TAF1_DROME
ID TAF1_DROME Reviewed; 2129 AA.
AC P51123; O97068; Q7KSX6; Q7KSX7; Q86LF7; Q9TX96;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 19-JUL-2005, sequence version 3.
DT 03-AUG-2022, entry version 202.
DE RecName: Full=Transcription initiation factor TFIID subunit 1;
DE EC=2.7.11.1;
DE AltName: Full=TAFII250;
DE AltName: Full=TBP-associated factor 230 kDa;
DE Short=p230;
DE AltName: Full=Transcription initiation factor TFIID 230 kDa subunit;
DE Short=TAFII-230;
GN Name=Taf1; Synonyms=TAF250; ORFNames=CG17603;
OS Drosophila melanogaster (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila; Sophophora.
OX NCBI_TaxID=7227;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM A), PROTEIN SEQUENCE OF 63-75 AND
RP 540-546, AND FUNCTION.
RX PubMed=8504928; DOI=10.1101/gad.7.6.1033;
RA Kokubo T., Gong D.-W., Yamashita S., Horikoshi M., Roeder R.G.,
RA Nakatani Y.;
RT "Drosophila 230-kD TFIID subunit, a functional homolog of the human cell
RT cycle gene product, negatively regulates DNA binding of the TATA box-
RT binding subunit of TFIID.";
RL Genes Dev. 7:1033-1046(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=Berkeley;
RA Celniker S.E., Pfeiffer B., Knafels J., Martin C.H., Mayeda C.A.,
RA Palazzolo M.J.;
RT "Complete sequence of the Antennapedia complex of Drosophila.";
RL Submitted (JAN-1999) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Berkeley;
RX PubMed=10731132; DOI=10.1126/science.287.5461.2185;
RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D.,
RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F.,
RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N.,
RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., Brandon R.C.,
RA Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C.,
RA Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A.,
RA An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A.,
RA Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V.,
RA Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J.,
RA Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E.,
RA Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B.,
RA Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I.,
RA Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C.,
RA Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S.,
RA Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M.,
RA Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M.,
RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D.,
RA Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F.,
RA Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D.,
RA Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A.,
RA Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C.,
RA McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C.,
RA Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L.,
RA Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R.,
RA Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V.,
RA Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F.,
RA Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J.,
RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R.,
RA Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y.,
RA Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T.,
RA Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S.,
RA Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W.,
RA Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M.,
RA Venter J.C.;
RT "The genome sequence of Drosophila melanogaster.";
RL Science 287:2185-2195(2000).
RN [4]
RP GENOME REANNOTATION, AND ALTERNATIVE SPLICING.
RC STRAIN=Berkeley;
RX PubMed=12537572; DOI=10.1186/gb-2002-3-12-research0083;
RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S.,
RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E.,
RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P.,
RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A.,
RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M.,
RA Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E.;
RT "Annotation of the Drosophila melanogaster euchromatic genome: a systematic
RT review.";
RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM A).
RC STRAIN=Berkeley; TISSUE=Embryo;
RX PubMed=12537569; DOI=10.1186/gb-2002-3-12-research0080;
RA Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., George R.A.,
RA Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., Rubin G.M.,
RA Celniker S.E.;
RT "A Drosophila full-length cDNA resource.";
RL Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002).
RN [6]
RP NUCLEOTIDE SEQUENCE OF 658-2129 (ISOFORM B), AND INTERACTION WITH TBP AND
RP TAF4.
RX PubMed=8464492; DOI=10.1038/362511a0;
RA Weinzierl R.O., Dynlacht B.D., Tjian R.;
RT "Largest subunit of Drosophila transcription factor IID directs assembly of
RT a complex containing TBP and a coactivator.";
RL Nature 362:511-517(1993).
RN [7]
RP FUNCTION, AUTOPHOSPHORYLATION, AND ATP-BINDING.
RX PubMed=8625415; DOI=10.1016/s0092-8674(00)81055-7;
RA Dikstein R., Ruppert S., Tjian R.;
RT "TAFII250 is a bipartite protein kinase that phosphorylates the base
RT transcription factor RAP74.";
RL Cell 84:781-790(1996).
RN [8]
RP INTERACTION WITH TAF6.
RC STRAIN=Oregon-R;
RX PubMed=8262073; DOI=10.1002/j.1460-2075.1993.tb06226.x;
RA Weinzierl R.O., Ruppert S., Dynlacht B.D., Tanese N., Tjian R.;
RT "Cloning and expression of Drosophila TAFII60 and human TAFII70 reveal
RT conserved interactions with other subunits of TFIID.";
RL EMBO J. 12:5303-5309(1993).
RN [9]
RP INTERACTION WITH TAF4.
RC TISSUE=Embryo;
RX PubMed=8327460; DOI=10.1073/pnas.90.13.5896;
RA Kokubo T., Gong D.-W., Roeder R.G., Horikoshi M., Nakatani Y.;
RT "The Drosophila 110-kDa transcription factor TFIID subunit directly
RT interacts with the N-terminal region of the 230-kDa subunit.";
RL Proc. Natl. Acad. Sci. U.S.A. 90:5896-5900(1993).
RN [10]
RP INTERACTION WITH TAF2.
RC TISSUE=Embryo;
RX PubMed=8178153; DOI=10.1126/science.8178153;
RA Verrijzer C.P., Yokomori K., Chen J.-L., Tjian R.;
RT "Drosophila TAFII150: similarity to yeast gene TSM-1 and specific binding
RT to core promoter DNA.";
RL Science 264:933-941(1994).
RN [11]
RP RETRACTED PAPER.
RX PubMed=15143281; DOI=10.1126/science.1095001;
RA Maile T., Kwoczynski S., Katzenberger R.J., Wassarman D.A., Sauer F.;
RT "TAF1 activates transcription by phosphorylation of serine 33 in histone
RT H2B.";
RL Science 304:1010-1014(2004).
RN [12]
RP RETRACTION NOTICE OF PUBMED:15143281.
RX PubMed=24876484; DOI=10.1126/science.344.6187.981-a;
RA McNutt M.;
RL Science 344:981-981(2014).
RN [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-286; SER-288; SER-290;
RP SER-603 AND SER-1740, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC TISSUE=Embryo;
RX PubMed=18327897; DOI=10.1021/pr700696a;
RA Zhai B., Villen J., Beausoleil S.A., Mintseris J., Gygi S.P.;
RT "Phosphoproteome analysis of Drosophila melanogaster embryos.";
RL J. Proteome Res. 7:1675-1682(2008).
RN [14]
RP STRUCTURE BY NMR OF 11-77, AND FUNCTION.
RX PubMed=9741622; DOI=10.1016/s0092-8674(00)81599-8;
RA Liu D., Ishima R., Tong K.I., Bagby S., Kokubo T., Muhandiram D.R.,
RA Kay L.E., Nakatani Y., Ikura M.;
RT "Solution structure of a TBP-TAF(II)230 complex: protein mimicry of the
RT minor groove surface of the TATA box unwound by TBP.";
RL Cell 94:573-583(1998).
CC -!- FUNCTION: TFIID is a multimeric protein complex that plays a central
CC role in mediating promoter responses to various activators and
CC repressors. Largest component and core scaffold of the complex.
CC Contains N- and C-terminal Ser/Thr kinase domains which can
CC autophosphorylate or transphosphorylate other transcription factors.
CC Possesses DNA-binding activity. Essential for progression of the G1
CC phase of the cell cycle. Negative regulator of the TATA box-binding
CC activity of Tbp. {ECO:0000269|PubMed:8504928,
CC ECO:0000269|PubMed:8625415, ECO:0000269|PubMed:9741622}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-
CC [protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-
CC COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.1;
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L-
CC threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060,
CC Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216;
CC EC=2.7.11.1;
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC -!- ACTIVITY REGULATION: Autophosphorylates on Ser residues.
CC -!- SUBUNIT: Belongs to the TFIID complex which is composed of TATA binding
CC protein (Tbp) and a number of TBP-associated factors (Tafs). Taf1 is
CC the largest component of the TFIID complex. Interacts with Tbp, Taf2,
CC Taf4 and Taf6. {ECO:0000269|PubMed:8178153, ECO:0000269|PubMed:8262073,
CC ECO:0000269|PubMed:8327460, ECO:0000269|PubMed:8464492}.
CC -!- INTERACTION:
CC P51123; P47825: Taf4; NbExp=7; IntAct=EBI-499582, EBI-277958;
CC P51123; P20227: Tbp; NbExp=3; IntAct=EBI-499582, EBI-169179;
CC -!- SUBCELLULAR LOCATION: Nucleus.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=B;
CC IsoId=P51123-1; Sequence=Displayed;
CC Name=A;
CC IsoId=P51123-2; Sequence=VSP_014794, VSP_014795;
CC Name=C;
CC IsoId=P51123-3; Sequence=VSP_014795;
CC -!- SIMILARITY: Belongs to the TAF1 family. {ECO:0000305}.
CC -!- CAUTION: The C-terminal Ser/Thr kinase domain was reported to
CC phosphorylate histone H2B at 'Ser-34'. However, the paper was retracted
CC because some data, results and conclusions in the paper are not
CC reliable. {ECO:0000305|PubMed:15143281, ECO:0000305|PubMed:24876484}.
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DR EMBL; S61883; AAB26991.2; -; mRNA.
DR EMBL; AE001572; AAD19815.1; -; Genomic_DNA.
DR EMBL; AE014297; AAF54102.3; -; Genomic_DNA.
DR EMBL; AE014297; AAS65116.1; -; Genomic_DNA.
DR EMBL; AE014297; AAS65117.1; -; Genomic_DNA.
DR EMBL; BT004888; AAO47866.1; -; mRNA.
DR PIR; A47371; A47371.
DR RefSeq; NP_476956.3; NM_057608.5. [P51123-2]
DR RefSeq; NP_996159.1; NM_206437.2. [P51123-3]
DR RefSeq; NP_996160.1; NM_206438.2. [P51123-1]
DR PDB; 1TBA; NMR; -; A=11-77.
DR PDBsum; 1TBA; -.
DR AlphaFoldDB; P51123; -.
DR BMRB; P51123; -.
DR SMR; P51123; -.
DR BioGRID; 66011; 26.
DR DIP; DIP-228N; -.
DR IntAct; P51123; 16.
DR MINT; P51123; -.
DR STRING; 7227.FBpp0293442; -.
DR iPTMnet; P51123; -.
DR PaxDb; P51123; -.
DR PRIDE; P51123; -.
DR EnsemblMetazoa; FBtr0081684; FBpp0081184; FBgn0010355. [P51123-2]
DR EnsemblMetazoa; FBtr0081685; FBpp0089369; FBgn0010355. [P51123-1]
DR EnsemblMetazoa; FBtr0081686; FBpp0089420; FBgn0010355. [P51123-3]
DR GeneID; 40813; -.
DR KEGG; dme:Dmel_CG17603; -.
DR CTD; 6872; -.
DR FlyBase; FBgn0010355; Taf1.
DR VEuPathDB; VectorBase:FBgn0010355; -.
DR eggNOG; KOG0008; Eukaryota.
DR GeneTree; ENSGT00940000155242; -.
DR InParanoid; P51123; -.
DR OMA; DSMAMQM; -.
DR PhylomeDB; P51123; -.
DR BRENDA; 2.3.1.48; 1994.
DR Reactome; R-DME-674695; RNA Polymerase II Pre-transcription Events.
DR Reactome; R-DME-6804756; Regulation of TP53 Activity through Phosphorylation.
DR Reactome; R-DME-73776; RNA Polymerase II Promoter Escape.
DR Reactome; R-DME-73779; RNA Polymerase II Transcription Pre-Initiation And Promoter Opening.
DR Reactome; R-DME-75953; RNA Polymerase II Transcription Initiation.
DR Reactome; R-DME-76042; RNA Polymerase II Transcription Initiation And Promoter Clearance.
DR SignaLink; P51123; -.
DR BioGRID-ORCS; 40813; 1 hit in 3 CRISPR screens.
DR EvolutionaryTrace; P51123; -.
DR GenomeRNAi; 40813; -.
DR PRO; PR:P51123; -.
DR Proteomes; UP000000803; Chromosome 3R.
DR Bgee; FBgn0010355; Expressed in eye disc (Drosophila) and 28 other tissues.
DR ExpressionAtlas; P51123; baseline and differential.
DR Genevisible; P51123; DM.
DR GO; GO:0005730; C:nucleolus; IDA:FlyBase.
DR GO; GO:0005654; C:nucleoplasm; IDA:FlyBase.
DR GO; GO:0005634; C:nucleus; IDA:FlyBase.
DR GO; GO:0035102; C:PRC1 complex; TAS:ParkinsonsUK-UCL.
DR GO; GO:0005669; C:transcription factor TFIID complex; IDA:FlyBase.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0010485; F:H4 histone acetyltransferase activity; IDA:FlyBase.
DR GO; GO:0036408; F:histone acetyltransferase activity (H3-K14 specific); IDA:FlyBase.
DR GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; ISS:FlyBase.
DR GO; GO:0001091; F:RNA polymerase II general transcription initiation factor binding; IEA:InterPro.
DR GO; GO:0043565; F:sequence-specific DNA binding; IDA:FlyBase.
DR GO; GO:0017025; F:TBP-class protein binding; IBA:GO_Central.
DR GO; GO:0004839; F:ubiquitin activating enzyme activity; IDA:FlyBase.
DR GO; GO:0061631; F:ubiquitin conjugating enzyme activity; IDA:FlyBase.
DR GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR GO; GO:0044154; P:histone H3-K14 acetylation; IDA:FlyBase.
DR GO; GO:0043967; P:histone H4 acetylation; IDA:FlyBase.
DR GO; GO:0010390; P:histone monoubiquitination; IDA:FlyBase.
DR GO; GO:0006468; P:protein phosphorylation; ISS:FlyBase.
DR GO; GO:0051123; P:RNA polymerase II preinitiation complex assembly; IDA:BHF-UCL.
DR GO; GO:0006367; P:transcription initiation from RNA polymerase II promoter; IDA:FlyBase.
DR DisProt; DP00081; -.
DR Gene3D; 1.10.1100.10; -; 1.
DR Gene3D; 1.20.920.10; -; 2.
DR InterPro; IPR017956; AT_hook_DNA-bd_motif.
DR InterPro; IPR001487; Bromodomain.
DR InterPro; IPR036427; Bromodomain-like_sf.
DR InterPro; IPR018359; Bromodomain_CS.
DR InterPro; IPR040240; TAF1.
DR InterPro; IPR011177; TAF1_animal.
DR InterPro; IPR022591; TAF1_HAT_dom.
DR InterPro; IPR009067; TAF_II_230-bd.
DR InterPro; IPR036741; TAFII-230_TBP-bd_sf.
DR InterPro; IPR041670; Znf-CCHC_6.
DR PANTHER; PTHR13900; PTHR13900; 2.
DR Pfam; PF00439; Bromodomain; 2.
DR Pfam; PF12157; DUF3591; 1.
DR Pfam; PF09247; TBP-binding; 1.
DR Pfam; PF15288; zf-CCHC_6; 1.
DR PIRSF; PIRSF003047; TAF1_animal; 1.
DR PRINTS; PR00503; BROMODOMAIN.
DR SMART; SM00384; AT_hook; 2.
DR SMART; SM00297; BROMO; 2.
DR SUPFAM; SSF47055; SSF47055; 1.
DR SUPFAM; SSF47370; SSF47370; 2.
DR PROSITE; PS00633; BROMODOMAIN_1; 2.
DR PROSITE; PS50014; BROMODOMAIN_2; 2.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; ATP-binding; Bromodomain; Cell cycle;
KW Direct protein sequencing; DNA-binding; Kinase; Nucleotide-binding;
KW Nucleus; Phosphoprotein; Reference proteome; Repeat;
KW Serine/threonine-protein kinase; Transcription; Transcription regulation;
KW Transferase.
FT CHAIN 1..2129
FT /note="Transcription initiation factor TFIID subunit 1"
FT /id="PRO_0000211216"
FT DOMAIN 1..423
FT /note="Protein kinase 1"
FT DOMAIN 1487..1557
FT /note="Bromo 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00035"
FT DOMAIN 1515..2065
FT /note="Protein kinase 2"
FT DOMAIN 1609..1679
FT /note="Bromo 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00035"
FT REGION 77..233
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 246..348
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 377..405
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 445..497
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1016..1038
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1149..1208
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1296..1336
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1368..1391
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1415..1435
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1710..1872
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1973..1992
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2018..2042
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2101..2129
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 1442..1448
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000255"
FT COMPBIAS 107..145
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 153..169
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 201..218
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 261..275
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 313..346
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 445..489
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1160..1180
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1316..1336
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1368..1382
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1710..1730
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1753..1767
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1790..1823
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1824..1838
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1840..1860
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1973..1991
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 286
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 288
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 290
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 315
FT /note="Phosphoserine; by autocatalysis"
FT /evidence="ECO:0000250"
FT MOD_RES 603
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 1740
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT VAR_SEQ 1805..1837
FT /note="Missing (in isoform A)"
FT /evidence="ECO:0000303|PubMed:12537569,
FT ECO:0000303|PubMed:8504928"
FT /id="VSP_014794"
FT VAR_SEQ 1904..1934
FT /note="Missing (in isoform A and isoform C)"
FT /evidence="ECO:0000303|PubMed:12537569,
FT ECO:0000303|PubMed:8504928"
FT /id="VSP_014795"
FT VARIANT 572
FT /note="P -> S"
FT CONFLICT 98
FT /note="E -> G (in Ref. 1; AAB26991)"
FT /evidence="ECO:0000305"
FT CONFLICT 113
FT /note="E -> EERE (in Ref. 1; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 169
FT /note="E -> D (in Ref. 5; AAO47866)"
FT /evidence="ECO:0000305"
FT CONFLICT 267..268
FT /note="KR -> QS (in Ref. 1; AAB26991)"
FT /evidence="ECO:0000305"
FT CONFLICT 361
FT /note="M -> I (in Ref. 1; AAB26991)"
FT /evidence="ECO:0000305"
FT CONFLICT 386
FT /note="P -> Q (in Ref. 1; AAB26991)"
FT /evidence="ECO:0000305"
FT CONFLICT 656..657
FT /note="KL -> NV (in Ref. 1; AAB26991)"
FT /evidence="ECO:0000305"
FT CONFLICT 670..671
FT /note="HG -> QR (in Ref. 6)"
FT /evidence="ECO:0000305"
FT CONFLICT 762
FT /note="F -> Y (in Ref. 1; AAB26991)"
FT /evidence="ECO:0000305"
FT CONFLICT 932
FT /note="A -> G (in Ref. 6)"
FT /evidence="ECO:0000305"
FT CONFLICT 966
FT /note="L -> M (in Ref. 6)"
FT /evidence="ECO:0000305"
FT CONFLICT 1088
FT /note="M -> I (in Ref. 5; AAO47866)"
FT /evidence="ECO:0000305"
FT CONFLICT 1420
FT /note="D -> G (in Ref. 6)"
FT /evidence="ECO:0000305"
FT CONFLICT 1437
FT /note="P -> G (in Ref. 6)"
FT /evidence="ECO:0000305"
FT CONFLICT 1462
FT /note="K -> E (in Ref. 5; AAO47866)"
FT /evidence="ECO:0000305"
FT CONFLICT 1472
FT /note="V -> G (in Ref. 6)"
FT /evidence="ECO:0000305"
FT CONFLICT 1487
FT /note="R -> G (in Ref. 6)"
FT /evidence="ECO:0000305"
FT CONFLICT 1525..1526
FT /note="RQ -> AKGGTRVARC (in Ref. 6)"
FT /evidence="ECO:0000305"
FT CONFLICT 1534
FT /note="M -> N (in Ref. 6)"
FT /evidence="ECO:0000305"
FT CONFLICT 1611
FT /note="L -> LG (in Ref. 6)"
FT /evidence="ECO:0000305"
FT CONFLICT 1680
FT /note="K -> E (in Ref. 5; AAO47866)"
FT /evidence="ECO:0000305"
FT CONFLICT 1685
FT /note="I -> IRYTKFSKKI (in Ref. 6)"
FT /evidence="ECO:0000305"
FT CONFLICT 2072
FT /note="V -> G (in Ref. 6)"
FT /evidence="ECO:0000305"
FT HELIX 23..26
FT /evidence="ECO:0007829|PDB:1TBA"
FT TURN 30..32
FT /evidence="ECO:0007829|PDB:1TBA"
FT STRAND 42..44
FT /evidence="ECO:0007829|PDB:1TBA"
FT TURN 50..52
FT /evidence="ECO:0007829|PDB:1TBA"
FT HELIX 53..56
FT /evidence="ECO:0007829|PDB:1TBA"
FT TURN 60..62
FT /evidence="ECO:0007829|PDB:1TBA"
FT HELIX 64..69
FT /evidence="ECO:0007829|PDB:1TBA"
SQ SEQUENCE 2129 AA; 239315 MW; 6BF505E5A3EFF160 CRC64;
MEMESDNSDD EGSIGNGLDL TGILFGNIDS EGRLLQDDDG EGRGGTGFDA ELRENIGSLS
KLGLDSMLLE VIDLKEAEPP SDDEEEEDAR PSAVSASEGM SAFDALKAGV KREDGAVKAQ
DDAIDYSDIT ELSEDCPRTP PEETSTYDDL EDAIPASKVE AKLTKDDKEL MPPPSAPMRS
GSGGGIEEPA KSNDASSPSD DSKSTDSKDA DRKLDTPLAD ILPSKYQNVD VRELFPDFRP
QKVLRFSRLF GPGKPTSLPQ IWRHVRKRRR KRNQSRDQKT TNTGGSDSPS DTEEPRKRGF
SLHYAAEPTP AECMSDDEDK LLGDFNSEDV RPEGPDNGEN SDQKPKVADW RFGPAQIWYD
MLEVPDSGEG FNYGFKTKAA STSSQPQLKD ERRVKSPEDD VEDPSIADDA FLMVSQLHWE
DDVVWDGNDI KAKVLQKLNS KTNAAGWLPS SGSRTAGAFS QPGKPSMPVG SGSSKQGSGA
SSKKAQQNAQ AKPAEAPDDT WYSLFPVENE ELIYYKWEDE VIWDAQQVSK VPKPKVLTLD
PNDENIILGI PDDIDPSKIN KSTGPPPKIK IPHPHVKKSK ILLGKAGVIN VLAEDTPPPP
PKSPDRDPFN ISNDTYYTPK TEPTLRLKVG GNLIQHSTPV VELRAPFVPT HMGPMKLRAF
HRPPLKKYSH GPMAQSIPHP VFPLLKTIAK KAKQREVERI ASGGGDVFFM RNPEDLSGRD
GDIVLAEFCE EHPPLINQVG MCSKIKNYYK RKAEKDSGPQ DFVYGEVAFA HTSPFLGILH
PGQCIQAIEN NMYRAPIYPH KMAHNDFLVI RTRNNYWIRS VNSIYTVGQE CPLYEVPGPN
SKRANNFTRD FLQVFIYRLF WKSRDNPRRI RMDDIKQAFP AHSESSIRKR LKQCADFKRT
GMDSNWWVIK PEFRLPSEEE IRAMVSPEQC CAYFSMIAAE QRLKDAGYGE KFLFAPQEDD
DEEAQLKLDD EVKVAPWNTT RAYIQAMRGK CLLQLSGPAD PTGCGEGFSY VRVPNKPTQT
KEEQESQPKR SVTGTDADLR RLPLQRAKEL LRQFKVPEEE IKKLSRWEVI DVVRTLSTEK
AKAGEEGMDK FSRGNRFSIA EHQERYKEEC QRIFDLQNRV LASSEVLSTD EAESSASEES
DLEELGKNLE NMLSNKKTST QLSREREELE RQELLRQLDE EHGGPSGSGG AKGAKGKDDP
GQQMLATNNQ GRILRITRTF RGNDGKEYTR VETVRRQPVI DAYIKIRTTK DEQFIKQFAT
LDEQQKEEMK REKRRIQEQL RRIKRNQERE RLAQLAQNQK LQPGGMPTSL GDPKSSGGHS
HKERDSGYKE VSPSRKKFKL KPDLKLKCGA CGQVGHMRTN KACPLYSGMQ SSLSQSNPSL
ADDFDEQSEK EMTMDDDDLV NVDGTKVTLS SKILKRHGGD DGKRRSGSSS GFTLKVPRDA
MGKKKRRVGG DLHCDYLQRH NKTANRRRTD PVVVLSSILE IIHNELRSMP DVSPFLFPVS
AKKVPDYYRV VTKPMDLQTM REYIRQRRYT SREMFLEDLK QIVDNSLIYN GPQSAYTLAA
QRMFSSCFEL LAEREDKLMR LEKAINPLLD DDDQVALSFI FDKLHSQIKQ LPESWPFLKP
VNKKQVKDYY TVIKRPMDLE TIGKNIEAHR YHSRAEYLAD IELIATNCEQ YNGSDTRYTK
FSKKILEYAQ TQLIEFSEHC GQLENNIAKT QERARENAPE FDEAWGNDDY NFDRGSRASS
PGDDYIDVEG HGGHASSSNS IHRSMGAEAG SSHTAPAVRK PAPPGPGEVK RGRGRPRKQR
DPVEEVKSQN PVKRGRGRPR KDSLASNMSH TQAYFLDEDL QCSTDDEDDD EEEDFQEVSE
DENNAASILD QGERINAPAD AMDGMFDPKN IKTEIDLEAH QMAEEPIGED DSQQVAEAMV
QLSGVGGYYA QQQQDESMDV DPNYDPSDFL AMHKQRQSLG EPSSLQGAFT NFLSHEQDDN
GPYNPAEAST SAASGADLGM DASMAMQMAP EMPVNTMNNG MGIDDDLDIS ESDEEDDGSR
VRIKKEVFDD GDYALQHQQM GQAASQSQIY MVDSSNEPTT LDYQQPPQLD FQQVQEMEQL
QHQVMPPMQS EQLQQQQTPQ GDNDYAWTF
