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P26367 (PAX6_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 175. 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·Interactions·Alt products·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Paired box protein Pax-6
Alternative name(s):
Aniridia type II protein
Oculorhombin
Gene names
Name:PAX6
Synonyms:AN2
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length422 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Transcription factor with important functions in the development of the eye, nose, central nervous system and pancreas. Required for the differentiation of pancreatic islet alpha cells By similarity. Competes with PAX4 in binding to a common element in the glucagon, insulin and somatostatin promoters. Regulates specification of the ventral neuron subtypes by establishing the correct progenitor domains By similarity. Isoform 5a appears to function as a molecular switch that specifies target genes.

Subunit structure

Interacts with MAF and MAFB By similarity. Interacts with TRIM11; this interaction leads to ubiquitination and proteasomal degradation, as well as inhibition of transactivation, possibly in part by preventing PAX6 binding to consensus DNA sequences By similarity.

Subcellular location

Nucleus.

Tissue specificity

Fetal eye, brain, spinal cord and olfactory epithelium. Isoform 5a is less abundant than the PAX6 shorter form.

Developmental stage

Expressed in the developing eye and brain. Expression in the retina peaks at fetal days 51-60. At 6-week old, in the retina, is predominantly detected in the neural layer (at protein level). At 8- and 10-week old, in the retina, the expression is strongest in the inner and middle layer of the neural part (at protein level). Ref.9

Post-translational modification

Ubiquitinated by TRIM11, leading to ubiquitination and proteasomal degradation By similarity.

Involvement in disease

Aniridia (AN) [MIM:106210]: A congenital, bilateral, panocular disorder characterized by complete absence of the iris or extreme iris hypoplasia. Aniridia is not just an isolated defect in iris development but it is associated with macular and optic nerve hypoplasia, cataract, corneal changes, nystagmus. Visual acuity is generally low but is unrelated to the degree of iris hypoplasia. Glaucoma is a secondary problem causing additional visual loss over time.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.11 Ref.14 Ref.16 Ref.17 Ref.18 Ref.19 Ref.21 Ref.23 Ref.24 Ref.25 Ref.26 Ref.28 Ref.29 Ref.30 Ref.31 Ref.32 Ref.33 Ref.34 Ref.35 Ref.37

Peters anomaly (PETAN) [MIM:604229]: Consists of a central corneal leukoma, absence of the posterior corneal stroma and Descemet membrane, and a variable degree of iris and lenticular attachments to the central aspect of the posterior cornea.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.15 Ref.22 Ref.32

Foveal hypoplasia 1 (FVH1) [MIM:136520]: An isolated form of foveal hypoplasia, a developmental defect of the eye defined as the lack of foveal depression with continuity of all neurosensory retinal layers in the presumed foveal area. Clinical features include absence of foveal pit on optical coherence tomography, absence of foveal hyperpigmentation, absence of foveal avascularity, absence of foveal and macular reflexes, decreased visual acuity, and nystagmus. Anterior segment anomalies and cataract are observed in some FVH1 patients.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.16 Ref.24

Keratitis hereditary (KERH) [MIM:148190]: An ocular disorder characterized by corneal opacification, recurrent stromal keratitis and vascularization.
Note: The disease is caused by mutations affecting the gene represented in this entry.

Coloboma of iris choroid and retina (COI) [MIM:120200]: Set of malformations resulting from abnormal morphogenesis of the optic cup and stalk, and the fusion of the fetal fissure (optic fissure). The clinical presentation of ocular coloboma is variable. Some individuals may present with minimal defects in the anterior iris leaf without other ocular defects. More complex malformations create a combination of iris, uveoretinal and/or optic nerve defects without or with microphthalmia or even anophthalmia.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.32

Coloboma of optic nerve (COLON) [MIM:120430]: An ocular defect that is due to malclosure of the fetal intraocular fissure affecting the optic nerve head. In some affected individuals, it appears as enlargement of the physiologic cup with severely affected eyes showing huge cavities at the site of the disk.
Note: The disease is caused by mutations affecting the gene represented in this entry.

Bilateral optic nerve hypoplasia (BONH) [MIM:165550]: A congenital anomaly in which the optic disk appears abnormally small. It may be an isolated finding or part of a spectrum of anatomic and functional abnormalities that includes partial or complete agenesis of the septum pellucidum, other midline brain defects, cerebral anomalies, pituitary dysfunction, and structural abnormalities of the pituitary.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.32

Aniridia, cerebellar ataxia and mental deficiency (ACAMD) [MIM:206700]: A rare condition consisting of partial rudimentary iris, cerebellar impairment of the ability to perform coordinated voluntary movements, and mental retardation.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.36

Sequence similarities

Belongs to the paired homeobox family.

Contains 1 homeobox DNA-binding domain.

Contains 1 paired domain.

Ontologies

Keywords
   Biological processDifferentiation
Transcription
Transcription regulation
   Cellular componentNucleus
   Coding sequence diversityAlternative splicing
   DiseaseDisease mutation
Mental retardation
Peters anomaly
   DomainHomeobox
Paired box
   LigandDNA-binding
   Molecular functionDevelopmental protein
Repressor
   PTMUbl conjugation
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processastrocyte differentiation

Inferred from electronic annotation. Source: Ensembl

axon guidance

Inferred from electronic annotation. Source: Ensembl

blood vessel development

Inferred from mutant phenotype PubMed 7550230. Source: DFLAT

cell fate determination

Inferred from electronic annotation. Source: Ensembl

central nervous system development

Traceable author statement PubMed 10747901. Source: ProtInc

cerebral cortex regionalization

Inferred from electronic annotation. Source: Ensembl

commitment of neuronal cell to specific neuron type in forebrain

Inferred from electronic annotation. Source: Ensembl

cornea development in camera-type eye

Inferred from mutant phenotype PubMed 7550230. Source: DFLAT

dorsal/ventral axis specification

Inferred from electronic annotation. Source: Ensembl

embryonic camera-type eye morphogenesis

Inferred from electronic annotation. Source: Ensembl

eye development

Traceable author statement PubMed 10747901. Source: ProtInc

eye photoreceptor cell development

Inferred from electronic annotation. Source: Ensembl

forebrain anterior/posterior pattern specification

Inferred from electronic annotation. Source: Ensembl

forebrain dorsal/ventral pattern formation

Inferred from electronic annotation. Source: Ensembl

forebrain-midbrain boundary formation

Inferred from electronic annotation. Source: Ensembl

glucose homeostasis

Inferred from mutant phenotype PubMed 11756345. Source: DFLAT

hindbrain development

Inferred from electronic annotation. Source: Ensembl

iris morphogenesis

Inferred from mutant phenotype PubMed 7550230. Source: DFLAT

keratinocyte differentiation

Inferred from electronic annotation. Source: Ensembl

lacrimal gland development

Inferred from electronic annotation. Source: Ensembl

lens development in camera-type eye

Inferred from electronic annotation. Source: Ensembl

negative regulation of epithelial cell proliferation

Inferred from electronic annotation. Source: Ensembl

negative regulation of neurogenesis

Inferred from sequence or structural similarity. Source: UniProtKB

negative regulation of neuron differentiation

Inferred from electronic annotation. Source: Ensembl

neuron fate commitment

Non-traceable author statement PubMed 17291498. Source: UniProtKB

neuron migration

Inferred from electronic annotation. Source: Ensembl

oligodendrocyte cell fate specification

Inferred from electronic annotation. Source: Ensembl

organ morphogenesis

Traceable author statement Ref.22. Source: ProtInc

pancreatic A cell development

Inferred from mutant phenotype PubMed 20592023. Source: BHF-UCL

pituitary gland development

Inferred from electronic annotation. Source: Ensembl

positive regulation of cell fate specification

Inferred from electronic annotation. Source: Ensembl

positive regulation of epithelial cell differentiation

Inferred from electronic annotation. Source: Ensembl

positive regulation of gene expression

Inferred from mutant phenotype PubMed 20592023. Source: BHF-UCL

positive regulation of neuroblast proliferation

Inferred from electronic annotation. Source: Ensembl

positive regulation of transcription from RNA polymerase II promoter

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

positive regulation of transcription, DNA-templated

Inferred from mutant phenotype PubMed 20592023. Source: BHF-UCL

protein localization to organelle

Inferred from electronic annotation. Source: Ensembl

protein ubiquitination

Inferred from sequence or structural similarity. Source: GOC

regulation of cell migration

Inferred from electronic annotation. Source: Ensembl

regulation of timing of cell differentiation

Inferred from electronic annotation. Source: Ensembl

regulation of transcription from RNA polymerase II promoter involved in somatic motor neuron fate commitment

Inferred from electronic annotation. Source: Ensembl

regulation of transcription from RNA polymerase II promoter involved in spinal cord motor neuron fate specification

Inferred from electronic annotation. Source: Ensembl

regulation of transcription from RNA polymerase II promoter involved in ventral spinal cord interneuron specification

Inferred from electronic annotation. Source: Ensembl

response to wounding

Inferred from expression pattern PubMed 17982423. Source: UniProtKB

salivary gland morphogenesis

Inferred from electronic annotation. Source: Ensembl

signal transduction involved in regulation of gene expression

Inferred from electronic annotation. Source: Ensembl

smoothened signaling pathway

Inferred from electronic annotation. Source: Ensembl

transcription from RNA polymerase II promoter

Inferred from mutant phenotype PubMed 20592023. Source: BHF-UCL

type B pancreatic cell differentiation

Inferred from electronic annotation. Source: Ensembl

visual perception

Traceable author statement Ref.22. Source: ProtInc

   Cellular_componentcytoplasm

Inferred from direct assay PubMed 17291498. Source: UniProtKB

nuclear chromatin

Inferred from direct assay PubMed 20592023. Source: BHF-UCL

nucleus

Inferred from direct assay PubMed 17291498. Source: UniProtKB

   Molecular_functionAT DNA binding

Inferred from electronic annotation. Source: Ensembl

DNA binding

Traceable author statement Ref.22. Source: ProtInc

R-SMAD binding

Inferred from physical interaction PubMed 17251190. Source: BHF-UCL

RNA polymerase II core promoter sequence-specific DNA binding

Inferred from direct assay PubMed 20592023. Source: BHF-UCL

double-stranded DNA binding

Inferred from electronic annotation. Source: Ensembl

histone acetyltransferase binding

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

protein binding

Inferred from physical interaction PubMed 16098226. Source: IntAct

protein kinase binding

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

sequence-specific DNA binding RNA polymerase II transcription factor activity

Inferred from direct assay PubMed 20592023. Source: BHF-UCL

sequence-specific DNA binding transcription factor activity

Traceable author statement Ref.22PubMed 10747901. Source: ProtInc

transcription factor binding

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

ubiquitin-protein transferase activity

Inferred from sequence or structural similarity. Source: UniProtKB

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

Dynll1P631683EBI-747278,EBI-349121From a different organism.
HOMER3Q9NSC53EBI-747278,EBI-748420

Alternative products

This entry describes 3 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: P26367-1)

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 5a (identifier: P26367-2)

Also known as: Pax6-5a;

The sequence of this isoform differs from the canonical sequence as follows:
     47-47: Q → QTHADAKVQVLDNQN
Isoform 3 (identifier: P26367-3)

Also known as: Pax6-5A,6*;

The sequence of this isoform is not available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 422422Paired box protein Pax-6
PRO_0000050185

Regions

Domain4 – 130127Paired
DNA binding210 – 26960Homeobox Ref.7
Compositional bias131 – 20979Gln/Gly-rich
Compositional bias279 – 422144Pro/Ser/Thr-rich

Natural variations

Alternative sequence471Q → QTHADAKVQVLDNQN in isoform 5a.
VSP_002366
Natural variant171N → S in AN. Ref.21
VAR_003808
Natural variant181G → W in AN. Ref.19
VAR_003809
Natural variant191R → P in AN. Ref.33
VAR_047860
Natural variant22 – 265Missing in AN.
VAR_008693
Natural variant261R → G in PETAN. Ref.15 Ref.17
VAR_003810
Natural variant291I → S in AN. Ref.25
VAR_008694
Natural variant291I → V in AN. Ref.21
VAR_003811
Natural variant331A → P in AN. Ref.24
VAR_008695
Natural variant37 – 393Missing in AN.
VAR_008696
Natural variant421I → S in AN; mild. Ref.23
VAR_008697
Natural variant431S → P in AN. Ref.24
VAR_008698
Natural variant441R → Q in AN. Ref.21
VAR_003812
Natural variant461L → R in AN; shows almost no binding efficiency; transcriptional activation ability is about 50% lower than that of the wild-type protein. Ref.34
VAR_047861
Natural variant521C → R in AN; shows almost no binding efficiency; transcriptional activation ability is about 50% lower than that of the wild-type protein. Ref.34
VAR_047862
Natural variant531V → D in PETAN; also found in patients with congenital cataract and foveal hypoplasia. Ref.22
VAR_008700
Natural variant531V → L in AN; mild; shows 50% lower DNA-binding and transactivation ability than the wild-type protein. Ref.23 Ref.34
VAR_008699
Natural variant561I → T in AN; shows only one-quarter to one-third the binding ability of the normal wild-type protein; exhibits normal transactivation. Ref.34
VAR_047863
Natural variant631T → P in AN; mild. Ref.23
VAR_008701
Natural variant641G → V in foveal hypoplasia; associated with presenile cataract syndrome. Ref.24
VAR_008702
Natural variant681P → S in morning glory disk anomaly; significant impairment of transcriptional activation ability. Ref.32
VAR_017540
Natural variant731G → D in AN; shows almost no binding efficiency; transcriptional activation ability is about 80% of that of the wild-type protein. Ref.34
VAR_047864
Natural variant791A → E in AN; mild. Ref.23
VAR_008703
Natural variant871I → K in AN. Ref.34
VAR_047865
Natural variant871I → R in AN; loss of activity. Ref.17
VAR_003813
Natural variant1181P → R in a family with nystagmus associated with a variant form of aniridia. Ref.27
VAR_015065
Natural variant1191S → R in AN. Ref.25 Ref.29
VAR_008704
Natural variant1251R → C in FVH1; isolated. Ref.16
VAR_017541
Natural variant1261V → D in AN; atypical form. Ref.24
VAR_008705
Natural variant1281R → C in FVH1; isolated. Ref.16
VAR_003814
Natural variant1781Q → H in AN. Ref.21
VAR_003815
Natural variant2081R → Q in AN; mild. Ref.23
VAR_008706
Natural variant2081R → W in AN. Ref.14
VAR_003816
Natural variant2421R → T in AN; the mutant homeodomain binds DNA as well as the wild-type homeodomain; the mutant does not modify the DNA-binding properties of the paired domain; the steady-state levels of the full length mutant protein are higher than those of the wild-type one; a responsive promoter is activated to a higher extend by the mutant protein than by the wild-type protein; the presence of the mutation reduces sensitivity to trypsin digestion. Ref.31 Ref.35
VAR_047866
Natural variant2581F → S in COI; significant impairment of transcriptional activation ability. Ref.32
VAR_017542
Natural variant2921S → I in BONH; significant impairment of ability to activate transcription. Ref.32
VAR_017543
Natural variant3211A → T Shows about two-fold higher binding efficiency than the normal wild-type protein; transcriptional activation ability is about 89% of that of the wild-type protein. Ref.34
VAR_047867
Natural variant3531S → A in AN. Ref.25
VAR_008707
Natural variant3631S → P in PETAN. Ref.32
VAR_017544
Natural variant3751P → Q in AN; reduced DNA binding ability. Ref.30
Corresponds to variant rs200015827 [ dbSNP | Ensembl ].
VAR_015066
Natural variant3781Q → R in optic nerve aplasia. Ref.32
VAR_017545
Natural variant3811M → V in BONH. Ref.32
VAR_017546
Natural variant3871G → D. Ref.28
VAR_047868
Natural variant3911T → A in BONH. Ref.32
VAR_017547
Natural variant3951G → R in AN. Ref.37
VAR_067698
Natural variant4221Q → R in AN and ocular anterior segment anomalies; loss of DNA binding ability. Ref.20 Ref.30
VAR_008708

Experimental info

Sequence conflict3171R → L in AAA59962. Ref.1
Sequence conflict3691Y → C in CAE45868. Ref.4

Secondary structure

........................... 422
Helix Strand Turn

Details...

Sequences

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

Last modified July 15, 1999. Version 2.
Checksum: C33CDD2C1B13C397

FASTA42246,683
        10         20         30         40         50         60 
MQNSHSGVNQ LGGVFVNGRP LPDSTRQKIV ELAHSGARPC DISRILQVSN GCVSKILGRY 

        70         80         90        100        110        120 
YETGSIRPRA IGGSKPRVAT PEVVSKIAQY KRECPSIFAW EIRDRLLSEG VCTNDNIPSV 

       130        140        150        160        170        180 
SSINRVLRNL ASEKQQMGAD GMYDKLRMLN GQTGSWGTRP GWYPGTSVPG QPTQDGCQQQ 

       190        200        210        220        230        240 
EGGGENTNSI SSNGEDSDEA QMRLQLKRKL QRNRTSFTQE QIEALEKEFE RTHYPDVFAR 

       250        260        270        280        290        300 
ERLAAKIDLP EARIQVWFSN RRAKWRREEK LRNQRRQASN TPSHIPISSS FSTSVYQPIP 

       310        320        330        340        350        360 
QPTTPVSSFT SGSMLGRTDT ALTNTYSALP PMPSFTMANN LPMQPPVPSQ TSSYSCMLPT 

       370        380        390        400        410        420 
SPSVNGRSYD TYTPPHMQTH MNSQPMGTSG TTSTGLISPG VSVPVQVPGS EPDMSQYWPR 


LQ 

« Hide

Isoform 5a (Pax6-5a) [UniParc].

Checksum: 74926827347A20B5
Show »

FASTA43648,218
Isoform 3 (Pax6-5A,6*) (Sequence not available).

References

« Hide 'large scale' references
[1]"Positional cloning and characterization of a paired box- and homeobox-containing gene from the aniridia region."
Ton C.C.T., Hirvonen H., Miwa H., Weil M.M., Monaghan P., Jordan T., van Heyningen V., Hastie N.D., Meijers-Heijboer H., Drechsler M., Royer-Pokora B., Collins F.S., Swaroop A., Strong L.C., Saunders G.F.
Cell 67:1059-1074(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
Tissue: Fetal eye.
[2]"Genomic structure, evolutionary conservation and aniridia mutations in the human PAX6 gene."
Glaser T., Walton D.S., Maas R.L.
Nat. Genet. 2:232-239(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
[3]Liu J., Zhang B., Zhou Y., Peng X., Yuan J., Qiang B.
Submitted (JUL-2001) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
[4]"The full-ORF clone resource of the German cDNA consortium."
Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U., Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A., Wiemann S., Schupp I.
BMC Genomics 8:399-399(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 5A).
Tissue: Cerebellum.
[5]"Human chromosome 11 DNA sequence and analysis including novel gene identification."
Taylor T.D., Noguchi H., Totoki Y., Toyoda A., Kuroki Y., Dewar K., Lloyd C., Itoh T., Takeda T., Kim D.-W., She X., Barlow K.F., Bloom T., Bruford E., Chang J.L., Cuomo C.A., Eichler E., FitzGerald M.G. expand/collapse author list , Jaffe D.B., LaButti K., Nicol R., Park H.-S., Seaman C., Sougnez C., Yang X., Zimmer A.R., Zody M.C., Birren B.W., Nusbaum C., Fujiyama A., Hattori M., Rogers J., Lander E.S., Sakaki Y.
Nature 440:497-500(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[6]"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: Lung.
[7]"Two independent and interactive DNA-binding subdomains of the Pax6 paired domain are regulated by alternative splicing."
Epstein J.A., Glaser T., Cai J., Jepeal L., Walton D.S., Maas R.L.
Genes Dev. 8:2022-2034(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: ALTERNATIVE SPLICING, DNA-BINDING.
[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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[9]"Expression of the homeobox genes PAX6, OTX2, and OTX1 in the early human fetal retina."
Larsen K.B., Lutterodt M., Rath M.F., Moeller M.
Int. J. Dev. Neurosci. 27:485-492(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: DEVELOPMENTAL STAGE.
[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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[11]"Crystal structure of the human Pax-6 paired domain-DNA complex reveals specific roles for the linker region and carboxyl-terminal subdomain in DNA binding."
Xu H.E., Rould M.A., Xu W., Epstein J.A., Maas R.L., Pabo C.O.
Genes Dev. 13:1263-1275(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 4-136.
[12]"PAX6 mutations reviewed."
Prosser J., van Heyningen V.
Hum. Mutat. 11:93-108(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: REVIEW ON VARIANTS.
[13]"Solution structure of the homeobox domain of the human paired box protein PAX-6."
RIKEN structural genomics initiative (RSGI)
Submitted (NOV-2005) to the PDB data bank
Cited for: STRUCTURE BY NMR OF 211-277.
[14]"PAX6 mutations in aniridia."
Hanson I.M., Seawright A., Hardman K., Hodgson S., Zaletayev D., Fekete G., van Heyningen V.
Hum. Mol. Genet. 2:915-920(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT AN TRP-208.
[15]"Mutations at the PAX6 locus are found in heterogeneous anterior segment malformations including Peters' anomaly."
Hanson I.M., Fletcher J.M., Jordan T., Brown A., Taylor D., Adams R.J., Punnet H.H., van Heyningen V.
Nat. Genet. 6:168-173(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT PETAN GLY-26.
[16]"PAX6 missense mutation in isolated foveal hypoplasia."
Azuma N., Nishina S., Yanagisawa H., Okuyama T., Yamada M.
Nat. Genet. 13:141-142(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS FVH1 CYS-125 AND CYS-128.
[17]"Functional analysis of paired box missense mutations in the PAX6 gene."
Tang H.K., Chao L.-Y., Saunders G.F.
Hum. Mol. Genet. 6:381-386(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT AN ARG-87, VARIANT GLY-26.
[18]"Combined SSCP/heteroduplex analysis in the screening for PAX6 mutations."
Axton R., Hanson I.M., Love J., Seawright A., Prosser J., van Heyningen V.
Mol. Cell. Probes 11:287-292(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT AN 22-PRO--ARG-26 DEL.
[19]"Ten novel mutations found in Aniridia."
Wolf M.T.F., Lorenz B., Winterpacht A., Drechsler M., Schumacher V., Royer-Pokora B., Blankenagel A., Zabel B., Wildhardt G.
Hum. Mutat. 12:304-313(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT AN TRP-18.
[20]"Missense mutation at the C-terminus of the PAX6 gene in ocular anterior segment anomalies."
Azuma N., Yamada M.
Invest. Ophthalmol. Vis. Sci. 39:828-830(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT EYE MALFORMATIONS ARG-422.
[21]"Missense mutations in the PAX6 gene in aniridia."
Azuma N., Hotta Y., Tanaka H., Yamada M.
Invest. Ophthalmol. Vis. Sci. 39:2524-2528(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS AN SER-17; VAL-29; GLN-44 AND HIS-178.
[22]"Missense mutation in the alternative splice region of the PAX6 gene in eye anomalies."
Azuma N., Yamaguchi Y., Handa H., Hayakawa M., Kanai A., Yamada M.
Am. J. Hum. Genet. 65:656-663(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT PETAN ASP-53.
[23]"Mutational analysis of PAX6: 16 novel mutations including 5 missense mutations with a mild aniridia phenotype."
Groenskov K., Rosenberg T., Sand A., Broendum-Nielsen K.
Eur. J. Hum. Genet. 7:274-286(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: ALTERNATIVE SPLICING, VARIANTS AN SER-42; LEU-53; PRO-63; GLU-79 AND GLN-208.
[24]"Missense mutations in the most ancient residues of the PAX6 paired domain underlie a spectrum of human congenital eye malformations."
Hanson I.M., Churchill A., Love J., Axton R., Moore T., Clarke M., Meire F., van Heyningen V.
Hum. Mol. Genet. 8:165-172(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS AN PRO-33; PRO-43 AND ASP-126, VARIANT FVH1 VAL-64.
[25]Wildhardt G.
Unpublished observations (APR-1999)
Cited for: VARIANTS AN SER-29; ARG-119 AND ALA-353.
[26]Saunders G.F.
Unpublished observations (AUG-1999)
Cited for: VARIANT AN 37-ALA--PRO-39 DEL.
[27]"A novel PAX6 gene mutation (P118R) in a family with congenital nystagmus associated with a variant form of aniridia."
Sonoda S., Isashiki Y., Tabata Y., Kimura K., Kakiuchi T., Ohba N.
Graefes Arch. Clin. Exp. Ophthalmol. 238:552-558(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT NYSTAGMUS ARG-118.
[28]"Mutation in the PAX6 gene in twenty patients with aniridia."
Chao L.-Y., Huff V., Strong L.C., Saunders G.F.
Hum. Mutat. 15:332-339(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT AN 37-ARG--PRO-39 DEL, VARIANT ASP-387.
[29]"PAX6 mutation in a family with aniridia, congenital ptosis, and mental retardation."
Malandrini A., Mari F., Palmeri S., Gambelli S., Berti G., Bruttini M., Bardelli A.M., Williamson K., van Heyningen V., Renieri A.
Clin. Genet. 60:151-154(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT AN ARG-119.
[30]"Missense mutation at the C-terminus of PAX6 negatively modulates homeodomain function."
Singh S., Chao L.-Y., Mishra R., Davies J., Saunders G.F.
Hum. Mol. Genet. 10:911-918(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS AN GLN-375 AND ARG-422.
[31]"National study of microphthalmia, anophthalmia, and coloboma (MAC) in Scotland: investigation of genetic aetiology."
Morrison D., FitzPatrick D., Hanson I., Williamson K., van Heyningen V., Fleck B., Jones I., Chalmers J., Campbell H.
J. Med. Genet. 39:16-22(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT AN THR-242.
[32]"Mutations of the PAX6 gene detected in patients with a variety of optic-nerve malformations."
Azuma N., Yamaguchi Y., Handa H., Tadokoro K., Asaka A., Kawase E., Yamada M.
Am. J. Hum. Genet. 72:1565-1570(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT MORNING GLORY DISK ANOMALY SER-68, VARIANT COI SER-258, VARIANT PETAN PRO-363, VARIANTS BONH ILE-292; ARG-378; VAL-381 AND ALA-391.
[33]"Screening for PAX6 gene mutations is consistent with haploinsufficiency as the main mechanism leading to various ocular defects."
Vincent M.-C., Pujo A.-L., Olivier D., Calvas P.
Eur. J. Hum. Genet. 11:163-169(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS AN PRO-19 AND 22-PRO--ARG-26 DEL.
[34]"Missense mutations in the DNA-binding region and termination codon in PAX6."
Chao L.-Y., Mishra R., Strong L.C., Saunders G.F.
Hum. Mutat. 21:138-145(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS AN ARG-46; ARG-52; THR-56; ASP-73 AND LYS-87, VARIANT THR-321, CHARACTERIZATION OF VARIANTS AN ARG-46; ARG-52; LEU-53; THR-56 AND ASP-73, CHARACTERIZATION OF VARIANT THR-321.
[35]"Molecular analysis of a human PAX6 homeobox mutant."
D'Elia A.V., Puppin C., Pellizzari L., Pianta A., Bregant E., Lonigro R., Tell G., Fogolari F., van Heyningen V., Damante G.
Eur. J. Hum. Genet. 14:744-751(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: CHARACTERIZATION OF VARIANT AN THR-242.
[36]"A de novo nonsense mutation of PAX6 gene in a patient with aniridia, ataxia, and mental retardation."
Graziano C., D'Elia A.V., Mazzanti L., Moscano F., Guidelli Guidi S., Scarano E., Turchetti D., Franzoni E., Romeo G., Damante G., Seri M.
Am. J. Med. Genet. A 143:1802-1805(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: INVOLVEMENT IN ACAMD.
[37]"Mutation spectrum of PAX6 in Chinese patients with aniridia."
Zhang X., Wang P., Li S., Xiao X., Guo X., Zhang Q.
Mol. Vis. 17:2139-2147(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT AN ARG-395.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M77844 mRNA. Translation: AAA59962.1.
M93650 mRNA. Translation: AAA36416.1.
AY047583 mRNA. Translation: AAK95849.1.
BX640762 mRNA. Translation: CAE45868.1.
Z95332, Z83307 Genomic DNA. Translation: CAG38363.1.
Z83307, Z95332 Genomic DNA. Translation: CAG38087.1.
BC011953 mRNA. Translation: AAH11953.1.
CCDSCCDS31451.1. [P26367-1]
CCDS31452.1. [P26367-2]
PIRA56674.
RefSeqNP_000271.1. NM_000280.4. [P26367-1]
NP_001121084.1. NM_001127612.1. [P26367-1]
NP_001245393.1. NM_001258464.1. [P26367-1]
NP_001245394.1. NM_001258465.1. [P26367-1]
NP_001595.2. NM_001604.5. [P26367-2]
XP_005253012.1. XM_005252955.2. [P26367-1]
XP_005253013.1. XM_005252956.2. [P26367-1]
UniGeneHs.270303.
Hs.611376.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2CUENMR-A211-277[»]
6PAXX-ray2.50A4-136[»]
ProteinModelPortalP26367.
SMRP26367. Positions 4-136, 211-278.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid111114. 31 interactions.
DIPDIP-37436N.
IntActP26367. 6 interactions.
MINTMINT-1465118.
STRING9606.ENSP00000368401.

PTM databases

PhosphoSiteP26367.

Polymorphism databases

DMDM6174889.

Proteomic databases

MaxQBP26367.
PaxDbP26367.
PRIDEP26367.

Protocols and materials databases

DNASU5080.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000241001; ENSP00000241001; ENSG00000007372. [P26367-1]
ENST00000379107; ENSP00000368401; ENSG00000007372. [P26367-2]
ENST00000379109; ENSP00000368403; ENSG00000007372. [P26367-1]
ENST00000379111; ENSP00000368406; ENSG00000007372. [P26367-1]
ENST00000379115; ENSP00000368410; ENSG00000007372. [P26367-2]
ENST00000379123; ENSP00000368418; ENSG00000007372. [P26367-1]
ENST00000379129; ENSP00000368424; ENSG00000007372. [P26367-2]
ENST00000379132; ENSP00000368427; ENSG00000007372. [P26367-1]
ENST00000419022; ENSP00000404100; ENSG00000007372. [P26367-2]
GeneID5080.
KEGGhsa:5080.
UCSCuc001mtd.4. human. [P26367-1]

Organism-specific databases

CTD5080.
GeneCardsGC11M031806.
GeneReviewsPAX6.
HGNCHGNC:8620. PAX6.
HPACAB034143.
HPA030775.
MIM106210. phenotype.
120200. phenotype.
120430. phenotype.
136520. phenotype.
148190. phenotype.
165550. phenotype.
206700. phenotype.
604229. phenotype.
607108. gene.
neXtProtNX_P26367.
Orphanet1065. Aniridia - cerebellar ataxia - intellectual disability.
2334. Autosomal dominant keratitis.
2253. Foveal hypoplasia - presenile cataract.
250923. Isolated aniridia.
137902. Isolated optic nerve hypoplasia.
35737. Morning glory syndrome.
194. Ocular coloboma.
708. Peters anomaly.
893. WAGR syndrome.
PharmGKBPA32960.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG326044.
HOVERGENHBG009115.
KOK08031.
OMAAGENTNS.
OrthoDBEOG7WT431.
PhylomeDBP26367.
TreeFamTF320146.

Enzyme and pathway databases

SignaLinkP26367.

Gene expression databases

ArrayExpressP26367.
BgeeP26367.
CleanExHS_PAX6.
GenevestigatorP26367.

Family and domain databases

Gene3D1.10.10.10. 2 hits.
1.10.10.60. 1 hit.
InterProIPR017970. Homeobox_CS.
IPR001356. Homeobox_dom.
IPR009057. Homeodomain-like.
IPR001523. Paired_dom.
IPR011991. WHTH_DNA-bd_dom.
[Graphical view]
PfamPF00046. Homeobox. 1 hit.
PF00292. PAX. 1 hit.
[Graphical view]
PRINTSPR00027. PAIREDBOX.
SMARTSM00389. HOX. 1 hit.
SM00351. PAX. 1 hit.
[Graphical view]
SUPFAMSSF46689. SSF46689. 2 hits.
PROSITEPS00027. HOMEOBOX_1. 1 hit.
PS50071. HOMEOBOX_2. 1 hit.
PS00034. PAIRED_1. 1 hit.
PS51057. PAIRED_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP26367.
GeneWikiPAX6.
GenomeRNAi5080.
NextBio19596.
PROP26367.
SOURCESearch...

Entry information

Entry namePAX6_HUMAN
AccessionPrimary (citable) accession number: P26367
Secondary accession number(s): Q6N006, Q99413
Entry history
Integrated into UniProtKB/Swiss-Prot: August 1, 1992
Last sequence update: July 15, 1999
Last modified: July 9, 2014
This is version 175 of the entry and version 2 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 11

Human chromosome 11: entries, gene names and cross-references to MIM