GLI2_MOUSE
ID GLI2_MOUSE Reviewed; 1544 AA.
AC Q0VGT2; E9PYJ4;
DT 05-APR-2011, integrated into UniProtKB/Swiss-Prot.
DT 27-JUL-2011, sequence version 2.
DT 03-AUG-2022, entry version 139.
DE RecName: Full=Zinc finger protein GLI2 {ECO:0000305};
DE AltName: Full=Tax helper protein {ECO:0000250|UniProtKB:P10070};
GN Name=Gli2 {ECO:0000312|MGI:MGI:95728};
GN Synonyms=Thp {ECO:0000250|UniProtKB:P10070};
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 [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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Eye;
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 [3]
RP DISRUPTION PHENOTYPE, AND FUNCTION.
RX PubMed=9006072; DOI=10.1242/dev.124.1.113;
RA Mo R., Freer A.M., Zinyk D.L., Crackower M.A., Michaud J., Heng H.H.,
RA Chik K.W., Shi X.M., Tsui L.C., Cheng S.H., Joyner A.L., Hui C.;
RT "Specific and redundant functions of Gli2 and Gli3 zinc finger genes in
RT skeletal patterning and development.";
RL Development 124:113-123(1997).
RN [4]
RP FUNCTION, AND DOMAIN.
RX PubMed=10433919; DOI=10.1242/dev.126.17.3915;
RA Sasaki H., Nishizaki Y., Hui C., Nakafuku M., Kondoh H.;
RT "Regulation of Gli2 and Gli3 activities by an amino-terminal repression
RT domain: implication of Gli2 and Gli3 as primary mediators of Shh
RT signaling.";
RL Development 126:3915-3924(1999).
RN [5]
RP FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH SUFU AND STK36.
RX PubMed=10806483; DOI=10.1038/35010610;
RA Murone M., Luoh S.-L., Stone D., Li W., Gurney A., Armanini M., Grey C.,
RA Rosenthal A., de Sauvage F.J.;
RT "Gli regulation by the opposing activities of fused and suppressor of
RT fused.";
RL Nat. Cell Biol. 2:310-312(2000).
RN [6]
RP INTERACTION WITH ZIC1 AND ZIC2.
RX PubMed=11238441; DOI=10.1074/jbc.c000773200;
RA Koyabu Y., Nakata K., Mizugishi K., Aruga J., Mikoshiba K.;
RT "Physical and functional interactions between Zic and Gli proteins.";
RL J. Biol. Chem. 276:6889-6892(2001).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-707 AND THR-708, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic fibroblast;
RX PubMed=19131326; DOI=10.1074/mcp.m800451-mcp200;
RA Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.;
RT "Large scale localization of protein phosphorylation by use of electron
RT capture dissociation mass spectrometry.";
RL Mol. Cell. Proteomics 8:904-912(2009).
RN [8]
RP INTERACTION WITH SUFU, AND SUBCELLULAR LOCATION.
RX PubMed=23034632; DOI=10.1242/dev.081190;
RA Li Z.J., Nieuwenhuis E., Nien W., Zhang X., Zhang J., Puviindran V.,
RA Wainwright B.J., Kim P.C., Hui C.C.;
RT "Kif7 regulates Gli2 through Sufu-dependent and -independent functions
RT during skin development and tumorigenesis.";
RL Development 139:4152-4161(2012).
RN [9]
RP INTERACTION WITH FOXC1.
RX PubMed=26565916; DOI=10.1016/j.celrep.2015.09.063;
RA Han B., Qu Y., Jin Y., Yu Y., Deng N., Wawrowsky K., Zhang X., Li N.,
RA Bose S., Wang Q., Sakkiah S., Abrol R., Jensen T.W., Berman B.P.,
RA Tanaka H., Johnson J., Gao B., Hao J., Liu Z., Buttyan R., Ray P.S.,
RA Hung M.C., Giuliano A.E., Cui X.;
RT "FOXC1 activates smoothened-independent Hedgehog signaling in basal-like
RT breast cancer.";
RL Cell Rep. 13:1046-1058(2015).
RN [10]
RP SUBCELLULAR LOCATION.
RX PubMed=25644602; DOI=10.1101/gad.252676.114;
RA Chong Y.C., Mann R.K., Zhao C., Kato M., Beachy P.A.;
RT "Bifurcating action of Smoothened in Hedgehog signaling is mediated by
RT Dlg5.";
RL Genes Dev. 29:262-276(2015).
RN [11]
RP INTERACTION WITH FOXC1.
RX PubMed=25808752; DOI=10.1038/ncomms7653;
RA Yoshida M., Hata K., Takashima R., Ono K., Nakamura E., Takahata Y.,
RA Murakami T., Iseki S., Takano-Yamamoto T., Nishimura R., Yoneda T.;
RT "The transcription factor Foxc1 is necessary for Ihh-Gli2-regulated
RT endochondral ossification.";
RL Nat. Commun. 6:6653-6653(2015).
CC -!- FUNCTION: Functions as transcription regulator in the hedgehog (Hh)
CC pathway (PubMed:9006072). Functions as transcriptional activator
CC (PubMed:10806483). May also function as transcriptional repressor
CC (PubMed:10433919). Requires STK36 for full transcriptional activator
CC activity (PubMed:10806483). Binds to the DNA sequence 5'-GAACCACCCA-3'
CC which is part of the TRE-2S regulatory element (By similarity). Is
CC involved in the smoothened (SHH) signaling pathway (PubMed:10433919).
CC Required for normal skeleton development (PubMed:9006072).
CC {ECO:0000250|UniProtKB:P10070, ECO:0000269|PubMed:10806483,
CC ECO:0000269|PubMed:9006072, ECO:0000305|PubMed:10433919}.
CC -!- SUBUNIT: Interacts with ZIC1 and ZIC2 (PubMed:11238441). Interacts with
CC STK36 (PubMed:10806483). Interacts with SUFU; this inhibits
CC transcriptional activation mediated by GLI2 (PubMed:10806483,
CC PubMed:23034632). Interacts (via C-terminal internal region) with FOXC1
CC (via N-terminus); this interaction is direct and increases GLI2 DNA-
CC binding and transcriptional activity through a smoothened (SMO)-
CC independent Hedgehog (Hh) signaling pathway (PubMed:26565916,
CC PubMed:25808752). {ECO:0000250|UniProtKB:P10070,
CC ECO:0000269|PubMed:10806483, ECO:0000269|PubMed:11238441,
CC ECO:0000269|PubMed:23034632, ECO:0000269|PubMed:25808752,
CC ECO:0000269|PubMed:26565916}.
CC -!- INTERACTION:
CC Q0VGT2; Q6ZWS8: Spop; NbExp=2; IntAct=EBI-9344284, EBI-7128920;
CC Q0VGT2; Q9UMX1: SUFU; Xeno; NbExp=3; IntAct=EBI-9344284, EBI-740595;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:10806483}. Cytoplasm
CC {ECO:0000269|PubMed:10806483}. Cell projection, cilium
CC {ECO:0000269|PubMed:25644602}. Note=STK36 promotes translocation to the
CC nucleus (PubMed:10806483). In keratinocytes, it is sequestered in the
CC cytoplasm by SUFU. In the absence of SUFU, it translocates to the
CC nucleus (PubMed:23034632). {ECO:0000269|PubMed:10806483,
CC ECO:0000269|PubMed:23034632}.
CC -!- DOMAIN: The N-terminal domain confers transcriptional repressor
CC activity, while the C-terminal domain mediates transcriptional
CC activation. {ECO:0000269|PubMed:10433919}.
CC -!- PTM: Phosphorylated in vitro by ULK3. Phosphorylated by DYRK2; this
CC inhibits GLI2 transcription factor activity and promotes proteasomal
CC degradation of GLI2. {ECO:0000250|UniProtKB:P10070}.
CC -!- PTM: Acetylation at Lys-740 inhibits Hh target gene expression,
CC probably by impeding entry into chromatin thus preventing promoter
CC occupancy. {ECO:0000250|UniProtKB:P10070}.
CC -!- DISRUPTION PHENOTYPE: Full embryonic lethality. Homozygous embryos are
CC detected at the expected Mendelian rate up to about 18.5 dpc, but there
CC are no live pups. Mutant embryos present important craniofacial
CC defects, including defects of the medial portion of the frontal and
CC parietal skull bones, absence of upper and/or lower incisors, often
CC combined with a cleft palate. Besides, mutant embryos show defects in
CC the ossification of skeletal bones and shortened limb bones.
CC {ECO:0000269|PubMed:9006072}.
CC -!- SIMILARITY: Belongs to the GLI C2H2-type zinc-finger protein family.
CC {ECO:0000305}.
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DR EMBL; AC109271; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC122287; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC132589; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC085190; AAH85190.1; -; mRNA.
DR CCDS; CCDS35692.1; -.
DR RefSeq; NP_001074594.1; NM_001081125.1.
DR AlphaFoldDB; Q0VGT2; -.
DR SMR; Q0VGT2; -.
DR BioGRID; 199943; 47.
DR ComplexPortal; CPX-149; GLI2-SUFU complex.
DR CORUM; Q0VGT2; -.
DR DIP; DIP-60772N; -.
DR ELM; Q0VGT2; -.
DR IntAct; Q0VGT2; 2.
DR STRING; 10090.ENSMUSP00000054837; -.
DR BindingDB; Q0VGT2; -.
DR ChEMBL; CHEMBL4523629; -.
DR iPTMnet; Q0VGT2; -.
DR PhosphoSitePlus; Q0VGT2; -.
DR PaxDb; Q0VGT2; -.
DR PeptideAtlas; Q0VGT2; -.
DR PRIDE; Q0VGT2; -.
DR ProteomicsDB; 268833; -.
DR Antibodypedia; 3768; 354 antibodies from 39 providers.
DR Ensembl; ENSMUST00000062483; ENSMUSP00000054837; ENSMUSG00000048402.
DR GeneID; 14633; -.
DR KEGG; mmu:14633; -.
DR UCSC; uc007cim.1; mouse.
DR CTD; 2736; -.
DR MGI; MGI:95728; Gli2.
DR VEuPathDB; HostDB:ENSMUSG00000048402; -.
DR eggNOG; KOG1721; Eukaryota.
DR GeneTree; ENSGT00940000159213; -.
DR HOGENOM; CLU_003666_2_0_1; -.
DR InParanoid; Q0VGT2; -.
DR OMA; FHSAHDV; -.
DR OrthoDB; 56870at2759; -.
DR PhylomeDB; Q0VGT2; -.
DR TreeFam; TF350216; -.
DR Reactome; R-MMU-5610787; Hedgehog 'off' state.
DR Reactome; R-MMU-5632684; Hedgehog 'on' state.
DR BioGRID-ORCS; 14633; 2 hits in 75 CRISPR screens.
DR ChiTaRS; Gli2; mouse.
DR PRO; PR:Q0VGT2; -.
DR Proteomes; UP000000589; Chromosome 1.
DR RNAct; Q0VGT2; protein.
DR Bgee; ENSMUSG00000048402; Expressed in spermatogonium and 276 other tissues.
DR ExpressionAtlas; Q0VGT2; baseline and differential.
DR Genevisible; Q0VGT2; MM.
DR GO; GO:0005930; C:axoneme; IDA:CACAO.
DR GO; GO:0097542; C:ciliary tip; IDA:MGI.
DR GO; GO:0005929; C:cilium; IDA:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; IDA:MGI.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:1990788; C:GLI-SUFU complex; IC:ComplexPortal.
DR GO; GO:0016020; C:membrane; IDA:MGI.
DR GO; GO:0031514; C:motile cilium; IDA:MGI.
DR GO; GO:0016607; C:nuclear speck; IDA:MGI.
DR GO; GO:0005730; C:nucleolus; ISO:MGI.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0003682; F:chromatin binding; IDA:MGI.
DR GO; GO:0001228; F:DNA-binding transcription activator activity, RNA polymerase II-specific; IDA:NTNU_SB.
DR GO; GO:0003700; F:DNA-binding transcription factor activity; IDA:MGI.
DR GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; IBA:GO_Central.
DR GO; GO:1990841; F:promoter-specific chromatin binding; IDA:UniProtKB.
DR GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; IDA:NTNU_SB.
DR GO; GO:0043565; F:sequence-specific DNA binding; IDA:MGI.
DR GO; GO:1990837; F:sequence-specific double-stranded DNA binding; ISO:MGI.
DR GO; GO:0000976; F:transcription cis-regulatory region binding; IDA:MGI.
DR GO; GO:0008270; F:zinc ion binding; ISO:MGI.
DR GO; GO:0048856; P:anatomical structure development; IMP:MGI.
DR GO; GO:0048646; P:anatomical structure formation involved in morphogenesis; IGI:MGI.
DR GO; GO:0009952; P:anterior/posterior pattern specification; IGI:MGI.
DR GO; GO:0007411; P:axon guidance; IMP:MGI.
DR GO; GO:0048754; P:branching morphogenesis of an epithelial tube; IMP:MGI.
DR GO; GO:0030154; P:cell differentiation; IMP:MGI.
DR GO; GO:0008283; P:cell population proliferation; IMP:MGI.
DR GO; GO:0071407; P:cellular response to organic cyclic compound; IDA:MGI.
DR GO; GO:0098586; P:cellular response to virus; ISO:MGI.
DR GO; GO:0021696; P:cerebellar cortex morphogenesis; IMP:MGI.
DR GO; GO:0002062; P:chondrocyte differentiation; IGI:MGI.
DR GO; GO:0090103; P:cochlea morphogenesis; IMP:MGI.
DR GO; GO:0048589; P:developmental growth; IMP:MGI.
DR GO; GO:0021904; P:dorsal/ventral neural tube patterning; IDA:MGI.
DR GO; GO:0009953; P:dorsal/ventral pattern formation; IGI:MGI.
DR GO; GO:0048566; P:embryonic digestive tract development; IMP:MGI.
DR GO; GO:0042733; P:embryonic digit morphogenesis; IMP:MGI.
DR GO; GO:0009913; P:epidermal cell differentiation; ISO:MGI.
DR GO; GO:0050673; P:epithelial cell proliferation; IMP:MGI.
DR GO; GO:0021508; P:floor plate formation; IMP:MGI.
DR GO; GO:0010467; P:gene expression; IMP:MGI.
DR GO; GO:0031069; P:hair follicle morphogenesis; ISO:MGI.
DR GO; GO:0060322; P:head development; IMP:MGI.
DR GO; GO:0007507; P:heart development; IGI:MGI.
DR GO; GO:0030902; P:hindbrain development; IMP:MGI.
DR GO; GO:0007442; P:hindgut morphogenesis; IMP:MGI.
DR GO; GO:0001701; P:in utero embryonic development; IMP:MGI.
DR GO; GO:0001822; P:kidney development; IGI:MGI.
DR GO; GO:0030324; P:lung development; IMP:MGI.
DR GO; GO:0030879; P:mammary gland development; IMP:MGI.
DR GO; GO:0060603; P:mammary gland duct morphogenesis; IMP:MGI.
DR GO; GO:0002009; P:morphogenesis of an epithelium; IMP:MGI.
DR GO; GO:0043066; P:negative regulation of apoptotic process; IDA:MGI.
DR GO; GO:0032331; P:negative regulation of chondrocyte differentiation; IMP:MGI.
DR GO; GO:1990787; P:negative regulation of hh target transcription factor activity; IC:ComplexPortal.
DR GO; GO:0045879; P:negative regulation of smoothened signaling pathway; IGI:MGI.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IGI:MGI.
DR GO; GO:0021915; P:neural tube development; IMP:MGI.
DR GO; GO:0048666; P:neuron development; IMP:MGI.
DR GO; GO:0030182; P:neuron differentiation; IGI:MGI.
DR GO; GO:0060032; P:notochord regression; IGI:MGI.
DR GO; GO:0042475; P:odontogenesis of dentin-containing tooth; IMP:MGI.
DR GO; GO:0002076; P:osteoblast development; IDA:MGI.
DR GO; GO:0001649; P:osteoblast differentiation; IGI:MGI.
DR GO; GO:0007389; P:pattern specification process; IMP:MGI.
DR GO; GO:0021983; P:pituitary gland development; IGI:MGI.
DR GO; GO:0008284; P:positive regulation of cell population proliferation; IMP:MGI.
DR GO; GO:0045740; P:positive regulation of DNA replication; ISO:MGI.
DR GO; GO:0050679; P:positive regulation of epithelial cell proliferation; IMP:MGI.
DR GO; GO:0045666; P:positive regulation of neuron differentiation; IGI:MGI.
DR GO; GO:2000648; P:positive regulation of stem cell proliferation; IMP:MGI.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IDA:NTNU_SB.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IDA:MGI.
DR GO; GO:0060513; P:prostatic bud formation; IMP:MGI.
DR GO; GO:0009954; P:proximal/distal pattern formation; IGI:MGI.
DR GO; GO:1901620; P:regulation of smoothened signaling pathway involved in dorsal/ventral neural tube patterning; IGI:MGI.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR GO; GO:0001501; P:skeletal system development; IMP:MGI.
DR GO; GO:0007224; P:smoothened signaling pathway; IMP:MGI.
DR GO; GO:0060831; P:smoothened signaling pathway involved in dorsal/ventral neural tube patterning; IGI:MGI.
DR GO; GO:0021938; P:smoothened signaling pathway involved in regulation of cerebellar granule cell precursor cell proliferation; IMP:MGI.
DR GO; GO:0021776; P:smoothened signaling pathway involved in spinal cord motor neuron cell fate specification; IGI:MGI.
DR GO; GO:0021775; P:smoothened signaling pathway involved in ventral spinal cord interneuron specification; IGI:MGI.
DR GO; GO:0021513; P:spinal cord dorsal/ventral patterning; IMP:MGI.
DR GO; GO:0021522; P:spinal cord motor neuron differentiation; IMP:MGI.
DR GO; GO:0021965; P:spinal cord ventral commissure morphogenesis; IMP:MGI.
DR GO; GO:0072089; P:stem cell proliferation; IMP:MGI.
DR GO; GO:0035295; P:tube development; IGI:MGI.
DR GO; GO:0007418; P:ventral midline development; IMP:MGI.
DR GO; GO:0021517; P:ventral spinal cord development; IMP:MGI.
DR InterPro; IPR043359; GLI-like.
DR InterPro; IPR036236; Znf_C2H2_sf.
DR InterPro; IPR013087; Znf_C2H2_type.
DR PANTHER; PTHR45718; PTHR45718; 1.
DR Pfam; PF00096; zf-C2H2; 4.
DR SMART; SM00355; ZnF_C2H2; 5.
DR SUPFAM; SSF57667; SSF57667; 3.
DR PROSITE; PS00028; ZINC_FINGER_C2H2_1; 4.
DR PROSITE; PS50157; ZINC_FINGER_C2H2_2; 4.
PE 1: Evidence at protein level;
KW Acetylation; Activator; Cell projection; Cilium; Cytoplasm;
KW Developmental protein; DNA-binding; Metal-binding; Nucleus; Phosphoprotein;
KW Reference proteome; Repeat; Repressor; Transcription;
KW Transcription regulation; Zinc; Zinc-finger.
FT CHAIN 1..1544
FT /note="Zinc finger protein GLI2"
FT /id="PRO_0000406215"
FT ZN_FING 417..444
FT /note="C2H2-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 455..477
FT /note="C2H2-type 2; degenerate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 483..507
FT /note="C2H2-type 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 513..538
FT /note="C2H2-type 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 544..569
FT /note="C2H2-type 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT REGION 1..26
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 338..364
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 557..619
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 635..682
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 781..800
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 805..861
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 908..963
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 995..1016
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1166..1220
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1422..1457
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 557..591
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 635..663
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 805..819
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 833..861
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 997..1015
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1168..1220
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1439..1457
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 145
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P10070"
FT MOD_RES 230
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P10070"
FT MOD_RES 232
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P10070"
FT MOD_RES 238
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P10070"
FT MOD_RES 385
FT /note="Phosphoserine; by DYRK2"
FT /evidence="ECO:0000250|UniProtKB:P10070"
FT MOD_RES 707
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19131326"
FT MOD_RES 708
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:19131326"
FT MOD_RES 740
FT /note="N6-acetyllysine; by EP300"
FT /evidence="ECO:0000250|UniProtKB:P10070"
FT MOD_RES 997
FT /note="Phosphoserine; by DYRK2"
FT /evidence="ECO:0000250|UniProtKB:P10070"
FT CONFLICT 71
FT /note="Y -> S (in Ref. 2; AAH85190)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1544 AA; 165031 MW; EA290773B3DE1D6A CRC64;
METSAPAPAL EKKEAKSGLL EDSSFPDPGK KACPLAVAAA VAAHGVPQQL LPAFHAPLPI
DMRHQEGRYH YDPHSVHSVH GPPTLSGSPV ISDISLIRLS PHPAGPGESP FSAHHPYVNP
HMEHYLRSVH SSPTLSMISA ARGLSPADVA HEHLKERGLF SLAAPGTNPS DYYHQMTLMA
SHPTPYGDLL MQSGGAASAP HLHDYLNPVD ASRFSSPRVT PRLSRKRALS ISPLSDASLD
LQRMIRTSPN SLVAYINNSR SSSAASGSYG HLSAGALSPA FTFPHPINPV AYQQILSQQR
GLGSAFGHTP PLIQPSPTFL AQQPMTLTSI STMPTQLSSS SSNCLNDANQ NKQNSESAVS
STVNPITIHK RSKVKTEAEG LRPASPLGLT QEQLADLKED LDRDDCKQEA EVVIYETNCH
WADCTKEYDT QEQLVHHINN EHIHGEKKEF VCRWQACTRE QKPFKAQYML VVHMRRHTGE
KPHKCTFEGC SKAYSRLENL KTHLRSHTGE KPYVCEHEGC NKAFSNASDR AKHQNRTHSN
EKPYICKIPG CTKRYTDPSS LRKHVKTVHG PDAHVTKKQR NDVHVRAPLL KENGDNEASA
EPGGRGPEES VEASSTSHTV EDCLHIKAIK TESSGLCQSS PGAQSSCSSE PSPLGSAPNN
DSGMEMPGTG PGSLGDLTAL ADTCPGADTS ALAAPSTGGL QLRKHMSTVH RFEQLKREKL
KSLKDSCSWA GPAPHTRNTK LPPLPVNGSV LENFNNTGGG GPAGLLPSQR LPELTEVTML
SQLQERRDSS TSTMSSAYTV SRRSSGISPY FSSRRSSEAS PLGGLRPHNA SSADSYDPIS
TDASRRSSEA SQCSGGGPGL LNLTPAQQYN LRAKYAAATG GPPPTPLPGL DRVSLRTRLA
LLDAPERALP GACPHPLGPR RGSDGPTYSH GHGHGYAGAA PAFPHEGPNS STRRASDPVR
RPDPLILPRV QRFHSTHNMN PGSLPPCADR RGLHVQSHPS VDSNLTRNAY SPRPPSINEN
VVMEAVAAGV DGPGLECDLG LVEDELVLPD DVVQYIKAHT GGTLDDGIRQ GYPTEGTGFP
ENSKLPSPGL QGHRRLAAAD SNMGPSAPGL GGCQLSYSPS SNLNKSNMPV QWNEVSSGTV
DALPTQVKPP PFPHSNLAVV QQKPAFGQYP GYNPQSVQSS SGGLDSTQPH LQLRGAPSAS
RGSYTQQPRQ PAAGSQCLGM SAAMSPQASY SQAHPQLSPN IVSGSLNQFS PSCSNMAAKP
SHLGLPQQME VVPNATIMNG HQREHGVPNS SLAAVSQPHP VLSYPQQDSY QQGSNLLSSH
QPGFMESQQN AGFGLMQPRP PLEPNTASRH RGVRSGQQQL YARTTGQAMV TSANQETAEA
MPKGPAGTMV SLAPQPSQDT GRAQDQNTLY YYGQIHMYEQ NGGCPAVQPQ PPQPQACSDS
IQPEPLPSPG VNQVSSTVDS QLLEPPQIDF DAIMDDGDHS SLFSGALSPT LLHNLSQNSS
RLTTPRNSLT LPSIPAGISN MAVGDMSSML TSLAEESKFL NMMT
