GLI1_MOUSE
ID GLI1_MOUSE Reviewed; 1111 AA.
AC P47806; G5E857; Q9QYK1;
DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT 03-OCT-2012, sequence version 4.
DT 03-AUG-2022, entry version 185.
DE RecName: Full=Zinc finger protein GLI1;
DE AltName: Full=Glioma-associated oncogene homolog;
GN Name=Gli1; Synonyms=Gli;
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].
RX PubMed=9524201; DOI=10.1016/s0378-1119(97)00668-9;
RA Liu C.Z., Yang J.T., Yoon J.W., Walterhouse D., Iannaccone P.;
RT "Characterization of the promoter region and genomic organization of GLI, a
RT member of the Sonic hedgehog-Patched signaling pathway.";
RL Gene 209:1-11(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=ICR;
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 [3]
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 272-837.
RC STRAIN=CD-1; TISSUE=Embryo;
RX PubMed=8364225; DOI=10.1002/aja.1001960203;
RA Waterhouse D., Ahmed M., Slusarski D., Kalamaras J., Boucher D.,
RA Holmgren R., Iannaccone P.;
RT "gli, a zinc finger transcription factor and oncogene, is expressed during
RT normal mouse development.";
RL Dev. Dyn. 196:91-102(1993).
RN [6]
RP INTERACTION WITH KIF7.
RX PubMed=19592253; DOI=10.1016/j.cub.2009.06.046;
RA Endoh-Yamagami S., Evangelista M., Wilson D., Wen X., Theunissen J.W.,
RA Phamluong K., Davis M., Scales S.J., Solloway M.J., de Sauvage F.J.,
RA Peterson A.S.;
RT "The mammalian Cos2 homolog Kif7 plays an essential role in modulating Hh
RT signal transduction during development.";
RL Curr. Biol. 19:1320-1326(2009).
CC -!- FUNCTION: Acts as a transcriptional activator. Binds to the DNA
CC consensus sequence 5'-GACCACCCA-3'. Regulates the transcription of
CC specific genes during normal development. Plays a role in craniofacial
CC development and digital development, as well as development of the
CC central nervous system and gastrointestinal tract. Mediates SHH
CC signaling. Plays a role in cell proliferation and differentiation via
CC its role in SHH signaling. {ECO:0000250|UniProtKB:P08151}.
CC -!- SUBUNIT: Interacts with KIF7 (PubMed:19592253). Interacts with STK36.
CC Interacts with ZIC1; the interaction enhances transcription activation.
CC Interacts with SUFU; this inhibits transcriptional activation by GLI1
CC (By similarity). {ECO:0000250|UniProtKB:P08151,
CC ECO:0000269|PubMed:19592253}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P08151}. Nucleus
CC {ECO:0000250|UniProtKB:P08151}. Note=Tethered in the cytoplasm by
CC binding to SUFU. Activation and translocation to the nucleus is
CC promoted by interaction with STK36. Phosphorylation by ULK3 may promote
CC nuclear localization. Translocation to the nucleus is promoted by
CC interaction with ZIC1. {ECO:0000250|UniProtKB:P08151}.
CC -!- DEVELOPMENTAL STAGE: Is detected on days 10 through 18 of embryonic
CC development. During gestation it is detected in meckels precartilage
CC mesenchyme, the basis occipitus, rib mesenchymal condensations,
CC primordial vertebral bodies, digital mesenchymal condensations in
CC forefoot and hindfoot plates, the ependymal layer of the spinal cord,
CC and the mesoderm of the gastrointestinal tract. Expression persists
CC throughout gestation in developing bone and cartilage of the
CC extremities, the ribs, and the vertebral bodies as well as the
CC gastrointestinal tract mesoderm.
CC -!- PTM: Phosphorylated in vitro by ULK3. {ECO:0000250|UniProtKB:P08151}.
CC -!- PTM: Acetylation at Lys-520 down-regulates transcriptional activity.
CC Deacetylated by HDAC1. {ECO:0000250|UniProtKB:P08151}.
CC -!- PTM: Ubiquitinated by the CRL2(FEM1B) complex, suppressing GLI1
CC transcriptional activator activity. {ECO:0000250|UniProtKB:P08151}.
CC -!- SIMILARITY: Belongs to the GLI C2H2-type zinc-finger protein family.
CC {ECO:0000305}.
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DR EMBL; AF026305; AAC09169.1; -; mRNA.
DR EMBL; AB025922; BAA85004.1; -; mRNA.
DR EMBL; AC114678; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH466578; EDL24501.1; -; Genomic_DNA.
DR CCDS; CCDS24238.1; -.
DR RefSeq; NP_034426.2; NM_010296.2.
DR AlphaFoldDB; P47806; -.
DR SMR; P47806; -.
DR BioGRID; 199942; 48.
DR ComplexPortal; CPX-147; GLI1-SUFU complex.
DR CORUM; P47806; -.
DR IntAct; P47806; 1.
DR STRING; 10090.ENSMUSP00000026474; -.
DR BindingDB; P47806; -.
DR ChEMBL; CHEMBL5007; -.
DR iPTMnet; P47806; -.
DR PhosphoSitePlus; P47806; -.
DR PaxDb; P47806; -.
DR PRIDE; P47806; -.
DR ProteomicsDB; 267728; -.
DR Antibodypedia; 4004; 871 antibodies from 44 providers.
DR DNASU; 14632; -.
DR Ensembl; ENSMUST00000026474; ENSMUSP00000026474; ENSMUSG00000025407.
DR GeneID; 14632; -.
DR KEGG; mmu:14632; -.
DR UCSC; uc007hjf.1; mouse.
DR CTD; 2735; -.
DR MGI; MGI:95727; Gli1.
DR VEuPathDB; HostDB:ENSMUSG00000025407; -.
DR eggNOG; KOG1721; Eukaryota.
DR GeneTree; ENSGT00940000160235; -.
DR HOGENOM; CLU_003666_0_0_1; -.
DR InParanoid; P47806; -.
DR OMA; CTEAPLF; -.
DR OrthoDB; 135929at2759; -.
DR PhylomeDB; P47806; -.
DR TreeFam; TF350216; -.
DR Reactome; R-MMU-5610780; Degradation of GLI1 by the proteasome.
DR Reactome; R-MMU-5610787; Hedgehog 'off' state.
DR Reactome; R-MMU-5632684; Hedgehog 'on' state.
DR BioGRID-ORCS; 14632; 3 hits in 74 CRISPR screens.
DR PRO; PR:P47806; -.
DR Proteomes; UP000000589; Chromosome 10.
DR RNAct; P47806; protein.
DR Bgee; ENSMUSG00000025407; Expressed in spermatogonium and 311 other tissues.
DR ExpressionAtlas; P47806; baseline and differential.
DR Genevisible; P47806; MM.
DR GO; GO:0005930; C:axoneme; IDA:CACAO.
DR GO; GO:0005929; C:cilium; IDA:MGI.
DR GO; GO:0005737; C:cytoplasm; IDA:MGI.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:1990788; C:GLI-SUFU complex; ISO:MGI.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005634; C:nucleus; IDA:MGI.
DR GO; GO:0003682; F:chromatin binding; IDA:MGI.
DR GO; GO:0003677; F:DNA binding; ISO:MGI.
DR GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; IDA:MGI.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0008017; F:microtubule binding; IDA:MGI.
DR GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; IDA:MGI.
DR GO; GO:0000977; F:RNA polymerase II transcription regulatory region sequence-specific DNA binding; ISO:MGI.
DR GO; GO:0043565; F:sequence-specific DNA binding; ISS:UniProtKB.
DR GO; GO:0000976; F:transcription cis-regulatory region binding; ISO:MGI.
DR GO; GO:0021696; P:cerebellar cortex morphogenesis; IGI:MGI.
DR GO; GO:0009953; P:dorsal/ventral pattern formation; IGI:MGI.
DR GO; GO:0009913; P:epidermal cell differentiation; ISO:MGI.
DR GO; GO:0097421; P:liver regeneration; IMP:MGI.
DR GO; GO:0030324; P:lung development; IGI:MGI.
DR GO; GO:0090090; P:negative regulation of canonical Wnt signaling pathway; ISO:MGI.
DR GO; GO:1990787; P:negative regulation of hh target transcription factor activity; ISO:MGI.
DR GO; GO:0060032; P:notochord regression; IGI:MGI.
DR GO; GO:0001649; P:osteoblast differentiation; ISO:MGI.
DR GO; GO:0021983; P:pituitary gland development; IGI:MGI.
DR GO; GO:0060045; P:positive regulation of cardiac muscle cell proliferation; ISO:MGI.
DR GO; GO:1902808; P:positive regulation of cell cycle G1/S phase transition; ISO:MGI.
DR GO; GO:0030335; P:positive regulation of cell migration; ISO:MGI.
DR GO; GO:0008284; P:positive regulation of cell population proliferation; ISO:MGI.
DR GO; GO:0045740; P:positive regulation of DNA replication; ISO:MGI.
DR GO; GO:0045880; P:positive regulation of smoothened signaling pathway; ISO:MGI.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IDA:MGI.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IDA:MGI.
DR GO; GO:0030850; P:prostate gland development; IEA:Ensembl.
DR GO; GO:0009954; P:proximal/distal pattern formation; IGI:MGI.
DR GO; GO:2000345; P:regulation of hepatocyte proliferation; IMP:MGI.
DR GO; GO:0045667; P:regulation of osteoblast differentiation; IMP:CACAO.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR GO; GO:0009611; P:response to wounding; IDA:MGI.
DR GO; GO:0007165; P:signal transduction; TAS:MGI.
DR GO; GO:0007224; P:smoothened signaling pathway; IDA:MGI.
DR GO; GO:0021938; P:smoothened signaling pathway involved in regulation of cerebellar granule cell precursor cell proliferation; IGI:MGI.
DR GO; GO:0007286; P:spermatid development; IEA:Ensembl.
DR GO; GO:0007283; P:spermatogenesis; IDA:MGI.
DR GO; GO:0007418; P:ventral midline development; IGI:MGI.
DR InterPro; IPR043359; GLI-like.
DR InterPro; IPR032850; GLI1.
DR InterPro; IPR036236; Znf_C2H2_sf.
DR InterPro; IPR013087; Znf_C2H2_type.
DR PANTHER; PTHR45718; PTHR45718; 2.
DR PANTHER; PTHR45718:SF2; PTHR45718:SF2; 2.
DR Pfam; PF00096; zf-C2H2; 3.
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; 5.
PE 1: Evidence at protein level;
KW Acetylation; Activator; Cytoplasm; Developmental protein; Differentiation;
KW DNA-binding; Isopeptide bond; Metal-binding; Nucleus; Phosphoprotein;
KW Proto-oncogene; Reference proteome; Repeat; Transcription;
KW Transcription regulation; Ubl conjugation; Zinc; Zinc-finger.
FT CHAIN 1..1111
FT /note="Zinc finger protein GLI1"
FT /id="PRO_0000047198"
FT ZN_FING 238..263
FT /note="C2H2-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 271..298
FT /note="C2H2-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 304..328
FT /note="C2H2-type 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 334..359
FT /note="C2H2-type 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 365..390
FT /note="C2H2-type 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT REGION 52..78
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 123..127
FT /note="Interaction with SUFU"
FT /evidence="ECO:0000250|UniProtKB:P08151"
FT REGION 286..294
FT /note="Interaction with DNA"
FT /evidence="ECO:0000250|UniProtKB:P08151"
FT REGION 348..353
FT /note="Interaction with DNA"
FT /evidence="ECO:0000250|UniProtKB:P08151"
FT REGION 378..487
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 378..384
FT /note="Interaction with DNA"
FT /evidence="ECO:0000250|UniProtKB:P08151"
FT REGION 528..583
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 598..649
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 673..692
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 832..891
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1064..1093
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 378..405
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 414..429
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 435..479
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 541..565
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 849..872
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1068..1088
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 520
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P08151"
FT CROSSLNK 1008
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P08151"
FT CONFLICT 154
FT /note="V -> L (in Ref. 1; AAC09169)"
FT /evidence="ECO:0000305"
FT CONFLICT 170
FT /note="H -> Y (in Ref. 1; AAC09169)"
FT /evidence="ECO:0000305"
FT CONFLICT 173
FT /note="S -> A (in Ref. 2; BAA85004)"
FT /evidence="ECO:0000305"
FT CONFLICT 179
FT /note="T -> I (in Ref. 1; AAC09169)"
FT /evidence="ECO:0000305"
FT CONFLICT 194
FT /note="P -> R (in Ref. 1; AAC09169)"
FT /evidence="ECO:0000305"
FT CONFLICT 210
FT /note="T -> I (in Ref. 2; BAA85004)"
FT /evidence="ECO:0000305"
FT CONFLICT 271
FT /note="F -> S (in Ref. 1; AAC09169)"
FT /evidence="ECO:0000305"
FT CONFLICT 474
FT /note="Missing (in Ref. 1; AAC09169)"
FT /evidence="ECO:0000305"
FT CONFLICT 567..569
FT /note="FPP -> LPT (in Ref. 1; AAC09169)"
FT /evidence="ECO:0000305"
FT CONFLICT 707
FT /note="E -> D (in Ref. 1; AAC09169)"
FT /evidence="ECO:0000305"
FT CONFLICT 777
FT /note="Missing (in Ref. 1; AAC09169)"
FT /evidence="ECO:0000305"
FT CONFLICT 864
FT /note="G -> V (in Ref. 1; AAC09169)"
FT /evidence="ECO:0000305"
FT CONFLICT 919..920
FT /note="GL -> RA (in Ref. 1; AAC09169)"
FT /evidence="ECO:0000305"
FT CONFLICT 936
FT /note="S -> Y (in Ref. 1; AAC09169)"
FT /evidence="ECO:0000305"
FT CONFLICT 947
FT /note="Missing (in Ref. 1; AAC09169)"
FT /evidence="ECO:0000305"
FT CONFLICT 951..952
FT /note="AA -> RR (in Ref. 1; AAC09169)"
FT /evidence="ECO:0000305"
FT CONFLICT 967
FT /note="G -> R (in Ref. 1; AAC09169)"
FT /evidence="ECO:0000305"
FT CONFLICT 990
FT /note="P -> A (in Ref. 1; AAC09169)"
FT /evidence="ECO:0000305"
FT CONFLICT 1029
FT /note="A -> P (in Ref. 1; AAC09169)"
FT /evidence="ECO:0000305"
FT CONFLICT 1062..1063
FT /note="QG -> R (in Ref. 1; AAC09169)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1111 AA; 118560 MW; 8A83B254DCBB9BDC CRC64;
MFNPMTPPQV NSYSEPCCLR PLHSQGVPSM GTEGLSGLPF CHQANFMSGS QGYGAARETS
SCTEGSLFPP PPPPRSSVKL TKKRALSISP LSDASLDLQT VIRTSPSSLV AFINSRCTSP
GGSYGHLSIG TMSPSLGFPP QMSHQKGTSP PYGVQPCVPH DSTRGSMMLH PQSRGPRATC
QLKSELDMMV GKCPEDPLEG DMSSPNSTGT QDHLLGMLDG REDLEREEKP EPESVYETDC
RWDGCSQEFD SQEQLVHHIN SEHIHGERKE FVCHWGGCSR ELRPFKAQYM LVVHMRRHTG
EKPHKCTFEG CRKSYSRLEN LKTHLRSHTG EKPYMCEQEG CSKAFSNASD RAKHQNRTHS
NEKPYVCKLP GCTKRYTDPS SLRKHVKTVH GPDAHVTKRH RGDGPLPRAQ PLSTVEPKRE
REGGSGREES RLTVPESAMP QQSPGAQSSC SSDHSPAGSA ANTDSGVEMA GNAGGSTEDL
SSLDEGPCVS ATGLSTLRRL ENLRLDQLHQ LRPIGSRGLK LPSLTHAGAP VSRRLGPPVS
LDRRSSSSSS MSSAYTVSRR SSLASPFPPG TPPENGASSL PGLTPAQHYM LRARYASARG
SGTPPTAAHS LDRMGGLSVP PWRSRTEYPG YNPNAGVTRR ASDPARAADH PAPARVQRFK
SLGCVHTPPS VATGRNFDPH HPTSVYSPQP PSITENVAMD TRGLQEEPEV GTSVMGNGLN
PYMDFSSTDT LGYGGPEGTA AEPYEARGPG SLPLGPGPPT NYGPGHCAQQ VSYPDPTPEN
WGEFPSHAGV YPSNKAPGAA YSQCPRLEHY GQVQVKPEQG CPVGSDSTGL APCLNAHPSE
GSPGPQPLFS HHPQLPQPQY PQSGPYPQPP HGYLSTEPRL GLNFNPSSSH STGQLKAQLV
CNYVQSQQEL LWEGRNRGGL PNQELPYQSP KFLGGSQVSQ SPAKTPAAAA AAYGSGFAPA
SANHKSGSYP APSPCHETFT VGVNRPSHRP AAPPRLLPPL SPCYGPLKVG DTNPSCGHPE
VGRLGAGPAL YPPPEGQVCN ALDSLDLDNT QLDFVAILDE AQGLSPPLSH EQGDSSKNTP
SPSGPPNMAV GNMSVLLGSL PGETQFLNSS A
