ID GLI1_HUMAN Reviewed; 1106 AA. AC P08151; D0EUY3; E9PQQ9; F5H6H8; Q8TDN9; DT 01-AUG-1988, integrated into UniProtKB/Swiss-Prot. DT 01-AUG-1988, sequence version 1. DT 11-NOV-2015, entry version 180. DE RecName: Full=Zinc finger protein GLI1; DE AltName: Full=Glioma-associated oncogene; DE AltName: Full=Oncogene GLI; GN Name=GLI1; Synonyms=GLI; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1). RX PubMed=2832761; DOI=10.1038/332371a0; RA Kinzler K.W., Ruppert J.M., Bigner S.H., Vogelstein B.; RT "The GLI gene is a member of the Kruppel family of zinc finger RT proteins."; RL Nature 332:371-374(1988). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANTS ASP-933 AND GLN-1100. RA Yoon J.W., Kent P., Clark A., Patterson J., Villavicencio E., RA Iannaccone P., Walterhouse D.; RT "Polymorphic variants of the human oncogene GLI1 function similarly."; RL Submitted (OCT-2000) to the EMBL/GenBank/DDBJ databases. RN [3] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), ALTERNATIVE SPLICING, RP FUNCTION, SUBCELLULAR LOCATION, INDUCTION, AND TISSUE SPECIFICITY. RX PubMed=19706761; DOI=10.1158/0008-5472.CAN-09-0886; RA Lo H.W., Zhu H., Cao X., Aldrich A., Ali-Osman F.; RT "A novel splice variant of GLI1 that promotes glioblastoma cell RT migration and invasion."; RL Cancer Res. 69:6790-6798(2009). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=16541075; DOI=10.1038/nature04569; RA Scherer S.E., Muzny D.M., Buhay C.J., Chen R., Cree A., Ding Y., RA Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C., RA Hernandez J., Hodgson A.V., Hume J., Jackson A., Khan Z.M., RA Kovar-Smith C., Lewis L.R., Lozado R.J., Metzker M.L., RA Milosavljevic A., Miner G.R., Montgomery K.T., Morgan M.B., RA Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D., RA Lovering R.C., Wheeler D.A., Worley K.C., Yuan Y., Zhang Z., RA Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z., RA Clerc-Blankenburg K.P., Davis C., Delgado O., Dinh H.H., Draper H., RA Gonzalez-Garay M.L., Havlak P., Jackson L.R., Jacob L.S., Kelly S.H., RA Li L., Li Z., Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., RA Okwuonu G.O., Pasternak S., Perez L.M., Plopper F.J.H., Santibanez J., RA Shen H., Tabor P.E., Verduzco D., Waldron L., Wang Q., Williams G.A., RA Zhang J., Zhou J., Allen C.C., Amin A.G., Anyalebechi V., Bailey M., RA Barbaria J.A., Bimage K.E., Bryant N.P., Burch P.E., Burkett C.E., RA Burrell K.L., Calderon E., Cardenas V., Carter K., Casias K., RA Cavazos I., Cavazos S.R., Ceasar H., Chacko J., Chan S.N., Chavez D., RA Christopoulos C., Chu J., Cockrell R., Cox C.D., Dang M., RA Dathorne S.R., David R., Davis C.M., Davy-Carroll L., Deshazo D.R., RA Donlin J.E., D'Souza L., Eaves K.A., Egan A., Emery-Cohen A.J., RA Escotto M., Flagg N., Forbes L.D., Gabisi A.M., Garza M., Hamilton C., RA Henderson N., Hernandez O., Hines S., Hogues M.E., Huang M., RA Idlebird D.G., Johnson R., Jolivet A., Jones S., Kagan R., King L.M., RA Leal B., Lebow H., Lee S., LeVan J.M., Lewis L.C., London P., RA Lorensuhewa L.M., Loulseged H., Lovett D.A., Lucier A., Lucier R.L., RA Ma J., Madu R.C., Mapua P., Martindale A.D., Martinez E., Massey E., RA Mawhiney S., Meador M.G., Mendez S., Mercado C., Mercado I.C., RA Merritt C.E., Miner Z.L., Minja E., Mitchell T., Mohabbat F., RA Mohabbat K., Montgomery B., Moore N., Morris S., Munidasa M., RA Ngo R.N., Nguyen N.B., Nickerson E., Nwaokelemeh O.O., Nwokenkwo S., RA Obregon M., Oguh M., Oragunye N., Oviedo R.J., Parish B.J., RA Parker D.N., Parrish J., Parks K.L., Paul H.A., Payton B.A., Perez A., RA Perrin W., Pickens A., Primus E.L., Pu L.-L., Puazo M., Quiles M.M., RA Quiroz J.B., Rabata D., Reeves K., Ruiz S.J., Shao H., Sisson I., RA Sonaike T., Sorelle R.P., Sutton A.E., Svatek A.F., Svetz L.A., RA Tamerisa K.S., Taylor T.R., Teague B., Thomas N., Thorn R.D., RA Trejos Z.Y., Trevino B.K., Ukegbu O.N., Urban J.B., Vasquez L.I., RA Vera V.A., Villasana D.M., Wang L., Ward-Moore S., Warren J.T., RA Wei X., White F., Williamson A.L., Wleczyk R., Wooden H.S., RA Wooden S.H., Yen J., Yoon L., Yoon V., Zorrilla S.E., Nelson D., RA Kucherlapati R., Weinstock G., Gibbs R.A.; RT "The finished DNA sequence of human chromosome 12."; RL Nature 440:346-351(2006). RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RC TISSUE=Muscle; 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 RT project: the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [6] RP FUNCTION, SUBCELLULAR LOCATION, AND DNA-BINDING. RX PubMed=2105456; RA Kinzler K.W., Vogelstein B.; RT "The GLI gene encodes a nuclear protein which binds specific sequences RT in the human genome."; RL Mol. Cell. Biol. 10:634-642(1990). RN [7] RP FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH STK36 AND SUFU. RX PubMed=10806483; DOI=10.1038/35010610; RA Murone M., Luoh S.-L., Stone D., Li W., Gurney A., Armanini M., RA Grey C., 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 [8] RP FUNCTION, INTERACTION WITH ZIC1, AND SUBCELLULAR LOCATION. 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 [9] RP SUBCELLULAR LOCATION, TISSUE SPECIFICITY, PHOSPHORYLATION, AND RP FUNCTION. RX PubMed=19878745; DOI=10.1016/j.yexcr.2009.10.018; RA Maloverjan A., Piirsoo M., Michelson P., Kogerman P., Osterlund T.; RT "Identification of a novel serine/threonine kinase ULK3 as a positive RT regulator of Hedgehog pathway."; RL Exp. Cell Res. 316:627-637(2010). RN [10] RP ACETYLATION AT LYS-518. RX PubMed=20081843; DOI=10.1038/ncb2013; RA Canettieri G., Di Marcotullio L., Greco A., Coni S., Antonucci L., RA Infante P., Pietrosanti L., De Smaele E., Ferretti E., Miele E., RA Pelloni M., De Simone G., Pedone E.M., Gallinari P., Giorgi A., RA Steinkuhler C., Vitagliano L., Pedone C., Schinin M.E., Screpanti I., RA Gulino A.; RT "Histone deacetylase and Cullin3-REN(KCTD11) ubiquitin ligase RT interplay regulates Hedgehog signalling through Gli acetylation."; RL Nat. Cell Biol. 12:132-142(2010). RN [11] RP X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) OF 234-388 IN COMPLEX WITH DNA, RP AND DNA-BINDING. RX PubMed=8378770; DOI=10.1126/science.8378770; RA Pavletich N.P., Pabo C.O.; RT "Crystal structure of a five-finger GLI-DNA complex: new perspectives RT on zinc fingers."; RL Science 261:1701-1707(1993). RN [12] RP X-RAY CRYSTALLOGRAPHY (2.80 ANGSTROMS) OF 115-131 IN COMPLEX WITH RP SUFU, INTERACTION WITH SUFU, AND FUNCTION. RX PubMed=24311597; DOI=10.1107/S0907444913028473; RA Cherry A.L., Finta C., Karlstrom M., Jin Q., Schwend T., RA Astorga-Wells J., Zubarev R.A., Del Campo M., Criswell A.R., RA de Sanctis D., Jovine L., Toftgard R.; RT "Structural basis of SUFU-GLI interaction in human Hedgehog signalling RT regulation."; RL Acta Crystallogr. D 69:2563-2579(2013). RN [13] RP X-RAY CRYSTALLOGRAPHY (1.70 ANGSTROMS) OF 112-128 IN COMPLEX WITH RP SUFU, INTERACTION WITH SUFU, AND FUNCTION. RX PubMed=24217340; DOI=10.1038/ncomms3608; RA Zhang Y., Fu L., Qi X., Zhang Z., Xia Y., Jia J., Jiang J., Zhao Y., RA Wu G.; RT "Structural insight into the mutual recognition and regulation between RT Suppressor of Fused and Gli/Ci."; RL Nat. Commun. 4:2608-2608(2013). RN [14] RP VARIANTS ALA-884; ASP-933 AND GLN-1100. RX PubMed=10951255; DOI=10.1046/j.1523-1747.2000.00065.x; RA Wang X.Q., Chan N., Rothnagel J.A.; RT "Identification of polymorphic variants of the GLI1 oncogene."; RL J. Invest. Dermatol. 115:328-329(2000). RN [15] RP VARIANTS [LARGE SCALE ANALYSIS] ALA-210; ILE-514 AND GLN-817. RX PubMed=16959974; DOI=10.1126/science.1133427; RA Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D., RA Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., RA Buckhaults P., Farrell C., Meeh P., Markowitz S.D., Willis J., RA Dawson D., Willson J.K.V., Gazdar A.F., Hartigan J., Wu L., Liu C., RA Parmigiani G., Park B.H., Bachman K.E., Papadopoulos N., RA Vogelstein B., Kinzler K.W., Velculescu V.E.; RT "The consensus coding sequences of human breast and colorectal RT cancers."; RL Science 314:268-274(2006). CC -!- FUNCTION: Acts as a transcriptional activator (PubMed:19706761, CC PubMed:10806483, PubMed:19878745, PubMed:24311597, CC PubMed:24217340). Binds to the DNA consensus sequence 5'- CC GACCACCCA-3' (PubMed:2105456, PubMed:8378770, PubMed:24217340). CC May regulate the transcription of specific genes during normal CC development (PubMed:19706761). May play 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 (PubMed:19706761). Plays a role in cell proliferation CC and differentiation via its role in SHH signaling (Probable). CC {ECO:0000269|PubMed:10806483, ECO:0000269|PubMed:11238441, CC ECO:0000269|PubMed:19706761, ECO:0000269|PubMed:19878745, CC ECO:0000269|PubMed:2105456, ECO:0000269|PubMed:24217340, CC ECO:0000269|PubMed:24311597, ECO:0000269|PubMed:8378770, CC ECO:0000305}. CC -!- FUNCTION: Isoform 2: Acts as a transcriptional activator, but CC activates a different set of genes than isoform 1. Activates CC expression of CD24, unlike isoform 1. Mediates SHH signaling. CC Promotes cancer cell migration. {ECO:0000269|PubMed:19706761}. CC -!- SUBUNIT: Interacts with KIF7 (By similarity). Interacts with STK36 CC (PubMed:10806483). Interacts with ZIC1; the interaction enhances CC transcription activation (PubMed:11238441). Interacts with SUFU; CC this inhibits transcriptional activation by GLI1 (PubMed:10806483, CC PubMed:24311597, PubMed:24217340). {ECO:0000250|UniProtKB:P47806, CC ECO:0000269|PubMed:10806483, ECO:0000269|PubMed:11238441, CC ECO:0000269|PubMed:24217340, ECO:0000269|PubMed:24311597}. CC -!- INTERACTION: CC Q96CN9:GCC1; NbExp=3; IntAct=EBI-308084, EBI-746252; CC Q96J02:ITCH; NbExp=4; IntAct=EBI-308084, EBI-1564678; CC Q9QZS3-2:Numb (xeno); NbExp=4; IntAct=EBI-308084, EBI-3896014; CC P54646:PRKAA2; NbExp=3; IntAct=EBI-308084, EBI-1383852; CC P23443:RPS6KB1; NbExp=4; IntAct=EBI-308084, EBI-1775921; CC P23443-2:RPS6KB1; NbExp=2; IntAct=EBI-308084, EBI-6093204; CC Q9NRP7:STK36; NbExp=2; IntAct=EBI-308084, EBI-863797; CC Q9UMX1:SUFU; NbExp=21; IntAct=EBI-308084, EBI-740595; CC Q9UMX1-1:SUFU; NbExp=2; IntAct=EBI-308084, EBI-740615; CC Q9UMX1-2:SUFU; NbExp=4; IntAct=EBI-308084, EBI-740621; CC A1L4B6:TRIM42; NbExp=3; IntAct=EBI-308084, EBI-10172216; CC P40337-1:VHL; NbExp=2; IntAct=EBI-308084, EBI-3504450; CC P40337-3:VHL; NbExp=2; IntAct=EBI-308084, EBI-301270; CC P46684:Zic1 (xeno); NbExp=2; IntAct=EBI-308084, EBI-308006; CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:10806483, CC ECO:0000269|PubMed:19706761, ECO:0000269|PubMed:19878745}. Nucleus CC {ECO:0000269|PubMed:10806483, ECO:0000269|PubMed:11238441, CC ECO:0000269|PubMed:19706761, ECO:0000269|PubMed:19878745, CC ECO:0000269|PubMed:2105456}. Note=Tethered in the cytoplasm by CC binding to SUFU (PubMed:10806483). Activation and translocation to CC the nucleus is promoted by interaction with STK36 CC (PubMed:10806483). Phosphorylation by ULK3 may promote nuclear CC localization (PubMed:19878745). Translocation to the nucleus is CC promoted by interaction with ZIC1 (PubMed:11238441). CC {ECO:0000269|PubMed:10806483, ECO:0000269|PubMed:11238441, CC ECO:0000269|PubMed:19878745}. CC -!- SUBCELLULAR LOCATION: Isoform 2: Cytoplasm CC {ECO:0000269|PubMed:19706761}. Nucleus CC {ECO:0000269|PubMed:19706761}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=3; CC Name=1; CC IsoId=P08151-1; Sequence=Displayed; CC Name=2; Synonyms=tGLI1; CC IsoId=P08151-2; Sequence=VSP_042215; CC Note=Undetectable in normal cells but highly expressed in cancer CC cells.; CC Name=3; CC IsoId=P08151-3; Sequence=VSP_054829; CC Note=No experimental confirmation available. Gene prediction CC based on partial mRNA and EST data.; CC -!- TISSUE SPECIFICITY: Detected in testis (at protein level) CC (PubMed:2105456). Testis, myometrium and fallopian tube. Also CC expressed in the brain with highest expression in the cerebellum, CC optic nerve and olfactory tract (PubMed:19878745). Isoform 1 is CC detected in brain, spleen, pancreas, liver, kidney and placenta; CC isoform 2 is not detectable in these tissues (PubMed:19706761). CC {ECO:0000269|PubMed:19706761, ECO:0000269|PubMed:19878745, CC ECO:0000269|PubMed:2105456}. CC -!- INDUCTION: Isoform 1 and isoform 2 are amplified in glioblastoma CC cells. {ECO:0000269|PubMed:19706761}. CC -!- PTM: Phosphorylated in vitro by ULK3. CC {ECO:0000269|PubMed:19878745}. CC -!- PTM: Acetylation at Lys-518 down-regulates transcriptional CC activity. Deacetylated by HDAC1. {ECO:0000269|PubMed:20081843}. CC -!- SIMILARITY: Belongs to the GLI C2H2-type zinc-finger protein CC family. {ECO:0000305}. CC -!- SIMILARITY: Contains 5 C2H2-type zinc fingers. CC {ECO:0000255|PROSITE-ProRule:PRU00042}. CC -!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology CC and Haematology; CC URL="http://atlasgeneticsoncology.org/Genes/GLIID310ch12q13.html"; CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; X07384; CAA30297.1; -; mRNA. DR EMBL; AF316573; AAM13391.1; -; Genomic_DNA. DR EMBL; GQ890670; ACX35434.1; -; mRNA. DR EMBL; AC022506; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; BC013000; AAH13000.1; -; mRNA. DR CCDS; CCDS53806.1; -. [P08151-2] DR CCDS; CCDS53807.1; -. [P08151-3] DR CCDS; CCDS8940.1; -. [P08151-1] DR PIR; S00672; TVHUGL. DR RefSeq; NP_001153517.1; NM_001160045.1. [P08151-3] DR RefSeq; NP_001161081.1; NM_001167609.1. [P08151-2] DR RefSeq; NP_005260.1; NM_005269.2. [P08151-1] DR RefSeq; XP_005268856.1; XM_005268799.2. [P08151-3] DR RefSeq; XP_011536491.1; XM_011538189.1. [P08151-1] DR UniGene; Hs.632702; -. DR PDB; 2GLI; X-ray; 2.60 A; A=234-388. DR PDB; 4BLB; X-ray; 2.80 A; E/F/G/H=115-131. DR PDB; 4KMD; X-ray; 1.70 A; B=112-128. DR PDBsum; 2GLI; -. DR PDBsum; 4BLB; -. DR PDBsum; 4KMD; -. DR ProteinModelPortal; P08151; -. DR SMR; P08151; 234-388. DR BioGrid; 108997; 26. DR DIP; DIP-32536N; -. DR IntAct; P08151; 17. DR MINT; MINT-189932; -. DR STRING; 9606.ENSP00000228682; -. DR BindingDB; P08151; -. DR ChEMBL; CHEMBL5461; -. DR PhosphoSite; P08151; -. DR BioMuta; GLI1; -. DR DMDM; 121323; -. DR MaxQB; P08151; -. DR PaxDb; P08151; -. DR PRIDE; P08151; -. DR Ensembl; ENST00000228682; ENSP00000228682; ENSG00000111087. [P08151-1] DR Ensembl; ENST00000528467; ENSP00000434408; ENSG00000111087. [P08151-2] DR Ensembl; ENST00000543426; ENSP00000437607; ENSG00000111087. [P08151-3] DR Ensembl; ENST00000546141; ENSP00000441006; ENSG00000111087. [P08151-2] DR GeneID; 2735; -. DR KEGG; hsa:2735; -. DR UCSC; uc001snx.3; human. [P08151-1] DR UCSC; uc021qzi.1; human. [P08151-2] DR CTD; 2735; -. DR GeneCards; GLI1; -. DR H-InvDB; HIX0010767; -. DR HGNC; HGNC:4317; GLI1. DR HPA; CAB009460; -. DR HPA; HPA034585; -. DR MIM; 165220; gene. DR neXtProt; NX_P08151; -. DR PharmGKB; PA28720; -. DR eggNOG; KOG1721; Eukaryota. DR eggNOG; COG5048; LUCA. DR GeneTree; ENSGT00760000118771; -. DR HOGENOM; HOG000290688; -. DR HOVERGEN; HBG080668; -. DR InParanoid; P08151; -. DR KO; K16797; -. DR OMA; CPRLEHY; -. DR OrthoDB; EOG7X6KZ8; -. DR PhylomeDB; P08151; -. DR TreeFam; TF350216; -. DR Reactome; R-HSA-5610780; Degradation of GLI1 by the proteasome. DR Reactome; R-HSA-5610787; Hedgehog 'off' state. DR Reactome; R-HSA-5632684; Hedgehog 'on' state. DR Reactome; R-HSA-5635851; GLI proteins bind promoters of Hh responsive genes to promote transcription. DR SignaLink; P08151; -. DR EvolutionaryTrace; P08151; -. DR GeneWiki; GLI1; -. DR GenomeRNAi; 2735; -. DR NextBio; 10780; -. DR PRO; PR:P08151; -. DR Proteomes; UP000005640; Chromosome 12. DR Bgee; P08151; -. DR CleanEx; HS_GLI1; -. DR ExpressionAtlas; P08151; baseline and differential. DR Genevisible; P08151; HS. DR GO; GO:0005930; C:axoneme; IEA:Ensembl. DR GO; GO:0097546; C:ciliary base; TAS:Reactome. DR GO; GO:0097542; C:ciliary tip; TAS:Reactome. DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB. DR GO; GO:0005829; C:cytosol; IDA:UniProtKB. DR GO; GO:0043231; C:intracellular membrane-bounded organelle; IDA:HPA. DR GO; GO:0005654; C:nucleoplasm; IDA:HPA. DR GO; GO:0005634; C:nucleus; IDA:UniProtKB. DR GO; GO:0072372; C:primary cilium; IEA:Ensembl. DR GO; GO:0003682; F:chromatin binding; IDA:UniProtKB. DR GO; GO:0003677; F:DNA binding; IDA:MGI. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0043565; F:sequence-specific DNA binding; IDA:UniProtKB. DR GO; GO:0003705; F:transcription factor activity, RNA polymerase II distal enhancer sequence-specific binding; IEA:Ensembl. DR GO; GO:0044212; F:transcription regulatory region DNA binding; IDA:UniProtKB. DR GO; GO:0021696; P:cerebellar cortex morphogenesis; IEA:Ensembl. DR GO; GO:0048546; P:digestive tract morphogenesis; TAS:BHF-UCL. DR GO; GO:0009953; P:dorsal/ventral pattern formation; IEA:Ensembl. DR GO; GO:0009913; P:epidermal cell differentiation; IDA:UniProtKB. DR GO; GO:0030324; P:lung development; IEA:Ensembl. DR GO; GO:0090090; P:negative regulation of canonical Wnt signaling pathway; IMP:UniProtKB. DR GO; GO:0060032; P:notochord regression; IEA:Ensembl. DR GO; GO:0001649; P:osteoblast differentiation; IDA:UniProtKB. DR GO; GO:0021983; P:pituitary gland development; IEA:Ensembl. DR GO; GO:0030335; P:positive regulation of cell migration; IDA:UniProtKB. DR GO; GO:0008284; P:positive regulation of cell proliferation; IMP:UniProtKB. DR GO; GO:0045740; P:positive regulation of DNA replication; IDA:UniProtKB. DR GO; GO:0045880; P:positive regulation of smoothened signaling pathway; IDA:UniProtKB. DR GO; GO:0045944; P:positive regulation of transcription from RNA polymerase II promoter; IDA:UniProtKB. DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IDA:UniProtKB. DR GO; GO:0009954; P:proximal/distal pattern formation; IEA:Ensembl. DR GO; GO:0045667; P:regulation of osteoblast differentiation; IEA:Ensembl. DR GO; GO:0008589; P:regulation of smoothened signaling pathway; TAS:UniProtKB. DR GO; GO:0007224; P:smoothened signaling pathway; IDA:UniProtKB. DR GO; GO:0021938; P:smoothened signaling pathway involved in regulation of cerebellar granule cell precursor cell proliferation; IEA:Ensembl. DR GO; GO:0007283; P:spermatogenesis; IEA:Ensembl. DR GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-KW. DR GO; GO:0007418; P:ventral midline development; IEA:Ensembl. DR Gene3D; 3.30.160.60; -; 5. DR InterPro; IPR007087; Znf_C2H2. DR InterPro; IPR015880; Znf_C2H2-like. DR InterPro; IPR013087; Znf_C2H2/integrase_DNA-bd. DR SMART; SM00355; ZnF_C2H2; 5. DR PROSITE; PS00028; ZINC_FINGER_C2H2_1; 4. DR PROSITE; PS50157; ZINC_FINGER_C2H2_2; 5. PE 1: Evidence at protein level; KW 3D-structure; Acetylation; Activator; Alternative splicing; KW Complete proteome; Cytoplasm; Developmental protein; Differentiation; KW DNA-binding; Metal-binding; Nucleus; Phosphoprotein; Polymorphism; KW Proto-oncogene; Reference proteome; Repeat; Transcription; KW Transcription regulation; Zinc; Zinc-finger. FT CHAIN 1 1106 Zinc finger protein GLI1. FT /FTId=PRO_0000047197. FT ZN_FING 235 260 C2H2-type 1. {ECO:0000255|PROSITE- FT ProRule:PRU00042}. FT ZN_FING 268 295 C2H2-type 2. {ECO:0000255|PROSITE- FT ProRule:PRU00042}. FT ZN_FING 301 325 C2H2-type 3. {ECO:0000255|PROSITE- FT ProRule:PRU00042}. FT ZN_FING 331 356 C2H2-type 4. {ECO:0000255|PROSITE- FT ProRule:PRU00042}. FT ZN_FING 362 387 C2H2-type 5. {ECO:0000255|PROSITE- FT ProRule:PRU00042}. FT REGION 1 20 SNAG domain. {ECO:0000250}. FT REGION 120 124 Interaction with SUFU. FT {ECO:0000269|PubMed:24217340, FT ECO:0000269|PubMed:24311597}. FT REGION 283 291 Interaction with DNA. FT {ECO:0000269|PubMed:8378770}. FT REGION 345 350 Interaction with DNA. FT {ECO:0000269|PubMed:8378770}. FT REGION 375 381 Interaction with DNA. FT {ECO:0000269|PubMed:8378770}. FT COMPBIAS 1038 1055 Asp/Glu-rich (acidic). FT MOD_RES 518 518 N6-acetyllysine. FT {ECO:0000269|PubMed:20081843}. FT VAR_SEQ 1 128 Missing (in isoform 3). {ECO:0000305}. FT /FTId=VSP_054829. FT VAR_SEQ 34 74 Missing (in isoform 2). FT {ECO:0000303|PubMed:19706761}. FT /FTId=VSP_042215. FT VARIANT 210 210 P -> A (in a breast cancer sample; FT somatic mutation). FT {ECO:0000269|PubMed:16959974}. FT /FTId=VAR_035557. FT VARIANT 514 514 T -> I (in a breast cancer sample; FT somatic mutation). FT {ECO:0000269|PubMed:16959974}. FT /FTId=VAR_035558. FT VARIANT 817 817 E -> Q (in a breast cancer sample; FT somatic mutation). FT {ECO:0000269|PubMed:16959974}. FT /FTId=VAR_035559. FT VARIANT 884 884 D -> A. {ECO:0000269|PubMed:10951255}. FT /FTId=VAR_015114. FT VARIANT 933 933 G -> D (in dbSNP:rs2228224). FT {ECO:0000269|PubMed:10951255, FT ECO:0000269|Ref.2}. FT /FTId=VAR_015115. FT VARIANT 1012 1012 G -> V (in dbSNP:rs2229300). FT /FTId=VAR_052723. FT VARIANT 1100 1100 E -> Q (in dbSNP:rs2228226). FT {ECO:0000269|PubMed:10951255, FT ECO:0000269|Ref.2}. FT /FTId=VAR_015116. FT CONFLICT 1106 1106 A -> AS (in Ref. 3; ACX35434). FT {ECO:0000305}. FT STRAND 120 123 {ECO:0000244|PDB:4KMD}. FT HELIX 249 259 {ECO:0000244|PDB:2GLI}. FT STRAND 261 263 {ECO:0000244|PDB:2GLI}. FT TURN 276 279 {ECO:0000244|PDB:2GLI}. FT HELIX 285 291 {ECO:0000244|PDB:2GLI}. FT HELIX 293 296 {ECO:0000244|PDB:2GLI}. FT HELIX 315 324 {ECO:0000244|PDB:2GLI}. FT STRAND 341 346 {ECO:0000244|PDB:2GLI}. FT HELIX 349 354 {ECO:0000244|PDB:2GLI}. FT TURN 367 369 {ECO:0000244|PDB:2GLI}. FT STRAND 372 375 {ECO:0000244|PDB:2GLI}. FT HELIX 376 381 {ECO:0000244|PDB:2GLI}. FT TURN 382 384 {ECO:0000244|PDB:2GLI}. SQ SEQUENCE 1106 AA; 117904 MW; E29B11D1A6CD3D91 CRC64; MFNSMTPPPI SSYGEPCCLR PLPSQGAPSV GTEGLSGPPF CHQANLMSGP HSYGPARETN SCTEGPLFSS PRSAVKLTKK RALSISPLSD ASLDLQTVIR TSPSSLVAFI NSRCTSPGGS YGHLSIGTMS PSLGFPAQMN HQKGPSPSFG VQPCGPHDSA RGGMIPHPQS RGPFPTCQLK SELDMLVGKC REEPLEGDMS SPNSTGIQDP LLGMLDGRED LEREEKREPE SVYETDCRWD GCSQEFDSQE QLVHHINSEH IHGERKEFVC HWGGCSRELR PFKAQYMLVV HMRRHTGEKP HKCTFEGCRK SYSRLENLKT HLRSHTGEKP YMCEHEGCSK AFSNASDRAK HQNRTHSNEK PYVCKLPGCT KRYTDPSSLR KHVKTVHGPD AHVTKRHRGD GPLPRAPSIS TVEPKREREG GPIREESRLT VPEGAMKPQP SPGAQSSCSS DHSPAGSAAN TDSGVEMTGN AGGSTEDLSS LDEGPCIAGT GLSTLRRLEN LRLDQLHQLR PIGTRGLKLP SLSHTGTTVS RRVGPPVSLE RRSSSSSSIS SAYTVSRRSS LASPFPPGSP PENGASSLPG LMPAQHYLLR ARYASARGGG TSPTAASSLD RIGGLPMPPW RSRAEYPGYN PNAGVTRRAS DPAQAADRPA PARVQRFKSL GCVHTPPTVA GGGQNFDPYL PTSVYSPQPP SITENAAMDA RGLQEEPEVG TSMVGSGLNP YMDFPPTDTL GYGGPEGAAA EPYGARGPGS LPLGPGPPTN YGPNPCPQQA SYPDPTQETW GEFPSHSGLY PGPKALGGTY SQCPRLEHYG QVQVKPEQGC PVGSDSTGLA PCLNAHPSEG PPHPQPLFSH YPQPSPPQYL QSGPYTQPPP DYLPSEPRPC LDFDSPTHST GQLKAQLVCN YVQSQQELLW EGGGREDAPA QEPSYQSPKF LGGSQVSPSR AKAPVNTYGP GFGPNLPNHK SGSYPTPSPC HENFVVGANR ASHRAAAPPR LLPPLPTCYG PLKVGGTNPS CGHPEVGRLG GGPALYPPPE GQVCNPLDSL DLDNTQLDFV AILDEPQGLS PPPSHDQRGS SGHTPPPSGP PNMAVGNMSV LLRSLPGETE FLNSSA //