GenomeNet

Database: UniProt
Entry: P08151
LinkDB: P08151
Original site: P08151 
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   07-OCT-2020, entry version 223.
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; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   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 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, FUNCTION,
RP   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 migration
RT   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., Kovar-Smith C.,
RA   Lewis L.R., Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R.,
RA   Montgomery K.T., Morgan M.B., Nazareth L.V., Scott G., Sodergren E.,
RA   Song X.-Z., Steffen D., Lovering R.C., Wheeler D.A., Worley K.C., Yuan Y.,
RA   Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G.,
RA   Chen Z., Clerc-Blankenburg K.P., Davis C., Delgado O., Dinh H.H.,
RA   Draper H., Gonzalez-Garay M.L., Havlak P., Jackson L.R., Jacob L.S.,
RA   Kelly S.H., Li L., Li Z., Liu J., Liu W., Lu J., Maheshwari M.,
RA   Nguyen B.-V., Okwuonu G.O., Pasternak S., Perez L.M., Plopper F.J.H.,
RA   Santibanez J., Shen H., Tabor P.E., Verduzco D., Waldron L., Wang Q.,
RA   Williams G.A., Zhang J., Zhou J., Allen C.C., Amin A.G., Anyalebechi V.,
RA   Bailey M., Barbaria J.A., Bimage K.E., Bryant N.P., Burch P.E.,
RA   Burkett C.E., 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., Dathorne S.R.,
RA   David R., Davis C.M., Davy-Carroll L., Deshazo D.R., Donlin J.E.,
RA   D'Souza L., Eaves K.A., Egan A., Emery-Cohen A.J., Escotto M., Flagg N.,
RA   Forbes L.D., Gabisi A.M., Garza M., Hamilton C., Henderson N.,
RA   Hernandez O., Hines S., Hogues M.E., Huang M., Idlebird D.G., Johnson R.,
RA   Jolivet A., Jones S., Kagan R., King L.M., Leal B., Lebow H., Lee S.,
RA   LeVan J.M., Lewis L.C., London P., Lorensuhewa L.M., Loulseged H.,
RA   Lovett D.A., Lucier A., Lucier R.L., Ma J., Madu R.C., Mapua P.,
RA   Martindale A.D., Martinez E., Massey E., Mawhiney S., Meador M.G.,
RA   Mendez S., Mercado C., Mercado I.C., Merritt C.E., Miner Z.L., Minja E.,
RA   Mitchell T., Mohabbat F., Mohabbat K., Montgomery B., Moore N., Morris S.,
RA   Munidasa M., Ngo R.N., Nguyen N.B., Nickerson E., Nwaokelemeh O.O.,
RA   Nwokenkwo S., 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., Trejos Z.Y.,
RA   Trevino B.K., Ukegbu O.N., Urban J.B., Vasquez L.I., Vera V.A.,
RA   Villasana D.M., Wang L., Ward-Moore S., Warren J.T., Wei X., White F.,
RA   Williamson A.L., Wleczyk R., Wooden H.S., Wooden S.H., Yen J., Yoon L.,
RA   Yoon V., Zorrilla S.E., Nelson D., Kucherlapati R., Weinstock G.,
RA   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 project:
RT   the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [6]
RP   FUNCTION, SUBCELLULAR LOCATION, AND DNA-BINDING.
RX   PubMed=2105456; DOI=10.1128/mcb.10.2.634;
RA   Kinzler K.W., Vogelstein B.;
RT   "The GLI gene encodes a nuclear protein which binds specific sequences in
RT   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., 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   [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 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 interplay
RT   regulates Hedgehog signalling through Gli acetylation.";
RL   Nat. Cell Biol. 12:132-142(2010).
RN   [11]
RP   INTERACTION WITH SUFU.
RX   PubMed=28965847; DOI=10.1016/j.ajhg.2017.08.017;
RA   De Mori R., Romani M., D'Arrigo S., Zaki M.S., Lorefice E., Tardivo S.,
RA   Biagini T., Stanley V., Musaev D., Fluss J., Micalizzi A., Nuovo S.,
RA   Illi B., Chiapparini L., Di Marcotullio L., Issa M.Y., Anello D.,
RA   Casella A., Ginevrino M., Leggins A.S., Roosing S., Alfonsi R., Rosati J.,
RA   Schot R., Mancini G.M.S., Bertini E., Dobyns W.B., Mazza T., Gleeson J.G.,
RA   Valente E.M.;
RT   "Hypomorphic Recessive Variants in SUFU Impair the Sonic Hedgehog Pathway
RT   and Cause Joubert Syndrome with Cranio-facial and Skeletal Defects.";
RL   Am. J. Hum. Genet. 101:552-563(2017).
RN   [12]
RP   FUNCTION, INVOLVEMENT IN PAPA8, VARIANTS PAPA8 113-ARG--ALA-1106 DEL;
RP   644-GLN--ALA-1106 DEL AND 780-TRP--ALA-1106 DEL, AND CHARACTERIZATION OF
RP   VARIANT 780-TRP--ALA-1106 DEL.
RX   PubMed=28973407; DOI=10.1093/hmg/ddx335;
RA   Palencia-Campos A., Ullah A., Nevado J., Yildirim R., Unal E., Ciorraga M.,
RA   Barruz P., Chico L., Piceci-Sparascio F., Guida V., De Luca A.,
RA   Kayserili H., Ullah I., Burmeister M., Lapunzina P., Ahmad W.,
RA   Morales A.V., Ruiz-Perez V.L.;
RT   "GLI1 inactivation is associated with developmental phenotypes overlapping
RT   with Ellis-van Creveld syndrome.";
RL   Hum. Mol. Genet. 26:4556-4571(2017).
RN   [13]
RP   SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-1003, AND IDENTIFICATION BY MASS
RP   SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=28112733; DOI=10.1038/nsmb.3366;
RA   Hendriks I.A., Lyon D., Young C., Jensen L.J., Vertegaal A.C.,
RA   Nielsen M.L.;
RT   "Site-specific mapping of the human SUMO proteome reveals co-modification
RT   with phosphorylation.";
RL   Nat. Struct. Mol. Biol. 24:325-336(2017).
RN   [14]
RP   X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) OF 234-388 IN COMPLEX WITH DNA, AND
RP   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 on
RT   zinc fingers.";
RL   Science 261:1701-1707(1993).
RN   [15]
RP   X-RAY CRYSTALLOGRAPHY (2.80 ANGSTROMS) OF 115-131 IN COMPLEX WITH SUFU,
RP   INTERACTION WITH SUFU, AND FUNCTION.
RX   PubMed=24311597; DOI=10.1107/s0907444913028473;
RA   Cherry A.L., Finta C., Karlstrom M., Jin Q., Schwend T., Astorga-Wells J.,
RA   Zubarev R.A., Del Campo M., Criswell A.R., de Sanctis D., Jovine L.,
RA   Toftgard R.;
RT   "Structural basis of SUFU-GLI interaction in human Hedgehog signalling
RT   regulation.";
RL   Acta Crystallogr. D 69:2563-2579(2013).
RN   [16]
RP   X-RAY CRYSTALLOGRAPHY (1.70 ANGSTROMS) OF 112-128 IN COMPLEX WITH SUFU,
RP   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., 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   [17]
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   [18]
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., Buckhaults P.,
RA   Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V.,
RA   Gazdar A.F., Hartigan J., Wu L., Liu C., Parmigiani G., Park B.H.,
RA   Bachman K.E., Papadopoulos N., Vogelstein B., Kinzler K.W.,
RA   Velculescu V.E.;
RT   "The consensus coding sequences of human breast and colorectal cancers.";
RL   Science 314:268-274(2006).
RN   [19]
RP   VARIANT PPD1 GLN-506, AND INVOLVEMENT IN PPD1.
RX   PubMed=30620395; DOI=10.1111/cge.13495;
RA   Ullah A., Umair M., Majeed A.I., Abdullah Jan A., Ahmad W.;
RT   "A novel homozygous sequence variant in GLI1 underlies first case of
RT   autosomal recessive pre-axial polydactyly.";
RL   Clin. Genet. 95:540-541(2019).
CC   -!- FUNCTION: Acts as a transcriptional activator (PubMed:19706761,
CC       PubMed:10806483, PubMed:19878745, PubMed:24311597, PubMed:24217340).
CC       Binds to the DNA consensus sequence 5'-GACCACCCA-3' (PubMed:2105456,
CC       PubMed:8378770, PubMed:24217340). Regulates the transcription of
CC       specific genes during normal development (PubMed:19706761). Plays a
CC       role in craniofacial development and digital development, as well as
CC       development of the central nervous system and gastrointestinal tract.
CC       Mediates SHH signaling (PubMed:19706761, PubMed:28973407). Plays a role
CC       in cell proliferation and differentiation via its role in SHH signaling
CC       (PubMed:11238441, PubMed:28973407). {ECO:0000269|PubMed:10806483,
CC       ECO:0000269|PubMed:11238441, ECO:0000269|PubMed:19706761,
CC       ECO:0000269|PubMed:19878745, ECO:0000269|PubMed:2105456,
CC       ECO:0000269|PubMed:24217340, ECO:0000269|PubMed:24311597,
CC       ECO:0000269|PubMed:28973407, ECO:0000269|PubMed:8378770}.
CC   -!- FUNCTION: [Isoform 2]: Acts as a transcriptional activator, but
CC       activates a different set of genes than isoform 1. Activates expression
CC       of CD24, unlike isoform 1. Mediates SHH signaling. Promotes cancer cell
CC       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; this
CC       inhibits transcriptional activation by GLI1 (PubMed:10806483,
CC       PubMed:24311597, PubMed:24217340, PubMed:28965847).
CC       {ECO:0000250|UniProtKB:P47806, ECO:0000269|PubMed:10806483,
CC       ECO:0000269|PubMed:11238441, ECO:0000269|PubMed:24217340,
CC       ECO:0000269|PubMed:24311597, ECO:0000269|PubMed:28965847}.
CC   -!- INTERACTION:
CC       P08151; P29972: AQP1; NbExp=3; IntAct=EBI-308084, EBI-745213;
CC       P08151; Q8NEC5: CATSPER1; NbExp=3; IntAct=EBI-308084, EBI-744545;
CC       P08151; P53673: CRYBA4; NbExp=3; IntAct=EBI-308084, EBI-7519711;
CC       P08151; Q96CN9: GCC1; NbExp=3; IntAct=EBI-308084, EBI-746252;
CC       P08151; Q96J02: ITCH; NbExp=4; IntAct=EBI-308084, EBI-1564678;
CC       P08151; Q13526: PIN1; NbExp=3; IntAct=EBI-308084, EBI-714158;
CC       P08151; P54646: PRKAA2; NbExp=3; IntAct=EBI-308084, EBI-1383852;
CC       P08151; P23443: RPS6KB1; NbExp=4; IntAct=EBI-308084, EBI-1775921;
CC       P08151; P23443-2: RPS6KB1; NbExp=2; IntAct=EBI-308084, EBI-6093204;
CC       P08151; Q9NRP7: STK36; NbExp=2; IntAct=EBI-308084, EBI-863797;
CC       P08151; Q9UMX1: SUFU; NbExp=26; IntAct=EBI-308084, EBI-740595;
CC       P08151; Q9UMX1-1: SUFU; NbExp=2; IntAct=EBI-308084, EBI-740615;
CC       P08151; Q9UMX1-2: SUFU; NbExp=4; IntAct=EBI-308084, EBI-740621;
CC       P08151; Q8IWZ5: TRIM42; NbExp=3; IntAct=EBI-308084, EBI-5235829;
CC       P08151; P40337-1: VHL; NbExp=2; IntAct=EBI-308084, EBI-3504450;
CC       P08151; P40337-3: VHL; NbExp=2; IntAct=EBI-308084, EBI-301270;
CC       P08151; Q9QZS3-2: Numb; Xeno; NbExp=4; IntAct=EBI-308084, EBI-3896014;
CC       P08151; P46684: Zic1; Xeno; NbExp=2; IntAct=EBI-308084, EBI-308006;
CC       P08151-1; P41743: PRKCI; NbExp=3; IntAct=EBI-16038799, EBI-286199;
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 binding
CC       to SUFU (PubMed:10806483). Activation and translocation to the nucleus
CC       is promoted by interaction with STK36 (PubMed:10806483).
CC       Phosphorylation by ULK3 may promote nuclear localization
CC       (PubMed:19878745). Translocation to the nucleus is promoted by
CC       interaction with ZIC1 (PubMed:11238441). {ECO:0000269|PubMed:10806483,
CC       ECO:0000269|PubMed:11238441, ECO:0000269|PubMed:19878745}.
CC   -!- SUBCELLULAR LOCATION: [Isoform 2]: Cytoplasm
CC       {ECO:0000269|PubMed:19706761}. Nucleus {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       Name=3;
CC         IsoId=P08151-3; Sequence=VSP_054829;
CC   -!- TISSUE SPECIFICITY: Detected in testis (at protein level)
CC       (PubMed:2105456). Testis, myometrium and fallopian tube. Also expressed
CC       in the brain with highest expression in the cerebellum, optic nerve and
CC       olfactory tract (PubMed:19878745). Isoform 1 is detected in brain,
CC       spleen, pancreas, liver, kidney and placenta; isoform 2 is not
CC       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 cells.
CC       {ECO:0000269|PubMed:19706761}.
CC   -!- PTM: Phosphorylated in vitro by ULK3. {ECO:0000269|PubMed:19878745}.
CC   -!- PTM: Acetylation at Lys-518 down-regulates transcriptional activity.
CC       Deacetylated by HDAC1. {ECO:0000269|PubMed:20081843}.
CC   -!- DISEASE: Polydactyly, postaxial, A8 (PAPA8) [MIM:618123]: A form of
CC       postaxial polydactyly, a condition characterized by the occurrence of
CC       supernumerary digits in the upper and/or lower extremities. In
CC       postaxial polydactyly type A, the extra digit is well-formed and
CC       articulates with the fifth or a sixth metacarpal/metatarsal. PAPA8 is
CC       an autosomal recessive condition characterized by the presence of
CC       postaxial extra digits (hexadactyly) on the hands and/or the feet.
CC       {ECO:0000269|PubMed:28973407}. Note=The disease is caused by mutations
CC       affecting the gene represented in this entry.
CC   -!- DISEASE: Polydactyly, preaxial 1 (PPD1) [MIM:174400]: A form of
CC       polydactyly, a condition defined by the occurrence of supernumerary
CC       digits in the upper and/or lower extremities. Preaxial or radial
CC       polydactyly refers to the presence of extra digits on the radial side
CC       of the hand. PPD1 is an autosomal recessive form characterized by
CC       duplication of the distal phalanx of the thumb.
CC       {ECO:0000269|PubMed:30620395}. Note=The disease may be caused by
CC       mutations affecting the gene represented in this entry.
CC   -!- MISCELLANEOUS: [Isoform 2]: Undetectable in normal cells but highly
CC       expressed in cancer cells. {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the GLI C2H2-type zinc-finger protein family.
CC       {ECO:0000305}.
CC   -!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology and
CC       Haematology;
CC       URL="http://atlasgeneticsoncology.org/Genes/GLIID310ch12q13.html";
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_011536491.1; XM_011538189.2. [P08151-1]
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   PDB; 5OM0; X-ray; 3.20 A; A/B=637-645.
DR   PDBsum; 2GLI; -.
DR   PDBsum; 4BLB; -.
DR   PDBsum; 4KMD; -.
DR   PDBsum; 5OM0; -.
DR   SMR; P08151; -.
DR   BioGRID; 108997; 82.
DR   ComplexPortal; CPX-56; GLI1-SUFU complex.
DR   DIP; DIP-32536N; -.
DR   ELM; P08151; -.
DR   IntAct; P08151; 41.
DR   MINT; P08151; -.
DR   STRING; 9606.ENSP00000228682; -.
DR   BindingDB; P08151; -.
DR   ChEMBL; CHEMBL5461; -.
DR   iPTMnet; P08151; -.
DR   PhosphoSitePlus; P08151; -.
DR   BioMuta; GLI1; -.
DR   DMDM; 121323; -.
DR   EPD; P08151; -.
DR   jPOST; P08151; -.
DR   MassIVE; P08151; -.
DR   MaxQB; P08151; -.
DR   PaxDb; P08151; -.
DR   PeptideAtlas; P08151; -.
DR   PRIDE; P08151; -.
DR   ProteomicsDB; 27194; -.
DR   ProteomicsDB; 52074; -. [P08151-1]
DR   ProteomicsDB; 52075; -. [P08151-2]
DR   Antibodypedia; 4004; 784 antibodies.
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.4; human. [P08151-1]
DR   CTD; 2735; -.
DR   DisGeNET; 2735; -.
DR   EuPathDB; HostDB:ENSG00000111087.9; -.
DR   GeneCards; GLI1; -.
DR   HGNC; HGNC:4317; GLI1.
DR   HPA; ENSG00000111087; Low tissue specificity.
DR   MalaCards; GLI1; -.
DR   MIM; 165220; gene.
DR   MIM; 174400; phenotype.
DR   MIM; 618123; phenotype.
DR   neXtProt; NX_P08151; -.
DR   OpenTargets; ENSG00000111087; -.
DR   Orphanet; 289; Ellis Van Creveld syndrome.
DR   Orphanet; 93339; Polydactyly of a biphalangeal thumb.
DR   Orphanet; 93334; Postaxial polydactyly type A.
DR   Orphanet; 93335; Postaxial polydactyly type B.
DR   PharmGKB; PA28720; -.
DR   eggNOG; KOG1721; Eukaryota.
DR   GeneTree; ENSGT00940000160235; -.
DR   HOGENOM; CLU_003666_0_0_1; -.
DR   InParanoid; P08151; -.
DR   KO; K16797; -.
DR   OMA; CPQQVSY; -.
DR   OrthoDB; 135929at2759; -.
DR   PhylomeDB; P08151; -.
DR   TreeFam; TF350216; -.
DR   PathwayCommons; P08151; -.
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   SIGNOR; P08151; -.
DR   BioGRID-ORCS; 2735; 21 hits in 895 CRISPR screens.
DR   EvolutionaryTrace; P08151; -.
DR   GeneWiki; GLI1; -.
DR   GenomeRNAi; 2735; -.
DR   Pharos; P08151; Tchem.
DR   PRO; PR:P08151; -.
DR   Proteomes; UP000005640; Chromosome 12.
DR   RNAct; P08151; protein.
DR   Bgee; ENSG00000111087; Expressed in tibial nerve and 163 other tissues.
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:0005654; C:nucleoplasm; IDA:HPA.
DR   GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR   GO; GO:0003682; F:chromatin binding; IDA:UniProtKB.
DR   GO; GO:0003677; F:DNA binding; IDA:MGI.
DR   GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; IBA:GO_Central.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0008017; F:microtubule binding; IEA:Ensembl.
DR   GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; IEA:Ensembl.
DR   GO; GO:0000977; F:RNA polymerase II transcription regulatory region sequence-specific DNA binding; IDA:MGI.
DR   GO; GO:0043565; F:sequence-specific DNA binding; IDA:UniProtKB.
DR   GO; GO:0000976; F:transcription regulatory region sequence-specific DNA binding; IDA:UniProtKB.
DR   GO; GO:0060070; P:canonical Wnt signaling pathway; IEA:Ensembl.
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:0097421; P:liver regeneration; IEA:Ensembl.
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:0060045; P:positive regulation of cardiac muscle cell proliferation; IDA:BHF-UCL.
DR   GO; GO:1902808; P:positive regulation of cell cycle G1/S phase transition; IDA:BHF-UCL.
DR   GO; GO:0030335; P:positive regulation of cell migration; IDA:UniProtKB.
DR   GO; GO:0008284; P:positive regulation of cell population 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 by RNA polymerase II; IDA:UniProtKB.
DR   GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IDA:UniProtKB.
DR   GO; GO:0030850; P:prostate gland development; IEA:Ensembl.
DR   GO; GO:0009954; P:proximal/distal pattern formation; IEA:Ensembl.
DR   GO; GO:2000345; P:regulation of hepatocyte proliferation; 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:0009611; P:response to wounding; IEA:Ensembl.
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:0007418; P:ventral midline development; IEA:Ensembl.
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; 1.
DR   PANTHER; PTHR45718:SF2; PTHR45718:SF2; 1.
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   3D-structure; Acetylation; Activator; Alternative splicing; Cytoplasm;
KW   Developmental protein; Differentiation; Disease mutation; DNA-binding;
KW   Isopeptide bond; Metal-binding; Nucleus; Phosphoprotein; Polymorphism;
KW   Proto-oncogene; Reference proteome; Repeat; Transcription;
KW   Transcription regulation; Ubl conjugation; Zinc; Zinc-finger.
FT   CHAIN           1..1106
FT                   /note="Zinc finger protein GLI1"
FT                   /id="PRO_0000047197"
FT   ZN_FING         235..260
FT                   /note="C2H2-type 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         268..295
FT                   /note="C2H2-type 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         301..325
FT                   /note="C2H2-type 3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         331..356
FT                   /note="C2H2-type 4"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         362..387
FT                   /note="C2H2-type 5"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   REGION          1..20
FT                   /note="SNAG domain"
FT                   /evidence="ECO:0000250"
FT   REGION          120..124
FT                   /note="Interaction with SUFU"
FT                   /evidence="ECO:0000269|PubMed:24217340,
FT                   ECO:0000269|PubMed:24311597"
FT   REGION          283..291
FT                   /note="Interaction with DNA"
FT                   /evidence="ECO:0000269|PubMed:8378770"
FT   REGION          345..350
FT                   /note="Interaction with DNA"
FT                   /evidence="ECO:0000269|PubMed:8378770"
FT   REGION          375..381
FT                   /note="Interaction with DNA"
FT                   /evidence="ECO:0000269|PubMed:8378770"
FT   COMPBIAS        1038..1055
FT                   /note="Asp/Glu-rich (acidic)"
FT   MOD_RES         518
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000269|PubMed:20081843"
FT   CROSSLNK        1003
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0000244|PubMed:28112733"
FT   VAR_SEQ         1..128
FT                   /note="Missing (in isoform 3)"
FT                   /evidence="ECO:0000305"
FT                   /id="VSP_054829"
FT   VAR_SEQ         34..74
FT                   /note="Missing (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:19706761"
FT                   /id="VSP_042215"
FT   VARIANT         113..1106
FT                   /note="Missing (in PAPA8)"
FT                   /evidence="ECO:0000269|PubMed:28973407"
FT                   /id="VAR_081480"
FT   VARIANT         210
FT                   /note="P -> A (in a breast cancer sample; somatic
FT                   mutation)"
FT                   /evidence="ECO:0000269|PubMed:16959974"
FT                   /id="VAR_035557"
FT   VARIANT         506
FT                   /note="L -> Q (in PPD1; unknown pathological significance;
FT                   dbSNP:rs753690500)"
FT                   /evidence="ECO:0000269|PubMed:30620395"
FT                   /id="VAR_082590"
FT   VARIANT         514
FT                   /note="T -> I (in a breast cancer sample; somatic
FT                   mutation)"
FT                   /evidence="ECO:0000269|PubMed:16959974"
FT                   /id="VAR_035558"
FT   VARIANT         644..1106
FT                   /note="Missing (in PAPA8)"
FT                   /evidence="ECO:0000269|PubMed:28973407"
FT                   /id="VAR_081481"
FT   VARIANT         780..1106
FT                   /note="Missing (in PAPA8; decreased transcriptional
FT                   activity; reduced expression of the GLI1 target PTCH1
FT                   observed in patient fibroblasts after chemical induction of
FT                   the hedgehog pathway)"
FT                   /evidence="ECO:0000269|PubMed:28973407"
FT                   /id="VAR_081482"
FT   VARIANT         817
FT                   /note="E -> Q (in a breast cancer sample; somatic
FT                   mutation)"
FT                   /evidence="ECO:0000269|PubMed:16959974"
FT                   /id="VAR_035559"
FT   VARIANT         884
FT                   /note="D -> A"
FT                   /evidence="ECO:0000269|PubMed:10951255"
FT                   /id="VAR_015114"
FT   VARIANT         933
FT                   /note="G -> D (in dbSNP:rs2228224)"
FT                   /evidence="ECO:0000269|PubMed:10951255, ECO:0000269|Ref.2"
FT                   /id="VAR_015115"
FT   VARIANT         1012
FT                   /note="G -> V (in dbSNP:rs2229300)"
FT                   /id="VAR_052723"
FT   VARIANT         1100
FT                   /note="E -> Q (in dbSNP:rs2228226)"
FT                   /evidence="ECO:0000269|PubMed:10951255, ECO:0000269|Ref.2"
FT                   /id="VAR_015116"
FT   CONFLICT        1106
FT                   /note="A -> AS (in Ref. 3; ACX35434)"
FT                   /evidence="ECO:0000305"
FT   STRAND          120..123
FT                   /evidence="ECO:0000244|PDB:4KMD"
FT   HELIX           249..259
FT                   /evidence="ECO:0000244|PDB:2GLI"
FT   STRAND          261..263
FT                   /evidence="ECO:0000244|PDB:2GLI"
FT   TURN            276..279
FT                   /evidence="ECO:0000244|PDB:2GLI"
FT   HELIX           285..291
FT                   /evidence="ECO:0000244|PDB:2GLI"
FT   HELIX           293..296
FT                   /evidence="ECO:0000244|PDB:2GLI"
FT   HELIX           315..324
FT                   /evidence="ECO:0000244|PDB:2GLI"
FT   STRAND          341..346
FT                   /evidence="ECO:0000244|PDB:2GLI"
FT   HELIX           349..354
FT                   /evidence="ECO:0000244|PDB:2GLI"
FT   TURN            367..369
FT                   /evidence="ECO:0000244|PDB:2GLI"
FT   STRAND          372..375
FT                   /evidence="ECO:0000244|PDB:2GLI"
FT   HELIX           376..381
FT                   /evidence="ECO:0000244|PDB:2GLI"
FT   TURN            382..384
FT                   /evidence="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
//
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