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High mobility group protein HMGI-C (High mobility group AT-hook protein 2)

 HMGA2_HUMAN             Reviewed;         109 AA.
P52926; E7EP85; E7EWA2; Q1M182; Q1M185; Q1M186; Q1M187; Q1M188;
01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
01-OCT-1996, sequence version 1.
27-SEP-2017, entry version 170.
RecName: Full=High mobility group protein HMGI-C;
AltName: Full=High mobility group AT-hook protein 2;
Name=HMGA2; Synonyms=HMGIC;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND CHROMOSOMAL TRANSLOCATION.
TISSUE=Hepatoma;
PubMed=8198613; DOI=10.1006/bbrc.1994.1669;
Patel U.A., Bandiera A., Manfioletti G., Giancotti V., Chau K.-Y.,
Crane-Robinson C.;
"Expression and cDNA cloning of human HMGI-C phosphoprotein.";
Biochem. Biophys. Res. Commun. 201:63-70(1994).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORM 1).
PubMed=7670494; DOI=10.1038/ng0895-436;
Schoenmakers E.F.P.M., Wanschura S., Mols R., Bullerdiek J.,
van den Berghe H., van de Ven W.J.M.;
"Recurrent rearrangements in the high mobility group protein gene,
HMGI-C, in benign mesenchymal tumours.";
Nat. Genet. 10:436-444(1995).
[3]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=7501444; DOI=10.1093/nar/23.21.4262;
Chau K.-Y., Patel U.A., Lee K.-L.D., Lam H.-Y.P., Crane-Robinson C.;
"The gene for the human architectural transcription factor HMGI-C
consists of five exons each coding for a distinct functional
element.";
Nucleic Acids Res. 23:4262-4266(1995).
[4]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
PubMed=8824803; DOI=10.1006/geno.1996.0033;
Ashar H.R., Cherath L., Przysybz K., Chada K.;
"Genomic characterization of human HMGIC, a member of the accessory
transcription factor family found at translocation breakpoints in
lipomas.";
Genomics 31:207-214(1996).
[5]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 2; 3; 4; 5 AND 6), AND
ALTERNATIVE SPLICING.
TISSUE=Fibroblast;
PubMed=15882911; DOI=10.1016/j.bbaexp.2005.03.006;
Hauke S., Leopold S., Schlueter C., Flohr A.M., Murua Escobar H.,
Rogalla P., Bullerdiek J.;
"Extensive expression studies revealed a complex alternative splicing
pattern of the HMGA2 gene.";
Biochim. Biophys. Acta 1729:24-31(2005).
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=16541075; DOI=10.1038/nature04569;
Scherer S.E., Muzny D.M., Buhay C.J., Chen R., Cree A., Ding Y.,
Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C.,
Hernandez J., Hodgson A.V., Hume J., Jackson A., Khan Z.M.,
Kovar-Smith C., Lewis L.R., Lozado R.J., Metzker M.L.,
Milosavljevic A., Miner G.R., Montgomery K.T., Morgan M.B.,
Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D.,
Lovering R.C., Wheeler D.A., Worley K.C., Yuan Y., Zhang Z.,
Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z.,
Clerc-Blankenburg K.P., Davis C., Delgado O., Dinh H.H., Draper H.,
Gonzalez-Garay M.L., Havlak P., Jackson L.R., Jacob L.S., Kelly S.H.,
Li L., Li Z., Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V.,
Okwuonu G.O., Pasternak S., Perez L.M., Plopper F.J.H., Santibanez J.,
Shen H., Tabor P.E., Verduzco D., Waldron L., Wang Q., Williams G.A.,
Zhang J., Zhou J., Allen C.C., Amin A.G., Anyalebechi V., Bailey M.,
Barbaria J.A., Bimage K.E., Bryant N.P., Burch P.E., Burkett C.E.,
Burrell K.L., Calderon E., Cardenas V., Carter K., Casias K.,
Cavazos I., Cavazos S.R., Ceasar H., Chacko J., Chan S.N., Chavez D.,
Christopoulos C., Chu J., Cockrell R., Cox C.D., Dang M.,
Dathorne S.R., David R., Davis C.M., Davy-Carroll L., Deshazo D.R.,
Donlin J.E., D'Souza L., Eaves K.A., Egan A., Emery-Cohen A.J.,
Escotto M., Flagg N., Forbes L.D., Gabisi A.M., Garza M., Hamilton C.,
Henderson N., Hernandez O., Hines S., Hogues M.E., Huang M.,
Idlebird D.G., Johnson R., Jolivet A., Jones S., Kagan R., King L.M.,
Leal B., Lebow H., Lee S., LeVan J.M., Lewis L.C., London P.,
Lorensuhewa L.M., Loulseged H., Lovett D.A., Lucier A., Lucier R.L.,
Ma J., Madu R.C., Mapua P., Martindale A.D., Martinez E., Massey E.,
Mawhiney S., Meador M.G., Mendez S., Mercado C., Mercado I.C.,
Merritt C.E., Miner Z.L., Minja E., Mitchell T., Mohabbat F.,
Mohabbat K., Montgomery B., Moore N., Morris S., Munidasa M.,
Ngo R.N., Nguyen N.B., Nickerson E., Nwaokelemeh O.O., Nwokenkwo S.,
Obregon M., Oguh M., Oragunye N., Oviedo R.J., Parish B.J.,
Parker D.N., Parrish J., Parks K.L., Paul H.A., Payton B.A., Perez A.,
Perrin W., Pickens A., Primus E.L., Pu L.-L., Puazo M., Quiles M.M.,
Quiroz J.B., Rabata D., Reeves K., Ruiz S.J., Shao H., Sisson I.,
Sonaike T., Sorelle R.P., Sutton A.E., Svatek A.F., Svetz L.A.,
Tamerisa K.S., Taylor T.R., Teague B., Thomas N., Thorn R.D.,
Trejos Z.Y., Trevino B.K., Ukegbu O.N., Urban J.B., Vasquez L.I.,
Vera V.A., Villasana D.M., Wang L., Ward-Moore S., Warren J.T.,
Wei X., White F., Williamson A.L., Wleczyk R., Wooden H.S.,
Wooden S.H., Yen J., Yoon L., Yoon V., Zorrilla S.E., Nelson D.,
Kucherlapati R., Weinstock G., Gibbs R.A.;
"The finished DNA sequence of human chromosome 12.";
Nature 440:346-351(2006).
[7]
PROTEIN SEQUENCE OF 2-27, CLEAVAGE OF INITIATOR METHIONINE,
ACETYLATION AT SER-2, AND IDENTIFICATION BY MASS SPECTROMETRY.
TISSUE=Hepatoma;
Bienvenut W.V., Fleming J., Leug H.Y.;
Submitted (JAN-2010) to UniProtKB.
[8]
CHROMOSOMAL TRANSLOCATION WITH LPP.
PubMed=9772904; DOI=10.1016/S0165-4608(98)00038-7;
Petit M.M., Swarts S., Bridge J.A., Van de Ven W.J.M.;
"Expression of reciprocal fusion transcripts of the HMGIC and LPP
genes in parosteal lipoma.";
Cancer Genet. Cytogenet. 106:18-23(1998).
[9]
CHROMOSOMAL TRANSLOCATION WITH RAD51B.
PubMed=9892177;
Schoenmakers E.F.P.M., Huysmans C., Van de Ven W.J.M.;
"Allelic knockout of novel splice variants of human recombination
repair gene RAD51B in t(12;14) uterine leiomyomas.";
Cancer Res. 59:19-23(1999).
[10]
CHROMOSOMAL TRANSLOCATION WITH LPP.
PubMed=11066083;
DOI=10.1002/1098-2264(2000)9999:9999<1::AID-GCC1043>3.3.CO;2-E;
Rogalla P., Lemke I., Kazmierczak B., Bullerdiek J.;
"An identical HMGIC-LPP fusion transcript is consistently expressed in
pulmonary chondroid hamartomas with t(3;12)(q27-28;q14-15).";
Genes Chromosomes Cancer 29:363-366(2000).
[11]
CHROMOSOMAL TRANSLOCATION WITH RAD51B.
PubMed=12649198;
Quade B.J., Weremowicz S., Neskey D.M., Vanni R., Ladd C., Dal Cin P.,
Morton C.C.;
"Fusion transcripts involving HMGA2 are not a common molecular
mechanism in uterine leiomyomata with rearrangements in 12q15.";
Cancer Res. 63:1351-1358(2003).
[12]
FUNCTION, AND INTERACTION WITH E4F1.
PubMed=14645522; DOI=10.1128/MCB.23.24.9104-9116.2003;
Tessari M.A., Gostissa M., Altamura S., Sgarra R., Rustighi A.,
Salvagno C., Caretti G., Imbriano C., Mantovani R., Del Sal G.,
Giancotti V., Manfioletti G.;
"Transcriptional activation of the cyclin A gene by the architectural
transcription factor HMGA2.";
Mol. Cell. Biol. 23:9104-9116(2003).
[13]
INVOLVEMENT IN STQTL9.
PubMed=17767157; DOI=10.1038/ng2121;
The Diabetes Genetics Initiative;
The Wellcome Trust case control consortium;
Weedon M.N., Lettre G., Freathy R.M., Lindgren C.M., Voight B.F.,
Perry J.R.B., Elliott K.S., Hackett R., Guiducci C., Shields B.,
Zeggini E., Lango H., Lyssenko V., Timpson N.J., Burtt N.P.,
Rayner N.W., Saxena R., Ardlie K., Tobias J.H., Ness A.R., Ring S.M.,
Palmer C.N.A., Morris A.D., Peltonen L., Salomaa V., Smith G.D.,
Groop L.C., Hattersley A.T., McCarthy M.I., Hirschhorn J.N.,
Frayling T.M.;
"A common variant of HMGA2 is associated with adult and childhood
height in the general population.";
Nat. Genet. 39:1245-1250(2007).
[14]
ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, CLEAVAGE OF INITIATOR
METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS
SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19413330; DOI=10.1021/ac9004309;
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,
Mohammed S.;
"Lys-N and trypsin cover complementary parts of the phosphoproteome in
a refined SCX-based approach.";
Anal. Chem. 81:4493-4501(2009).
[15]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21269460; DOI=10.1186/1752-0509-5-17;
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
"Initial characterization of the human central proteome.";
BMC Syst. Biol. 5:17-17(2011).
[16]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-40; SER-44 AND SER-105,
AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21406692; DOI=10.1126/scisignal.2001570;
Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J.,
Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V.,
Blagoev B.;
"System-wide temporal characterization of the proteome and
phosphoproteome of human embryonic stem cell differentiation.";
Sci. Signal. 4:RS3-RS3(2011).
-!- FUNCTION: Functions as a transcriptional regulator. Functions in
cell cycle regulation through CCNA2. Plays an important role in
chromosome condensation during the meiotic G2/M transition of
spermatocytes. Plays a role in postnatal myogenesis, is involved
in satellite cell activation (By similarity).
{ECO:0000250|UniProtKB:P52927, ECO:0000269|PubMed:14645522}.
-!- SUBUNIT: Interacts with E4F1 (PubMed:14645522). Interacts with
NEK2 (By similarity). {ECO:0000250|UniProtKB:P52927,
ECO:0000269|PubMed:14645522}.
-!- INTERACTION:
Q96LA8:PRMT6; NbExp=2; IntAct=EBI-912511, EBI-912440;
-!- SUBCELLULAR LOCATION: Nucleus.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=6;
Comment=Additional isoforms seem to exist.;
Name=1; Synonyms=HMGA2a;
IsoId=P52926-1; Sequence=Displayed;
Name=2; Synonyms=HMGA2f;
IsoId=P52926-2; Sequence=VSP_042564;
Name=3; Synonyms=HMGA2d';
IsoId=P52926-3; Sequence=VSP_047772;
Name=4; Synonyms=HMGA2d;
IsoId=P52926-4; Sequence=VSP_047773;
Name=5; Synonyms=HMGA2c';
IsoId=P52926-5; Sequence=VSP_047774;
Name=6; Synonyms=HMGA2c;
IsoId=P52926-6; Sequence=VSP_047775;
-!- DEVELOPMENTAL STAGE: Expressed predominantly during embryogenesis.
-!- PTM: Regulated by cell cycle-dependent phosphorylation which
alters its DNA binding affinity. Phosphorylated by NEK2 (By
similarity). {ECO:0000250|UniProtKB:P52927}.
-!- POLYMORPHISM: Genetic variations in HMGA2 define the stature
quantitative trait locus 9 (STQTL9) [MIM:611547]. Human height is
a classic, highly heritable quantitative trait.
{ECO:0000269|PubMed:17767157}.
-!- DISEASE: Note=A chromosomal aberration involving HMGA2 is
associated with a subclass of benign mesenchymal tumors known as
lipomas. Translocation t(3;12)(q27-q28;q13-q15) with LPP is shown
in lipomas. HMGA2 is also fused with a number of other genes in
lipomas. {ECO:0000269|PubMed:8824803}.
-!- DISEASE: Note=A chromosomal aberration involving HMGA2 is
associated with pulmonary chondroid hamartomas. Translocation
t(3;12)(q27-q28;q14-q15) with LPP is detected in pulmonary
chondroid hamartomas. {ECO:0000269|PubMed:11066083}.
-!- DISEASE: Note=A chromosomal aberration involving HMGA2 is
associated with parosteal lipomas. Translocation t(3;12)(q28;q14)
with LPP is also shown in one parosteal lipoma.
{ECO:0000269|PubMed:9772904}.
-!- DISEASE: Note=A chromosomal aberration involving HMGA2 is found in
uterine leiomyoma. Translocation t(12;14)(q15;q23-24) with RAD51B.
Chromosomal rearrangements involving HMGA2 do not seem to be the
principle pathobiological mechanism in uterine leiomyoma.
{ECO:0000269|PubMed:12649198, ECO:0000269|PubMed:9892177}.
-!- SIMILARITY: Belongs to the HMGA family. {ECO:0000305}.
-!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology
and Haematology;
URL="http://atlasgeneticsoncology.org/Genes/HMGICID82.html";
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EMBL; Z31595; CAA83472.1; -; mRNA.
EMBL; U28749; AAA68613.1; -; mRNA.
EMBL; U28754; AAA68614.1; -; Genomic_DNA.
EMBL; U28750; AAA68614.1; JOINED; Genomic_DNA.
EMBL; U28751; AAA68614.1; JOINED; Genomic_DNA.
EMBL; U28752; AAA68614.1; JOINED; Genomic_DNA.
EMBL; U28753; AAA68614.1; JOINED; Genomic_DNA.
EMBL; L46353; AAA96484.1; -; Genomic_DNA.
EMBL; L41044; AAA96484.1; JOINED; Genomic_DNA.
EMBL; L44578; AAA96484.1; JOINED; Genomic_DNA.
EMBL; X92518; CAA63295.1; -; mRNA.
EMBL; AY601861; AAU43851.1; -; mRNA.
EMBL; AY601862; AAU43852.1; -; mRNA.
EMBL; AY601863; AAU43853.1; -; mRNA.
EMBL; AY601864; AAU43854.1; -; mRNA.
EMBL; AY601867; AAU43857.1; -; mRNA.
EMBL; AC090673; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AC107308; -; NOT_ANNOTATED_CDS; Genomic_DNA.
CCDS; CCDS31854.1; -. [P52926-2]
CCDS; CCDS44936.1; -. [P52926-1]
CCDS; CCDS81709.1; -. [P52926-6]
PIR; JC2232; JC2232.
RefSeq; NP_001317119.1; NM_001330190.1. [P52926-6]
RefSeq; NP_003474.1; NM_003483.4. [P52926-1]
RefSeq; NP_003475.1; NM_003484.1. [P52926-2]
UniGene; Hs.505924; -.
UniGene; Hs.666976; -.
ProteinModelPortal; P52926; -.
BioGrid; 113763; 25.
IntAct; P52926; 9.
STRING; 9606.ENSP00000384026; -.
iPTMnet; P52926; -.
PhosphoSitePlus; P52926; -.
BioMuta; HMGA2; -.
DMDM; 1708263; -.
EPD; P52926; -.
MaxQB; P52926; -.
PaxDb; P52926; -.
PeptideAtlas; P52926; -.
PRIDE; P52926; -.
TopDownProteomics; P52926-1; -. [P52926-1]
TopDownProteomics; P52926-2; -. [P52926-2]
DNASU; 8091; -.
Ensembl; ENST00000354636; ENSP00000346658; ENSG00000149948. [P52926-2]
Ensembl; ENST00000393578; ENSP00000377206; ENSG00000149948. [P52926-6]
Ensembl; ENST00000403681; ENSP00000384026; ENSG00000149948. [P52926-1]
Ensembl; ENST00000425208; ENSP00000407306; ENSG00000149948. [P52926-4]
Ensembl; ENST00000537275; ENSP00000437747; ENSG00000149948. [P52926-5]
Ensembl; ENST00000537429; ENSP00000443372; ENSG00000149948. [P52926-3]
GeneID; 8091; -.
KEGG; hsa:8091; -.
UCSC; uc001sss.2; human. [P52926-1]
CTD; 8091; -.
DisGeNET; 8091; -.
EuPathDB; HostDB:ENSG00000149948.13; -.
GeneCards; HMGA2; -.
HGNC; HGNC:5009; HMGA2.
HPA; CAB017809; -.
HPA; HPA039076; -.
MalaCards; HMGA2; -.
MIM; 150699; phenotype.
MIM; 600698; gene.
MIM; 611547; phenotype.
neXtProt; NX_P52926; -.
OpenTargets; ENSG00000149948; -.
Orphanet; 94063; 12q14 microdeletion syndrome.
Orphanet; 99970; Dedifferentiated liposarcoma.
Orphanet; 99971; Well-differentiated liposarcoma.
PharmGKB; PA30059; -.
PharmGKB; PA35093; -.
eggNOG; ENOG410IZGR; Eukaryota.
eggNOG; ENOG410YWK3; LUCA.
GeneTree; ENSGT00730000111387; -.
HOGENOM; HOG000076308; -.
HOVERGEN; HBG051913; -.
InParanoid; P52926; -.
KO; K09283; -.
OMA; PRKWPRK; -.
PhylomeDB; P52926; -.
TreeFam; TF351623; -.
Reactome; R-HSA-2559584; Formation of Senescence-Associated Heterochromatin Foci (SAHF).
SignaLink; P52926; -.
SIGNOR; P52926; -.
ChiTaRS; HMGA2; human.
GeneWiki; HMGA2; -.
GenomeRNAi; 8091; -.
PRO; PR:P52926; -.
Proteomes; UP000005640; Chromosome 12.
Bgee; ENSG00000149948; -.
CleanEx; HS_HMGA2; -.
ExpressionAtlas; P52926; baseline and differential.
Genevisible; P52926; HS.
GO; GO:0000228; C:nuclear chromosome; ISS:UniProtKB.
GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
GO; GO:0005634; C:nucleus; IDA:UniProtKB.
GO; GO:0032993; C:protein-DNA complex; IDA:UniProtKB.
GO; GO:0035985; C:senescence-associated heterochromatin focus; IDA:UniProtKB.
GO; GO:0071141; C:SMAD protein complex; IDA:UniProtKB.
GO; GO:0051575; F:5'-deoxyribose-5-phosphate lyase activity; IDA:UniProtKB.
GO; GO:0003680; F:AT DNA binding; IDA:UniProtKB.
GO; GO:0070742; F:C2H2 zinc finger domain binding; IMP:UniProtKB.
GO; GO:0035497; F:cAMP response element binding; IDA:UniProtKB.
GO; GO:0001047; F:core promoter binding; IDA:UniProtKB.
GO; GO:0003677; F:DNA binding; NAS:UniProtKB.
GO; GO:0008301; F:DNA binding, bending; IDA:UniProtKB.
GO; GO:0003906; F:DNA-(apurinic or apyrimidinic site) lyase activity; IDA:UniProtKB.
GO; GO:0004677; F:DNA-dependent protein kinase activity; IDA:UniProtKB.
GO; GO:0035501; F:MH1 domain binding; IDA:UniProtKB.
GO; GO:0035500; F:MH2 domain binding; IDA:UniProtKB.
GO; GO:0031492; F:nucleosomal DNA binding; IDA:UniProtKB.
GO; GO:0000975; F:regulatory region DNA binding; IDA:UniProtKB.
GO; GO:0046332; F:SMAD binding; IPI:UniProtKB.
GO; GO:0008134; F:transcription factor binding; IPI:UniProtKB.
GO; GO:0001077; F:transcriptional activator activity, RNA polymerase II core promoter proximal region sequence-specific binding; IDA:UniProtKB.
GO; GO:0001078; F:transcriptional repressor activity, RNA polymerase II core promoter proximal region sequence-specific binding; IDA:UniProtKB.
GO; GO:0006284; P:base-excision repair; IDA:UniProtKB.
GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
GO; GO:0002062; P:chondrocyte differentiation; IDA:UniProtKB.
GO; GO:0035988; P:chondrocyte proliferation; IDA:UniProtKB.
GO; GO:0006325; P:chromatin organization; TAS:UniProtKB.
GO; GO:0031052; P:chromosome breakage; IDA:UniProtKB.
GO; GO:0030261; P:chromosome condensation; IEA:UniProtKB-KW.
GO; GO:0042769; P:DNA damage response, detection of DNA damage; IDA:UniProtKB.
GO; GO:0035987; P:endodermal cell differentiation; IMP:UniProtKB.
GO; GO:0001837; P:epithelial to mesenchymal transition; IMP:UniProtKB.
GO; GO:0045444; P:fat cell differentiation; IMP:UniProtKB.
GO; GO:0031507; P:heterochromatin assembly; IDA:UniProtKB.
GO; GO:0035978; P:histone H2A-S139 phosphorylation; IDA:UniProtKB.
GO; GO:0048762; P:mesenchymal cell differentiation; IMP:UniProtKB.
GO; GO:0048333; P:mesodermal cell differentiation; IMP:UniProtKB.
GO; GO:0003131; P:mesodermal-endodermal cell signaling; IMP:UniProtKB.
GO; GO:0007095; P:mitotic G2 DNA damage checkpoint; IDA:UniProtKB.
GO; GO:0007275; P:multicellular organism development; TAS:ProtInc.
GO; GO:0043922; P:negative regulation by host of viral transcription; IDA:UniProtKB.
GO; GO:0043066; P:negative regulation of apoptotic process; IDA:UniProtKB.
GO; GO:0043392; P:negative regulation of DNA binding; IDA:UniProtKB.
GO; GO:2001033; P:negative regulation of double-strand break repair via nonhomologous end joining; IDA:UniProtKB.
GO; GO:0045869; P:negative regulation of single stranded viral RNA replication via double stranded DNA intermediate; IDA:UniProtKB.
GO; GO:0000122; P:negative regulation of transcription from RNA polymerase II promoter; IDA:UniProtKB.
GO; GO:0045892; P:negative regulation of transcription, DNA-templated; IDA:UniProtKB.
GO; GO:0090402; P:oncogene-induced cell senescence; IDA:UniProtKB.
GO; GO:0043065; P:positive regulation of apoptotic process; IDA:UniProtKB.
GO; GO:0071158; P:positive regulation of cell cycle arrest; IDA:UniProtKB.
GO; GO:2000685; P:positive regulation of cellular response to X-ray; IDA:UniProtKB.
GO; GO:2000774; P:positive regulation of cellular senescence; IMP:UniProtKB.
GO; GO:0010628; P:positive regulation of gene expression; IDA:UniProtKB.
GO; GO:2001022; P:positive regulation of response to DNA damage stimulus; IDA:UniProtKB.
GO; GO:2000648; P:positive regulation of stem cell proliferation; IDA:UniProtKB.
GO; GO:0045944; P:positive regulation of transcription from RNA polymerase II promoter; IDA:UniProtKB.
GO; GO:2000679; P:positive regulation of transcription regulatory region DNA binding; IDA:UniProtKB.
GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IDA:UniProtKB.
GO; GO:0010564; P:regulation of cell cycle process; IDA:UniProtKB.
GO; GO:2001038; P:regulation of cellular response to drug; IDA:UniProtKB.
GO; GO:0040008; P:regulation of growth; IEA:UniProtKB-KW.
GO; GO:2000036; P:regulation of stem cell population maintenance; IMP:UniProtKB.
GO; GO:0006355; P:regulation of transcription, DNA-templated; IMP:UniProtKB.
GO; GO:0009615; P:response to virus; IEP:UniProtKB.
GO; GO:0035986; P:senescence-associated heterochromatin focus assembly; IDA:UniProtKB.
GO; GO:0048863; P:stem cell differentiation; IEP:UniProtKB.
InterPro; IPR017956; AT_hook_DNA-bd_motif.
InterPro; IPR000116; HMGA.
InterPro; IPR000637; HMGI/Y_DNA-bd_CS.
Pfam; PF02178; AT_hook; 3.
PRINTS; PR00929; ATHOOK.
PRINTS; PR00930; HIGHMOBLTYIY.
SMART; SM00384; AT_hook; 3.
PROSITE; PS00354; HMGI_Y; 2.
1: Evidence at protein level;
Acetylation; Alternative splicing; Cell cycle; Cell division;
Chromosomal rearrangement; Complete proteome;
Direct protein sequencing; DNA condensation; DNA-binding;
Growth regulation; Mitosis; Nucleus; Phosphoprotein; Proto-oncogene;
Reference proteome; Repeat; Transcription; Transcription regulation.
INIT_MET 1 1 Removed. {ECO:0000244|PubMed:19413330,
ECO:0000269|Ref.7}.
CHAIN 2 109 High mobility group protein HMGI-C.
/FTId=PRO_0000206711.
DNA_BIND 24 34 A.T hook 1.
DNA_BIND 44 54 A.T hook 2.
DNA_BIND 71 82 A.T hook 3.
REGION 44 63 Interaction with E4F1.
{ECO:0000269|PubMed:14645522}.
MOD_RES 2 2 N-acetylserine.
{ECO:0000244|PubMed:19413330,
ECO:0000269|Ref.7}.
MOD_RES 40 40 Phosphothreonine.
{ECO:0000244|PubMed:21406692}.
MOD_RES 44 44 Phosphoserine.
{ECO:0000244|PubMed:21406692}.
MOD_RES 101 101 Phosphoserine.
{ECO:0000250|UniProtKB:P52927}.
MOD_RES 105 105 Phosphoserine.
{ECO:0000244|PubMed:21406692}.
VAR_SEQ 84 109 PQQVVQKKPAQEETEETSSQESAEED -> DNLLPRTSSKK
KTSLGNSTKRSH (in isoform 2).
{ECO:0000303|PubMed:15882911}.
/FTId=VSP_042564.
VAR_SEQ 84 109 PQQVVQKKPAQEETEETSSQESAEED -> LQN (in
isoform 3).
{ECO:0000303|PubMed:15882911}.
/FTId=VSP_047772.
VAR_SEQ 84 109 PQQVVQKKPAQEETEETSSQESAEED -> WLLMKSPCW
(in isoform 4).
{ECO:0000303|PubMed:15882911}.
/FTId=VSP_047773.
VAR_SEQ 84 109 PQQVVQKKPAQEETEETSSQESAEED -> LRAQALDSDGL
GSNSGPSLS (in isoform 5).
{ECO:0000303|PubMed:15882911}.
/FTId=VSP_047774.
VAR_SEQ 84 109 PQQVVQKKPAQEETEETSSQESAEED -> EEFYIAA (in
isoform 6).
{ECO:0000303|PubMed:15882911}.
/FTId=VSP_047775.
SEQUENCE 109 AA; 11832 MW; F36BABE623DA4615 CRC64;
MSARGEGAGQ PSTSAQGQPA APAPQKRGRG RPRKQQQEPT GEPSPKRPRG RPKGSKNKSP
SKAAQKKAEA TGEKRPRGRP RKWPQQVVQK KPAQEETEET SSQESAEED


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