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Protein

Transcriptional activator GLI3

Gene

Gli3

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: 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'.5 Publications

Regions

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

GO - Molecular functioni

GO - Biological processi

  • anatomical structure development Source: MGI
  • anatomical structure formation involved in morphogenesis Source: MGI
  • anterior/posterior pattern specification Source: MGI
  • anterior semicircular canal development Source: MGI
  • artery development Source: MGI
  • axon guidance Source: MGI
  • brain development Source: MGI
  • branching involved in ureteric bud morphogenesis Source: MGI
  • branching morphogenesis of an epithelial tube Source: MGI
  • camera-type eye development Source: MGI
  • camera-type eye morphogenesis Source: MGI
  • cell differentiation involved in kidney development Source: MGI
  • central nervous system development Source: MGI
  • cerebral cortex radial glia guided migration Source: MGI
  • developmental growth Source: MGI
  • dorsal/ventral pattern formation Source: MGI
  • embryonic digestive tract development Source: MGI
  • embryonic digestive tract morphogenesis Source: MGI
  • embryonic digit morphogenesis Source: MGI
  • embryonic limb morphogenesis Source: MGI
  • embryonic morphogenesis Source: MGI
  • embryonic skeletal system morphogenesis Source: MGI
  • forebrain development Source: MGI
  • forebrain dorsal/ventral pattern formation Source: MGI
  • forebrain radial glial cell differentiation Source: MGI
  • frontal suture morphogenesis Source: MGI
  • heart development Source: MGI
  • hindgut morphogenesis Source: MGI
  • hippocampus development Source: MGI
  • inner ear development Source: MGI
  • in utero embryonic development Source: MGI
  • kidney development Source: MGI
  • lambdoid suture morphogenesis Source: MGI
  • lateral ganglionic eminence cell proliferation Source: MGI
  • lateral semicircular canal development Source: MGI
  • layer formation in cerebral cortex Source: MGI
  • limb development Source: UniProtKB
  • limb morphogenesis Source: MGI
  • lung development Source: MGI
  • mammary gland development Source: MGI
  • mammary gland specification Source: MGI
  • melanocyte differentiation Source: MGI
  • metanephros development Source: MGI
  • negative regulation of alpha-beta T cell differentiation Source: BHF-UCL
  • negative regulation of apoptotic process Source: MGI
  • negative regulation of canonical Wnt signaling pathway Source: MGI
  • negative regulation of cell differentiation Source: MGI
  • negative regulation of cell proliferation Source: MGI
  • negative regulation of neuron differentiation Source: MGI
  • negative regulation of smoothened signaling pathway Source: BHF-UCL
  • negative regulation of transcription, DNA-templated Source: UniProtKB
  • negative regulation of transcription from RNA polymerase II promoter Source: MGI
  • negative thymic T cell selection Source: BHF-UCL
  • neural tube development Source: MGI
  • neuron fate commitment Source: MGI
  • odontogenesis of dentin-containing tooth Source: MGI
  • oligodendrocyte differentiation Source: MGI
  • optic nerve morphogenesis Source: MGI
  • palate development Source: MGI
  • pallium development Source: MGI
  • pattern specification process Source: MGI
  • positive regulation of alpha-beta T cell differentiation Source: BHF-UCL
  • positive regulation of chondrocyte differentiation Source: MGI
  • positive regulation of neuroblast proliferation Source: MGI
  • positive regulation of osteoblast differentiation Source: MGI
  • positive regulation of protein import into nucleus Source: MGI
  • positive regulation of transcription, DNA-templated Source: UniProtKB
  • positive regulation of transcription from RNA polymerase II promoter Source: BHF-UCL
  • protein processing Source: MGI
  • proximal/distal pattern formation Source: MGI
  • regulation of apoptotic process Source: MGI
  • regulation of cell differentiation Source: MGI
  • regulation of cell proliferation Source: MGI
  • regulation of gene expression Source: MGI
  • regulation of transcription, DNA-templated Source: MGI
  • response to estrogen Source: Ensembl
  • sagittal suture morphogenesis Source: MGI
  • smoothened signaling pathway Source: MGI
  • smoothened signaling pathway involved in dorsal/ventral neural tube patterning Source: MGI
  • smoothened signaling pathway involved in spinal cord motor neuron cell fate specification Source: MGI
  • smoothened signaling pathway involved in ventral spinal cord interneuron specification Source: MGI
  • spinal cord dorsal/ventral patterning Source: MGI
  • spinal cord motor neuron differentiation Source: MGI
  • subpallium development Source: MGI
  • T cell differentiation in thymus Source: BHF-UCL
  • telencephalon development Source: MGI
  • thymocyte apoptotic process Source: BHF-UCL
  • tongue development Source: MGI
  • transcription, DNA-templated Source: UniProtKB-KW
  • tube development Source: MGI
  • 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

ReactomeiREACT_278699. Hedgehog 'off' state.
REACT_351311. Hedgehog 'on' state.
REACT_353777. GLI3 is processed to GLI3R by the proteasome.

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
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589 Componenti: Chromosome 13

Organism-specific databases

MGIiMGI:95729. Gli3.

Subcellular locationi

  • Nucleus 1 Publication
  • Cytoplasm 1 Publication
  • Cell projectioncilium 1 Publication

  • Note: Translocation to the nucleus is promoted by interaction with ZIC1 (By similarity). GLI3FL is localized predominantly in the cytoplasm while GLI3R resides mainly in the nucleus. Ciliary accumulation requires the presence of KIF7 and SMO.By similarity

GO - Cellular componenti

  • axoneme Source: CACAO
  • cilium Source: MGI
  • cytoplasm Source: UniProtKB
  • cytosol Source: MGI
  • mediator complex Source: Ensembl
  • nuclear speck Source: MGI
  • nucleus Source: UniProtKB
  • primary cilium Source: BHF-UCL
  • transcriptional repressor complex Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Cell projection, Cilium, Cytoplasm, Nucleus

Pathology & Biotechi

Involvement in diseasei

Several mutations result in developmental defects of cranofacial and limb structures. In particular the add (anterior digit-pattern deformity) and pdn (polydactyly Nagoya) alleles.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 15831583Transcriptional activator GLI3PRO_0000047203Add
BLAST
Chaini1 – ?Transcriptional repressor GLI3RPRO_0000406138

Amino acid modifications

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

Post-translational modificationi

Phosphorylated by DYRK2 (in vitro) (By similarity). Phosphorylated on multiple sites by protein kinase A (PKA) and phosphorylation by PKA primes further phosphorylation by CK1 and GSK3. Phosphorylation is essential for its proteolytic processing.By similarity1 Publication
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 ULK3.1 Publication

Keywords - PTMi

Acetylation, Isopeptide bond, Phosphoprotein, Ubl conjugation

Proteomic databases

MaxQBiQ61602.
PaxDbiQ61602.
PRIDEiQ61602.

PTM databases

PhosphoSiteiQ61602.

Expressioni

Gene expression databases

BgeeiQ61602.
CleanExiMM_GLI3.
ExpressionAtlasiQ61602. baseline and differential.
GenevisibleiQ61602. MM.

Interactioni

Subunit structurei

The phosphorylated form interacts with BTRC (By similarity). 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. Interacts with KIF7. The activator form of GLI3 (GLI3A) but not the repressor form (GLI3R) can interact with TRPS1. Interacts with ZIC1. Interacts with ZIC3 (via C2H2-type domains 3, 4 and 5); the interaction enhances its transcriptional activity (By similarity).By similarity

Protein-protein interaction databases

BioGridi199944. 7 interactions.
STRINGi10090.ENSMUSP00000106137.

Structurei

3D structure databases

ProteinModelPortaliQ61602.
SMRiQ61602. Positions 479-633.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi120 – 19980Pro-richAdd
BLAST
Compositional biasi849 – 91062Ser-richAdd
BLAST
Compositional biasi1494 – 151421Asp/Glu-rich (acidic)Add
BLAST

Sequence similaritiesi

Contains 5 C2H2-type zinc fingers.PROSITE-ProRule annotation

Zinc finger

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

Keywords - Domaini

Repeat, Zinc-finger

Phylogenomic databases

eggNOGiCOG5048.
GeneTreeiENSGT00760000118771.
HOGENOMiHOG000290688.
HOVERGENiHBG005844.
InParanoidiQ61602.
KOiK06230.
OMAiPRDSGSH.
PhylomeDBiQ61602.
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.

Q61602-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MEAQAHSSTA TERKKAENSI GKCPTRTDVS EKAVASSTTS NEDESPGQIY
60 70 80 90 100
HRERRNAITM QPQSVQGLNK ISEEPSTSSD ERASLIKKEI HGSLPHLAEP
110 120 130 140 150
SLPYRGTVFA MDPRNGYMEP HYHPPHLFPA FHPPVPIDAR HHEGRYHYDP
160 170 180 190 200
SPIPPLHVPS ALSSSPTYPD LPFIRISPHR NPTAASESPF SPPHPYINPY
210 220 230 240 250
MDYIRSLHSS PSLSMISAAR GLSPTDAPHA GVSPAEYYHQ MALLTGQRSP
260 270 280 290 300
YADILPSAAT AGAGAIHMEY LHAMDSTRFP SPRLSARPSR KRTLSISPLS
310 320 330 340 350
DHSFDLQTMI RTSPNSLVTI LNNSRSSSSA SGSYGHLSAS AISPALSFTY
360 370 380 390 400
PSAPVSLHMH QQILSRQQSL GSAFGHSPPL IHPAPTFPTQ RPIPGIPTVL
410 420 430 440 450
NPVQVSSGPS ESSQSKPTSE SAVSSTGDPM HNKRSKIKPD EDLPSPGSRG
460 470 480 490 500
QQEQPEGTTL VKEEADKDES KQEPEVIYET NCHWEGCTRE FDTQDQLVHH
510 520 530 540 550
INNDHIHGEK KEFVCRWLDC SREQKPFKAQ YMLVVHMRRH TGEKPHKCTF
560 570 580 590 600
EGCTKAYSRL ENLKTHLRSH TGEKPYVCEH EGCNKAFSNA SDRAKHQNRT
610 620 630 640 650
HSNEKPYVCK IPGCTKRYTD PSSLRKHVKT VHGPEAHVTK KQRGDMHPRP
660 670 680 690 700
PPPRDSGSHS QSRSPGRPTQ GAFGEQKELS NTTSKREECL QVKTVKAEKP
710 720 730 740 750
MTSQPSPGGQ SSCSSQQSPI SNYSNSGLEL PLTDGGSVAD LSAIDETPIM
760 770 780 790 800
DSTISTATTA LALQARRNPA GTKWMEHIKL ERLKQVNGMF PRLNPILPSK
810 820 830 840 850
APAVSPLIGN GTQSNNNYSS GGPGTLLPSR SDLSGVDFTV LNTLNRRDSN
860 870 880 890 900
TSTISSAYLS SRRSSGISPC FSSRRSSEAS QAEGRPQNVS VADSYDPIST
910 920 930 940 950
DASRRSSEAS QGDGLPSLLS LTPVQQYRLK AKYAAATGGP PPTPLPHMER
960 970 980 990 1000
LSLKTKMALL GEGRDSGVTL PPVHPPRRCS DGGGHTYRGR HLMPHDALAN
1010 1020 1030 1040 1050
SVRRASDPVR TVSENMSLAR VQRFSSLNSF NPPNLPPSVE KRSLVLQNYT
1060 1070 1080 1090 1100
RQESSQPRYF QASPCPPSIT ENVALEALTM DADANLNDED LLPDDVVQYL
1110 1120 1130 1140 1150
NSQNQTGYGQ QLQSGISEDS KVAHEPEDLD LAGLPDSHVG QEYPALEQPC
1160 1170 1180 1190 1200
SEGSKTDLPI QWNEVSSGTS DLSSSKLKCG QQRPSAQQPR GFGLYNNMVV
1210 1220 1230 1240 1250
HPHNLWKVGT GPAGGYQTLG ENSSTYNGPE HFAIHSGDGL GTNGNTFHEQ
1260 1270 1280 1290 1300
PFKTQQYGSQ LNRQPLTSSA LDHACGTGIQ GSKLKGNSLQ ENGGLLDFSL
1310 1320 1330 1340 1350
SVAPNELAGN TVNGMQTQDQ MGQGYIAHQL LSGSMQHQGP SRPGQQVLGQ
1360 1370 1380 1390 1400
VGATSHINIY QGTESCLPGT QDNSSQPSSM AAIRGYQPCA SYGGNRRQAM
1410 1420 1430 1440 1450
PRGNLTLQQG QLSDMSQSSR VNSIKMEAQG QSQQLCSTVQ NYSGQFYDQT
1460 1470 1480 1490 1500
MGFSQQDRKA GSFSLSDANC LLQGNGTENS ELLSPGANQV TSTVDSFESH
1510 1520 1530 1540 1550
DLEGVQIDFD AIIDDGDHTS LMSGALSPSI IQNLSHSSSR LTTPRASLPF
1560 1570 1580
PSLSMGTTNM AIGDMSSLLT SLAEESKFLA VMQ
Length:1,583
Mass (Da):171,655
Last modified:September 11, 2007 - v2
Checksum:i37ECC0C3ACF26C24
GO

Sequence cautioni

The sequence CAA64543.1 differs from that shown. Reason: Frameshift at position 1552. Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti209 – 2091S → C in CAA64543 (PubMed:8688459).Curated
Sequence conflicti428 – 4281D → G in CAA64543 (PubMed:8688459).Curated
Sequence conflicti928 – 9281R → A in CAA64543 (PubMed:8688459).Curated
Sequence conflicti936 – 9361A → P in CAA64543 (PubMed:8688459).Curated
Sequence conflicti1005 – 10051A → D in CAA64543 (PubMed:8688459).Curated
Sequence conflicti1185 – 11862SA → R in CAA64543 (PubMed:8688459).Curated
Sequence conflicti1475 – 14762NG → TC in CAA64543 (PubMed:8688459).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X95255 mRNA. Translation: CAA64543.1. Frameshift.
AC163610 Genomic DNA. No translation available.
AC173115 Genomic DNA. No translation available.
AC173210 Genomic DNA. No translation available.
CCDSiCCDS36603.1.
RefSeqiNP_032156.2. NM_008130.2.
XP_006516617.1. XM_006516554.2.
UniGeneiMm.5098.

Genome annotation databases

EnsembliENSMUST00000110510; ENSMUSP00000106137; ENSMUSG00000021318.
GeneIDi14634.
KEGGimmu:14634.
UCSCiuc007pns.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X95255 mRNA. Translation: CAA64543.1. Frameshift.
AC163610 Genomic DNA. No translation available.
AC173115 Genomic DNA. No translation available.
AC173210 Genomic DNA. No translation available.
CCDSiCCDS36603.1.
RefSeqiNP_032156.2. NM_008130.2.
XP_006516617.1. XM_006516554.2.
UniGeneiMm.5098.

3D structure databases

ProteinModelPortaliQ61602.
SMRiQ61602. Positions 479-633.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi199944. 7 interactions.
STRINGi10090.ENSMUSP00000106137.

PTM databases

PhosphoSiteiQ61602.

Proteomic databases

MaxQBiQ61602.
PaxDbiQ61602.
PRIDEiQ61602.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000110510; ENSMUSP00000106137; ENSMUSG00000021318.
GeneIDi14634.
KEGGimmu:14634.
UCSCiuc007pns.1. mouse.

Organism-specific databases

CTDi2737.
MGIiMGI:95729. Gli3.

Phylogenomic databases

eggNOGiCOG5048.
GeneTreeiENSGT00760000118771.
HOGENOMiHOG000290688.
HOVERGENiHBG005844.
InParanoidiQ61602.
KOiK06230.
OMAiPRDSGSH.
PhylomeDBiQ61602.
TreeFamiTF350216.

Enzyme and pathway databases

ReactomeiREACT_278699. Hedgehog 'off' state.
REACT_351311. Hedgehog 'on' state.
REACT_353777. GLI3 is processed to GLI3R by the proteasome.

Miscellaneous databases

NextBioi286490.
PROiQ61602.
SOURCEiSearch...

Gene expression databases

BgeeiQ61602.
CleanExiMM_GLI3.
ExpressionAtlasiQ61602. baseline and differential.
GenevisibleiQ61602. MM.

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]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Cloning and sequence analysis of the murine Gli3 cDNA."
    Thien H., Buescher D., Ruether U.
    Biochim. Biophys. Acta 1307:267-269(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Strain: NIH Swiss.
  2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: C57BL/6J.
  3. "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.
  4. "Molecular properties of Zic proteins as transcriptional regulators and their relationship to GLI proteins."
    Mizugishi K., Aruga J., Nakata K., Mikoshiba K.
    J. Biol. Chem. 276:2180-2188(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, DNA-BINDING.
  5. "The Shh-independent activator function of the full-length Gli3 protein and its role in vertebrate limb digit patterning."
    Wang C., Ruther U., Wang B.
    Dev. Biol. 305:460-469(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  6. "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: PROTEOLYTIC PROCESSING.
  7. "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: FUNCTION, INTERACTION WITH TRPS1.
  8. "The kinesin protein Kif7 is a critical regulator of Gli transcription factors in mammalian hedgehog signaling."
    Cheung H.O., Zhang X., Ribeiro A., Mo R., Makino S., Puviindran V., Law K.K., Briscoe J., Hui C.C.
    Sci. Signal. 2:RA29-RA29(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH KIF7.
  9. "The output of Hedgehog signaling is controlled by the dynamic association between Suppressor of Fused and the Gli proteins."
    Humke E.W., Dorn K.V., Milenkovic L., Scott M.P., Rohatgi R.
    Genes Dev. 24:670-682(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION, PHOSPHORYLATION, INTERACTION WITH SUFU.

Entry informationi

Entry nameiGLI3_MOUSE
AccessioniPrimary (citable) accession number: Q61602
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: September 11, 2007
Last modified: June 24, 2015
This is version 135 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.