HMGA1_CANLF
ID HMGA1_CANLF Reviewed; 107 AA.
AC Q6URC2;
DT 26-APR-2005, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 114.
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 Canis lupus familiaris (Dog) (Canis familiaris).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Carnivora; Caniformia; Canidae; Canis.
OX NCBI_TaxID=9615;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS HMG-I AND HMG-Y).
RC STRAIN=Alsatian, Bull terrier, Collie, Dachshund, Doberman pinscher,
RC German shorthaired pointer, Golden retriever, Jack Russel terrier,
RC Munsterland, and West Highland terrier;
RX PubMed=15087128; DOI=10.1016/j.gene.2004.01.009;
RA Murua Escobar H., Soller J.T., Richter A., Meyer B., Winkler S.,
RA Flohr A.M., Nolte I., Bullerdiek J.;
RT "The canine HMGA1.";
RL Gene 330:93-99(2004).
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 {ECO:0000250}. Chromosome {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=HMG-I; Synonyms=HMGA1a;
CC IsoId=Q6URC2-1; Sequence=Displayed;
CC Name=HMG-Y; Synonyms=HMGA1b;
CC IsoId=Q6URC2-2; Sequence=VSP_013473;
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; AY366390; AAR21596.1; -; mRNA.
DR EMBL; AY366391; AAR21597.1; -; mRNA.
DR EMBL; AY363599; AAR12011.1; -; mRNA.
DR EMBL; AY363600; AAR12012.1; -; mRNA.
DR EMBL; AY363601; AAR12013.1; -; mRNA.
DR EMBL; AY363602; AAR12014.1; -; mRNA.
DR EMBL; AY363603; AAR12015.1; -; mRNA.
DR EMBL; AY363604; AAR12016.1; -; mRNA.
DR EMBL; AY363605; AAR12017.1; -; mRNA.
DR EMBL; AY363606; AAR12018.1; -; mRNA.
DR EMBL; AY363607; AAR12019.1; -; mRNA.
DR EMBL; AY363608; AAR12020.1; -; mRNA.
DR EMBL; AY363609; AAR12021.1; -; mRNA.
DR EMBL; AY363610; AAR12022.1; -; mRNA.
DR RefSeq; NP_001003387.1; NM_001003387.1. [Q6URC2-1]
DR AlphaFoldDB; Q6URC2; -.
DR BMRB; Q6URC2; -.
DR SMR; Q6URC2; -.
DR STRING; 9612.ENSCAFP00000001724; -.
DR PaxDb; Q6URC2; -.
DR Ensembl; ENSCAFT00030007609; ENSCAFP00030006668; ENSCAFG00030004107. [Q6URC2-1]
DR Ensembl; ENSCAFT00040021076; ENSCAFP00040018299; ENSCAFG00040011381. [Q6URC2-1]
DR Ensembl; ENSCAFT00845046941; ENSCAFP00845036824; ENSCAFG00845026595. [Q6URC2-2]
DR GeneID; 442946; -.
DR KEGG; cfa:442946; -.
DR CTD; 3159; -.
DR eggNOG; ENOG502S5JW; Eukaryota.
DR GeneTree; ENSGT00730000111329; -.
DR InParanoid; Q6URC2; -.
DR Proteomes; UP000002254; Chromosome 12.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0035985; C:senescence-associated heterochromatin focus; ISS:UniProtKB.
DR GO; GO:0000987; F:cis-regulatory region sequence-specific DNA binding; IEA:Ensembl.
DR GO; GO:0019899; F:enzyme binding; IEA:Ensembl.
DR GO; GO:0003680; F:minor groove of adenine-thymine-rich DNA binding; IEA:Ensembl.
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:0003712; F:transcription coregulator activity; IBA:GO_Central.
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 GO; GO:0006355; P:regulation of transcription, DNA-templated; IBA:GO_Central.
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;
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_0000206706"
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:15087128"
FT /id="VSP_013473"
SQ SEQUENCE 107 AA; 11676 MW; E9C4E3F2200914B8 CRC64;
MSESSSKSSQ PLASKQEKDG TEKRGRGRPR KQPPVSPGTA LVGSQKEPSE VPTPKRPRGR
PKGSKNKGAA KTRKTTTTPG RKPRGRPKKL EKEEEEGISQ ESSEEEQ
