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O60481 (ZIC3_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 137. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | 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

Names and origin

Protein namesRecommended name:
Zinc finger protein ZIC 3
Alternative name(s):
Zinc finger protein 203
Zinc finger protein of the cerebellum 3
Gene names
Name:ZIC3
Synonyms:ZNF203
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length467 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

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'. Ref.5

Subunit structure

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. Ref.5 Ref.8

Subcellular location

Nucleus. Cytoplasm By similarity. Note: Localizes in the cytoplasm in presence of MDFIC overexpression By similarity. Translocation to the nucleus requires KPNA1 or KPNA6.

Domain

The C2H2-type 3, 4 and 5 zinc finger domains are necessary for transcription activation By similarity.

Involvement in 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.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.1 Ref.5 Ref.8 Ref.9 Ref.11

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.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.12

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.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.5 Ref.9

Sequence similarities

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

Contains 5 C2H2-type zinc fingers.

Ontologies

Keywords
   Biological processDifferentiation
Neurogenesis
Transcription
Transcription regulation
   Cellular componentCytoplasm
Nucleus
   Coding sequence diversityAlternative splicing
Polymorphism
Triplet repeat expansion
   DiseaseDisease mutation
Heterotaxy
   DomainRepeat
Zinc-finger
   LigandDNA-binding
Metal-binding
Zinc
   Molecular functionActivator
Developmental protein
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processanterior/posterior pattern specification

Inferred from electronic annotation. Source: Ensembl

cell differentiation

Inferred from electronic annotation. Source: UniProtKB-KW

determination of digestive tract left/right asymmetry

Inferred from mutant phenotype Ref.1. Source: BHF-UCL

determination of left/right asymmetry in nervous system

Inferred from electronic annotation. Source: Ensembl

determination of left/right symmetry

Inferred from mutant phenotype Ref.1. Source: BHF-UCL

determination of liver left/right asymmetry

Inferred from mutant phenotype Ref.1. Source: BHF-UCL

determination of pancreatic left/right asymmetry

Inferred from mutant phenotype Ref.1. Source: BHF-UCL

heart looping

Inferred from mutant phenotype Ref.1. Source: BHF-UCL

lung development

Inferred from mutant phenotype Ref.1. Source: BHF-UCL

positive regulation of transcription from RNA polymerase II promoter

Inferred from direct assay Ref.5. Source: UniProtKB

positive regulation of transcription, DNA-templated

Inferred from sequence or structural similarity. Source: UniProtKB

transcription, DNA-templated

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular_componentcytoplasm

Inferred from sequence or structural similarity. Source: UniProtKB

nucleus

Inferred from sequence or structural similarity. Source: UniProtKB

   Molecular_functionmetal ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

protein binding

Inferred from physical interaction Ref.5Ref.8. Source: UniProtKB

sequence-specific DNA binding

Inferred from direct assay Ref.5. Source: UniProtKB

sequence-specific DNA binding transcription factor activity

Inferred from direct assay Ref.5. Source: UniProtKB

Complete GO annotation...

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: O60481-1)

Also known as: ZIC3-A;

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 2 (identifier: O60481-2)

Also known as: ZIC3-B;

The sequence of this isoform differs from the canonical sequence as follows:
     409-467: VHESQGSDSS...LPPNFNEWYV → CCPAWYPGQS...AEPTVQEMIY

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 467467Zinc finger protein ZIC 3
PRO_0000047250

Regions

Zinc finger251 – 28636C2H2-type 1; atypical
Zinc finger295 – 32228C2H2-type 2; atypical
Zinc finger328 – 35225C2H2-type 3
Zinc finger358 – 38225C2H2-type 4
Zinc finger388 – 41023C2H2-type 5
Region297 – 32226Nuclear localization signal
Region330 – 35223Nuclear localization signal
Compositional bias46 – 5510Poly-Ala
Compositional bias87 – 9711Poly-His

Natural variations

Alternative sequence409 – 46759VHESQ…NEWYV → CCPAWYPGQSLIPDEELDTD VGMQQPALHNTTYPKCRVNA EPTVQEMIY in isoform 2.
VSP_044010
Natural variant461A → AAA in VACTERLX. Ref.12
VAR_066626
Natural variant2171P → A in CHTD1; lacks DNA-binding; does not inhibit transcriptional activation and interaction with GLI3. Ref.5 Ref.9 Ref.10
VAR_025632
Natural variant2531C → S in HTX1; increases strongly its cytoplasmic localization; lacks DNA-binding; does not inhibit transcriptional activation and interaction with GLI3. Ref.5 Ref.8 Ref.9
VAR_025633
Natural variant2551W → G in HTX1; decreases protein expression and transcriptional activity and increases its cytoplasmic localization. Ref.8 Ref.11
VAR_042416
Natural variant2861H → R in HTX1; inreases weakly its cytoplasmic localization; lacks DNA-binding; does not inhibit transcriptional activation and interaction with GLI3. Ref.1 Ref.5 Ref.8
VAR_025634
Natural variant3231T → M in HTX1; lacks DNA-binding; does not inhibit transcriptional activation and interaction with GLI3. Ref.1 Ref.5
VAR_007753
Natural variant4051K → E in HTX1; lacks DNA-binding; does not inhibit transcriptional activation and interaction with GLI3. Ref.5 Ref.9
VAR_025635

Experimental info

Mutagenesis2681C → S: Increases weakly its cytoplasmic localization. Ref.8
Mutagenesis2811H → R: Increases its cytoplasmic localization. Ref.8
Mutagenesis3041R → M: Increases its cytoplasmic localization. Ref.8
Mutagenesis3071K → M: Increases its cytoplasmic localization. Ref.8
Mutagenesis3101K → M: Increases its cytoplasmic localization. Ref.8
Mutagenesis3121K → M: Increases its cytoplasmic localization. Ref.8
Mutagenesis3141K → M: Does not increase its cytoplasmic localization. Ref.8
Mutagenesis3201R → 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. Ref.8
Mutagenesis3261K → M: Does not increase its cytoplasmic localization. Ref.8
Mutagenesis3371K → 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. Ref.8
Mutagenesis3411R → 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. Ref.8
Mutagenesis3461K → 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. Ref.8
Mutagenesis3491K → 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. Ref.8
Mutagenesis3501R → 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. Ref.8
Mutagenesis3561K → A: Does not increase its cytoplasmic localization. Ref.8

Secondary structure

....................... 467
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 (ZIC3-A) [UniParc].

Last modified August 1, 1998. Version 1.
Checksum: 3150CF13C0679568

FASTA46750,569
        10         20         30         40         50         60 
MTMLLDGGPQ FPGLGVGSFG APRHHEMPNR EPAGMGLNPF GDSTHAAAAA AAAAAFKLSP 

        70         80         90        100        110        120 
AAAHDLSSGQ SSAFTPQGSG YANALGHHHH HHHHHHHTSQ VPSYGGAASA AFNSTREFLF 

       130        140        150        160        170        180 
RQRSSGLSEA ASGGGQHGLF AGSASSLHAP AGIPEPPSYL LFPGLHEQGA GHPSPTGHVD 

       190        200        210        220        230        240 
NNQVHLGLRG ELFGRADPYR PVASPRTDPY AAGAQFPNYS PMNMNMGVNV AAHHGPGAFF 

       250        260        270        280        290        300 
RYMRQPIKQE LSCKWIDEAQ LSRPKKSCDR TFSTMHELVT HVTMEHVGGP EQNNHVCYWE 

       310        320        330        340        350        360 
ECPREGKSFK AKYKLVNHIR VHTGEKPFPC PFPGCGKIFA RSENLKIHKR THTGEKPFKC 

       370        380        390        400        410        420 
EFEGCDRRFA NSSDRKKHMH VHTSDKPYIC KVCDKSYTHP SSLRKHMKVH ESQGSDSSPA 

       430        440        450        460 
ASSGYESSTP PAIASANSKD TTKTPSAVQT STSHNPGLPP NFNEWYV 

« Hide

Isoform 2 (ZIC3-B) [UniParc].

Checksum: 28FFD09D87CC2AF5
Show »

FASTA45750,045

References

« Hide 'large scale' references
[1]"X-linked situs abnormalities result from mutations in ZIC3."
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.
Nat. Genet. 17:305-308(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), VARIANTS HTX1 ARG-286 AND MET-323.
[2]"Genome-wide analysis of histidine repeats reveals their role in the localization of human proteins to the nuclear speckles compartment."
Salichs E., Ledda A., Mularoni L., Alba M.M., de la Luna S.
PLoS Genet. 5:E1000397-E1000397(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
[3]"The DNA sequence of the human X chromosome."
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. expand/collapse author list , 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.
Nature 434:325-337(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[4]"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: Brain.
[5]"Characterization of the interactions of human ZIC3 mutants with GLI3."
Zhu L., Zhou G., Poole S., Belmont J.W.
Hum. Mutat. 29:99-105(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH GLI3, DNA-BINDING, CHARACTERIZATION OF VARIANTS HTX1 SER-253; ARG-286; MET-323 AND GLU-405, CHARACTERIZATION OF VARIANT CHTD1 ALA-217.
[6]"Identification of a novel ZIC3 isoform and mutation screening in patients with heterotaxy and congenital heart disease."
Bedard J.E., Haaning A.M., Ware S.M.
PLoS ONE 6:E23755-E23755(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: ALTERNATIVE SPLICING (ISOFORM 2).
[7]"System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[8]"Functional and structural basis of the nuclear localization signal in the ZIC3 zinc finger domain."
Hatayama M., Tomizawa T., Sakai-Kato K., Bouvagnet P., Kose S., Imamoto N., Yokoyama S., Utsunomiya-Tate N., Mikoshiba K., Kigawa T., Aruga J.
Hum. Mol. Genet. 17:3459-3473(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: 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, 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.
[9]"Identification and functional analysis of ZIC3 mutations in heterotaxy and related congenital heart defects."
Ware S.M., Peng J., Zhu L., Fernbach S., Colicos S., Casey B., Towbin J., Belmont J.W.
Am. J. Hum. Genet. 74:93-105(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT CHTD1 ALA-217, VARIANTS HTX1 SER-253 AND GLU-405.
[10]"The consensus coding sequences of human breast and colorectal cancers."
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. expand/collapse author list , 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.
Science 314:268-274(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT [LARGE SCALE ANALYSIS] ALA-217.
[11]"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."
Chhin B., Hatayama M., Bozon D., Ogawa M., Schoen P., Tohmonda T., Sassolas F., Aruga J., Valard A.-G., Chen S.-C., Bouvagnet P.
Hum. Mutat. 28:563-570(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT HTX1 GLY-255, CHARACTERIZATION OF VARIANT HTX1 GLY-255.
[12]"Polyalanine expansion in the ZIC3 gene leading to X-linked heterotaxy with VACTERL association: a new polyalanine disorder?"
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.
J. Med. Genet. 47:351-355(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT VACTERLX ALA-ALA-46 INS.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF028706 mRNA. Translation: AAC05594.1.
EU532020 mRNA. Translation: ACB30403.1.
AL035443 Genomic DNA. Translation: CAB41648.1.
AL035443 Genomic DNA. Translation: CAI42303.1.
BC113393 mRNA. Translation: AAI13394.1.
BC113395 mRNA. Translation: AAI13396.1.
CCDSCCDS14663.1. [O60481-1]
RefSeqNP_003404.1. NM_003413.3. [O60481-1]
UniGeneHs.111227.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2EJ4NMR-A245-326[»]
2RPCNMR-A245-386[»]
ProteinModelPortalO60481.
SMRO60481. Positions 245-412.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid113379. 1 interaction.
STRING9606.ENSP00000287538.

Proteomic databases

PaxDbO60481.
PRIDEO60481.

Protocols and materials databases

DNASU7547.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000287538; ENSP00000287538; ENSG00000156925. [O60481-1]
ENST00000370606; ENSP00000359638; ENSG00000156925. [O60481-2]
GeneID7547.
KEGGhsa:7547.
UCSCuc004fak.3. human. [O60481-1]

Organism-specific databases

CTD7547.
GeneCardsGC0XP136648.
HGNCHGNC:12874. ZIC3.
HPAHPA052936.
MIM300265. gene.
306955. phenotype.
314390. phenotype.
neXtProtNX_O60481.
Orphanet3426. Double outlet right ventricle.
216718. Isolated congenitally uncorrected transposition of the great arteries.
157769. Situs ambiguus.
PharmGKBPA37463.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG5048.
HOGENOMHOG000232057.
HOVERGENHBG007135.
InParanoidO60481.
KOK09224.
OMAKKTCDRT.
OrthoDBEOG76472R.
PhylomeDBO60481.
TreeFamTF351425.

Enzyme and pathway databases

ReactomeREACT_111045. Developmental Biology.
SignaLinkO60481.

Gene expression databases

BgeeO60481.
CleanExHS_ZIC3.
GenevestigatorO60481.

Family and domain databases

Gene3D3.30.160.60. 4 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. 3 hits.
PS50157. ZINC_FINGER_C2H2_2. 4 hits.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceO60481.
GeneWikiZIC3.
GenomeRNAi7547.
NextBio29529.
PROO60481.
SOURCESearch...

Entry information

Entry nameZIC3_HUMAN
AccessionPrimary (citable) accession number: O60481
Secondary accession number(s): B2CNW4, Q14DE5, Q5JY75
Entry history
Integrated into UniProtKB/Swiss-Prot: December 15, 1998
Last sequence update: August 1, 1998
Last modified: July 9, 2014
This is version 137 of the entry and version 1 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

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

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

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome X

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