TLE1_MOUSE
ID TLE1_MOUSE Reviewed; 770 AA.
AC Q62440; Q5SQA8;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 25-MAR-2003, sequence version 2.
DT 03-AUG-2022, entry version 190.
DE RecName: Full=Transducin-like enhancer protein 1;
DE AltName: Full=Groucho-related protein 1;
DE Short=Grg-1;
GN Name=Tle1; Synonyms=Grg1;
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] (ISOFORM 1).
RX PubMed=8892234; DOI=10.1016/0925-4773(96)00582-5;
RA Koop K.E., Macdonald L.M., Lobe C.G.;
RT "Transcripts of Grg4, a murine groucho-related gene, are detected in
RT adjacent tissues to other murine neurogenic gene homologues during
RT embryonic development.";
RL Mech. Dev. 59:73-87(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1; 2; 3; 6 AND 8), PARTIAL NUCLEOTIDE
RP SEQUENCE [MRNA] (ISOFORM 4), SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RC STRAIN=C57BL/6J, and ICR; TISSUE=Fetal intestine;
RX PubMed=12359720; DOI=10.1074/jbc.m208154200;
RA Lepourcelet M., Shivdasani R.A.;
RT "Characterization of a novel mammalian groucho isoform and its role in
RT transcriptional regulation.";
RL J. Biol. Chem. 277:47732-47740(2002).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 5 AND 7).
RC STRAIN=C57BL/6J; TISSUE=Cerebellum;
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 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 [5]
RP SUBCELLULAR LOCATION, AND PHOSPHORYLATION.
RX PubMed=8713081; DOI=10.1042/bj3170523;
RA Husain J., Lo R., Grbavec D., Stifani S.;
RT "Affinity for the nuclear compartment and expression during cell
RT differentiation implicate phosphorylated Groucho/TLE1 forms of higher
RT molecular mass in nuclear functions.";
RL Biochem. J. 317:523-531(1996).
RN [6]
RP INTERACTION WITH TCF7; LEF1; TCF7L1 AND TCF7L2.
RX PubMed=11266540; DOI=10.1093/nar/29.7.1410;
RA Brantjes H., Roose J., van De Wetering M., Clevers H.;
RT "All Tcf HMG box transcription factors interact with Groucho-related co-
RT repressors.";
RL Nucleic Acids Res. 29:1410-1419(2001).
RN [7]
RP PHOSPHORYLATION DURING NEURAL CELL DIFFERENTIATION.
RX PubMed=11756536; DOI=10.1128/mcb.22.2.389-399.2002;
RA Nuthall H.N., Husain J., McLarren K.W., Stifani S.;
RT "Role for Hes1-induced phosphorylation in Groucho-mediated transcriptional
RT repression.";
RL Mol. Cell. Biol. 22:389-399(2002).
RN [8]
RP FUNCTION, AND INTERACTION WITH TLE4 AND FOXG1.
RX PubMed=16314515; DOI=10.1128/mcb.25.24.10916-10929.2005;
RA Marcal N., Patel H., Dong Z., Belanger-Jasmin S., Hoffman B.,
RA Helgason C.D., Dang J., Stifani S.;
RT "Antagonistic effects of Grg6 and Groucho/TLE on the transcription
RT repression activity of brain factor 1/FoxG1 and cortical neuron
RT differentiation.";
RL Mol. Cell. Biol. 25:10916-10929(2005).
RN [9]
RP REVIEW.
RX PubMed=18254933; DOI=10.1186/gb-2008-9-1-205;
RA Jennings B.H., Ish-Horowicz D.;
RT "The Groucho/TLE/Grg family of transcriptional co-repressors.";
RL Genome Biol. 9:R205.1-R205.7(2008).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-284, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=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).
RN [11]
RP INTERACTION WITH EFNB1.
RX PubMed=21429299; DOI=10.5483/bmbrep.2011.44.3.199;
RA Kamata T., Bong Y.S., Mood K., Park M.J., Nishanian T.G., Lee H.S.;
RT "EphrinB1 interacts with the transcriptional co-repressor Groucho/xTLE4.";
RL BMB Rep. 44:199-204(2011).
RN [12]
RP TISSUE SPECIFICITY.
RX PubMed=23990468; DOI=10.1074/jbc.m113.461848;
RA Kogawa M., Hisatake K., Atkins G.J., Findlay D.M., Enoki Y., Sato T.,
RA Gray P.C., Kanesaki-Yatsuka Y., Anderson P.H., Wada S., Kato N., Fukuda A.,
RA Katayama S., Tsujimoto M., Yoda T., Suda T., Okazaki Y., Matsumoto M.;
RT "The paired-box homeodomain transcription factor Pax6 binds to the upstream
RT region of the TRAP gene promoter and suppresses receptor activator of NF-
RT kappaB ligand (RANKL)-induced osteoclast differentiation.";
RL J. Biol. Chem. 288:31299-31312(2013).
CC -!- FUNCTION: Transcriptional corepressor that binds to a number of
CC transcription factors. Inhibits NF-kappa-B-regulated gene expression.
CC Inhibits the transcriptional activation mediated by FOXA2, and by
CC CTNNB1 and TCF family members in Wnt signaling. Enhances FOXG1/BF-
CC 1- and HES1-mediated transcriptional repression (PubMed:16314515). The
CC effects of full-length TLE family members may be modulated by
CC association with dominant-negative AES. Unusual function as coactivator
CC for ESRRG (By similarity). {ECO:0000250, ECO:0000269|PubMed:16314515}.
CC -!- SUBUNIT: Homooligomer and heterooligomer with other family members.
CC Binds RUNX1, RUNX3, FOXA2, KDM6A, UTY, histone H3, HESX1, ESRRG and the
CC NF-kappa-B subunit RELA. Interacts with HES1 (via WRPW motif) (By
CC similarity). Binds TCF7, LEF1, TCF7L1 and TCF7L2 (PubMed:11266540).
CC Interacts with SIX3 (By similarity). Interacts with EFNB1. Interacts
CC with TLE4 (PubMed:16314515). Interacts with FOXG1/BF-1; the interaction
CC is inhibited by TLE6/GRG6 (PubMed:16314515). {ECO:0000250,
CC ECO:0000250|UniProtKB:Q04724, ECO:0000269|PubMed:11266540,
CC ECO:0000269|PubMed:16314515, ECO:0000269|PubMed:21429299}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:8713081}.
CC Note=Nuclear and chromatin-associated, depending on isoforms and
CC phosphorylation status. Hyperphosphorylation decreases the affinity for
CC nuclear components.
CC -!- SUBCELLULAR LOCATION: [Isoform 7]: Nucleus
CC {ECO:0000269|PubMed:12359720}. Cytoplasm {ECO:0000269|PubMed:12359720}.
CC -!- SUBCELLULAR LOCATION: [Isoform 8]: Nucleus
CC {ECO:0000269|PubMed:12359720}. Cytoplasm {ECO:0000269|PubMed:12359720}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=8;
CC Name=1;
CC IsoId=Q62440-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q62440-2; Sequence=VSP_006989;
CC Name=3;
CC IsoId=Q62440-3; Sequence=VSP_006988;
CC Name=4;
CC IsoId=Q62440-4; Sequence=VSP_006989, VSP_006991;
CC Name=5;
CC IsoId=Q62440-5; Sequence=VSP_006987;
CC Name=6;
CC IsoId=Q62440-6; Sequence=VSP_006994, VSP_006995;
CC Name=7;
CC IsoId=Q62440-7; Sequence=VSP_006992, VSP_006993;
CC Name=8;
CC IsoId=Q62440-8; Sequence=VSP_006990, VSP_006992, VSP_006993;
CC -!- TISSUE SPECIFICITY: Highly expressed in liver and lung. Detected at
CC slightly lower levels in heart, brain, kidney and testis. Detected in
CC fetal and adult stomach and small intestine, in adult ileum, duodenum
CC and colon. Expressed in bone marrow-derived macrophages
CC (PubMed:23990468). {ECO:0000269|PubMed:23990468}.
CC -!- TISSUE SPECIFICITY: [Isoform 7]: Most abundant at the base of the
CC crypts of Lieberkuhn in the small intestine.
CC {ECO:0000269|PubMed:12359720}.
CC -!- TISSUE SPECIFICITY: [Isoform 8]: Most abundant at the base of the
CC crypts of Lieberkuhn in the small intestine.
CC {ECO:0000269|PubMed:12359720}.
CC -!- DOMAIN: WD repeat Groucho/TLE family members are characterized by 5
CC regions, a glutamine-rich Q domain, a glycine/proline-rich GP domain, a
CC central CcN domain, containing a nuclear localization signal, and a
CC serine/proline-rich SP domain. The most highly conserved are the N-
CC terminal Q domain and the C-terminal WD-repeat domain.
CC {ECO:0000305|PubMed:18254933}.
CC -!- PTM: Phosphorylated, probably by CDK1. The degree of phosphorylation
CC varies throughout the cell cycle, and is highest at the G2/M
CC transition. Becomes hyperphosphorylated in response to cell
CC differentiation and interaction with HES1 or RUNX1.
CC {ECO:0000269|PubMed:11756536, ECO:0000269|PubMed:8713081}.
CC -!- PTM: Ubiquitinated by XIAP/BIRC4. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the WD repeat Groucho/TLE family. {ECO:0000305}.
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DR EMBL; U61362; AAB49934.1; -; mRNA.
DR EMBL; AY155195; AAN77514.1; -; mRNA.
DR EMBL; AY155196; AAN77515.1; -; mRNA.
DR EMBL; AY155197; AAN77516.1; -; mRNA.
DR EMBL; AY155198; AAN77517.1; -; mRNA.
DR EMBL; AY155199; AAN77518.1; -; mRNA.
DR EMBL; AY155200; AAN77519.1; -; mRNA.
DR EMBL; AK046402; BAC32708.1; -; mRNA.
DR EMBL; AK052961; BAC35221.1; -; mRNA.
DR EMBL; AK076750; BAC36464.1; -; mRNA.
DR EMBL; AK082499; BAC38509.1; -; mRNA.
DR EMBL; AL773513; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR CCDS; CCDS18274.1; -. [Q62440-1]
DR CCDS; CCDS71407.1; -. [Q62440-7]
DR RefSeq; NP_001272459.1; NM_001285530.1.
DR RefSeq; NP_001272460.1; NM_001285531.1. [Q62440-7]
DR RefSeq; NP_001272461.1; NM_001285532.1. [Q62440-8]
DR RefSeq; NP_035729.3; NM_011599.5.
DR AlphaFoldDB; Q62440; -.
DR SMR; Q62440; -.
DR BioGRID; 204216; 16.
DR CORUM; Q62440; -.
DR IntAct; Q62440; 7.
DR MINT; Q62440; -.
DR STRING; 10090.ENSMUSP00000072481; -.
DR iPTMnet; Q62440; -.
DR PhosphoSitePlus; Q62440; -.
DR MaxQB; Q62440; -.
DR PaxDb; Q62440; -.
DR PeptideAtlas; Q62440; -.
DR PRIDE; Q62440; -.
DR ProteomicsDB; 259192; -. [Q62440-1]
DR ProteomicsDB; 259193; -. [Q62440-2]
DR ProteomicsDB; 259194; -. [Q62440-3]
DR ProteomicsDB; 259195; -. [Q62440-4]
DR ProteomicsDB; 259196; -. [Q62440-5]
DR ProteomicsDB; 259197; -. [Q62440-6]
DR ProteomicsDB; 259198; -. [Q62440-7]
DR ProteomicsDB; 259199; -. [Q62440-8]
DR Antibodypedia; 3147; 595 antibodies from 36 providers.
DR DNASU; 21885; -.
DR Ensembl; ENSMUST00000107337; ENSMUSP00000102960; ENSMUSG00000008305. [Q62440-7]
DR GeneID; 21885; -.
DR KEGG; mmu:21885; -.
DR UCSC; uc008tic.2; mouse. [Q62440-1]
DR UCSC; uc008tii.3; mouse. [Q62440-2]
DR UCSC; uc008tij.3; mouse. [Q62440-7]
DR UCSC; uc008tik.3; mouse. [Q62440-8]
DR UCSC; uc012dgd.2; mouse. [Q62440-3]
DR CTD; 7088; -.
DR MGI; MGI:104636; Tle1.
DR VEuPathDB; HostDB:ENSMUSG00000008305; -.
DR eggNOG; KOG0639; Eukaryota.
DR GeneTree; ENSGT01030000234519; -.
DR InParanoid; Q62440; -.
DR OrthoDB; 546143at2759; -.
DR Reactome; R-MMU-201722; Formation of the beta-catenin:TCF transactivating complex.
DR Reactome; R-MMU-3769402; Deactivation of the beta-catenin transactivating complex.
DR Reactome; R-MMU-4641265; Repression of WNT target genes.
DR BioGRID-ORCS; 21885; 2 hits in 74 CRISPR screens.
DR ChiTaRS; Tle1; mouse.
DR PRO; PR:Q62440; -.
DR Proteomes; UP000000589; Chromosome 4.
DR RNAct; Q62440; protein.
DR Bgee; ENSMUSG00000008305; Expressed in rostral migratory stream and 293 other tissues.
DR ExpressionAtlas; Q62440; baseline and differential.
DR Genevisible; Q62440; MM.
DR GO; GO:1990907; C:beta-catenin-TCF complex; ISO:MGI.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005634; C:nucleus; IDA:MGI.
DR GO; GO:0005667; C:transcription regulator complex; IDA:MGI.
DR GO; GO:0003682; F:chromatin binding; IDA:MGI.
DR GO; GO:0140297; F:DNA-binding transcription factor binding; ISO:MGI.
DR GO; GO:0042802; F:identical protein binding; ISO:MGI.
DR GO; GO:0003714; F:transcription corepressor activity; IDA:MGI.
DR GO; GO:2000811; P:negative regulation of anoikis; ISO:MGI.
DR GO; GO:0090090; P:negative regulation of canonical Wnt signaling pathway; IBA:GO_Central.
DR GO; GO:0043124; P:negative regulation of I-kappaB kinase/NF-kappaB signaling; ISS:UniProtKB.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IDA:MGI.
DR GO; GO:0045892; P:negative regulation of transcription, DNA-templated; ISO:MGI.
DR GO; GO:0030178; P:negative regulation of Wnt signaling pathway; ISO:MGI.
DR GO; GO:0010628; P:positive regulation of gene expression; ISO:MGI.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IGI:MGI.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; IDA:MGI.
DR GO; GO:0016055; P:Wnt signaling pathway; IEA:UniProtKB-KW.
DR Gene3D; 2.130.10.10; -; 1.
DR InterPro; IPR005617; Groucho/TLE_N.
DR InterPro; IPR009146; Groucho_enhance.
DR InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
DR InterPro; IPR001680; WD40_repeat.
DR InterPro; IPR019775; WD40_repeat_CS.
DR InterPro; IPR036322; WD40_repeat_dom_sf.
DR PANTHER; PTHR10814; PTHR10814; 1.
DR Pfam; PF03920; TLE_N; 1.
DR Pfam; PF00400; WD40; 2.
DR PRINTS; PR01850; GROUCHOFAMLY.
DR SMART; SM00320; WD40; 7.
DR SUPFAM; SSF50978; SSF50978; 1.
DR PROSITE; PS00678; WD_REPEATS_1; 2.
DR PROSITE; PS50082; WD_REPEATS_2; 2.
DR PROSITE; PS50294; WD_REPEATS_REGION; 2.
PE 1: Evidence at protein level;
KW Alternative splicing; Cytoplasm; Nucleus; Phosphoprotein;
KW Reference proteome; Repeat; Repressor; Transcription;
KW Transcription regulation; Ubl conjugation; WD repeat;
KW Wnt signaling pathway.
FT CHAIN 1..770
FT /note="Transducin-like enhancer protein 1"
FT /id="PRO_0000051277"
FT REPEAT 470..501
FT /note="WD 1"
FT REPEAT 528..558
FT /note="WD 2"
FT REPEAT 572..602
FT /note="WD 3"
FT REPEAT 614..644
FT /note="WD 4"
FT REPEAT 696..726
FT /note="WD 5"
FT REPEAT 737..767
FT /note="WD 6"
FT REGION 1..131
FT /note="Q domain"
FT /evidence="ECO:0000250|UniProtKB:Q04724"
FT REGION 128..157
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 132..199
FT /note="GP domain"
FT /evidence="ECO:0000250|UniProtKB:Q04724"
FT REGION 176..346
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 200..266
FT /note="CcN domain"
FT /evidence="ECO:0000250|UniProtKB:Q04724"
FT REGION 267..450
FT /note="SP domain"
FT /evidence="ECO:0000250|UniProtKB:Q04724"
FT MOTIF 225..228
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000255"
FT COMPBIAS 140..154
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 177..197
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 208..248
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 249..264
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 281..299
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 309..329
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 237
FT /note="Phosphoserine; by CK2"
FT /evidence="ECO:0000250|UniProtKB:Q04724, ECO:0000255"
FT MOD_RES 257
FT /note="Phosphoserine; by CDK1"
FT /evidence="ECO:0000255"
FT MOD_RES 261
FT /note="Phosphoserine; by CDK1"
FT /evidence="ECO:0000255"
FT MOD_RES 265
FT /note="Phosphoserine; by CDK1"
FT /evidence="ECO:0000255"
FT MOD_RES 284
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT VAR_SEQ 1..41
FT /note="MFPQSRHPTPHQAAGQPFKFTIPESLDRIKEEFQFLQAQYH -> MFTLSCL
FT FCFP (in isoform 5)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_006987"
FT VAR_SEQ 79..198
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:12359720"
FT /id="VSP_006988"
FT VAR_SEQ 125..198
FT /note="Missing (in isoform 2 and isoform 4)"
FT /evidence="ECO:0000303|PubMed:12359720"
FT /id="VSP_006989"
FT VAR_SEQ 127
FT /note="Missing (in isoform 8)"
FT /evidence="ECO:0000303|PubMed:12359720"
FT /id="VSP_006990"
FT VAR_SEQ 193..200
FT /note="DRESGTSN -> GERPGKPD (in isoform 7 and isoform 8)"
FT /evidence="ECO:0000303|PubMed:12359720,
FT ECO:0000303|PubMed:16141072"
FT /id="VSP_006992"
FT VAR_SEQ 201..770
FT /note="Missing (in isoform 7 and isoform 8)"
FT /evidence="ECO:0000303|PubMed:12359720,
FT ECO:0000303|PubMed:16141072"
FT /id="VSP_006993"
FT VAR_SEQ 477..658
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000305"
FT /id="VSP_006991"
FT VAR_SEQ 649..653
FT /note="RQLQQ -> NKSYQ (in isoform 6)"
FT /evidence="ECO:0000303|PubMed:12359720"
FT /id="VSP_006994"
FT VAR_SEQ 654..770
FT /note="Missing (in isoform 6)"
FT /evidence="ECO:0000303|PubMed:12359720"
FT /id="VSP_006995"
FT CONFLICT 48
FT /note="E -> G (in Ref. 2; AAN77514)"
FT /evidence="ECO:0000305"
FT CONFLICT 92
FT /note="V -> D (in Ref. 1; AAB49934)"
FT /evidence="ECO:0000305"
FT CONFLICT 122
FT /note="I -> T (in Ref. 2; AAN77518)"
FT /evidence="ECO:0000305"
FT CONFLICT 163
FT /note="S -> G (in Ref. 1; AAB49934)"
FT /evidence="ECO:0000305"
FT CONFLICT 196
FT /note="S -> P (in Ref. 1, 2; AAN77514/AAN77518 and 3;
FT BAC35221)"
FT /evidence="ECO:0000305"
FT CONFLICT 210
FT /note="S -> G (in Ref. 1, 2; AAN77519 and 3; BAC35221/
FT BAC38509)"
FT /evidence="ECO:0000305"
FT CONFLICT 247
FT /note="V -> I (in Ref. 2; AAN77514)"
FT /evidence="ECO:0000305"
FT CONFLICT 258
FT /note="P -> S (in Ref. 2; AAN77514/AAN77518)"
FT /evidence="ECO:0000305"
FT CONFLICT 428
FT /note="R -> S (in Ref. 2; AAN77518)"
FT /evidence="ECO:0000305"
FT CONFLICT 464..465
FT /note="DA -> MP (in Ref. 1; AAB49934)"
FT /evidence="ECO:0000305"
FT CONFLICT 471
FT /note="I -> F (in Ref. 1; AAB49934)"
FT /evidence="ECO:0000305"
FT CONFLICT 535
FT /note="S -> T (in Ref. 1; AAB49934)"
FT /evidence="ECO:0000305"
FT CONFLICT 542
FT /note="G -> D (in Ref. 1; AAB49934)"
FT /evidence="ECO:0000305"
FT CONFLICT 551
FT /note="A -> T (in Ref. 2; AAN77517)"
FT /evidence="ECO:0000305"
FT CONFLICT 612
FT /note="F -> Y (in Ref. 3; BAC35221)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 770 AA; 83097 MW; 65803C8F39BB0703 CRC64;
MFPQSRHPTP HQAAGQPFKF TIPESLDRIK EEFQFLQAQY HSLKLECEKL ASEKTEMQRH
YVMYYEMSYG LNIEMHKQTE IAKRLNTICA QVIPFLSQEH QQQVAQAVER AKQVTMAELN
AIIGQQQLQA QHLSHGHGPP VPLTPHPSGL QPPGIPPLGG SASLLALSSA LSGQSHLAIK
DDKKHHDAER HRDRESGTSN SLLVPDSLRS TDKRRNGPEF SSDIKKRKVD DKDNYDSDGD
KSDDNLVVDV SNEDPSSPHA SPTHSPRENG IDKNRLLKKD ASGSPASTAS SGSSSSLKSK
EVSLHEKANT PVLKSSTPTP RSDMPTPGTS ATPGLRPGLG KPPAMEPLVN QAAAGLRTPL
AVPGPYPAPF GMVPHAGMNG ELTSPGAAYA GLHSMSPQMS AAAAAAAAAV VAYGRSPMVG
FDPPPHMRVP SIPPNLAGIP GGKPAYSFHV TADGQMQPVP FPPDALIGPG IPRHARQINT
LNHGEVVCAV TISNPTRHVY TGGKGCVKVW DISHPGNKSP VSQLDCLNRD NYIRSCKLLP
DGCTLIVGGE ASTLSIWDLA APTPRIKAEL TSSAPACYAL AISPDSKVCF SCCSDGNIAV
WDLHNQTLVR QFQGHTDGAS CIDISNDGTK LWTGGLDNTV RSWDLREGRQ LQQHDFTSQI
FSLGYCPTGE WLAVGMESSN VEVLHVNKPD KYQLHLHESC VLSLKFAYCG KWFVSTGKDN
LLNAWRTPYG ASIFQSKESS SVLSCDISVD DKYIVTGSGD KKATVYEVIY
