HMGB3_ARATH
ID HMGB3_ARATH Reviewed; 141 AA.
AC P93047; A8MQS4; Q2L6T4;
DT 02-NOV-2010, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1997, sequence version 1.
DT 03-AUG-2022, entry version 148.
DE RecName: Full=High mobility group B protein 3;
DE AltName: Full=High mobility group protein B 2;
DE Short=AtHMGbeta2;
DE Short=HMG beta 2;
DE AltName: Full=Nucleosome/chromatin assembly factor group D 03;
DE Short=Nucleosome/chromatin assembly factor group D 3;
GN Name=HMGB3; Synonyms=HMG1, HMGB2, HMGBETA2, NFD03, NFD3;
GN OrderedLocusNames=At1g20696; ORFNames=F2D10;
OS Arabidopsis thaliana (Mouse-ear cress).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX NCBI_TaxID=3702;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, AND TISSUE SPECIFICITY.
RC TISSUE=Leaf;
RX PubMed=9461286; DOI=10.1111/j.1432-1033.1997.00646.x;
RA Stemmer C., Ritt C., Igloi G.L., Grimm R., Grasser K.D.;
RT "Variability in Arabidopsis thaliana chromosomal high-mobility-group-1-like
RT proteins.";
RL Eur. J. Biochem. 250:646-652(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC STRAIN=cv. Columbia;
RA Webster C.I., Gray J.C.;
RL Submitted (NOV-1996) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=11130712; DOI=10.1038/35048500;
RA Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O.,
RA Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E.,
RA Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K., Conn L.,
RA Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P.,
RA Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D.,
RA Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J.,
RA Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L.,
RA Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A.,
RA Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A.,
RA Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M.,
RA Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M.,
RA Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P.,
RA Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D.,
RA Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D.,
RA Yu G., Fraser C.M., Venter J.C., Davis R.W.;
RT "Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana.";
RL Nature 408:816-820(2000).
RN [4]
RP GENOME REANNOTATION.
RC STRAIN=cv. Columbia;
RX PubMed=27862469; DOI=10.1111/tpj.13415;
RA Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA Town C.D.;
RT "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT genome.";
RL Plant J. 89:789-804(2017).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC STRAIN=cv. Columbia;
RX PubMed=14593172; DOI=10.1126/science.1088305;
RA Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M.,
RA Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
RA Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
RA Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
RA Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
RA Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
RA Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
RA Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
RA Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
RA Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
RA Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
RA Ecker J.R.;
RT "Empirical analysis of transcriptional activity in the Arabidopsis
RT genome.";
RL Science 302:842-846(2003).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RA Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B.,
RA Feldmann K.A.;
RT "Full-length cDNA from Arabidopsis thaliana.";
RL Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP PHOSPHORYLATION.
RX PubMed=12653554; DOI=10.1021/bi027350d;
RA Stemmer C., Leeming D.J., Franssen L., Grimm R., Grasser K.D.;
RT "Phosphorylation of maize and Arabidopsis HMGB proteins by protein kinase
RT CK2alpha.";
RL Biochemistry 42:3503-3508(2003).
RN [8]
RP TISSUE SPECIFICITY.
RX PubMed=17316617; DOI=10.1016/j.febslet.2007.02.015;
RA Launholt D., Groenlund J.T., Nielsen H.K., Grasser K.D.;
RT "Overlapping expression patterns among the genes encoding Arabidopsis
RT chromosomal high mobility group (HMG) proteins.";
RL FEBS Lett. 581:1114-1118(2007).
RN [9]
RP TISSUE SPECIFICITY, AND INDUCTION BY COLD; DROUGHT AND SALT.
RX PubMed=17169924; DOI=10.1093/pcp/pcl057;
RA Kwak K.J., Kim J.Y., Kim Y.O., Kang H.;
RT "Characterization of transgenic Arabidopsis plants overexpressing high
RT mobility group B proteins under high salinity, drought or cold stress.";
RL Plant Cell Physiol. 48:221-231(2007).
RN [10]
RP REVIEW, AND SUBCELLULAR LOCATION.
RX PubMed=20123078; DOI=10.1016/j.bbagrm.2009.11.004;
RA Pedersen D.S., Grasser K.D.;
RT "The role of chromosomal HMGB proteins in plants.";
RL Biochim. Biophys. Acta 1799:171-174(2010).
CC -!- FUNCTION: Binds preferentially double-stranded DNA.
CC {ECO:0000269|PubMed:9461286}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00267,
CC ECO:0000269|PubMed:20123078}. Cytoplasm, cytosol
CC {ECO:0000269|PubMed:20123078}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=P93047-1; Sequence=Displayed;
CC Name=2;
CC IsoId=P93047-2; Sequence=VSP_039943;
CC Name=3;
CC IsoId=P93047-3; Sequence=VSP_039942;
CC -!- TISSUE SPECIFICITY: Expressed in lateral roots, root tips, stems,
CC cotyledons, leaves and flowers (excluding ovary and pedicels).
CC {ECO:0000269|PubMed:17169924, ECO:0000269|PubMed:17316617,
CC ECO:0000269|PubMed:9461286}.
CC -!- INDUCTION: Up-regulated by cold stress, but down-regulated by drought
CC and salt stress. {ECO:0000269|PubMed:17169924}.
CC -!- SIMILARITY: Belongs to the HMGB family. {ECO:0000305}.
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DR EMBL; Y14073; CAA74402.1; -; mRNA.
DR EMBL; Y09482; CAA70691.1; -; mRNA.
DR EMBL; AC069251; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CP002684; AEE30009.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE30010.1; -; Genomic_DNA.
DR EMBL; AF411789; AAL06479.1; -; mRNA.
DR EMBL; AY097385; AAM19901.1; -; mRNA.
DR EMBL; AY136309; AAM96975.1; -; mRNA.
DR EMBL; BT000420; AAN15739.1; -; mRNA.
DR EMBL; AY084848; AAM61413.1; -; mRNA.
DR PIR; T51598; T51598.
DR RefSeq; NP_001031075.1; NM_001035998.1. [P93047-3]
DR RefSeq; NP_564124.1; NM_101921.4. [P93047-1]
DR AlphaFoldDB; P93047; -.
DR SMR; P93047; -.
DR BioGRID; 23898; 2.
DR STRING; 3702.AT1G20696.2; -.
DR iPTMnet; P93047; -.
DR PaxDb; P93047; -.
DR PRIDE; P93047; -.
DR ProteomicsDB; 230229; -. [P93047-1]
DR EnsemblPlants; AT1G20696.1; AT1G20696.1; AT1G20696. [P93047-1]
DR EnsemblPlants; AT1G20696.2; AT1G20696.2; AT1G20696. [P93047-3]
DR GeneID; 838659; -.
DR Gramene; AT1G20696.1; AT1G20696.1; AT1G20696. [P93047-1]
DR Gramene; AT1G20696.2; AT1G20696.2; AT1G20696. [P93047-3]
DR KEGG; ath:AT1G20696; -.
DR Araport; AT1G20696; -.
DR TAIR; locus:505006136; AT1G20696.
DR eggNOG; KOG0381; Eukaryota.
DR HOGENOM; CLU_082854_1_1_1; -.
DR InParanoid; P93047; -.
DR OMA; PLSAYMH; -.
DR OrthoDB; 1641977at2759; -.
DR PhylomeDB; P93047; -.
DR PRO; PR:P93047; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; P93047; baseline and differential.
DR Genevisible; P93047; AT.
DR GO; GO:0000785; C:chromatin; TAS:TAIR.
DR GO; GO:0005829; C:cytosol; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; HDA:TAIR.
DR GO; GO:0003682; F:chromatin binding; TAS:TAIR.
DR GO; GO:0003677; F:DNA binding; IDA:TAIR.
DR GO; GO:0003700; F:DNA-binding transcription factor activity; ISS:TAIR.
DR GO; GO:0030527; F:structural constituent of chromatin; TAS:TAIR.
DR GO; GO:0006325; P:chromatin organization; TAS:TAIR.
DR Gene3D; 1.10.30.10; -; 1.
DR InterPro; IPR009071; HMG_box_dom.
DR InterPro; IPR036910; HMG_box_dom_sf.
DR InterPro; IPR031061; HMGB_plant.
DR PANTHER; PTHR46261; PTHR46261; 1.
DR Pfam; PF00505; HMG_box; 1.
DR SMART; SM00398; HMG; 1.
DR SUPFAM; SSF47095; SSF47095; 1.
DR PROSITE; PS50118; HMG_BOX_2; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Cytoplasm; DNA-binding; Nucleus; Phosphoprotein;
KW Reference proteome.
FT CHAIN 1..141
FT /note="High mobility group B protein 3"
FT /id="PRO_0000399929"
FT DNA_BIND 35..104
FT /note="HMG box"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00267"
FT REGION 1..40
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 54..141
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..16
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 74..119
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 120..141
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 122
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O49595"
FT VAR_SEQ 108..141
FT /note="EEGPKEDEESDKSVSEVNDEDDAEDGSEEEEDDD -> VIALRKMRNLTSQF
FT QRLTMRMMLRMAVKRRKTMIKKLKLW (in isoform 3)"
FT /evidence="ECO:0000305"
FT /id="VSP_039942"
FT VAR_SEQ 137..141
FT /note="EEDDD -> VRRR (in isoform 2)"
FT /evidence="ECO:0000305"
FT /id="VSP_039943"
SQ SEQUENCE 141 AA; 15681 MW; 0E9F554C38903DC6 CRC64;
MKGAKSKAET RSTKLSVTKK PAKGAKGAAK DPNKPKRPSS AFFVFMEDFR VTYKEEHPKN
KSVAAVGKAG GEKWKSLSDS EKAPYVAKAD KRKVEYEKNM KAYNKKLEEG PKEDEESDKS
VSEVNDEDDA EDGSEEEEDD D
