DEKP4_ARATH
ID DEKP4_ARATH Reviewed; 778 AA.
AC F4K4Y5; B9DFC8; Q9FM72;
DT 29-SEP-2021, integrated into UniProtKB/Swiss-Prot.
DT 28-JUN-2011, sequence version 1.
DT 03-AUG-2022, entry version 74.
DE RecName: Full=DEK domain-containing chromatin-associated protein 4 {ECO:0000303|PubMed:15496452};
DE Short=At-DEK4 {ECO:0000303|PubMed:25387881};
DE Short=AtDEK-4 {ECO:0000303|PubMed:15496452};
DE Short=Protein DEK 4 {ECO:0000303|PubMed:15496452};
GN Name=DEK4 {ECO:0000303|PubMed:15496452};
GN OrderedLocusNames=At5g55660 {ECO:0000312|Araport:AT5G55660};
GN ORFNames=MDF20.10 {ECO:0000312|EMBL:BAB09233.1};
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=9628582; DOI=10.1093/dnares/5.1.41;
RA Sato S., Kaneko T., Kotani H., Nakamura Y., Asamizu E., Miyajima N.,
RA Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 5. IV. Sequence
RT features of the regions of 1,456,315 bp covered by nineteen physically
RT assigned P1 and TAC clones.";
RL DNA Res. 5:41-54(1998).
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] OF 136-778.
RC STRAIN=cv. Columbia; TISSUE=Rosette leaf;
RX PubMed=19423640; DOI=10.1093/dnares/dsp009;
RA Iida K., Fukami-Kobayashi K., Toyoda A., Sakaki Y., Kobayashi M., Seki M.,
RA Shinozaki K.;
RT "Analysis of multiple occurrences of alternative splicing events in
RT Arabidopsis thaliana using novel sequenced full-length cDNAs.";
RL DNA Res. 16:155-164(2009).
RN [4]
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 [5]
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 [6]
RP INTERACTION WITH DEK3, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC STRAIN=cv. Columbia;
RX PubMed=25387881; DOI=10.1105/tpc.114.129254;
RA Waidmann S., Kusenda B., Mayerhofer J., Mechtler K., Jonak C.;
RT "A DEK domain-containing protein modulates chromatin structure and function
RT in Arabidopsis.";
RL Plant Cell 26:4328-4344(2014).
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: Interacts with DEK3. {ECO:0000269|PubMed:25387881}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q9SUA1,
CC ECO:0000255|PROSITE-ProRule:PRU00768}. Nucleus, nucleolus
CC {ECO:0000250|UniProtKB:Q9SUA1}. Note=Associates with chromatin (By
CC similarity). Enriched in regions where chromatin is decondensed or
CC sparse in the interphase nuclei (By similarity).
CC {ECO:0000250|UniProtKB:P35659, ECO:0000250|UniProtKB:Q9SUA1}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAB09233.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AB009050; BAB09233.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002688; AED96664.1; -; Genomic_DNA.
DR EMBL; AK316718; BAH19445.1; -; mRNA.
DR RefSeq; NP_200377.1; NM_124948.4.
DR AlphaFoldDB; F4K4Y5; -.
DR SMR; F4K4Y5; -.
DR IntAct; F4K4Y5; 6.
DR STRING; 3702.AT5G55660.1; -.
DR PaxDb; F4K4Y5; -.
DR PRIDE; F4K4Y5; -.
DR ProteomicsDB; 216037; -.
DR EnsemblPlants; AT5G55660.1; AT5G55660.1; AT5G55660.
DR GeneID; 835660; -.
DR Gramene; AT5G55660.1; AT5G55660.1; AT5G55660.
DR KEGG; ath:AT5G55660; -.
DR Araport; AT5G55660; -.
DR TAIR; locus:2162097; AT5G55660.
DR eggNOG; KOG2266; Eukaryota.
DR HOGENOM; CLU_011980_0_0_1; -.
DR InParanoid; F4K4Y5; -.
DR OMA; QLHDAIC; -.
DR OrthoDB; 1076774at2759; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; F4K4Y5; baseline and differential.
DR GO; GO:0005739; C:mitochondrion; HDA:TAIR.
DR GO; GO:0005730; C:nucleolus; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0009536; C:plastid; HDA:TAIR.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0042393; F:histone binding; IBA:GO_Central.
DR GO; GO:0006325; P:chromatin organization; IEA:UniProtKB-KW.
DR GO; GO:2000779; P:regulation of double-strand break repair; IBA:GO_Central.
DR InterPro; IPR044198; DEK.
DR InterPro; IPR014876; DEK_C.
DR PANTHER; PTHR13468; PTHR13468; 2.
DR Pfam; PF08766; DEK_C; 1.
DR PROSITE; PS51998; DEK_C; 1.
PE 1: Evidence at protein level;
KW Chromatin regulator; Coiled coil; DNA-binding; Nucleus; Reference proteome;
KW Transcription; Transcription regulation.
FT CHAIN 1..778
FT /note="DEK domain-containing chromatin-associated protein
FT 4"
FT /id="PRO_0000453267"
FT DOMAIN 685..740
FT /note="DEK-C"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01342"
FT DNA_BIND 703..717
FT /evidence="ECO:0000250|UniProtKB:P35659"
FT DNA_BIND 732..736
FT /evidence="ECO:0000250|UniProtKB:P35659"
FT REGION 1..334
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 475..689
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 741..778
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 191..300
FT /evidence="ECO:0000255"
FT COILED 526..587
FT /evidence="ECO:0000255"
FT COILED 732..766
FT /evidence="ECO:0000255"
FT MOTIF 289..296
FT /note="Nuclear localization signal 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00768"
FT MOTIF 489..496
FT /note="Nuclear localization signal 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00768"
FT MOTIF 618..625
FT /note="Nuclear localization signal 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00768"
FT COMPBIAS 11..31
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 36..109
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 121..180
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 189..246
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 247..282
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 283..300
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 308..334
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 505..527
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 528..557
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 580..605
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 606..622
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 628..656
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 668..689
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 742..760
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 761..778
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 778 AA; 87207 MW; 38B1FCFB0CAFBDA7 CRC64;
MGEEDTKVIV EPTANGTSSL QKTSDAISGK EVQENASGKE VQESKKEEDT GLEKMEIDDE
GKQHEGESET GDKEVEVTEE EKKDVGEDKE QPEADKMDED TDDKNLKADD GVSGVATEED
AVMKESVESA DNKDAENPEG EQEKESKEEK LEGGKANGNE EGDTEEKLVG GDKGDDVDEA
EKVENVDEDD KEEALKEKNE AELAEEEETN KGEEVKEANK EDDVEADTKV AEPEVEDKKT
ESKDENEDKE EEKEDEKEES MDDKEDEKEE SNDDDKEDEK EESNDDKEDK KEDIKKSNKR
GKGKTEKTRG KTKSDEEKKD IEPKTPFFSD RPVRERKSVE RLVAVVDKDS SREFHVEKGK
GTPLKDIPNV AYKVSRKKSD EVFKQLHTIL FGGKRVKATQ LKAHILRFSG YKWQGDEEKA
KLKVKEKFEK INKEKLLEFC DLFDISVAKA TTKKEDIVTK LVEFLEKPHA TTDVLVNEKE
KGVKRKRTPK KSSPAAGSSS SKRSAKSQKK TEEATRTNKK SVAHSDDESE EEKEDDEEEE
KEQEVEEEEE ENENGIPDKS EDEAPQLSES EENVESEEES EEETKKKKRG SRTSSDKKES
AGKSRSKKTA VPTKSSPPKK ATQKRSAGKR KKSDDDSDTS PKASSKRKKT EKPAKEQAAA
PLKSVSKEKP VIGKRGGKGK DKNKEPSDEE LKTAIIDILK GVDFNTATFT DILKRLDAKF
NISLASKKSS IKRMIQDELT KLADEAEDEE GEEEDAEHEE EEEKEKAKGS GGGEEVKA
