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Zinc finger protein GLIS2 (GLI-similar 2) (Neuronal Krueppel-like protein) (Zinc finger protein GLI5)

 GLIS2_MOUSE             Reviewed;         521 AA.
Q8VDL9; Q8R4X9; Q99MY6; Q99P73;
15-MAY-2007, integrated into UniProtKB/Swiss-Prot.
01-MAR-2002, sequence version 1.
27-SEP-2017, entry version 130.
RecName: Full=Zinc finger protein GLIS2;
AltName: Full=GLI-similar 2;
AltName: Full=Neuronal Krueppel-like protein;
AltName: Full=Zinc finger protein GLI5;
Name=Glis2; Synonyms=Gli5, Nkl;
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE [MRNA], DEVELOPMENTAL STAGE, AND FUNCTION.
PubMed=11262234;
Lamar E., Kintner C., Goulding M.;
"Identification of NKL, a novel Gli-Kruppel zinc-finger protein that
promotes neuronal differentiation.";
Development 128:1335-1346(2001).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA], SUBCELLULAR LOCATION, TISSUE
SPECIFICITY, AND FUNCTION.
STRAIN=129/SvJ, and BALB/cJ; TISSUE=Kidney;
PubMed=11741991; DOI=10.1074/jbc.M108062200;
Zhang F., Nakanishi G., Kurebayashi S., Yoshino K., Perantoni A.,
Kim Y.-S., Jetten A.M.;
"Characterization of Glis2, a novel gene encoding a Gli-related,
Kruppel-like transcription factor with transactivation and repressor
functions. Roles in kidney development and neurogenesis.";
J. Biol. Chem. 277:10139-10149(2002).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=FVB/N; TISSUE=Mammary tumor;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[4]
FUNCTION, INTERACTION WITH CTBP1 AND HDAC3, CLEAVAGE, AND SUBCELLULAR
LOCATION.
PubMed=16326862; DOI=10.1093/nar/gki985;
Kim S.-C., Kim Y.-S., Jetten A.M.;
"Kruppel-like zinc finger protein Gli-similar 2 (Glis2) represses
transcription through interaction with C-terminal binding protein 1
(CtBP1).";
Nucleic Acids Res. 33:6805-6815(2005).
[5]
FUNCTION, INTERACTION WITH CTNNB1, MUTAGENESIS OF CYS-175, AND
SUBCELLULAR LOCATION.
PubMed=17289029; DOI=10.1016/j.febslet.2007.01.058;
Kim Y.-S., Kang H.S., Jetten A.M.;
"The Kruppel-like zinc finger protein Glis2 functions as a negative
modulator of the Wnt/beta-catenin signaling pathway.";
FEBS Lett. 581:858-864(2007).
[6]
FUNCTION, INTERACTION WITH CTNND1, CLEAVAGE SITE, DNA-BINDING,
SUBCELLULAR LOCATION, AND MUTAGENESIS OF CYS-170; TYR-288 AND ASP-290.
PubMed=17344476; DOI=10.1091/mbc.E06-10-0941;
Hosking C.R., Ulloa F., Hogan C., Ferber E.C., Figueroa A.,
Gevaert K., Birchmeier W., Briscoe J., Fujita Y.;
"The transcriptional repressor Glis2 is a novel binding partner for
p120 catenin.";
Mol. Biol. Cell 18:1918-1927(2007).
[7]
FUNCTION, AND INTERACTION WITH SUFU.
PubMed=21816948; DOI=10.1093/hmg/ddr339;
Li B., Rauhauser A.A., Dai J., Sakthivel R., Igarashi P., Jetten A.M.,
Attanasio M.;
"Increased hedgehog signaling in postnatal kidney results in aberrant
activation of nephron developmental programs.";
Hum. Mol. Genet. 20:4155-4166(2011).
-!- FUNCTION: Can act either as a transcriptional repressor or as a
transcriptional activator, depending on the cell context. Acts as
a repressor of the Hedgehog signaling pathway. Represses the
Hedgehog-dependent expression of Wnt4. Necessary to maintain the
differentiated epithelial phenotype in renal cells through the
inhibition of SNAI1, which itself induces the epithelial-to-
mesenchymal transition. Represses transcriptional activation by
CTNNB1 in the Wnt signaling pathway. May act by recruiting the
corepressors CTBP1 and HDAC3. May be involved in neuron
differentiation. {ECO:0000269|PubMed:11262234,
ECO:0000269|PubMed:11741991, ECO:0000269|PubMed:16326862,
ECO:0000269|PubMed:17289029, ECO:0000269|PubMed:17344476,
ECO:0000269|PubMed:21816948}.
-!- SUBUNIT: Interacts with CTBP1 and HDAC3. Interacts with CTNNB1 and
CTNND1. Interacts with SUFU. {ECO:0000269|PubMed:16326862,
ECO:0000269|PubMed:17289029, ECO:0000269|PubMed:17344476,
ECO:0000269|PubMed:21816948}.
-!- SUBCELLULAR LOCATION: Nucleus speckle. Cytoplasm.
-!- TISSUE SPECIFICITY: Expressed at high levels in kidney, and at
lower levels in heart and lung. {ECO:0000269|PubMed:11741991}.
-!- DEVELOPMENTAL STAGE: Expression begins at E9.5 in cranial ganglia,
dorsal root ganglia and neural tube. At E10.5, broadly expressed
in the intermediate zone of the hindbrain, spinal cord and dorsal
root ganglia. By E12.5, expression in the spinal cord becomes
restricted to a narrow band of cells in the ventricular zone.
{ECO:0000269|PubMed:11262234}.
-!- DOMAIN: The C2H2-type zinc finger 1 has a major repressor function
and is required for CTNNB1 binding.
-!- PTM: C-terminus cleavage is induced by interaction with CTNND1 and
enhances by Src tyrosine kinase. {ECO:0000269|PubMed:16326862,
ECO:0000269|PubMed:17344476}.
-!- SIMILARITY: Belongs to the GLI C2H2-type zinc-finger protein
family. {ECO:0000305}.
-----------------------------------------------------------------------
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-----------------------------------------------------------------------
EMBL; AF249340; AAK28410.1; -; mRNA.
EMBL; AF325913; AAK00953.1; -; mRNA.
EMBL; AF336135; AAL93213.1; -; Genomic_DNA.
EMBL; BC021517; AAH21517.1; -; mRNA.
CCDS; CCDS27920.1; -.
RefSeq; NP_112461.2; NM_031184.3.
RefSeq; XP_006522831.1; XM_006522768.3.
UniGene; Mm.134072; -.
ProteinModelPortal; Q8VDL9; -.
SMR; Q8VDL9; -.
BioGrid; 219913; 2.
CORUM; Q8VDL9; -.
STRING; 10090.ENSMUSP00000014447; -.
PhosphoSitePlus; Q8VDL9; -.
PaxDb; Q8VDL9; -.
PRIDE; Q8VDL9; -.
Ensembl; ENSMUST00000014447; ENSMUSP00000014447; ENSMUSG00000014303.
GeneID; 83396; -.
KEGG; mmu:83396; -.
UCSC; uc007xzw.1; mouse.
CTD; 84662; -.
MGI; MGI:1932535; Glis2.
eggNOG; KOG1721; Eukaryota.
eggNOG; COG5048; LUCA.
GeneTree; ENSGT00760000118771; -.
HOGENOM; HOG000065778; -.
HOVERGEN; HBG101807; -.
InParanoid; Q8VDL9; -.
KO; K09233; -.
OMA; DKCLSPE; -.
OrthoDB; EOG091G0IZP; -.
PhylomeDB; Q8VDL9; -.
TreeFam; TF351425; -.
PRO; PR:Q8VDL9; -.
Proteomes; UP000000589; Chromosome 16.
Bgee; ENSMUSG00000014303; -.
CleanEx; MM_GLIS2; -.
ExpressionAtlas; Q8VDL9; baseline and differential.
Genevisible; Q8VDL9; MM.
GO; GO:0005737; C:cytoplasm; IDA:MGI.
GO; GO:0097730; C:non-motile cilium; IDA:MGI.
GO; GO:0016607; C:nuclear speck; IDA:UniProtKB.
GO; GO:0005634; C:nucleus; IDA:BHF-UCL.
GO; GO:0005667; C:transcription factor complex; ISS:MGI.
GO; GO:0003677; F:DNA binding; IDA:MGI.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0000977; F:RNA polymerase II regulatory region sequence-specific DNA binding; IDA:MGI.
GO; GO:0003700; F:transcription factor activity, sequence-specific DNA binding; ISS:MGI.
GO; GO:0044212; F:transcription regulatory region DNA binding; IDA:BHF-UCL.
GO; GO:0001077; F:transcriptional activator activity, RNA polymerase II core promoter proximal region sequence-specific binding; IDA:BHF-UCL.
GO; GO:0061005; P:cell differentiation involved in kidney development; IMP:MGI.
GO; GO:0001822; P:kidney development; IMP:MGI.
GO; GO:0043433; P:negative regulation of sequence-specific DNA binding transcription factor activity; IDA:BHF-UCL.
GO; GO:0045879; P:negative regulation of smoothened signaling pathway; IMP:UniProtKB.
GO; GO:0000122; P:negative regulation of transcription from RNA polymerase II promoter; IDA:BHF-UCL.
GO; GO:0045892; P:negative regulation of transcription, DNA-templated; IDA:UniProtKB.
GO; GO:0007399; P:nervous system development; IEA:UniProtKB-KW.
GO; GO:1900182; P:positive regulation of protein localization to nucleus; IGI:MGI.
GO; GO:0045944; P:positive regulation of transcription from RNA polymerase II promoter; IDA:BHF-UCL.
GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IDA:UniProtKB.
GO; GO:0006357; P:regulation of transcription from RNA polymerase II promoter; ISS:MGI.
GO; GO:0060994; P:regulation of transcription from RNA polymerase II promoter involved in kidney development; IMP:MGI.
InterPro; IPR013087; Znf_C2H2_type.
SMART; SM00355; ZnF_C2H2; 5.
SUPFAM; SSF57667; SSF57667; 3.
PROSITE; PS00028; ZINC_FINGER_C2H2_1; 4.
PROSITE; PS50157; ZINC_FINGER_C2H2_2; 4.
1: Evidence at protein level;
Activator; Complete proteome; Cytoplasm; Developmental protein;
Differentiation; DNA-binding; Metal-binding; Neurogenesis; Nucleus;
Reference proteome; Repeat; Repressor; Transcription;
Transcription regulation; Zinc; Zinc-finger.
CHAIN 1 521 Zinc finger protein GLIS2.
/FTId=PRO_0000286984.
ZN_FING 168 193 C2H2-type 1. {ECO:0000255|PROSITE-
ProRule:PRU00042}.
ZN_FING 202 229 C2H2-type 2; atypical.
{ECO:0000255|PROSITE-ProRule:PRU00042}.
ZN_FING 235 257 C2H2-type 3. {ECO:0000255|PROSITE-
ProRule:PRU00042}.
ZN_FING 263 287 C2H2-type 4. {ECO:0000255|PROSITE-
ProRule:PRU00042}.
ZN_FING 293 317 C2H2-type 5. {ECO:0000255|PROSITE-
ProRule:PRU00042}.
REGION 35 174 Interaction with CTNND1.
{ECO:0000269|PubMed:17344476}.
REGION 71 137 Transcription activation.
REGION 148 171 Transcription repression.
COMPBIAS 333 378 Pro-rich.
COMPBIAS 387 447 Gly-rich.
SITE 287 288 Cleavage.
MUTAGEN 170 170 C->A: Impairs DNA-binding.
{ECO:0000269|PubMed:17344476}.
MUTAGEN 175 175 C->A: Abolishes interaction with CTNNB1.
No effect on nuclear localization.
{ECO:0000269|PubMed:17289029}.
MUTAGEN 288 288 Y->A: No effect on C-terminus cleavage.
{ECO:0000269|PubMed:17344476}.
MUTAGEN 290 290 D->A: Impairs C-terminus cleavage.
{ECO:0000269|PubMed:17344476}.
CONFLICT 87 88 SG -> CE (in Ref. 2; AAL93213).
{ECO:0000305}.
CONFLICT 208 208 G -> D (in Ref. 2; AAK00953).
{ECO:0000305}.
CONFLICT 210 210 Missing (in Ref. 1; AAK28410).
{ECO:0000305}.
CONFLICT 249 249 N -> K (in Ref. 2; AAL93213).
{ECO:0000305}.
CONFLICT 315 318 KAHG -> RPW (in Ref. 2; AAL93213).
{ECO:0000305}.
CONFLICT 387 387 G -> A (in Ref. 1; AAK28410).
{ECO:0000305}.
CONFLICT 458 458 D -> N (in Ref. 2; AAL93213/AAK00953).
{ECO:0000305}.
SEQUENCE 521 AA; 55842 MW; 6B5F78F4A742C72D CRC64;
MHSLDEPLDL KLSITKLRAA REKRERTLGV VRHHALHREL GLVDDSPAPG SPGSPPPGFL
LNPKFPEKVD GRFSAAPLVD LSLSPPSGLD SPNGSSSLSP ECQGNGDLPP LPTAVDFQPL
RYLDGVPSSF QFFLPLGSGG ALHLPASSFL PPPKDKCLSP ELPLAKQLVC RWAKCNQLFE
LLQDLVDHVN DHHVKPEQDA RYCCHWEGCA RHGRGFNARY KMLIHIRTHT NEKPHRCPTC
NKSFSRLENL KIHNRSHTGE KPYVCPYEGC NKRYSNSSDR FKHTRTHYVD KPYYCKMPGC
HKRYTDPSSL RKHIKAHGHF VSHEQQELLQ LRPPPKPPLP TPDSGSYVSG AQIIIPNPAA
LFGGPSLPGL PLPLPPGPLD LSALACGNGG GGGGGIGPGL PGSVLPLNLA KNPLLPSPFG
AGGLGLPVVS LLGGSAGSKA EGEKGRGSVP ARVLGLEDHK TPLERTERSR SRPSPDGLPL
LPGTVLDLST GNSAASSPEV LTPGWVVIPP GSVLLKPAVV N


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