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Zinc finger protein ZIC 3 (Zinc finger protein 203) (Zinc finger protein of the cerebellum 3)

 ZIC3_HUMAN              Reviewed;         467 AA.
O60481; B2CNW4; Q14DE5; Q5JY75;
15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
01-AUG-1998, sequence version 1.
22-NOV-2017, entry version 169.
RecName: Full=Zinc finger protein ZIC 3;
AltName: Full=Zinc finger protein 203;
AltName: Full=Zinc finger protein of the cerebellum 3;
Name=ZIC3; Synonyms=ZNF203;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND VARIANTS HTX1 ARG-286 AND
MET-323.
PubMed=9354794; DOI=10.1038/ng1197-305;
Gebbia M., Ferrero G.B., Pilia G., Bassi M.T., Aylsworth A.S.,
Penman-Splitt M., Bird L.M., Bamforth J.S., Burn J., Schlessiner D.,
Nelson D.L., Casey B.;
"X-linked situs abnormalities result from mutations in ZIC3.";
Nat. Genet. 17:305-308(1997).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
PubMed=19266028; DOI=10.1371/journal.pgen.1000397;
Salichs E., Ledda A., Mularoni L., Alba M.M., de la Luna S.;
"Genome-wide analysis of histidine repeats reveals their role in the
localization of human proteins to the nuclear speckles compartment.";
PLoS Genet. 5:E1000397-E1000397(2009).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=15772651; DOI=10.1038/nature03440;
Ross M.T., Grafham D.V., Coffey A.J., Scherer S., McLay K., Muzny D.,
Platzer M., Howell G.R., Burrows C., Bird C.P., Frankish A.,
Lovell F.L., Howe K.L., Ashurst J.L., Fulton R.S., Sudbrak R., Wen G.,
Jones M.C., Hurles M.E., Andrews T.D., Scott C.E., Searle S.,
Ramser J., Whittaker A., Deadman R., Carter N.P., Hunt S.E., Chen R.,
Cree A., Gunaratne P., Havlak P., Hodgson A., Metzker M.L.,
Richards S., Scott G., Steffen D., Sodergren E., Wheeler D.A.,
Worley K.C., Ainscough R., Ambrose K.D., Ansari-Lari M.A., Aradhya S.,
Ashwell R.I., Babbage A.K., Bagguley C.L., Ballabio A., Banerjee R.,
Barker G.E., Barlow K.F., Barrett I.P., Bates K.N., Beare D.M.,
Beasley H., Beasley O., Beck A., Bethel G., Blechschmidt K., Brady N.,
Bray-Allen S., Bridgeman A.M., Brown A.J., Brown M.J., Bonnin D.,
Bruford E.A., Buhay C., Burch P., Burford D., Burgess J., Burrill W.,
Burton J., Bye J.M., Carder C., Carrel L., Chako J., Chapman J.C.,
Chavez D., Chen E., Chen G., Chen Y., Chen Z., Chinault C.,
Ciccodicola A., Clark S.Y., Clarke G., Clee C.M., Clegg S.,
Clerc-Blankenburg K., Clifford K., Cobley V., Cole C.G., Conquer J.S.,
Corby N., Connor R.E., David R., Davies J., Davis C., Davis J.,
Delgado O., Deshazo D., Dhami P., Ding Y., Dinh H., Dodsworth S.,
Draper H., Dugan-Rocha S., Dunham A., Dunn M., Durbin K.J., Dutta I.,
Eades T., Ellwood M., Emery-Cohen A., Errington H., Evans K.L.,
Faulkner L., Francis F., Frankland J., Fraser A.E., Galgoczy P.,
Gilbert J., Gill R., Gloeckner G., Gregory S.G., Gribble S.,
Griffiths C., Grocock R., Gu Y., Gwilliam R., Hamilton C., Hart E.A.,
Hawes A., Heath P.D., Heitmann K., Hennig S., Hernandez J.,
Hinzmann B., Ho S., Hoffs M., Howden P.J., Huckle E.J., Hume J.,
Hunt P.J., Hunt A.R., Isherwood J., Jacob L., Johnson D., Jones S.,
de Jong P.J., Joseph S.S., Keenan S., Kelly S., Kershaw J.K., Khan Z.,
Kioschis P., Klages S., Knights A.J., Kosiura A., Kovar-Smith C.,
Laird G.K., Langford C., Lawlor S., Leversha M., Lewis L., Liu W.,
Lloyd C., Lloyd D.M., Loulseged H., Loveland J.E., Lovell J.D.,
Lozado R., Lu J., Lyne R., Ma J., Maheshwari M., Matthews L.H.,
McDowall J., McLaren S., McMurray A., Meidl P., Meitinger T.,
Milne S., Miner G., Mistry S.L., Morgan M., Morris S., Mueller I.,
Mullikin J.C., Nguyen N., Nordsiek G., Nyakatura G., O'dell C.N.,
Okwuonu G., Palmer S., Pandian R., Parker D., Parrish J.,
Pasternak S., Patel D., Pearce A.V., Pearson D.M., Pelan S.E.,
Perez L., Porter K.M., Ramsey Y., Reichwald K., Rhodes S.,
Ridler K.A., Schlessinger D., Schueler M.G., Sehra H.K.,
Shaw-Smith C., Shen H., Sheridan E.M., Shownkeen R., Skuce C.D.,
Smith M.L., Sotheran E.C., Steingruber H.E., Steward C.A., Storey R.,
Swann R.M., Swarbreck D., Tabor P.E., Taudien S., Taylor T.,
Teague B., Thomas K., Thorpe A., Timms K., Tracey A., Trevanion S.,
Tromans A.C., d'Urso M., Verduzco D., Villasana D., Waldron L.,
Wall M., Wang Q., Warren J., Warry G.L., Wei X., West A.,
Whitehead S.L., Whiteley M.N., Wilkinson J.E., Willey D.L.,
Williams G., Williams L., Williamson A., Williamson H., Wilming L.,
Woodmansey R.L., Wray P.W., Yen J., Zhang J., Zhou J., Zoghbi H.,
Zorilla S., Buck D., Reinhardt R., Poustka A., Rosenthal A.,
Lehrach H., Meindl A., Minx P.J., Hillier L.W., Willard H.F.,
Wilson R.K., Waterston R.H., Rice C.M., Vaudin M., Coulson A.,
Nelson D.L., Weinstock G., Sulston J.E., Durbin R.M., Hubbard T.,
Gibbs R.A., Beck S., Rogers J., Bentley D.R.;
"The DNA sequence of the human X chromosome.";
Nature 434:325-337(2005).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Brain;
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).
[5]
FUNCTION, INTERACTION WITH GLI3, DNA-BINDING, CHARACTERIZATION OF
VARIANTS HTX1 SER-253; ARG-286; MET-323 AND GLU-405, AND
CHARACTERIZATION OF VARIANT CHTD1 ALA-217.
PubMed=17764085; DOI=10.1002/humu.20606;
Zhu L., Zhou G., Poole S., Belmont J.W.;
"Characterization of the interactions of human ZIC3 mutants with
GLI3.";
Hum. Mutat. 29:99-105(2008).
[6]
ALTERNATIVE SPLICING (ISOFORM 2).
PubMed=21858219; DOI=10.1371/journal.pone.0023755;
Bedard J.E., Haaning A.M., Ware S.M.;
"Identification of a novel ZIC3 isoform and mutation screening in
patients with heterotaxy and congenital heart disease.";
PLoS ONE 6:E23755-E23755(2011).
[7]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21406692; DOI=10.1126/scisignal.2001570;
Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J.,
Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V.,
Blagoev B.;
"System-wide temporal characterization of the proteome and
phosphoproteome of human embryonic stem cell differentiation.";
Sci. Signal. 4:RS3-RS3(2011).
[8]
SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-248, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=28112733; DOI=10.1038/nsmb.3366;
Hendriks I.A., Lyon D., Young C., Jensen L.J., Vertegaal A.C.,
Nielsen M.L.;
"Site-specific mapping of the human SUMO proteome reveals co-
modification with phosphorylation.";
Nat. Struct. Mol. Biol. 24:325-336(2017).
[9]
STRUCTURE BY NMR OF 246-329 IN COMPLEX WITH ZINC IONS, INTERACTION
WITH KPNA1 AND KPNA6, CHARACTERIZATION OF VARIANTS HTX1 SER-253;
GLY-255 AND ARG-286, AND MUTAGENESIS OF CYS-268; HIS-281; ARG-304;
LYS-307; LYS-310; LYS-312; LYS-314; ARG-320; LYS-326; LYS-337;
ARG-341; LYS-346; LYS-349; ARG-350 AND LYS-356.
PubMed=18716025; DOI=10.1093/hmg/ddn239;
Hatayama M., Tomizawa T., Sakai-Kato K., Bouvagnet P., Kose S.,
Imamoto N., Yokoyama S., Utsunomiya-Tate N., Mikoshiba K., Kigawa T.,
Aruga J.;
"Functional and structural basis of the nuclear localization signal in
the ZIC3 zinc finger domain.";
Hum. Mol. Genet. 17:3459-3473(2008).
[10]
VARIANT CHTD1 ALA-217, AND VARIANTS HTX1 SER-253 AND GLU-405.
PubMed=14681828; DOI=10.1086/380998;
Ware S.M., Peng J., Zhu L., Fernbach S., Colicos S., Casey B.,
Towbin J., Belmont J.W.;
"Identification and functional analysis of ZIC3 mutations in
heterotaxy and related congenital heart defects.";
Am. J. Hum. Genet. 74:93-105(2004).
[11]
VARIANT [LARGE SCALE ANALYSIS] ALA-217.
PubMed=16959974; DOI=10.1126/science.1133427;
Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D.,
Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S.,
Buckhaults P., Farrell C., Meeh P., Markowitz S.D., Willis J.,
Dawson D., Willson J.K.V., Gazdar A.F., Hartigan J., Wu L., Liu C.,
Parmigiani G., Park B.H., Bachman K.E., Papadopoulos N.,
Vogelstein B., Kinzler K.W., Velculescu V.E.;
"The consensus coding sequences of human breast and colorectal
cancers.";
Science 314:268-274(2006).
[12]
VARIANT HTX1 GLY-255, AND CHARACTERIZATION OF VARIANT HTX1 GLY-255.
PubMed=17295247; DOI=10.1002/humu.20480;
Chhin B., Hatayama M., Bozon D., Ogawa M., Schoen P., Tohmonda T.,
Sassolas F., Aruga J., Valard A.-G., Chen S.-C., Bouvagnet P.;
"Elucidation of penetrance variability of a ZIC3 mutation in a family
with complex heart defects and functional analysis of ZIC3 mutations
in the first zinc finger domain.";
Hum. Mutat. 28:563-570(2007).
[13]
VARIANT VACTERLX ALA-ALA-46 INS.
PubMed=20452998; DOI=10.1136/jmg.2008.060913;
Wessels M.W., Kuchinka B., Heydanus R., Smit B.J., Dooijes D.,
de Krijger R.R., Lequin M.H., de Jong E.M., Husen M., Willems P.J.,
Casey B.;
"Polyalanine expansion in the ZIC3 gene leading to X-linked heterotaxy
with VACTERL association: a new polyalanine disorder?";
J. Med. Genet. 47:351-355(2010).
[14]
VARIANTS CYS-17 AND ALA-53 INS, VARIANTS CHTD1 CYS-109; ALA-217 AND
GLY-447, VARIANT HTX1 ALA-217, VARIANT VACTERLX ASN-318,
CHARACTERIZATION OF VARIANTS CYS-17 AND ALA-53 INS, CHARACTERIZATION
OF VARIANTS CHTD1 CYS-109 AND GLY-447, CHARACTERIZATION OF VARIANT
CHTD1 ALA-217, CHARACTERIZATION OF VARIANT HTX1 ALA-217, AND
CHARACTERIZATION OF VARIANT VACTERLX ASN-318.
PubMed=24123890; DOI=10.1002/humu.22457;
Cowan J., Tariq M., Ware S.M.;
"Genetic and functional analyses of ZIC3 variants in congenital heart
disease.";
Hum. Mutat. 35:66-75(2014).
-!- FUNCTION: Acts as transcriptional activator. Required in the
earliest stages in both axial midline development and left-right
(LR) asymmetry specification. Binds to the minimal GLI-consensus
sequence 5'-GGGTGGTC-3'. {ECO:0000269|PubMed:17764085}.
-!- SUBUNIT: Interacts (via the C2H2-type domains 3, 4 and 5) with
MDFIC (via the C2H2-type domains 3, 4 and 5); the interaction
reduces its transcriptional activity (By similarity). Interacts
with KPNA1 and KPNA6. Interacts (via C2H2-type domains 3, 4 and 5)
with GLI3; the interaction enhances its transcriptional activity.
{ECO:0000250, ECO:0000269|PubMed:17764085,
ECO:0000269|PubMed:18716025}.
-!- SUBCELLULAR LOCATION: Nucleus. Cytoplasm {ECO:0000250}.
Note=Localizes in the cytoplasm in presence of MDFIC
overexpression (By similarity). Translocation to the nucleus
requires KPNA1 or KPNA6. {ECO:0000250}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1; Synonyms=ZIC3-A;
IsoId=O60481-1; Sequence=Displayed;
Name=2; Synonyms=ZIC3-B;
IsoId=O60481-2; Sequence=VSP_044010;
-!- DOMAIN: The C2H2-type 3, 4 and 5 zinc finger domains are necessary
for transcription activation. {ECO:0000250}.
-!- DISEASE: Heterotaxy, visceral, 1, X-linked (HTX1) [MIM:306955]: A
form of visceral heterotaxy, a complex disorder due to disruption
of the normal left-right asymmetry of the thoracoabdominal organs.
Visceral heterotaxy or situs ambiguus results in randomization of
the placement of visceral organs, including the heart, lungs,
liver, spleen, and stomach. The organs are oriented randomly with
respect to the left-right axis and with respect to one another. It
can been associated with variety of congenital defects including
cardiac malformations. {ECO:0000269|PubMed:14681828,
ECO:0000269|PubMed:17295247, ECO:0000269|PubMed:17764085,
ECO:0000269|PubMed:18716025, ECO:0000269|PubMed:24123890,
ECO:0000269|PubMed:9354794}. Note=The disease is caused by
mutations affecting the gene represented in this entry.
-!- DISEASE: VACTERL association X-linked with or without
hydrocephalus (VACTERLX) [MIM:314390]: A syndrome characterized by
a non-random association of congenital defects. Affected
individuals manifest vertebral anomalies (V), anal atresia (A),
cardiac malformations (C), tracheoesophageal fistula (TE), renal
anomalies (R) such as urethral atresia with hydronephrosis, and
limb anomalies (L) such as hexadactyly, humeral hypoplasia, radial
aplasia, and proximally placed thumb. Some patients may have
hydrocephalus. Some cases of VACTERL-H are associated with
increased chromosome breakage and rearrangement.
{ECO:0000269|PubMed:20452998, ECO:0000269|PubMed:24123890}.
Note=The disease is caused by mutations affecting the gene
represented in this entry.
-!- DISEASE: Congenital heart defects, multiple types, 1, X-linked
(CHTD1) [MIM:306955]: A disorder characterized by congenital
developmental abnormalities involving structures of the heart.
Common defects include transposition of the great arteries, aortic
stenosis, atrial septal defect, ventricular septal defect,
pulmonic stenosis, and patent ductus arteriosus. The etiology of
CHTD is complex, with contributions from environmental exposure,
chromosomal abnormalities, and gene defects. Some patients with
CHTD also have cardiac arrhythmias, which may be due to the
anatomic defect itself or to surgical interventions.
{ECO:0000269|PubMed:14681828, ECO:0000269|PubMed:17764085,
ECO:0000269|PubMed:24123890}. Note=The disease is caused by
mutations affecting the gene represented in this entry.
-!- SIMILARITY: Belongs to the GLI C2H2-type zinc-finger protein
family. {ECO:0000305}.
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EMBL; AF028706; AAC05594.1; -; mRNA.
EMBL; EU532020; ACB30403.1; -; mRNA.
EMBL; AL035443; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; BC113393; AAI13394.1; -; mRNA.
EMBL; BC113395; AAI13396.1; -; mRNA.
CCDS; CCDS14663.1; -. [O60481-1]
CCDS; CCDS83494.1; -. [O60481-2]
RefSeq; NP_001317590.1; NM_001330661.1. [O60481-2]
RefSeq; NP_003404.1; NM_003413.3. [O60481-1]
UniGene; Hs.111227; -.
PDB; 2EJ4; NMR; -; A=245-326.
PDB; 2RPC; NMR; -; A=245-386.
PDBsum; 2EJ4; -.
PDBsum; 2RPC; -.
ProteinModelPortal; O60481; -.
SMR; O60481; -.
BioGrid; 113379; 7.
IntAct; O60481; 3.
STRING; 9606.ENSP00000287538; -.
iPTMnet; O60481; -.
PhosphoSitePlus; O60481; -.
BioMuta; ZIC3; -.
EPD; O60481; -.
MaxQB; O60481; -.
PaxDb; O60481; -.
PeptideAtlas; O60481; -.
PRIDE; O60481; -.
DNASU; 7547; -.
Ensembl; ENST00000287538; ENSP00000287538; ENSG00000156925. [O60481-1]
Ensembl; ENST00000370606; ENSP00000359638; ENSG00000156925. [O60481-2]
GeneID; 7547; -.
KEGG; hsa:7547; -.
UCSC; uc004fak.4; human. [O60481-1]
CTD; 7547; -.
DisGeNET; 7547; -.
EuPathDB; HostDB:ENSG00000156925.11; -.
GeneCards; ZIC3; -.
HGNC; HGNC:12874; ZIC3.
HPA; HPA047934; -.
HPA; HPA052936; -.
MalaCards; ZIC3; -.
MIM; 300265; gene.
MIM; 306955; phenotype.
MIM; 314390; phenotype.
neXtProt; NX_O60481; -.
OpenTargets; ENSG00000156925; -.
Orphanet; 3426; Double outlet right ventricle.
Orphanet; 216718; Isolated congenitally uncorrected transposition of the great arteries.
Orphanet; 157769; Situs ambiguus.
PharmGKB; PA37463; -.
eggNOG; KOG1721; Eukaryota.
eggNOG; COG5048; LUCA.
GeneTree; ENSGT00900000140802; -.
HOGENOM; HOG000232057; -.
HOVERGEN; HBG007135; -.
InParanoid; O60481; -.
KO; K18487; -.
OMA; KKTCDRT; -.
OrthoDB; EOG091G0M59; -.
PhylomeDB; O60481; -.
TreeFam; TF351425; -.
Reactome; R-HSA-2892247; POU5F1 (OCT4), SOX2, NANOG activate genes related to proliferation.
Reactome; R-HSA-452723; Transcriptional regulation of pluripotent stem cells.
SignaLink; O60481; -.
SIGNOR; O60481; -.
EvolutionaryTrace; O60481; -.
GeneWiki; ZIC3; -.
GenomeRNAi; 7547; -.
PRO; PR:O60481; -.
Proteomes; UP000005640; Chromosome X.
Bgee; ENSG00000156925; -.
CleanEx; HS_ZIC3; -.
Genevisible; O60481; HS.
GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
GO; GO:0005654; C:nucleoplasm; IDA:HPA.
GO; GO:0005634; C:nucleus; ISS:UniProtKB.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0000978; F:RNA polymerase II core promoter proximal region sequence-specific DNA binding; IDA:NTNU_SB.
GO; GO:0043565; F:sequence-specific DNA binding; IDA:UniProtKB.
GO; GO:0003700; F:transcription factor activity, sequence-specific DNA binding; IDA:UniProtKB.
GO; GO:0001077; F:transcriptional activator activity, RNA polymerase II core promoter proximal region sequence-specific binding; IDA:NTNU_SB.
GO; GO:0009952; P:anterior/posterior pattern specification; IEA:Ensembl.
GO; GO:0030154; P:cell differentiation; IEA:UniProtKB-KW.
GO; GO:0071907; P:determination of digestive tract left/right asymmetry; IMP:BHF-UCL.
GO; GO:0035545; P:determination of left/right asymmetry in nervous system; IEA:Ensembl.
GO; GO:0007368; P:determination of left/right symmetry; IMP:BHF-UCL.
GO; GO:0071910; P:determination of liver left/right asymmetry; IMP:BHF-UCL.
GO; GO:0035469; P:determination of pancreatic left/right asymmetry; IMP:BHF-UCL.
GO; GO:0001947; P:heart looping; IMP:BHF-UCL.
GO; GO:0030324; P:lung development; IMP:BHF-UCL.
GO; GO:0045944; P:positive regulation of transcription from RNA polymerase II promoter; IDA:UniProtKB.
GO; GO:0045893; P:positive regulation of transcription, DNA-templated; ISS:UniProtKB.
GO; GO:0035019; P:somatic stem cell population maintenance; TAS:Reactome.
InterPro; IPR036236; Znf_C2H2_sf.
InterPro; IPR013087; Znf_C2H2_type.
SMART; SM00355; ZnF_C2H2; 5.
SUPFAM; SSF57667; SSF57667; 2.
PROSITE; PS00028; ZINC_FINGER_C2H2_1; 3.
PROSITE; PS50157; ZINC_FINGER_C2H2_2; 4.
1: Evidence at protein level;
3D-structure; Activator; Alternative splicing; Complete proteome;
Cytoplasm; Developmental protein; Differentiation; Disease mutation;
DNA-binding; Heterotaxy; Isopeptide bond; Metal-binding; Neurogenesis;
Nucleus; Polymorphism; Reference proteome; Repeat; Transcription;
Transcription regulation; Triplet repeat expansion; Ubl conjugation;
Zinc; Zinc-finger.
CHAIN 1 467 Zinc finger protein ZIC 3.
/FTId=PRO_0000047250.
ZN_FING 251 286 C2H2-type 1; atypical.
{ECO:0000255|PROSITE-ProRule:PRU00042}.
ZN_FING 295 322 C2H2-type 2; atypical.
{ECO:0000255|PROSITE-ProRule:PRU00042}.
ZN_FING 328 352 C2H2-type 3. {ECO:0000255|PROSITE-
ProRule:PRU00042}.
ZN_FING 358 382 C2H2-type 4. {ECO:0000255|PROSITE-
ProRule:PRU00042}.
ZN_FING 388 410 C2H2-type 5. {ECO:0000255|PROSITE-
ProRule:PRU00042}.
MOTIF 297 322 Nuclear localization signal.
MOTIF 330 352 Nuclear localization signal.
COMPBIAS 46 55 Poly-Ala.
COMPBIAS 87 97 Poly-His.
CROSSLNK 248 248 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:28112733}.
VAR_SEQ 409 467 VHESQGSDSSPAASSGYESSTPPAIASANSKDTTKTPSAVQ
TSTSHNPGLPPNFNEWYV -> CCPAWYPGQSLIPDEELDT
DVGMQQPALHNTTYPKCRVNAEPTVQEMIY (in
isoform 2). {ECO:0000305}.
/FTId=VSP_044010.
VARIANT 17 17 G -> C (unknown pathological
significance; no effect on its
transcriptional activator activity or
subcellular localization;
dbSNP:rs147232392).
{ECO:0000269|PubMed:24123890}.
/FTId=VAR_071330.
VARIANT 46 46 A -> AAA (in VACTERLX).
{ECO:0000269|PubMed:20452998}.
/FTId=VAR_066626.
VARIANT 53 53 A -> AA (unknown pathological
significance; no effect on its
transcriptional activator activity or
subcellular localization).
{ECO:0000269|PubMed:24123890}.
/FTId=VAR_071331.
VARIANT 109 109 S -> C (in CHTD1; does not affect its
transcriptional activator activity;
decrease in nuclear localization;
dbSNP:rs373628598).
{ECO:0000269|PubMed:24123890}.
/FTId=VAR_071332.
VARIANT 217 217 P -> A (in HTX1 and CHTD1; lacks DNA-
binding; does not inhibit transcriptional
activation and interaction with GLI3;
decrease in nuclear localization;
dbSNP:rs104894963).
{ECO:0000269|PubMed:14681828,
ECO:0000269|PubMed:16959974,
ECO:0000269|PubMed:17764085,
ECO:0000269|PubMed:24123890}.
/FTId=VAR_025632.
VARIANT 253 253 C -> S (in HTX1; increases strongly its
cytoplasmic localization; lacks DNA-
binding; does not inhibit transcriptional
activation and interaction with GLI3;
dbSNP:rs104894961).
{ECO:0000269|PubMed:14681828,
ECO:0000269|PubMed:17764085,
ECO:0000269|PubMed:18716025}.
/FTId=VAR_025633.
VARIANT 255 255 W -> G (in HTX1; decreases protein
expression and transcriptional activity
and increases its cytoplasmic
localization; dbSNP:rs122463168).
{ECO:0000269|PubMed:17295247,
ECO:0000269|PubMed:18716025}.
/FTId=VAR_042416.
VARIANT 286 286 H -> R (in HTX1; inreases weakly its
cytoplasmic localization; lacks DNA-
binding; does not inhibit transcriptional
activation and interaction with GLI3).
{ECO:0000269|PubMed:17764085,
ECO:0000269|PubMed:18716025,
ECO:0000269|PubMed:9354794}.
/FTId=VAR_025634.
VARIANT 318 318 H -> N (in VACTERLX; decrease in
transcriptional activator activity;
significant decrease in nuclear
localization).
{ECO:0000269|PubMed:24123890}.
/FTId=VAR_071333.
VARIANT 323 323 T -> M (in HTX1; lacks DNA-binding; does
not inhibit transcriptional activation
and interaction with GLI3;
dbSNP:rs122462165).
{ECO:0000269|PubMed:17764085,
ECO:0000269|PubMed:9354794}.
/FTId=VAR_007753.
VARIANT 405 405 K -> E (in HTX1; lacks DNA-binding; does
not inhibit transcriptional activation
and interaction with GLI3;
dbSNP:rs104894962).
{ECO:0000269|PubMed:14681828,
ECO:0000269|PubMed:17764085}.
/FTId=VAR_025635.
VARIANT 447 447 A -> G (in CHTD1; Increase in
transcriptional activator activity;
decrease in nuclear localization).
{ECO:0000269|PubMed:24123890}.
/FTId=VAR_071334.
MUTAGEN 268 268 C->S: Increases weakly its cytoplasmic
localization.
{ECO:0000269|PubMed:18716025}.
MUTAGEN 281 281 H->R: Increases its cytoplasmic
localization.
{ECO:0000269|PubMed:18716025}.
MUTAGEN 304 304 R->M: Increases its cytoplasmic
localization.
{ECO:0000269|PubMed:18716025}.
MUTAGEN 307 307 K->M: Increases its cytoplasmic
localization.
{ECO:0000269|PubMed:18716025}.
MUTAGEN 310 310 K->M: Increases its cytoplasmic
localization.
{ECO:0000269|PubMed:18716025}.
MUTAGEN 312 312 K->M: Increases its cytoplasmic
localization.
{ECO:0000269|PubMed:18716025}.
MUTAGEN 314 314 K->M: Does not increase its cytoplasmic
localization.
{ECO:0000269|PubMed:18716025}.
MUTAGEN 320 320 R->A: Increases its cytoplasmic
localization. Does not interact with
KPNA1 and KPNA6 and increases strongly
its cytoplasmic localization; when
associated with A-337; A-341; A-346; A-
349 and A-350.
{ECO:0000269|PubMed:18716025}.
MUTAGEN 326 326 K->M: Does not increase its cytoplasmic
localization.
{ECO:0000269|PubMed:18716025}.
MUTAGEN 337 337 K->A: Increases its cytoplasmic
localization. Does not interact with
KPNA1 and KPNA6 and increases strongly
its cytoplasmic localization; when
associated with A-320; A-341; A-346; A-
349 and A-350.
{ECO:0000269|PubMed:18716025}.
MUTAGEN 341 341 R->A: Increases its cytoplasmic
localization. Does not interact with
KPNA1 and KPNA6 and increases strongly
its cytoplasmic localization; when
associated with A-320; A-337; A-346; A-
349 and A-350.
{ECO:0000269|PubMed:18716025}.
MUTAGEN 346 346 K->A: Increases its cytoplasmic
localization. Does not interact with
KPNA1 and KPNA6 and increases strongly
its cytoplasmic localization; when
associated with A-320; A-337; A-341; A-
349 and A-350.
{ECO:0000269|PubMed:18716025}.
MUTAGEN 349 349 K->A: Increases its cytoplasmic
localization. Does not interacts with
KPNA1 and KPNA6 and increases strongly
its cytoplasmic localization; when
associated with A-320; A-337; A-341; A-
346 and A-350.
{ECO:0000269|PubMed:18716025}.
MUTAGEN 350 350 R->A: Increases its cytoplasmic
localization. Does not interact with
KPNA1 and KPNA6 and increases strongly
its cytoplasmic localization; when
associated with A-320; A-337; A-341; A-
346 and A-349.
{ECO:0000269|PubMed:18716025}.
MUTAGEN 356 356 K->A: Does not increase its cytoplasmic
localization.
{ECO:0000269|PubMed:18716025}.
STRAND 261 264 {ECO:0000244|PDB:2EJ4}.
STRAND 272 274 {ECO:0000244|PDB:2RPC}.
HELIX 275 284 {ECO:0000244|PDB:2EJ4}.
TURN 285 287 {ECO:0000244|PDB:2EJ4}.
HELIX 312 323 {ECO:0000244|PDB:2EJ4}.
STRAND 327 329 {ECO:0000244|PDB:2RPC}.
TURN 333 335 {ECO:0000244|PDB:2RPC}.
STRAND 338 340 {ECO:0000244|PDB:2RPC}.
HELIX 342 349 {ECO:0000244|PDB:2RPC}.
TURN 350 352 {ECO:0000244|PDB:2RPC}.
STRAND 369 371 {ECO:0000244|PDB:2RPC}.
HELIX 372 377 {ECO:0000244|PDB:2RPC}.
TURN 380 383 {ECO:0000244|PDB:2RPC}.
SEQUENCE 467 AA; 50569 MW; 3150CF13C0679568 CRC64;
MTMLLDGGPQ FPGLGVGSFG APRHHEMPNR EPAGMGLNPF GDSTHAAAAA AAAAAFKLSP
AAAHDLSSGQ SSAFTPQGSG YANALGHHHH HHHHHHHTSQ VPSYGGAASA AFNSTREFLF
RQRSSGLSEA ASGGGQHGLF AGSASSLHAP AGIPEPPSYL LFPGLHEQGA GHPSPTGHVD
NNQVHLGLRG ELFGRADPYR PVASPRTDPY AAGAQFPNYS PMNMNMGVNV AAHHGPGAFF
RYMRQPIKQE LSCKWIDEAQ LSRPKKSCDR TFSTMHELVT HVTMEHVGGP EQNNHVCYWE
ECPREGKSFK AKYKLVNHIR VHTGEKPFPC PFPGCGKIFA RSENLKIHKR THTGEKPFKC
EFEGCDRRFA NSSDRKKHMH VHTSDKPYIC KVCDKSYTHP SSLRKHMKVH ESQGSDSSPA
ASSGYESSTP PAIASANSKD TTKTPSAVQT STSHNPGLPP NFNEWYV


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