HMGA1_CHITE
ID HMGA1_CHITE Reviewed; 99 AA.
AC Q23794; Q23793;
DT 29-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 25-MAY-2022, entry version 79.
DE RecName: Full=High mobility group protein I;
DE Short=HMG-I;
DE AltName: Full=High mobility group AT-hook protein 1;
DE Short=High mobility group protein A1;
DE AltName: Full=cHMG1;
OS Chironomus tentans (Midge) (Camptochironomus tentans).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Nematocera; Chironomoidea; Chironomidae;
OC Chironominae; Chironomus.
OX NCBI_TaxID=7153;
RN [1] {ECO:0000305, ECO:0000312|EMBL:CAA85365.1}
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA], PARTIAL PROTEIN SEQUENCE,
RP FUNCTION, AND SUBCELLULAR LOCATION.
RC TISSUE=Embryonic epithelium {ECO:0000269|PubMed:7806532}, and
RC Salivary gland {ECO:0000269|PubMed:7806532};
RX PubMed=7806532; DOI=10.1016/s0021-9258(20)30095-8;
RA Claus P., Schulze E., Wisniewski J.R.;
RT "Insect proteins homologous to mammalian high mobility group proteins I/Y
RT (HMG I/Y). Characterization and binding to linear and four-way junction
RT DNA.";
RL J. Biol. Chem. 269:33042-33048(1994).
RN [2] {ECO:0000305}
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=9087379; DOI=10.1007/bf02529752;
RA Ghidelli S., Claus P., Thies G., Wisniewski J.R.;
RT "High mobility group proteins cHMG1a, cHMG1b, and cHMGI are distinctly
RT distributed in chromosomes and differentially expressed during ecdysone
RT dependent cell differentiation.";
RL Chromosoma 105:369-379(1997).
RN [3] {ECO:0000305}
RP PHOSPHORYLATION AT SER-4; SER-23 AND SER-73.
RX PubMed=9341202; DOI=10.1074/jbc.272.43.27476;
RA Schwanbeck R., Wisniewski J.R.;
RT "Cdc2 and mitogen-activated protein kinases modulate DNA binding properties
RT of the putative transcriptional regulator Chironomus high mobility group
RT protein I.";
RL J. Biol. Chem. 272:27476-27483(1997).
RN [4] {ECO:0000305}
RP DNA-BINDING ACTIVITY.
RX PubMed=11034995; DOI=10.1074/jbc.m004065200;
RA Piekielko A., Drung A., Rogalla P., Schwanbeck R., Heyduk T., Gerharz M.,
RA Bullerdiek J., Wisniewski J.R.;
RT "Distinct organization of DNA complexes of various HMGI/Y family proteins
RT and their modulation upon mitotic phosphorylation.";
RL J. Biol. Chem. 276:1984-1992(2001).
CC -!- FUNCTION: Binds preferentially to the minor groove of A+T rich regions
CC in double-stranded DNA via the second and third DBA-binding domains. It
CC is suggested that these proteins could function in nucleosome phasing
CC and in the 3'-end processing of mRNA transcripts. They are also
CC involved in the transcription regulation of genes containing, or in
CC close proximity to A+T-rich regions. {ECO:0000269|PubMed:7806532,
CC ECO:0000269|PubMed:9087379}.
CC -!- SUBCELLULAR LOCATION: Nucleus, nucleolus. Chromosome. Note=In
CC chromosomal puffs. {ECO:0000269|PubMed:7806532,
CC ECO:0000269|PubMed:9087379}.
CC -!- PTM: Phosphorylated in a cell-cycle dependent manner; substantially
CC reduced in cells that have finished proliferating and are
CC differentiated. Phosphorylation at Ser-4 and Ser-23 results in a 10-
CC fold weakening of DNA-binding activity and altered the mode of protein-
CC DNA interaction. {ECO:0000269|PubMed:9341202}.
CC -!- SIMILARITY: Belongs to the HMGA family. {ECO:0000255}.
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DR EMBL; Z36897; CAA85364.1; -; Genomic_DNA.
DR EMBL; Z36898; CAA85365.1; -; mRNA.
DR PIR; A55819; A55819.
DR AlphaFoldDB; Q23794; -.
DR iPTMnet; Q23794; -.
DR GO; GO:0005694; C:chromosome; IEA:UniProtKB-SubCell.
DR GO; GO:0005730; C:nucleolus; IDA:UniProtKB.
DR GO; GO:0005667; C:transcription regulator complex; IDA:UniProtKB.
DR GO; GO:0003700; F:DNA-binding transcription factor activity; IDA:UniProtKB.
DR GO; GO:0003680; F:minor groove of adenine-thymine-rich DNA binding; IDA:UniProtKB.
DR InterPro; IPR017956; AT_hook_DNA-bd_motif.
DR PRINTS; PR00929; ATHOOK.
DR SMART; SM00384; AT_hook; 3.
PE 1: Evidence at protein level;
KW Chromosome; Direct protein sequencing; DNA-binding; Nucleus;
KW Phosphoprotein; Repeat; Transcription; Transcription regulation.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:7806532"
FT CHAIN 2..99
FT /note="High mobility group protein I"
FT /id="PRO_0000289153"
FT DNA_BIND 7..19
FT /note="A.T hook 1"
FT /evidence="ECO:0000255"
FT DNA_BIND 54..66
FT /note="A.T hook 2"
FT /evidence="ECO:0000255"
FT DNA_BIND 74..86
FT /note="A.T hook 3"
FT /evidence="ECO:0000255"
FT REGION 1..99
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..71
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 4
FT /note="Phosphoserine; by CDC2 and MAPK"
FT /evidence="ECO:0000269|PubMed:9341202"
FT MOD_RES 23
FT /note="Phosphoserine; by MAPK"
FT /evidence="ECO:0000269|PubMed:9341202"
FT MOD_RES 73
FT /note="Phosphoserine; by PKC"
FT /evidence="ECO:0000269|PubMed:9341202"
FT CONFLICT 92
FT /note="T -> A (in Ref. 1; CAA85364)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 99 AA; 10502 MW; 1AA44A226B8A698C CRC64;
MSDSPVKKGR GRPAKAKPEE TASPKAAKKE EKKVEEVPKK IEESTKPENG AAPKKGRGRP
SKGDKAAPKR PASGKGRGRP AKNAKKVDDA DTEEVNSSD
