DEKP2_ARATH
ID DEKP2_ARATH Reviewed; 530 AA.
AC Q84JB7; Q9FFQ8;
DT 29-SEP-2021, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 03-AUG-2022, entry version 127.
DE RecName: Full=DEK domain-containing chromatin-associated protein 2 {ECO:0000303|PubMed:15496452};
DE Short=At-DEK2 {ECO:0000305};
DE Short=AtDEK-2 {ECO:0000303|PubMed:15496452};
DE Short=Protein DEK 2 {ECO:0000303|PubMed:15496452};
GN Name=DEK2 {ECO:0000303|PubMed:15496452};
GN OrderedLocusNames=At5g63550 {ECO:0000312|Araport:AT5G63550};
GN ORFNames=MLE2.18 {ECO:0000312|EMBL:BAB10448.1};
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 [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=9330910; DOI=10.1093/dnares/4.3.215;
RA Sato S., Kotani H., Nakamura Y., Kaneko T., Asamizu E., Fukami M.,
RA Miyajima N., Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 5. I. Sequence
RT features of the 1.6 Mb regions covered by twenty physically assigned P1
RT clones.";
RL DNA Res. 4:215-230(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=9501997; DOI=10.1093/dnares/4.6.401;
RA Nakamura Y., Sato S., Kaneko T., Kotani H., Asamizu E., Miyajima N.,
RA Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 5. III. Sequence
RT features of the regions of 1,191,918 bp covered by seventeen physically
RT assigned P1 clones.";
RL DNA Res. 4:401-414(1997).
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 GENE FAMILY, AND NOMENCLATURE.
RX PubMed=15496452; DOI=10.1091/mbc.e04-09-0791;
RA Pendle A.F., Clark G.P., Boon R., Lewandowska D., Lam Y.W., Andersen J.,
RA Mann M., Lamond A.I., Brown J.W., Shaw P.J.;
RT "Proteomic analysis of the Arabidopsis nucleolus suggests novel nucleolar
RT functions.";
RL Mol. Biol. Cell 16:260-269(2005).
RN [6]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19245862; DOI=10.1016/j.jprot.2009.02.004;
RA Jones A.M.E., MacLean D., Studholme D.J., Serna-Sanz A., Andreasson E.,
RA Rathjen J.P., Peck S.C.;
RT "Phosphoproteomic analysis of nuclei-enriched fractions from Arabidopsis
RT thaliana.";
RL J. Proteomics 72:439-451(2009).
RN [7]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19376835; DOI=10.1104/pp.109.138677;
RA Reiland S., Messerli G., Baerenfaller K., Gerrits B., Endler A.,
RA Grossmann J., Gruissem W., Baginsky S.;
RT "Large-scale Arabidopsis phosphoproteome profiling reveals novel
RT chloroplast kinase substrates and phosphorylation networks.";
RL Plant Physiol. 150:889-903(2009).
RN [8]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22223895; DOI=10.1074/mcp.m111.015131;
RA Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T.,
RA Giglione C.;
RT "Comparative large-scale characterisation of plant vs. mammal proteins
RT reveals similar and idiosyncratic N-alpha acetylation features.";
RL Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012).
CC -!- FUNCTION: Chromatin-associated protein which contributes to the
CC modulation of chromatin structure (such as super-helical structure of
CC DNA) and function (By similarity). Binds to chromatin of protein-coding
CC genes throughout the genome to regulate nucleosome occupancy and
CC chromatin accessibility, and to modulate the expression of target genes
CC (By similarity). {ECO:0000250|UniProtKB:Q9SUA1}.
CC -!- SUBUNIT: Found in a mRNA splicing-dependent exon junction complex (EJC)
CC (By similarity). Binds specifically histones H3 and H4 (By similarity).
CC {ECO:0000250|UniProtKB:Q9SUA1}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00768}.
CC Nucleus, nucleolus {ECO:0000250|UniProtKB:Q9SUA1}. Note=Associates with
CC chromatin (By similarity). Enriched in regions where chromatin is
CC decondensed or sparse in the interphase nuclei (By similarity).
CC {ECO:0000250|UniProtKB:P35659, ECO:0000250|UniProtKB:Q9SUA1}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q84JB7-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q84JB7-2; Sequence=VSP_061115;
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DR EMBL; AB005234; BAB10448.1; -; Genomic_DNA.
DR EMBL; AB007649; BAB10448.1; JOINED; Genomic_DNA.
DR EMBL; CP002688; AED97767.1; -; Genomic_DNA.
DR EMBL; CP002688; AED97768.1; -; Genomic_DNA.
DR EMBL; BT004149; AAO42170.1; -; mRNA.
DR EMBL; BT005478; AAO63898.1; -; mRNA.
DR RefSeq; NP_001154794.1; NM_001161322.2. [Q84JB7-2]
DR RefSeq; NP_201160.2; NM_125750.6. [Q84JB7-1]
DR SMR; Q84JB7; -.
DR STRING; 3702.AT5G63550.2; -.
DR PRIDE; Q84JB7; -.
DR ProteomicsDB; 187843; -.
DR ProteomicsDB; 187893; -.
DR EnsemblPlants; AT5G63550.1; AT5G63550.1; AT5G63550. [Q84JB7-1]
DR EnsemblPlants; AT5G63550.2; AT5G63550.2; AT5G63550. [Q84JB7-2]
DR GeneID; 836474; -.
DR Gramene; AT5G63550.1; AT5G63550.1; AT5G63550. [Q84JB7-1]
DR Gramene; AT5G63550.2; AT5G63550.2; AT5G63550. [Q84JB7-2]
DR KEGG; ath:AT5G63550; -.
DR Araport; AT5G63550; -.
DR TAIR; locus:2167301; AT5G63550.
DR eggNOG; KOG2266; Eukaryota.
DR HOGENOM; CLU_011980_2_0_1; -.
DR OMA; MEANAEM; -.
DR OrthoDB; 1076774at2759; -.
DR PhylomeDB; Q84JB7; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q84JB7; baseline and differential.
DR GO; GO:0005730; C:nucleolus; ISS:UniProtKB.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0003682; F:chromatin binding; ISS:UniProtKB.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0042393; F:histone binding; ISS:UniProtKB.
DR GO; GO:0006338; P:chromatin remodeling; ISS:UniProtKB.
DR GO; GO:0045892; P:negative regulation of transcription, DNA-templated; ISS:UniProtKB.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; ISS:UniProtKB.
DR InterPro; IPR044198; DEK.
DR InterPro; IPR014876; DEK_C.
DR PANTHER; PTHR13468; PTHR13468; 1.
DR Pfam; PF08766; DEK_C; 1.
DR PROSITE; PS51998; DEK_C; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Chromatin regulator; Coiled coil; DNA-binding;
KW Nucleus; Reference proteome; Transcription; Transcription regulation.
FT CHAIN 1..530
FT /note="DEK domain-containing chromatin-associated protein
FT 2"
FT /id="PRO_0000453265"
FT DOMAIN 426..481
FT /note="DEK-C"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01342"
FT DNA_BIND 444..458
FT /evidence="ECO:0000250|UniProtKB:P35659"
FT DNA_BIND 473..477
FT /evidence="ECO:0000250|UniProtKB:P35659"
FT REGION 1..130
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 246..430
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 482..530
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 41..61
FT /evidence="ECO:0000255"
FT COILED 185..205
FT /evidence="ECO:0000255"
FT COILED 492..527
FT /evidence="ECO:0000255"
FT MOTIF 260..267
FT /note="Nuclear localization signal 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00768"
FT MOTIF 343..350
FT /note="Nuclear localization signal 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00768"
FT MOTIF 384..391
FT /note="Nuclear localization signal 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00768"
FT COMPBIAS 11..46
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 66..81
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 82..112
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 246..289
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 290..323
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 324..364
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 365..383
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 384..430
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 482..499
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT VAR_SEQ 252
FT /note="K -> KQ (in isoform 2)"
FT /evidence="ECO:0000305"
FT /id="VSP_061115"
SQ SEQUENCE 530 AA; 59428 MW; D26189E1AF9763CF CRC64;
MATETLDEKT PEVNSPAKEE IDVVPKEEKE VEKEKVDSPR IGEAEEEKKE DEEEGEAKEG
ELGEKDKEDD VESEEEEEEE EGSGSKKSSE KETVTPTSER PTRERKKVER FSLSTPMRAP
PSKSVSIEKG RGTPLREIPN VAHKLSKRKA DDNLMLLHTI LFGKKAKAQM VKRNIGQFSG
FAWSEKEEEK QRARIKEKID KCVKEKLIVF CDVLDIPISR SNVKKEELAV KVLEFLESPK
ETRDVIIADQ EKAKKRKSTP KRGKSGESSD TPAKRKRQTK KRDLPSDTEE GKDEGDADSE
GTNDPHEEDD AAPEEESDHE KTDTDDEKDE VEVEKPSKKK SSSKKTVEES SGSKGKDKQP
SAKGSARSGE KSSKQIAKST SSPAKKQKVD HVESSKEKSK KQPSKPQAKG SKEKGKATKK
GKAKAEPTRK EMLEVVSKIL KEVDFNTATL SDILQKLSDH FGVELSHRKP EVKDVITEAI
NAMTDDEEED EEEEAEAGSD KEKEEVKGEE EEEKAEAESD KEKEKEEPKD
