EP400_MOUSE
ID EP400_MOUSE Reviewed; 3072 AA.
AC Q8CHI8; E9QKV1; Q3TPY1; Q5RKN8; Q80TC8; Q8BXI5; Q8BYW3; Q8C0P6; Q8CHI7;
AC Q8VDF4; Q9DA54;
DT 23-NOV-2004, integrated into UniProtKB/Swiss-Prot.
DT 27-JUL-2011, sequence version 3.
DT 03-AUG-2022, entry version 166.
DE RecName: Full=E1A-binding protein p400;
DE EC=3.6.4.-;
DE AltName: Full=Domino homolog;
DE Short=mDomino;
DE AltName: Full=p400 kDa SWI2/SNF2-related protein;
GN Name=Ep400; Synonyms=Kiaa1498;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 2 AND 3), AND INTERACTION WITH ZNF42.
RX PubMed=12653961; DOI=10.1046/j.1365-2443.2003.00636.x;
RA Ogawa H., Ueda T., Aoyama T., Aronheim A., Nagata S., Fukunaga R.;
RT "A SWI2/SNF2-type ATPase/helicase protein, mDomino, interacts with myeloid
RT zinc finger protein 2A (MZF-2A) to regulate its transcriptional activity.";
RL Genes Cells 8:325-339(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-896 (ISOFORM 3), NUCLEOTIDE
RP SEQUENCE [LARGE SCALE MRNA] OF 1-894 (ISOFORM 2), NUCLEOTIDE SEQUENCE
RP [LARGE SCALE MRNA] OF 1-677 (ISOFORM 1), AND NUCLEOTIDE SEQUENCE [LARGE
RP SCALE MRNA] OF 992-2359.
RC STRAIN=C57BL/6J;
RC TISSUE=Cerebellum, Corpora quadrigemina, Embryo, Testis, and Thymus;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1415-3072 (ISOFORM 5).
RC TISSUE=Brain;
RX PubMed=14621295; DOI=10.1093/dnares/10.4.167;
RA Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S.,
RA Saga Y., Nagase T., Ohara O., Koga H.;
RT "Prediction of the coding sequences of mouse homologues of KIAA gene: III.
RT The complete nucleotide sequences of 500 mouse KIAA-homologous cDNAs
RT identified by screening of terminal sequences of cDNA clones randomly
RT sampled from size-fractionated libraries.";
RL DNA Res. 10:167-180(2003).
RN [5]
RP SEQUENCE REVISION.
RA Okazaki N., Kikuno R., Nagase T., Ohara O., Koga H.;
RL Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1881-3072 (ISOFORM 4), AND
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 2429-3072 (ISOFORMS 1/2/3).
RC STRAIN=C57BL/6J, and FVB/N-3; TISSUE=Brain, and Mammary gland;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [7]
RP PROTEIN SEQUENCE OF 2443-2450, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC STRAIN=OF1; TISSUE=Hippocampus;
RA Lubec G., Sunyer B., Chen W.-Q.;
RL Submitted (JAN-2009) to UniProtKB.
RN [8]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT "Large-scale phosphorylation analysis of mouse liver.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN [9]
RP INTERACTION WITH PHF5A.
RX PubMed=18758164; DOI=10.1159/000138890;
RA Rzymski T., Grzmil P., Meinhardt A., Wolf S., Burfeind P.;
RT "PHF5A represents a bridge protein between splicing proteins and ATP-
RT dependent helicases and is differentially expressed during mouse
RT spermatogenesis.";
RL Cytogenet. Genome Res. 121:232-244(2008).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-52; SER-134; SER-315;
RP SER-321; SER-741; SER-754; THR-922; SER-923; SER-927; SER-940; THR-944;
RP SER-1009 AND SER-1010, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP ANALYSIS].
RC TISSUE=Brain, Heart, Kidney, Liver, Lung, Pancreas, Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
CC -!- FUNCTION: Component of the NuA4 histone acetyltransferase complex which
CC is involved in transcriptional activation of select genes principally
CC by acetylation of nucleosomal histones H4 and H2A. This modification
CC may both alter nucleosome - DNA interactions and promote interaction of
CC the modified histones with other proteins which positively regulate
CC transcription. May be required for transcriptional activation of E2F1
CC and MYC target genes during cellular proliferation. The NuA4 complex
CC ATPase and helicase activities seem to be, at least in part,
CC contributed by the association of RUVBL1 and RUVBL2 with EP400.
CC Component of a SWR1-like complex that specifically mediates the removal
CC of histone H2A.Z/H2AZ1 from the nucleosome (By similarity). Regulates
CC transcriptional activity of ZNF42. {ECO:0000250}.
CC -!- SUBUNIT: Component of the NuA4 histone acetyltransferase complex which
CC contains the catalytic subunit KAT5/TIP60 and the subunits EP400,
CC TRRAP/PAF400, BRD8/SMAP, EPC1, DMAP1/DNMAP1, RUVBL1/TIP49, RUVBL2,
CC ING3, actin, ACTL6A/BAF53A, MORF4L1/MRG15, MORF4L2/MRGX, MRGBP,
CC YEATS4/GAS41, VPS72/YL1 and MEAF6. May also participate in the
CC formation of NuA4 related complexes which lack the KAT5/TIP60 catalytic
CC subunit, but which include the SWI/SNF related protein SRCAP. The NuA4
CC complex interacts with MYC. EP400 interacts with TRRAP, RUVBL1 and
CC RUVBL2. Component of a SWR1-like complex (By similarity). Interacts
CC with ZNF42. Interacts with PHF5A. {ECO:0000250,
CC ECO:0000269|PubMed:12653961, ECO:0000269|PubMed:18758164}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00549}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=5;
CC Name=1;
CC IsoId=Q8CHI8-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8CHI8-2; Sequence=VSP_011996;
CC Name=3;
CC IsoId=Q8CHI8-3; Sequence=VSP_011996, VSP_011997;
CC Name=4;
CC IsoId=Q8CHI8-4; Sequence=VSP_011998;
CC Name=5;
CC IsoId=Q8CHI8-5; Sequence=VSP_017127, VSP_011998;
CC -!- TISSUE SPECIFICITY: Expressed in brain, thymus, lung, liver, spleen,
CC kidney, colon and bone marrow.
CC -!- SIMILARITY: Belongs to the SNF2/RAD54 helicase family. SWR1 subfamily.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAB24439.1; Type=Miscellaneous discrepancy; Note=Intron retention.; Evidence={ECO:0000305};
CC Sequence=BAC26781.1; Type=Miscellaneous discrepancy; Note=Intron retention.; Evidence={ECO:0000305};
CC Sequence=BAC32913.2; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AB092694; BAC45253.1; -; mRNA.
DR EMBL; AB092695; BAC45254.1; -; mRNA.
DR EMBL; AC161348; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AK006168; BAB24439.1; ALT_SEQ; mRNA.
DR EMBL; AK030095; BAC26781.1; ALT_SEQ; mRNA.
DR EMBL; AK037693; BAC29849.2; -; mRNA.
DR EMBL; AK046892; BAC32913.2; ALT_INIT; mRNA.
DR EMBL; AK163566; BAE37399.1; -; mRNA.
DR EMBL; AK164049; BAE37604.1; -; mRNA.
DR EMBL; AK122517; BAC65799.2; -; Transcribed_RNA.
DR EMBL; BC022153; AAH22153.1; -; mRNA.
DR EMBL; BC085511; AAH85511.1; -; mRNA.
DR CCDS; CCDS19529.1; -. [Q8CHI8-2]
DR CCDS; CCDS51612.1; -. [Q8CHI8-3]
DR RefSeq; NP_083613.2; NM_029337.2. [Q8CHI8-2]
DR RefSeq; NP_775089.1; NM_173066.1. [Q8CHI8-3]
DR RefSeq; XP_006535339.1; XM_006535276.3. [Q8CHI8-4]
DR SMR; Q8CHI8; -.
DR BioGRID; 217577; 18.
DR ComplexPortal; CPX-990; NuA4 histone acetyltransferase complex.
DR DIP; DIP-61766N; -.
DR IntAct; Q8CHI8; 12.
DR MINT; Q8CHI8; -.
DR STRING; 10090.ENSMUSP00000049038; -.
DR iPTMnet; Q8CHI8; -.
DR PhosphoSitePlus; Q8CHI8; -.
DR CPTAC; non-CPTAC-3461; -.
DR EPD; Q8CHI8; -.
DR jPOST; Q8CHI8; -.
DR MaxQB; Q8CHI8; -.
DR PaxDb; Q8CHI8; -.
DR PeptideAtlas; Q8CHI8; -.
DR PRIDE; Q8CHI8; -.
DR ProteomicsDB; 275620; -. [Q8CHI8-1]
DR ProteomicsDB; 275621; -. [Q8CHI8-2]
DR ProteomicsDB; 275622; -. [Q8CHI8-3]
DR ProteomicsDB; 275623; -. [Q8CHI8-4]
DR ProteomicsDB; 275624; -. [Q8CHI8-5]
DR Antibodypedia; 19445; 103 antibodies from 19 providers.
DR DNASU; 75560; -.
DR Ensembl; ENSMUST00000041558; ENSMUSP00000049038; ENSMUSG00000029505. [Q8CHI8-2]
DR Ensembl; ENSMUST00000112435; ENSMUSP00000108054; ENSMUSG00000029505. [Q8CHI8-5]
DR Ensembl; ENSMUST00000112436; ENSMUSP00000108055; ENSMUSG00000029505. [Q8CHI8-3]
DR GeneID; 75560; -.
DR KEGG; mmu:75560; -.
DR UCSC; uc008yrf.1; mouse. [Q8CHI8-4]
DR UCSC; uc008yrg.1; mouse. [Q8CHI8-2]
DR UCSC; uc008yrh.1; mouse. [Q8CHI8-3]
DR CTD; 57634; -.
DR MGI; MGI:1276124; Ep400.
DR VEuPathDB; HostDB:ENSMUSG00000029505; -.
DR eggNOG; KOG0391; Eukaryota.
DR GeneTree; ENSGT00940000154764; -.
DR HOGENOM; CLU_000397_0_0_1; -.
DR InParanoid; Q8CHI8; -.
DR OMA; YGEDCRG; -.
DR OrthoDB; 188211at2759; -.
DR TreeFam; TF106424; -.
DR Reactome; R-MMU-2559584; Formation of Senescence-Associated Heterochromatin Foci (SAHF).
DR Reactome; R-MMU-2559586; DNA Damage/Telomere Stress Induced Senescence.
DR BioGRID-ORCS; 75560; 21 hits in 78 CRISPR screens.
DR ChiTaRS; Ep400; mouse.
DR PRO; PR:Q8CHI8; -.
DR Proteomes; UP000000589; Chromosome 5.
DR RNAct; Q8CHI8; protein.
DR Bgee; ENSMUSG00000029505; Expressed in animal zygote and 194 other tissues.
DR ExpressionAtlas; Q8CHI8; baseline and differential.
DR Genevisible; Q8CHI8; MM.
DR GO; GO:0035267; C:NuA4 histone acetyltransferase complex; ISS:UniProtKB.
DR GO; GO:0016607; C:nuclear speck; IDA:UniProtKB.
DR GO; GO:0000786; C:nucleosome; ISO:MGI.
DR GO; GO:0005634; C:nucleus; ISO:MGI.
DR GO; GO:0000812; C:Swr1 complex; ISS:UniProtKB.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0140658; F:ATP-dependent chromatin remodeler activity; IEA:InterPro.
DR GO; GO:0003682; F:chromatin binding; ISO:MGI.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0004386; F:helicase activity; IEA:UniProtKB-KW.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR GO; GO:1990405; F:protein antigen binding; ISO:MGI.
DR GO; GO:0006281; P:DNA repair; IBA:GO_Central.
DR GO; GO:0016573; P:histone acetylation; IC:ComplexPortal.
DR GO; GO:0043968; P:histone H2A acetylation; ISS:UniProtKB.
DR GO; GO:0043967; P:histone H4 acetylation; ISS:UniProtKB.
DR GO; GO:1905168; P:positive regulation of double-strand break repair via homologous recombination; ISO:MGI.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IC:ComplexPortal.
DR GO; GO:0042981; P:regulation of apoptotic process; IC:ComplexPortal.
DR GO; GO:0051726; P:regulation of cell cycle; ISO:MGI.
DR GO; GO:2000779; P:regulation of double-strand break repair; IC:ComplexPortal.
DR Gene3D; 3.40.50.10810; -; 1.
DR Gene3D; 3.40.50.300; -; 1.
DR InterPro; IPR031575; EP400_N.
DR InterPro; IPR014001; Helicase_ATP-bd.
DR InterPro; IPR001650; Helicase_C.
DR InterPro; IPR014012; HSA_dom.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR001005; SANT/Myb.
DR InterPro; IPR038718; SNF2-like_sf.
DR InterPro; IPR000330; SNF2_N.
DR Pfam; PF15790; EP400_N; 1.
DR Pfam; PF00271; Helicase_C; 1.
DR Pfam; PF07529; HSA; 1.
DR Pfam; PF00176; SNF2-rel_dom; 1.
DR SMART; SM00487; DEXDc; 1.
DR SMART; SM00490; HELICc; 1.
DR SMART; SM00573; HSA; 1.
DR SUPFAM; SSF52540; SSF52540; 2.
DR PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR PROSITE; PS51194; HELICASE_CTER; 1.
DR PROSITE; PS51204; HSA; 1.
DR PROSITE; PS50090; MYB_LIKE; 1.
PE 1: Evidence at protein level;
KW Acetylation; Alternative splicing; ATP-binding; Chromatin regulator;
KW Direct protein sequencing; DNA-binding; Helicase; Hydrolase;
KW Nucleotide-binding; Nucleus; Phosphoprotein; Reference proteome.
FT CHAIN 1..3072
FT /note="E1A-binding protein p400"
FT /id="PRO_0000074313"
FT DOMAIN 798..870
FT /note="HSA"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00549"
FT DOMAIN 1102..1267
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT DOMAIN 1815..1972
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT DOMAIN 2276..2345
FT /note="Myb-like"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00133"
FT REGION 1..55
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 125..149
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 222..250
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 485..519
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 544..601
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 635..769
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 914..952
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 950..1364
FT /note="Interactions with RUVBL1 and RUVBL2"
FT /evidence="ECO:0000250"
FT REGION 997..1024
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1473..1503
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2033..2062
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2203..2227
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2440..2699
FT /note="Interaction with ZNF42"
FT /evidence="ECO:0000269|PubMed:12653961"
FT REGION 2441..2534
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2734..2790
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 3028..3072
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 1218..1221
FT /note="DEAD box-like"
FT COMPBIAS 1..26
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 30..47
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 125..146
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 547..586
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 639..655
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 664..742
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 751..769
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1483..1500
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2038..2053
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2203..2226
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2462..2476
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2477..2496
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2520..2534
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2737..2759
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2760..2790
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 3028..3054
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 1115..1122
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT MOD_RES 52
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 134
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 315
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 321
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 735
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q96L91"
FT MOD_RES 741
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 754
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 922
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 923
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 927
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 940
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 944
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1009
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1010
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1471
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q96L91"
FT MOD_RES 1646
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q96L91"
FT MOD_RES 1650
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q96L91"
FT MOD_RES 2265
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q96L91"
FT MOD_RES 2272
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q96L91"
FT MOD_RES 2614
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q96L91"
FT VAR_SEQ 446..482
FT /note="Missing (in isoform 2 and isoform 3)"
FT /evidence="ECO:0000303|PubMed:12653961,
FT ECO:0000303|PubMed:16141072"
FT /id="VSP_011996"
FT VAR_SEQ 513..548
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:12653961,
FT ECO:0000303|PubMed:16141072"
FT /id="VSP_011997"
FT VAR_SEQ 1764..1919
FT /note="Missing (in isoform 5)"
FT /evidence="ECO:0000303|PubMed:14621295"
FT /id="VSP_017127"
FT VAR_SEQ 2800..2806
FT /note="Missing (in isoform 4 and isoform 5)"
FT /evidence="ECO:0000303|PubMed:14621295,
FT ECO:0000303|PubMed:15489334"
FT /id="VSP_011998"
FT CONFLICT 102
FT /note="G -> S (in Ref. 3; BAC26781)"
FT /evidence="ECO:0000305"
FT CONFLICT 107
FT /note="A -> D (in Ref. 3; BAC29849)"
FT /evidence="ECO:0000305"
FT CONFLICT 163
FT /note="N -> S (in Ref. 1; BAC45253/BAC45254)"
FT /evidence="ECO:0000305"
FT CONFLICT 678..686
FT /note="TVASTRPPL -> VLCGHWLFY (in Ref. 3; BAB24439/
FT BAC26781)"
FT /evidence="ECO:0000305"
FT CONFLICT 896
FT /note="E -> G (in Ref. 3; BAC29849)"
FT /evidence="ECO:0000305"
FT CONFLICT 2249
FT /note="K -> N (in Ref. 3; BAC32913)"
FT /evidence="ECO:0000305"
FT CONFLICT 2353..2359
FT /note="SKNNRPL -> LICEANP (in Ref. 3; BAC32913)"
FT /evidence="ECO:0000305"
FT CONFLICT 2518
FT /note="T -> A (in Ref. 1; BAC45253/BAC45254 and 6;
FT AAH22153)"
FT /evidence="ECO:0000305"
FT CONFLICT 2539
FT /note="A -> V (in Ref. 1; BAC45253/BAC45254)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 3072 AA; 337180 MW; 02990AAF5FAB7CEF CRC64;
MHHGSGPQNV QHQLQRSRSF TGSEEEQPAH PNLPPSPAAP FAPSASPSAP QSPGYQIQQL
MSRSPVAGQN VNITLQNVGP VVGGNQQITL APLPLPNPTS PGFQFGAQQR RFEHGSPSYI
QVTSPMSQQV QTQSPTQPSP GPGQTLQNVR AGAPGPGLGI CSNSPTGGFV DASVLVRQIS
LSPSSGGHFV FQEAPGLTQM AQGAQVQLQH SGAPITVRER RLSQPHAQSG GTIHHLGPQS
PAAAGGTGLQ PLASPNHITT ASLPPQISSI IQGQLIQQQQ QVLQGQPMNR SLGFERTPGV
LLPGVGGPSA FGMTSPPPPT SPSRTTMPPG LSSVPLTSMG SSGMKKVPKK LEEIPPASQE
MAQMRKQCLD YHYKEMEALK EVFKEYLIEL FFLQHLQGNM MDFLAFKKKH YAPLQAYLRQ
NDLDIEEEEE EEEEEEGKSE VINDEVKVVT GKDGQTGTPV AIATQLPPNV SAAFSSQQQP
FQHQSLTGSL VVGPGSATEA DPFKRQQVMP PTEQSKRPRL EVGHPGVVFQ HPGVNAGVPL
QQLMPTVQGG MPPTPQATQL TGQKQSQQQY DPSTGPPVQN AASLHTPPPQ LPARLPPASV
PATALPSTLQ FSQQSQMVEA STQLQIPVKT QQLNAPIPAP LPSQLPAPSS QPAQPALHVP
MPGKAQMQTS QLSSQTQTVA STRPPLDSAQ PCQRSLPTSS SSSSLVPVSG SGPGPSPARS
SPVNRPSSAT NKALSPITSR SPGVAVSAPP KPQSPAQNAA SSQDGSQDKL AEQITLENQI
HQRIADLRKE GLWSLRRLPK LQEAPRPKSH WDYLLEEMQW MATDFAQERR WKLAAAKKLV
RTVARHHEEK KLREERGKKE EQSRLRRIAA TTAREIEYFW SNIEQVVEIK LQVELEEKRK
KALNLQKVSR RGKESRLKGF DTSPEHSLDL GISGRKRKAS TSLTDDEVED EEETIEEEEA
HEGLVDHHTE LTNLAKEAEL PLIDLMKLYE GAFLPNFQWP QPEPDHEESS GEEDVEDCPS
DRESRRDSVL IDSLFIMDQF KAAERMSIGK SNTKDITEVT AVAEAILPKG SARVTTAVKF
SAPSLLYGAL RDYQKIGLDW LAKLYRKNLN GILADEAGLG KTVQIIAFFA HLACNEGNWG
PHLVVMRSCN ILKWELELKR WCPGLKTLSY VGSHRELKAK RQEWTEPNNF HICITSYKQF
FRGYTAFSRV HWKCLVVDEM QRVKGMTERH WEAIFKLQSQ QRLLLIDVPL HNTFLELWTM
VHFLIPGISR PYLSFPLKAP NEENQDYYHK MVIRLHRVTQ PFILRRTKRD VEKQLTRKYE
HVLKCRLSSR QKALYEDVIL QPRTQEALKS GHFVSVLSVL TRLQRICNHP GLVEPRVPGS
SFAAGSLQYK SASLILRVLE REFWKETDLS IFDLIGLENK ITRHEAELLC KKKVTRKLME
EVFASPPPSA RPAAVKLKAS RLFQPVQYGQ KPEGRTVAFP STHPPRMANT NTSTATPQGQ
VRGRPPIATF SANPDTKGGE VVKIAQLASI AGPQSRVAQP ETPVTLQFQG NKFTLSHSQL
RQLTAGQPLQ LQGSVLQIVS APGQPYLRAP GPVVMQTVSQ AGAVHSTLGS KPPTSGPSPA
PLTPQVGVPG RVAVSAMAVG EPGLASKPAS PAAGPTQEEK SRLLKERLDQ IHFINERRCS
QAPVYGRDLL RICSLPGRRK RPLCWSLDSN FGKGPKGVNY DMSLSKSEGD LILTLSQESL
QDVLGRVACV IPPVVATPPS LWVARPPSLY SSRLRALRQC LREHTGPYHR QLQQLTALRS
LQFPELRLVQ FDSGKLEALA ILLQKLKSEG RRVLILSQMV LMLDILEMFL NFHYLTYVRI
DENANSEQRQ ELMRSFNRDR RIFCALLSTH SRATGINLVE ADTVVFYDND LNPVMDAKAQ
EWCDRIGRCK DIHIYRLVSG NSIEEKLLKN GTKDLIREVA AQGNDYSMAF LTQRTIQELF
EVYSPMDDTG FPVKAEEFVV LSQEPSVSET IAPKIARPFI EALKSIECLE EDAQRSTEEA
VPGSSSVAVS SDSDGSRYDE EPSQLEELAD FMEQLTPIEK YALNYLELFH TTTEQEKERI
SEDLVMASMK DWETRNARAL QEREARLQLE QEEAELLTYT REDAYTMEYV YEDADGQTEV
MPLWTPPTPP QDDNDIYIDS VMCLMYETTP IPEAKLPPVY VRKERKRHKT DPSAAGRKKK
QRHGEAVVPP RSLFDRATPG MLKIRREGKE QKKNLLLKQQ TPFAKPLPTY VKSSGEPAQD
SPDWLIGEDW ALLQAVKQLL ELPLNLTIVS PAHTPNWDLV SDVVNSCSRI YRSSKQCRNR
YENVIIPREE GKSKNNRPLR TSQIYAQDEN ATHTQLYTSH FELMKMTAGK RSPPIKPLLG
MNPFQKNPKH ASVLAESGIN YDKPLPPIQV ASLRAERIAK EKKALADQQK AQQPPVTQPP
PQQQQQQQQQ QQQQQQQQQP PPPPQQPPPP VPQPQAASSQ TPAGQPAVQP QPQPQVQTQP
QPVQPQSKGQ PTMTTVGSAA VLAGTIKTSV TGTSIPTGTV SGNVIVNTIA GVPAATFQSI
NKRLASPVAP GTLTTSGGSA PAQVVHTQQR AVGSPATATT DLVSMTTTQG VRAVTSVTAS
AVVTTNLTPV QTPTRSLVTQ VSQATGVQLP GKTITPAAHF QLLRQQQQQQ QQQQQQQQTS
QVQVPQLQSQ AQSPAQIKAV SKLGPEHIIK MQKQKMQLPP QPPPPQAQPG PPQQPAQVQV
QTPQPPQQQQ SPQLTTVTAP RPGALLTGTT VTNLQVARLT RVPTSQLQAQ GQMQTQTPQP
AQVALAKPPV VSVPAAVVSS PGVTTLPMNV AGISVAIGQP QKTAGQTVVA QPVNVQQLLK
YKQQTAVQQQ KAIQPQVAQG QAAVQQKLTT QQITTQGPQQ KVAYAAQPAL KTQFLTTPIS
QAQKLAGTQQ VQTQIQVAKL PQVVQQQTPV ASIQQVASAS QQASPQTVTL TQATAAGQQV
QMIPTVTATA QLVQQKLIQQ QVVTTASASL QTPGGPSPAQ LPASSDSPSQ QPKLQMRVPA
VRLKTPTKPP CQ
