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Transcriptional activator GLI3 (GLI3 form of 190 kDa) (GLI3-190) (GLI3 full length protein) (GLI3FL) [Cleaved into: Transcriptional repressor GLI3R (GLI3 C-terminally truncated form) (GLI3 form of 83 kDa) (GLI3-83)]

 GLI3_HUMAN              Reviewed;        1580 AA.
P10071; A4D1W1; O75219; Q17RW4; Q75MT0; Q75MU9; Q9UDT5; Q9UJ39;
01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
24-NOV-2009, sequence version 6.
22-NOV-2017, entry version 191.
RecName: Full=Transcriptional activator GLI3;
AltName: Full=GLI3 form of 190 kDa;
Short=GLI3-190;
AltName: Full=GLI3 full-length protein;
Short=GLI3FL;
Contains:
RecName: Full=Transcriptional repressor GLI3R;
AltName: Full=GLI3 C-terminally truncated form;
AltName: Full=GLI3 form of 83 kDa;
Short=GLI3-83;
Name=GLI3;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA], AND VARIANTS ALA-183 AND LEU-998.
PubMed=2118997; DOI=10.1128/MCB.10.10.5408;
Ruppert J.M., Vogelstein B., Arheden K., Kinzler K.W.;
"GLI3 encodes a 190-kilodalton protein with multiple regions of GLI
similarity.";
Mol. Cell. Biol. 10:5408-5415(1990).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANTS GCPS GLY-515; TYR-520 AND
MET-808, AND VARIANTS ALA-183; GLU-440; LEU-998 AND CYS-1537.
PubMed=10441342; DOI=10.1093/hmg/8.9.1769;
Kalff-Suske M., Wild A., Topp J., Wessling M., Jacobsen E.-M.,
Bornholdt D., Engel H., Heuer H., Aalfs C.M., Ausems M.G.E.M.,
Barone R., Herzog A., Heutink P., Homfray T., Gillessen-Kaesbach G.,
Koenig R., Kunze J., Meinecke P., Mueller D., Rizzo R., Strenge S.,
Superti-Furga A., Grzeschik K.-H.;
"Point mutations throughout the GLI3 gene cause Greig
cephalopolysyndactylysyndrome.";
Hum. Mol. Genet. 8:1769-1777(1999).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=12853948; DOI=10.1038/nature01782;
Hillier L.W., Fulton R.S., Fulton L.A., Graves T.A., Pepin K.H.,
Wagner-McPherson C., Layman D., Maas J., Jaeger S., Walker R.,
Wylie K., Sekhon M., Becker M.C., O'Laughlin M.D., Schaller M.E.,
Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Cordes M., Du H.,
Sun H., Edwards J., Bradshaw-Cordum H., Ali J., Andrews S., Isak A.,
Vanbrunt A., Nguyen C., Du F., Lamar B., Courtney L., Kalicki J.,
Ozersky P., Bielicki L., Scott K., Holmes A., Harkins R., Harris A.,
Strong C.M., Hou S., Tomlinson C., Dauphin-Kohlberg S.,
Kozlowicz-Reilly A., Leonard S., Rohlfing T., Rock S.M.,
Tin-Wollam A.-M., Abbott A., Minx P., Maupin R., Strowmatt C.,
Latreille P., Miller N., Johnson D., Murray J., Woessner J.P.,
Wendl M.C., Yang S.-P., Schultz B.R., Wallis J.W., Spieth J.,
Bieri T.A., Nelson J.O., Berkowicz N., Wohldmann P.E., Cook L.L.,
Hickenbotham M.T., Eldred J., Williams D., Bedell J.A., Mardis E.R.,
Clifton S.W., Chissoe S.L., Marra M.A., Raymond C., Haugen E.,
Gillett W., Zhou Y., James R., Phelps K., Iadanoto S., Bubb K.,
Simms E., Levy R., Clendenning J., Kaul R., Kent W.J., Furey T.S.,
Baertsch R.A., Brent M.R., Keibler E., Flicek P., Bork P., Suyama M.,
Bailey J.A., Portnoy M.E., Torrents D., Chinwalla A.T., Gish W.R.,
Eddy S.R., McPherson J.D., Olson M.V., Eichler E.E., Green E.D.,
Waterston R.H., Wilson R.K.;
"The DNA sequence of human chromosome 7.";
Nature 424:157-164(2003).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=12690205; DOI=10.1126/science.1083423;
Scherer S.W., Cheung J., MacDonald J.R., Osborne L.R., Nakabayashi K.,
Herbrick J.-A., Carson A.R., Parker-Katiraee L., Skaug J., Khaja R.,
Zhang J., Hudek A.K., Li M., Haddad M., Duggan G.E., Fernandez B.A.,
Kanematsu E., Gentles S., Christopoulos C.C., Choufani S.,
Kwasnicka D., Zheng X.H., Lai Z., Nusskern D.R., Zhang Q., Gu Z.,
Lu F., Zeesman S., Nowaczyk M.J., Teshima I., Chitayat D., Shuman C.,
Weksberg R., Zackai E.H., Grebe T.A., Cox S.R., Kirkpatrick S.J.,
Rahman N., Friedman J.M., Heng H.H.Q., Pelicci P.G., Lo-Coco F.,
Belloni E., Shaffer L.G., Pober B., Morton C.C., Gusella J.F.,
Bruns G.A.P., Korf B.R., Quade B.J., Ligon A.H., Ferguson H.,
Higgins A.W., Leach N.T., Herrick S.R., Lemyre E., Farra C.G.,
Kim H.-G., Summers A.M., Gripp K.W., Roberts W., Szatmari P.,
Winsor E.J.T., Grzeschik K.-H., Teebi A., Minassian B.A., Kere J.,
Armengol L., Pujana M.A., Estivill X., Wilson M.D., Koop B.F.,
Tosi S., Moore G.E., Boright A.P., Zlotorynski E., Kerem B.,
Kroisel P.M., Petek E., Oscier D.G., Mould S.J., Doehner H.,
Doehner K., Rommens J.M., Vincent J.B., Venter J.C., Li P.W.,
Mural R.J., Adams M.D., Tsui L.-C.;
"Human chromosome 7: DNA sequence and biology.";
Science 300:767-772(2003).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANTS ALA-183 AND
LEU-998.
TISSUE=Cerebellum;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[6]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 500-549.
PubMed=2850480; DOI=10.1128/MCB.8.8.3104;
Ruppert J.M., Kinzler K.W., Wong A.J., Bigner S.H., Kao F.T.,
Law M.L., Seuanez H.N., O'Brien S.J., Vogelstein B.;
"The GLI-Kruppel family of human genes.";
Mol. Cell. Biol. 8:3104-3113(1988).
[7]
FUNCTION, PROTEOLYTIC PROCESSING, PHOSPHORYLATION AT SER-849; SER-865;
SER-877; SER-907; SER-980 AND SER-1006, AND MUTAGENESIS OF SER-849;
SER-865; SER-877; SER-907; SER-980 AND SER-1006.
PubMed=10693759; DOI=10.1016/S0092-8674(00)80678-9;
Wang B., Fallon J.F., Beachy P.A.;
"Hedgehog-regulated processing of Gli3 produces an anterior/posterior
repressor gradient in the developing vertebrate limb.";
Cell 100:423-434(2000).
[8]
FUNCTION, INTERACTION WITH ZIC1, AND SUBCELLULAR LOCATION.
PubMed=11238441; DOI=10.1074/jbc.C000773200;
Koyabu Y., Nakata K., Mizugishi K., Aruga J., Mikoshiba K.;
"Physical and functional interactions between Zic and Gli proteins.";
J. Biol. Chem. 276:6889-6892(2001).
[9]
PROTEOLYTIC PROCESSING, PHOSPHORYLATION, INTERACTION WITH BTRC,
UBIQUITINATION AT LYS-773; LYS-779; LYS-784 AND LYS-800, AND
MUTAGENESIS OF LYS-773; LYS-779; LYS-784; LYS-800; SER-849; SER-855;
SER-856; SER-861; SER-864; SER-873; SER-877; SER-903 AND SER-907.
PubMed=16705181; DOI=10.1128/MCB.02183-05;
Tempe D., Casas M., Karaz S., Blanchet-Tournier M.F., Concordet J.P.;
"Multisite protein kinase A and glycogen synthase kinase 3beta
phosphorylation leads to Gli3 ubiquitination by SCFbetaTrCP.";
Mol. Cell. Biol. 26:4316-4326(2006).
[10]
PROTEOLYTIC PROCESSING, PHOSPHORYLATION, POLYUBIQUITINATION, AND
INTERACTION WITH BTRC.
PubMed=16371461; DOI=10.1073/pnas.0509927103;
Wang B., Li Y.;
"Evidence for the direct involvement of {beta}TrCP in Gli3 protein
processing.";
Proc. Natl. Acad. Sci. U.S.A. 103:33-38(2006).
[11]
PHOSPHORYLATION.
PubMed=18455992; DOI=10.1016/j.cell.2008.02.047;
Varjosalo M., Bjorklund M., Cheng F., Syvanen H., Kivioja T.,
Kilpinen S., Sun Z., Kallioniemi O., Stunnenberg H.G., He W.W.,
Ojala P., Taipale J.;
"Application of active and kinase-deficient kinome collection for
identification of kinases regulating hedgehog signaling.";
Cell 133:537-548(2008).
[12]
FUNCTION, AND INTERACTION WITH ZIC3.
PubMed=17764085; DOI=10.1002/humu.20606;
Zhu L., Zhou G., Poole S., Belmont J.W.;
"Characterization of the interactions of human ZIC3 mutants with
GLI3.";
Hum. Mutat. 29:99-105(2008).
[13]
ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19413330; DOI=10.1021/ac9004309;
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,
Mohammed S.;
"Lys-N and trypsin cover complementary parts of the phosphoproteome in
a refined SCX-based approach.";
Anal. Chem. 81:4493-4501(2009).
[14]
SUBCELLULAR LOCATION, AND 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).
[15]
INTERACTION WITH TRPS1.
PubMed=19389374; DOI=10.1016/j.ydbio.2009.01.012;
Wuelling M., Kaiser F.J., Buelens L.A., Braunholz D., Shivdasani R.A.,
Depping R., Vortkamp A.;
"Trps1, a regulator of chondrocyte proliferation and differentiation,
interacts with the activator form of Gli3.";
Dev. Biol. 328:40-53(2009).
[16]
PHOSPHORYLATION.
PubMed=19878745; DOI=10.1016/j.yexcr.2009.10.018;
Maloverjan A., Piirsoo M., Michelson P., Kogerman P., Osterlund T.;
"Identification of a novel serine/threonine kinase ULK3 as a positive
regulator of Hedgehog pathway.";
Exp. Cell Res. 316:627-637(2010).
[17]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-664, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21406692; DOI=10.1126/scisignal.2001570;
Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J.,
Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V.,
Blagoev B.;
"System-wide temporal characterization of the proteome and
phosphoproteome of human embryonic stem cell differentiation.";
Sci. Signal. 4:RS3-RS3(2011).
[18]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-664, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=23186163; DOI=10.1021/pr300630k;
Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
Mohammed S.;
"Toward a comprehensive characterization of a human cancer cell
phosphoproteome.";
J. Proteome Res. 12:260-271(2013).
[19]
SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-438; LYS-462 AND LYS-779,
AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=28112733; DOI=10.1038/nsmb.3366;
Hendriks I.A., Lyon D., Young C., Jensen L.J., Vertegaal A.C.,
Nielsen M.L.;
"Site-specific mapping of the human SUMO proteome reveals co-
modification with phosphorylation.";
Nat. Struct. Mol. Biol. 24:325-336(2017).
[20]
X-RAY CRYSTALLOGRAPHY (2.80 ANGSTROMS) OF 328-344 IN COMPLEX WITH
SUFU, AND INTERACTION WITH SUFU.
PubMed=24311597; DOI=10.1107/S0907444913028473;
Cherry A.L., Finta C., Karlstrom M., Jin Q., Schwend T.,
Astorga-Wells J., Zubarev R.A., Del Campo M., Criswell A.R.,
de Sanctis D., Jovine L., Toftgard R.;
"Structural basis of SUFU-GLI interaction in human Hedgehog signalling
regulation.";
Acta Crystallogr. D 69:2563-2579(2013).
[21]
VARIANT GCPS SER-707.
PubMed=9302279; DOI=10.1093/hmg/6.11.1979;
Wild A., Kalff-Suske M., Vortkamp A., Bornholdt D., Koenig R.,
Grzeschik K.-H.;
"Point mutations in human GLI3 cause Greig syndrome.";
Hum. Mol. Genet. 6:1979-1984(1997).
[22]
VARIANT PAPA1 ARG-727, VARIANT PAPB ARG-727, INVOLVEMENT IN PAPA1,
INVOLVEMENT IN PAPB, INVOLVEMENT IN PHS, AND INVOLVEMENT IN POP4.
PubMed=10441570; DOI=10.1086/302557;
Radhakrishna U., Bornholdt D., Scott H.S., Patel U.C., Rossier C.,
Engel H., Bottani A., Chandal D., Blouin J.-L., Solanki J.V.,
Grzeschik K.-H., Antonarakis S.E.;
"The phenotypic spectrum of GLI3 morphopathies includes autosomal
dominant preaxial polydactyly type-IV and postaxial polydactyly type-
A/B; no phenotype prediction from the position of GLI3 mutations.";
Am. J. Hum. Genet. 65:645-655(1999).
[23]
VARIANT GCPS PRO-934.
PubMed=12414818; DOI=10.1136/jmg.39.11.804;
Elson E., Perveen R., Donnai D., Wall S., Black G.C.M.;
"De novo GLI3 mutation in acrocallosal syndrome: broadening the
phenotypic spectrum of GLI3 defects and overlap with murine models.";
J. Med. Genet. 39:804-806(2002).
[24]
VARIANT GCPS TRP-625.
PubMed=12794692; DOI=10.1002/ajmg.a.20018;
Debeer P., Peeters H., Driess S., De Smet L., Freese K., Matthijs G.,
Bornholdt D., Devriendt K., Grzeschik K.-H., Fryns J.-P.,
Kalff-Suske M.;
"Variable phenotype in Greig cephalopolysyndactyly syndrome: clinical
and radiological findings in 4 independent families and 3 sporadic
cases with identified GLI3 mutations.";
Am. J. Med. Genet. A 120:49-58(2003).
[25]
VARIANTS [LARGE SCALE ANALYSIS] LEU-169 AND PRO-1304.
PubMed=16959974; DOI=10.1126/science.1133427;
Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D.,
Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S.,
Buckhaults P., Farrell C., Meeh P., Markowitz S.D., Willis J.,
Dawson D., Willson J.K.V., Gazdar A.F., Hartigan J., Wu L., Liu C.,
Parmigiani G., Park B.H., Bachman K.E., Papadopoulos N.,
Vogelstein B., Kinzler K.W., Velculescu V.E.;
"The consensus coding sequences of human breast and colorectal
cancers.";
Science 314:268-274(2006).
-!- FUNCTION: Has a dual function as a transcriptional activator and a
repressor of the sonic hedgehog (Shh) pathway, and plays a role in
limb development. The full-length GLI3 form (GLI3FL) after
phosphorylation and nuclear translocation, acts as an activator
(GLI3A) while GLI3R, its C-terminally truncated form, acts as a
repressor. A proper balance between the GLI3 activator and the
repressor GLI3R, rather than the repressor gradient itself or the
activator/repressor ratio gradient, specifies limb digit number
and identity. In concert with TRPS1, plays a role in regulating
the size of the zone of distal chondrocytes, in restricting the
zone of PTHLH expression in distal cells and in activating
chondrocyte proliferation. Binds to the minimal GLI-consensus
sequence 5'-GGGTGGTC-3'. {ECO:0000269|PubMed:10693759,
ECO:0000269|PubMed:11238441, ECO:0000269|PubMed:17764085}.
-!- SUBUNIT: The full-length GLI3 form (GLI3FL) interacts with SUFU
and this interaction regulates the formation of either repressor
or activator forms of GLI3. Its association with SUFU is regulated
by Hh signaling and dissociation of the SUFU-GLI3 interaction
requires the presence of the ciliary motor KIF3A (By similarity).
Interacts with KIF7. The activator form of GLI3 (GLI3A) but not
the repressor form (GLI3R) can interact with TRPS1. The
phosphorylated form interacts with BTRC. Interacts with ZIC1.
Interacts with ZIC3 (via C2H2-type domains 3, 4 and 5); the
interaction enhances its transcriptional activity. {ECO:0000250,
ECO:0000269|PubMed:11238441, ECO:0000269|PubMed:16371461,
ECO:0000269|PubMed:16705181, ECO:0000269|PubMed:17764085,
ECO:0000269|PubMed:19389374, ECO:0000269|PubMed:19592253,
ECO:0000269|PubMed:24311597}.
-!- INTERACTION:
Q6ZWS8:Spop (xeno); NbExp=2; IntAct=EBI-308055, EBI-7128920;
Q9NRP7:STK36; NbExp=2; IntAct=EBI-308055, EBI-863797;
Q9UMX1:SUFU; NbExp=3; IntAct=EBI-308055, EBI-740595;
P46684:Zic1 (xeno); NbExp=2; IntAct=EBI-308055, EBI-308006;
Q62520:Zic2 (xeno); NbExp=2; IntAct=EBI-308055, EBI-308076;
-!- SUBCELLULAR LOCATION: Nucleus. Cytoplasm. Cell projection, cilium.
Note=GLI3FL is localized predominantly in the cytoplasm while
GLI3R resides mainly in the nucleus. Ciliary accumulation requires
the presence of KIF7 and SMO. Translocation to the nucleus is
promoted by interaction with ZIC1.
-!- TISSUE SPECIFICITY: Is expressed in a wide variety of normal adult
tissues, including lung, colon, spleen, placenta, testis, and
myometrium.
-!- PTM: Phosphorylated on multiple sites by protein kinase A (PKA)
and phosphorylation by PKA primes further phosphorylation by CK1
and GSK3. Phosphorylated by DYRK2 (in vitro). Phosphorylation is
essential for its proteolytic processing.
-!- PTM: Transcriptional repressor GLI3R, a C-terminally truncated
form, is generated from the full-length GLI3 protein (GLI3FL/GLI3-
190) through proteolytic processing. This process requires PKA-
primed phosphorylation of GLI3, ubiquitination of GLI3 and the
presence of BTRC. GLI3FL is complexed with SUFU in the cytoplasm
and is maintained in a neutral state. Without the Hh signal, the
SUFU-GLI3 complex is recruited to cilia, leading to the efficient
processing of GLI3FL into GLI3R. GLI3R formation leads to its
dissociation from SUFU, allowing it to translocate into the
nucleus, and repress Hh target genes. When Hh signaling is
initiated, SUFU dissociates from GLI3FL and this has two
consequences. First, GLI3R production is halted. Second, free
GLI3FL translocates to the nucleus, where it is phosphorylated,
destabilized, and converted to a transcriptional activator
(GLI3A). Phosphorylated in vitro by ULK3.
{ECO:0000269|PubMed:16371461, ECO:0000269|PubMed:16705181}.
-!- DISEASE: Greig cephalo-poly-syndactyly syndrome (GCPS)
[MIM:175700]: Autosomal dominant disorder affecting limb and
craniofacial development. It is characterized by pre- and
postaxial polydactyly, syndactyly of fingers and toes,
macrocephaly and hypertelorism. {ECO:0000269|PubMed:10441342,
ECO:0000269|PubMed:12414818, ECO:0000269|PubMed:12794692,
ECO:0000269|PubMed:9302279}. Note=The disease is caused by
mutations affecting the gene represented in this entry.
-!- DISEASE: Pallister-Hall syndrome (PHS) [MIM:146510]: An autosomal
dominant disorder characterized by a wide range of clinical
manifestations. Clinical features include hypothalamic hamartoma,
pituitary dysfunction, central or postaxial polydactyly, and
syndactyly. Malformations are frequent in the viscera, e.g. anal
atresia, bifid uvula, congenital heart malformations, pulmonary or
renal dysplasia. {ECO:0000269|PubMed:10441570}. Note=The disease
is caused by mutations affecting the gene represented in this
entry.
-!- DISEASE: Polydactyly, postaxial A1 (PAPA1) [MIM:174200]: A
condition characterized by the occurrence of supernumerary digits
in the upper and/or lower extremities. In postaxial polydactyly
type A, the extra digit is well-formed and articulates with the
fifth or a sixth metacarpal/metatarsal.
{ECO:0000269|PubMed:10441570}. Note=The disease is caused by
mutations affecting the gene represented in this entry.
-!- DISEASE: Polydactyly, postaxial B (PAPB) [MIM:174200]: A condition
characterized by an extra digit in the occurrence of supernumerary
digits in the upper and/or lower extremities. In postaxial
polydactyly type B the extra digit is not well formed and is
frequently in the form of a skin. {ECO:0000269|PubMed:10441570}.
Note=The disease is caused by mutations affecting the gene
represented in this entry.
-!- DISEASE: Polydactyly preaxial 4 (POP4) [MIM:174700]: Preaxial
polydactyly (i.e., polydactyly on the radial/tibial side of the
hand/foot) covers a heterogeneous group of entities. In preaxial
polydactyly type IV, the thumb shows only the mildest degree of
duplication, and syndactyly of various degrees affects fingers 3
and 4. {ECO:0000269|PubMed:10441570}. Note=The disease is caused
by mutations affecting the gene represented in this entry.
-!- SIMILARITY: Belongs to the GLI C2H2-type zinc-finger protein
family. {ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=AAA52564.1; Type=Frameshift; Positions=1549; Evidence={ECO:0000305};
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EMBL; M57609; AAA52564.1; ALT_FRAME; mRNA.
EMBL; AJ250408; CAB59315.1; -; Genomic_DNA.
EMBL; AC005026; AAP21869.1; -; Genomic_DNA.
EMBL; AC005028; AAS01998.1; -; Genomic_DNA.
EMBL; AC005158; AAS02015.1; -; Genomic_DNA.
EMBL; AC073852; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; CH236951; EAL24002.1; -; Genomic_DNA.
EMBL; M20674; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; BC113616; AAI13617.1; -; mRNA.
EMBL; BC117168; AAI17169.1; -; mRNA.
CCDS; CCDS5465.1; -.
PIR; A35927; A35927.
RefSeq; NP_000159.3; NM_000168.5.
UniGene; Hs.21509; -.
PDB; 4BLD; X-ray; 2.80 A; E/F/G/H=328-344.
PDBsum; 4BLD; -.
ProteinModelPortal; P10071; -.
SMR; P10071; -.
BioGrid; 108999; 30.
CORUM; P10071; -.
DIP; DIP-32538N; -.
ELM; P10071; -.
IntAct; P10071; 12.
MINT; MINT-189869; -.
STRING; 9606.ENSP00000379258; -.
iPTMnet; P10071; -.
PhosphoSitePlus; P10071; -.
BioMuta; GLI3; -.
DMDM; 269849770; -.
EPD; P10071; -.
MaxQB; P10071; -.
PaxDb; P10071; -.
PeptideAtlas; P10071; -.
PRIDE; P10071; -.
Ensembl; ENST00000395925; ENSP00000379258; ENSG00000106571.
GeneID; 2737; -.
KEGG; hsa:2737; -.
UCSC; uc011kbh.3; human.
CTD; 2737; -.
DisGeNET; 2737; -.
EuPathDB; HostDB:ENSG00000106571.12; -.
GeneCards; GLI3; -.
GeneReviews; GLI3; -.
H-InvDB; HIX0033636; -.
HGNC; HGNC:4319; GLI3.
HPA; HPA005534; -.
MalaCards; GLI3; -.
MIM; 146510; phenotype.
MIM; 165240; gene.
MIM; 174200; phenotype.
MIM; 174700; phenotype.
MIM; 175700; phenotype.
neXtProt; NX_P10071; -.
OpenTargets; ENSG00000106571; -.
Orphanet; 36; Acrocallosal syndrome.
Orphanet; 380; Greig cephalopolysyndactyly syndrome.
Orphanet; 672; Pallister-Hall syndrome.
Orphanet; 295161; Polysyndactyly, bilateral.
Orphanet; 295159; Polysyndactyly, unilateral.
Orphanet; 295165; Postaxial polydactyly type A, bilateral.
Orphanet; 295163; Postaxial polydactyly type A, unilateral.
Orphanet; 295169; Postaxial polydactyly type B, bilateral.
Orphanet; 295167; Postaxial polydactyly type B, unilateral.
PharmGKB; PA28722; -.
eggNOG; KOG1721; Eukaryota.
eggNOG; COG5048; LUCA.
GeneTree; ENSGT00900000140802; -.
HOVERGEN; HBG005844; -.
InParanoid; P10071; -.
KO; K06230; -.
OMA; MHNKRSK; -.
OrthoDB; EOG091G01XS; -.
PhylomeDB; P10071; -.
TreeFam; TF350216; -.
Reactome; R-HSA-5610785; GLI3 is processed to GLI3R by the proteasome.
Reactome; R-HSA-5610787; Hedgehog 'off' state.
Reactome; R-HSA-5632684; Hedgehog 'on' state.
Reactome; R-HSA-5635851; GLI proteins bind promoters of Hh responsive genes to promote transcription.
Reactome; R-HSA-8940973; RUNX2 regulates osteoblast differentiation.
SignaLink; P10071; -.
SIGNOR; P10071; -.
ChiTaRS; GLI3; human.
GeneWiki; GLI3; -.
GenomeRNAi; 2737; -.
PRO; PR:P10071; -.
Proteomes; UP000005640; Chromosome 7.
Bgee; ENSG00000106571; -.
CleanEx; HS_GLI3; -.
ExpressionAtlas; P10071; baseline and differential.
Genevisible; P10071; HS.
GO; GO:0005930; C:axoneme; IEA:Ensembl.
GO; GO:0097546; C:ciliary base; TAS:Reactome.
GO; GO:0097542; C:ciliary tip; TAS:Reactome.
GO; GO:0005929; C:cilium; IDA:UniProtKB.
GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
GO; GO:0005829; C:cytosol; IDA:UniProtKB.
GO; GO:0016607; C:nuclear speck; IEA:Ensembl.
GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
GO; GO:0005634; C:nucleus; IDA:UniProtKB.
GO; GO:0017053; C:transcriptional repressor complex; IEA:Ensembl.
GO; GO:0008013; F:beta-catenin binding; IPI:UniProtKB.
GO; GO:0003682; F:chromatin binding; IEA:Ensembl.
GO; GO:0035035; F:histone acetyltransferase binding; IPI:UniProtKB.
GO; GO:0042826; F:histone deacetylase binding; IDA:UniProtKB.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0000978; F:RNA polymerase II core promoter proximal region sequence-specific DNA binding; IDA:MGI.
GO; GO:0000977; F:RNA polymerase II regulatory region sequence-specific DNA binding; IDA:MGI.
GO; GO:0003700; F:transcription factor activity, sequence-specific DNA binding; IDA:UniProtKB.
GO; GO:0001077; F:transcriptional activator activity, RNA polymerase II core promoter proximal region sequence-specific binding; IC:NTNU_SB.
GO; GO:0060873; P:anterior semicircular canal development; IEA:Ensembl.
GO; GO:0009952; P:anterior/posterior pattern specification; IEA:Ensembl.
GO; GO:0060840; P:artery development; IEA:Ensembl.
GO; GO:0007411; P:axon guidance; IEA:Ensembl.
GO; GO:0001658; P:branching involved in ureteric bud morphogenesis; IEA:Ensembl.
GO; GO:0048593; P:camera-type eye morphogenesis; IEA:Ensembl.
GO; GO:0061005; P:cell differentiation involved in kidney development; IEA:Ensembl.
GO; GO:0048589; P:developmental growth; IEA:Ensembl.
GO; GO:0048566; P:embryonic digestive tract development; TAS:BHF-UCL.
GO; GO:0048557; P:embryonic digestive tract morphogenesis; IEA:Ensembl.
GO; GO:0042733; P:embryonic digit morphogenesis; TAS:BHF-UCL.
GO; GO:0048704; P:embryonic skeletal system morphogenesis; IEA:Ensembl.
GO; GO:0021798; P:forebrain dorsal/ventral pattern formation; IEA:Ensembl.
GO; GO:0021861; P:forebrain radial glial cell differentiation; IEA:Ensembl.
GO; GO:0060364; P:frontal suture morphogenesis; IEA:Ensembl.
GO; GO:0007507; P:heart development; IEA:Ensembl.
GO; GO:0007442; P:hindgut morphogenesis; IEA:Ensembl.
GO; GO:0021766; P:hippocampus development; IEA:Ensembl.
GO; GO:0001701; P:in utero embryonic development; IEA:Ensembl.
GO; GO:0060366; P:lambdoid suture morphogenesis; IEA:Ensembl.
GO; GO:0022018; P:lateral ganglionic eminence cell proliferation; IEA:Ensembl.
GO; GO:0060875; P:lateral semicircular canal development; IEA:Ensembl.
GO; GO:0021819; P:layer formation in cerebral cortex; IEA:Ensembl.
GO; GO:0035108; P:limb morphogenesis; IMP:UniProtKB.
GO; GO:0097421; P:liver regeneration; IEA:Ensembl.
GO; GO:0030324; P:lung development; IEA:Ensembl.
GO; GO:0060594; P:mammary gland specification; IEA:Ensembl.
GO; GO:0030318; P:melanocyte differentiation; IEA:Ensembl.
GO; GO:0001656; P:metanephros development; IEA:Ensembl.
GO; GO:0046639; P:negative regulation of alpha-beta T cell differentiation; ISS:BHF-UCL.
GO; GO:0043066; P:negative regulation of apoptotic process; IEA:Ensembl.
GO; GO:0090090; P:negative regulation of canonical Wnt signaling pathway; IDA:UniProtKB.
GO; GO:0008285; P:negative regulation of cell proliferation; IEA:Ensembl.
GO; GO:0045665; P:negative regulation of neuron differentiation; IEA:Ensembl.
GO; GO:0045879; P:negative regulation of smoothened signaling pathway; ISS:BHF-UCL.
GO; GO:0000122; P:negative regulation of transcription from RNA polymerase II promoter; IDA:UniProtKB.
GO; GO:0045892; P:negative regulation of transcription, DNA-templated; IDA:UniProtKB.
GO; GO:0045060; P:negative thymic T cell selection; ISS:BHF-UCL.
GO; GO:0043585; P:nose morphogenesis; TAS:BHF-UCL.
GO; GO:0042475; P:odontogenesis of dentin-containing tooth; IEA:Ensembl.
GO; GO:0048709; P:oligodendrocyte differentiation; IEA:Ensembl.
GO; GO:0021631; P:optic nerve morphogenesis; IEA:Ensembl.
GO; GO:0060021; P:palate development; IEA:Ensembl.
GO; GO:0046638; P:positive regulation of alpha-beta T cell differentiation; ISS:BHF-UCL.
GO; GO:0032332; P:positive regulation of chondrocyte differentiation; IEA:Ensembl.
GO; GO:0002052; P:positive regulation of neuroblast proliferation; IEA:Ensembl.
GO; GO:0045669; P:positive regulation of osteoblast differentiation; IEA:Ensembl.
GO; GO:0042307; P:positive regulation of protein import into nucleus; IEA:Ensembl.
GO; GO:0045944; P:positive regulation of transcription from RNA polymerase II promoter; IDA:UniProtKB.
GO; GO:0045893; P:positive regulation of transcription, DNA-templated; ISS:UniProtKB.
GO; GO:0030850; P:prostate gland development; IEA:Ensembl.
GO; GO:0016485; P:protein processing; IEA:Ensembl.
GO; GO:0009954; P:proximal/distal pattern formation; IEA:Ensembl.
GO; GO:1903010; P:regulation of bone development; IEA:Ensembl.
GO; GO:0043627; P:response to estrogen; IEA:Ensembl.
GO; GO:0060367; P:sagittal suture morphogenesis; IEA:Ensembl.
GO; GO:0007224; P:smoothened signaling pathway; TAS:BHF-UCL.
GO; GO:0060831; P:smoothened signaling pathway involved in dorsal/ventral neural tube patterning; IEA:Ensembl.
GO; GO:0021776; P:smoothened signaling pathway involved in spinal cord motor neuron cell fate specification; IEA:Ensembl.
GO; GO:0021775; P:smoothened signaling pathway involved in ventral spinal cord interneuron specification; IEA:Ensembl.
GO; GO:0033077; P:T cell differentiation in thymus; ISS:BHF-UCL.
GO; GO:0070242; P:thymocyte apoptotic process; ISS:BHF-UCL.
GO; GO:0043586; P:tongue development; IEA:Ensembl.
GO; GO:0042060; P:wound healing; IEA:Ensembl.
InterPro; IPR032851; GLI3.
InterPro; IPR036236; Znf_C2H2_sf.
InterPro; IPR013087; Znf_C2H2_type.
PANTHER; PTHR19818:SF5; PTHR19818:SF5; 1.
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;
3D-structure; Acetylation; Activator; Cell projection; Cilium;
Complete proteome; Cytoplasm; Disease mutation; DNA-binding;
Isopeptide bond; Metal-binding; Methylation; Nucleus; Phosphoprotein;
Polymorphism; Reference proteome; Repeat; Repressor; Transcription;
Transcription regulation; Ubl conjugation; Zinc; Zinc-finger.
CHAIN 1 1580 Transcriptional activator GLI3.
/FTId=PRO_0000047202.
CHAIN 1 ? Transcriptional repressor GLI3R.
/FTId=PRO_0000406137.
ZN_FING 480 505 C2H2-type 1. {ECO:0000255|PROSITE-
ProRule:PRU00042}.
ZN_FING 513 540 C2H2-type 2. {ECO:0000255|PROSITE-
ProRule:PRU00042}.
ZN_FING 546 570 C2H2-type 3. {ECO:0000255|PROSITE-
ProRule:PRU00042}.
ZN_FING 576 601 C2H2-type 4. {ECO:0000255|PROSITE-
ProRule:PRU00042}.
ZN_FING 607 632 C2H2-type 5. {ECO:0000255|PROSITE-
ProRule:PRU00042}.
COMPBIAS 1492 1512 Asp/Glu-rich (acidic).
MOD_RES 1 1 N-acetylmethionine.
{ECO:0000244|PubMed:19413330}.
MOD_RES 175 175 Omega-N-methylarginine.
{ECO:0000250|UniProtKB:Q61602}.
MOD_RES 664 664 Phosphoserine.
{ECO:0000244|PubMed:21406692,
ECO:0000244|PubMed:23186163}.
MOD_RES 849 849 Phosphoserine; by PKA.
{ECO:0000269|PubMed:10693759}.
MOD_RES 865 865 Phosphoserine; by PKA.
{ECO:0000269|PubMed:10693759}.
MOD_RES 877 877 Phosphoserine; by PKA.
{ECO:0000269|PubMed:10693759}.
MOD_RES 907 907 Phosphoserine; by PKA.
{ECO:0000269|PubMed:10693759}.
MOD_RES 980 980 Phosphoserine; by PKA.
{ECO:0000269|PubMed:10693759}.
MOD_RES 1006 1006 Phosphoserine; by PKA.
{ECO:0000269|PubMed:10693759}.
CROSSLNK 438 438 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:28112733}.
CROSSLNK 462 462 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:28112733}.
CROSSLNK 773 773 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in ubiquitin).
{ECO:0000269|PubMed:16705181}.
CROSSLNK 779 779 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2);
alternate. {ECO:0000244|PubMed:28112733}.
CROSSLNK 779 779 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in ubiquitin);
alternate. {ECO:0000269|PubMed:16705181}.
CROSSLNK 784 784 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in ubiquitin).
{ECO:0000269|PubMed:16705181}.
CROSSLNK 800 800 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in ubiquitin).
{ECO:0000269|PubMed:16705181}.
VARIANT 169 169 P -> L (in a colorectal cancer sample;
somatic mutation).
{ECO:0000269|PubMed:16959974}.
/FTId=VAR_035560.
VARIANT 183 183 T -> A (in dbSNP:rs846266).
{ECO:0000269|PubMed:10441342,
ECO:0000269|PubMed:15489334,
ECO:0000269|PubMed:2118997}.
/FTId=VAR_028276.
VARIANT 440 440 D -> E. {ECO:0000269|PubMed:10441342}.
/FTId=VAR_010052.
VARIANT 515 515 C -> G (in GCPS).
{ECO:0000269|PubMed:10441342}.
/FTId=VAR_010053.
VARIANT 520 520 C -> Y (in GCPS).
{ECO:0000269|PubMed:10441342}.
/FTId=VAR_010054.
VARIANT 625 625 R -> W (in GCPS; dbSNP:rs121917712).
{ECO:0000269|PubMed:12794692}.
/FTId=VAR_021481.
VARIANT 707 707 P -> S (in GCPS; dbSNP:rs121917716).
{ECO:0000269|PubMed:9302279}.
/FTId=VAR_010055.
VARIANT 727 727 G -> R (in PAPA1 and PAPB;
dbSNP:rs121917710).
{ECO:0000269|PubMed:10441570}.
/FTId=VAR_009876.
VARIANT 808 808 I -> M (in GCPS; dbSNP:rs62622373).
{ECO:0000269|PubMed:10441342}.
/FTId=VAR_010056.
VARIANT 934 934 A -> P (in GCPS; the patient was
originally classifed as being affected by
acrocallosal syndrome due to the absence
of corpus callosum; dbSNP:rs28933372).
{ECO:0000269|PubMed:12414818}.
/FTId=VAR_021482.
VARIANT 998 998 P -> L (in dbSNP:rs929387).
{ECO:0000269|PubMed:10441342,
ECO:0000269|PubMed:15489334,
ECO:0000269|PubMed:2118997}.
/FTId=VAR_028278.
VARIANT 1304 1304 S -> P (in a colorectal cancer sample;
somatic mutation).
{ECO:0000269|PubMed:16959974}.
/FTId=VAR_035561.
VARIANT 1336 1336 G -> E (in dbSNP:rs35280470).
/FTId=VAR_034865.
VARIANT 1537 1537 R -> C (in dbSNP:rs35364414).
{ECO:0000269|PubMed:10441342}.
/FTId=VAR_010057.
MUTAGEN 773 773 K->R: Loss of proteolytic processing.
{ECO:0000269|PubMed:16705181}.
MUTAGEN 779 779 K->R: Loss of proteolytic processing.
{ECO:0000269|PubMed:16705181}.
MUTAGEN 784 784 K->R: Loss of proteolytic processing.
{ECO:0000269|PubMed:16705181}.
MUTAGEN 800 800 K->R: Loss of proteolytic processing.
{ECO:0000269|PubMed:16705181}.
MUTAGEN 849 849 S->A: Loss of phosphorylation and
proteolytic processing.
{ECO:0000269|PubMed:10693759,
ECO:0000269|PubMed:16705181}.
MUTAGEN 855 855 S->A: Loss of proteolytic processing.
{ECO:0000269|PubMed:16705181}.
MUTAGEN 856 856 S->A: Loss of proteolytic processing.
{ECO:0000269|PubMed:16705181}.
MUTAGEN 861 861 S->A: Loss of proteolytic processing.
{ECO:0000269|PubMed:16705181}.
MUTAGEN 864 864 S->A: Loss of proteolytic processing.
{ECO:0000269|PubMed:16705181}.
MUTAGEN 865 865 S->A: Loss of phosphorylation and
proteolytic processing.
{ECO:0000269|PubMed:10693759}.
MUTAGEN 873 873 S->A: Loss of proteolytic processing.
{ECO:0000269|PubMed:16705181}.
MUTAGEN 877 877 S->A: Loss of phosphorylation and
proteolytic processing.
{ECO:0000269|PubMed:10693759,
ECO:0000269|PubMed:16705181}.
MUTAGEN 903 903 S->A: Loss of proteolytic processing.
{ECO:0000269|PubMed:16705181}.
MUTAGEN 907 907 S->A: Loss of phosphorylation and
proteolytic processing.
{ECO:0000269|PubMed:10693759,
ECO:0000269|PubMed:16705181}.
MUTAGEN 980 980 S->A: Loss of phosphorylation and
proteolytic processing.
{ECO:0000269|PubMed:10693759}.
MUTAGEN 1006 1006 S->A: Loss of phosphorylation and
proteolytic processing.
{ECO:0000269|PubMed:10693759}.
STRAND 334 337 {ECO:0000244|PDB:4BLD}.
SEQUENCE 1580 AA; 169863 MW; 423B7495FCE3C37C CRC64;
MEAQSHSSTT TEKKKVENSI VKCSTRTDVS EKAVASSTTS NEDESPGQTY HRERRNAITM
QPQNVQGLSK VSEEPSTSSD ERASLIKKEI HGSLPHVAEP SVPYRGTVFA MDPRNGYMEP
HYHPPHLFPA FHPPVPIDAR HHEGRYHYDP SPIPPLHMTS ALSSSPTYPD LPFIRISPHR
NPTAASESPF SPPHPYINPY MDYIRSLHSS PSLSMISATR GLSPTDAPHA GVSPAEYYHQ
MALLTGQRSP YADIIPSAAT AGTGAIHMEY LHAMDSTRFS SPRLSARPSR KRTLSISPLS
DHSFDLQTMI RTSPNSLVTI LNNSRSSSSA SGSYGHLSAS AISPALSFTY SSAPVSLHMH
QQILSRQQSL GSAFGHSPPL IHPAPTFPTQ RPIPGIPTVL NPVQVSSGPS ESSQNKPTSE
SAVSSTGDPM HNKRSKIKPD EDLPSPGARG QQEQPEGTTL VKEEGDKDES KQEPEVIYET
NCHWEGCARE FDTQEQLVHH INNDHIHGEK KEFVCRWLDC SREQKPFKAQ YMLVVHMRRH
TGEKPHKCTF EGCTKAYSRL ENLKTHLRSH TGEKPYVCEH EGCNKAFSNA SDRAKHQNRT
HSNEKPYVCK IPGCTKRYTD PSSLRKHVKT VHGPEAHVTK KQRGDIHPRP PPPRDSGSHS
QSRSPGRPTQ GALGEQQDLS NTTSKREECL QVKTVKAEKP MTSQPSPGGQ SSCSSQQSPI
SNYSNSGLEL PLTDGGSIGD LSAIDETPIM DSTISTATTA LALQARRNPA GTKWMEHVKL
ERLKQVNGMF PRLNPILPPK APAVSPLIGN GTQSNNTCSL GGPMTLLPGR SDLSGVDVTM
LNMLNRRDSS ASTISSAYLS SRRSSGISPC FSSRRSSEAS QAEGRPQNVS VADSYDPIST
DASRRSSEAS QSDGLPSLLS LTPAQQYRLK AKYAAATGGP PPTPLPNMER MSLKTRLALL
GDALEPGVAL PPVHAPRRCS DGGAHGYGRR HLQPHDAPGH GVRRASDPVR TGSEGLALPR
VPRFSSLSSC NPPAMATSAE KRSLVLQNYT RPEGGQSRNF HSSPCPPSIT ENVTLESLTM
DADANLNDED FLPDDVVQYL NSQNQAGYEQ HFPSALPDDS KVPHGPGDFD APGLPDSHAG
QQFHALEQPC PEGSKTDLPI QWNEVSSGSA DLSSSKLKCG PRPAVPQTRA FGFCNGMVVH
PQNPLRSGPA GGYQTLGENS NPYGGPEHLM LHNSPGSGTS GNAFHEQPCK APQYGNCLNR
QPVAPGALDG ACGAGIQASK LKSTPMQGSG GQLNFGLPVA PNESAGSMVN GMQNQDPVGQ
GYLAHQLLGD SMQHPGAGRP GQQMLGQISA TSHINIYQGP ESCLPGAHGM GSQPSSLAVV
RGYQPCASFG GSRRQAMPRD SLALQSGQLS DTSQTCRVNG IKMEMKGQPH PLCSNLQNYS
GQFYDQTVGF SQQDTKAGSF SISDASCLLQ GTSAKNSELL SPGANQVTST VDSLDSHDLE
GVQIDFDAII DDGDHSSLMS GALSPSIIQN LSHSSSRLTT PRASLPFPAL SMSTTNMAIG
DMSSLLTSLA EESKFLAVMQ


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