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   27-MAR-2024, entry version 148.
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 a transcription regulator in the hedgehog (Hh)
CC       pathway (PubMed:9006072). Functions as a 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   GlyGen; Q0VGT2; 1 site, 1 O-linked glycan (1 site).
DR   iPTMnet; Q0VGT2; -.
DR   PhosphoSitePlus; Q0VGT2; -.
DR   PaxDb; 10090-ENSMUSP00000054837; -.
DR   PeptideAtlas; Q0VGT2; -.
DR   ProteomicsDB; 268833; -.
DR   Pumba; Q0VGT2; -.
DR   Antibodypedia; 3768; 419 antibodies from 39 providers.
DR   Ensembl; ENSMUST00000062483.15; ENSMUSP00000054837.9; ENSMUSG00000048402.15.
DR   GeneID; 14633; -.
DR   KEGG; mmu:14633; -.
DR   UCSC; uc007cim.1; mouse.
DR   AGR; MGI:95728; -.
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; PPESTCF; -.
DR   OrthoDB; 3304552at2759; -.
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 80 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 277 other cell types or tissues.
DR   ExpressionAtlas; Q0VGT2; baseline and differential.
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; ISS: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:0031490; F:chromatin DNA 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: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:0032967; P:positive regulation of collagen biosynthetic process; ISO:MGI.
DR   GO; GO:0045740; P:positive regulation of DNA replication; ISO:MGI.
DR   GO; GO:0045893; P:positive regulation of DNA-templated transcription; IDA:CACAO.
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:0060513; P:prostatic bud formation; IMP:MGI.
DR   GO; GO:0009954; P:proximal/distal pattern formation; IGI:MGI.
DR   GO; GO:0006355; P:regulation of DNA-templated transcription; ISS:ComplexPortal.
DR   GO; GO:0008589; P:regulation of smoothened signaling pathway; 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: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   Gene3D; 3.30.160.60; Classic Zinc Finger; 5.
DR   InterPro; IPR043359; GLI-like.
DR   InterPro; IPR036236; Znf_C2H2_sf.
DR   InterPro; IPR013087; Znf_C2H2_type.
DR   PANTHER; PTHR45718; TRANSCRIPTIONAL ACTIVATOR CUBITUS INTERRUPTUS; 1.
DR   PANTHER; PTHR45718:SF6; ZINC FINGER PROTEIN GLI2; 1.
DR   Pfam; PF00096; zf-C2H2; 2.
DR   SMART; SM00355; ZnF_C2H2; 5.
DR   SUPFAM; SSF57667; beta-beta-alpha zinc fingers; 3.
DR   PROSITE; PS00028; ZINC_FINGER_C2H2_1; 4.
DR   PROSITE; PS50157; ZINC_FINGER_C2H2_2; 4.
DR   Genevisible; Q0VGT2; MM.
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
//