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P08151

- GLI1_HUMAN

UniProt

P08151 - GLI1_HUMAN

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Protein
Zinc finger protein GLI1
Gene
GLI1, GLI
Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

Acts as a transcriptional activator. May regulate the transcription of specific genes during normal development. May play a role in craniofacial development and digital development, as well as development of the central nervous system and gastrointestinal tract. Mediates SHH signaling and thus cell proliferation and differentiation.2 Publications

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri235 – 26026C2H2-type 1
Add
BLAST
Zinc fingeri268 – 29528C2H2-type 2
Add
BLAST
Zinc fingeri301 – 32525C2H2-type 3
Add
BLAST
Zinc fingeri331 – 35626C2H2-type 4
Add
BLAST
Zinc fingeri362 – 38726C2H2-type 5
Add
BLAST

GO - Molecular functioni

  1. DNA binding Source: MGI
  2. RNA polymerase II distal enhancer sequence-specific DNA binding transcription factor activity Source: Ensembl
  3. chromatin binding Source: Ensembl
  4. metal ion binding Source: UniProtKB-KW
  5. protein binding Source: UniProtKB
  6. transcription regulatory region DNA binding Source: UniProtKB
Complete GO annotation...

GO - Biological processi

  1. cerebellar cortex morphogenesis Source: Ensembl
  2. digestive tract morphogenesis Source: BHF-UCL
  3. dorsal/ventral pattern formation Source: Ensembl
  4. epidermal cell differentiation Source: UniProtKB
  5. lung development Source: Ensembl
  6. negative regulation of canonical Wnt signaling pathway Source: UniProtKB
  7. notochord regression Source: Ensembl
  8. osteoblast differentiation Source: UniProtKB
  9. pituitary gland development Source: Ensembl
  10. positive regulation of DNA replication Source: UniProtKB
  11. positive regulation of cell proliferation Source: UniProtKB
  12. positive regulation of smoothened signaling pathway Source: UniProtKB
  13. positive regulation of transcription from RNA polymerase II promoter Source: UniProtKB
  14. positive regulation of transcription, DNA-templated Source: UniProtKB
  15. proximal/distal pattern formation Source: Ensembl
  16. regulation of smoothened signaling pathway Source: UniProtKB
  17. smoothened signaling pathway Source: UniProtKB
  18. smoothened signaling pathway involved in regulation of cerebellar granule cell precursor cell proliferation Source: Ensembl
  19. spermatogenesis Source: Ensembl
  20. ventral midline development Source: Ensembl
Complete GO annotation...

Keywords - Molecular functioni

Activator, Developmental protein

Keywords - Biological processi

Differentiation, Transcription, Transcription regulation

Keywords - Ligandi

DNA-binding, Metal-binding, Zinc

Enzyme and pathway databases

SignaLinkiP08151.

Names & Taxonomyi

Protein namesi
Recommended name:
Zinc finger protein GLI1
Alternative name(s):
Glioma-associated oncogene
Oncogene GLI
Gene namesi
Name:GLI1
Synonyms:GLI
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 12

Organism-specific databases

HGNCiHGNC:4317. GLI1.

Subcellular locationi

Cytoplasm. Nucleus
Note: Tethered in the cytoplasm by binding to SUFU. Activation and translocation to the nucleus is promoted by interaction with STK36. Phosphorylation by ULK3 may promote nuclear localization. Translocation to the nucleus is promoted by interaction with ZIC1.3 Publications

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB
  2. cytosol Source: UniProtKB
  3. intracellular membrane-bounded organelle Source: HPA
  4. nucleus Source: UniProtKB
  5. primary cilium Source: Ensembl
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

Pathology & Biotechi

Keywords - Diseasei

Proto-oncogene

Organism-specific databases

PharmGKBiPA28720.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 11061106Zinc finger protein GLI1
PRO_0000047197Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei518 – 5181N6-acetyllysine1 Publication

Post-translational modificationi

Phosphorylated in vitro by ULK3.1 Publication
Acetylation at Lys-518 down-regulates transcriptional activity. Deacetylated by HDAC1.1 Publication

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

PaxDbiP08151.
PRIDEiP08151.

PTM databases

PhosphoSiteiP08151.

Expressioni

Tissue specificityi

Testis, myometrium and fallopian tube. Also expressed in the brain with highest expression in the cerebellum, optic nerve and olfactory tract.1 Publication

Inductioni

Amplified in glioblastoma cells.

Gene expression databases

ArrayExpressiP08151.
BgeeiP08151.
CleanExiHS_GLI1.
GenevestigatoriP08151.

Organism-specific databases

HPAiCAB009460.
HPA034585.

Interactioni

Subunit structurei

Interacts with KIF7 By similarity. Interacts with ZIC1; the interaction enhances transcription activation.2 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
ITCHQ96J024EBI-308084,EBI-1564678
NumbQ9QZS3-24EBI-308084,EBI-3896014From a different organism.
RPS6KB1P234434EBI-308084,EBI-1775921
RPS6KB1P23443-22EBI-308084,EBI-6093204
SUFUQ9UMX18EBI-308084,EBI-740595
SUFUQ9UMX1-12EBI-308084,EBI-740615
SUFUQ9UMX1-24EBI-308084,EBI-740621
VHLP40337-12EBI-308084,EBI-3504450
VHLP40337-32EBI-308084,EBI-301270
Zic1P466842EBI-308084,EBI-308006From a different organism.

Protein-protein interaction databases

BioGridi108997. 20 interactions.
DIPiDIP-32536N.
IntActiP08151. 14 interactions.
MINTiMINT-189932.
STRINGi9606.ENSP00000228682.

Structurei

Secondary structure

Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi120 – 1234
Helixi249 – 25911
Beta strandi261 – 2633
Turni276 – 2794
Helixi285 – 2917
Helixi293 – 2964
Helixi315 – 32410
Beta strandi341 – 3466
Helixi349 – 3546
Turni367 – 3693
Beta strandi372 – 3754
Helixi376 – 3816
Turni382 – 3843

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2GLIX-ray2.60A234-388[»]
4BLBX-ray2.80E/F/G/H115-131[»]
4KMDX-ray1.70B112-128[»]
ProteinModelPortaliP08151.
SMRiP08151. Positions 143-181, 234-388.

Miscellaneous databases

EvolutionaryTraceiP08151.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni1 – 2020SNAG domain By similarity
Add
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi1038 – 105518Asp/Glu-rich (acidic)
Add
BLAST

Sequence similaritiesi

Keywords - Domaini

Repeat, Zinc-finger

Phylogenomic databases

eggNOGiCOG5048.
HOGENOMiHOG000290688.
HOVERGENiHBG080668.
InParanoidiP08151.
KOiK16797.
OMAiCPRLEHY.
OrthoDBiEOG7X6KZ8.
PhylomeDBiP08151.
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]

Sequences (3)i

Sequence statusi: Complete.

This entry describes 3 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: P08151-1) [UniParc]FASTAAdd to Basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

MFNSMTPPPI SSYGEPCCLR PLPSQGAPSV GTEGLSGPPF CHQANLMSGP     50
HSYGPARETN SCTEGPLFSS PRSAVKLTKK RALSISPLSD ASLDLQTVIR 100
TSPSSLVAFI NSRCTSPGGS YGHLSIGTMS PSLGFPAQMN HQKGPSPSFG 150
VQPCGPHDSA RGGMIPHPQS RGPFPTCQLK SELDMLVGKC REEPLEGDMS 200
SPNSTGIQDP LLGMLDGRED LEREEKREPE SVYETDCRWD GCSQEFDSQE 250
QLVHHINSEH IHGERKEFVC HWGGCSRELR PFKAQYMLVV HMRRHTGEKP 300
HKCTFEGCRK SYSRLENLKT HLRSHTGEKP YMCEHEGCSK AFSNASDRAK 350
HQNRTHSNEK PYVCKLPGCT KRYTDPSSLR KHVKTVHGPD AHVTKRHRGD 400
GPLPRAPSIS TVEPKREREG GPIREESRLT VPEGAMKPQP SPGAQSSCSS 450
DHSPAGSAAN TDSGVEMTGN AGGSTEDLSS LDEGPCIAGT GLSTLRRLEN 500
LRLDQLHQLR PIGTRGLKLP SLSHTGTTVS RRVGPPVSLE RRSSSSSSIS 550
SAYTVSRRSS LASPFPPGSP PENGASSLPG LMPAQHYLLR ARYASARGGG 600
TSPTAASSLD RIGGLPMPPW RSRAEYPGYN PNAGVTRRAS DPAQAADRPA 650
PARVQRFKSL GCVHTPPTVA GGGQNFDPYL PTSVYSPQPP SITENAAMDA 700
RGLQEEPEVG TSMVGSGLNP YMDFPPTDTL GYGGPEGAAA EPYGARGPGS 750
LPLGPGPPTN YGPNPCPQQA SYPDPTQETW GEFPSHSGLY PGPKALGGTY 800
SQCPRLEHYG QVQVKPEQGC PVGSDSTGLA PCLNAHPSEG PPHPQPLFSH 850
YPQPSPPQYL QSGPYTQPPP DYLPSEPRPC LDFDSPTHST GQLKAQLVCN 900
YVQSQQELLW EGGGREDAPA QEPSYQSPKF LGGSQVSPSR AKAPVNTYGP 950
GFGPNLPNHK SGSYPTPSPC HENFVVGANR ASHRAAAPPR LLPPLPTCYG 1000
PLKVGGTNPS CGHPEVGRLG GGPALYPPPE GQVCNPLDSL DLDNTQLDFV 1050
AILDEPQGLS PPPSHDQRGS SGHTPPPSGP PNMAVGNMSV LLRSLPGETE 1100
FLNSSA 1106
Length:1,106
Mass (Da):117,904
Last modified:August 1, 1988 - v1
Checksum:iE29B11D1A6CD3D91
GO
Isoform 2 (identifier: P08151-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     34-74: Missing.

Note: Undetectable in normal cells but highly expressed in cancer cells.

Show »
Length:1,065
Mass (Da):113,676
Checksum:iBEDBBC5D160A6A1C
GO
Isoform 3 (identifier: P08151-3) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-128: Missing.

Note: No experimental confirmation available. Gene prediction based on partial mRNA and EST data.

Show »
Length:978
Mass (Da):104,627
Checksum:i947FFF4234D96403
GO

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti210 – 2101P → A in a breast cancer sample; somatic mutation. 1 Publication
VAR_035557
Natural varianti514 – 5141T → I in a breast cancer sample; somatic mutation. 1 Publication
VAR_035558
Natural varianti817 – 8171E → Q in a breast cancer sample; somatic mutation. 1 Publication
VAR_035559
Natural varianti884 – 8841D → A.1 Publication
VAR_015114
Natural varianti933 – 9331G → D.2 Publications
Corresponds to variant rs2228224 [ dbSNP | Ensembl ].
VAR_015115
Natural varianti1012 – 10121G → V.
Corresponds to variant rs2229300 [ dbSNP | Ensembl ].
VAR_052723
Natural varianti1100 – 11001E → Q.2 Publications
Corresponds to variant rs2228226 [ dbSNP | Ensembl ].
VAR_015116

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 128128Missing in isoform 3.
VSP_054829Add
BLAST
Alternative sequencei34 – 7441Missing in isoform 2.
VSP_042215Add
BLAST

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti1106 – 11061A → AS in ACX35434. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
X07384 mRNA. Translation: CAA30297.1.
AF316573 Genomic DNA. Translation: AAM13391.1.
GQ890670 mRNA. Translation: ACX35434.1.
AC022506 Genomic DNA. No translation available.
BC013000 mRNA. Translation: AAH13000.1.
CCDSiCCDS53806.1. [P08151-2]
CCDS53807.1. [P08151-3]
CCDS8940.1. [P08151-1]
PIRiS00672. TVHUGL.
RefSeqiNP_001153517.1. NM_001160045.1. [P08151-3]
NP_001161081.1. NM_001167609.1. [P08151-2]
NP_005260.1. NM_005269.2. [P08151-1]
XP_005268856.1. XM_005268799.1. [P08151-3]
UniGeneiHs.632702.

Genome annotation databases

EnsembliENST00000228682; ENSP00000228682; ENSG00000111087. [P08151-1]
ENST00000528467; ENSP00000434408; ENSG00000111087. [P08151-2]
ENST00000543426; ENSP00000437607; ENSG00000111087.
ENST00000546141; ENSP00000441006; ENSG00000111087. [P08151-2]
GeneIDi2735.
KEGGihsa:2735.
UCSCiuc001snx.3. human. [P08151-1]
uc021qzi.1. human. [P08151-2]

Polymorphism databases

DMDMi121323.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Web resourcesi

Atlas of Genetics and Cytogenetics in Oncology and Haematology

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
X07384 mRNA. Translation: CAA30297.1 .
AF316573 Genomic DNA. Translation: AAM13391.1 .
GQ890670 mRNA. Translation: ACX35434.1 .
AC022506 Genomic DNA. No translation available.
BC013000 mRNA. Translation: AAH13000.1 .
CCDSi CCDS53806.1. [P08151-2 ]
CCDS53807.1. [P08151-3 ]
CCDS8940.1. [P08151-1 ]
PIRi S00672. TVHUGL.
RefSeqi NP_001153517.1. NM_001160045.1. [P08151-3 ]
NP_001161081.1. NM_001167609.1. [P08151-2 ]
NP_005260.1. NM_005269.2. [P08151-1 ]
XP_005268856.1. XM_005268799.1. [P08151-3 ]
UniGenei Hs.632702.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
2GLI X-ray 2.60 A 234-388 [» ]
4BLB X-ray 2.80 E/F/G/H 115-131 [» ]
4KMD X-ray 1.70 B 112-128 [» ]
ProteinModelPortali P08151.
SMRi P08151. Positions 143-181, 234-388.
ModBasei Search...

Protein-protein interaction databases

BioGridi 108997. 20 interactions.
DIPi DIP-32536N.
IntActi P08151. 14 interactions.
MINTi MINT-189932.
STRINGi 9606.ENSP00000228682.

Chemistry

BindingDBi P08151.
ChEMBLi CHEMBL5461.

PTM databases

PhosphoSitei P08151.

Polymorphism databases

DMDMi 121323.

Proteomic databases

PaxDbi P08151.
PRIDEi P08151.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000228682 ; ENSP00000228682 ; ENSG00000111087 . [P08151-1 ]
ENST00000528467 ; ENSP00000434408 ; ENSG00000111087 . [P08151-2 ]
ENST00000543426 ; ENSP00000437607 ; ENSG00000111087 .
ENST00000546141 ; ENSP00000441006 ; ENSG00000111087 . [P08151-2 ]
GeneIDi 2735.
KEGGi hsa:2735.
UCSCi uc001snx.3. human. [P08151-1 ]
uc021qzi.1. human. [P08151-2 ]

Organism-specific databases

CTDi 2735.
GeneCardsi GC12P057853.
H-InvDB HIX0010767.
HGNCi HGNC:4317. GLI1.
HPAi CAB009460.
HPA034585.
MIMi 165220. gene.
neXtProti NX_P08151.
PharmGKBi PA28720.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG5048.
HOGENOMi HOG000290688.
HOVERGENi HBG080668.
InParanoidi P08151.
KOi K16797.
OMAi CPRLEHY.
OrthoDBi EOG7X6KZ8.
PhylomeDBi P08151.
TreeFami TF350216.

Enzyme and pathway databases

SignaLinki P08151.

Miscellaneous databases

EvolutionaryTracei P08151.
GeneWikii GLI1.
GenomeRNAii 2735.
NextBioi 10780.
PROi P08151.
SOURCEi Search...

Gene expression databases

ArrayExpressi P08151.
Bgeei P08151.
CleanExi HS_GLI1.
Genevestigatori P08151.

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. "The GLI gene is a member of the Kruppel family of zinc finger proteins."
    Kinzler K.W., Ruppert J.M., Bigner S.H., Vogelstein B.
    Nature 332:371-374(1988) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
  2. "Polymorphic variants of the human oncogene GLI1 function similarly."
    Yoon J.W., Kent P., Clark A., Patterson J., Villavicencio E., Iannaccone P., Walterhouse D.
    Submitted (OCT-2000) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANTS ASP-933 AND GLN-1100.
  3. "A novel splice variant of GLI1 that promotes glioblastoma cell migration and invasion."
    Lo H.W., Zhu H., Cao X., Aldrich A., Ali-Osman F.
    Cancer Res. 69:6790-6798(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), ALTERNATIVE SPLICING.
  4. "The finished DNA sequence of human chromosome 12."
    Scherer S.E., Muzny D.M., Buhay C.J., Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V., Hume J., Jackson A., Khan Z.M., Kovar-Smith C., Lewis L.R.
    , Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R., Montgomery K.T., Morgan M.B., Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D., Lovering R.C., Wheeler D.A., Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z., Clerc-Blankenburg K.P., Davis C., Delgado O., Dinh H.H., Draper H., Gonzalez-Garay M.L., Havlak P., Jackson L.R., Jacob L.S., Kelly S.H., Li L., Li Z., Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O., Pasternak S., Perez L.M., Plopper F.J.H., Santibanez J., Shen H., Tabor P.E., Verduzco D., Waldron L., Wang Q., Williams G.A., Zhang J., Zhou J., Allen C.C., Amin A.G., Anyalebechi V., Bailey M., Barbaria J.A., Bimage K.E., Bryant N.P., Burch P.E., Burkett C.E., Burrell K.L., Calderon E., Cardenas V., Carter K., Casias K., Cavazos I., Cavazos S.R., Ceasar H., Chacko J., Chan S.N., Chavez D., Christopoulos C., Chu J., Cockrell R., Cox C.D., Dang M., Dathorne S.R., David R., Davis C.M., Davy-Carroll L., Deshazo D.R., Donlin J.E., D'Souza L., Eaves K.A., Egan A., Emery-Cohen A.J., Escotto M., Flagg N., Forbes L.D., Gabisi A.M., Garza M., Hamilton C., Henderson N., Hernandez O., Hines S., Hogues M.E., Huang M., Idlebird D.G., Johnson R., Jolivet A., Jones S., Kagan R., King L.M., Leal B., Lebow H., Lee S., LeVan J.M., Lewis L.C., London P., Lorensuhewa L.M., Loulseged H., Lovett D.A., Lucier A., Lucier R.L., Ma J., Madu R.C., Mapua P., Martindale A.D., Martinez E., Massey E., Mawhiney S., Meador M.G., Mendez S., Mercado C., Mercado I.C., Merritt C.E., Miner Z.L., Minja E., Mitchell T., Mohabbat F., Mohabbat K., Montgomery B., Moore N., Morris S., Munidasa M., Ngo R.N., Nguyen N.B., Nickerson E., Nwaokelemeh O.O., Nwokenkwo S., Obregon M., Oguh M., Oragunye N., Oviedo R.J., Parish B.J., Parker D.N., Parrish J., Parks K.L., Paul H.A., Payton B.A., Perez A., Perrin W., Pickens A., Primus E.L., Pu L.-L., Puazo M., Quiles M.M., Quiroz J.B., Rabata D., Reeves K., Ruiz S.J., Shao H., Sisson I., Sonaike T., Sorelle R.P., Sutton A.E., Svatek A.F., Svetz L.A., Tamerisa K.S., Taylor T.R., Teague B., Thomas N., Thorn R.D., Trejos Z.Y., Trevino B.K., Ukegbu O.N., Urban J.B., Vasquez L.I., Vera V.A., Villasana D.M., Wang L., Ward-Moore S., Warren J.T., Wei X., White F., Williamson A.L., Wleczyk R., Wooden H.S., Wooden S.H., Yen J., Yoon L., Yoon V., Zorrilla S.E., Nelson D., Kucherlapati R., Weinstock G., Gibbs R.A.
    Nature 440:346-351(2006) [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] (ISOFORM 1).
    Tissue: Muscle.
  6. "Gli regulation by the opposing activities of fused and suppressor of fused."
    Murone M., Luoh S.-L., Stone D., Li W., Gurney A., Armanini M., Grey C., Rosenthal A., de Sauvage F.J.
    Nat. Cell Biol. 2:310-312(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH STK36 AND SUFU.
  7. "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.
  8. "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: SUBCELLULAR LOCATION, TISSUE SPECIFICITY, PHOSPHORYLATION.
  9. Cited for: ACETYLATION AT LYS-518.
  10. "Crystal structure of a five-finger GLI-DNA complex: new perspectives on zinc fingers."
    Pavletich N.P., Pabo C.O.
    Science 261:1701-1707(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) OF 234-388.
  11. "Identification of polymorphic variants of the GLI1 oncogene."
    Wang X.Q., Chan N., Rothnagel J.A.
    J. Invest. Dermatol. 115:328-329(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANTS ALA-884; ASP-933 AND GLN-1100.
  12. Cited for: VARIANTS [LARGE SCALE ANALYSIS] ALA-210; ILE-514 AND GLN-817.

Entry informationi

Entry nameiGLI1_HUMAN
AccessioniPrimary (citable) accession number: P08151
Secondary accession number(s): D0EUY3
, E9PQQ9, F5H6H8, Q8TDN9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 1, 1988
Last sequence update: August 1, 1988
Last modified: September 3, 2014
This is version 166 of the entry and version 1 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 12
    Human chromosome 12: 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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