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Zinc finger protein GLI2 (GLI family zinc finger protein 2) (Tax helper protein)

 GLI2_HUMAN              Reviewed;        1586 AA.
P10070; O60252; O60253; O60254; O60255; Q15590; Q15591; Q4JHT4;
01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
25-NOV-2008, sequence version 4.
23-MAY-2018, entry version 192.
RecName: Full=Zinc finger protein GLI2 {ECO:0000305};
AltName: Full=GLI family zinc finger protein 2 {ECO:0000312|HGNC:HGNC:4318};
AltName: Full=Tax helper protein {ECO:0000303|PubMed:9557682};
Name=GLI2 {ECO:0000312|HGNC:HGNC:4318};
Synonyms=THP {ECO:0000303|PubMed:9557682};
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1; 2; 3 AND 4), FUNCTION,
DNA-BINDING, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND VARIANTS
SER-1156 AND ASN-1306.
PubMed=9557682;
Tanimura A., Dan S., Yoshida M.;
"Cloning of novel isoforms of the human Gli2 oncogene and their
activities to enhance tax-dependent transcription of the human T-cell
leukemia virus type 1 genome.";
J. Virol. 72:3958-3964(1998).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 5), FUNCTION, AND INVOLVEMENT IN
CJS.
PubMed=15994174; DOI=10.1093/hmg/ddi222;
Roessler E., Ermilov A.N., Grange D.K., Wang A., Grachtchouk M.,
Dlugosz A.A., Muenke M.;
"A previously unidentified amino-terminal domain regulates
transcriptional activity of wild-type and disease-associated human
GLI2.";
Hum. Mol. Genet. 14:2181-2188(2005).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=15815621; DOI=10.1038/nature03466;
Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H.,
Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M.,
Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E.,
Kremitzki C., Oddy L., Du H., Sun H., Bradshaw-Cordum H., Ali J.,
Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C.,
Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J.,
Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A.,
Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K.,
Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M.,
Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K.,
McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C.,
Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N.,
Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M.,
Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E.,
Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P.,
Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A.,
Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A.,
Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T.,
Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D.,
Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X.,
McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C.,
Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S.,
Miller W., Eichler E.E., Bork P., Suyama M., Torrents D.,
Waterston R.H., Wilson R.K.;
"Generation and annotation of the DNA sequences of human chromosomes 2
and 4.";
Nature 434:724-731(2005).
[4]
NUCLEOTIDE SEQUENCE [MRNA] OF 1-857 (ISOFORMS 1; 2; 3 AND 4).
PubMed=8350401;
Tanimura A., Teshima H., Fujisawa J., Yoshida M.;
"A new regulatory element that augments the Tax-dependent enhancer of
human T-cell leukemia virus type 1 and cloning of cDNAs encoding its
binding proteins.";
J. Virol. 67:5375-5382(1993).
[5]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 456-560 (ISOFORMS 1; 2; 3 AND 4).
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).
[6]
INTERACTION WITH STK36.
PubMed=10806483; DOI=10.1038/35010610;
Murone M., Luoh S.-L., Stone D., Li W., Gurney A., Armanini M.,
Grey C., Rosenthal A., de Sauvage F.J.;
"Gli regulation by the opposing activities of fused and suppressor of
fused.";
Nat. Cell Biol. 2:310-312(2000).
[7]
INVOLVEMENT IN HPE9.
PubMed=14581620; DOI=10.1073/pnas.2235734100;
Roessler E., Du Y.-Z., Mullor J.L., Casas E., Allen W.P.,
Gillessen-Kaesbach G., Roeder E.R., Ming J.E., Ruiz i Altaba A.,
Muenke M.;
"Loss-of-function mutations in the human GLI2 gene are associated with
pituitary anomalies and holoprosencephaly-like features.";
Proc. Natl. Acad. Sci. U.S.A. 100:13424-13429(2003).
[8]
FUNCTION, AND PHOSPHORYLATION AT SER-388 AND SER-1011.
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).
[9]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-234 AND SER-236, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18669648; DOI=10.1073/pnas.0805139105;
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
Elledge S.J., Gygi S.P.;
"A quantitative atlas of mitotic phosphorylation.";
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
[10]
PHOSPHORYLATION, AND FUNCTION.
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).
[11]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-149; SER-234; SER-236
AND SER-242, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=20068231; DOI=10.1126/scisignal.2000475;
Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S.,
Mann M.;
"Quantitative phosphoproteomics reveals widespread full
phosphorylation site occupancy during mitosis.";
Sci. Signal. 3:RA3-RA3(2010).
[12]
ACETYLATION AT LYS-757.
PubMed=23762415; DOI=10.1371/journal.pone.0065718;
Coni S., Antonucci L., D'Amico D., Di Magno L., Infante P.,
De Smaele E., Giannini G., Di Marcotullio L., Screpanti I., Gulino A.,
Canettieri G.;
"Gli2 acetylation at lysine 757 regulates hedgehog-dependent
transcriptional output by preventing its promoter occupancy.";
PLoS ONE 8:E65718-E65718(2013).
[13]
FUNCTION, 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).
[14]
INVOLVEMENT BY HPE9, INVOLVEMENT IN CJS, VARIANT CJS LEU-608, AND
FUNCTION.
PubMed=20685856; DOI=10.1210/jc.2010-1050;
Franca M.M., Jorge A.A., Carvalho L.R., Costalonga E.F., Vasques G.A.,
Leite C.C., Mendonca B.B., Arnhold I.J.;
"Novel heterozygous nonsense GLI2 mutations in patients with
hypopituitarism and ectopic posterior pituitary lobe without
holoprosencephaly.";
J. Clin. Endocrinol. Metab. 95:E384-E391(2010).
[15]
FUNCTION, INTERACTION WITH FOXC1, AND SUBCELLULAR LOCATION.
PubMed=26565916; DOI=10.1016/j.celrep.2015.09.063;
Han B., Qu Y., Jin Y., Yu Y., Deng N., Wawrowsky K., Zhang X., Li N.,
Bose S., Wang Q., Sakkiah S., Abrol R., Jensen T.W., Berman B.P.,
Tanaka H., Johnson J., Gao B., Hao J., Liu Z., Buttyan R., Ray P.S.,
Hung M.C., Giuliano A.E., Cui X.;
"FOXC1 activates smoothened-independent Hedgehog signaling in basal-
like breast cancer.";
Cell Rep. 13:1046-1058(2015).
[16]
SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-50 (ISOFORMS 2 AND 4), 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).
[17]
VARIANTS HPE9 GLY-479; SER-932 AND LEU-1554, AND VARIANT ILE-1444.
PubMed=17096318; DOI=10.1002/ajmg.a.31370;
Rahimov F., Ribeiro L.A., de Miranda E., Richieri-Costa A.,
Murray J.C.;
"GLI2 mutations in four Brazilian patients: how wide is the phenotypic
spectrum?";
Am. J. Med. Genet. A 140:2571-2576(2006).
[18]
VARIANTS CJS PRO-516; VAL-1352; 1444-ILE-PHE-1445 AND ASN-1520,
CHARACTERIZATION OF VARIANTS CJS PRO-516; VAL-1352; 1444-ILE-PHE-1445
AND ASN-1520, VARIANT HIS-1543, AND CHARACTERIZATION OF VARIANT
HIS-1543.
PubMed=23408573; DOI=10.1210/jc.2012-3224;
Flemming G.M., Klammt J., Ambler G., Bao Y., Blum W.F., Cowell C.,
Donaghue K., Howard N., Kumar A., Sanchez J., Stobbe H.,
Pfaeffle R.W.;
"Functional characterization of a heterozygous GLI2 missense mutation
in patients with multiple pituitary hormone deficiency.";
J. Clin. Endocrinol. Metab. 98:E567-E575(2013).
[19]
VARIANT ILE-1444.
PubMed=27535533; DOI=10.1038/nature19057;
Exome Aggregation Consortium;
Lek M., Karczewski K.J., Minikel E.V., Samocha K.E., Banks E.,
Fennell T., O'Donnell-Luria A.H., Ware J.S., Hill A.J., Cummings B.B.,
Tukiainen T., Birnbaum D.P., Kosmicki J.A., Duncan L.E., Estrada K.,
Zhao F., Zou J., Pierce-Hoffman E., Berghout J., Cooper D.N.,
Deflaux N., DePristo M., Do R., Flannick J., Fromer M., Gauthier L.,
Goldstein J., Gupta N., Howrigan D., Kiezun A., Kurki M.I.,
Moonshine A.L., Natarajan P., Orozco L., Peloso G.M., Poplin R.,
Rivas M.A., Ruano-Rubio V., Rose S.A., Ruderfer D.M., Shakir K.,
Stenson P.D., Stevens C., Thomas B.P., Tiao G., Tusie-Luna M.T.,
Weisburd B., Won H.H., Yu D., Altshuler D.M., Ardissino D.,
Boehnke M., Danesh J., Donnelly S., Elosua R., Florez J.C.,
Gabriel S.B., Getz G., Glatt S.J., Hultman C.M., Kathiresan S.,
Laakso M., McCarroll S., McCarthy M.I., McGovern D., McPherson R.,
Neale B.M., Palotie A., Purcell S.M., Saleheen D., Scharf J.M.,
Sklar P., Sullivan P.F., Tuomilehto J., Tsuang M.T., Watkins H.C.,
Wilson J.G., Daly M.J., MacArthur D.G.;
"Analysis of protein-coding genetic variation in 60,706 humans.";
Nature 536:285-291(2016).
-!- FUNCTION: Functions as transcription regulator in the hedgehog
(Hh) pathway (PubMed:18455992, PubMed:26565916). Functions as
transcriptional activator (PubMed:9557682, PubMed:19878745,
PubMed:24311597). May also function as transcriptional repressor
(By similarity). Requires STK36 for full transcriptional activator
activity. Required for normal embryonic development
(PubMed:15994174, PubMed:20685856). {ECO:0000250|UniProtKB:Q0VGT2,
ECO:0000269|PubMed:15994174, ECO:0000269|PubMed:18455992,
ECO:0000269|PubMed:19878745, ECO:0000269|PubMed:24311597,
ECO:0000269|PubMed:26565916, ECO:0000269|PubMed:9557682,
ECO:0000305|PubMed:20685856}.
-!- FUNCTION: Isoform 1, isoform 2, isoform 3 and isoform 4: Act as
transcriptional activators in T-cell leukemia virus type 1 (HTLV-
1)-infected cells in a Tax-dependent manner. Bind to the DNA
sequence 5'-GAACCACCCA-3' which is part of the Tax-responsive
element (TRE-2S) regulatory element that augments the Tax-
dependent enhancer of HTLV-1 (PubMed:9557682). Are involved in the
smoothened (SHH) signaling pathway (PubMed:18455992).
{ECO:0000269|PubMed:15994174, ECO:0000269|PubMed:18455992,
ECO:0000269|PubMed:9557682}.
-!- FUNCTION: Isoform 5: Acts as a transcriptional repressor.
{ECO:0000269|PubMed:15994174}.
-!- SUBUNIT: Interaction with ZIC1 and ZIC2 (By similarity). Interacts
with STK36 (PubMed:10806483). Interacts with SUFU; this inhibits
transcriptional activation mediated by GLI2 (PubMed:24311597).
Interacts (via C-terminal internal region) with FOXC1 (via N-
terminus); this interaction is direct and increases GLI2 DNA-
binding and transcriptional activity through a smoothened (SMO)-
independent Hedgehog (Hh) signaling pathway (PubMed:26565916).
{ECO:0000250|UniProtKB:Q0VGT2, ECO:0000269|PubMed:10806483,
ECO:0000269|PubMed:24311597, ECO:0000269|PubMed:26565916}.
-!- INTERACTION:
Q9Y297:BTRC; NbExp=4; IntAct=EBI-10821567, EBI-307461;
P84022:SMAD3; NbExp=4; IntAct=EBI-10821567, EBI-347161;
-!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:26565916}.
Cytoplasm {ECO:0000250|UniProtKB:Q0VGT2}. Cell projection, cilium
{ECO:0000250|UniProtKB:Q0VGT2}. Note=STK36 promotes translocation
to the nucleus. In keratinocytes, it is sequestered in the
cytoplasm by SUFU. In the absence of SUFU, it translocates to the
nucleus. {ECO:0000250|UniProtKB:Q0VGT2}.
-!- SUBCELLULAR LOCATION: Isoform 1: Nucleus
{ECO:0000269|PubMed:9557682}.
-!- SUBCELLULAR LOCATION: Isoform 2: Nucleus
{ECO:0000269|PubMed:9557682}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=5;
Name=5; Synonyms=GLI2 {ECO:0000303|PubMed:15994174};
IsoId=P10070-5; Sequence=Displayed;
Name=1; Synonyms=Alpha, GLI2star, GLI2deltaN
{ECO:0000303|PubMed:15994174, ECO:0000303|PubMed:9557682};
IsoId=P10070-1; Sequence=VSP_035708;
Name=2; Synonyms=Beta {ECO:0000303|PubMed:9557682};
IsoId=P10070-2; Sequence=VSP_035708, VSP_006877;
Note=Contains a glycyl lysine isopeptide (Lys-Gly) (interchain
with G-Cter in SUMO2) at position 50.
{ECO:0000244|PubMed:28112733};
Name=3; Synonyms=Gamma {ECO:0000303|PubMed:9557682};
IsoId=P10070-3; Sequence=VSP_035708, VSP_006878, VSP_006879;
Name=4; Synonyms=Delta {ECO:0000303|PubMed:9557682};
IsoId=P10070-4; Sequence=VSP_035708, VSP_006877, VSP_006878,
VSP_006879;
Note=Contains a glycyl lysine isopeptide (Lys-Gly) (interchain
with G-Cter in SUMO2) at position 50.
{ECO:0000244|PubMed:28112733};
-!- TISSUE SPECIFICITY: Expressed in breast cancers (at protein level)
(PubMed:26565916). Isoform 1 and isoform 4 are expressed in HTLV-
1-infected T-cell lines (at protein level) (PubMed:9557682).
Isoform 1 and isoform 2 are strongly expressed in HTLV-1-infected
T-cell lines (PubMed:9557682). Isoform 3 and isoform 4 are weakly
expressed in HTLV-1-infected T-cell lines (PubMed:9557682).
{ECO:0000269|PubMed:26565916, ECO:0000269|PubMed:9557682}.
-!- DOMAIN: The N-terminal domain confers transcriptional repressor
activity, while the C-terminal domain mediates transcriptional
activation. {ECO:0000250|UniProtKB:Q0VGT2}.
-!- PTM: Phosphorylated in vitro by ULK3. Phosphorylated by DYRK2;
this inhibits GLI2 transcription factor activity and promotes
proteasomal degradation of GLI2. {ECO:0000269|PubMed:18455992,
ECO:0000269|PubMed:19878745}.
-!- PTM: Acetylation at Lys-757 inhibits Hh target gene expression,
probably by impeding entry into chromatin thus preventing promoter
occupancy. {ECO:0000269|PubMed:23762415}.
-!- DISEASE: Holoprosencephaly 9 (HPE9) [MIM:610829]: A structural
anomaly of the brain, in which the developing forebrain fails to
correctly separate into right and left hemispheres.
Holoprosencephaly is genetically heterogeneous and associated with
several distinct facies and phenotypic variability.
Holoprosencephaly type 9 is characterized by defective anterior
pituitary formation and pan-hypopituitarism, with or without overt
forebrain cleavage abnormalities, and holoprosencephaly-like
midfacial hypoplasia. {ECO:0000269|PubMed:14581620,
ECO:0000269|PubMed:17096318, ECO:0000269|PubMed:20685856}.
Note=The disease is caused by mutations affecting the gene
represented in this entry.
-!- DISEASE: Culler-Jones syndrome (CJS) [MIM:615849]: 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:15994174,
ECO:0000269|PubMed:20685856, ECO:0000269|PubMed:23408573}.
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=BAA03568.1; Type=Frameshift; Positions=754, 760; Evidence={ECO:0000305};
Sequence=BAA03569.1; Type=Frameshift; Positions=398, 410, 754, 760; Evidence={ECO:0000305};
Sequence=BAA25665.1; Type=Frameshift; Positions=398, 410; Evidence={ECO:0000305};
Sequence=BAA25667.1; Type=Frameshift; Positions=398, 410; Evidence={ECO:0000305};
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EMBL; AB007295; BAA25665.1; ALT_FRAME; mRNA.
EMBL; AB007296; BAA25666.1; -; mRNA.
EMBL; AB007297; BAA25667.1; ALT_FRAME; mRNA.
EMBL; AB007298; BAA25668.1; -; mRNA.
EMBL; DQ086814; AAY87165.1; -; mRNA.
EMBL; AC016764; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AC017033; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; D14827; BAA03568.1; ALT_FRAME; mRNA.
EMBL; D14828; BAA03569.1; ALT_FRAME; mRNA.
EMBL; M20672; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; M20673; AAA35898.1; -; Genomic_DNA.
CCDS; CCDS33283.1; -. [P10070-5]
PIR; A31201; A31201.
PIR; A40679; A40679.
PIR; B40679; B40679.
RefSeq; NP_005261.2; NM_005270.4. [P10070-5]
UniGene; Hs.111867; -.
ProteinModelPortal; P10070; -.
SMR; P10070; -.
BioGrid; 108998; 12.
IntAct; P10070; 6.
STRING; 9606.ENSP00000354586; -.
BindingDB; P10070; -.
ChEMBL; CHEMBL5119; -.
iPTMnet; P10070; -.
PhosphoSitePlus; P10070; -.
BioMuta; GLI2; -.
DMDM; 215274258; -.
EPD; P10070; -.
PaxDb; P10070; -.
PeptideAtlas; P10070; -.
PRIDE; P10070; -.
DNASU; 2736; -.
Ensembl; ENST00000361492; ENSP00000354586; ENSG00000074047. [P10070-5]
Ensembl; ENST00000452319; ENSP00000390436; ENSG00000074047. [P10070-5]
GeneID; 2736; -.
KEGG; hsa:2736; -.
UCSC; uc010flp.4; human. [P10070-5]
CTD; 2736; -.
DisGeNET; 2736; -.
EuPathDB; HostDB:ENSG00000074047.20; -.
GeneCards; GLI2; -.
GeneReviews; GLI2; -.
HGNC; HGNC:4318; GLI2.
HPA; CAB008558; -.
HPA; HPA074275; -.
MalaCards; GLI2; -.
MIM; 165230; gene.
MIM; 610829; phenotype.
MIM; 615849; phenotype.
neXtProt; NX_P10070; -.
OpenTargets; ENSG00000074047; -.
Orphanet; 93925; Alobar holoprosencephaly.
Orphanet; 95494; Combined pituitary hormone deficiencies, genetic forms.
Orphanet; 93924; Lobar holoprosencephaly.
Orphanet; 280200; Microform holoprosencephaly.
Orphanet; 93926; Midline interhemispheric variant of holoprosencephaly.
Orphanet; 220386; Semilobar holoprosencephaly.
Orphanet; 280195; Septopreoptic holoprosencephaly.
PharmGKB; PA28721; -.
eggNOG; KOG1721; Eukaryota.
eggNOG; COG5048; LUCA.
GeneTree; ENSGT00900000140802; -.
HOVERGEN; HBG005844; -.
InParanoid; P10070; -.
KO; K16798; -.
OMA; GQIHMYE; -.
OrthoDB; EOG091G01XS; -.
PhylomeDB; P10070; -.
TreeFam; TF350216; -.
Reactome; R-HSA-5610783; Degradation of GLI2 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-8941284; RUNX2 regulates chondrocyte maturation.
SignaLink; P10070; -.
SIGNOR; P10070; -.
ChiTaRS; GLI2; human.
GeneWiki; GLI2; -.
GenomeRNAi; 2736; -.
PRO; PR:P10070; -.
Proteomes; UP000005640; Chromosome 2.
Bgee; ENSG00000074047; -.
CleanEx; HS_GLI2; -.
ExpressionAtlas; P10070; baseline and differential.
Genevisible; P10070; 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; ISS:UniProtKB.
GO; GO:0005829; C:cytosol; TAS:Reactome.
GO; GO:0016020; C:membrane; IEA:Ensembl.
GO; GO:0031514; C:motile cilium; IEA:Ensembl.
GO; GO:0016607; C:nuclear speck; IEA:Ensembl.
GO; GO:0005730; C:nucleolus; IDA:HPA.
GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
GO; GO:0005634; C:nucleus; IDA:UniProtKB.
GO; GO:0003700; F:DNA binding transcription factor activity; IDA:UniProtKB.
GO; GO:1990841; F:promoter-specific chromatin binding; IDA:UniProtKB.
GO; GO:0000978; F:RNA polymerase II proximal promoter sequence-specific DNA binding; IEA:Ensembl.
GO; GO:0000981; F:RNA polymerase II transcription factor activity, sequence-specific DNA binding; ISA:NTNU_SB.
GO; GO:0043565; F:sequence-specific DNA binding; IDA:UniProtKB.
GO; GO:0008134; F:transcription factor binding; IPI:UniProtKB.
GO; GO:0001077; F:transcriptional activator activity, RNA polymerase II proximal promoter sequence-specific DNA binding; IEA:Ensembl.
GO; GO:0008270; F:zinc ion binding; IDA:UniProtKB.
GO; GO:0009952; P:anterior/posterior pattern specification; IEA:Ensembl.
GO; GO:0007411; P:axon guidance; ISS:UniProtKB.
GO; GO:0048754; P:branching morphogenesis of an epithelial tube; ISS:UniProtKB.
GO; GO:0008283; P:cell proliferation; IDA:UniProtKB.
GO; GO:0071407; P:cellular response to organic cyclic compound; IEA:Ensembl.
GO; GO:0098586; P:cellular response to virus; IDA:UniProtKB.
GO; GO:0021696; P:cerebellar cortex morphogenesis; ISS:UniProtKB.
GO; GO:0002062; P:chondrocyte differentiation; IEA:Ensembl.
GO; GO:0090103; P:cochlea morphogenesis; IEA:Ensembl.
GO; GO:0048589; P:developmental growth; ISS:UniProtKB.
GO; GO:0048566; P:embryonic digestive tract development; ISS:UniProtKB.
GO; GO:0042733; P:embryonic digit morphogenesis; IEA:Ensembl.
GO; GO:0009913; P:epidermal cell differentiation; IDA:UniProtKB.
GO; GO:0021508; P:floor plate formation; ISS:UniProtKB.
GO; GO:0007507; P:heart development; ISS:UniProtKB.
GO; GO:0030902; P:hindbrain development; ISS:UniProtKB.
GO; GO:0007442; P:hindgut morphogenesis; ISS:UniProtKB.
GO; GO:0001701; P:in utero embryonic development; IEA:Ensembl.
GO; GO:0001822; P:kidney development; ISS:UniProtKB.
GO; GO:0030324; P:lung development; ISS:UniProtKB.
GO; GO:0030879; P:mammary gland development; ISS:UniProtKB.
GO; GO:0060603; P:mammary gland duct morphogenesis; IEA:Ensembl.
GO; GO:0043066; P:negative regulation of apoptotic process; IEA:Ensembl.
GO; GO:0032331; P:negative regulation of chondrocyte differentiation; IEA:Ensembl.
GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IDA:UniProtKB.
GO; GO:0048666; P:neuron development; ISS:UniProtKB.
GO; GO:0060032; P:notochord regression; IEA:Ensembl.
GO; GO:0042475; P:odontogenesis of dentin-containing tooth; ISS:UniProtKB.
GO; GO:0002076; P:osteoblast development; ISS:UniProtKB.
GO; GO:0001649; P:osteoblast differentiation; IDA:UniProtKB.
GO; GO:0007389; P:pattern specification process; ISS:UniProtKB.
GO; GO:0021983; P:pituitary gland development; ISS:UniProtKB.
GO; GO:0045740; P:positive regulation of DNA replication; IDA:UniProtKB.
GO; GO:0045666; P:positive regulation of neuron differentiation; IEA:Ensembl.
GO; GO:0033089; P:positive regulation of T cell differentiation in thymus; ISS:BHF-UCL.
GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IDA:UniProtKB.
GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IDA:UniProtKB.
GO; GO:0060513; P:prostatic bud formation; IEA:Ensembl.
GO; GO:0009954; P:proximal/distal pattern formation; ISS:UniProtKB.
GO; GO:0008589; P:regulation of smoothened signaling pathway; IEA:Ensembl.
GO; GO:0009612; P:response to mechanical stimulus; IEA:Ensembl.
GO; GO:0001501; P:skeletal system development; ISS:UniProtKB.
GO; GO:0007224; P:smoothened signaling pathway; IDA:UniProtKB.
GO; GO:0060831; P:smoothened signaling pathway involved in dorsal/ventral neural tube patterning; IEA:Ensembl.
GO; GO:0021938; P:smoothened signaling pathway involved in regulation of cerebellar granule cell precursor cell proliferation; 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; ISS:UniProtKB.
GO; GO:0021513; P:spinal cord dorsal/ventral patterning; ISS:UniProtKB.
GO; GO:0021965; P:spinal cord ventral commissure morphogenesis; ISS:UniProtKB.
GO; GO:0035295; P:tube development; ISS:UniProtKB.
GO; GO:0007418; P:ventral midline development; ISS:UniProtKB.
GO; GO:0021517; P:ventral spinal cord development; ISS:UniProtKB.
InterPro; IPR036236; Znf_C2H2_sf.
InterPro; IPR013087; Znf_C2H2_type.
SMART; SM00355; ZnF_C2H2; 5.
SUPFAM; SSF57667; SSF57667; 3.
PROSITE; PS00028; ZINC_FINGER_C2H2_1; 4.
PROSITE; PS50157; ZINC_FINGER_C2H2_2; 4.
1: Evidence at protein level;
Acetylation; Activator; Alternative splicing; Cell projection; Cilium;
Complete proteome; Cytoplasm; Developmental protein; Disease mutation;
DNA-binding; Holoprosencephaly; Isopeptide bond; Metal-binding;
Nucleus; Phosphoprotein; Reference proteome; Repeat; Repressor;
Transcription; Transcription regulation; Ubl conjugation; Zinc;
Zinc-finger.
CHAIN 1 1586 Zinc finger protein GLI2.
/FTId=PRO_0000354050.
ZN_FING 437 464 C2H2-type 1. {ECO:0000255|PROSITE-
ProRule:PRU00042}.
ZN_FING 475 497 C2H2-type 2; degenerate.
{ECO:0000255|PROSITE-ProRule:PRU00042}.
ZN_FING 503 527 C2H2-type 3. {ECO:0000255|PROSITE-
ProRule:PRU00042}.
ZN_FING 533 558 C2H2-type 4. {ECO:0000255|PROSITE-
ProRule:PRU00042}.
ZN_FING 564 589 C2H2-type 5. {ECO:0000255|PROSITE-
ProRule:PRU00042}.
COMPBIAS 789 876 Ser-rich.
MOD_RES 149 149 Phosphoserine.
{ECO:0000244|PubMed:20068231}.
MOD_RES 234 234 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:20068231}.
MOD_RES 236 236 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:20068231}.
MOD_RES 242 242 Phosphoserine.
{ECO:0000244|PubMed:20068231}.
MOD_RES 388 388 Phosphoserine; by DYRK2.
{ECO:0000269|PubMed:18455992}.
MOD_RES 725 725 Phosphothreonine.
{ECO:0000250|UniProtKB:Q0VGT2}.
MOD_RES 757 757 N6-acetyllysine; by EP300.
{ECO:0000269|PubMed:23762415}.
MOD_RES 1011 1011 Phosphoserine; by DYRK2.
{ECO:0000269|PubMed:18455992}.
VAR_SEQ 1 328 Missing (in isoform 1, isoform 2, isoform
3 and isoform 4).
{ECO:0000303|PubMed:8350401,
ECO:0000303|PubMed:9557682}.
/FTId=VSP_035708.
VAR_SEQ 394 410 Missing (in isoform 2 and isoform 4).
{ECO:0000303|PubMed:8350401,
ECO:0000303|PubMed:9557682}.
/FTId=VSP_006877.
VAR_SEQ 1149 1157 VSSGTVDAL -> ASATWLSGT (in isoform 3 and
isoform 4). {ECO:0000303|PubMed:8350401,
ECO:0000303|PubMed:9557682}.
/FTId=VSP_006878.
VAR_SEQ 1158 1586 Missing (in isoform 3 and isoform 4).
{ECO:0000303|PubMed:8350401,
ECO:0000303|PubMed:9557682}.
/FTId=VSP_006879.
VARIANT 449 449 D -> H (in dbSNP:rs13427953).
/FTId=VAR_047303.
VARIANT 479 479 R -> G (in HPE9; unknown pathological
significance; dbSNP:rs121917708).
{ECO:0000269|PubMed:17096318}.
/FTId=VAR_032975.
VARIANT 516 516 R -> P (in CJS; loss of DNA-binding; loss
of transcription factor activity).
{ECO:0000269|PubMed:23408573}.
/FTId=VAR_075214.
VARIANT 579 579 S -> I (in dbSNP:rs12618388).
/FTId=VAR_047304.
VARIANT 608 608 P -> L (in CJS; dbSNP:rs149800897).
{ECO:0000269|PubMed:20685856}.
/FTId=VAR_071700.
VARIANT 625 625 P -> S (in dbSNP:rs3099537).
/FTId=VAR_047305.
VARIANT 932 932 P -> S (in HPE9; unknown pathological
significance).
{ECO:0000269|PubMed:17096318}.
/FTId=VAR_032976.
VARIANT 1156 1156 A -> S (in dbSNP:rs3738880).
{ECO:0000269|PubMed:9557682}.
/FTId=VAR_047306.
VARIANT 1306 1306 D -> N (in dbSNP:rs12711538).
{ECO:0000269|PubMed:9557682}.
/FTId=VAR_047307.
VARIANT 1352 1352 M -> V (in CJS; associated with N-1520;
unknown pathological significance;
decreased transcription factor activity
when associated with N-1520;
dbSNP:rs149140724).
{ECO:0000269|PubMed:23408573}.
/FTId=VAR_075215.
VARIANT 1444 1445 ML -> IF (in CJS; unknown pathological
significance; decreased transcription
factor activity).
{ECO:0000269|PubMed:23408573}.
/FTId=VAR_075216.
VARIANT 1444 1444 M -> I (in dbSNP:rs146467786).
{ECO:0000269|PubMed:17096318,
ECO:0000269|PubMed:27535533}.
/FTId=VAR_032977.
VARIANT 1520 1520 D -> N (in CJS; associated with V-1352;
unknown pathological significance;
decreased transcription factor activity
when associated with V-1352;
dbSNP:rs114814747).
{ECO:0000269|PubMed:23408573}.
/FTId=VAR_075217.
VARIANT 1543 1543 R -> H (polymorphism; no effect on
transcription factor activity;
dbSNP:rs138987487).
{ECO:0000269|PubMed:23408573}.
/FTId=VAR_075218.
VARIANT 1554 1554 P -> L (in HPE9; unknown pathological
significance; dbSNP:rs767802807).
{ECO:0000269|PubMed:17096318}.
/FTId=VAR_032978.
CONFLICT 456 456 H -> Q (in Ref. 5; M20672).
{ECO:0000305}.
CONFLICT 718 719 QL -> HV (in Ref. 4; BAA03568/BAA03569).
{ECO:0000305}.
CONFLICT 923 925 PER -> AEG (in Ref. 1; BAA25665/BAA25667/
BAA25666/BAA25668). {ECO:0000305}.
CONFLICT 966 966 A -> T (in Ref. 1; BAA25665/BAA25667/
BAA25666/BAA25668). {ECO:0000305}.
SEQUENCE 1586 AA; 167783 MW; 86556112E13DE106 CRC64;
METSASATAS EKQEAKSGIL EAAGFPDPGK KASPLVVAAA AAAAVAAQGV PQHLLPPFHA
PLPIDMRHQE GRYHYEPHSV HGVHGPPALS GSPVISDISL IRLSPHPAGP GESPFNAPHP
YVNPHMEHYL RSVHSSPTLS MISAARGLSP ADVAQEHLKE RGLFGLPAPG TTPSDYYHQM
TLVAGHPAPY GDLLMQSGGA ASAPHLHDYL NPVDVSRFSS PRVTPRLSRK RALSISPLSD
ASLDLQRMIR TSPNSLVAYI NNSRSSSAAS GSYGHLSAGA LSPAFTFPHP INPVAYQQIL
SQQRGLGSAF GHTPPLIQPS PTFLAQQPMA LTSINATPTQ LSSSSNCLSD TNQNKQSSES
AVSSTVNPVA IHKRSKVKTE PEGLRPASPL ALTQGQVSGH GSCGCALPLS QEQLADLKED
LDRDDCKQEA EVVIYETNCH WEDCTKEYDT QEQLVHHINN EHIHGEKKEF VCRWQACTRE
QKPFKAQYML VVHMRRHTGE KPHKCTFEGC SKAYSRLENL KTHLRSHTGE KPYVCEHEGC
NKAFSNASDR AKHQNRTHSN EKPYICKIPG CTKRYTDPSS LRKHVKTVHG PDAHVTKKQR
NDVHLRTPLL KENGDSEAGT EPGGPESTEA SSTSQAVEDC LHVRAIKTES SGLCQSSPGA
QSSCSSEPSP LGSAPNNDSG VEMPGTGPGS LGDLTALDDT PPGADTSALA APSAGGLQLR
KHMTTMHRFE QLKKEKLKSL KDSCSWAGPT PHTRNTKLPP LPGSGSILEN FSGSGGGGPA
GLLPNPRLSE LSASEVTMLS QLQERRDSST STVSSAYTVS RRSSGISPYF SSRRSSEASP
LGAGRPHNAS SADSYDPIST DASRRSSEAS QCSGGSGLLN LTPAQQYSLR AKYAAATGGP
PPTPLPGLER MSLRTRLALL DAPERTLPAG CPRPLGPRRG SDGPTYGHGH AGAAPAFPHE
APGGGARRAS DPVRRPDALS LPRVQRFHST HNVNPGPLPP CADRRGLRLQ SHPSTDGGLA
RGAYSPRPPS ISENVAMEAV AAGVDGAGPE ADLGLPEDDL VLPDDVVQYI KAHASGALDE
GTGQVYPTES TGFSDNPRLP SPGLHGQRRM VAADSNVGPS APMLGGCQLG FGAPSSLNKN
NMPVQWNEVS SGTVDALASQ VKPPPFPQGN LAVVQQKPAF GQYPGYSPQG LQASPGGLDS
TQPHLQPRSG APSQGIPRVN YMQQLRQPVA GSQCPGMTTT MSPHACYGQV HPQLSPSTIS
GALNQFPQSC SNMPAKPGHL GHPQQTEVAP DPTTMGNRHR ELGVPDSALA GVPPPHPVQS
YPQQSHHLAA SMSQEGYHQV PSLLPARQPG FMEPQTGPMG VATAGFGLVQ PRPPLEPSPT
GRHRGVRAVQ QQLAYARATG HAMAAMPSSQ ETAEAVPKGA MGNMGSVPPQ PPPQDAGGAP
DHSMLYYYGQ IHMYEQDGGL ENLGSCQVMR SQPPQPQACQ DSIQPQPLPS PGVNQVSSTV
DSQLLEAPQI DFDAIMDDGD HSSLFSGALS PSLLHSLSQN SSRLTTPRNS LTLPSIPAGI
SNMAVGDMSS MLTSLAEESK FLNMMT


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