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P10070 (GLI2_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 139. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (5) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Zinc finger protein GLI2
Alternative name(s):
Tax helper protein
Gene names
Name:GLI2
Synonyms:THP
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length1586 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Acts as a transcriptional activator. May play a role during embryogenesis. Binds to the DNA sequence 5'-GAACCACCCA-3' which is part of the TRE-2S regulatory element that augments the Tax-dependent enhancer of human T-cell leukemia virus type 1. Is involved in the smoothened (SHH) signaling pathway. Ref.7

Subunit structure

Interaction with ZIC By similarity.

Subcellular location

Nucleus By similarity.

Post-translational modification

Phosphorylated in vitro by ULK3. Phosphorylated by DYRK2; this inhibits GLI2 transcription factor activity and promotes proteasomal degradation of GLI2. Ref.7 Ref.9

Involvement in disease

Holoprosencephaly 9 (HPE9) [MIM:610829]: A structural anomaly of the brain, in which the developing forebrain fails to correctly separate into right and left hemispheres. Holoprosencephaly is genetically heterogeneous and associated with several distinct facies and phenotypic variability. Holoprosencephaly type 9 is characterized by defective anterior pituitary formation and pan-hypopituitarism, with or without overt forebrain cleavage abnormalities, and holoprosencephaly-like midfacial hypoplasia.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.6 Ref.11

Sequence similarities

Belongs to the GLI C2H2-type zinc-finger protein family.

Contains 5 C2H2-type zinc fingers.

Sequence caution

The sequence BAA03568.1 differs from that shown. Reason: Frameshift at positions 754 and 760.

The sequence BAA03569.1 differs from that shown. Reason: Frameshift at positions 398, 410, 754 and 760.

The sequence BAA25665.1 differs from that shown. Reason: Frameshift at positions 398 and 410.

The sequence BAA25667.1 differs from that shown. Reason: Frameshift at positions 398 and 410.

Ontologies

Keywords
   Biological processTranscription
Transcription regulation
   Cellular componentNucleus
   Coding sequence diversityAlternative splicing
   DiseaseDisease mutation
Holoprosencephaly
   DomainRepeat
Zinc-finger
   LigandDNA-binding
Metal-binding
Zinc
   Molecular functionActivator
   PTMPhosphoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processapoptotic process

Inferred from electronic annotation. Source: Compara

axon guidance

Inferred from sequence or structural similarity. Source: UniProtKB

branching morphogenesis of an epithelial tube

Inferred from sequence or structural similarity. Source: UniProtKB

cell proliferation

Inferred from direct assay Ref.2. Source: UniProtKB

cellular response to organic cyclic compound

Inferred from electronic annotation. Source: Compara

cerebellar cortex morphogenesis

Inferred from sequence or structural similarity. Source: UniProtKB

cochlea morphogenesis

Inferred from electronic annotation. Source: Compara

developmental growth

Inferred from sequence or structural similarity. Source: UniProtKB

embryonic digestive tract development

Inferred from sequence or structural similarity. Source: UniProtKB

embryonic digit morphogenesis

Inferred from electronic annotation. Source: Compara

epidermal cell differentiation

Inferred from direct assay PubMed 12165851. Source: UniProtKB

floor plate formation

Inferred from sequence or structural similarity. Source: UniProtKB

head development

Inferred from electronic annotation. Source: Compara

heart development

Inferred from sequence or structural similarity. Source: UniProtKB

hindgut morphogenesis

Inferred from sequence or structural similarity. Source: UniProtKB

in utero embryonic development

Inferred from electronic annotation. Source: Compara

kidney development

Inferred from sequence or structural similarity. Source: UniProtKB

lung development

Inferred from sequence or structural similarity. Source: UniProtKB

mammary gland development

Inferred from sequence or structural similarity. Source: UniProtKB

mammary gland duct morphogenesis

Inferred from electronic annotation. Source: Compara

negative regulation of chondrocyte differentiation

Inferred from electronic annotation. Source: Compara

negative regulation of transcription from RNA polymerase II promoter

Inferred from mutant phenotype Ref.2. Source: UniProtKB

notochord regression

Inferred from electronic annotation. Source: Compara

odontogenesis of dentin-containing tooth

Inferred from sequence or structural similarity. Source: UniProtKB

osteoblast development

Inferred from sequence or structural similarity. Source: UniProtKB

osteoblast differentiation

Inferred from direct assay PubMed 12165851. Source: UniProtKB

pituitary gland development

Inferred from sequence or structural similarity. Source: UniProtKB

positive regulation of DNA replication

Inferred from direct assay PubMed 12165851. Source: UniProtKB

positive regulation of T cell differentiation in thymus

Inferred from sequence or structural similarity. Source: BHF-UCL

positive regulation of neuron differentiation

Inferred from electronic annotation. Source: Compara

positive regulation of transcription from RNA polymerase II promoter

Inferred from direct assay PubMed 12165851Ref.2PubMed 12165851PubMed 16553965PubMed 16553965. Source: UniProtKB

prostatic bud formation

Inferred from electronic annotation. Source: Compara

proximal/distal pattern formation

Inferred from sequence or structural similarity. Source: UniProtKB

regulation of smoothened signaling pathway

Inferred from electronic annotation. Source: Compara

response to mechanical stimulus

Inferred from electronic annotation. Source: Compara

skeletal system development

Inferred from sequence or structural similarity. Source: UniProtKB

smoothened signaling pathway involved in dorsal/ventral neural tube patterning

Inferred from electronic annotation. Source: Compara

smoothened signaling pathway involved in regulation of cerebellar granule cell precursor cell proliferation

Inferred from electronic annotation. Source: Compara

smoothened signaling pathway involved in spinal cord motor neuron cell fate specification

Inferred from electronic annotation. Source: Compara

smoothened signaling pathway involved in ventral spinal cord interneuron specification

Inferred from sequence or structural similarity. Source: UniProtKB

spinal cord ventral commissure morphogenesis

Inferred from sequence or structural similarity. Source: UniProtKB

transcription, DNA-dependent

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular_componentcytoplasm

Inferred from electronic annotation. Source: Compara

membrane

Inferred from electronic annotation. Source: Compara

motile primary cilium

Inferred from electronic annotation. Source: Compara

nucleus

Inferred from direct assay Ref.1. Source: UniProtKB

   Molecular_functionchromatin binding

Inferred from electronic annotation. Source: Compara

sequence-specific DNA binding

Inferred from direct assay PubMed 15175043Ref.1. Source: UniProtKB

sequence-specific DNA binding transcription factor activity

Inferred from direct assay Ref.2Ref.1. Source: UniProtKB

transcription regulatory region DNA binding

Inferred from electronic annotation. Source: Compara

zinc ion binding

Inferred from direct assay PubMed 8378770. Source: UniProtKB

Complete GO annotation...

Alternative products

This entry describes 5 isoforms produced by alternative splicing. [Align] [Select]
Isoform 5 (identifier: P10070-5)

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.
Isoform Alpha (identifier: P10070-1)

The sequence of this isoform differs from the canonical sequence as follows:
     1-328: Missing.
Isoform Beta (identifier: P10070-2)

The sequence of this isoform differs from the canonical sequence as follows:
     1-328: Missing.
     394-410: Missing.
Isoform Gamma (identifier: P10070-3)

The sequence of this isoform differs from the canonical sequence as follows:
     1-328: Missing.
     1149-1157: VSSGTVDAL → ASATWLSGT
     1158-1586: Missing.
Isoform Delta (identifier: P10070-4)

The sequence of this isoform differs from the canonical sequence as follows:
     1-328: Missing.
     394-410: Missing.
     1149-1157: VSSGTVDAL → ASATWLSGT
     1158-1586: Missing.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 15861586Zinc finger protein GLI2
PRO_0000354050

Regions

Zinc finger437 – 46428C2H2-type 1
Zinc finger475 – 49723C2H2-type 2; degenerate
Zinc finger503 – 52725C2H2-type 3
Zinc finger533 – 55826C2H2-type 4
Zinc finger564 – 58926C2H2-type 5
Compositional bias789 – 87688Ser-rich

Amino acid modifications

Modified residue1491Phosphoserine Ref.10
Modified residue2341Phosphoserine Ref.8 Ref.10
Modified residue2361Phosphoserine Ref.8 Ref.10
Modified residue2421Phosphoserine Ref.10
Modified residue3881Phosphoserine; by DYRK2 Ref.7
Modified residue7251Phosphothreonine By similarity
Modified residue10111Phosphoserine; by DYRK2 Ref.7

Natural variations

Alternative sequence1 – 328328Missing in isoform Alpha, isoform Beta, isoform Delta and isoform Gamma.
VSP_035708
Alternative sequence394 – 41017Missing in isoform Beta and isoform Delta.
VSP_006877
Alternative sequence1149 – 11579VSSGTVDAL → ASATWLSGT in isoform Gamma and isoform Delta.
VSP_006878
Alternative sequence1158 – 1586429Missing in isoform Gamma and isoform Delta.
VSP_006879
Natural variant4491D → H.
Corresponds to variant rs13427953 [ dbSNP | Ensembl ].
VAR_047303
Natural variant4791R → G in HPE9. Ref.11
VAR_032975
Natural variant5791S → I.
Corresponds to variant rs12618388 [ dbSNP | Ensembl ].
VAR_047304
Natural variant6251P → S.
Corresponds to variant rs3099537 [ dbSNP | Ensembl ].
VAR_047305
Natural variant9321P → S in HPE9. Ref.11
VAR_032976
Natural variant11561A → S. Ref.1
Corresponds to variant rs3738880 [ dbSNP | Ensembl ].
VAR_047306
Natural variant13061D → N. Ref.1
Corresponds to variant rs12711538 [ dbSNP | Ensembl ].
VAR_047307
Natural variant14441M → I in HPE9. Ref.11
VAR_032977
Natural variant15541P → L in HPE9. Ref.11
VAR_032978

Experimental info

Sequence conflict4561H → Q in M20672. Ref.5
Sequence conflict718 – 7192QL → HV in BAA03568. Ref.4
Sequence conflict718 – 7192QL → HV in BAA03569. Ref.4
Sequence conflict923 – 9253PER → AEG in BAA25665. Ref.1
Sequence conflict923 – 9253PER → AEG in BAA25667. Ref.1
Sequence conflict923 – 9253PER → AEG in BAA25666. Ref.1
Sequence conflict923 – 9253PER → AEG in BAA25668. Ref.1
Sequence conflict9661A → T in BAA25665. Ref.1
Sequence conflict9661A → T in BAA25667. Ref.1
Sequence conflict9661A → T in BAA25666. Ref.1
Sequence conflict9661A → T in BAA25668. Ref.1

Sequences

Sequence LengthMass (Da)Tools
Isoform 5 [UniParc].

Last modified November 25, 2008. Version 4.
Checksum: 86556112E13DE106

FASTA1,586167,783
        10         20         30         40         50         60 
METSASATAS EKQEAKSGIL EAAGFPDPGK KASPLVVAAA AAAAVAAQGV PQHLLPPFHA 

        70         80         90        100        110        120 
PLPIDMRHQE GRYHYEPHSV HGVHGPPALS GSPVISDISL IRLSPHPAGP GESPFNAPHP 

       130        140        150        160        170        180 
YVNPHMEHYL RSVHSSPTLS MISAARGLSP ADVAQEHLKE RGLFGLPAPG TTPSDYYHQM 

       190        200        210        220        230        240 
TLVAGHPAPY GDLLMQSGGA ASAPHLHDYL NPVDVSRFSS PRVTPRLSRK RALSISPLSD 

       250        260        270        280        290        300 
ASLDLQRMIR TSPNSLVAYI NNSRSSSAAS GSYGHLSAGA LSPAFTFPHP INPVAYQQIL 

       310        320        330        340        350        360 
SQQRGLGSAF GHTPPLIQPS PTFLAQQPMA LTSINATPTQ LSSSSNCLSD TNQNKQSSES 

       370        380        390        400        410        420 
AVSSTVNPVA IHKRSKVKTE PEGLRPASPL ALTQGQVSGH GSCGCALPLS QEQLADLKED 

       430        440        450        460        470        480 
LDRDDCKQEA EVVIYETNCH WEDCTKEYDT QEQLVHHINN EHIHGEKKEF VCRWQACTRE 

       490        500        510        520        530        540 
QKPFKAQYML VVHMRRHTGE KPHKCTFEGC SKAYSRLENL KTHLRSHTGE KPYVCEHEGC 

       550        560        570        580        590        600 
NKAFSNASDR AKHQNRTHSN EKPYICKIPG CTKRYTDPSS LRKHVKTVHG PDAHVTKKQR 

       610        620        630        640        650        660 
NDVHLRTPLL KENGDSEAGT EPGGPESTEA SSTSQAVEDC LHVRAIKTES SGLCQSSPGA 

       670        680        690        700        710        720 
QSSCSSEPSP LGSAPNNDSG VEMPGTGPGS LGDLTALDDT PPGADTSALA APSAGGLQLR 

       730        740        750        760        770        780 
KHMTTMHRFE QLKKEKLKSL KDSCSWAGPT PHTRNTKLPP LPGSGSILEN FSGSGGGGPA 

       790        800        810        820        830        840 
GLLPNPRLSE LSASEVTMLS QLQERRDSST STVSSAYTVS RRSSGISPYF SSRRSSEASP 

       850        860        870        880        890        900 
LGAGRPHNAS SADSYDPIST DASRRSSEAS QCSGGSGLLN LTPAQQYSLR AKYAAATGGP 

       910        920        930        940        950        960 
PPTPLPGLER MSLRTRLALL DAPERTLPAG CPRPLGPRRG SDGPTYGHGH AGAAPAFPHE 

       970        980        990       1000       1010       1020 
APGGGARRAS DPVRRPDALS LPRVQRFHST HNVNPGPLPP CADRRGLRLQ SHPSTDGGLA 

      1030       1040       1050       1060       1070       1080 
RGAYSPRPPS ISENVAMEAV AAGVDGAGPE ADLGLPEDDL VLPDDVVQYI KAHASGALDE 

      1090       1100       1110       1120       1130       1140 
GTGQVYPTES TGFSDNPRLP SPGLHGQRRM VAADSNVGPS APMLGGCQLG FGAPSSLNKN 

      1150       1160       1170       1180       1190       1200 
NMPVQWNEVS SGTVDALASQ VKPPPFPQGN LAVVQQKPAF GQYPGYSPQG LQASPGGLDS 

      1210       1220       1230       1240       1250       1260 
TQPHLQPRSG APSQGIPRVN YMQQLRQPVA GSQCPGMTTT MSPHACYGQV HPQLSPSTIS 

      1270       1280       1290       1300       1310       1320 
GALNQFPQSC SNMPAKPGHL GHPQQTEVAP DPTTMGNRHR ELGVPDSALA GVPPPHPVQS 

      1330       1340       1350       1360       1370       1380 
YPQQSHHLAA SMSQEGYHQV PSLLPARQPG FMEPQTGPMG VATAGFGLVQ PRPPLEPSPT 

      1390       1400       1410       1420       1430       1440 
GRHRGVRAVQ QQLAYARATG HAMAAMPSSQ ETAEAVPKGA MGNMGSVPPQ PPPQDAGGAP 

      1450       1460       1470       1480       1490       1500 
DHSMLYYYGQ IHMYEQDGGL ENLGSCQVMR SQPPQPQACQ DSIQPQPLPS PGVNQVSSTV 

      1510       1520       1530       1540       1550       1560 
DSQLLEAPQI DFDAIMDDGD HSSLFSGALS PSLLHSLSQN SSRLTTPRNS LTLPSIPAGI 

      1570       1580 
SNMAVGDMSS MLTSLAEESK FLNMMT

« Hide

Isoform Alpha [UniParc].

Checksum: 0240AD781CDAB1CB
Show »

FASTA1,258133,241
Isoform Beta [UniParc].

Checksum: CAD32033BE131937
Show »

FASTA1,241131,659
Isoform Gamma [UniParc].

Checksum: FBCD29D12CFCC01C
Show »

FASTA82988,065
Isoform Delta [UniParc].

Checksum: FE9721B04A860A5C
Show »

FASTA81286,482

References

« Hide 'large scale' references
[1]"Cloning of novel isoforms of the human Gli2 oncogene and their activities to enhance tax-dependent transcription of the human T-cell leukemia virus type 1 genome."
Tanimura A., Dan S., Yoshida M.
J. Virol. 72:3958-3964(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS ALPHA; BETA; GAMMA AND DELTA), VARIANTS SER-1156 AND ASN-1306.
[2]"A previously unidentified amino-terminal domain regulates transcriptional activity of wild-type and disease-associated human GLI2."
Roessler E., Ermilov A.N., Grange D.K., Wang A., Grachtchouk M., Dlugosz A.A., Muenke M.
Hum. Mol. Genet. 14:2181-2188(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 5).
[3]"Generation and annotation of the DNA sequences of human chromosomes 2 and 4."
Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L., Du H. expand/collapse author list , Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K., McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C., Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S., Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H., Wilson R.K.
Nature 434:724-731(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[4]"A new regulatory element that augments the Tax-dependent enhancer of human T-cell leukemia virus type 1 and cloning of cDNAs encoding its binding proteins."
Tanimura A., Teshima H., Fujisawa J., Yoshida M.
J. Virol. 67:5375-5382(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1-857 (ISOFORMS ALPHA; BETA; GAMMA AND DELTA).
[5]"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 456-560 (ISOFORMS ALPHA; BETA; GAMMA AND DELTA).
[6]"Loss-of-function mutations in the human GLI2 gene are associated with pituitary anomalies and holoprosencephaly-like features."
Roessler E., Du Y.-Z., Mullor J.L., Casas E., Allen W.P., Gillessen-Kaesbach G., Roeder E.R., Ming J.E., Ruiz i Altaba A., Muenke M.
Proc. Natl. Acad. Sci. U.S.A. 100:13424-13429(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: INVOLVEMENT IN HPE9.
[7]"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: FUNCTION, PHOSPHORYLATION AT SER-388 AND SER-1011.
[8]"A quantitative atlas of mitotic phosphorylation."
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-234 AND SER-236, MASS SPECTROMETRY.
Tissue: Cervix carcinoma.
[9]"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.
[10]"Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-149; SER-234; SER-236 AND SER-242, MASS SPECTROMETRY.
Tissue: Cervix carcinoma.
[11]"GLI2 mutations in four Brazilian patients: how wide is the phenotypic spectrum?"
Rahimov F., Ribeiro L.A., de Miranda E., Richieri-Costa A., Murray J.C.
Am. J. Med. Genet. A 140:2571-2576(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS HPE9 GLY-479; SER-932; ILE-1444 AND LEU-1554.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		AB007295 mRNA. Translation: BAA25665.1. Frameshift.
AB007296 mRNA. Translation: BAA25666.1.
AB007297 mRNA. Translation: BAA25667.1. Frameshift.
AB007298 mRNA. Translation: BAA25668.1.
DQ086814 mRNA. Translation: AAY87165.1.
AC016764 Genomic DNA. No translation available.
AC017033 Genomic DNA. No translation available.
D14827 mRNA. Translation: BAA03568.1. Frameshift.
D14828 mRNA. Translation: BAA03569.1. Frameshift.
M20672 Genomic DNA. No translation available.
M20673 Genomic DNA. Translation: AAA35898.1.
IPIIPI00018888.
IPI00221102.
IPI00332823.
IPI00784005.
IPI00914989.
PIRA31201.
A40679.
B40679.
RefSeqNP_005261.2. NM_005270.4.
UniGeneHs.111867.

3D structure databases

ProteinModelPortalP10070.
ModBaseSearch...

Protein-protein interaction databases

STRING9606.ENSP00000354586.

PTM databases

PhosphoSiteP10070.

Polymorphism databases

DMDM215274258.

Proteomic databases

PaxDbP10070.
PRIDEP10070.

Protocols and materials databases

DNASU2736.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000314490; ENSP00000312694; ENSG00000074047.
ENST00000361492; ENSP00000354586; ENSG00000074047.
ENST00000452319; ENSP00000390436; ENSG00000074047.
GeneID2736.
KEGGhsa:2736.
UCSCuc002tmq.1. human.
uc002tmr.1. human.
uc002tmt.4. human.
uc002tmu.4. human.

Organism-specific databases

CTD2736.
GeneCardsGC02P121495.
HGNCHGNC:4318. GLI2.
HPACAB008558.
MIM165230. gene.
610829. phenotype.
neXtProtNX_P10070.
Orphanet93925. Alobar holoprosencephaly.
95494. Combined pituitary hormone deficiencies, genetic forms.
93924. Lobar holoprosencephaly.
280200. Microform holoprosencephaly.
93926. Midline interhemispheric variant of holoprosencephaly.
220386. Semilobar holoprosencephaly.
280195. Septopreoptic holoprosencephaly.
PharmGKBPA28721.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG5048.
HOVERGENHBG005844.
KOK16798.
OMAIHMYEQN.
OrthoDBEOG4V16ZZ.

Enzyme and pathway databases

Pathway_Interaction_DBhedgehog_glipathway. Hedgehog signaling events mediated by Gli proteins.
hedgehog_2pathway. Signaling events mediated by the Hedgehog family.

Gene expression databases

ArrayExpressP10070.
BgeeP10070.
CleanExHS_GLI2.
GenevestigatorP10070.
GermOnlineENSG00000074047. Homo sapiens.

Family and domain databases

Gene3D3.30.160.60. 5 hits.
InterProIPR007087. Znf_C2H2.
IPR015880. Znf_C2H2-like.
IPR013087. Znf_C2H2/integrase_DNA-bd.
[Graphical view]
PfamPF00096. zf-C2H2. 1 hit.
[Graphical view]
SMARTSM00355. ZnF_C2H2. 5 hits.
[Graphical view]
PROSITEPS00028. ZINC_FINGER_C2H2_1. 4 hits.
PS50157. ZINC_FINGER_C2H2_2. 4 hits.
[Graphical view]
ProtoNetSearch...

Other

BindingDBP10070.
ChEMBLCHEMBL5119.
GenomeRNAi2736.
NextBio10784.
SOURCESearch...

Entry information

Entry nameGLI2_HUMAN
AccessionPrimary (citable) accession number: P10070
Secondary accession number(s): O60252 expand/collapse secondary AC list , O60253, O60254, O60255, Q15590, Q15591, Q4JHT4
Entry history
Integrated into UniProtKB/Swiss-Prot: July 1, 1989
Last sequence update: November 25, 2008
Last modified: May 1, 2013
This is version 139 of the entry and version 4 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

Human chromosome 2

Human chromosome 2: entries, gene names and cross-references to MIM

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

SIMILARITY comments

Index of protein domains and families

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