNA. Translation: AAH63434.1.
    BC067083 mRNA. Translation: AAH67083.1.
    BC071864 mRNA. Translation: AAH71864.1.
    CCDSiCCDS4788.1. [P17096-2]
    CCDS4789.1. [P17096-1]
    PIRiA32794.
    RefSeqiNP_002122.1. NM_002131.3. [P17096-2]
    NP_665906.1. NM_145899.2. [P17096-1]
    NP_665908.1. NM_145901.2. [P17096-1]
    NP_665909.1. NM_145902.2. [P17096-2]
    NP_665910.1. NM_145903.2. [P17096-2]
    NP_665912.1. NM_145905.2. [P17096-2]
    XP_005249118.1. XM_005249061.1. [P17096-1]
    UniGeneiHs.518805.
    Hs.703764.

    Genome annotation databases

    EnsembliENST00000311487; ENSP00000308227; ENSG00000137309. [P17096-1]
    ENST00000347617; ENSP00000288245; ENSG00000137309. [P17096-2]
    ENST00000374116; ENSP00000363230; ENSG00000137309. [P17096-2]
    ENST00000401473; ENSP00000385693; ENSG00000137309. [P17096-2]
    ENST00000447654; ENSP00000399888; ENSG00000137309. [P17096-1]
    GeneIDi3159.
    KEGGihsa:3159.
    UCSCiuc003oit.3. human. [P17096-1]

    Polymorphism databases

    DMDMi123377.

    Keywords - Coding sequence diversityi

    Alternative splicing, Chromosomal rearrangement

    Cross-referencesi

    Web resourcesi

    Atlas of Genetics and Cytogenetics in Oncology and Haematology

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X14957 mRNA. Translation: CAA33080.1 .
    X14958 mRNA. Translation: CAA33081.1 .
    M23614 mRNA. Translation: AAA88072.1 .
    M23615 mRNA. Translation: AAA88073.1 .
    M23616 mRNA. Translation: AAA88074.1 .
    M23617 mRNA. Translation: AAA88075.1 .
    M23618 mRNA. Translation: AAA88076.1 .
    M23619 mRNA. Translation: AAA35998.1 .
    L17131 Genomic DNA. Translation: AAB00145.1 .
    AF176039 mRNA. Translation: AAD53889.1 .
    AL354740 Genomic DNA. Translation: CAI14991.1 .
    BC004924 mRNA. Translation: AAH04924.1 .
    BC008832 mRNA. Translation: AAH08832.1 .
    BC063434 mRNA. Translation: AAH63434.1 .
    BC067083 mRNA. Translation: AAH67083.1 .
    BC071864 mRNA. Translation: AAH71864.1 .
    CCDSi CCDS4788.1. [P17096-2 ]
    CCDS4789.1. [P17096-1 ]
    PIRi A32794.
    RefSeqi NP_002122.1. NM_002131.3. [P17096-2 ]
    NP_665906.1. NM_145899.2. [P17096-1 ]
    NP_665908.1. NM_145901.2. [P17096-1 ]
    NP_665909.1. NM_145902.2. [P17096-2 ]
    NP_665910.1. NM_145903.2. [P17096-2 ]
    NP_665912.1. NM_145905.2. [P17096-2 ]
    XP_005249118.1. XM_005249061.1. [P17096-1 ]
    UniGenei Hs.518805.
    Hs.703764.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2EZD NMR - A 51-71 [» ]
    2EZE NMR - A 51-75 [» ]
    2EZF NMR - A 80-89 [» ]
    2EZG NMR - A 80-89 [» ]
    DisProti DP00040.
    ProteinModelPortali P17096.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 109402. 70 interactions.
    DIPi DIP-29687N.
    IntActi P17096. 39 interactions.
    MINTi MINT-262941.
    STRINGi 9606.ENSP00000308227.

    PTM databases

    PhosphoSitei P17096.

    Polymorphism databases

    DMDMi 123377.

    Proteomic databases

    MaxQBi P17096.
    PaxDbi P17096.
    PRIDEi P17096.

    Protocols and materials databases

    DNASUi 3159.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000311487 ; ENSP00000308227 ; ENSG00000137309 . [P17096-1 ]
    ENST00000347617 ; ENSP00000288245 ; ENSG00000137309 . [P17096-2 ]
    ENST00000374116 ; ENSP00000363230 ; ENSG00000137309 . [P17096-2 ]
    ENST00000401473 ; ENSP00000385693 ; ENSG00000137309 . [P17096-2 ]
    ENST00000447654 ; ENSP00000399888 ; ENSG00000137309 . [P17096-1 ]
    GeneIDi 3159.
    KEGGi hsa:3159.
    UCSCi uc003oit.3. human. [P17096-1 ]

    Organism-specific databases

    CTDi 3159.
    GeneCardsi GC06P036298.
    HGNCi HGNC:5010. HMGA1.
    HPAi CAB032200.
    MIMi 600701. gene.
    neXtProti NX_P17096.
    PharmGKBi PA35094.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG41800.
    HOGENOMi HOG000076308.
    HOVERGENi HBG063451.
    KOi K09282.
    OMAi QQEPSEA.
    TreeFami TF351623.

    Enzyme and pathway databases

    Reactomei REACT_169121. Formation of Senescence-Associated Heterochromatin Foci (SAHF).
    REACT_6866. Autointegration results in viral DNA circles.
    REACT_6918. Integration of provirus.
    REACT_7991. Vpr-mediated nuclear import of PICs.
    REACT_8990. Integration of viral DNA into host genomic DNA.
    REACT_9058. 2-LTR circle formation.
    REACT_9406. APOBEC3G mediated resistance to HIV-1 infection.
    SignaLinki P17096.

    Miscellaneous databases

    ChiTaRSi HMGA1. human.
    GeneWikii HMGA1.
    GenomeRNAii 3159.
    NextBioi 12514.
    PROi P17096.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P17096.
    Bgeei P17096.
    CleanExi HS_HMGA1.
    Genevestigatori P17096.

    Family and domain databases

    InterProi IPR020478. AT_hook-like.
    IPR017956. AT_hook_DNA-bd_motif.
    IPR000116. HMGI/HMGY.
    IPR000637. HMGI/Y_DNA-bd_CS.
    [Graphical view ]
    Pfami PF02178. AT_hook. 3 hits.
    [Graphical view ]
    PRINTSi PR00929. ATHOOK.
    PR00930. HIGHMOBLTYIY.
    SMARTi SM00384. AT_hook. 3 hits.
    [Graphical view ]
    PROSITEi PS00354. HMGI_Y. 3 hits.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Cloning of cDNAs coding for human HMG I and HMG Y proteins: both are capable of binding to the octamer sequence motif."
      Eckner R., Birnstiel M.L.
      Nucleic Acids Res. 17:5947-5959(1989) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS HMG-I AND HMG-Y).
    2. "Alternative processing of mRNAs encoding mammalian chromosomal high-mobility-group proteins HMG-I and HMG-Y."
      Johnson K.R., Lehn D.A., Reeves R.
      Mol. Cell. Biol. 9:2114-2123(1989) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS HMG-I AND HMG-Y).
    3. "Organization, inducible-expression and chromosome localization of the human HMG-I(Y) nonhistone protein gene."
      Friedmann M., Holth L.T., Zoghbi H.Y., Reeves R.
      Nucleic Acids Res. 21:4259-4267(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Tissue: Placenta.
    4. "Retinoid-dependent recruitment of a histone H1 displacement activity by retinoic acid receptor."
      Nagpal S., Ghosn C., DiSepio D., Molina Y., Sutter M., Klein E.S., Chandraratna R.A.S.
      J. Biol. Chem. 274:22563-22568(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM HMG-R).
    5. "The DNA sequence and analysis of human chromosome 6."
      Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L., Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., Gilbert J.G.R., Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D., Andrews T.D.
      , Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H., Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J., Brown J.Y., Burford D.C., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V., Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J., Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., Ellington A.E., Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J., French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J., Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C., Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A., Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R., Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M., Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A., Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L., Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I., Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y., Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E., Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A., Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W., Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M., West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J., Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M., Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I., Rogers J., Beck S.
      Nature 425:805-811(2003) [PubMed] [Europe PMC] [Abstract]
      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] (ISOFORMS HMG-I AND HMG-Y).
      Tissue: B-cell, Mammary gland, Muscle, Pancreas and Uterus.
    7. "The human chromosomal protein HMG I contains two identical palindrome amino acid sequences."
      Lund T., Dahl K.H., Mork E., Holtlund J., Laland S.G.
      Biochem. Biophys. Res. Commun. 146:725-730(1987) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 4-107 (HMG-I).
    8. "The amino acid sequence of the chromosomal protein HMG-Y, its relation to HMG-I and possible domains for the preferential binding of the proteins to stretches of A-T base pairs."
      Karlson J.R., Mork E., Holtlund J., Laland S.G., Lund T.
      Biochem. Biophys. Res. Commun. 158:646-651(1989) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 4-107 (HMG-Y).
    9. "The A.T-DNA-binding domain of mammalian high mobility group I chromosomal proteins. A novel peptide motif for recognizing DNA structure."
      Reeves R., Nissen M.S.
      J. Biol. Chem. 265:8573-8582(1990) [PubMed] [Europe PMC] [Abstract]
      Cited for: DNA-BINDING DOMAINS.
    10. "Intragenic breakpoint within RAD51L1 in a t(6;14)(p21.3;q24) of a pulmonary chondroid hamartoma."
      Blank C., Schoenmakers E.F.P.M., Rogalla P., Huys E.H., van Rijk A.A., Drieschner N., Bullerdiek J.
      Cytogenet. Cell Genet. 95:17-19(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: CHROMOSOMAL TRANSLOCATION WITH RAD51B.
    11. "During apoptosis of tumor cells HMGA1a protein undergoes methylation: identification of the modification site by mass spectrometry."
      Sgarra R., Diana F., Bellarosa C., Dekleva V., Rustighi A., Toller M., Manfioletti G., Giancotti V.
      Biochemistry 42:3575-3585(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION, METHYLATION AT ARG-26, IDENTIFICATION BY MASS SPECTROMETRY.
    12. "Protein arginine methyltransferase 6 specifically methylates the nonhistone chromatin protein HMGA1a."
      Miranda T.B., Webb K.J., Edberg D.D., Reeves R., Clarke S.
      Biochem. Biophys. Res. Commun. 336:831-835(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: METHYLATION BY PRMT6.
    13. "Tandem mass spectrometry for the examination of the posttranslational modifications of high-mobility group A1 proteins: symmetric and asymmetric dimethylation of Arg25 in HMGA1a protein."
      Zou Y., Wang Y.
      Biochemistry 44:6293-6301(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION AT SER-99; SER-102 AND SER-103, METHYLATION AT ARG-26, MASS SPECTROMETRY.
    14. "Dynamics of human protein arginine methyltransferase 1(PRMT1) in vivo."
      Herrmann F., Lee J., Bedford M.T., Fackelmayer F.O.
      J. Biol. Chem. 280:38005-38010(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: METHYLATION AT ARG-58 AND ARG-60 BY PRMT6, MUTAGENESIS OF ARG-26; ARG-58 AND ARG-60.
    15. "Global, in vivo, and site-specific phosphorylation dynamics in signaling networks."
      Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.
      Cell 127:635-648(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-36; SER-99; SER-102 AND SER-103, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    16. "Improved titanium dioxide enrichment of phosphopeptides from HeLa cells and high confident phosphopeptide identification by cross-validation of MS/MS and MS/MS/MS spectra."
      Yu L.R., Zhu Z., Chan K.C., Issaq H.J., Dimitrov D.S., Veenstra T.D.
      J. Proteome Res. 6:4150-4162(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-36 AND THR-53, PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-42 (ISOFORM HMG-Y), IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    17. "Homeodomain-interacting protein kinase-2 (HIPK2) phosphorylates HMGA1a at Ser-35, Thr-52, and Thr-77 and modulates its DNA binding affinity."
      Zhang Q., Wang Y.
      J. Proteome Res. 6:4711-4719(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION AT SER-36; THR-53 AND THR-78 BY HIPK2 AND CDK1/CDC2 (ISOFORM HMG-I), PHOSPHORYLATION AT THR-42 AND THR-67 BY HIPK2 AND CDK1/CDC2 (ISOFORM HMG-Y).
    18. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-99; SER-102 AND SER-103, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Embryonic kidney.
    19. "Phosphorylation analysis of primary human T lymphocytes using sequential IMAC and titanium oxide enrichment."
      Carrascal M., Ovelleiro D., Casas V., Gay M., Abian J.
      J. Proteome Res. 7:5167-5176(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: T-cell.
    20. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-36; THR-39; SER-44; SER-49 AND THR-53, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    21. "Large-scale phosphoproteome analysis of human liver tissue by enrichment and fractionation of phosphopeptides with strong anion exchange chromatography."
      Han G., Ye M., Zhou H., Jiang X., Feng S., Jiang X., Tian R., Wan D., Zou H., Gu J.
      Proteomics 8:1346-1361(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Liver.
    22. "Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
      Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
      Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    23. "Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
      Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
      Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-99; SER-102 AND SER-103, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Leukemic T-cell.
    24. "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-15, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    25. "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-36; THR-53; SER-99; SER-102 AND SER-103, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    26. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    27. "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-36; SER-44; THR-53; SER-99 AND SER-102, PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-42 (ISOFORM HMG-Y), IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    28. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    29. "The solution structure of an HMG-I(Y)-DNA complex defines a new architectural minor groove binding motif."
      Huth J.R., Bewley C.A., Nissen M.S., Evans J.N., Reeves R., Gronenborn A.M., Clore G.M.
      Nat. Struct. Biol. 4:657-665(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: STRUCTURE BY NMR OF 51-75 AND 80-89.

    Entry informationi

    Entry nameiHMGA1_HUMAN
    AccessioniPrimary (citable) accession number: P17096
    Secondary accession number(s): P10910, Q5T6U9, Q9UKB0
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: August 1, 1990
    Last sequence update: January 23, 2007
    Last modified: October 1, 2014
    This is version 175 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 6
      Human chromosome 6: entries, gene names and cross-references to MIM
    2. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    3. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    4. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3