HMGA2_HUMAN
ID HMGA2_HUMAN Reviewed; 109 AA.
AC P52926; E7EP85; E7EWA2; Q1M182; Q1M185; Q1M186; Q1M187; Q1M188;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 03-AUG-2022, entry version 203.
DE RecName: Full=High mobility group protein HMGI-C;
DE AltName: Full=High mobility group AT-hook protein 2;
GN Name=HMGA2; Synonyms=HMGIC;
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] (ISOFORM 1), AND CHROMOSOMAL TRANSLOCATION.
RC TISSUE=Hepatoma;
RX PubMed=8198613; DOI=10.1006/bbrc.1994.1669;
RA Patel U.A., Bandiera A., Manfioletti G., Giancotti V., Chau K.-Y.,
RA Crane-Robinson C.;
RT "Expression and cDNA cloning of human HMGI-C phosphoprotein.";
RL Biochem. Biophys. Res. Commun. 201:63-70(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORM 1).
RX PubMed=7670494; DOI=10.1038/ng0895-436;
RA Schoenmakers E.F.P.M., Wanschura S., Mols R., Bullerdiek J.,
RA van den Berghe H., van de Ven W.J.M.;
RT "Recurrent rearrangements in the high mobility group protein gene, HMGI-C,
RT in benign mesenchymal tumours.";
RL Nat. Genet. 10:436-444(1995).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=7501444; DOI=10.1093/nar/23.21.4262;
RA Chau K.-Y., Patel U.A., Lee K.-L.D., Lam H.-Y.P., Crane-Robinson C.;
RT "The gene for the human architectural transcription factor HMGI-C consists
RT of five exons each coding for a distinct functional element.";
RL Nucleic Acids Res. 23:4262-4266(1995).
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RX PubMed=8824803; DOI=10.1006/geno.1996.0033;
RA Ashar H.R., Cherath L., Przysybz K., Chada K.;
RT "Genomic characterization of human HMGIC, a member of the accessory
RT transcription factor family found at translocation breakpoints in
RT lipomas.";
RL Genomics 31:207-214(1996).
RN [5]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 2; 3; 4; 5 AND 6), AND ALTERNATIVE
RP SPLICING.
RC TISSUE=Fibroblast;
RX PubMed=15882911; DOI=10.1016/j.bbaexp.2005.03.006;
RA Hauke S., Leopold S., Schlueter C., Flohr A.M., Murua Escobar H.,
RA Rogalla P., Bullerdiek J.;
RT "Extensive expression studies revealed a complex alternative splicing
RT pattern of the HMGA2 gene.";
RL Biochim. Biophys. Acta 1729:24-31(2005).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16541075; DOI=10.1038/nature04569;
RA Scherer S.E., Muzny D.M., Buhay C.J., Chen R., Cree A., Ding Y.,
RA Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C.,
RA Hernandez J., Hodgson A.V., Hume J., Jackson A., Khan Z.M., Kovar-Smith C.,
RA Lewis L.R., Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R.,
RA Montgomery K.T., Morgan M.B., Nazareth L.V., Scott G., Sodergren E.,
RA Song X.-Z., Steffen D., Lovering R.C., Wheeler D.A., Worley K.C., Yuan Y.,
RA Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G.,
RA Chen Z., Clerc-Blankenburg K.P., Davis C., Delgado O., Dinh H.H.,
RA Draper H., Gonzalez-Garay M.L., Havlak P., Jackson L.R., Jacob L.S.,
RA Kelly S.H., Li L., Li Z., Liu J., Liu W., Lu J., Maheshwari M.,
RA Nguyen B.-V., Okwuonu G.O., Pasternak S., Perez L.M., Plopper F.J.H.,
RA Santibanez J., Shen H., Tabor P.E., Verduzco D., Waldron L., Wang Q.,
RA Williams G.A., Zhang J., Zhou J., Allen C.C., Amin A.G., Anyalebechi V.,
RA Bailey M., Barbaria J.A., Bimage K.E., Bryant N.P., Burch P.E.,
RA Burkett C.E., Burrell K.L., Calderon E., Cardenas V., Carter K., Casias K.,
RA Cavazos I., Cavazos S.R., Ceasar H., Chacko J., Chan S.N., Chavez D.,
RA Christopoulos C., Chu J., Cockrell R., Cox C.D., Dang M., Dathorne S.R.,
RA David R., Davis C.M., Davy-Carroll L., Deshazo D.R., Donlin J.E.,
RA D'Souza L., Eaves K.A., Egan A., Emery-Cohen A.J., Escotto M., Flagg N.,
RA Forbes L.D., Gabisi A.M., Garza M., Hamilton C., Henderson N.,
RA Hernandez O., Hines S., Hogues M.E., Huang M., Idlebird D.G., Johnson R.,
RA Jolivet A., Jones S., Kagan R., King L.M., Leal B., Lebow H., Lee S.,
RA LeVan J.M., Lewis L.C., London P., Lorensuhewa L.M., Loulseged H.,
RA Lovett D.A., Lucier A., Lucier R.L., Ma J., Madu R.C., Mapua P.,
RA Martindale A.D., Martinez E., Massey E., Mawhiney S., Meador M.G.,
RA Mendez S., Mercado C., Mercado I.C., Merritt C.E., Miner Z.L., Minja E.,
RA Mitchell T., Mohabbat F., Mohabbat K., Montgomery B., Moore N., Morris S.,
RA Munidasa M., Ngo R.N., Nguyen N.B., Nickerson E., Nwaokelemeh O.O.,
RA Nwokenkwo S., Obregon M., Oguh M., Oragunye N., Oviedo R.J., Parish B.J.,
RA Parker D.N., Parrish J., Parks K.L., Paul H.A., Payton B.A., Perez A.,
RA Perrin W., Pickens A., Primus E.L., Pu L.-L., Puazo M., Quiles M.M.,
RA Quiroz J.B., Rabata D., Reeves K., Ruiz S.J., Shao H., Sisson I.,
RA Sonaike T., Sorelle R.P., Sutton A.E., Svatek A.F., Svetz L.A.,
RA Tamerisa K.S., Taylor T.R., Teague B., Thomas N., Thorn R.D., Trejos Z.Y.,
RA Trevino B.K., Ukegbu O.N., Urban J.B., Vasquez L.I., Vera V.A.,
RA Villasana D.M., Wang L., Ward-Moore S., Warren J.T., Wei X., White F.,
RA Williamson A.L., Wleczyk R., Wooden H.S., Wooden S.H., Yen J., Yoon L.,
RA Yoon V., Zorrilla S.E., Nelson D., Kucherlapati R., Weinstock G.,
RA Gibbs R.A.;
RT "The finished DNA sequence of human chromosome 12.";
RL Nature 440:346-351(2006).
RN [7]
RP PROTEIN SEQUENCE OF 2-27, CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION AT
RP SER-2, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC TISSUE=Hepatoma;
RA Bienvenut W.V., Fleming J., Leug H.Y.;
RL Submitted (JAN-2010) to UniProtKB.
RN [8]
RP CHROMOSOMAL TRANSLOCATION WITH LPP.
RX PubMed=9772904; DOI=10.1016/s0165-4608(98)00038-7;
RA Petit M.M., Swarts S., Bridge J.A., Van de Ven W.J.M.;
RT "Expression of reciprocal fusion transcripts of the HMGIC and LPP genes in
RT parosteal lipoma.";
RL Cancer Genet. Cytogenet. 106:18-23(1998).
RN [9]
RP CHROMOSOMAL TRANSLOCATION WITH RAD51B.
RX PubMed=9892177;
RA Schoenmakers E.F.P.M., Huysmans C., Van de Ven W.J.M.;
RT "Allelic knockout of novel splice variants of human recombination repair
RT gene RAD51B in t(12;14) uterine leiomyomas.";
RL Cancer Res. 59:19-23(1999).
RN [10]
RP CHROMOSOMAL TRANSLOCATION WITH LPP.
RX PubMed=11066083;
RX DOI=10.1002/1098-2264(2000)9999:9999<1::aid-gcc1043>3.0.co;2-n;
RA Rogalla P., Lemke I., Kazmierczak B., Bullerdiek J.;
RT "An identical HMGIC-LPP fusion transcript is consistently expressed in
RT pulmonary chondroid hamartomas with t(3;12)(q27-28;q14-15).";
RL Genes Chromosomes Cancer 29:363-366(2000).
RN [11]
RP CHROMOSOMAL TRANSLOCATION WITH RAD51B.
RX PubMed=12649198;
RA Quade B.J., Weremowicz S., Neskey D.M., Vanni R., Ladd C., Dal Cin P.,
RA Morton C.C.;
RT "Fusion transcripts involving HMGA2 are not a common molecular mechanism in
RT uterine leiomyomata with rearrangements in 12q15.";
RL Cancer Res. 63:1351-1358(2003).
RN [12]
RP FUNCTION, AND INTERACTION WITH E4F1.
RX PubMed=14645522; DOI=10.1128/mcb.23.24.9104-9116.2003;
RA Tessari M.A., Gostissa M., Altamura S., Sgarra R., Rustighi A.,
RA Salvagno C., Caretti G., Imbriano C., Mantovani R., Del Sal G.,
RA Giancotti V., Manfioletti G.;
RT "Transcriptional activation of the cyclin A gene by the architectural
RT transcription factor HMGA2.";
RL Mol. Cell. Biol. 23:9104-9116(2003).
RN [13]
RP INVOLVEMENT IN STQTL9.
RX PubMed=17767157; DOI=10.1038/ng2121;
RG The Diabetes Genetics Initiative;
RG The Wellcome Trust case control consortium;
RA Weedon M.N., Lettre G., Freathy R.M., Lindgren C.M., Voight B.F.,
RA Perry J.R.B., Elliott K.S., Hackett R., Guiducci C., Shields B.,
RA Zeggini E., Lango H., Lyssenko V., Timpson N.J., Burtt N.P., Rayner N.W.,
RA Saxena R., Ardlie K., Tobias J.H., Ness A.R., Ring S.M., Palmer C.N.A.,
RA Morris A.D., Peltonen L., Salomaa V., Smith G.D., Groop L.C.,
RA Hattersley A.T., McCarthy M.I., Hirschhorn J.N., Frayling T.M.;
RT "A common variant of HMGA2 is associated with adult and childhood height in
RT the general population.";
RL Nat. Genet. 39:1245-1250(2007).
RN [14]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [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 [15]
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 [16]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-40; SER-44 AND SER-105, AND
RP 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 [17]
RP INVOLVEMENT IN SRS5.
RX PubMed=25809938; DOI=10.1038/jhg.2015.29;
RA De Crescenzo A., Citro V., Freschi A., Sparago A., Palumbo O.,
RA Cubellis M.V., Carella M., Castelluccio P., Cavaliere M.L., Cerrato F.,
RA Riccio A.;
RT "A splicing mutation of the HMGA2 gene is associated with Silver-Russell
RT syndrome phenotype.";
RL J. Hum. Genet. 60:287-293(2015).
RN [18]
RP FUNCTION, INVOLVEMENT IN SRS5, AND VARIANT SRS5 65-GLN--ASP-109 DEL.
RX PubMed=28796236; DOI=10.1038/gim.2017.105;
RA Abi Habib W., Brioude F., Edouard T., Bennett J.T., Lienhardt-Roussie A.,
RA Tixier F., Salem J., Yuen T., Azzi S., Le Bouc Y., Harbison M.D.,
RA Netchine I.;
RT "Genetic disruption of the oncogenic HMGA2-PLAG1-IGF2 pathway causes fetal
RT growth restriction.";
RL Genet. Med. 20:250-258(2018).
CC -!- FUNCTION: Functions as a transcriptional regulator. Functions in cell
CC cycle regulation through CCNA2. Plays an important role in chromosome
CC condensation during the meiotic G2/M transition of spermatocytes. Plays
CC a role in postnatal myogenesis, is involved in satellite cell
CC activation (By similarity). Positively regulates IGF2 expression
CC through PLAG1 and in a PLAG1-independent manner (PubMed:28796236).
CC {ECO:0000250|UniProtKB:P52927, ECO:0000269|PubMed:14645522,
CC ECO:0000269|PubMed:28796236}.
CC -!- SUBUNIT: Interacts with E4F1 (PubMed:14645522). Interacts with NEK2 (By
CC similarity). {ECO:0000250|UniProtKB:P52927,
CC ECO:0000269|PubMed:14645522}.
CC -!- INTERACTION:
CC P52926; Q96LA8: PRMT6; NbExp=2; IntAct=EBI-912511, EBI-912440;
CC P52926; Q01196: RUNX1; NbExp=2; IntAct=EBI-912511, EBI-925904;
CC -!- SUBCELLULAR LOCATION: Nucleus.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=6;
CC Comment=Additional isoforms seem to exist.;
CC Name=1; Synonyms=HMGA2a;
CC IsoId=P52926-1; Sequence=Displayed;
CC Name=2; Synonyms=HMGA2f;
CC IsoId=P52926-2; Sequence=VSP_042564;
CC Name=3; Synonyms=HMGA2d';
CC IsoId=P52926-3; Sequence=VSP_047772;
CC Name=4; Synonyms=HMGA2d;
CC IsoId=P52926-4; Sequence=VSP_047773;
CC Name=5; Synonyms=HMGA2c';
CC IsoId=P52926-5; Sequence=VSP_047774;
CC Name=6; Synonyms=HMGA2c;
CC IsoId=P52926-6; Sequence=VSP_047775;
CC -!- DEVELOPMENTAL STAGE: Expressed predominantly during embryogenesis.
CC -!- PTM: Regulated by cell cycle-dependent phosphorylation which alters its
CC DNA binding affinity. Phosphorylated by NEK2 (By similarity).
CC {ECO:0000250|UniProtKB:P52927}.
CC -!- POLYMORPHISM: Genetic variations in HMGA2 define the stature
CC quantitative trait locus 9 (STQTL9) [MIM:611547]. Human height is a
CC classic, highly heritable quantitative trait.
CC {ECO:0000269|PubMed:17767157}.
CC -!- DISEASE: Silver-Russell syndrome 5 (SRS5) [MIM:618908]: A form of
CC Silver-Russell syndrome, a clinically heterogeneous condition
CC characterized by severe intrauterine growth retardation, poor postnatal
CC growth, craniofacial features such as a triangular shaped face and a
CC broad forehead, body asymmetry, and a variety of minor malformations.
CC The phenotypic expression changes during childhood and adolescence,
CC with the facial features and asymmetry usually becoming more subtle
CC with age. SRS5 inheritance is autosomal dominant.
CC {ECO:0000269|PubMed:25809938, ECO:0000269|PubMed:28796236}. Note=The
CC disease is caused by variants affecting the gene represented in this
CC entry.
CC -!- DISEASE: Note=A chromosomal aberration involving HMGA2 is associated
CC with a subclass of benign mesenchymal tumors known as lipomas.
CC Translocation t(3;12)(q27-q28;q13-q15) with LPP is shown in lipomas.
CC HMGA2 is also fused with a number of other genes in lipomas.
CC {ECO:0000269|PubMed:8824803}.
CC -!- DISEASE: Note=A chromosomal aberration involving HMGA2 is associated
CC with pulmonary chondroid hamartomas. Translocation t(3;12)(q27-q28;q14-
CC q15) with LPP is detected in pulmonary chondroid hamartomas.
CC {ECO:0000269|PubMed:11066083}.
CC -!- DISEASE: Note=A chromosomal aberration involving HMGA2 is associated
CC with parosteal lipomas. Translocation t(3;12)(q28;q14) with LPP is also
CC shown in one parosteal lipoma. {ECO:0000269|PubMed:9772904}.
CC -!- DISEASE: Note=A chromosomal aberration involving HMGA2 is found in
CC uterine leiomyoma. Translocation t(12;14)(q15;q23-24) with RAD51B.
CC Chromosomal rearrangements involving HMGA2 do not seem to be the
CC principle pathobiological mechanism in uterine leiomyoma.
CC {ECO:0000269|PubMed:12649198, ECO:0000269|PubMed:9892177}.
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/HMGICID82.html";
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DR EMBL; Z31595; CAA83472.1; -; mRNA.
DR EMBL; U28749; AAA68613.1; -; mRNA.
DR EMBL; U28754; AAA68614.1; -; Genomic_DNA.
DR EMBL; U28750; AAA68614.1; JOINED; Genomic_DNA.
DR EMBL; U28751; AAA68614.1; JOINED; Genomic_DNA.
DR EMBL; U28752; AAA68614.1; JOINED; Genomic_DNA.
DR EMBL; U28753; AAA68614.1; JOINED; Genomic_DNA.
DR EMBL; L46353; AAA96484.1; -; Genomic_DNA.
DR EMBL; L41044; AAA96484.1; JOINED; Genomic_DNA.
DR EMBL; L44578; AAA96484.1; JOINED; Genomic_DNA.
DR EMBL; X92518; CAA63295.1; -; mRNA.
DR EMBL; AY601861; AAU43851.1; -; mRNA.
DR EMBL; AY601862; AAU43852.1; -; mRNA.
DR EMBL; AY601863; AAU43853.1; -; mRNA.
DR EMBL; AY601864; AAU43854.1; -; mRNA.
DR EMBL; AY601867; AAU43857.1; -; mRNA.
DR EMBL; AC090673; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC107308; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR CCDS; CCDS31854.1; -. [P52926-2]
DR CCDS; CCDS44936.1; -. [P52926-1]
DR CCDS; CCDS81709.1; -. [P52926-6]
DR PIR; JC2232; JC2232.
DR RefSeq; NP_001317119.1; NM_001330190.1. [P52926-6]
DR RefSeq; NP_003474.1; NM_003483.4. [P52926-1]
DR RefSeq; NP_003475.1; NM_003484.1. [P52926-2]
DR AlphaFoldDB; P52926; -.
DR BioGRID; 113763; 77.
DR IntAct; P52926; 17.
DR MINT; P52926; -.
DR STRING; 9606.ENSP00000437621; -.
DR iPTMnet; P52926; -.
DR PhosphoSitePlus; P52926; -.
DR BioMuta; HMGA2; -.
DR DMDM; 1708263; -.
DR EPD; P52926; -.
DR jPOST; P52926; -.
DR MassIVE; P52926; -.
DR MaxQB; P52926; -.
DR PaxDb; P52926; -.
DR PeptideAtlas; P52926; -.
DR PRIDE; P52926; -.
DR ProteomicsDB; 56551; -. [P52926-1]
DR ProteomicsDB; 56552; -. [P52926-2]
DR ProteomicsDB; 61224; -.
DR ProteomicsDB; 61225; -.
DR ProteomicsDB; 61226; -.
DR ProteomicsDB; 61227; -.
DR TopDownProteomics; P52926-1; -. [P52926-1]
DR TopDownProteomics; P52926-2; -. [P52926-2]
DR Antibodypedia; 4500; 287 antibodies from 43 providers.
DR DNASU; 8091; -.
DR Ensembl; ENST00000354636.7; ENSP00000346658.3; ENSG00000149948.14. [P52926-2]
DR Ensembl; ENST00000393578.7; ENSP00000377206.3; ENSG00000149948.14. [P52926-6]
DR Ensembl; ENST00000403681.7; ENSP00000384026.2; ENSG00000149948.14. [P52926-1]
DR Ensembl; ENST00000425208.6; ENSP00000407306.2; ENSG00000149948.14. [P52926-4]
DR Ensembl; ENST00000537275.5; ENSP00000437747.1; ENSG00000149948.14. [P52926-5]
DR Ensembl; ENST00000537429.5; ENSP00000443372.1; ENSG00000149948.14. [P52926-3]
DR GeneID; 8091; -.
DR KEGG; hsa:8091; -.
DR MANE-Select; ENST00000403681.7; ENSP00000384026.2; NM_003483.6; NP_003474.1.
DR UCSC; uc001sss.2; human. [P52926-1]
DR CTD; 8091; -.
DR DisGeNET; 8091; -.
DR GeneCards; HMGA2; -.
DR GeneReviews; HMGA2; -.
DR HGNC; HGNC:5009; HMGA2.
DR HPA; ENSG00000149948; Tissue enhanced (bone marrow, testis).
DR MalaCards; HMGA2; -.
DR MIM; 150699; phenotype.
DR MIM; 600698; gene.
DR MIM; 611547; phenotype.
DR MIM; 618908; phenotype.
DR neXtProt; NX_P52926; -.
DR OpenTargets; ENSG00000149948; -.
DR Orphanet; 94063; 12q14 microdeletion syndrome.
DR Orphanet; 99970; Dedifferentiated liposarcoma.
DR Orphanet; 454821; Pleomorphic salivary gland adenoma.
DR Orphanet; 397590; Silver-Russell syndrome due to a point mutation.
DR Orphanet; 99971; Well-differentiated liposarcoma.
DR PharmGKB; PA30059; -.
DR PharmGKB; PA35093; -.
DR VEuPathDB; HostDB:ENSG00000149948; -.
DR eggNOG; ENOG502S80S; Eukaryota.
DR GeneTree; ENSGT00940000163109; -.
DR HOGENOM; CLU_138888_1_0_1; -.
DR InParanoid; P52926; -.
DR OMA; KPIGIRR; -.
DR PhylomeDB; P52926; -.
DR TreeFam; TF351623; -.
DR PathwayCommons; P52926; -.
DR Reactome; R-HSA-2559584; Formation of Senescence-Associated Heterochromatin Foci (SAHF).
DR SignaLink; P52926; -.
DR SIGNOR; P52926; -.
DR BioGRID-ORCS; 8091; 14 hits in 1079 CRISPR screens.
DR ChiTaRS; HMGA2; human.
DR GeneWiki; HMGA2; -.
DR GenomeRNAi; 8091; -.
DR Pharos; P52926; Tbio.
DR PRO; PR:P52926; -.
DR Proteomes; UP000005640; Chromosome 12.
DR RNAct; P52926; protein.
DR Bgee; ENSG00000149948; Expressed in sural nerve and 101 other tissues.
DR ExpressionAtlas; P52926; baseline and differential.
DR Genevisible; P52926; HS.
DR GO; GO:0000228; C:nuclear chromosome; ISS:UniProtKB.
DR GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0032993; C:protein-DNA complex; IDA:UniProtKB.
DR GO; GO:0035985; C:senescence-associated heterochromatin focus; IDA:UniProtKB.
DR GO; GO:0071141; C:SMAD protein complex; IDA:UniProtKB.
DR GO; GO:0051575; F:5'-deoxyribose-5-phosphate lyase activity; IDA:UniProtKB.
DR GO; GO:0070742; F:C2H2 zinc finger domain binding; IMP:UniProtKB.
DR GO; GO:0035497; F:cAMP response element binding; IDA:UniProtKB.
DR GO; GO:0008301; F:DNA binding, bending; IDA:UniProtKB.
DR GO; GO:0003906; F:DNA-(apurinic or apyrimidinic site) endonuclease activity; IDA:UniProtKB.
DR GO; GO:0035501; F:MH1 domain binding; IDA:UniProtKB.
DR GO; GO:0035500; F:MH2 domain binding; IDA:UniProtKB.
DR GO; GO:0003680; F:minor groove of adenine-thymine-rich DNA binding; IDA:UniProtKB.
DR GO; GO:0031492; F:nucleosomal DNA binding; IDA:UniProtKB.
DR GO; GO:0061629; F:RNA polymerase II-specific DNA-binding transcription factor binding; IPI:UniProtKB.
DR GO; GO:0046332; F:SMAD binding; IPI:UniProtKB.
DR GO; GO:0000976; F:transcription cis-regulatory region binding; IDA:UniProtKB.
DR GO; GO:0003712; F:transcription coregulator activity; IBA:GO_Central.
DR GO; GO:0003714; F:transcription corepressor activity; IDA:GO_Central.
DR GO; GO:0006284; P:base-excision repair; IDA:UniProtKB.
DR GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR GO; GO:0002062; P:chondrocyte differentiation; IDA:UniProtKB.
DR GO; GO:0035988; P:chondrocyte proliferation; IDA:UniProtKB.
DR GO; GO:0006325; P:chromatin organization; TAS:UniProtKB.
DR GO; GO:0030261; P:chromosome condensation; IEA:UniProtKB-KW.
DR GO; GO:0035987; P:endodermal cell differentiation; IMP:UniProtKB.
DR GO; GO:0001837; P:epithelial to mesenchymal transition; IMP:UniProtKB.
DR GO; GO:0045444; P:fat cell differentiation; IMP:UniProtKB.
DR GO; GO:0031507; P:heterochromatin assembly; IDA:UniProtKB.
DR GO; GO:0035556; P:intracellular signal transduction; IDA:UniProtKB.
DR GO; GO:0048762; P:mesenchymal cell differentiation; IMP:UniProtKB.
DR GO; GO:0048333; P:mesodermal cell differentiation; IMP:UniProtKB.
DR GO; GO:0003131; P:mesodermal-endodermal cell signaling; IMP:UniProtKB.
DR GO; GO:0043922; P:negative regulation by host of viral transcription; IDA:UniProtKB.
DR GO; GO:0043066; P:negative regulation of apoptotic process; IDA:UniProtKB.
DR GO; GO:2000773; P:negative regulation of cellular senescence; ISS:BHF-UCL.
DR GO; GO:0043392; P:negative regulation of DNA binding; IDA:UniProtKB.
DR GO; GO:2001033; P:negative regulation of double-strand break repair via nonhomologous end joining; IDA:UniProtKB.
DR GO; GO:0045869; P:negative regulation of single stranded viral RNA replication via double stranded DNA intermediate; IDA:UniProtKB.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IDA:UniProtKB.
DR GO; GO:0045892; P:negative regulation of transcription, DNA-templated; IDA:UniProtKB.
DR GO; GO:0090402; P:oncogene-induced cell senescence; IDA:UniProtKB.
DR GO; GO:0045766; P:positive regulation of angiogenesis; ISS:BHF-UCL.
DR GO; GO:0071864; P:positive regulation of cell proliferation in bone marrow; ISS:BHF-UCL.
DR GO; GO:0010628; P:positive regulation of gene expression; IDA:UniProtKB.
DR GO; GO:0071902; P:positive regulation of protein serine/threonine kinase activity; IDA:UniProtKB.
DR GO; GO:2000648; P:positive regulation of stem cell proliferation; IDA:UniProtKB.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IDA:UniProtKB.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IDA:UniProtKB.
DR GO; GO:0010564; P:regulation of cell cycle process; IDA:UniProtKB.
DR GO; GO:0040008; P:regulation of growth; IEA:UniProtKB-KW.
DR GO; GO:2000036; P:regulation of stem cell population maintenance; IMP:UniProtKB.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; IMP:UniProtKB.
DR GO; GO:0009615; P:response to virus; IEP:UniProtKB.
DR GO; GO:0048863; P:stem cell differentiation; IEP:UniProtKB.
DR DisProt; DP01876; -.
DR InterPro; IPR017956; AT_hook_DNA-bd_motif.
DR InterPro; IPR000116; HMGA.
DR InterPro; IPR000637; HMGI/Y_DNA-bd_CS.
DR Pfam; PF02178; AT_hook; 3.
DR PRINTS; PR00929; ATHOOK.
DR PRINTS; PR00930; HIGHMOBLTYIY.
DR SMART; SM00384; AT_hook; 3.
DR PROSITE; PS00354; HMGI_Y; 2.
PE 1: Evidence at protein level;
KW Acetylation; Alternative splicing; Cell cycle; Cell division;
KW Chromosomal rearrangement; Direct protein sequencing; Disease variant;
KW DNA condensation; DNA-binding; Dwarfism; Growth regulation; Mitosis;
KW Nucleus; Phosphoprotein; Proto-oncogene; Reference proteome; Repeat;
KW Transcription; Transcription regulation.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|Ref.7, ECO:0007744|PubMed:19413330"
FT CHAIN 2..109
FT /note="High mobility group protein HMGI-C"
FT /id="PRO_0000206711"
FT DNA_BIND 24..34
FT /note="A.T hook 1"
FT DNA_BIND 44..54
FT /note="A.T hook 2"
FT DNA_BIND 71..82
FT /note="A.T hook 3"
FT REGION 1..109
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 44..63
FT /note="Interaction with E4F1"
FT /evidence="ECO:0000269|PubMed:14645522"
FT COMPBIAS 1..20
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 2
FT /note="N-acetylserine"
FT /evidence="ECO:0000269|Ref.7, ECO:0007744|PubMed:19413330"
FT MOD_RES 40
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:21406692"
FT MOD_RES 44
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21406692"
FT MOD_RES 101
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P52927"
FT MOD_RES 105
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21406692"
FT VAR_SEQ 84..109
FT /note="PQQVVQKKPAQEETEETSSQESAEED -> DNLLPRTSSKKKTSLGNSTKRS
FT H (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15882911"
FT /id="VSP_042564"
FT VAR_SEQ 84..109
FT /note="PQQVVQKKPAQEETEETSSQESAEED -> LQN (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:15882911"
FT /id="VSP_047772"
FT VAR_SEQ 84..109
FT /note="PQQVVQKKPAQEETEETSSQESAEED -> WLLMKSPCW (in isoform
FT 4)"
FT /evidence="ECO:0000303|PubMed:15882911"
FT /id="VSP_047773"
FT VAR_SEQ 84..109
FT /note="PQQVVQKKPAQEETEETSSQESAEED -> LRAQALDSDGLGSNSGPSLS
FT (in isoform 5)"
FT /evidence="ECO:0000303|PubMed:15882911"
FT /id="VSP_047774"
FT VAR_SEQ 84..109
FT /note="PQQVVQKKPAQEETEETSSQESAEED -> EEFYIAA (in isoform
FT 6)"
FT /evidence="ECO:0000303|PubMed:15882911"
FT /id="VSP_047775"
FT VARIANT 65..109
FT /note="Missing (in SRS5)"
FT /evidence="ECO:0000269|PubMed:28796236"
FT /id="VAR_084335"
SQ SEQUENCE 109 AA; 11832 MW; F36BABE623DA4615 CRC64;
MSARGEGAGQ PSTSAQGQPA APAPQKRGRG RPRKQQQEPT GEPSPKRPRG RPKGSKNKSP
SKAAQKKAEA TGEKRPRGRP RKWPQQVVQK KPAQEETEET SSQESAEED
