HMGB2_ARATH
ID HMGB2_ARATH Reviewed; 144 AA.
AC O49596; A8MQZ3; Q2V4M2; Q9LM85;
DT 02-NOV-2010, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-1998, sequence version 1.
DT 03-AUG-2022, entry version 144.
DE RecName: Full=High mobility group B protein 2;
DE AltName: Full=High mobility group protein B 1;
DE Short=AtHMGbeta1;
DE Short=HMG beta 1;
DE AltName: Full=Nucleosome/chromatin assembly factor group D 02;
DE Short=Nucleosome/chromatin assembly factor group D 2;
GN Name=HMGB2; Synonyms=HMGB1, HMGBETA1, NFD02, NFD2;
GN OrderedLocusNames=At1g20693; ORFNames=F2D10.18;
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 [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 [3]
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 [4]
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC STRAIN=cv. Columbia;
RX PubMed=11910074; DOI=10.1126/science.1071006;
RA Seki M., Narusaka M., Kamiya A., Ishida J., Satou M., Sakurai T.,
RA Nakajima M., Enju A., Akiyama K., Oono Y., Muramatsu M., Hayashizaki Y.,
RA Kawai J., Carninci P., Itoh M., Ishii Y., Arakawa T., Shibata K.,
RA Shinagawa A., Shinozaki K.;
RT "Functional annotation of a full-length Arabidopsis cDNA collection.";
RL Science 296:141-145(2002).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RA Fujita M., Mizukado S., Seki M., Shinozaki K., Mitsuda N., Takiguchi Y.,
RA Takagi M.;
RT "ORF cloning and analysis of Arabidopsis transcription factor genes.";
RL Submitted (MAR-2009) to the EMBL/GenBank/DDBJ databases.
RN [7]
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 [8]
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 [9]
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 [10]
RP FUNCTION, 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 [11]
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. Confers sensitivity
CC to salt and drought stresses. {ECO:0000269|PubMed:17169924,
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=O49596-1; Sequence=Displayed;
CC Name=2;
CC IsoId=O49596-2; Sequence=VSP_039940;
CC Name=3;
CC IsoId=O49596-3; Sequence=VSP_039941;
CC -!- TISSUE SPECIFICITY: Mostly expressed in cotyledons, hypocotyls, leaves,
CC and flowers (excluding pedicels), also present in roots and stems.
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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAF80615.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; Y14072; CAA74401.1; -; mRNA.
DR EMBL; AC069251; AAF80615.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002684; AEE30006.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE30007.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE30008.1; -; Genomic_DNA.
DR EMBL; AF370248; AAK44063.1; -; mRNA.
DR EMBL; AY063064; AAL34238.1; -; mRNA.
DR EMBL; AK118543; BAC43146.1; -; mRNA.
DR EMBL; AB493468; BAH30306.1; -; mRNA.
DR EMBL; AY084731; AAM61305.1; -; mRNA.
DR PIR; F86339; F86339.
DR PIR; T51597; T51597.
DR RefSeq; NP_001031074.1; NM_001035997.1. [O49596-2]
DR RefSeq; NP_001077569.1; NM_001084100.1. [O49596-3]
DR RefSeq; NP_564123.1; NM_101920.3. [O49596-1]
DR AlphaFoldDB; O49596; -.
DR SMR; O49596; -.
DR BioGRID; 23897; 5.
DR IntAct; O49596; 4.
DR STRING; 3702.AT1G20693.1; -.
DR iPTMnet; O49596; -.
DR PaxDb; O49596; -.
DR PRIDE; O49596; -.
DR ProteomicsDB; 230263; -. [O49596-1]
DR EnsemblPlants; AT1G20693.1; AT1G20693.1; AT1G20693. [O49596-1]
DR EnsemblPlants; AT1G20693.2; AT1G20693.2; AT1G20693. [O49596-2]
DR EnsemblPlants; AT1G20693.3; AT1G20693.3; AT1G20693. [O49596-3]
DR GeneID; 838658; -.
DR Gramene; AT1G20693.1; AT1G20693.1; AT1G20693. [O49596-1]
DR Gramene; AT1G20693.2; AT1G20693.2; AT1G20693. [O49596-2]
DR Gramene; AT1G20693.3; AT1G20693.3; AT1G20693. [O49596-3]
DR KEGG; ath:AT1G20693; -.
DR Araport; AT1G20693; -.
DR TAIR; locus:505006135; AT1G20693.
DR eggNOG; KOG0381; Eukaryota.
DR InParanoid; O49596; -.
DR OMA; FMEDFRT; -.
DR OrthoDB; 1641977at2759; -.
DR PhylomeDB; O49596; -.
DR PRO; PR:O49596; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; O49596; baseline and differential.
DR Genevisible; O49596; AT.
DR GO; GO:0000785; C:chromatin; TAS:TAIR.
DR GO; GO:0005829; C:cytosol; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IDA: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..144
FT /note="High mobility group B protein 2"
FT /id="PRO_0000399928"
FT DNA_BIND 38..107
FT /note="HMG box"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00267"
FT REGION 1..42
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 57..94
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 106..144
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 77..94
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 106..122
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 123..144
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 125
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O49595"
FT VAR_SEQ 140..144
FT /note="EEDDD -> DDD (in isoform 2)"
FT /evidence="ECO:0000305"
FT /id="VSP_039940"
FT VAR_SEQ 141..144
FT /note="EDDD -> DDD (in isoform 3)"
FT /evidence="ECO:0000305"
FT /id="VSP_039941"
SQ SEQUENCE 144 AA; 15982 MW; 7A0AD686D4DB9AC3 CRC64;
MKGAKSKTET RSSKLSVTKK PAKGAGRGKA AAKDPNKPKR PASAFFVFME DFRETFKKEN
PKNKSVATVG KAAGDKWKSL SDSEKAPYVA KAEKRKVEYE KNIKAYNKKL EEGPKEDEES
DKSVSEVNDE DDAEDGSEEE EDDD
