Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

Q61602

- GLI3_MOUSE

UniProt

Q61602 - GLI3_MOUSE

(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Protein

Transcriptional activator GLI3

Gene

Gli3

Organism
Mus musculus (Mouse)
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'.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

  1. chromatin binding Source: MGI
  2. metal ion binding Source: UniProtKB-KW
  3. RNA polymerase II core promoter proximal region sequence-specific DNA binding Source: Ensembl
  4. sequence-specific DNA binding Source: MGI
  5. sequence-specific DNA binding transcription factor activity Source: UniProtKB

GO - Biological processi

  1. anatomical structure development Source: MGI
  2. anatomical structure formation involved in morphogenesis Source: MGI
  3. anterior/posterior pattern specification Source: MGI
  4. anterior semicircular canal development Source: MGI
  5. artery development Source: MGI
  6. axon guidance Source: MGI
  7. brain development Source: MGI
  8. branching involved in ureteric bud morphogenesis Source: MGI
  9. branching morphogenesis of an epithelial tube Source: MGI
  10. camera-type eye development Source: MGI
  11. camera-type eye morphogenesis Source: MGI
  12. cell differentiation involved in kidney development Source: MGI
  13. central nervous system development Source: MGI
  14. cerebral cortex radial glia guided migration Source: MGI
  15. developmental growth Source: MGI
  16. dorsal/ventral pattern formation Source: MGI
  17. embryonic digestive tract development Source: MGI
  18. embryonic digestive tract morphogenesis Source: MGI
  19. embryonic digit morphogenesis Source: MGI
  20. embryonic limb morphogenesis Source: MGI
  21. embryonic morphogenesis Source: MGI
  22. embryonic skeletal system morphogenesis Source: MGI
  23. forebrain development Source: MGI
  24. forebrain dorsal/ventral pattern formation Source: MGI
  25. forebrain radial glial cell differentiation Source: MGI
  26. frontal suture morphogenesis Source: MGI
  27. heart development Source: MGI
  28. hindgut morphogenesis Source: MGI
  29. hippocampus development Source: MGI
  30. inner ear development Source: MGI
  31. in utero embryonic development Source: MGI
  32. kidney development Source: MGI
  33. lambdoid suture morphogenesis Source: MGI
  34. lateral ganglionic eminence cell proliferation Source: MGI
  35. lateral semicircular canal development Source: MGI
  36. limb development Source: UniProtKB
  37. limb morphogenesis Source: MGI
  38. lung development Source: MGI
  39. mammary gland development Source: MGI
  40. mammary gland specification Source: MGI
  41. melanocyte differentiation Source: MGI
  42. metanephros development Source: MGI
  43. negative regulation of alpha-beta T cell differentiation Source: BHF-UCL
  44. negative regulation of apoptotic process Source: MGI
  45. negative regulation of canonical Wnt signaling pathway Source: Ensembl
  46. negative regulation of cell differentiation Source: MGI
  47. negative regulation of cell proliferation Source: MGI
  48. negative regulation of neuron differentiation Source: MGI
  49. negative regulation of smoothened signaling pathway Source: BHF-UCL
  50. negative regulation of transcription, DNA-templated Source: UniProtKB
  51. negative regulation of transcription from RNA polymerase II promoter Source: Ensembl
  52. negative thymic T cell selection Source: BHF-UCL
  53. neural tube development Source: MGI
  54. neuron fate commitment Source: MGI
  55. odontogenesis of dentin-containing tooth Source: MGI
  56. oligodendrocyte differentiation Source: MGI
  57. optic nerve morphogenesis Source: MGI
  58. palate development Source: MGI
  59. pallium development Source: MGI
  60. pattern specification process Source: MGI
  61. positive regulation of alpha-beta T cell differentiation Source: BHF-UCL
  62. positive regulation of chondrocyte differentiation Source: MGI
  63. positive regulation of neuroblast proliferation Source: MGI
  64. positive regulation of osteoblast differentiation Source: MGI
  65. positive regulation of protein import into nucleus Source: MGI
  66. positive regulation of transcription, DNA-templated Source: UniProtKB
  67. positive regulation of transcription from RNA polymerase II promoter Source: BHF-UCL
  68. protein processing Source: MGI
  69. proximal/distal pattern formation Source: MGI
  70. regulation of apoptotic process Source: MGI
  71. regulation of cell differentiation Source: MGI
  72. regulation of cell proliferation Source: MGI
  73. regulation of gene expression Source: MGI
  74. regulation of transcription, DNA-templated Source: MGI
  75. response to estrogen Source: Ensembl
  76. sagittal suture morphogenesis Source: MGI
  77. smoothened signaling pathway Source: MGI
  78. smoothened signaling pathway involved in dorsal/ventral neural tube patterning Source: MGI
  79. smoothened signaling pathway involved in spinal cord motor neuron cell fate specification Source: MGI
  80. smoothened signaling pathway involved in ventral spinal cord interneuron specification Source: MGI
  81. spinal cord dorsal/ventral patterning Source: MGI
  82. spinal cord motor neuron differentiation Source: MGI
  83. subpallium development Source: MGI
  84. T cell differentiation in thymus Source: BHF-UCL
  85. telencephalon development Source: MGI
  86. thymocyte apoptotic process Source: BHF-UCL
  87. tongue development Source: MGI
  88. transcription, DNA-templated Source: UniProtKB-KW
  89. tube development Source: MGI
  90. 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_268522. GLI3 is processed to GLI3R by the proteasome.
REACT_269412. Hedgehog 'off' state.

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: 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

  1. cilium Source: MGI
  2. cytoplasm Source: UniProtKB
  3. cytosol Source: Ensembl
  4. mediator complex Source: Ensembl
  5. nuclear speck Source: MGI
  6. nucleus Source: UniProtKB
  7. primary cilium Source: BHF-UCL
  8. 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.
GenevestigatoriQ61602.

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_006516554.1.
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.
CCDSi CCDS36603.1.
RefSeqi NP_032156.2. NM_008130.2.
XP_006516617.1. XM_006516554.1.
UniGenei Mm.5098.

3D structure databases

ProteinModelPortali Q61602.
SMRi Q61602. Positions 479-633.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 199944. 7 interactions.
STRINGi 10090.ENSMUSP00000106137.

PTM databases

PhosphoSitei Q61602.

Proteomic databases

MaxQBi Q61602.
PaxDbi Q61602.
PRIDEi Q61602.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSMUST00000110510 ; ENSMUSP00000106137 ; ENSMUSG00000021318 .
GeneIDi 14634.
KEGGi mmu:14634.
UCSCi uc007pns.1. mouse.

Organism-specific databases

CTDi 2737.
MGIi MGI:95729. Gli3.

Phylogenomic databases

eggNOGi COG5048.
GeneTreei ENSGT00760000118771.
HOGENOMi HOG000290688.
HOVERGENi HBG005844.
InParanoidi Q61602.
KOi K06230.
OMAi PRDSGSH.
PhylomeDBi Q61602.
TreeFami TF350216.

Enzyme and pathway databases

Reactomei REACT_268522. GLI3 is processed to GLI3R by the proteasome.
REACT_269412. Hedgehog 'off' state.

Miscellaneous databases

NextBioi 286490.
PROi Q61602.
SOURCEi Search...

Gene expression databases

Bgeei Q61602.
CleanExi MM_GLI3.
ExpressionAtlasi Q61602. baseline and differential.
Genevestigatori Q61602.

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. "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: November 26, 2014
This is version 128 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