HMGA2_MOUSE
ID HMGA2_MOUSE Reviewed; 108 AA.
AC P52927; Q3UQW0;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 03-AUG-2022, entry version 176.
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 Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=1762909; DOI=10.1093/nar/19.24.6793;
RA Manfioletti G., Giancotti V., Bandiera A., Buratti E., Sautiere P.,
RA Cary P., Crane-Robinson C., Coles B., Goodwin G.H.;
RT "cDNA cloning of the HMGI-C phosphoprotein, a nuclear protein associated
RT with neoplastic and undifferentiated phenotypes.";
RL Nucleic Acids Res. 19:6793-6797(1991).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=8566786; DOI=10.1016/0378-1119(95)00666-4;
RA Manfioletti G., Rustighi A., Mantovani F., Goodwin G.H., Giancotti V.;
RT "Isolation and characterization of the gene coding for murine high-
RT mobility-group protein HMGI-C.";
RL Gene 167:249-253(1995).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
RX PubMed=8918814; DOI=10.1093/nar/24.20.4071;
RA Zhou X., Benson K.F., Przybysz K., Liu J., Hou Y., Cherath L., Chada K.;
RT "Genomic structure and expression of the murine Hmgi-c gene.";
RL Nucleic Acids Res. 24:4071-4077(1996).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Eye;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Embryo, and Limb;
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 [6]
RP FUNCTION, SUBCELLULAR LOCATION, PHOSPHORYLATION, INTERACTION WITH NEK2, AND
RP TISSUE SPECIFICITY.
RX PubMed=14668482; DOI=10.1091/mbc.e03-09-0638;
RA Di Agostino S., Fedele M., Chieffi P., Fusco A., Rossi P., Geremia R.,
RA Sette C.;
RT "Phosphorylation of high-mobility group protein A2 by Nek2 kinase during
RT the first meiotic division in mouse spermatocytes.";
RL Mol. Biol. Cell 15:1224-1232(2004).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-104, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic fibroblast;
RX PubMed=19131326; DOI=10.1074/mcp.m800451-mcp200;
RA Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.;
RT "Large scale localization of protein phosphorylation by use of electron
RT capture dissociation mass spectrometry.";
RL Mol. Cell. Proteomics 8:904-912(2009).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-100 AND SER-104, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Kidney, Liver, Lung, Pancreas, Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [9]
RP FUNCTION, DEVELOPMENTAL STAGE, AND TISSUE SPECIFICITY.
RX PubMed=27446912; DOI=10.3389/fcell.2016.00058;
RA Alonso-Martin S., Rochat A., Mademtzoglou D., Morais J., de Reynies A.,
RA Aurade F., Chang T.H., Zammit P.S., Relaix F.;
RT "Gene expression profiling of muscle stem cells identifies novel regulators
RT of postnatal myogenesis.";
RL Front. Cell Dev. Biol. 4:58-58(2016).
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 (PubMed:27446912). Positively regulates IGF2 expression
CC through PLAG1 and in a PLAG1-independent manner (By similarity).
CC {ECO:0000250|UniProtKB:P52926, ECO:0000269|PubMed:14668482,
CC ECO:0000269|PubMed:27446912}.
CC -!- SUBUNIT: Interacts with E4F1 (By similarity). Interacts with NEK2
CC (PubMed:14668482). {ECO:0000250|UniProtKB:P52926,
CC ECO:0000269|PubMed:14668482}.
CC -!- INTERACTION:
CC P52927; P06400: RB1; Xeno; NbExp=5; IntAct=EBI-912574, EBI-491274;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:14668482}.
CC -!- TISSUE SPECIFICITY: Expressed in mitotic spermatogonia, meiotic
CC spermatocytes, and postmeiotic round spermatids (at protein level)
CC (PubMed:14668482). Expressed in embryonic myogenic progenitor cells
CC (PubMed:27446912). {ECO:0000269|PubMed:14668482,
CC ECO:0000269|PubMed:27446912}.
CC -!- DEVELOPMENTAL STAGE: Expressed predominantly during embryogenesis. In
CC myogenic progenitor cells, expressed during early myogenic development
CC (11.5 dpc) to be gradually down-regulated during the fetal stages (17.5
CC dpc) (PubMed:27446912). {ECO:0000269|PubMed:27446912}.
CC -!- PTM: Regulated by cell cycle-dependent phosphorylation which alters its
CC DNA binding affinity. Phosphorylated by NEK2.
CC {ECO:0000269|PubMed:14668482}.
CC -!- SIMILARITY: Belongs to the HMGA family. {ECO:0000305}.
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DR EMBL; L41621; AAC69244.1; -; Genomic_DNA.
DR EMBL; L41617; AAC69244.1; JOINED; Genomic_DNA.
DR EMBL; L41618; AAC69244.1; JOINED; Genomic_DNA.
DR EMBL; L41619; AAC69244.1; JOINED; Genomic_DNA.
DR EMBL; L41620; AAC69244.1; JOINED; Genomic_DNA.
DR EMBL; X58380; CAA41270.1; -; mRNA.
DR EMBL; X99915; CAA68187.1; -; Genomic_DNA.
DR EMBL; X99916; CAA68187.1; JOINED; Genomic_DNA.
DR EMBL; X99917; CAA68187.1; JOINED; Genomic_DNA.
DR EMBL; X99918; CAA68187.1; JOINED; Genomic_DNA.
DR EMBL; X99919; CAA68187.1; JOINED; Genomic_DNA.
DR EMBL; AK028346; BAC25896.1; -; mRNA.
DR EMBL; AK142059; BAE24928.1; -; mRNA.
DR EMBL; BC052158; AAH52158.1; -; mRNA.
DR EMBL; BC085085; AAH85085.1; -; mRNA.
DR CCDS; CCDS36073.1; -.
DR PIR; JC4575; JC4575.
DR RefSeq; NP_001334099.1; NM_001347170.1.
DR RefSeq; NP_034571.1; NM_010441.3.
DR AlphaFoldDB; P52927; -.
DR BioGRID; 200341; 8.
DR IntAct; P52927; 475.
DR STRING; 10090.ENSMUSP00000072556; -.
DR iPTMnet; P52927; -.
DR PhosphoSitePlus; P52927; -.
DR MaxQB; P52927; -.
DR PaxDb; P52927; -.
DR PeptideAtlas; P52927; -.
DR PRIDE; P52927; -.
DR ProteomicsDB; 267051; -.
DR DNASU; 15364; -.
DR Ensembl; ENSMUST00000072777; ENSMUSP00000072556; ENSMUSG00000056758.
DR GeneID; 15364; -.
DR KEGG; mmu:15364; -.
DR UCSC; uc007hfb.1; mouse.
DR CTD; 8091; -.
DR MGI; MGI:101761; Hmga2.
DR VEuPathDB; HostDB:ENSMUSG00000056758; -.
DR eggNOG; ENOG502S80S; Eukaryota.
DR GeneTree; ENSGT00940000163109; -.
DR HOGENOM; CLU_138888_1_0_1; -.
DR InParanoid; P52927; -.
DR OMA; KPIGIRR; -.
DR PhylomeDB; P52927; -.
DR TreeFam; TF351623; -.
DR Reactome; R-MMU-2559584; Formation of Senescence-Associated Heterochromatin Foci (SAHF).
DR BioGRID-ORCS; 15364; 1 hit in 110 CRISPR screens.
DR ChiTaRS; Hmga2; mouse.
DR PRO; PR:P52927; -.
DR Proteomes; UP000000589; Chromosome 10.
DR RNAct; P52927; protein.
DR Bgee; ENSMUSG00000056758; Expressed in undifferentiated genital tubercle and 192 other tissues.
DR ExpressionAtlas; P52927; baseline and differential.
DR Genevisible; P52927; MM.
DR GO; GO:0001673; C:male germ cell nucleus; IDA:MGI.
DR GO; GO:0000228; C:nuclear chromosome; IDA:MGI.
DR GO; GO:0005634; C:nucleus; IDA:MGI.
DR GO; GO:0032993; C:protein-DNA complex; ISS:UniProtKB.
DR GO; GO:0035985; C:senescence-associated heterochromatin focus; ISS:UniProtKB.
DR GO; GO:0071141; C:SMAD protein complex; ISS:UniProtKB.
DR GO; GO:0051575; F:5'-deoxyribose-5-phosphate lyase activity; ISS:UniProtKB.
DR GO; GO:0070742; F:C2H2 zinc finger domain binding; ISS:UniProtKB.
DR GO; GO:0035497; F:cAMP response element binding; ISS:UniProtKB.
DR GO; GO:0008301; F:DNA binding, bending; ISS:UniProtKB.
DR GO; GO:0003906; F:DNA-(apurinic or apyrimidinic site) endonuclease activity; ISS:UniProtKB.
DR GO; GO:0019899; F:enzyme binding; ISO:MGI.
DR GO; GO:0035501; F:MH1 domain binding; ISS:UniProtKB.
DR GO; GO:0035500; F:MH2 domain binding; ISS:UniProtKB.
DR GO; GO:0003680; F:minor groove of adenine-thymine-rich DNA binding; IDA:MGI.
DR GO; GO:0031492; F:nucleosomal DNA binding; ISS:UniProtKB.
DR GO; GO:0061629; F:RNA polymerase II-specific DNA-binding transcription factor binding; ISO:MGI.
DR GO; GO:0046332; F:SMAD binding; ISO:MGI.
DR GO; GO:0000976; F:transcription cis-regulatory region binding; ISS:UniProtKB.
DR GO; GO:0003712; F:transcription coregulator activity; IBA:GO_Central.
DR GO; GO:0003714; F:transcription corepressor activity; ISS:GO_Central.
DR GO; GO:0060612; P:adipose tissue development; IMP:MGI.
DR GO; GO:0030325; P:adrenal gland development; IMP:MGI.
DR GO; GO:0048708; P:astrocyte differentiation; IDA:MGI.
DR GO; GO:0006284; P:base-excision repair; ISS:UniProtKB.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR GO; GO:0021846; P:cell proliferation in forebrain; IMP:MGI.
DR GO; GO:0002062; P:chondrocyte differentiation; ISS:UniProtKB.
DR GO; GO:0035988; P:chondrocyte proliferation; ISS:UniProtKB.
DR GO; GO:0030261; P:chromosome condensation; IEA:UniProtKB-KW.
DR GO; GO:0035987; P:endodermal cell differentiation; ISS:UniProtKB.
DR GO; GO:0001837; P:epithelial to mesenchymal transition; ISS:UniProtKB.
DR GO; GO:0060441; P:epithelial tube branching involved in lung morphogenesis; IMP:MGI.
DR GO; GO:0045444; P:fat cell differentiation; ISS:UniProtKB.
DR GO; GO:0060613; P:fat pad development; IGI:MGI.
DR GO; GO:0048144; P:fibroblast proliferation; IMP:MGI.
DR GO; GO:0031507; P:heterochromatin assembly; ISS:UniProtKB.
DR GO; GO:0035978; P:histone H2A-S139 phosphorylation; ISO:MGI.
DR GO; GO:0035556; P:intracellular signal transduction; ISS:UniProtKB.
DR GO; GO:0060428; P:lung epithelium development; IMP:MGI.
DR GO; GO:0008584; P:male gonad development; IMP:MGI.
DR GO; GO:0051321; P:meiotic cell cycle; IEA:UniProtKB-KW.
DR GO; GO:0048762; P:mesenchymal cell differentiation; ISS:UniProtKB.
DR GO; GO:0048333; P:mesodermal cell differentiation; ISS:UniProtKB.
DR GO; GO:0003131; P:mesodermal-endodermal cell signaling; ISS:UniProtKB.
DR GO; GO:0007095; P:mitotic G2 DNA damage checkpoint signaling; ISO:MGI.
DR GO; GO:0043922; P:negative regulation by host of viral transcription; ISS:UniProtKB.
DR GO; GO:0043066; P:negative regulation of apoptotic process; ISS:UniProtKB.
DR GO; GO:0048712; P:negative regulation of astrocyte differentiation; IDA:MGI.
DR GO; GO:2000773; P:negative regulation of cellular senescence; IMP:BHF-UCL.
DR GO; GO:0043392; P:negative regulation of DNA binding; ISS:UniProtKB.
DR GO; GO:2001033; P:negative regulation of double-strand break repair via nonhomologous end joining; ISS:UniProtKB.
DR GO; GO:0033144; P:negative regulation of intracellular steroid hormone receptor signaling pathway; ISO:MGI.
DR GO; GO:0046426; P:negative regulation of receptor signaling pathway via JAK-STAT; ISO:MGI.
DR GO; GO:0045869; P:negative regulation of single stranded viral RNA replication via double stranded DNA intermediate; ISS:UniProtKB.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; ISS:UniProtKB.
DR GO; GO:0045892; P:negative regulation of transcription, DNA-templated; ISS:UniProtKB.
DR GO; GO:0030178; P:negative regulation of Wnt signaling pathway; IMP:MGI.
DR GO; GO:0090402; P:oncogene-induced cell senescence; ISS:UniProtKB.
DR GO; GO:0021983; P:pituitary gland development; IMP:MGI.
DR GO; GO:0045766; P:positive regulation of angiogenesis; IMP:BHF-UCL.
DR GO; GO:0043065; P:positive regulation of apoptotic process; ISO:MGI.
DR GO; GO:0071864; P:positive regulation of cell proliferation in bone marrow; IMP:BHF-UCL.
DR GO; GO:2000685; P:positive regulation of cellular response to X-ray; ISO:MGI.
DR GO; GO:0051091; P:positive regulation of DNA-binding transcription factor activity; ISO:MGI.
DR GO; GO:0060501; P:positive regulation of epithelial cell proliferation involved in lung morphogenesis; IMP:MGI.
DR GO; GO:0048146; P:positive regulation of fibroblast proliferation; IMP:MGI.
DR GO; GO:0010628; P:positive regulation of gene expression; IMP:UniProtKB.
DR GO; GO:0040018; P:positive regulation of multicellular organism growth; IMP:MGI.
DR GO; GO:0071902; P:positive regulation of protein serine/threonine kinase activity; ISS:UniProtKB.
DR GO; GO:2001022; P:positive regulation of response to DNA damage stimulus; ISO:MGI.
DR GO; GO:2000648; P:positive regulation of stem cell proliferation; IMP:MGI.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IDA:MGI.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; ISO:MGI.
DR GO; GO:0010564; P:regulation of cell cycle process; IDA:UniProtKB.
DR GO; GO:0060123; P:regulation of growth hormone secretion; IMP:MGI.
DR GO; GO:0090276; P:regulation of peptide hormone secretion; IMP:MGI.
DR GO; GO:2000036; P:regulation of stem cell population maintenance; ISS:UniProtKB.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; ISS:UniProtKB.
DR GO; GO:0007165; P:signal transduction; ISO:MGI.
DR GO; GO:0035019; P:somatic stem cell population maintenance; IMP:MGI.
DR GO; GO:0007283; P:spermatogenesis; IMP:MGI.
DR GO; GO:0072089; P:stem cell proliferation; IMP:MGI.
DR InterPro; IPR017956; AT_hook_DNA-bd_motif.
DR InterPro; IPR000116; HMGA.
DR Pfam; PF02178; AT_hook; 3.
DR PRINTS; PR00929; ATHOOK.
DR PRINTS; PR00930; HIGHMOBLTYIY.
DR SMART; SM00384; AT_hook; 3.
PE 1: Evidence at protein level;
KW Acetylation; Cell cycle; Cell division; DNA condensation; DNA-binding;
KW Growth regulation; Meiosis; Mitosis; Nucleus; Phosphoprotein;
KW Reference proteome; Repeat; Transcription; Transcription regulation.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:P52926"
FT CHAIN 2..108
FT /note="High mobility group protein HMGI-C"
FT /id="PRO_0000206712"
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..108
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 44..63
FT /note="Interaction with E4F1"
FT /evidence="ECO:0000250"
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:0000250|UniProtKB:P52926"
FT MOD_RES 40
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P52926"
FT MOD_RES 44
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P52926"
FT MOD_RES 100
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 104
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19131326,
FT ECO:0007744|PubMed:21183079"
SQ SEQUENCE 108 AA; 11819 MW; 40A3E38F62268C09 CRC64;
MSARGEGAGQ PSTSAQGQPA APVPQKRGRG RPRKQQQEPT CEPSPKRPRG RPKGSKNKSP
SKAAQKKAET IGEKRPRGRP RKWPQQVVQK KPAQETEETS SQESAEED
