HMGA1_CRIGR
ID HMGA1_CRIGR Reviewed; 107 AA.
AC Q9QXP3; Q9QXP2;
DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 126.
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; Synonyms=HMGIY;
OS Cricetulus griseus (Chinese hamster) (Cricetulus barabensis griseus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea;
OC Cricetidae; Cricetinae; Cricetulus.
OX NCBI_TaxID=10029;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS HMG-I AND HMG-Y).
RA Aldrich T.L., Reeves R., Lee C.C., Thomas J.N., Morris A.E.;
RT "HMG-I(Y) proteins implicated in amplification of CHO cell DNA.";
RL Submitted (DEC-1999) to the EMBL/GenBank/DDBJ databases.
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=Q9QXP3-1; Sequence=Displayed;
CC Name=HMG-Y; Synonyms=HMGA1b;
CC IsoId=Q9QXP3-2; Sequence=VSP_002181;
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 -!- SIMILARITY: Belongs to the HMGA family. {ECO:0000305}.
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DR EMBL; AF193762; AAF06666.2; -; mRNA.
DR EMBL; AF193763; AAF06667.2; -; mRNA.
DR RefSeq; NP_001230957.1; NM_001244028.1. [Q9QXP3-1]
DR RefSeq; XP_007644977.1; XM_007646787.2. [Q9QXP3-1]
DR RefSeq; XP_007644984.1; XM_007646794.2. [Q9QXP3-2]
DR AlphaFoldDB; Q9QXP3; -.
DR BMRB; Q9QXP3; -.
DR STRING; 10029.NP_001230957.1; -.
DR Ensembl; ENSCGRT00001002870; ENSCGRP00001002230; ENSCGRG00001002340. [Q9QXP3-1]
DR GeneID; 100689040; -.
DR KEGG; cge:100689040; -.
DR CTD; 3159; -.
DR eggNOG; ENOG502S5JW; Eukaryota.
DR GeneTree; ENSGT00730000111329; -.
DR OMA; HKKKQGP; -.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0035985; C:senescence-associated heterochromatin focus; ISS:UniProtKB.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
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:0001221; F:transcription coregulator binding; ISS:UniProtKB.
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:0045893; P:positive regulation of transcription, DNA-templated; ISS:UniProtKB.
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 3: Inferred from homology;
KW Acetylation; ADP-ribosylation; Alternative splicing; Chromosome;
KW DNA-binding; Isopeptide bond; Methylation; Nucleus; Phosphoprotein; Repeat;
KW Transcription; Transcription regulation; 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_0000206707"
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 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|Ref.1"
FT /id="VSP_002181"
SQ SEQUENCE 107 AA; 11616 MW; F4723882201D45FD CRC64;
MSESSSKSSQ PLASKQEKDG TEKRGRGRPR KQPPVSPGTA LVGSQKEPSE VPTPKRPRGR
PKGSKNKGAA KTRKATTAPG RKPRGRPKKL EKEEEEGISQ ESSEEEQ
