HMGA1_HUMAN
ID HMGA1_HUMAN Reviewed; 107 AA.
AC P17096; P10910; Q5T6U9; Q9UKB0;
DT 01-AUG-1990, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 236.
DE RecName: Full=High mobility group protein HMG-I/HMG-Y;
DE Short=HMG-I(Y);
DE AltName: Full=High mobility group AT-hook protein 1;
DE Short=High mobility group protein A1;
DE AltName: Full=High mobility group protein R;
GN Name=HMGA1; Synonyms=HMGIY;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS HMG-I AND HMG-Y).
RX PubMed=2505228; DOI=10.1093/nar/17.15.5947;
RA Eckner R., Birnstiel M.L.;
RT "Cloning of cDNAs coding for human HMG I and HMG Y proteins: both are
RT capable of binding to the octamer sequence motif.";
RL Nucleic Acids Res. 17:5947-5959(1989).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS HMG-I AND HMG-Y).
RX PubMed=2701943; DOI=10.1128/mcb.9.5.2114-2123.1989;
RA Johnson K.R., Lehn D.A., Reeves R.;
RT "Alternative processing of mRNAs encoding mammalian chromosomal high-
RT mobility-group proteins HMG-I and HMG-Y.";
RL Mol. Cell. Biol. 9:2114-2123(1989).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC TISSUE=Placenta;
RX PubMed=8414980; DOI=10.1093/nar/21.18.4259;
RA Friedmann M., Holth L.T., Zoghbi H.Y., Reeves R.;
RT "Organization, inducible-expression and chromosome localization of the
RT human HMG-I(Y) nonhistone protein gene.";
RL Nucleic Acids Res. 21:4259-4267(1993).
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM HMG-R).
RX PubMed=10428834; DOI=10.1074/jbc.274.32.22563;
RA Nagpal S., Ghosn C., DiSepio D., Molina Y., Sutter M., Klein E.S.,
RA Chandraratna R.A.S.;
RT "Retinoid-dependent recruitment of a histone H1 displacement activity by
RT retinoic acid receptor.";
RL J. Biol. Chem. 274:22563-22568(1999).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=14574404; DOI=10.1038/nature02055;
RA Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L.,
RA Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., Gilbert J.G.R.,
RA Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D.,
RA Andrews T.D., Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J.,
RA Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H.,
RA Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J.,
RA Brown J.Y., Burford D.C., Burrill W., Burton J., Carder C., Carter N.P.,
RA Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V.,
RA Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J.,
RA Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., Ellington A.E.,
RA Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J.,
RA French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J.,
RA Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C.,
RA Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A.,
RA Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R.,
RA Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M.,
RA Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K.,
RA Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R.,
RA Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M.,
RA Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A.,
RA Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L.,
RA Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I.,
RA Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y.,
RA Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E.,
RA Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A.,
RA Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W.,
RA Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M.,
RA West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J.,
RA Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M.,
RA Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I.,
RA Rogers J., Beck S.;
RT "The DNA sequence and analysis of human chromosome 6.";
RL Nature 425:805-811(2003).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS HMG-I AND HMG-Y).
RC TISSUE=B-cell, Mammary gland, Muscle, Pancreas, and Uterus;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [7]
RP PROTEIN SEQUENCE OF 4-107 (HMG-I).
RX PubMed=3619901; DOI=10.1016/0006-291x(87)90589-4;
RA Lund T., Dahl K.H., Mork E., Holtlund J., Laland S.G.;
RT "The human chromosomal protein HMG I contains two identical palindrome
RT amino acid sequences.";
RL Biochem. Biophys. Res. Commun. 146:725-730(1987).
RN [8]
RP PROTEIN SEQUENCE OF 4-107 (HMG-Y).
RX PubMed=2920035; DOI=10.1016/0006-291x(89)92770-8;
RA Karlson J.R., Mork E., Holtlund J., Laland S.G., Lund T.;
RT "The amino acid sequence of the chromosomal protein HMG-Y, its relation to
RT HMG-I and possible domains for the preferential binding of the proteins to
RT stretches of A-T base pairs.";
RL Biochem. Biophys. Res. Commun. 158:646-651(1989).
RN [9]
RP DNA-BINDING DOMAINS.
RX PubMed=1692833; DOI=10.1016/s0021-9258(19)38926-4;
RA Reeves R., Nissen M.S.;
RT "The A.T-DNA-binding domain of mammalian high mobility group I chromosomal
RT proteins. A novel peptide motif for recognizing DNA structure.";
RL J. Biol. Chem. 265:8573-8582(1990).
RN [10]
RP CHROMOSOMAL TRANSLOCATION WITH RAD51B.
RX PubMed=11978964; DOI=10.1159/000057011;
RA Blank C., Schoenmakers E.F.P.M., Rogalla P., Huys E.H., van Rijk A.A.,
RA Drieschner N., Bullerdiek J.;
RT "Intragenic breakpoint within RAD51L1 in a t(6;14)(p21.3;q24) of a
RT pulmonary chondroid hamartoma.";
RL Cytogenet. Cell Genet. 95:17-19(2001).
RN [11]
RP PHOSPHORYLATION, METHYLATION AT ARG-26, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RX PubMed=12653562; DOI=10.1021/bi027338l;
RA Sgarra R., Diana F., Bellarosa C., Dekleva V., Rustighi A., Toller M.,
RA Manfioletti G., Giancotti V.;
RT "During apoptosis of tumor cells HMGA1a protein undergoes methylation:
RT identification of the modification site by mass spectrometry.";
RL Biochemistry 42:3575-3585(2003).
RN [12]
RP METHYLATION BY PRMT6.
RX PubMed=16157300; DOI=10.1016/j.bbrc.2005.08.179;
RA Miranda T.B., Webb K.J., Edberg D.D., Reeves R., Clarke S.;
RT "Protein arginine methyltransferase 6 specifically methylates the
RT nonhistone chromatin protein HMGA1a.";
RL Biochem. Biophys. Res. Commun. 336:831-835(2005).
RN [13]
RP PHOSPHORYLATION AT SER-99; SER-102 AND SER-103, METHYLATION AT ARG-26, AND
RP MASS SPECTROMETRY.
RX PubMed=15835918; DOI=10.1021/bi0475525;
RA Zou Y., Wang Y.;
RT "Tandem mass spectrometry for the examination of the posttranslational
RT modifications of high-mobility group A1 proteins: symmetric and asymmetric
RT dimethylation of Arg25 in HMGA1a protein.";
RL Biochemistry 44:6293-6301(2005).
RN [14]
RP METHYLATION AT ARG-58 AND ARG-60 BY PRMT6, AND MUTAGENESIS OF ARG-26;
RP ARG-58 AND ARG-60.
RX PubMed=16159886; DOI=10.1074/jbc.m502458200;
RA Herrmann F., Lee J., Bedford M.T., Fackelmayer F.O.;
RT "Dynamics of human protein arginine methyltransferase 1(PRMT1) in vivo.";
RL J. Biol. Chem. 280:38005-38010(2005).
RN [15]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-36; SER-99; SER-102 AND
RP SER-103, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
RA Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.;
RT "Global, in vivo, and site-specific phosphorylation dynamics in signaling
RT networks.";
RL Cell 127:635-648(2006).
RN [16]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-36 AND THR-53,
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-42 (ISOFORM HMG-Y), AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=17924679; DOI=10.1021/pr070152u;
RA Yu L.R., Zhu Z., Chan K.C., Issaq H.J., Dimitrov D.S., Veenstra T.D.;
RT "Improved titanium dioxide enrichment of phosphopeptides from HeLa cells
RT and high confident phosphopeptide identification by cross-validation of
RT MS/MS and MS/MS/MS spectra.";
RL J. Proteome Res. 6:4150-4162(2007).
RN [17]
RP PHOSPHORYLATION AT SER-36; THR-53 AND THR-78 BY HIPK2 AND CDK1/CDC2
RP (ISOFORM HMG-I), AND PHOSPHORYLATION AT THR-42 AND THR-67 BY HIPK2 AND
RP CDK1/CDC2 (ISOFORM HMG-Y).
RX PubMed=17960875; DOI=10.1021/pr700571d;
RA Zhang Q., Wang Y.;
RT "Homeodomain-interacting protein kinase-2 (HIPK2) phosphorylates HMGA1a at
RT Ser-35, Thr-52, and Thr-77 and modulates its DNA binding affinity.";
RL J. Proteome Res. 6:4711-4719(2007).
RN [18]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-99; SER-102 AND SER-103, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic kidney;
RX PubMed=17525332; DOI=10.1126/science.1140321;
RA Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III, Hurov K.E.,
RA Luo J., Bakalarski C.E., Zhao Z., Solimini N., Lerenthal Y., Shiloh Y.,
RA Gygi S.P., Elledge S.J.;
RT "ATM and ATR substrate analysis reveals extensive protein networks
RT responsive to DNA damage.";
RL Science 316:1160-1166(2007).
RN [19]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=T-cell;
RX PubMed=19367720; DOI=10.1021/pr800500r;
RA Carrascal M., Ovelleiro D., Casas V., Gay M., Abian J.;
RT "Phosphorylation analysis of primary human T lymphocytes using sequential
RT IMAC and titanium oxide enrichment.";
RL J. Proteome Res. 7:5167-5176(2008).
RN [20]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-36; THR-39; SER-44; SER-49
RP AND THR-53, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [21]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=18318008; DOI=10.1002/pmic.200700884;
RA Han G., Ye M., Zhou H., Jiang X., Feng S., Jiang X., Tian R., Wan D.,
RA Zou H., Gu J.;
RT "Large-scale phosphoproteome analysis of human liver tissue by enrichment
RT and fractionation of phosphopeptides with strong anion exchange
RT chromatography.";
RL Proteomics 8:1346-1361(2008).
RN [22]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a
RT refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [23]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-99; SER-102 AND SER-103, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Leukemic T-cell;
RX PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA Rodionov V., Han D.K.;
RT "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT reveals system-wide modulation of protein-protein interactions.";
RL Sci. Signal. 2:RA46-RA46(2009).
RN [24]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-15, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19608861; DOI=10.1126/science.1175371;
RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C.,
RA Olsen J.V., Mann M.;
RT "Lysine acetylation targets protein complexes and co-regulates major
RT cellular functions.";
RL Science 325:834-840(2009).
RN [25]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-36; THR-53; SER-99; SER-102
RP AND SER-103, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [26]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [27]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-36; THR-53; SER-99 AND
RP SER-102, PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-42 (ISOFORM HMG-Y),
RP AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T.,
RA Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.;
RT "System-wide temporal characterization of the proteome and phosphoproteome
RT of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [28]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-terminal
RT acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN [29]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-9; SER-36; SER-44; THR-53;
RP SER-99; SER-102 AND SER-103, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE
RP SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma, and Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [30]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-36; THR-39; SER-44 AND
RP SER-49, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [31]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25944712; DOI=10.1002/pmic.201400617;
RA Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., Ayoub D.,
RA Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
RT "N-terminome analysis of the human mitochondrial proteome.";
RL Proteomics 15:2519-2524(2015).
RN [32]
RP ADP-RIBOSYLATION AT SER-8 AND SER-9.
RX PubMed=28190768; DOI=10.1016/j.molcel.2017.01.003;
RA Bonfiglio J.J., Fontana P., Zhang Q., Colby T., Gibbs-Seymour I.,
RA Atanassov I., Bartlett E., Zaja R., Ahel I., Matic I.;
RT "Serine ADP-ribosylation depends on HPF1.";
RL Mol. Cell 0:0-0(2017).
RN [33]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-15, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=28112733; DOI=10.1038/nsmb.3366;
RA Hendriks I.A., Lyon D., Young C., Jensen L.J., Vertegaal A.C.,
RA Nielsen M.L.;
RT "Site-specific mapping of the human SUMO proteome reveals co-modification
RT with phosphorylation.";
RL Nat. Struct. Mol. Biol. 24:325-336(2017).
RN [34]
RP STRUCTURE BY NMR OF 51-75 AND 80-89.
RX PubMed=9253416; DOI=10.1038/nsb0897-657;
RA Huth J.R., Bewley C.A., Nissen M.S., Evans J.N., Reeves R.,
RA Gronenborn A.M., Clore G.M.;
RT "The solution structure of an HMG-I(Y)-DNA complex defines a new
RT architectural minor groove binding motif.";
RL Nat. Struct. Biol. 4:657-665(1997).
CC -!- FUNCTION: HMG-I/Y bind preferentially to the minor groove of A+T rich
CC regions in double-stranded DNA. It is suggested that these proteins
CC could function in nucleosome phasing and in the 3'-end processing of
CC mRNA transcripts. They are also involved in the transcription
CC regulation of genes containing, or in close proximity to A+T-rich
CC regions.
CC -!- SUBUNIT: Interacts with HIPK2 (By similarity). {ECO:0000250}.
CC -!- INTERACTION:
CC P17096; Q9Y5N6: ORC6; NbExp=4; IntAct=EBI-746843, EBI-374840;
CC P17096-1; Q96LA8: PRMT6; NbExp=4; IntAct=EBI-746854, EBI-912440;
CC -!- SUBCELLULAR LOCATION: Nucleus. Chromosome.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=HMG-I; Synonyms=HMGA1a;
CC IsoId=P17096-1; Sequence=Displayed;
CC Name=HMG-Y; Synonyms=HMGA1b;
CC IsoId=P17096-2; Sequence=VSP_002182;
CC Name=HMG-R; Synonyms=HMGA1c;
CC IsoId=P17096-3; Sequence=VSP_018084;
CC -!- PTM: Constitutively phosphorylated on two or three sites.
CC Hyperphosphorylated at early stages of apoptosis, followed by
CC dephosphorylation and methylation, which coincides with chromatin
CC condensation. Isoforms HMG-I and HMG-Y can be phosphorylated by HIPK2.
CC Phosphorylation of HMG-I at Ser-36, Thr-53 and Thr-78 and of HMG-Y at
CC Thr-42 and Thr-67 by HIPK2 modulates DNA-binding affinity.
CC {ECO:0000269|PubMed:12653562, ECO:0000269|PubMed:15835918}.
CC -!- PTM: HMG-Y is not methylated.
CC -!- PTM: Methylation at Arg-58 is mutually exclusive with methylation at
CC Arg-60. {ECO:0000269|PubMed:16159886}.
CC -!- MASS SPECTROMETRY: [Isoform HMG-I]: Mass=11750; Mass_error=12;
CC Method=MALDI; Note=With 1 acetyl and 2 phosphate groups. The measured
CC range is 2-107.; Evidence={ECO:0000269|PubMed:15835918};
CC -!- MASS SPECTROMETRY: [Isoform HMG-I]: Mass=11828; Mass_error=12;
CC Method=MALDI; Note=With 1 acetyl and 3 phosphate groups. The measured
CC range is 2-107.; Evidence={ECO:0000269|PubMed:15835918};
CC -!- MASS SPECTROMETRY: [Isoform HMG-I]: Mass=11765; Mass_error=12;
CC Method=MALDI; Note=With 1 acetyl, 1 methyl and 2 phosphate groups. The
CC measured range is 2-107.; Evidence={ECO:0000269|PubMed:15835918};
CC -!- MASS SPECTROMETRY: [Isoform HMG-I]: Mass=11844; Mass_error=12;
CC Method=MALDI; Note=With 1 acetyl, 1 methyl and 3 phosphate groups. The
CC measured range is 2-107.; Evidence={ECO:0000269|PubMed:15835918};
CC -!- MASS SPECTROMETRY: [Isoform HMG-I]: Mass=11780; Mass_error=12;
CC Method=MALDI; Note=With 1 acetyl, 2 methyl and 2 phosphate groups. The
CC measured range is 2-107.; Evidence={ECO:0000269|PubMed:15835918};
CC -!- MASS SPECTROMETRY: [Isoform HMG-I]: Mass=11858; Mass_error=12;
CC Method=MALDI; Note=With 1 acetyl, 2 methyl and 3 phosphate groups. The
CC measured range is 2-107.; Evidence={ECO:0000269|PubMed:15835918};
CC -!- DISEASE: Note=A chromosomal aberration involving HMGA1 is found in
CC pulmonary chondroid hamartoma. Translocation t(6;14)(p21;q23-24) with
CC RAD51B. {ECO:0000269|PubMed:11978964}.
CC -!- SIMILARITY: Belongs to the HMGA family. {ECO:0000305}.
CC -!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology and
CC Haematology;
CC URL="http://atlasgeneticsoncology.org/Genes/HMGIYID221.html";
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DR EMBL; X14957; CAA33080.1; -; mRNA.
DR EMBL; X14958; CAA33081.1; -; mRNA.
DR EMBL; M23614; AAA88072.1; -; mRNA.
DR EMBL; M23615; AAA88073.1; -; mRNA.
DR EMBL; M23616; AAA88074.1; -; mRNA.
DR EMBL; M23617; AAA88075.1; -; mRNA.
DR EMBL; M23618; AAA88076.1; -; mRNA.
DR EMBL; M23619; AAA35998.1; -; mRNA.
DR EMBL; L17131; AAB00145.1; -; Genomic_DNA.
DR EMBL; AF176039; AAD53889.1; -; mRNA.
DR EMBL; AL354740; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC004924; AAH04924.1; -; mRNA.
DR EMBL; BC008832; AAH08832.1; -; mRNA.
DR EMBL; BC063434; AAH63434.1; -; mRNA.
DR EMBL; BC067083; AAH67083.1; -; mRNA.
DR EMBL; BC071864; AAH71864.1; -; mRNA.
DR CCDS; CCDS4788.1; -. [P17096-2]
DR CCDS; CCDS4789.1; -. [P17096-1]
DR PIR; A32794; A32794.
DR RefSeq; NP_001306006.1; NM_001319077.1. [P17096-2]
DR RefSeq; NP_001306007.1; NM_001319078.1. [P17096-1]
DR RefSeq; NP_001306008.1; NM_001319079.1. [P17096-1]
DR RefSeq; NP_001306009.1; NM_001319080.1.
DR RefSeq; NP_001306010.1; NM_001319081.1. [P17096-1]
DR RefSeq; NP_001306011.1; NM_001319082.1. [P17096-1]
DR RefSeq; NP_002122.1; NM_002131.3. [P17096-2]
DR RefSeq; NP_665906.1; NM_145899.2. [P17096-1]
DR RefSeq; NP_665908.1; NM_145901.2. [P17096-1]
DR RefSeq; NP_665909.1; NM_145902.2. [P17096-2]
DR RefSeq; NP_665910.1; NM_145903.2. [P17096-2]
DR RefSeq; NP_665912.1; NM_145905.2. [P17096-2]
DR PDB; 2EZD; NMR; -; A=51-71.
DR PDB; 2EZE; NMR; -; A=51-75.
DR PDB; 2EZF; NMR; -; A=80-89.
DR PDB; 2EZG; NMR; -; A=80-89.
DR PDBsum; 2EZD; -.
DR PDBsum; 2EZE; -.
DR PDBsum; 2EZF; -.
DR PDBsum; 2EZG; -.
DR AlphaFoldDB; P17096; -.
DR BMRB; P17096; -.
DR SMR; P17096; -.
DR BioGRID; 109402; 240.
DR DIP; DIP-29687N; -.
DR IntAct; P17096; 131.
DR MINT; P17096; -.
DR STRING; 9606.ENSP00000399888; -.
DR GlyGen; P17096; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; P17096; -.
DR PhosphoSitePlus; P17096; -.
DR SwissPalm; P17096; -.
DR BioMuta; HMGA1; -.
DR DMDM; 123377; -.
DR EPD; P17096; -.
DR jPOST; P17096; -.
DR MassIVE; P17096; -.
DR MaxQB; P17096; -.
DR PaxDb; P17096; -.
DR PeptideAtlas; P17096; -.
DR PRIDE; P17096; -.
DR ProteomicsDB; 53453; -. [P17096-1]
DR ProteomicsDB; 53454; -. [P17096-2]
DR ProteomicsDB; 53455; -. [P17096-3]
DR TopDownProteomics; P17096-1; -. [P17096-1]
DR TopDownProteomics; P17096-2; -. [P17096-2]
DR TopDownProteomics; P17096-3; -. [P17096-3]
DR Antibodypedia; 29318; 405 antibodies from 39 providers.
DR DNASU; 3159; -.
DR Ensembl; ENST00000311487.9; ENSP00000308227.4; ENSG00000137309.20. [P17096-1]
DR Ensembl; ENST00000347617.10; ENSP00000288245.9; ENSG00000137309.20. [P17096-2]
DR Ensembl; ENST00000374116.3; ENSP00000363230.3; ENSG00000137309.20. [P17096-2]
DR Ensembl; ENST00000401473.7; ENSP00000385693.2; ENSG00000137309.20. [P17096-2]
DR Ensembl; ENST00000447654.5; ENSP00000399888.1; ENSG00000137309.20. [P17096-1]
DR GeneID; 3159; -.
DR KEGG; hsa:3159; -.
DR MANE-Select; ENST00000311487.9; ENSP00000308227.4; NM_145899.3; NP_665906.1.
DR UCSC; uc003oit.4; human. [P17096-1]
DR CTD; 3159; -.
DR DisGeNET; 3159; -.
DR GeneCards; HMGA1; -.
DR HGNC; HGNC:5010; HMGA1.
DR HPA; ENSG00000137309; Tissue enhanced (esophagus).
DR MalaCards; HMGA1; -.
DR MIM; 600701; gene.
DR neXtProt; NX_P17096; -.
DR OpenTargets; ENSG00000137309; -.
DR PharmGKB; PA35094; -.
DR VEuPathDB; HostDB:ENSG00000137309; -.
DR eggNOG; ENOG502S5JW; Eukaryota.
DR GeneTree; ENSGT00730000111329; -.
DR HOGENOM; CLU_138888_0_0_1; -.
DR InParanoid; P17096; -.
DR OMA; HKKKQGP; -.
DR TreeFam; TF351623; -.
DR PathwayCommons; P17096; -.
DR Reactome; R-HSA-162592; Integration of provirus.
DR Reactome; R-HSA-164843; 2-LTR circle formation.
DR Reactome; R-HSA-175567; Integration of viral DNA into host genomic DNA.
DR Reactome; R-HSA-177539; Autointegration results in viral DNA circles.
DR Reactome; R-HSA-180689; APOBEC3G mediated resistance to HIV-1 infection.
DR Reactome; R-HSA-180910; Vpr-mediated nuclear import of PICs.
DR Reactome; R-HSA-2559584; Formation of Senescence-Associated Heterochromatin Foci (SAHF).
DR SignaLink; P17096; -.
DR SIGNOR; P17096; -.
DR BioGRID-ORCS; 3159; 444 hits in 1010 CRISPR screens.
DR ChiTaRS; HMGA1; human.
DR GeneWiki; HMGA1; -.
DR GenomeRNAi; 3159; -.
DR Pharos; P17096; Tbio.
DR PRO; PR:P17096; -.
DR Proteomes; UP000005640; Chromosome 6.
DR RNAct; P17096; protein.
DR Bgee; ENSG00000137309; Expressed in lower esophagus mucosa and 202 other tissues.
DR ExpressionAtlas; P17096; baseline and differential.
DR Genevisible; P17096; HS.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0005925; C:focal adhesion; HDA:UniProtKB.
DR GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0090575; C:RNA polymerase II transcription regulator complex; ISS:BHF-UCL.
DR GO; GO:0035985; C:senescence-associated heterochromatin focus; IDA:UniProtKB.
DR GO; GO:0005667; C:transcription regulator complex; TAS:UniProtKB.
DR GO; GO:0051575; F:5'-deoxyribose-5-phosphate lyase activity; IDA:UniProtKB.
DR GO; GO:0003682; F:chromatin binding; ISS:BHF-UCL.
DR GO; GO:0000987; F:cis-regulatory region sequence-specific DNA binding; IDA:CAFA.
DR GO; GO:0003677; F:DNA binding; TAS:ProtInc.
DR GO; GO:0003906; F:DNA-(apurinic or apyrimidinic site) endonuclease activity; IDA:UniProtKB.
DR GO; GO:0019899; F:enzyme binding; IPI:UniProtKB.
DR GO; GO:0003680; F:minor groove of adenine-thymine-rich DNA binding; IDA:CAFA.
DR GO; GO:0030374; F:nuclear receptor coactivator activity; IMP:UniProtKB.
DR GO; GO:0042974; F:nuclear retinoic acid receptor binding; IDA:UniProtKB.
DR GO; GO:0046965; F:nuclear retinoid X receptor binding; IDA:UniProtKB.
DR GO; GO:0042975; F:peroxisome proliferator activated receptor binding; IDA:UniProtKB.
DR GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; ISS:ARUK-UCL.
DR GO; GO:0030527; F:structural constituent of chromatin; TAS:ARUK-UCL.
DR GO; GO:0003713; F:transcription coactivator activity; ISS:ARUK-UCL.
DR GO; GO:0003712; F:transcription coregulator activity; IBA:GO_Central.
DR GO; GO:0001221; F:transcription coregulator binding; IDA:UniProtKB.
DR GO; GO:0006284; P:base-excision repair; IDA:UniProtKB.
DR GO; GO:0006268; P:DNA unwinding involved in DNA replication; NAS:UniProtKB.
DR GO; GO:0008285; P:negative regulation of cell population proliferation; IMP:UniProtKB.
DR GO; GO:0045892; P:negative regulation of transcription, DNA-templated; IMP:UniProtKB.
DR GO; GO:0006337; P:nucleosome disassembly; TAS:UniProtKB.
DR GO; GO:0090402; P:oncogene-induced cell senescence; IDA:UniProtKB.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; ISS:BHF-UCL.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IMP:UniProtKB.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; IBA:GO_Central.
DR DisProt; DP00040; -.
DR IDEAL; IID00145; -.
DR InterPro; IPR017956; AT_hook_DNA-bd_motif.
DR InterPro; IPR000116; HMGA.
DR InterPro; IPR031079; HMGA1_chordates.
DR InterPro; IPR000637; HMGI/Y_DNA-bd_CS.
DR PANTHER; PTHR23341:SF6; PTHR23341:SF6; 1.
DR PRINTS; PR00929; ATHOOK.
DR PRINTS; PR00930; HIGHMOBLTYIY.
DR SMART; SM00384; AT_hook; 3.
DR PROSITE; PS00354; HMGI_Y; 3.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; ADP-ribosylation; Alternative splicing;
KW Chromosomal rearrangement; Chromosome; Direct protein sequencing;
KW DNA-binding; Isopeptide bond; Methylation; Nucleus; Phosphoprotein;
KW Reference proteome; Repeat; Transcription; Transcription regulation;
KW Ubl conjugation.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:P17095"
FT CHAIN 2..107
FT /note="High mobility group protein HMG-I/HMG-Y"
FT /id="PRO_0000206708"
FT DNA_BIND 21..31
FT /note="A.T hook 1"
FT DNA_BIND 53..63
FT /note="A.T hook 2"
FT DNA_BIND 78..89
FT /note="A.T hook 3"
FT REGION 1..107
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 53..77
FT /note="Interaction with HIPK2"
FT /evidence="ECO:0000250"
FT COMPBIAS 1..15
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 2
FT /note="N-acetylserine"
FT /evidence="ECO:0000250|UniProtKB:P17095"
FT MOD_RES 7
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P17095"
FT MOD_RES 8
FT /note="ADP-ribosylserine"
FT /evidence="ECO:0000269|PubMed:28190768"
FT MOD_RES 9
FT /note="ADP-ribosylserine; alternate"
FT /evidence="ECO:0000269|PubMed:28190768"
FT MOD_RES 9
FT /note="Phosphoserine; alternate"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 15
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0007744|PubMed:19608861"
FT MOD_RES 26
FT /note="Asymmetric dimethylarginine; alternate"
FT /evidence="ECO:0000269|PubMed:12653562,
FT ECO:0000269|PubMed:15835918"
FT MOD_RES 26
FT /note="Omega-N-methylarginine; alternate"
FT /evidence="ECO:0000269|PubMed:12653562,
FT ECO:0000269|PubMed:15835918"
FT MOD_RES 26
FT /note="Symmetric dimethylarginine; alternate"
FT /evidence="ECO:0000269|PubMed:12653562,
FT ECO:0000269|PubMed:15835918"
FT MOD_RES 36
FT /note="Phosphoserine; by HIPK2 and CDC2"
FT /evidence="ECO:0007744|PubMed:17081983,
FT ECO:0007744|PubMed:17924679, ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
FT ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569"
FT MOD_RES 39
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:24275569"
FT MOD_RES 44
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569"
FT MOD_RES 49
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:24275569"
FT MOD_RES 53
FT /note="Phosphothreonine; by HIPK2 and CDC2"
FT /evidence="ECO:0007744|PubMed:17924679,
FT ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163"
FT MOD_RES 58
FT /note="Asymmetric dimethylarginine; by PRMT6; alternate"
FT /evidence="ECO:0000269|PubMed:16159886"
FT MOD_RES 58
FT /note="Omega-N-methylarginine; by PRMT6; alternate"
FT /evidence="ECO:0000269|PubMed:16159886"
FT MOD_RES 60
FT /note="Asymmetric dimethylarginine; by PRMT6; alternate"
FT /evidence="ECO:0000269|PubMed:16159886"
FT MOD_RES 60
FT /note="Omega-N-methylarginine; by PRMT6; alternate"
FT /evidence="ECO:0000269|PubMed:16159886"
FT MOD_RES 78
FT /note="Phosphothreonine; by HIPK2 and CDC2"
FT /evidence="ECO:0000269|PubMed:12653562"
FT MOD_RES 99
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:15835918,
FT ECO:0007744|PubMed:17081983, ECO:0007744|PubMed:17525332,
FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163"
FT MOD_RES 102
FT /note="Phosphoserine; by CK"
FT /evidence="ECO:0000269|PubMed:15835918,
FT ECO:0007744|PubMed:17081983, ECO:0007744|PubMed:17525332,
FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163"
FT MOD_RES 103
FT /note="Phosphoserine; by CK"
FT /evidence="ECO:0000269|PubMed:15835918,
FT ECO:0007744|PubMed:17081983, ECO:0007744|PubMed:17525332,
FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:23186163"
FT CROSSLNK 15
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2); alternate"
FT /evidence="ECO:0007744|PubMed:28112733"
FT VAR_SEQ 35..45
FT /note="Missing (in isoform HMG-Y)"
FT /evidence="ECO:0000303|PubMed:15489334,
FT ECO:0000303|PubMed:2505228, ECO:0000303|PubMed:2701943"
FT /id="VSP_002182"
FT VAR_SEQ 66..107
FT /note="NKGAAKTRKTTTTPGRKPRGRPKKLEKEEEEGISQESSEEEQ -> KNWRRR
FT KRRASRRSPRRRSSDPCVPPAPHWRSSFLLGLDSFAPLPPPPPLPQAHHHHRLWPPPPS
FT STCALTTTLHSTPAAAGLPWAEWGAVFPWPQFPAPPAHPRIHTCPPGQG (in
FT isoform HMG-R)"
FT /evidence="ECO:0000303|PubMed:10428834"
FT /id="VSP_018084"
FT MUTAGEN 26
FT /note="R->A: Does not affect methylation by PRMT6."
FT /evidence="ECO:0000269|PubMed:16159886"
FT MUTAGEN 58
FT /note="R->A: Decreases methylation by PRMT6. Abolishes
FT methylation by PRMT6; when associated with A-60."
FT /evidence="ECO:0000269|PubMed:16159886"
FT MUTAGEN 60
FT /note="R->A: Decreases methylation by PRMT6. Abolishes
FT methylation by PRMT6; when associated with A-58."
FT /evidence="ECO:0000269|PubMed:16159886"
FT CONFLICT 107
FT /note="Q -> QQQ (in Ref. 8; AA sequence)"
FT /evidence="ECO:0000305"
FT STRAND 53..55
FT /evidence="ECO:0007829|PDB:2EZE"
FT MOD_RES P17096-2:42
FT /note="Phosphothreonine"
FT /evidence="ECO:0000269|PubMed:17960875,
FT ECO:0007744|PubMed:17924679, ECO:0007744|PubMed:21406692"
FT MOD_RES P17096-2:67
FT /note="Phosphothreonine"
FT /evidence="ECO:0000269|PubMed:17960875"
SQ SEQUENCE 107 AA; 11676 MW; E9C4E3F2200914B8 CRC64;
MSESSSKSSQ PLASKQEKDG TEKRGRGRPR KQPPVSPGTA LVGSQKEPSE VPTPKRPRGR
PKGSKNKGAA KTRKTTTTPG RKPRGRPKKL EKEEEEGISQ ESSEEEQ
