HMGA1_RAT
ID HMGA1_RAT Reviewed; 107 AA.
AC Q8K585; Q8K1F5;
DT 06-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 149.
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;
GN Name=Hmga1;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS HMG-I AND HMG-Y), PHOSPHORYLATION,
RP METHYLATION AT ARG-26, AND MASS SPECTROMETRY.
RC STRAIN=COP; TISSUE=Prostatic carcinoma;
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 [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM HMG-I).
RC STRAIN=Sprague-Dawley; TISSUE=Lung;
RA Claus P.;
RL Submitted (APR-2002) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
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 (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Interacts with HIPK2. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Nucleus. Chromosome.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=HMG-I; Synonyms=HMGA1a;
CC IsoId=Q8K585-1; Sequence=Displayed;
CC Name=HMG-Y; Synonyms=HMGA1b;
CC IsoId=Q8K585-2; Sequence=VSP_016395;
CC -!- PTM: Isoforms HMG-I and HMG-Y can be phosphorylated by HIPK2.
CC Phosphorylation may modulate DNA-binding affinity (By similarity).
CC {ECO:0000250}.
CC -!- PTM: Methylation at Arg-58 is mutually exclusive with methylation at
CC Arg-60. {ECO:0000250}.
CC -!- MASS SPECTROMETRY: Mass=11776.8; Mass_error=1; Method=MALDI; Note=With
CC 1 acetyl and 2 phosphate groups.;
CC Evidence={ECO:0000269|PubMed:12653562};
CC -!- MASS SPECTROMETRY: Mass=11856.8; Mass_error=1; Method=MALDI; Note=With
CC 1 acetyl and 3 phosphate groups.;
CC Evidence={ECO:0000269|PubMed:12653562};
CC -!- MASS SPECTROMETRY: Mass=11791.2; Mass_error=1; Method=MALDI; Note=With
CC 1 acetyl, 1 methyl and 2 phosphate groups.;
CC Evidence={ECO:0000269|PubMed:12653562};
CC -!- MASS SPECTROMETRY: Mass=11871.3; Mass_error=1; Method=MALDI; Note=With
CC 1 acetyl, 1 methyl and 3 phosphate groups.;
CC Evidence={ECO:0000269|PubMed:12653562};
CC -!- SIMILARITY: Belongs to the HMGA family. {ECO:0000305}.
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DR EMBL; AF511040; AAM74157.1; -; mRNA.
DR EMBL; AF507966; AAM33433.1; -; mRNA.
DR RefSeq; NP_647543.1; NM_139327.1.
DR RefSeq; XP_006256218.1; XM_006256156.2. [Q8K585-1]
DR RefSeq; XP_006256219.1; XM_006256157.3. [Q8K585-1]
DR RefSeq; XP_006256220.1; XM_006256158.3. [Q8K585-1]
DR RefSeq; XP_006256224.1; XM_006256162.3. [Q8K585-2]
DR RefSeq; XP_006256225.1; XM_006256163.3. [Q8K585-2]
DR RefSeq; XP_017457021.1; XM_017601532.1. [Q8K585-2]
DR AlphaFoldDB; Q8K585; -.
DR BioGRID; 250659; 1.
DR CORUM; Q8K585; -.
DR STRING; 10116.ENSRNOP00000000580; -.
DR iPTMnet; Q8K585; -.
DR PhosphoSitePlus; Q8K585; -.
DR jPOST; Q8K585; -.
DR PaxDb; Q8K585; -.
DR PRIDE; Q8K585; -.
DR Ensembl; ENSRNOT00000113836; ENSRNOP00000086846; ENSRNOG00000000488. [Q8K585-1]
DR GeneID; 117062; -.
DR KEGG; rno:117062; -.
DR UCSC; RGD:628699; rat. [Q8K585-1]
DR CTD; 3159; -.
DR RGD; 628699; Hmga1.
DR eggNOG; ENOG502S5JW; Eukaryota.
DR GeneTree; ENSGT00730000111329; -.
DR HOGENOM; CLU_138888_0_0_1; -.
DR InParanoid; Q8K585; -.
DR OMA; HKKKQGP; -.
DR OrthoDB; 1603551at2759; -.
DR PhylomeDB; Q8K585; -.
DR TreeFam; TF351623; -.
DR Reactome; R-RNO-2559584; Formation of Senescence-Associated Heterochromatin Foci (SAHF).
DR PRO; PR:Q8K585; -.
DR Proteomes; UP000002494; Chromosome 20.
DR Bgee; ENSRNOG00000000488; Expressed in thymus and 20 other tissues.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0090575; C:RNA polymerase II transcription regulator complex; ISO:RGD.
DR GO; GO:0035985; C:senescence-associated heterochromatin focus; ISS:UniProtKB.
DR GO; GO:0051575; F:5'-deoxyribose-5-phosphate lyase activity; ISO:RGD.
DR GO; GO:0003682; F:chromatin binding; ISO:RGD.
DR GO; GO:0000987; F:cis-regulatory region sequence-specific DNA binding; ISO:RGD.
DR GO; GO:0003677; F:DNA binding; ISO:RGD.
DR GO; GO:0003906; F:DNA-(apurinic or apyrimidinic site) endonuclease activity; ISO:RGD.
DR GO; GO:0001228; F:DNA-binding transcription activator activity, RNA polymerase II-specific; ISO:RGD.
DR GO; GO:0019899; F:enzyme binding; ISO:RGD.
DR GO; GO:0003680; F:minor groove of adenine-thymine-rich DNA binding; ISO:RGD.
DR GO; GO:0030374; F:nuclear receptor coactivator activity; ISS:UniProtKB.
DR GO; GO:0042974; F:nuclear retinoic acid receptor binding; ISS:UniProtKB.
DR GO; GO:0046965; F:nuclear retinoid X receptor binding; ISS:UniProtKB.
DR GO; GO:0042975; F:peroxisome proliferator activated receptor binding; ISS:UniProtKB.
DR GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; ISO:RGD.
DR GO; GO:0003713; F:transcription coactivator activity; ISO:RGD.
DR GO; GO:0003712; F:transcription coregulator activity; IBA:GO_Central.
DR GO; GO:0001221; F:transcription coregulator binding; ISS:UniProtKB.
DR GO; GO:0006284; P:base-excision repair; ISO:RGD.
DR GO; GO:0008285; P:negative regulation of cell population proliferation; ISS:UniProtKB.
DR GO; GO:0045892; P:negative regulation of transcription, DNA-templated; ISS:UniProtKB.
DR GO; GO:0090402; P:oncogene-induced cell senescence; ISS:UniProtKB.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; ISO:RGD.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; ISS:UniProtKB.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; IBA:GO_Central.
DR GO; GO:0007283; P:spermatogenesis; ISO:RGD.
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 Pfam; PF02178; AT_hook; 3.
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 Acetylation; ADP-ribosylation; Alternative splicing; Chromosome;
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_0000206710"
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:0000250|UniProtKB:P17096"
FT MOD_RES 9
FT /note="ADP-ribosylserine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P17096"
FT MOD_RES 9
FT /note="Phosphoserine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P17096"
FT MOD_RES 15
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P17096"
FT MOD_RES 26
FT /note="Asymmetric dimethylarginine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P17096"
FT MOD_RES 26
FT /note="Omega-N-methylarginine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P17096"
FT MOD_RES 26
FT /note="Symmetric dimethylarginine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P17096"
FT MOD_RES 36
FT /note="Phosphoserine; by HIPK2 and CDC2"
FT /evidence="ECO:0000250|UniProtKB:P17096"
FT MOD_RES 39
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P17096"
FT MOD_RES 44
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P17096"
FT MOD_RES 49
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P17096"
FT MOD_RES 53
FT /note="Phosphothreonine; by HIPK2 and CDC2"
FT /evidence="ECO:0000250|UniProtKB:P17096"
FT MOD_RES 58
FT /note="Asymmetric dimethylarginine; by PRMT6; alternate"
FT /evidence="ECO:0000250|UniProtKB:P17096"
FT MOD_RES 58
FT /note="Omega-N-methylarginine; by PRMT6; alternate"
FT /evidence="ECO:0000250|UniProtKB:P17096"
FT MOD_RES 60
FT /note="Asymmetric dimethylarginine; by PRMT6; alternate"
FT /evidence="ECO:0000250|UniProtKB:P17096"
FT MOD_RES 60
FT /note="Omega-N-methylarginine; by PRMT6; alternate"
FT /evidence="ECO:0000250|UniProtKB:P17096"
FT MOD_RES 78
FT /note="Phosphothreonine; by HIPK2 and CDC2"
FT /evidence="ECO:0000250|UniProtKB:P17096"
FT MOD_RES 99
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P17096"
FT MOD_RES 102
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P17096"
FT MOD_RES 103
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P17096"
FT CROSSLNK 15
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2); alternate"
FT /evidence="ECO:0000250|UniProtKB:P17096"
FT VAR_SEQ 35..45
FT /note="Missing (in isoform HMG-Y)"
FT /evidence="ECO:0000303|PubMed:12653562"
FT /id="VSP_016395"
FT CONFLICT 5
FT /note="V -> G (in Ref. 2; AAM33433)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 107 AA; 11706 MW; 0F944B183384C10E CRC64;
MSESVSKSSQ PLASKQEKDG TEKRGRGRPR KQPSVSPGTA LVGSQKEPSE VPTPKRPRGR
PKGSKNKGTA KTRKVTTTPG RKPRGRPKKL EKEEEEGISQ ESSEEEQ
