CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-002606
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Zinc finger protein GLI1 
Protein Synonyms/Alias
 Glioma-associated oncogene; Oncogene GLI 
Gene Name
 GLI1 
Gene Synonyms/Alias
 GLI 
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
180PFPTCQLKSELDMLVsumoylation[1]
518PIGTRGLKLPSLSHTacetylation[2]
815HYGQVQVKPEQGCPVsumoylation[1]
Reference
 [1] SUMOylation by Pias1 regulates the activity of the Hedgehog dependent Gli transcription factors.
 Cox B, Briscoe J, Ulloa F.
 PLoS One. 2010 Aug 11;5(8):e11996. [PMID: 20711444]
 [2] Histone deacetylase and Cullin3-REN(KCTD11) ubiquitin ligase interplay regulates Hedgehog signalling through Gli acetylation.
 Canettieri G, Di Marcotullio L, Greco A, Coni S, Antonucci L, Infante P, Pietrosanti L, De Smaele E, Ferretti E, Miele E, Pelloni M, De Simone G, Pedone EM, Gallinari P, Giorgi A, Steinkühler C, Vitagliano L, Pedone C, Schinin ME, Screpanti I, Gulino A.
 Nat Cell Biol. 2010 Feb;12(2):132-42. [PMID: 20081843] 
Functional Description
 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. 
Sequence Annotation
 ZN_FING 235 260 C2H2-type 1.
 ZN_FING 268 295 C2H2-type 2.
 ZN_FING 301 325 C2H2-type 3.
 ZN_FING 331 356 C2H2-type 4.
 ZN_FING 362 387 C2H2-type 5.
 REGION 1 20 SNAG domain (By similarity).
 MOD_RES 518 518 N6-acetyllysine.  
Keyword
 3D-structure; Acetylation; Activator; Alternative splicing; Complete proteome; Cytoplasm; Developmental protein; Differentiation; DNA-binding; Metal-binding; Nucleus; Phosphoprotein; Polymorphism; Proto-oncogene; Reference proteome; Repeat; Transcription; Transcription regulation; Zinc; Zinc-finger. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 1106 AA 
Protein Sequence
MFNSMTPPPI SSYGEPCCLR PLPSQGAPSV GTEGLSGPPF CHQANLMSGP HSYGPARETN 60
SCTEGPLFSS PRSAVKLTKK RALSISPLSD ASLDLQTVIR TSPSSLVAFI NSRCTSPGGS 120
YGHLSIGTMS PSLGFPAQMN HQKGPSPSFG VQPCGPHDSA RGGMIPHPQS RGPFPTCQLK 180
SELDMLVGKC REEPLEGDMS SPNSTGIQDP LLGMLDGRED LEREEKREPE SVYETDCRWD 240
GCSQEFDSQE QLVHHINSEH IHGERKEFVC HWGGCSRELR PFKAQYMLVV HMRRHTGEKP 300
HKCTFEGCRK SYSRLENLKT HLRSHTGEKP YMCEHEGCSK AFSNASDRAK HQNRTHSNEK 360
PYVCKLPGCT KRYTDPSSLR KHVKTVHGPD AHVTKRHRGD GPLPRAPSIS TVEPKREREG 420
GPIREESRLT VPEGAMKPQP SPGAQSSCSS DHSPAGSAAN TDSGVEMTGN AGGSTEDLSS 480
LDEGPCIAGT GLSTLRRLEN LRLDQLHQLR PIGTRGLKLP SLSHTGTTVS RRVGPPVSLE 540
RRSSSSSSIS SAYTVSRRSS LASPFPPGSP PENGASSLPG LMPAQHYLLR ARYASARGGG 600
TSPTAASSLD RIGGLPMPPW RSRAEYPGYN PNAGVTRRAS DPAQAADRPA PARVQRFKSL 660
GCVHTPPTVA GGGQNFDPYL PTSVYSPQPP SITENAAMDA RGLQEEPEVG TSMVGSGLNP 720
YMDFPPTDTL GYGGPEGAAA EPYGARGPGS LPLGPGPPTN YGPNPCPQQA SYPDPTQETW 780
GEFPSHSGLY PGPKALGGTY SQCPRLEHYG QVQVKPEQGC PVGSDSTGLA PCLNAHPSEG 840
PPHPQPLFSH YPQPSPPQYL QSGPYTQPPP DYLPSEPRPC LDFDSPTHST GQLKAQLVCN 900
YVQSQQELLW EGGGREDAPA QEPSYQSPKF LGGSQVSPSR AKAPVNTYGP GFGPNLPNHK 960
SGSYPTPSPC HENFVVGANR ASHRAAAPPR LLPPLPTCYG PLKVGGTNPS CGHPEVGRLG 1020
GGPALYPPPE GQVCNPLDSL DLDNTQLDFV AILDEPQGLS PPPSHDQRGS SGHTPPPSGP 1080
PNMAVGNMSV LLRSLPGETE FLNSSA 1106 
Gene Ontology
 GO:0005929; C:cilium; IEA:Compara.
 GO:0005829; C:cytosol; IDA:UniProtKB.
 GO:0005634; C:nucleus; IDA:UniProtKB.
 GO:0003682; F:chromatin binding; IEA:Compara.
 GO:0003705; F:RNA polymerase II distal enhancer sequence-specific DNA binding transcription factor activity; IEA:Compara.
 GO:0044212; F:transcription regulatory region DNA binding; IDA:UniProtKB.
 GO:0008270; F:zinc ion binding; IEA:InterPro.
 GO:0021696; P:cerebellar cortex morphogenesis; IEA:Compara.
 GO:0048546; P:digestive tract morphogenesis; TAS:BHF-UCL.
 GO:0009953; P:dorsal/ventral pattern formation; IEA:Compara.
 GO:0009913; P:epidermal cell differentiation; IDA:UniProtKB.
 GO:0030324; P:lung development; IEA:Compara.
 GO:0090090; P:negative regulation of canonical Wnt receptor signaling pathway; IMP:UniProtKB.
 GO:0060032; P:notochord regression; IEA:Compara.
 GO:0001649; P:osteoblast differentiation; IDA:UniProtKB.
 GO:0021983; P:pituitary gland development; IEA:Compara.
 GO:0008284; P:positive regulation of cell proliferation; IMP:UniProtKB.
 GO:0045740; P:positive regulation of DNA replication; IDA:UniProtKB.
 GO:0045880; P:positive regulation of smoothened signaling pathway; IDA:UniProtKB.
 GO:0045944; P:positive regulation of transcription from RNA polymerase II promoter; IDA:UniProtKB.
 GO:0009954; P:proximal/distal pattern formation; IEA:Compara.
 GO:0007224; P:smoothened signaling pathway; IDA:UniProtKB.
 GO:0021938; P:smoothened signaling pathway involved in regulation of cerebellar granule cell precursor cell proliferation; IEA:Compara.
 GO:0007283; P:spermatogenesis; IEA:Compara.
 GO:0007418; P:ventral midline development; IEA:Compara. 
Interpro
 IPR007087; Znf_C2H2.
 IPR015880; Znf_C2H2-like.
 IPR013087; Znf_C2H2/integrase_DNA-bd. 
Pfam
 PF00096; zf-C2H2 
SMART
 SM00355; ZnF_C2H2 
PROSITE
 PS00028; ZINC_FINGER_C2H2_1
 PS50157; ZINC_FINGER_C2H2_2 
PRINTS