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P10071

- GLI3_HUMAN

UniProt

P10071 - GLI3_HUMAN

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Protein

Transcriptional activator GLI3

Gene
GLI3
Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

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'.3 Publications

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri480 – 50526C2H2-type 1Add
BLAST
Zinc fingeri513 – 54028C2H2-type 2Add
BLAST
Zinc fingeri546 – 57025C2H2-type 3Add
BLAST
Zinc fingeri576 – 60126C2H2-type 4Add
BLAST
Zinc fingeri607 – 63226C2H2-type 5Add
BLAST

GO - Molecular functioni

  1. beta-catenin binding Source: UniProtKB
  2. chromatin binding Source: Ensembl
  3. histone acetyltransferase binding Source: UniProtKB
  4. histone deacetylase binding Source: UniProtKB
  5. metal ion binding Source: UniProtKB-KW
  6. protein binding Source: UniProtKB
  7. RNA polymerase II core promoter proximal region sequence-specific DNA binding Source: MGI
  8. sequence-specific DNA binding transcription factor activity Source: UniProtKB

GO - Biological processi

  1. anterior/posterior pattern specification Source: Ensembl
  2. anterior semicircular canal development Source: Ensembl
  3. artery development Source: Ensembl
  4. axon guidance Source: Ensembl
  5. branching involved in ureteric bud morphogenesis Source: Ensembl
  6. camera-type eye morphogenesis Source: Ensembl
  7. cell differentiation involved in kidney development Source: Ensembl
  8. cerebral cortex radial glia guided migration Source: Ensembl
  9. developmental growth Source: Ensembl
  10. embryonic digestive tract development Source: BHF-UCL
  11. embryonic digestive tract morphogenesis Source: Ensembl
  12. embryonic digit morphogenesis Source: BHF-UCL
  13. embryonic skeletal system morphogenesis Source: Ensembl
  14. forebrain dorsal/ventral pattern formation Source: Ensembl
  15. forebrain radial glial cell differentiation Source: Ensembl
  16. frontal suture morphogenesis Source: Ensembl
  17. heart development Source: Ensembl
  18. hindgut morphogenesis Source: Ensembl
  19. in utero embryonic development Source: Ensembl
  20. lambdoid suture morphogenesis Source: Ensembl
  21. lateral ganglionic eminence cell proliferation Source: Ensembl
  22. lateral semicircular canal development Source: Ensembl
  23. limb morphogenesis Source: UniProtKB
  24. lung development Source: Ensembl
  25. mammary gland specification Source: Ensembl
  26. melanocyte differentiation Source: Ensembl
  27. metanephros development Source: Ensembl
  28. negative regulation of alpha-beta T cell differentiation Source: BHF-UCL
  29. negative regulation of apoptotic process Source: Ensembl
  30. negative regulation of canonical Wnt signaling pathway Source: UniProtKB
  31. negative regulation of cell proliferation Source: Ensembl
  32. negative regulation of neuron differentiation Source: Ensembl
  33. negative regulation of smoothened signaling pathway Source: BHF-UCL
  34. negative regulation of transcription, DNA-templated Source: UniProtKB
  35. negative regulation of transcription from RNA polymerase II promoter Source: UniProtKB
  36. negative thymic T cell selection Source: BHF-UCL
  37. nose morphogenesis Source: BHF-UCL
  38. odontogenesis of dentin-containing tooth Source: Ensembl
  39. oligodendrocyte differentiation Source: Ensembl
  40. optic nerve morphogenesis Source: Ensembl
  41. palate development Source: Ensembl
  42. positive regulation of alpha-beta T cell differentiation Source: BHF-UCL
  43. positive regulation of chondrocyte differentiation Source: Ensembl
  44. positive regulation of neuroblast proliferation Source: Ensembl
  45. positive regulation of osteoblast differentiation Source: Ensembl
  46. positive regulation of protein import into nucleus Source: Ensembl
  47. positive regulation of transcription, DNA-templated Source: UniProtKB
  48. positive regulation of transcription from RNA polymerase II promoter Source: UniProtKB
  49. protein processing Source: Ensembl
  50. proximal/distal pattern formation Source: Ensembl
  51. response to estrogen Source: Ensembl
  52. sagittal suture morphogenesis Source: Ensembl
  53. smoothened signaling pathway Source: BHF-UCL
  54. smoothened signaling pathway involved in dorsal/ventral neural tube patterning Source: Ensembl
  55. smoothened signaling pathway involved in spinal cord motor neuron cell fate specification Source: Ensembl
  56. smoothened signaling pathway involved in ventral spinal cord interneuron specification Source: Ensembl
  57. T cell differentiation in thymus Source: BHF-UCL
  58. thymocyte apoptotic process Source: BHF-UCL
  59. tongue development Source: Ensembl
  60. transcription, DNA-templated Source: UniProtKB-KW
  61. wound healing Source: Ensembl
Complete GO annotation...

Keywords - Molecular functioni

Activator, Repressor

Keywords - Biological processi

Transcription, Transcription regulation

Keywords - Ligandi

DNA-binding, Metal-binding, Zinc

Enzyme and pathway databases

SignaLinkiP10071.

Names & Taxonomyi

Protein namesi
Recommended name:
Transcriptional activator GLI3
Alternative name(s):
GLI3 form of 190 kDa
Short name:
GLI3-190
GLI3 full length protein
Short name:
GLI3FL
Cleaved into the following chain:
Alternative name(s):
GLI3 C-terminally truncated form
GLI3 form of 83 kDa
Short name:
GLI3-83
Gene namesi
Name:GLI3
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 7

Organism-specific databases

HGNCiHGNC:4319. GLI3.

Subcellular locationi

Nucleus. Cytoplasm. Cell projectioncilium
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 ZIC1.2 Publications

GO - Cellular componenti

  1. cilium Source: UniProtKB
  2. cytoplasm Source: UniProtKB
  3. cytosol Source: UniProtKB
  4. nuclear speck Source: Ensembl
  5. nucleus Source: UniProtKB
  6. primary cilium Source: Ensembl
  7. transcriptional repressor complex Source: Ensembl
Complete GO annotation...

Keywords - Cellular componenti

Cell projection, Cilium, Cytoplasm, Nucleus

Pathology & Biotechi

Involvement in diseasei

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.
Note: The disease is caused by mutations affecting the gene represented in this entry.4 Publications
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti515 – 5151C → G in GCPS. 1 Publication
VAR_010053
Natural varianti520 – 5201C → Y in GCPS. 1 Publication
VAR_010054
Natural varianti625 – 6251R → W in GCPS. 1 Publication
VAR_021481
Natural varianti707 – 7071P → S in GCPS. 1 Publication
VAR_010055
Natural varianti808 – 8081I → M in GCPS. 1 Publication
Corresponds to variant rs62622373 [ dbSNP | Ensembl ].
VAR_010056
Natural varianti934 – 9341A → P in GCPS; the patient was originally classifed as being affected by acrocallosal syndrome due to the absence of corpus callosum. 1 Publication
Corresponds to variant rs28933372 [ dbSNP | Ensembl ].
VAR_021482
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.
Note: The disease is caused by mutations affecting the gene represented in this entry.
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.
Note: The disease is caused by mutations affecting the gene represented in this entry.1 Publication
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti727 – 7271G → R in PAPA1 and PAPB. 1 Publication
Corresponds to variant rs121917710 [ dbSNP | Ensembl ].
VAR_009876
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.
Note: The disease is caused by mutations affecting the gene represented in this entry.1 Publication
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti727 – 7271G → R in PAPA1 and PAPB. 1 Publication
Corresponds to variant rs121917710 [ dbSNP | Ensembl ].
VAR_009876
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.
Note: The disease is caused by mutations affecting the gene represented in this entry.

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi773 – 7731K → R: Loss of proteolytic processing. 1 Publication
Mutagenesisi779 – 7791K → R: Loss of proteolytic processing. 1 Publication
Mutagenesisi784 – 7841K → R: Loss of proteolytic processing. 1 Publication
Mutagenesisi800 – 8001K → R: Loss of proteolytic processing. 1 Publication
Mutagenesisi849 – 8491S → A: Loss of phosphorylation and proteolytic processing. 2 Publications
Mutagenesisi855 – 8551S → A: Loss of proteolytic processing. 1 Publication
Mutagenesisi856 – 8561S → A: Loss of proteolytic processing. 1 Publication
Mutagenesisi861 – 8611S → A: Loss of proteolytic processing. 1 Publication
Mutagenesisi864 – 8641S → A: Loss of proteolytic processing. 1 Publication
Mutagenesisi865 – 8651S → A: Loss of phosphorylation and proteolytic processing. 1 Publication
Mutagenesisi873 – 8731S → A: Loss of proteolytic processing. 1 Publication
Mutagenesisi877 – 8771S → A: Loss of phosphorylation and proteolytic processing. 2 Publications
Mutagenesisi903 – 9031S → A: Loss of proteolytic processing. 1 Publication
Mutagenesisi907 – 9071S → A: Loss of phosphorylation and proteolytic processing. 2 Publications
Mutagenesisi980 – 9801S → A: Loss of phosphorylation and proteolytic processing. 1 Publication
Mutagenesisi1006 – 10061S → A: Loss of phosphorylation and proteolytic processing. 1 Publication

Keywords - Diseasei

Disease mutation

Organism-specific databases

MIMi146510. phenotype.
174200. phenotype.
174700. phenotype.
175700. phenotype.
Orphaneti36. Acrocallosal syndrome.
380. Greig cephalopolysyndactyly syndrome.
672. Pallister-Hall syndrome.
295161. Polysyndactyly, bilateral.
295159. Polysyndactyly, unilateral.
295165. Postaxial polydactyly type A, bilateral.
295163. Postaxial polydactyly type A, unilateral.
295169. Postaxial polydactyly type B, bilateral.
295167. Postaxial polydactyly type B, unilateral.
PharmGKBiPA28722.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 15801580Transcriptional activator GLI3PRO_0000047202Add
BLAST
Chaini1 – ?Transcriptional repressor GLI3RPRO_0000406137

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei1 – 11N-acetylmethionine1 Publication
Modified residuei664 – 6641Phosphoserine1 Publication
Cross-linki773 – 773Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)1 Publication
Cross-linki779 – 779Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)1 Publication
Cross-linki784 – 784Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)1 Publication
Cross-linki800 – 800Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)1 Publication
Modified residuei849 – 8491Phosphoserine; by PKA1 Publication
Modified residuei865 – 8651Phosphoserine; by PKA1 Publication
Modified residuei877 – 8771Phosphoserine; by PKA1 Publication
Modified residuei907 – 9071Phosphoserine; by PKA1 Publication
Modified residuei980 – 9801Phosphoserine; by PKA1 Publication
Modified residuei1006 – 10061Phosphoserine; by PKA1 Publication

Post-translational modificationi

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.5 Publications
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 ULK3.5 Publications

Keywords - PTMi

Acetylation, Isopeptide bond, Phosphoprotein, Ubl conjugation

Proteomic databases

MaxQBiP10071.
PaxDbiP10071.
PRIDEiP10071.

PTM databases

PhosphoSiteiP10071.

Expressioni

Tissue specificityi

Is expressed in a wide variety of normal adult tissues, including lung, colon, spleen, placenta, testis, and myometrium.

Gene expression databases

ArrayExpressiP10071.
BgeeiP10071.
CleanExiHS_GLI3.
GenevestigatoriP10071.

Organism-specific databases

HPAiHPA005534.

Interactioni

Subunit structurei

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.6 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
Zic1P466842EBI-308055,EBI-308006From a different organism.
Zic2Q625202EBI-308055,EBI-308076From a different organism.

Protein-protein interaction databases

BioGridi108999. 20 interactions.
DIPiDIP-32538N.
IntActiP10071. 9 interactions.
MINTiMINT-189869.
STRINGi9606.ENSP00000379255.

Structurei

Secondary structure

1
1580
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi334 – 3374

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4BLDX-ray2.80E/F/G/H328-344[»]
ProteinModelPortaliP10071.

Family & Domainsi

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi1492 – 151221Asp/Glu-rich (acidic)Add
BLAST

Sequence similaritiesi

Zinc finger

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri480 – 50526C2H2-type 1Add
BLAST
Zinc fingeri513 – 54028C2H2-type 2Add
BLAST
Zinc fingeri546 – 57025C2H2-type 3Add
BLAST
Zinc fingeri576 – 60126C2H2-type 4Add
BLAST
Zinc fingeri607 – 63226C2H2-type 5Add
BLAST

Keywords - Domaini

Repeat, Zinc-finger

Phylogenomic databases

eggNOGiCOG5048.
HOVERGENiHBG005844.
InParanoidiP10071.
KOiK06230.
OMAiPRDSGSH.
OrthoDBiEOG7X6KZ8.
PhylomeDBiP10071.
TreeFamiTF350216.

Family and domain databases

Gene3Di3.30.160.60. 5 hits.
InterProiIPR007087. Znf_C2H2.
IPR015880. Znf_C2H2-like.
IPR013087. Znf_C2H2/integrase_DNA-bd.
[Graphical view]
PfamiPF00096. zf-C2H2. 1 hit.
[Graphical view]
SMARTiSM00355. ZnF_C2H2. 5 hits.
[Graphical view]
PROSITEiPS00028. ZINC_FINGER_C2H2_1. 4 hits.
PS50157. ZINC_FINGER_C2H2_2. 5 hits.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P10071-1 [UniParc]FASTAAdd to Basket

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MEAQSHSSTT TEKKKVENSI VKCSTRTDVS EKAVASSTTS NEDESPGQTY     50
HRERRNAITM QPQNVQGLSK VSEEPSTSSD ERASLIKKEI HGSLPHVAEP 100
SVPYRGTVFA MDPRNGYMEP HYHPPHLFPA FHPPVPIDAR HHEGRYHYDP 150
SPIPPLHMTS ALSSSPTYPD LPFIRISPHR NPTAASESPF SPPHPYINPY 200
MDYIRSLHSS PSLSMISATR GLSPTDAPHA GVSPAEYYHQ MALLTGQRSP 250
YADIIPSAAT AGTGAIHMEY LHAMDSTRFS SPRLSARPSR KRTLSISPLS 300
DHSFDLQTMI RTSPNSLVTI LNNSRSSSSA SGSYGHLSAS AISPALSFTY 350
SSAPVSLHMH QQILSRQQSL GSAFGHSPPL IHPAPTFPTQ RPIPGIPTVL 400
NPVQVSSGPS ESSQNKPTSE SAVSSTGDPM HNKRSKIKPD EDLPSPGARG 450
QQEQPEGTTL VKEEGDKDES KQEPEVIYET NCHWEGCARE FDTQEQLVHH 500
INNDHIHGEK KEFVCRWLDC SREQKPFKAQ YMLVVHMRRH TGEKPHKCTF 550
EGCTKAYSRL ENLKTHLRSH TGEKPYVCEH EGCNKAFSNA SDRAKHQNRT 600
HSNEKPYVCK IPGCTKRYTD PSSLRKHVKT VHGPEAHVTK KQRGDIHPRP 650
PPPRDSGSHS QSRSPGRPTQ GALGEQQDLS NTTSKREECL QVKTVKAEKP 700
MTSQPSPGGQ SSCSSQQSPI SNYSNSGLEL PLTDGGSIGD LSAIDETPIM 750
DSTISTATTA LALQARRNPA GTKWMEHVKL ERLKQVNGMF PRLNPILPPK 800
APAVSPLIGN GTQSNNTCSL GGPMTLLPGR SDLSGVDVTM LNMLNRRDSS 850
ASTISSAYLS SRRSSGISPC FSSRRSSEAS QAEGRPQNVS VADSYDPIST 900
DASRRSSEAS QSDGLPSLLS LTPAQQYRLK AKYAAATGGP PPTPLPNMER 950
MSLKTRLALL GDALEPGVAL PPVHAPRRCS DGGAHGYGRR HLQPHDAPGH 1000
GVRRASDPVR TGSEGLALPR VPRFSSLSSC NPPAMATSAE KRSLVLQNYT 1050
RPEGGQSRNF HSSPCPPSIT ENVTLESLTM DADANLNDED FLPDDVVQYL 1100
NSQNQAGYEQ HFPSALPDDS KVPHGPGDFD APGLPDSHAG QQFHALEQPC 1150
PEGSKTDLPI QWNEVSSGSA DLSSSKLKCG PRPAVPQTRA FGFCNGMVVH 1200
PQNPLRSGPA GGYQTLGENS NPYGGPEHLM LHNSPGSGTS GNAFHEQPCK 1250
APQYGNCLNR QPVAPGALDG ACGAGIQASK LKSTPMQGSG GQLNFGLPVA 1300
PNESAGSMVN GMQNQDPVGQ GYLAHQLLGD SMQHPGAGRP GQQMLGQISA 1350
TSHINIYQGP ESCLPGAHGM GSQPSSLAVV RGYQPCASFG GSRRQAMPRD 1400
SLALQSGQLS DTSQTCRVNG IKMEMKGQPH PLCSNLQNYS GQFYDQTVGF 1450
SQQDTKAGSF SISDASCLLQ GTSAKNSELL SPGANQVTST VDSLDSHDLE 1500
GVQIDFDAII DDGDHSSLMS GALSPSIIQN LSHSSSRLTT PRASLPFPAL 1550
SMSTTNMAIG DMSSLLTSLA EESKFLAVMQ 1580
Length:1,580
Mass (Da):169,863
Last modified:November 24, 2009 - v6
Checksum:i423B7495FCE3C37C
GO

Sequence cautioni

The sequence AAA52564.1 differs from that shown. Reason: Frameshift at position 1549.

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti169 – 1691P → L in a colorectal cancer sample; somatic mutation. 1 Publication
VAR_035560
Natural varianti183 – 1831T → A.3 Publications
Corresponds to variant rs846266 [ dbSNP | Ensembl ].
VAR_028276
Natural varianti440 – 4401D → E.1 Publication
VAR_010052
Natural varianti515 – 5151C → G in GCPS. 1 Publication
VAR_010053
Natural varianti520 – 5201C → Y in GCPS. 1 Publication
VAR_010054
Natural varianti625 – 6251R → W in GCPS. 1 Publication
VAR_021481
Natural varianti707 – 7071P → S in GCPS. 1 Publication
VAR_010055
Natural varianti727 – 7271G → R in PAPA1 and PAPB. 1 Publication
Corresponds to variant rs121917710 [ dbSNP | Ensembl ].
VAR_009876
Natural varianti808 – 8081I → M in GCPS. 1 Publication
Corresponds to variant rs62622373 [ dbSNP | Ensembl ].
VAR_010056
Natural varianti934 – 9341A → P in GCPS; the patient was originally classifed as being affected by acrocallosal syndrome due to the absence of corpus callosum. 1 Publication
Corresponds to variant rs28933372 [ dbSNP | Ensembl ].
VAR_021482
Natural varianti998 – 9981P → L.3 Publications
Corresponds to variant rs929387 [ dbSNP | Ensembl ].
VAR_028278
Natural varianti1304 – 13041S → P in a colorectal cancer sample; somatic mutation. 1 Publication
VAR_035561
Natural varianti1336 – 13361G → E.
Corresponds to variant rs35280470 [ dbSNP | Ensembl ].
VAR_034865
Natural varianti1537 – 15371R → C.1 Publication
Corresponds to variant rs35364414 [ dbSNP | Ensembl ].
VAR_010057

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
M57609 mRNA. Translation: AAA52564.1. Frameshift.
AJ250408 Genomic DNA. Translation: CAB59315.1.
AC005026 Genomic DNA. Translation: AAP21869.1.
AC005028 Genomic DNA. Translation: AAS01998.1.
AC005158 Genomic DNA. Translation: AAS02015.1.
AC073852 Genomic DNA. No translation available.
CH236951 Genomic DNA. Translation: EAL24002.1.
M20674 Genomic DNA. No translation available.
BC113616 mRNA. Translation: AAI13617.1.
BC117168 mRNA. Translation: AAI17169.1.
CCDSiCCDS5465.1.
PIRiA35927.
RefSeqiNP_000159.3. NM_000168.5.
XP_005249760.1. XM_005249703.1.
XP_005249761.1. XM_005249704.1.
UniGeneiHs.21509.

Genome annotation databases

EnsembliENST00000395925; ENSP00000379258; ENSG00000106571.
GeneIDi2737.
KEGGihsa:2737.
UCSCiuc011kbg.2. human.

Polymorphism databases

DMDMi269849770.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
M57609 mRNA. Translation: AAA52564.1 . Frameshift.
AJ250408 Genomic DNA. Translation: CAB59315.1 .
AC005026 Genomic DNA. Translation: AAP21869.1 .
AC005028 Genomic DNA. Translation: AAS01998.1 .
AC005158 Genomic DNA. Translation: AAS02015.1 .
AC073852 Genomic DNA. No translation available.
CH236951 Genomic DNA. Translation: EAL24002.1 .
M20674 Genomic DNA. No translation available.
BC113616 mRNA. Translation: AAI13617.1 .
BC117168 mRNA. Translation: AAI17169.1 .
CCDSi CCDS5465.1.
PIRi A35927.
RefSeqi NP_000159.3. NM_000168.5.
XP_005249760.1. XM_005249703.1.
XP_005249761.1. XM_005249704.1.
UniGenei Hs.21509.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
4BLD X-ray 2.80 E/F/G/H 328-344 [» ]
ProteinModelPortali P10071.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 108999. 20 interactions.
DIPi DIP-32538N.
IntActi P10071. 9 interactions.
MINTi MINT-189869.
STRINGi 9606.ENSP00000379255.

PTM databases

PhosphoSitei P10071.

Polymorphism databases

DMDMi 269849770.

Proteomic databases

MaxQBi P10071.
PaxDbi P10071.
PRIDEi P10071.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000395925 ; ENSP00000379258 ; ENSG00000106571 .
GeneIDi 2737.
KEGGi hsa:2737.
UCSCi uc011kbg.2. human.

Organism-specific databases

CTDi 2737.
GeneCardsi GC07M041970.
GeneReviewsi GLI3.
H-InvDB HIX0033636.
HGNCi HGNC:4319. GLI3.
HPAi HPA005534.
MIMi 146510. phenotype.
165240. gene.
174200. phenotype.
174700. phenotype.
175700. phenotype.
neXtProti NX_P10071.
Orphaneti 36. Acrocallosal syndrome.
380. Greig cephalopolysyndactyly syndrome.
672. Pallister-Hall syndrome.
295161. Polysyndactyly, bilateral.
295159. Polysyndactyly, unilateral.
295165. Postaxial polydactyly type A, bilateral.
295163. Postaxial polydactyly type A, unilateral.
295169. Postaxial polydactyly type B, bilateral.
295167. Postaxial polydactyly type B, unilateral.
PharmGKBi PA28722.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG5048.
HOVERGENi HBG005844.
InParanoidi P10071.
KOi K06230.
OMAi PRDSGSH.
OrthoDBi EOG7X6KZ8.
PhylomeDBi P10071.
TreeFami TF350216.

Enzyme and pathway databases

SignaLinki P10071.

Miscellaneous databases

ChiTaRSi GLI3. human.
GeneWikii GLI3.
GenomeRNAii 2737.
NextBioi 10788.
PROi P10071.
SOURCEi Search...

Gene expression databases

ArrayExpressi P10071.
Bgeei P10071.
CleanExi HS_GLI3.
Genevestigatori P10071.

Family and domain databases

Gene3Di 3.30.160.60. 5 hits.
InterProi IPR007087. Znf_C2H2.
IPR015880. Znf_C2H2-like.
IPR013087. Znf_C2H2/integrase_DNA-bd.
[Graphical view ]
Pfami PF00096. zf-C2H2. 1 hit.
[Graphical view ]
SMARTi SM00355. ZnF_C2H2. 5 hits.
[Graphical view ]
PROSITEi PS00028. ZINC_FINGER_C2H2_1. 4 hits.
PS50157. ZINC_FINGER_C2H2_2. 5 hits.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "GLI3 encodes a 190-kilodalton protein with multiple regions of GLI similarity."
    Ruppert J.M., Vogelstein B., Arheden K., Kinzler K.W.
    Mol. Cell. Biol. 10:5408-5415(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], VARIANTS ALA-183 AND LEU-998.
  2. Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANTS GCPS GLY-515; TYR-520 AND MET-808, VARIANTS ALA-183; GLU-440; LEU-998 AND CYS-1537.
  3. "The DNA sequence of human chromosome 7."
    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.
    Nature 424:157-164(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  4. "Human chromosome 7: DNA sequence and biology."
    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.
    Science 300:767-772(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  5. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], VARIANTS ALA-183 AND LEU-998.
    Tissue: Cerebellum.
  6. "The GLI-Kruppel family of human genes."
    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.
    Mol. Cell. Biol. 8:3104-3113(1988) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 500-549.
  7. "Hedgehog-regulated processing of Gli3 produces an anterior/posterior repressor gradient in the developing vertebrate limb."
    Wang B., Fallon J.F., Beachy P.A.
    Cell 100:423-434(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, PROTEOLYTIC PROCESSING, PHOSPHORYLATION AT SER-849; SER-865; SER-877; SER-907; SER-980 AND SER-1006, MUTAGENESIS OF SER-849; SER-865; SER-877; SER-907; SER-980 AND SER-1006.
  8. "Physical and functional interactions between Zic and Gli proteins."
    Koyabu Y., Nakata K., Mizugishi K., Aruga J., Mikoshiba K.
    J. Biol. Chem. 276:6889-6892(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH ZIC1, SUBCELLULAR LOCATION.
  9. "Multisite protein kinase A and glycogen synthase kinase 3beta phosphorylation leads to Gli3 ubiquitination by SCFbetaTrCP."
    Tempe D., Casas M., Karaz S., Blanchet-Tournier M.F., Concordet J.P.
    Mol. Cell. Biol. 26:4316-4326(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEOLYTIC PROCESSING, PHOSPHORYLATION, INTERACTION WITH BTRC, UBIQUITINATION AT LYS-773; LYS-779; LYS-784 AND LYS-800, 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.
  10. "Evidence for the direct involvement of {beta}TrCP in Gli3 protein processing."
    Wang B., Li Y.
    Proc. Natl. Acad. Sci. U.S.A. 103:33-38(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEOLYTIC PROCESSING, PHOSPHORYLATION, POLYUBIQUITINATION, INTERACTION WITH BTRC.
  11. "Application of active and kinase-deficient kinome collection for identification of kinases regulating hedgehog signaling."
    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.
    Cell 133:537-548(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION.
  12. "Characterization of the interactions of human ZIC3 mutants with GLI3."
    Zhu L., Zhou G., Poole S., Belmont J.W.
    Hum. Mutat. 29:99-105(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH ZIC3.
  13. "Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
    Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
    Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  14. "The mammalian Cos2 homolog Kif7 plays an essential role in modulating Hh signal transduction during development."
    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.
    Curr. Biol. 19:1320-1326(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION, INTERACTION WITH KIF7.
  15. "Trps1, a regulator of chondrocyte proliferation and differentiation, interacts with the activator form of Gli3."
    Wuelling M., Kaiser F.J., Buelens L.A., Braunholz D., Shivdasani R.A., Depping R., Vortkamp A.
    Dev. Biol. 328:40-53(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH TRPS1.
  16. "Identification of a novel serine/threonine kinase ULK3 as a positive regulator of Hedgehog pathway."
    Maloverjan A., Piirsoo M., Michelson P., Kogerman P., Osterlund T.
    Exp. Cell Res. 316:627-637(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION.
  17. "System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
    Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
    Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-664, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  18. Cited for: VARIANT GCPS SER-707.
  19. "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."
    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.
    Am. J. Hum. Genet. 65:645-655(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANT PAPA1 ARG-727, VARIANT PAPB ARG-727.
  20. "De novo GLI3 mutation in acrocallosal syndrome: broadening the phenotypic spectrum of GLI3 defects and overlap with murine models."
    Elson E., Perveen R., Donnai D., Wall S., Black G.C.M.
    J. Med. Genet. 39:804-806(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANT GCPS PRO-934.
  21. "Variable phenotype in Greig cephalopolysyndactyly syndrome: clinical and radiological findings in 4 independent families and 3 sporadic cases with identified GLI3 mutations."
    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.
    Am. J. Med. Genet. A 120:49-58(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANT GCPS TRP-625.
  22. Cited for: VARIANTS [LARGE SCALE ANALYSIS] LEU-169 AND PRO-1304.

Entry informationi

Entry nameiGLI3_HUMAN
AccessioniPrimary (citable) accession number: P10071
Secondary accession number(s): A4D1W1
, O75219, Q17RW4, Q75MT0, Q75MU9, Q9UDT5, Q9UJ39
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 1, 1989
Last sequence update: November 24, 2009
Last modified: July 9, 2014
This is version 156 of the entry and version 6 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 7
    Human chromosome 7: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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