CCA1_ARATH
ID CCA1_ARATH Reviewed; 608 AA.
AC P92973; Q8S8N5;
DT 24-NOV-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1997, sequence version 1.
DT 03-AUG-2022, entry version 162.
DE RecName: Full=Protein CCA1 {ECO:0000303|PubMed:9144958};
DE AltName: Full=MYB-related transcription factor CCA1 {ECO:0000303|PubMed:9144958};
DE AltName: Full=Protein CIRCADIAN CLOCK ASSOCIATED 1 {ECO:0000303|PubMed:9144958};
GN Name=CCA1 {ECO:0000303|PubMed:9144958};
GN OrderedLocusNames=At2g46830 {ECO:0000312|Araport:AT2G46830};
GN ORFNames=F19D11 {ECO:0000312|EMBL:AAC33507.1};
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 [GENOMIC DNA / MRNA] (ISOFORM 1), SUBCELLULAR LOCATION,
RP INDUCTION BY LIGHT, AND DNA-BINDING.
RC STRAIN=cv. Columbia;
RX PubMed=9144958; DOI=10.2307/3870502;
RA Wang Z.-Y., Kenigsbuch D., Sun L., Harel E., Ong M.S., Tobin E.M.;
RT "A Myb-related transcription factor is involved in the phytochrome
RT regulation of an Arabidopsis Lhcb gene.";
RL Plant Cell 9:491-507(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND GENE FAMILY.
RX PubMed=16463103; DOI=10.1007/s11103-005-2910-y;
RA Chen Y., Yang X., He K., Liu M., Li J., Gao Z., Lin Z., Zhang Y., Wang X.,
RA Qiu X., Shen Y., Zhang L., Deng X., Luo J., Deng X.-W., Chen Z., Gu H.,
RA Qu L.-J.;
RT "The MYB transcription factor superfamily of Arabidopsis: expression
RT analysis and phylogenetic comparison with the rice MYB family.";
RL Plant Mol. Biol. 60:107-124(2006).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10617197; DOI=10.1038/45471;
RA Lin X., Kaul S., Rounsley S.D., Shea T.P., Benito M.-I., Town C.D.,
RA Fujii C.Y., Mason T.M., Bowman C.L., Barnstead M.E., Feldblyum T.V.,
RA Buell C.R., Ketchum K.A., Lee J.J., Ronning C.M., Koo H.L., Moffat K.S.,
RA Cronin L.A., Shen M., Pai G., Van Aken S., Umayam L., Tallon L.J.,
RA Gill J.E., Adams M.D., Carrera A.J., Creasy T.H., Goodman H.M.,
RA Somerville C.R., Copenhaver G.P., Preuss D., Nierman W.C., White O.,
RA Eisen J.A., Salzberg S.L., Fraser C.M., Venter J.C.;
RT "Sequence and analysis of chromosome 2 of the plant Arabidopsis thaliana.";
RL Nature 402:761-768(1999).
RN [4]
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
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 [6]
RP FUNCTION, AND INDUCTION.
RX PubMed=9657153; DOI=10.1016/s0092-8674(00)81464-6;
RA Wang Z.-Y., Tobin E.M.;
RT "Constitutive expression of the CIRCADIAN CLOCK ASSOCIATED 1 (CCA1) gene
RT disrupts circadian rhythms and suppresses its own expression.";
RL Cell 93:1207-1217(1998).
RN [7]
RP INTERACTION WITH CKB1; CKB2 AND CKB3, AND PHOSPHORYLATION.
RX PubMed=9724822; DOI=10.1073/pnas.95.18.11020;
RA Sugano S., Andronis C., Green R.M., Wang Z.-Y., Tobin E.M.;
RT "Protein kinase CK2 interacts with and phosphorylates the Arabidopsis
RT circadian clock-associated 1 protein.";
RL Proc. Natl. Acad. Sci. U.S.A. 95:11020-11025(1998).
RN [8]
RP DISRUPTION PHENOTYPE.
RX PubMed=10097183; DOI=10.1073/pnas.96.7.4176;
RA Green R.M., Tobin E.M.;
RT "Loss of the circadian clock-associated protein 1 in Arabidopsis results in
RT altered clock-regulated gene expression.";
RL Proc. Natl. Acad. Sci. U.S.A. 96:4176-4179(1999).
RN [9]
RP FUNCTION, AND DNA-BINDING.
RX PubMed=11486091; DOI=10.1126/science.1061320;
RA Alabadi D., Oyama T., Yanovsky M.J., Harmon F.G., Mas P., Kay S.A.;
RT "Reciprocal regulation between TOC1 and LHY/CCA1 within the Arabidopsis
RT circadian clock.";
RL Science 293:880-883(2001).
RN [10]
RP FUNCTION.
RX PubMed=12007421; DOI=10.1016/s0960-9822(02)00815-1;
RA Alabadi D., Yanovsky M.J., Mas P., Harmer S.L., Kay S.A.;
RT "Critical role for CCA1 and LHY in maintaining circadian rhythmicity in
RT Arabidopsis.";
RL Curr. Biol. 12:757-761(2002).
RN [11]
RP FUNCTION.
RX PubMed=12015970; DOI=10.1016/s1534-5807(02)00170-3;
RA Mizoguchi T., Wheatley K., Hanzawa Y., Wright L., Mizoguchi M., Song H.-R.,
RA Carre I.A., Coupland G.;
RT "LHY and CCA1 are partially redundant genes required to maintain circadian
RT rhythms in Arabidopsis.";
RL Dev. Cell 2:629-641(2002).
RN [12]
RP INTERACTION WITH CKB3, MUTAGENESIS OF SER-5; SER-6; SER-431; SER-432;
RP SER-433 AND SER-484, AND PHOSPHORYLATION AT SER-5 AND SER-6.
RX PubMed=14978263; DOI=10.1073/pnas.0400163101;
RA Daniel X., Sugano S., Tobin E.M.;
RT "CK2 phosphorylation of CCA1 is necessary for its circadian oscillator
RT function in Arabidopsis.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:3292-3297(2004).
RN [13]
RP INDUCTION BY LIGHT.
RX PubMed=17873091; DOI=10.1104/pp.107.103812;
RA Yakir E., Hilman D., Hassidim M., Green R.M.;
RT "CIRCADIAN CLOCK ASSOCIATED1 transcript stability and the entrainment of
RT the circadian clock in Arabidopsis.";
RL Plant Physiol. 145:925-932(2007).
RN [14]
RP FUNCTION, TISSUE SPECIFICITY, AND INDUCTION.
RX PubMed=19095940; DOI=10.1126/science.1161403;
RA James A.B., Monreal J.A., Nimmo G.A., Kelly C.L., Herzyk P., Jenkins G.I.,
RA Nimmo H.G.;
RT "The circadian clock in Arabidopsis roots is a simplified slave version of
RT the clock in shoots.";
RL Science 322:1832-1835(2008).
RN [15]
RP FUNCTION, INDUCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, SUBUNIT,
RP INTERACTION WITH LHY, AND DISRUPTION PHENOTYPE.
RX PubMed=19218364; DOI=10.1104/pp.108.133272;
RA Lu S.X., Knowles S.M., Andronis C., Ong M.S., Tobin E.M.;
RT "CIRCADIAN CLOCK ASSOCIATED1 and LATE ELONGATED HYPOCOTYL function
RT synergistically in the circadian clock of Arabidopsis.";
RL Plant Physiol. 150:834-843(2009).
RN [16]
RP FUNCTION, SUBCELLULAR LOCATION, SUBUNIT, AND INTERACTION WITH LHY.
RX PubMed=19339503; DOI=10.1104/pp.109.137414;
RA Yakir E., Hilman D., Kron I., Hassidim M., Melamed-Book N., Green R.M.;
RT "Posttranslational regulation of CIRCADIAN CLOCK ASSOCIATED1 in the
RT circadian oscillator of Arabidopsis.";
RL Plant Physiol. 150:844-857(2009).
RN [17]
RP INDUCTION.
RX PubMed=19286557; DOI=10.1126/science.1167206;
RA Pruneda-Paz J.L., Breton G., Para A., Kay S.A.;
RT "A functional genomics approach reveals CHE as a component of the
RT Arabidopsis circadian clock.";
RL Science 323:1481-1485(2009).
RN [18]
RP INDUCTION.
RX PubMed=20233950; DOI=10.1105/tpc.109.072892;
RA Nakamichi N., Kiba T., Henriques R., Mizuno T., Chua N.H., Sakakibara H.;
RT "PSEUDO-RESPONSE REGULATORS 9, 7, and 5 are transcriptional repressors in
RT the Arabidopsis circadian clock.";
RL Plant Cell 22:594-605(2010).
RN [19]
RP INTERACTION WITH LNK1 AND LNK2.
RX PubMed=25012192; DOI=10.1105/tpc.114.126573;
RA Xie Q., Wang P., Liu X., Yuan L., Wang L., Zhang C., Li Y., Xing H.,
RA Zhi L., Yue Z., Zhao C., McClung C.R., Xu X.;
RT "LNK1 and LNK2 are transcriptional coactivators in the Arabidopsis
RT circadian oscillator.";
RL Plant Cell 26:2843-2857(2014).
RN [20]
RP FUNCTION, DISRUPTION PHENOTYPE, AND INDUCTION BY BHLH80/FBH1.
RC STRAIN=cv. Columbia, and cv. Wassilewskija;
RX PubMed=25246594; DOI=10.1073/pnas.1416666111;
RA Nagel D.H., Pruneda-Paz J.L., Kay S.A.;
RT "FBH1 affects warm temperature responses in the Arabidopsis circadian
RT clock.";
RL Proc. Natl. Acad. Sci. U.S.A. 111:14595-14600(2014).
RN [21]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RC STRAIN=cv. Columbia;
RX PubMed=31429787; DOI=10.1186/s13059-019-1777-1;
RA Song Q., Huang T.-Y., Yu H.H., Ando A., Mas P., Ha M., Chen Z.J.;
RT "Diurnal regulation of SDG2 and JMJ14 by circadian clock oscillators
RT orchestrates histone modification rhythms in Arabidopsis.";
RL Genome Biol. 20:RESEARCH170.1-RESEARCH170.12(2019).
CC -!- FUNCTION: Transcription factor involved in the circadian clock and in
CC the phytochrome regulation. Binds to the promoter regions of APRR1/TOC1
CC and TCP21/CHE to repress their transcription. Binds to the promoter
CC regions of CAB2A and CAB2B to promote their transcription. Represses
CC both LHY and itself. Recognizes the promoter of JMJ14 to regulates its
CC expression during the night in a circadian manner (PubMed:31429787).
CC Binds to the promoter of BHLH80/FBH1 and regulates its expression in
CC response to warm temperature, thus contributing to temperature
CC compensation of the circadian clock (PubMed:25246594).
CC {ECO:0000269|PubMed:11486091, ECO:0000269|PubMed:12007421,
CC ECO:0000269|PubMed:12015970, ECO:0000269|PubMed:19095940,
CC ECO:0000269|PubMed:19218364, ECO:0000269|PubMed:19339503,
CC ECO:0000269|PubMed:25246594, ECO:0000269|PubMed:31429787,
CC ECO:0000269|PubMed:9657153}.
CC -!- SUBUNIT: Homodimer or heterodimer with LHY. Interacts with LHY;
CC independently of photoperiod. Probably part of a large complex.
CC Interacts with CKB1, CKB2 and CKB3. Interacts with LNK1 and LNK2
CC (PubMed:25012192). {ECO:0000269|PubMed:14978263,
CC ECO:0000269|PubMed:19218364, ECO:0000269|PubMed:19339503,
CC ECO:0000269|PubMed:25012192, ECO:0000269|PubMed:9724822}.
CC -!- INTERACTION:
CC P92973; Q08467: CKA1; NbExp=4; IntAct=EBI-1644880, EBI-1644972;
CC P92973; P40228: CKB1; NbExp=3; IntAct=EBI-1644880, EBI-1644917;
CC P92973; O81275: CKB3; NbExp=6; IntAct=EBI-1644880, EBI-1644873;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00625,
CC ECO:0000269|PubMed:19218364, ECO:0000269|PubMed:19339503,
CC ECO:0000269|PubMed:9144958}. Note=Moves into the nucleus very soo after
CC translation. This translocation is unaffected by light and dark.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=P92973-1; Sequence=Displayed;
CC Name=2;
CC IsoId=P92973-2; Sequence=VSP_038391;
CC -!- TISSUE SPECIFICITY: Expressed in leaves, roots, stems, flowers and
CC siliques. {ECO:0000269|PubMed:19095940, ECO:0000269|PubMed:19218364}.
CC -!- INDUCTION: Circadian-regulation with peak levels occurring around 1
CC hour after dawn. Up-regulated by APRR1/TOC1 and transiently by light
CC treatment. Down-regulated by APRR5, APRR7 and APRR9. The CCA1 mRNA is
CC relatively stable in the dark and in far-red light but has a short
CC half-life in red and blue light. Modulated by BHLH80/FBH1 via direct
CC negative promoter regulation in response to warm temperature (at 28
CC degrees Celsius) (PubMed:25246594). {ECO:0000269|PubMed:17873091,
CC ECO:0000269|PubMed:19095940, ECO:0000269|PubMed:19218364,
CC ECO:0000269|PubMed:19286557, ECO:0000269|PubMed:20233950,
CC ECO:0000269|PubMed:25246594, ECO:0000269|PubMed:9144958,
CC ECO:0000269|PubMed:9657153}.
CC -!- DOMAIN: The N-terminal part (11-82) is essential for DNA binding, an
CC internal domain (136-316) is important for homodimerization and for
CC interaction with LHY and the C-terminal part (317-608) is necessary for
CC interaction with CKB3.
CC -!- PTM: Phosphorylated at Ser-5, Ser-6, and at least at one of the
CC position Ser-431, Ser-432, Ser-433 or Ser-484. Phosphorylation is
CC involved in dimerization and is necessary for binding to promoters and
CC regulation of the circadian clock. {ECO:0000269|PubMed:14978263,
CC ECO:0000269|PubMed:9724822}.
CC -!- DISRUPTION PHENOTYPE: Altered phytochrome regulation and shorter
CC circadian oscillations (PubMed:10097183, PubMed:19218364). Abnormal
CC pace and rhythmicity of the circadian clock (PubMed:25246594). The
CC double mutant cca1 lhy accumulates higher levels of JMJ14 but lower
CC levels of ATXR3/SDG2, and exhibits damped H3K4me3 levels near the
CC transcription start sites of genic regions (PubMed:31429787).
CC {ECO:0000269|PubMed:10097183, ECO:0000269|PubMed:19218364,
CC ECO:0000269|PubMed:25246594, ECO:0000269|PubMed:31429787}.
CC -!- MISCELLANEOUS: CCA1 and LHY are only partially redundant, but they bind
CC to the same region of the promoters.
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DR EMBL; U28422; AAB40525.1; -; mRNA.
DR EMBL; U79156; AAC98813.1; -; Genomic_DNA.
DR EMBL; AY519511; AAS09981.1; -; mRNA.
DR EMBL; AC005310; AAC33507.1; -; Genomic_DNA.
DR EMBL; AC005310; AAM15022.1; -; Genomic_DNA.
DR EMBL; CP002685; AEC10760.1; -; Genomic_DNA.
DR EMBL; CP002685; AEC10761.1; -; Genomic_DNA.
DR EMBL; CP002685; ANM61754.1; -; Genomic_DNA.
DR EMBL; BT001096; AAN61004.1; -; mRNA.
DR EMBL; BT001105; AAN64169.1; -; mRNA.
DR PIR; T02684; T02684.
DR RefSeq; NP_001318437.1; NM_001337221.1. [P92973-2]
DR RefSeq; NP_850460.1; NM_180129.4. [P92973-1]
DR RefSeq; NP_850461.1; NM_180130.2. [P92973-2]
DR AlphaFoldDB; P92973; -.
DR SMR; P92973; -.
DR BioGRID; 4631; 24.
DR IntAct; P92973; 10.
DR STRING; 3702.AT2G46830.1; -.
DR iPTMnet; P92973; -.
DR PaxDb; P92973; -.
DR PRIDE; P92973; -.
DR ProteomicsDB; 239154; -. [P92973-1]
DR EnsemblPlants; AT2G46830.1; AT2G46830.1; AT2G46830. [P92973-1]
DR EnsemblPlants; AT2G46830.2; AT2G46830.2; AT2G46830. [P92973-2]
DR EnsemblPlants; AT2G46830.3; AT2G46830.3; AT2G46830. [P92973-2]
DR GeneID; 819296; -.
DR Gramene; AT2G46830.1; AT2G46830.1; AT2G46830. [P92973-1]
DR Gramene; AT2G46830.2; AT2G46830.2; AT2G46830. [P92973-2]
DR Gramene; AT2G46830.3; AT2G46830.3; AT2G46830. [P92973-2]
DR KEGG; ath:AT2G46830; -.
DR Araport; AT2G46830; -.
DR TAIR; locus:2044345; AT2G46830.
DR eggNOG; KOG0724; Eukaryota.
DR HOGENOM; CLU_025358_0_0_1; -.
DR InParanoid; P92973; -.
DR OMA; ICTDEMQ; -.
DR PhylomeDB; P92973; -.
DR PRO; PR:P92973; -.
DR Proteomes; UP000006548; Chromosome 2.
DR ExpressionAtlas; P92973; baseline and differential.
DR Genevisible; P92973; AT.
DR GO; GO:0005634; C:nucleus; IDA:TAIR.
DR GO; GO:0000987; F:cis-regulatory region sequence-specific DNA binding; IDA:UniProtKB.
DR GO; GO:0003677; F:DNA binding; IDA:TAIR.
DR GO; GO:0003700; F:DNA-binding transcription factor activity; ISS:TAIR.
DR GO; GO:0043565; F:sequence-specific DNA binding; IDA:TAIR.
DR GO; GO:0007623; P:circadian rhythm; IMP:UniProtKB.
DR GO; GO:0048574; P:long-day photoperiodism, flowering; IGI:TAIR.
DR GO; GO:0042754; P:negative regulation of circadian rhythm; IMP:TAIR.
DR GO; GO:0045892; P:negative regulation of transcription, DNA-templated; IMP:TAIR.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IMP:TAIR.
DR GO; GO:0010468; P:regulation of gene expression; IMP:TAIR.
DR GO; GO:0043254; P:regulation of protein-containing complex assembly; IMP:TAIR.
DR GO; GO:0009409; P:response to cold; IGI:TAIR.
DR GO; GO:0009408; P:response to heat; IEP:UniProtKB.
DR GO; GO:0010243; P:response to organonitrogen compound; IEP:TAIR.
DR GO; GO:0010378; P:temperature compensation of the circadian clock; IMP:UniProtKB.
DR CDD; cd00167; SANT; 1.
DR InterPro; IPR009057; Homeobox-like_sf.
DR InterPro; IPR017930; Myb_dom.
DR InterPro; IPR006447; Myb_dom_plants.
DR InterPro; IPR001005; SANT/Myb.
DR InterPro; IPR017884; SANT_dom.
DR Pfam; PF00249; Myb_DNA-binding; 1.
DR SMART; SM00717; SANT; 1.
DR SUPFAM; SSF46689; SSF46689; 1.
DR TIGRFAMs; TIGR01557; myb_SHAQKYF; 1.
DR PROSITE; PS51294; HTH_MYB; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Biological rhythms; DNA-binding; Nucleus;
KW Phosphoprotein; Reference proteome; Transcription;
KW Transcription regulation.
FT CHAIN 1..608
FT /note="Protein CCA1"
FT /id="PRO_0000388997"
FT DOMAIN 19..73
FT /note="HTH myb-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00625"
FT DNA_BIND 46..69
FT /note="H-T-H motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00625"
FT REGION 86..152
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 188..225
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 238..260
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 362..483
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 105..123
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 127..152
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 368..394
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 421..435
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 436..460
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 461..483
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 5
FT /note="Phosphoserine; by CK2"
FT /evidence="ECO:0000269|PubMed:14978263"
FT MOD_RES 6
FT /note="Phosphoserine; by CK2"
FT /evidence="ECO:0000269|PubMed:14978263"
FT VAR_SEQ 1..82
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14593172"
FT /id="VSP_038391"
FT MUTAGEN 5
FT /note="S->A: No effect on CKB3 binding, but loss of DNA
FT binding; when associated with A-6; A-431; A-432; A-433 and
FT A-484."
FT /evidence="ECO:0000269|PubMed:14978263"
FT MUTAGEN 6
FT /note="S->A: No effect on CKB3 binding, but loss of DNA
FT binding; when associated with A-5; A-431; A-432; A-433 and
FT A-484."
FT /evidence="ECO:0000269|PubMed:14978263"
FT MUTAGEN 431
FT /note="S->A: No effect on CKB3 binding; but loss of DNA
FT binding; when associated with A-5; A-6; A-432; A-433 and A-
FT 484."
FT /evidence="ECO:0000269|PubMed:14978263"
FT MUTAGEN 432
FT /note="S->A: No effect on CKB3 binding, but loss of DNA
FT binding; when associated with A-5; A-6; A-431; A-433 and A-
FT 484."
FT /evidence="ECO:0000269|PubMed:14978263"
FT MUTAGEN 433
FT /note="S->A: No effect on CKB3 binding, but loss of DNA
FT binding; when associated with A-5; A-6; A-431; A-432 and A-
FT 484."
FT /evidence="ECO:0000269|PubMed:14978263"
FT MUTAGEN 484
FT /note="S->A: No effect on CKB3 binding, but loss of DNA
FT binding; when associated with A-5; A-6; A-431; A-432 and A-
FT 433."
FT /evidence="ECO:0000269|PubMed:14978263"
SQ SEQUENCE 608 AA; 66976 MW; 083C963EE6DD53A6 CRC64;
METNSSGEDL VIKTRKPYTI TKQRERWTEE EHNRFIEALR LYGRAWQKIE EHVATKTAVQ
IRSHAQKFFS KVEKEAEAKG VAMGQALDIA IPPPRPKRKP NNPYPRKTGS GTILMSKTGV
NDGKESLGSE KVSHPEMANE DRQQSKPEEK TLQEDNCSDC FTHQYLSAAS SMNKSCIETS
NASTFREFLP SREEGSQNNR VRKESNSDLN AKSLENGNEQ GPQTYPMHIP VLVPLGSSIT
SSLSHPPSEP DSHPHTVAGD YQSFPNHIMS TLLQTPALYT AATFASSFWP PDSSGGSPVP
GNSPPNLAAM AAATVAAASA WWAANGLLPL CAPLSSGGFT SHPPSTFGPS CDVEYTKAST
LQHGSVQSRE QEHSEASKAR SSLDSEDVEN KSKPVCHEQP SATPESDAKG SDGAGDRKQV
DRSSCGSNTP SSSDDVEADA SERQEDGTNG EVKETNEDTN KPQTSESNAR RSRISSNITD
PWKSVSDEGR IAFQALFSRE VLPQSFTYRE EHREEEQQQQ EQRYPMALDL NFTAQLTPVD
DQEEKRNTGF LGIGLDASKL MSRGRTGFKP YKRCSMEAKE SRILNNNPII HVEQKDPKRM
RLETQAST
