O60481 (ZIC3_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended 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

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	467 AA.
Sequence status	Complete.
Protein existence	Evidence 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 process	Differentiation Neurogenesis Transcription Transcription regulation
Cellular component	Cytoplasm Nucleus
Coding sequence diversity	Alternative splicing Polymorphism Triplet repeat expansion
Disease	Disease mutation Heterotaxy
Domain	Repeat Zinc-finger
Ligand	DNA-binding Metal-binding Zinc
Molecular function	Activator Developmental protein
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	anterior/posterior pattern specification Inferred from electronic annotation. Source: Compara 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: Compara 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 transcription, DNA-dependent Inferred from electronic annotation. Source: UniProtKB-KW
Cellular_component	cytoplasm Inferred from sequence or structural similarity. Source: UniProtKB nucleus Inferred from sequence or structural similarity. Source: UniProtKB
Molecular_function	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 zinc ion binding Inferred from electronic annotation. Source: InterPro
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 key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 467

467

Zinc finger protein ZIC 3

PRO_0000047250

Regions

Zinc finger

251 – 286

36

C2H2-type 1; atypical

Zinc finger

295 – 322

28

C2H2-type 2; atypical

Zinc finger

328 – 352

25

C2H2-type 3

Zinc finger

358 – 382

25

C2H2-type 4

Zinc finger

388 – 410

23

C2H2-type 5

Region

297 – 322

26

Nuclear localization signal

Region

330 – 352

23

Nuclear localization signal

Compositional bias

46 – 55

10

Poly-Ala

Compositional bias

87 – 97

11

Poly-His

Natural variations

Alternative sequence

409 – 467

59

VHESQ…NEWYV → CCPAWYPGQSLIPDEELDTD VGMQQPALHNTTYPKCRVNA EPTVQEMIY in isoform 2.

VSP_044010

Natural variant

46

1

A → AAA in VACTERLX. Ref.12

VAR_066626

Natural variant

217

1

P → A in CHTD1; lacks DNA-binding; does not inhibit transcriptional activation and interaction with GLI3. Ref.5 Ref.9 Ref.10

VAR_025632

Natural variant

253

1

C → 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 variant

255

1

W → G in HTX1; decreases protein expression and transcriptional activity and increases its cytoplasmic localization. Ref.8 Ref.11

VAR_042416

Natural variant

286

1

H → 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 variant

323

1

T → M in HTX1; lacks DNA-binding; does not inhibit transcriptional activation and interaction with GLI3. Ref.1 Ref.5

VAR_007753

Natural variant

405

1

K → E in HTX1; lacks DNA-binding; does not inhibit transcriptional activation and interaction with GLI3. Ref.5 Ref.9

VAR_025635

Experimental info

Mutagenesis

268

1

C → S: Increases weakly its cytoplasmic localization. Ref.8

Mutagenesis

281

1

H → R: Increases its cytoplasmic localization. Ref.8

Mutagenesis

304

1

R → M: Increases its cytoplasmic localization. Ref.8

Mutagenesis

307

1

K → M: Increases its cytoplasmic localization. Ref.8

Mutagenesis

310

1

K → M: Increases its cytoplasmic localization. Ref.8

Mutagenesis

312

1

K → M: Increases its cytoplasmic localization. Ref.8

Mutagenesis

314

1

K → M: Does not increase its cytoplasmic localization. Ref.8

Mutagenesis

320

1

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. Ref.8

Mutagenesis

326

1

K → M: Does not increase its cytoplasmic localization. Ref.8

Mutagenesis

337

1

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. Ref.8

Mutagenesis

341

1

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. Ref.8

Mutagenesis

346

1

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. Ref.8

Mutagenesis

349

1

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. Ref.8

Mutagenesis

350

1

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. Ref.8

Mutagenesis

356

1

K → A: Does not increase its cytoplasmic localization. Ref.8

Secondary structure

1

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

467

Helix Strand Turn

Details...

Beta strand

261 – 264

4

Beta strand

272 – 274

3

Helix

275 – 284

10

Turn

285 – 287

3

Helix

312 – 323

12

Beta strand

327 – 329

3

Turn

333 – 335

3

Beta strand

338 – 340

3

Helix

342 – 349

8

Turn

350 – 352

3

Beta strand

369 – 371

3

Helix

372 – 377

6

Turn

380 – 383

4

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 (ZIC3-A) [UniParc]. Last modified August 1, 1998. Version 1. Checksum: 3150CF13C0679568	FASTA	467	50,569
	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
	Isoform 2 (ZIC3-B) [UniParc]. Checksum: 28FFD09D87CC2AF5	FASTA	457	50,045
	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 SSLRKHMKCC PAWYPGQSLI 430 440 450 PDEELDTDVG MQQPALHNTT YPKCRVNAEP TVQEMIY

References

	« Hide 'large scale' referencesShow '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. , 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. , 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.

Web resources

GeneReviews

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.

IPI

IPI00029724.
IPI00552994.

RefSeq

NP_003404.1. NM_003413.3.

UniGene

Hs.111227.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
2EJ4	NMR	-	A	245-326	[»]
2RPC	NMR	-	A	245-386	[»]

ProteinModelPortal

O60481.

ModBase

Search...

Protein-protein interaction databases

STRING

9606.ENSP00000287538.

Proteomic databases

PaxDb

O60481.

PRIDE

O60481.

Protocols and materials databases

DNASU

7547.

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000287538; ENSP00000287538; ENSG00000156925.
ENST00000370606; ENSP00000359638; ENSG00000156925.

GeneID

7547.

KEGG

hsa:7547.

UCSC

uc004fak.3. human.

Organism-specific databases

CTD

7547.

GeneCards

GC0XP136648.

HGNC

HGNC:12874. ZIC3.

MIM

300265. gene.
306955. phenotype.
314390. phenotype.

neXtProt

NX_O60481.

Orphanet

157769. Situs ambiguus.

PharmGKB

PA37463.

GenAtlas

Search...

Phylogenomic databases

eggNOG

COG5048.

HOGENOM

HOG000232057.

HOVERGEN

HBG007135.

InParanoid

O60481.

KO

K09224.

OMA

RGDIFGR.

OrthoDB

EOG4FFD3K.

PhylomeDB

O60481.

Gene expression databases

Bgee

O60481.

CleanEx

HS_ZIC3.

Genevestigator

O60481.

GermOnline

ENSG00000156925. Homo sapiens.

Family and domain databases

Gene3D

3.30.160.60. 4 hits.

InterPro

IPR007087. Znf_C2H2.
IPR015880. Znf_C2H2-like.
IPR013087. Znf_C2H2/integrase_DNA-bd.
[Graphical view]

Pfam

PF00096. zf-C2H2. 1 hit.
[Graphical view]

SMART

SM00355. ZnF_C2H2. 5 hits.
[Graphical view]

PROSITE

PS00028. ZINC_FINGER_C2H2_1. 3 hits.
PS50157. ZINC_FINGER_C2H2_2. 4 hits.
[Graphical view]

ProtoNet

Search...

Other

EvolutionaryTrace

O60481.

GenomeRNAi

7547.

NextBio

29529.

SOURCE

Search...

Entry information

Entry name

ZIC3_HUMAN

Accession

Primary (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:	May 1, 2013
This is version 125 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.