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Zinc finger protein GLI1 (Glioma-associated oncogene homolog)

 GLI1_MOUSE              Reviewed;        1111 AA.
P47806; G5E857; Q9QYK1;
01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
03-OCT-2012, sequence version 4.
10-OCT-2018, entry version 164.
RecName: Full=Zinc finger protein GLI1;
AltName: Full=Glioma-associated oncogene homolog;
Name=Gli1; Synonyms=Gli;
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=9524201; DOI=10.1016/S0378-1119(97)00668-9;
Liu C.Z., Yang J.T., Yoon J.W., Walterhouse D., Iannaccone P.;
"Characterization of the promoter region and genomic organization of
GLI, a member of the Sonic hedgehog-Patched signaling pathway.";
Gene 209:1-11(1998).
[2]
NUCLEOTIDE SEQUENCE [MRNA].
STRAIN=ICR;
PubMed=10433919;
Sasaki H., Nishizaki Y., Hui C., Nakafuku M., Kondoh H.;
"Regulation of Gli2 and Gli3 activities by an amino-terminal
repression domain: implication of Gli2 and Gli3 as primary mediators
of Shh signaling.";
Development 126:3915-3924(1999).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=C57BL/6J;
PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
Lindblad-Toh K., Eichler E.E., Ponting C.P.;
"Lineage-specific biology revealed by a finished genome assembly of
the mouse.";
PLoS Biol. 7:E1000112-E1000112(2009).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
[5]
NUCLEOTIDE SEQUENCE [MRNA] OF 272-837.
STRAIN=CD-1; TISSUE=Embryo;
PubMed=8364225; DOI=10.1002/aja.1001960203;
Waterhouse D., Ahmed M., Slusarski D., Kalamaras J., Boucher D.,
Holmgren R., Iannaccone P.;
"gli, a zinc finger transcription factor and oncogene, is expressed
during normal mouse development.";
Dev. Dyn. 196:91-102(1993).
[6]
INTERACTION WITH KIF7.
PubMed=19592253; DOI=10.1016/j.cub.2009.06.046;
Endoh-Yamagami S., Evangelista M., Wilson D., Wen X., Theunissen J.W.,
Phamluong K., Davis M., Scales S.J., Solloway M.J., de Sauvage F.J.,
Peterson A.S.;
"The mammalian Cos2 homolog Kif7 plays an essential role in modulating
Hh signal transduction during development.";
Curr. Biol. 19:1320-1326(2009).
-!- FUNCTION: Acts as a transcriptional activator. Binds to the DNA
consensus sequence 5'-GACCACCCA-3'. May regulate the transcription
of specific genes during normal development. May play a role in
craniofacial development and digital development, as well as
development of the central nervous system and gastrointestinal
tract. Mediates SHH signaling. Plays a role in cell proliferation
and differentiation via its role in SHH signaling.
{ECO:0000250|UniProtKB:P08151}.
-!- SUBUNIT: Interacts with KIF7 (PubMed:19592253). Interacts with
STK36. Interacts with ZIC1; the interaction enhances transcription
activation. Interacts with SUFU; this inhibits transcriptional
activation by GLI1 (By similarity). {ECO:0000250|UniProtKB:P08151,
ECO:0000269|PubMed:19592253}.
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P08151}.
Nucleus {ECO:0000250|UniProtKB:P08151}. Note=Tethered in the
cytoplasm by binding to SUFU. Activation and translocation to the
nucleus is promoted by interaction with STK36. Phosphorylation by
ULK3 may promote nuclear localization. Translocation to the
nucleus is promoted by interaction with ZIC1.
{ECO:0000250|UniProtKB:P08151}.
-!- DEVELOPMENTAL STAGE: Is detected on days 10 through 18 of
embryonic development. During gestation it is detected in meckels
precartilage mesenchyme, the basis occipitus, rib mesenchymal
condensations, primordial vertebral bodies, digital mesenchymal
condensations in forefoot and hindfoot plates, the ependymal layer
of the spinal cord, and the mesoderm of the gastrointestinal
tract. Expression persists throughout gestation in developing bone
and cartilage of the extremities, the ribs, and the vertebral
bodies as well as the gastrointestinal tract mesoderm.
-!- PTM: Phosphorylated in vitro by ULK3.
{ECO:0000250|UniProtKB:P08151}.
-!- PTM: Acetylation at Lys-520 down-regulates transcriptional
activity. Deacetylated by HDAC1. {ECO:0000250|UniProtKB:P08151}.
-!- SIMILARITY: Belongs to the GLI C2H2-type zinc-finger protein
family. {ECO:0000305}.
-----------------------------------------------------------------------
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EMBL; AF026305; AAC09169.1; -; mRNA.
EMBL; AB025922; BAA85004.1; -; mRNA.
EMBL; AC114678; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; CH466578; EDL24501.1; -; Genomic_DNA.
CCDS; CCDS24238.1; -.
RefSeq; NP_034426.2; NM_010296.2.
UniGene; Mm.391450; -.
ProteinModelPortal; P47806; -.
SMR; P47806; -.
BioGrid; 199942; 4.
ComplexPortal; CPX-147; GLI1-SUFU complex.
CORUM; P47806; -.
IntAct; P47806; 1.
STRING; 10090.ENSMUSP00000026474; -.
ChEMBL; CHEMBL5007; -.
iPTMnet; P47806; -.
PhosphoSitePlus; P47806; -.
PaxDb; P47806; -.
PRIDE; P47806; -.
Ensembl; ENSMUST00000026474; ENSMUSP00000026474; ENSMUSG00000025407.
GeneID; 14632; -.
KEGG; mmu:14632; -.
UCSC; uc007hjf.1; mouse.
CTD; 2735; -.
MGI; MGI:95727; Gli1.
eggNOG; KOG1721; Eukaryota.
eggNOG; COG5048; LUCA.
GeneTree; ENSGT00900000140802; -.
HOGENOM; HOG000290688; -.
HOVERGEN; HBG080668; -.
InParanoid; P47806; -.
KO; K16797; -.
OMA; VTKRHRG; -.
OrthoDB; EOG091G01XS; -.
TreeFam; TF350216; -.
Reactome; R-MMU-5610780; Degradation of GLI1 by the proteasome.
Reactome; R-MMU-5610787; Hedgehog 'off' state.
Reactome; R-MMU-5632684; Hedgehog 'on' state.
PRO; PR:P47806; -.
Proteomes; UP000000589; Chromosome 10.
Bgee; ENSMUSG00000025407; Expressed in 312 organ(s), highest expression level in spermatogonium.
CleanEx; MM_GLI1; -.
ExpressionAtlas; P47806; baseline and differential.
Genevisible; P47806; MM.
GO; GO:0005930; C:axoneme; IDA:CACAO.
GO; GO:0005929; C:cilium; IDA:MGI.
GO; GO:0005737; C:cytoplasm; IDA:MGI.
GO; GO:0005829; C:cytosol; ISO:MGI.
GO; GO:0005654; C:nucleoplasm; ISO:MGI.
GO; GO:0005634; C:nucleus; IDA:MGI.
GO; GO:0003682; F:chromatin binding; IDA:MGI.
GO; GO:0003677; F:DNA binding; IDA:MGI.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0008017; F:microtubule binding; IDA:MGI.
GO; GO:0000978; F:RNA polymerase II proximal promoter sequence-specific DNA binding; IDA:MGI.
GO; GO:0000977; F:RNA polymerase II regulatory region sequence-specific DNA binding; ISO:MGI.
GO; GO:0043565; F:sequence-specific DNA binding; ISS:UniProtKB.
GO; GO:0003705; F:transcription factor activity, RNA polymerase II distal enhancer sequence-specific binding; IDA:MGI.
GO; GO:0044212; F:transcription regulatory region DNA binding; ISO:MGI.
GO; GO:0060070; P:canonical Wnt signaling pathway; IDA:MGI.
GO; GO:0021696; P:cerebellar cortex morphogenesis; IGI:MGI.
GO; GO:0009953; P:dorsal/ventral pattern formation; IGI:MGI.
GO; GO:0009913; P:epidermal cell differentiation; ISO:MGI.
GO; GO:0097421; P:liver regeneration; IMP:MGI.
GO; GO:0030324; P:lung development; IGI:MGI.
GO; GO:0090090; P:negative regulation of canonical Wnt signaling pathway; ISO:MGI.
GO; GO:0060032; P:notochord regression; IGI:MGI.
GO; GO:0001649; P:osteoblast differentiation; ISO:MGI.
GO; GO:0021983; P:pituitary gland development; IGI:MGI.
GO; GO:0060045; P:positive regulation of cardiac muscle cell proliferation; ISO:MGI.
GO; GO:1902808; P:positive regulation of cell cycle G1/S phase transition; ISO:MGI.
GO; GO:0030335; P:positive regulation of cell migration; ISO:MGI.
GO; GO:0008284; P:positive regulation of cell proliferation; ISO:MGI.
GO; GO:0045740; P:positive regulation of DNA replication; ISO:MGI.
GO; GO:0045880; P:positive regulation of smoothened signaling pathway; ISO:MGI.
GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IDA:MGI.
GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IDA:CACAO.
GO; GO:0030850; P:prostate gland development; IEA:Ensembl.
GO; GO:0009954; P:proximal/distal pattern formation; IGI:MGI.
GO; GO:2000345; P:regulation of hepatocyte proliferation; IMP:MGI.
GO; GO:0045667; P:regulation of osteoblast differentiation; IMP:CACAO.
GO; GO:0009611; P:response to wounding; IDA:MGI.
GO; GO:0007165; P:signal transduction; TAS:MGI.
GO; GO:0007224; P:smoothened signaling pathway; IDA:MGI.
GO; GO:0021938; P:smoothened signaling pathway involved in regulation of cerebellar granule cell precursor cell proliferation; IGI:MGI.
GO; GO:0007283; P:spermatogenesis; IDA:MGI.
GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-KW.
GO; GO:0007418; P:ventral midline development; IGI:MGI.
InterPro; IPR032850; GLI1.
InterPro; IPR036236; Znf_C2H2_sf.
InterPro; IPR013087; Znf_C2H2_type.
PANTHER; PTHR19818:SF2; PTHR19818:SF2; 1.
Pfam; PF00096; zf-C2H2; 3.
SMART; SM00355; ZnF_C2H2; 5.
SUPFAM; SSF57667; SSF57667; 3.
PROSITE; PS00028; ZINC_FINGER_C2H2_1; 4.
PROSITE; PS50157; ZINC_FINGER_C2H2_2; 5.
1: Evidence at protein level;
Acetylation; Activator; Complete proteome; Cytoplasm;
Developmental protein; Differentiation; DNA-binding; Isopeptide bond;
Metal-binding; Nucleus; Phosphoprotein; Proto-oncogene;
Reference proteome; Repeat; Transcription; Transcription regulation;
Ubl conjugation; Zinc; Zinc-finger.
CHAIN 1 1111 Zinc finger protein GLI1.
/FTId=PRO_0000047198.
ZN_FING 238 263 C2H2-type 1. {ECO:0000255|PROSITE-
ProRule:PRU00042}.
ZN_FING 271 298 C2H2-type 2. {ECO:0000255|PROSITE-
ProRule:PRU00042}.
ZN_FING 304 328 C2H2-type 3. {ECO:0000255|PROSITE-
ProRule:PRU00042}.
ZN_FING 334 359 C2H2-type 4. {ECO:0000255|PROSITE-
ProRule:PRU00042}.
ZN_FING 365 390 C2H2-type 5. {ECO:0000255|PROSITE-
ProRule:PRU00042}.
REGION 123 127 Interaction with SUFU.
{ECO:0000250|UniProtKB:P08151}.
REGION 286 294 Interaction with DNA.
{ECO:0000250|UniProtKB:P08151}.
REGION 348 353 Interaction with DNA.
{ECO:0000250|UniProtKB:P08151}.
REGION 378 384 Interaction with DNA.
{ECO:0000250|UniProtKB:P08151}.
COMPBIAS 1042 1059 Asp/Glu-rich (acidic).
MOD_RES 520 520 N6-acetyllysine.
{ECO:0000250|UniProtKB:P08151}.
CROSSLNK 1008 1008 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000250|UniProtKB:P08151}.
CONFLICT 154 154 V -> L (in Ref. 1; AAC09169).
{ECO:0000305}.
CONFLICT 170 170 H -> Y (in Ref. 1; AAC09169).
{ECO:0000305}.
CONFLICT 173 173 S -> A (in Ref. 2; BAA85004).
{ECO:0000305}.
CONFLICT 179 179 T -> I (in Ref. 1; AAC09169).
{ECO:0000305}.
CONFLICT 194 194 P -> R (in Ref. 1; AAC09169).
{ECO:0000305}.
CONFLICT 210 210 T -> I (in Ref. 2; BAA85004).
{ECO:0000305}.
CONFLICT 271 271 F -> S (in Ref. 1; AAC09169).
{ECO:0000305}.
CONFLICT 474 474 Missing (in Ref. 1; AAC09169).
{ECO:0000305}.
CONFLICT 567 569 FPP -> LPT (in Ref. 1; AAC09169).
{ECO:0000305}.
CONFLICT 707 707 E -> D (in Ref. 1; AAC09169).
{ECO:0000305}.
CONFLICT 777 777 Missing (in Ref. 1; AAC09169).
{ECO:0000305}.
CONFLICT 864 864 G -> V (in Ref. 1; AAC09169).
{ECO:0000305}.
CONFLICT 919 920 GL -> RA (in Ref. 1; AAC09169).
{ECO:0000305}.
CONFLICT 936 936 S -> Y (in Ref. 1; AAC09169).
{ECO:0000305}.
CONFLICT 947 947 Missing (in Ref. 1; AAC09169).
{ECO:0000305}.
CONFLICT 951 952 AA -> RR (in Ref. 1; AAC09169).
{ECO:0000305}.
CONFLICT 967 967 G -> R (in Ref. 1; AAC09169).
{ECO:0000305}.
CONFLICT 990 990 P -> A (in Ref. 1; AAC09169).
{ECO:0000305}.
CONFLICT 1029 1029 A -> P (in Ref. 1; AAC09169).
{ECO:0000305}.
CONFLICT 1062 1063 QG -> R (in Ref. 1; AAC09169).
{ECO:0000305}.
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


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