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P17095

- HMGA1_MOUSE

UniProt

P17095 - HMGA1_MOUSE

Protein

High mobility group protein HMG-I/HMG-Y

Gene

Hmga1

Organism
Mus musculus (Mouse)
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. DNA binding Source: UniProtKB-KW
    2. ligand-dependent nuclear receptor transcription coactivator activity Source: UniProtKB
    3. peroxisome proliferator activated receptor binding Source: UniProtKB
    4. retinoic acid receptor binding Source: UniProtKB
    5. retinoid X receptor binding Source: UniProtKB
    6. sequence-specific DNA binding transcription factor activity Source: UniProtKB
    7. transcription factor binding Source: UniProtKB

    GO - Biological processi

    1. negative regulation of cell proliferation Source: UniProtKB
    2. negative regulation of transcription, DNA-templated Source: UniProtKB
    3. oncogene-induced cell senescence Source: UniProtKB
    4. positive regulation of cellular senescence Source: UniProtKB
    5. positive regulation of transcription, DNA-templated Source: UniProtKB
    6. senescence-associated heterochromatin focus assembly Source: UniProtKB
    7. transcription, DNA-templated Source: UniProtKB-KW

    Keywords - Biological processi

    Transcription, Transcription regulation

    Keywords - Ligandi

    DNA-binding

    Enzyme and pathway databases

    ReactomeiREACT_209428. Formation of Senescence-Associated Heterochromatin Foci (SAHF).

    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
    Gene namesi
    Name:Hmga1
    Synonyms:Hmgi, Hmgiy
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome 17

    Organism-specific databases

    MGIiMGI:96160. Hmga1.

    Subcellular locationi

    GO - Cellular componenti

    1. nucleus Source: UniProtKB
    2. senescence-associated heterochromatin focus Source: UniProtKB

    Keywords - Cellular componenti

    Chromosome, Nucleus

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed2 Publications
    Chaini2 – 107106High mobility group protein HMG-I/HMG-YPRO_0000206709Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei2 – 21N-acetylserine2 Publications
    Modified residuei7 – 71N6-acetyllysine1 Publication
    Modified residuei15 – 151N6-acetyllysine1 Publication
    Modified residuei26 – 261Asymmetric dimethylarginine; alternateBy similarity
    Modified residuei26 – 261Omega-N-methylarginine; alternateBy similarity
    Modified residuei26 – 261Symmetric dimethylarginine; alternateBy similarity
    Modified residuei36 – 361Phosphoserine; by HIPK2 and CDC2By similarity
    Modified residuei39 – 391PhosphothreonineBy similarity
    Modified residuei44 – 441Phosphoserine1 Publication
    Modified residuei49 – 491Phosphoserine1 Publication
    Modified residuei53 – 531Phosphothreonine; by HIPK2 and CDC22 Publications
    Modified residuei58 – 581Asymmetric dimethylarginine; by PRMT6; alternateBy similarity
    Modified residuei58 – 581Omega-N-methylarginine; by PRMT6; alternateBy similarity
    Modified residuei60 – 601Asymmetric dimethylarginine; by PRMT6; alternateBy similarity
    Modified residuei60 – 601Omega-N-methylarginine; by PRMT6; alternateBy similarity
    Modified residuei99 – 991Phosphoserine4 Publications
    Modified residuei102 – 1021Phosphoserine6 Publications
    Modified residuei103 – 1031Phosphoserine6 Publications

    Post-translational modificationi

    Isoforms HMG-I and HMG-Y can be phosphorylated by HIPK2. Phosphorylation may modulate DNA-binding affinity By similarity.By similarity
    Methylation at Arg-58 is mutually exclusive with methylation at Arg-60.By similarity

    Keywords - PTMi

    Acetylation, Methylation, Phosphoprotein

    Proteomic databases

    PaxDbiP17095.
    PRIDEiP17095.

    PTM databases

    PhosphoSiteiP17095.

    Expressioni

    Gene expression databases

    BgeeiP17095.
    CleanExiMM_HMGA1.
    GenevestigatoriP17095.

    Interactioni

    Subunit structurei

    Interacts with HIPK2.1 Publication

    Protein-protein interaction databases

    BioGridi200340. 8 interactions.
    DIPiDIP-53N.
    IntActiP17095. 4 interactions.
    MINTiMINT-1848156.
    STRINGi10090.ENSMUSP00000113015.

    Structurei

    3D structure databases

    ProteinModelPortaliP17095.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni53 – 7725Interaction with HIPK2Add
    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.
    InParanoidiP17095.
    KOiK09282.
    OMAiQQEPSEA.
    OrthoDBiEOG71CFQJ.
    PhylomeDBiP17095.
    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 (2)i

    Sequence statusi: Complete.

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

    This entry describes 2 isoformsi produced by alternative splicing. Align

    Isoform HMG-I (identifier: P17095-2) [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

    MSESGSKSSQ PLASKQEKDG TEKRGRGRPR KQPPVSPGTA LVGSQKEPSE    50
    VPTPKRPRGR PKGSKNKGAA KTRKVTTAPG RKPRGRPKKL EKEEEEGISQ 100
    ESSEEEQ 107
    Length:107
    Mass (Da):11,614
    Last modified:January 23, 2007 - v4
    Checksum:i4EC39386611959FC
    GO
    Isoform HMG-Y (identifier: P17095-1) [UniParc]FASTAAdd to Basket

    Also known as: HMGA1b, HMGI-E

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

    Show »
    Length:96
    Mass (Da):10,617
    Checksum:iA77A3FD7CA6C08EC
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti106 – 1061E → G in AAK66158. (PubMed:11410365)Curated
    Sequence conflicti106 – 1061E → G in AAK66159. (PubMed:11410365)Curated

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei35 – 4511Missing in isoform HMG-Y. 2 PublicationsVSP_012406Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    J04179 mRNA. Translation: AAA37820.1.
    AF285780 Genomic DNA. Translation: AAK66158.1.
    AF285780 Genomic DNA. Translation: AAK66159.1.
    AK010617 mRNA. Translation: BAB27065.1.
    BC013455 mRNA. Translation: AAH13455.1.
    CCDSiCCDS28564.1. [P17095-2]
    CCDS49010.1. [P17095-2]
    CCDS50044.1. [P17095-1]
    PIRiA31895.
    RefSeqiNP_001020598.1. NM_001025427.3. [P17095-2]
    NP_001034445.1. NM_001039356.2. [P17095-2]
    NP_001159948.1. NM_001166476.1. [P17095-2]
    NP_001159949.1. NM_001166477.1. [P17095-1]
    NP_001160007.1. NM_001166535.1. [P17095-2]
    NP_001160008.1. NM_001166536.1. [P17095-2]
    NP_001160009.1. NM_001166537.1. [P17095-1]
    NP_001160011.1. NM_001166539.1. [P17095-1]
    NP_001160012.1. NM_001166540.1. [P17095-1]
    NP_001160013.1. NM_001166541.1. [P17095-1]
    NP_001160014.1. NM_001166542.1. [P17095-1]
    NP_057869.2. NM_016660.3. [P17095-2]
    UniGeneiMm.426212.
    Mm.440289.
    Mm.4438.

    Genome annotation databases

    EnsembliENSMUST00000105046; ENSMUSP00000100667; ENSMUSG00000078249. [P17095-2]
    ENSMUST00000114888; ENSMUSP00000110538; ENSMUSG00000046711. [P17095-1]
    ENSMUST00000117254; ENSMUSP00000113011; ENSMUSG00000046711. [P17095-2]
    ENSMUST00000117600; ENSMUSP00000113068; ENSMUSG00000046711. [P17095-2]
    ENSMUST00000118570; ENSMUSP00000114101; ENSMUSG00000046711. [P17095-1]
    ENSMUST00000118599; ENSMUSP00000113015; ENSMUSG00000046711. [P17095-2]
    ENSMUST00000119486; ENSMUSP00000113916; ENSMUSG00000046711. [P17095-2]
    GeneIDi111241.
    15361.
    KEGGimmu:111241.
    mmu:15361.
    UCSCiuc008boz.2. mouse. [P17095-2]

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    J04179 mRNA. Translation: AAA37820.1 .
    AF285780 Genomic DNA. Translation: AAK66158.1 .
    AF285780 Genomic DNA. Translation: AAK66159.1 .
    AK010617 mRNA. Translation: BAB27065.1 .
    BC013455 mRNA. Translation: AAH13455.1 .
    CCDSi CCDS28564.1. [P17095-2 ]
    CCDS49010.1. [P17095-2 ]
    CCDS50044.1. [P17095-1 ]
    PIRi A31895.
    RefSeqi NP_001020598.1. NM_001025427.3. [P17095-2 ]
    NP_001034445.1. NM_001039356.2. [P17095-2 ]
    NP_001159948.1. NM_001166476.1. [P17095-2 ]
    NP_001159949.1. NM_001166477.1. [P17095-1 ]
    NP_001160007.1. NM_001166535.1. [P17095-2 ]
    NP_001160008.1. NM_001166536.1. [P17095-2 ]
    NP_001160009.1. NM_001166537.1. [P17095-1 ]
    NP_001160011.1. NM_001166539.1. [P17095-1 ]
    NP_001160012.1. NM_001166540.1. [P17095-1 ]
    NP_001160013.1. NM_001166541.1. [P17095-1 ]
    NP_001160014.1. NM_001166542.1. [P17095-1 ]
    NP_057869.2. NM_016660.3. [P17095-2 ]
    UniGenei Mm.426212.
    Mm.440289.
    Mm.4438.

    3D structure databases

    ProteinModelPortali P17095.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 200340. 8 interactions.
    DIPi DIP-53N.
    IntActi P17095. 4 interactions.
    MINTi MINT-1848156.
    STRINGi 10090.ENSMUSP00000113015.

    PTM databases

    PhosphoSitei P17095.

    Proteomic databases

    PaxDbi P17095.
    PRIDEi P17095.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000105046 ; ENSMUSP00000100667 ; ENSMUSG00000078249 . [P17095-2 ]
    ENSMUST00000114888 ; ENSMUSP00000110538 ; ENSMUSG00000046711 . [P17095-1 ]
    ENSMUST00000117254 ; ENSMUSP00000113011 ; ENSMUSG00000046711 . [P17095-2 ]
    ENSMUST00000117600 ; ENSMUSP00000113068 ; ENSMUSG00000046711 . [P17095-2 ]
    ENSMUST00000118570 ; ENSMUSP00000114101 ; ENSMUSG00000046711 . [P17095-1 ]
    ENSMUST00000118599 ; ENSMUSP00000113015 ; ENSMUSG00000046711 . [P17095-2 ]
    ENSMUST00000119486 ; ENSMUSP00000113916 ; ENSMUSG00000046711 . [P17095-2 ]
    GeneIDi 111241.
    15361.
    KEGGi mmu:111241.
    mmu:15361.
    UCSCi uc008boz.2. mouse. [P17095-2 ]

    Organism-specific databases

    CTDi 111241.
    3159.
    MGIi MGI:96160. Hmga1.

    Phylogenomic databases

    eggNOGi NOG41800.
    HOGENOMi HOG000076308.
    HOVERGENi HBG063451.
    InParanoidi P17095.
    KOi K09282.
    OMAi QQEPSEA.
    OrthoDBi EOG71CFQJ.
    PhylomeDBi P17095.
    TreeFami TF351623.

    Enzyme and pathway databases

    Reactomei REACT_209428. Formation of Senescence-Associated Heterochromatin Foci (SAHF).

    Miscellaneous databases

    NextBioi 287980.
    PROi P17095.
    SOURCEi Search...

    Gene expression databases

    Bgeei P17095.
    CleanExi MM_HMGA1.
    Genevestigatori P17095.

    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. "Complete murine cDNA sequence, genomic structure, and tissue expression of the high mobility group protein HMG-I(Y)."
      Johnson K.R., Lehn D.A., Elton T.S., Barr P.J., Reeves R.
      J. Biol. Chem. 263:18338-18342(1988) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM HMG-Y).
    2. "Sequence and analysis of the murine Hmgiy (Hmga1) gene locus."
      Pedulla M.L., Treff N.R., Resar L.M.S., Reeves R.
      Gene 271:51-58(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORMS HMG-I AND HMG-Y).
      Strain: BALB/c.
    3. "The transcriptional landscape of the mammalian genome."
      Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
      , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
      Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM HMG-Y).
      Strain: C57BL/6J.
      Tissue: Embryonic stem cell.
    4. "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] (ISOFORM HMG-I).
      Strain: FVB/N.
      Tissue: Colon.
    5. "Mass spectrometric analysis of the HMGY protein from Lewis lung carcinoma. Identification of phosphorylation sites."
      Ferranti P., Malorni A., Marino G., Pucci P., Goodwin G.H., Manfioletti G., Giancotti V.
      J. Biol. Chem. 267:22486-22489(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION AT SER-99; SER-102 AND SER-103, ACETYLATION AT SER-2, IDENTIFICATION BY MASS SPECTROMETRY.
    6. "High mobility group I (Y) proteins bind HIPK2, a serine-threonine kinase protein which inhibits cell growth."
      Pierantoni G.M., Fedele M., Pentimalli F., Benvenuto G., Pero R., Viglietto G., Santoro M., Chiariotti L., Fusco A.
      Oncogene 20:6132-6141(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH HIPK2, PHOSPHORYLATION.
    7. "Comprehensive identification of phosphorylation sites in postsynaptic density preparations."
      Trinidad J.C., Specht C.G., Thalhammer A., Schoepfer R., Burlingame A.L.
      Mol. Cell. Proteomics 5:914-922(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Brain.
    8. "A differential phosphoproteomic analysis of retinoic acid-treated P19 cells."
      Smith J.C., Duchesne M.A., Tozzi P., Ethier M., Figeys D.
      J. Proteome Res. 6:3174-3186(2007) [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: Teratocarcinoma.
    9. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-102 AND SER-103, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Liver.
    10. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Embryonic fibroblast.
    11. "Specific phosphopeptide enrichment with immobilized titanium ion affinity chromatography adsorbent for phosphoproteome analysis."
      Zhou H., Ye M., Dong J., Han G., Jiang X., Wu R., Zou H.
      J. Proteome Res. 7:3957-3967(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-102 AND SER-103, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Liver.
    12. "Large scale localization of protein phosphorylation by use of electron capture dissociation mass spectrometry."
      Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.
      Mol. Cell. Proteomics 8:904-912(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-53; SER-99; SER-102 AND SER-103, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Embryonic fibroblast.
    13. "SIRT5-mediated lysine desuccinylation impacts diverse metabolic pathways."
      Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y., Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.
      Mol. Cell 50:919-930(2013) [PubMed] [Europe PMC] [Abstract]
      Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2; LYS-7 AND LYS-15, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Embryonic fibroblast.

    Entry informationi

    Entry nameiHMGA1_MOUSE
    AccessioniPrimary (citable) accession number: P17095
    Secondary accession number(s): Q91WV2, Q924L7, Q924L8
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: August 1, 1990
    Last sequence update: January 23, 2007
    Last modified: October 1, 2014
    This is version 149 of the entry and version 4 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. MGD cross-references
      Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
    2. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3