DEKP1_ARATH
ID DEKP1_ARATH Reviewed; 462 AA.
AC Q9SMM8; A0A178VK90; Q0WMA0; Q8LFD2;
DT 29-SEP-2021, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 144.
DE RecName: Full=DEK domain-containing chromatin-associated protein 1 {ECO:0000303|PubMed:15496452};
DE Short=At-DEK1 {ECO:0000305};
DE Short=AtDEK-1 {ECO:0000303|PubMed:15496452};
DE Short=Protein DEK 1 {ECO:0000303|PubMed:15496452};
GN Name=DEK1 {ECO:0000303|PubMed:15496452};
GN OrderedLocusNames=At3g48710 {ECO:0000312|Araport:AT3G48710};
GN ORFNames=T8P19.220 {ECO:0000312|EMBL:CAB62360.1};
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=11130713; DOI=10.1038/35048706;
RA Salanoubat M., Lemcke K., Rieger M., Ansorge W., Unseld M., Fartmann B.,
RA Valle G., Bloecker H., Perez-Alonso M., Obermaier B., Delseny M.,
RA Boutry M., Grivell L.A., Mache R., Puigdomenech P., De Simone V.,
RA Choisne N., Artiguenave F., Robert C., Brottier P., Wincker P.,
RA Cattolico L., Weissenbach J., Saurin W., Quetier F., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Benes V., Wurmbach E., Drzonek H.,
RA Erfle H., Jordan N., Bangert S., Wiedelmann R., Kranz H., Voss H.,
RA Holland R., Brandt P., Nyakatura G., Vezzi A., D'Angelo M., Pallavicini A.,
RA Toppo S., Simionati B., Conrad A., Hornischer K., Kauer G., Loehnert T.-H.,
RA Nordsiek G., Reichelt J., Scharfe M., Schoen O., Bargues M., Terol J.,
RA Climent J., Navarro P., Collado C., Perez-Perez A., Ottenwaelder B.,
RA Duchemin D., Cooke R., Laudie M., Berger-Llauro C., Purnelle B., Masuy D.,
RA de Haan M., Maarse A.C., Alcaraz J.-P., Cottet A., Casacuberta E.,
RA Monfort A., Argiriou A., Flores M., Liguori R., Vitale D., Mannhaupt G.,
RA Haase D., Schoof H., Rudd S., Zaccaria P., Mewes H.-W., Mayer K.F.X.,
RA Kaul S., Town C.D., Koo H.L., Tallon L.J., Jenkins J., Rooney T., Rizzo M.,
RA Walts A., Utterback T., Fujii C.Y., Shea T.P., Creasy T.H., Haas B.,
RA Maiti R., Wu D., Peterson J., Van Aken S., Pai G., Militscher J.,
RA Sellers P., Gill J.E., Feldblyum T.V., Preuss D., Lin X., Nierman W.C.,
RA Salzberg S.L., White O., Venter J.C., Fraser C.M., Kaneko T., Nakamura Y.,
RA Sato S., Kato T., Asamizu E., Sasamoto S., Kimura T., Idesawa K.,
RA Kawashima K., Kishida Y., Kiyokawa C., Kohara M., Matsumoto M., Matsuno A.,
RA Muraki A., Nakayama S., Nakazaki N., Shinpo S., Takeuchi C., Wada T.,
RA Watanabe A., Yamada M., Yasuda M., Tabata S.;
RT "Sequence and analysis of chromosome 3 of the plant Arabidopsis thaliana.";
RL Nature 408:820-822(2000).
RN [2]
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RA Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A.,
RA Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y.,
RA Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K.,
RA Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J., Hayashizaki Y.,
RA Shinozaki K.;
RT "Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs.";
RL Submitted (JUL-2006) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RA Bautista V.R., Kim C.J., Chen H., Quinitio C., Ecker J.R.;
RT "Arabidopsis ORF Clone.";
RL Submitted (OCT-2006) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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 [6]
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 [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).
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}.
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DR EMBL; AL133315; CAB62360.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE78448.1; -; Genomic_DNA.
DR EMBL; AK229882; BAF01711.1; -; mRNA.
DR EMBL; AK229930; BAF01756.1; -; mRNA.
DR EMBL; AK229931; BAF01757.1; -; mRNA.
DR EMBL; AK229982; BAF01807.1; -; mRNA.
DR EMBL; AK230134; BAF01949.1; -; mRNA.
DR EMBL; BT029155; ABJ17090.1; -; mRNA.
DR EMBL; AY084914; AAM61476.1; -; mRNA.
DR PIR; T46215; T46215.
DR RefSeq; NP_190440.1; NM_114730.3.
DR AlphaFoldDB; Q9SMM8; -.
DR SMR; Q9SMM8; -.
DR STRING; 3702.AT3G48710.1; -.
DR PaxDb; Q9SMM8; -.
DR PRIDE; Q9SMM8; -.
DR ProteomicsDB; 185769; -.
DR EnsemblPlants; AT3G48710.1; AT3G48710.1; AT3G48710.
DR GeneID; 824032; -.
DR Gramene; AT3G48710.1; AT3G48710.1; AT3G48710.
DR KEGG; ath:AT3G48710; -.
DR Araport; AT3G48710; -.
DR TAIR; locus:2114495; AT3G48710.
DR eggNOG; KOG2266; Eukaryota.
DR HOGENOM; CLU_011980_2_0_1; -.
DR InParanoid; Q9SMM8; -.
DR OMA; IAPGKGQ; -.
DR OrthoDB; 1076774at2759; -.
DR PhylomeDB; Q9SMM8; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q9SMM8; baseline and differential.
DR GO; GO:0005829; C:cytosol; HDA:TAIR.
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:2000779; P:regulation of double-strand break repair; IBA:GO_Central.
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 Chromatin regulator; DNA-binding; Nucleus; Reference proteome;
KW Transcription; Transcription regulation.
FT CHAIN 1..462
FT /note="DEK domain-containing chromatin-associated protein
FT 1"
FT /id="PRO_0000453264"
FT DOMAIN 384..439
FT /note="DEK-C"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01342"
FT DNA_BIND 402..416
FT /evidence="ECO:0000250|UniProtKB:P35659"
FT DNA_BIND 431..435
FT /evidence="ECO:0000250|UniProtKB:P35659"
FT REGION 18..91
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 212..390
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 438..462
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 344..351
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00768"
FT COMPBIAS 20..36
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 58..72
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 232..250
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 251..267
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 268..284
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 285..302
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 310..334
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 341..363
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 372..390
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 439..456
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CONFLICT 2
FT /note="A -> T (in Ref. 5; AAM61476)"
FT /evidence="ECO:0000305"
FT CONFLICT 20..33
FT /note="TEKDTETKKKDEVE -> IEKDRETKKNDEVG (in Ref. 5;
FT AAM61476)"
FT /evidence="ECO:0000305"
FT CONFLICT 45
FT /note="I -> N (in Ref. 5; AAM61476)"
FT /evidence="ECO:0000305"
FT CONFLICT 52
FT /note="S -> L (in Ref. 5; AAM61476)"
FT /evidence="ECO:0000305"
FT CONFLICT 237
FT /note="R -> K (in Ref. 5; AAM61476)"
FT /evidence="ECO:0000305"
FT CONFLICT 267
FT /note="N -> T (in Ref. 5; AAM61476)"
FT /evidence="ECO:0000305"
FT CONFLICT 288..290
FT /note="DEK -> VER (in Ref. 3; BAF01711/BAF01756)"
FT /evidence="ECO:0000305"
FT CONFLICT 300
FT /note="T -> I (in Ref. 5; AAM61476)"
FT /evidence="ECO:0000305"
FT CONFLICT 319
FT /note="E -> K (in Ref. 5; AAM61476)"
FT /evidence="ECO:0000305"
FT CONFLICT 333
FT /note="F -> S (in Ref. 5; AAM61476)"
FT /evidence="ECO:0000305"
FT CONFLICT 341
FT /note="T -> S (in Ref. 5; AAM61476)"
FT /evidence="ECO:0000305"
FT CONFLICT 443
FT /note="D -> E (in Ref. 5; AAM61476)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 462 AA; 52067 MW; ABF12A09220F97DE CRC64;
MATETLELKT PQLADTVAVT EKDTETKKKD EVEKDEAMEE KGEEIDGEKV KSPVTPVSER
PIRERKRTGR YVIDTPPRSS GNKPLSITQG RGTRLKEIPN VAYKLSKRKP DDNLFLLHTI
LYGKKAKAQM LKKNIGQFSG FVWSEQEEEK QRAKAKEKLD KCIKEKLIDF CDVLDIPVNK
STVKKEELAV RVLEFLVCPK ATRDILLADS EKETKKRKKS TSKNVTSGES SHVPAKRRRQ
AKKQEQPTET EGNGESDVGS EGTNDSNGED DVAPEEENNK SEDTETEDEK DKAKEKTKST
DKKRLSKRTK KEKPAAEEEK SIKGSAKSSR KSFRQVDKST TSSSKKQKVD KDDSSKEKGK
TQTSKPQAKG SKDQGQSRKK GKKEPTRKEL HVVVTKILKE VDFNTATLSD ILRKLGSHFG
IDLMHRKAEV KDIITDAINE MSDDDDEKEE DTEDEGEKEG KD
