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Q02962 (PAX2_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 154. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (5) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Paired box protein Pax-2
Gene names
Name:PAX2
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length417 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Probable transcription factor that may have a role in kidney cell differentiation. Has a critical role in the development of the urogenital tract, the eyes, and the CNS.

Subunit structure

Interacts with ELGN3; the interaction targets PAX2 for destruction. Ref.8

Subcellular location

Nucleus.

Tissue specificity

Expressed in primitive cells of the kidney, ureter, eye, ear and central nervous system.

Developmental stage

Mainly in fetal kidney and juvenile nephrogenic rests.

Involvement in disease

Renal-coloboma syndrome (RCS) [MIM:120330]: An autosomal dominant disorder characterized by both ocular and renal anomalies, but may also include vesicoureteral reflux, high frequency hearing loss, central nervous system anomalies, and/or genital anomalies. Eye anomalies in this disorder consist of a wide and sometimes excavated dysplastic optic disk with the emergence of the retinal vessels from the periphery of the disk, designated optic nerve coloboma or 'morning glory' anomaly. Associated findings may include a small corneal diameter, retinal coloboma, scleral staphyloma, optic nerve cyst, microphthalmia, and pigmentary macular dysplasia. The kidneys are small and abnormally formed (renal hypodysplasia), and have fewer than the normal number of glomeruli, which are enlarged (oligomeganephronia). These ocular and renal anomalies result in decreased visual acuity and retinal detachment, as well as hypertension, proteinuria, and renal insufficiency that frequently progresses to end-stage renal disease.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.10 Ref.13 Ref.14 Ref.15

Defects in PAX2 can be responsible for isolated renal hypodysplasia and oligomeganephronia (OMN). This is a rare congenital and usually sporadic anomaly characterized by bilateral renal hypoplasia, with a reduced number of enlarged nephrons and without urinary tract abnormalities. Ref.12

Sequence similarities

Contains 1 paired domain.

Ontologies

Keywords
   Biological processDifferentiation
Transcription
Transcription regulation
   Cellular componentNucleus
   Coding sequence diversityAlternative splicing
Polymorphism
   DiseaseDisease mutation
   DomainPaired box
   LigandDNA-binding
   Molecular functionDevelopmental protein
   PTMPhosphoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processaging

Inferred from electronic annotation. Source: Ensembl

axonogenesis

Traceable author statement PubMed 9106533. Source: ProtInc

brain morphogenesis

Inferred from sequence or structural similarity. Source: UniProtKB

branching involved in ureteric bud morphogenesis

Inferred from expression pattern PubMed 1337742. Source: UniProtKB

camera-type eye development

Inferred from sequence or structural similarity. Source: UniProtKB

cell fate determination

Inferred from sequence or structural similarity. Source: UniProtKB

cellular response to epidermal growth factor stimulus

Inferred from electronic annotation. Source: Ensembl

cellular response to glucose stimulus

Inferred from sequence or structural similarity. Source: UniProtKB

cellular response to hydrogen peroxide

Inferred from sequence or structural similarity. Source: UniProtKB

cellular response to mechanical stimulus

Inferred from electronic annotation. Source: Ensembl

cellular response to retinoic acid

Inferred from sequence or structural similarity. Source: UniProtKB

cochlea development

Inferred from sequence or structural similarity. Source: UniProtKB

cochlea morphogenesis

Inferred from sequence or structural similarity. Source: UniProtKB

glial cell differentiation

Inferred from sequence or structural similarity. Source: UniProtKB

inner ear morphogenesis

Inferred from sequence or structural similarity. Source: UniProtKB

mesenchymal to epithelial transition

Inferred from sequence or structural similarity. Source: UniProtKB

mesenchymal to epithelial transition involved in metanephros morphogenesis

Inferred from sequence or structural similarity. Source: UniProtKB

mesodermal cell fate specification

Inferred from sequence or structural similarity. Source: UniProtKB

mesonephric duct development

Inferred from electronic annotation. Source: Ensembl

mesonephric tubule formation

Inferred from electronic annotation. Source: Ensembl

mesonephros development

Inferred from sequence or structural similarity. Source: UniProtKB

metanephric collecting duct development

Inferred from sequence or structural similarity. Source: UniProtKB

metanephric distal convoluted tubule development

Inferred from sequence or structural similarity. Source: UniProtKB

metanephric epithelium development

Inferred from expression pattern PubMed 7856737. Source: UniProtKB

metanephric mesenchymal cell differentiation

Inferred from sequence or structural similarity. Source: UniProtKB

metanephric mesenchyme development

Inferred from sequence or structural similarity. Source: UniProtKB

metanephric nephron tubule formation

Inferred from sequence or structural similarity. Source: UniProtKB

negative regulation of apoptotic process

Inferred from direct assay PubMed 10980123. Source: UniProtKB

negative regulation of apoptotic process involved in metanephric collecting duct development

Inferred from sequence or structural similarity. Source: UniProtKB

negative regulation of apoptotic process involved in metanephric nephron tubule development

Inferred from sequence or structural similarity. Source: UniProtKB

negative regulation of cysteine-type endopeptidase activity involved in apoptotic process

Inferred from direct assay PubMed 10980123PubMed 17357786. Source: UniProtKB

negative regulation of cytolysis

Inferred from mutant phenotype PubMed 19118900. Source: UniProtKB

negative regulation of mesenchymal cell apoptotic process involved in metanephric nephron morphogenesis

Inferred from sequence or structural similarity. Source: UniProtKB

negative regulation of mesenchymal cell apoptotic process involved in metanephros development

Inferred from sequence or structural similarity. Source: UniProtKB

negative regulation of programmed cell death

Inferred from sequence or structural similarity. Source: UniProtKB

negative regulation of reactive oxygen species metabolic process

Inferred from direct assay PubMed 17357786. Source: UniProtKB

negative regulation of transcription from RNA polymerase II promoter

Inferred from electronic annotation. Source: Ensembl

negative regulation of transcription, DNA-templated

Inferred from mutant phenotype PubMed 19118900. Source: UniProtKB

nephric duct formation

Inferred from sequence or structural similarity. Source: UniProtKB

neural tube closure

Inferred from sequence or structural similarity. Source: UniProtKB

optic chiasma development

Inferred from sequence or structural similarity. Source: UniProtKB

optic cup morphogenesis involved in camera-type eye development

Inferred from sequence or structural similarity. Source: UniProtKB

optic nerve development

Inferred from sequence or structural similarity. Source: UniProtKB

optic nerve morphogenesis

Inferred from sequence or structural similarity. Source: UniProtKB

optic nerve structural organization

Inferred from sequence or structural similarity. Source: UniProtKB

oxidation-reduction process

Inferred from sequence or structural similarity. Source: GOC

pancreas development

Inferred from electronic annotation. Source: Ensembl

paramesonephric duct development

Inferred from electronic annotation. Source: Ensembl

positive regulation of branching involved in ureteric bud morphogenesis

Inferred from sequence or structural similarity. Source: UniProtKB

positive regulation of epithelial cell proliferation

Inferred from direct assay PubMed 17357786. Source: UniProtKB

positive regulation of mesenchymal to epithelial transition involved in metanephros morphogenesis

Inferred from sequence or structural similarity. Source: UniProtKB

positive regulation of metanephric DCT cell differentiation

Inferred from sequence or structural similarity. Source: UniProtKB

positive regulation of metanephric glomerulus development

Inferred from sequence or structural similarity. Source: UniProtKB

positive regulation of optic nerve formation

Inferred from sequence or structural similarity. Source: UniProtKB

positive regulation of transcription from RNA polymerase II promoter

Inferred from direct assay PubMed 16735463. Source: UniProtKB

positive regulation of transcription, DNA-templated

Inferred from direct assay PubMed 16368682PubMed 17357786PubMed 19048125. Source: UniProtKB

pronephric field specification

Inferred from sequence or structural similarity. Source: UniProtKB

pronephros development

Inferred from sequence or structural similarity. Source: UniProtKB

protein kinase B signaling

Inferred from sequence or structural similarity. Source: UniProtKB

reactive oxygen species metabolic process

Inferred from sequence or structural similarity. Source: UniProtKB

regulation of metanephric nephron tubule epithelial cell differentiation

Inferred from sequence or structural similarity. Source: UniProtKB

regulation of metanephros size

Inferred from mutant phenotype PubMed 17513325. Source: UniProtKB

response to nutrient levels

Inferred from electronic annotation. Source: Ensembl

retinal pigment epithelium development

Inferred from sequence or structural similarity. Source: UniProtKB

stem cell differentiation

Inferred from sequence or structural similarity. Source: UniProtKB

transcription from RNA polymerase II promoter

Traceable author statement PubMed 8760285. Source: ProtInc

transcription, DNA-templated

Inferred from sequence or structural similarity. Source: UniProtKB

ureter development

Inferred from sequence or structural similarity. Source: UniProtKB

ureter maturation

Inferred from sequence or structural similarity. Source: UniProtKB

ureter morphogenesis

Inferred from electronic annotation. Source: Ensembl

urogenital system development

Inferred from sequence or structural similarity. Source: UniProtKB

vestibulocochlear nerve formation

Inferred from sequence or structural similarity. Source: UniProtKB

visual perception

Traceable author statement PubMed 9106533. Source: ProtInc

   Cellular_componentcentriolar satellite

Inferred from direct assay PubMed 18000879. Source: BHF-UCL

lysosome

Inferred from electronic annotation. Source: Ensembl

microtubule organizing center

Inferred from direct assay PubMed 18000879. Source: BHF-UCL

nucleus

Inferred from direct assay PubMed 19048125. Source: UniProtKB

protein complex

Inferred from sequence or structural similarity. Source: UniProtKB

protein-DNA complex

Inferred from sequence or structural similarity. Source: UniProtKB

   Molecular_functionDNA binding

Inferred from sequence or structural similarity. Source: UniProtKB

core promoter proximal region sequence-specific DNA binding

Inferred from direct assay PubMed 19118900. Source: UniProtKB

protein binding

Inferred from physical interaction Ref.8PubMed 9178767. Source: UniProtKB

superoxide-generating NADPH oxidase activity

Inferred from sequence or structural similarity. Source: UniProtKB

transcription regulatory region DNA binding

Inferred from direct assay PubMed 16368682PubMed 16735463PubMed 19048125PubMed 9178767. Source: UniProtKB

Complete GO annotation...

Alternative products

This entry describes 4 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q02962-1)

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 2 (identifier: Q02962-2)

Also known as: Fetal kidney;

The sequence of this isoform differs from the canonical sequence as follows:
     364-417: GSEFSGNPYS...AAAAAAYDRH → EAAVGPSSSL...RLGDSATPPY
Isoform 3 (identifier: Q02962-3)

The sequence of this isoform differs from the canonical sequence as follows:
     206-228: Missing.
Isoform 4 (identifier: Q02962-4)

The sequence of this isoform differs from the canonical sequence as follows:
     206-228: Missing.
     364-417: GSEFSGNPYS...AAAAAAYDRH → EAAVGPSSSL...RLGDSATPPY

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 417417Paired box protein Pax-2
PRO_0000050175

Regions

Domain16 – 142127Paired

Amino acid modifications

Modified residue2261Phosphothreonine Ref.7

Natural variations

Alternative sequence206 – 22823Missing in isoform 3 and isoform 4.
VSP_002345
Alternative sequence364 – 41754GSEFS…AYDRH → EAAVGPSSSLMSKPGRKLAE VPPCVQPTGASSPATRTATP STRPTTRLGDSATPPY in isoform 2 and isoform 4.
VSP_002346
Natural variant241G → E Probable disease-associated mutation found in a patient with renal hypodysplasia. Ref.9
VAR_068079
Natural variant251G → V in RCS. Ref.15
VAR_068080
Natural variant331L → R in RCS. Ref.15
VAR_068081
Natural variant39 – 402Missing in OMN; with bilateral coloboma.
VAR_012442
Natural variant611S → I in RCS. Ref.15
VAR_068082
Natural variant611S → N in RCS. Ref.15
VAR_068083
Natural variant62 – 665Missing in RCS.
VAR_068084
Natural variant691L → P in RCS. Ref.15
VAR_068085
Natural variant711R → T in RCS. Ref.13
VAR_068086
Natural variant751T → TET in RCS.
VAR_003788
Natural variant751T → TT in RCS. Ref.15
VAR_068087
Natural variant761G → S in RCS. Ref.10
VAR_003789
Natural variant841G → GSIKPGVIG in RCS.
VAR_068088
Natural variant841G → S in RCS. Ref.15
VAR_068089
Natural variant1171R → P in RCS. Ref.15
VAR_068090
Natural variant1301P → H in RCS. Ref.14
VAR_068091
Natural variant1301P → S in RCS. Ref.15
VAR_068092
Natural variant1601A → T. Ref.15
Corresponds to variant rs201383632 [ dbSNP | Ensembl ].
VAR_068093
Natural variant1641T → N. Ref.15
VAR_068094
Natural variant1751S → T. Ref.15
VAR_068095
Natural variant3341A → V. Ref.11 Ref.15
Corresponds to variant rs78738655 [ dbSNP | Ensembl ].
VAR_012443
Natural variant3871S → N Found in a patient with bilateral optic nerve colobomas; uncertain pathological significance. Ref.15
VAR_068096

Experimental info

Sequence conflict15 – 162PG → R in AAC41711. Ref.6
Sequence conflict4041Missing in AAA60024. Ref.1
Sequence conflict4041Missing in AAC63385. Ref.3
Sequence conflict4101A → R in AAA60024. Ref.1
Sequence conflict4101A → R in AAC63385. Ref.3

Sequences

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

Last modified February 10, 2009. Version 4.
Checksum: 7EA24F9EB8C843F8

FASTA41744,706
        10         20         30         40         50         60 
MDMHCKADPF SAMHPGHGGV NQLGGVFVNG RPLPDVVRQR IVELAHQGVR PCDISRQLRV 

        70         80         90        100        110        120 
SHGCVSKILG RYYETGSIKP GVIGGSKPKV ATPKVVDKIA EYKRQNPTMF AWEIRDRLLA 

       130        140        150        160        170        180 
EGICDNDTVP SVSSINRIIR TKVQQPFHPT PDGAGTGVTA PGHTIVPSTA SPPVSSASND 

       190        200        210        220        230        240 
PVGSYSINGI LGIPRSNGEK RKRDEVEVYT DPAHIRGGGG LHLVWTLRDV SEGSVPNGDS 

       250        260        270        280        290        300 
QSGVDSLRKH LRADTFTQQQ LEALDRVFER PSYPDVFQAS EHIKSEQGNE YSLPALTPGL 

       310        320        330        340        350        360 
DEVKSSLSAS TNPELGSNVS GTQTYPVVTG RDMASTTLPG YPPHVPPTGQ GSYPTSTLAG 

       370        380        390        400        410 
MVPGSEFSGN PYSHPQYTAY NEAWRFSNPA LLSSPYYYSA APRGSAPAAA AAAYDRH 

« Hide

Isoform 2 (Fetal kidney) [UniParc].

Checksum: 0FE028784294B10E
Show »

FASTA41944,485
Isoform 3 [UniParc].

Checksum: B0CF2E31D3D09900
Show »

FASTA39442,177
Isoform 4 [UniParc].

Checksum: AE946615233BDA16
Show »

FASTA39641,956

References

« Hide 'large scale' references
[1]"Expression of the PAX2 gene in human fetal kidney and Wilms' tumor."
Eccles M.R., Wallis L.J., Fidler A.E., Spurr N.K., Goodfellow P.J., Reeve A.E.
Cell Growth Differ. 3:279-289(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3).
Tissue: Kidney.
[2]"Alternative messenger RNA forms and open reading frames within an additional conserved region of the human PAX-2 gene."
Ward T.A., Nebel A., Reeve A.E., Eccles M.R.
Cell Growth Differ. 5:1015-1021(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 4).
Tissue: Kidney cortex.
[3]"Genomic structure of the human PAX2 gene."
Sanyanusin P., Norrish J.H., Ward T.A., Nebel A., McNoe L.A., Eccles M.R.
Genomics 35:258-261(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], ALTERNATIVE SPLICING (ISOFORM 1).
[4]"The DNA sequence and comparative analysis of human chromosome 10."
Deloukas P., Earthrowl M.E., Grafham D.V., Rubenfield M., French L., Steward C.A., Sims S.K., Jones M.C., Searle S., Scott C., Howe K., Hunt S.E., Andrews T.D., Gilbert J.G.R., Swarbreck D., Ashurst J.L., Taylor A., Battles J. expand/collapse author list , Bird C.P., Ainscough R., Almeida J.P., Ashwell R.I.S., Ambrose K.D., Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Bates K., Beasley H., Bray-Allen S., Brown A.J., Brown J.Y., Burford D.C., Burrill W., Burton J., Cahill P., Camire D., Carter N.P., Chapman J.C., Clark S.Y., Clarke G., Clee C.M., Clegg S., Corby N., Coulson A., Dhami P., Dutta I., Dunn M., Faulkner L., Frankish A., Frankland J.A., Garner P., Garnett J., Gribble S., Griffiths C., Grocock R., Gustafson E., Hammond S., Harley J.L., Hart E., Heath P.D., Ho T.P., Hopkins B., Horne J., Howden P.J., Huckle E., Hynds C., Johnson C., Johnson D., Kana A., Kay M., Kimberley A.M., Kershaw J.K., Kokkinaki M., Laird G.K., Lawlor S., Lee H.M., Leongamornlert D.A., Laird G., Lloyd C., Lloyd D.M., Loveland J., Lovell J., McLaren S., McLay K.E., McMurray A., Mashreghi-Mohammadi M., Matthews L., Milne S., Nickerson T., Nguyen M., Overton-Larty E., Palmer S.A., Pearce A.V., Peck A.I., Pelan S., Phillimore B., Porter K., Rice C.M., Rogosin A., Ross M.T., Sarafidou T., Sehra H.K., Shownkeen R., Skuce C.D., Smith M., Standring L., Sycamore N., Tester J., Thorpe A., Torcasso W., Tracey A., Tromans A., Tsolas J., Wall M., Walsh J., Wang H., Weinstock K., West A.P., Willey D.L., Whitehead S.L., Wilming L., Wray P.W., Young L., Chen Y., Lovering R.C., Moschonas N.K., Siebert R., Fechtel K., Bentley D., Durbin R.M., Hubbard T., Doucette-Stamm L., Beck S., Smith D.R., Rogers J.
Nature 429:375-381(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[5]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[6]"Chromosomal localization of seven PAX genes and cloning of a novel family member, PAX-9."
Stapleton P., Weith A., Urbanek P., Kozmik Z., Busslinger M.
Nat. Genet. 3:292-298(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-136.
[7]"Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-226, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Leukemic T-cell.
[8]"Prolyl hydroxylase domain protein 3 targets Pax2 for destruction."
Yan B., Jiao S., Zhang H.S., Lv D.D., Xue J., Fan L., Wu G.H., Fang J.
Biochem. Biophys. Res. Commun. 409:315-320(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH EGLN3.
[9]"HNF1B and PAX2 mutations are a common cause of renal hypodysplasia in the CKiD cohort."
Thomas R., Sanna-Cherchi S., Warady B.A., Furth S.L., Kaskel F.J., Gharavi A.G.
Pediatr. Nephrol. 26:897-903(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: INVOLVEMENT IN RENAL HYPODYSPLASIA, VARIANT GLU-24.
[10]"Missense mutation and hexanucleotide duplication in the PAX2 gene in two unrelated families with renal-coloboma syndrome (MIM 120330)."
Devriendt K., Matthijs G., van Damme B., van Caesbroeck D., Eccles M.R., Vanrenterghem Y., Fryns J.-P., Leys A.
Hum. Genet. 103:149-153(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS RCS GLU-THR-75 INS AND SER-76.
[11]"Identification of two novel polymorphisms (g.903C>T and g.1544C>T) in the PAX2 gene."
Gelb A.C., Manligas G.S., Gharaybeh S., Schimmenti L.A.
Hum. Mutat. 17:155-155(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT VAL-334.
[12]"PAX2 mutations in oligomeganephronia."
Salomon R., Tellier A.-L., Attie-Bitach T., Amiel J., Vekemans M., Lyonnet S., Dureau P., Niaudet P., Gubler M.-C., Broyer M.
Kidney Int. 59:457-462(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT OMN 39-GLN-ARG-40 DEL.
[13]"Macular abnormalities and optic disk anomaly associated with a new PAX2 missense mutation."
Higashide T., Wada T., Sakurai M., Yokoyama H., Sugiyama K.
Am. J. Ophthalmol. 139:203-205(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT RCS THR-71.
[14]"A case of renal-coloboma syndrome associated with mental developmental delay exhibiting a novel PAX2 gene mutation."
Miyazawa T., Nakano M., Takemura Y., Miyazaki K., Yanagida H., Fujita S., Sugimoto K., Okada M., Takemura T.
Clin. Nephrol. 72:497-500(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT RCS HIS-130.
[15]"Update of PAX2 mutations in renal coloboma syndrome and establishment of a locus-specific database."
Bower M., Salomon R., Allanson J., Antignac C., Benedicenti F., Benetti E., Binenbaum G., Jensen U.B., Cochat P., DeCramer S., Dixon J., Drouin R., Falk M.J., Feret H., Gise R., Hunter A., Johnson K., Kumar R. expand/collapse author list , Lavocat M.P., Martin L., Moriniere V., Mowat D., Murer L., Nguyen H.T., Peretz-Amit G., Pierce E., Place E., Rodig N., Salerno A., Sastry S., Sato T., Sayer J.A., Schaafsma G.C., Shoemaker L., Stockton D.W., Tan W.H., Tenconi R., Vanhille P., Vats A., Wang X., Warman B., Weleber R.G., White S.M., Wilson-Brackett C., Zand D.J., Eccles M., Schimmenti L.A., Heidet L.
Hum. Mutat. 33:457-466(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS RCS VAL-25; ARG-33; ILE-61; ASN-61; 62-HIS--SER-66 DEL; PRO-69; THR-75 INS; SER-84; SER-ILE-LYS-PRO-GLY-VAL-ILE-GLY-84 INS; PRO-117 AND SER-130, VARIANTS THR-160; ASN-164; THR-175; VAL-334 AND ASN-387.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M89470 mRNA. Translation: AAA60024.1.
L25597 mRNA. Translation: AAA36417.1.
U45255 expand/collapse EMBL AC list , U45245, U45246, U45247, U45248, U45249, U45250, U45251, U45253, U45254 Genomic DNA. Translation: AAC63385.1.
AL138762, AL589862 Genomic DNA. Translation: CAH70951.1.
AL138762, AL589862 Genomic DNA. Translation: CAH70952.1.
AL589862, AL138762 Genomic DNA. Translation: CAI17855.1.
AL589862, AL138762 Genomic DNA. Translation: CAI17856.1.
CH471066 Genomic DNA. Translation: EAW49812.1.
CH471066 Genomic DNA. Translation: EAW49813.1.
L09747, L09748, L09746 Genomic DNA. Translation: AAC41711.1.
CCDSCCDS7499.1. [Q02962-4]
PIRA49008.
RefSeqNP_000269.2. NM_000278.3.
NP_003978.2. NM_003987.3.
NP_003979.2. NM_003988.3. [Q02962-4]
NP_003980.2. NM_003989.3.
NP_003981.2. NM_003990.3.
UniGeneHs.155644.

3D structure databases

ProteinModelPortalQ02962.
SMRQ02962. Positions 19-142, 252-309.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid111110. 9 interactions.
IntActQ02962. 4 interactions.
STRING9606.ENSP00000355069.

PTM databases

PhosphoSiteQ02962.

Polymorphism databases

DMDM223590261.

Proteomic databases

PaxDbQ02962.
PRIDEQ02962.

Protocols and materials databases

DNASU5076.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000355243; ENSP00000347385; ENSG00000075891. [Q02962-3]
ENST00000361791; ENSP00000355069; ENSG00000075891. [Q02962-4]
ENST00000370296; ENSP00000359319; ENSG00000075891. [Q02962-2]
ENST00000428433; ENSP00000396259; ENSG00000075891. [Q02962-1]
GeneID5076.
KEGGhsa:5076.
UCSCuc001krk.4. human. [Q02962-1]
uc001krl.4. human. [Q02962-4]
uc001krm.4. human. [Q02962-2]
uc001krn.4. human. [Q02962-3]

Organism-specific databases

CTD5076.
GeneCardsGC10P102495.
GeneReviewsPAX2.
HGNCHGNC:8616. PAX2.
HPACAB013024.
HPA047704.
MIM120330. phenotype.
167409. gene.
neXtProtNX_Q02962.
Orphanet1475. Renal coloboma syndrome.
PharmGKBPA32956.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG326044.
HOGENOMHOG000230938.
HOVERGENHBG009115.
KOK15608.
OMADSHPSYP.
PhylomeDBQ02962.
TreeFamTF315397.

Enzyme and pathway databases

SignaLinkQ02962.

Gene expression databases

ArrayExpressQ02962.
BgeeQ02962.
CleanExHS_PAX2.
GenevestigatorQ02962.

Family and domain databases

Gene3D1.10.10.10. 2 hits.
InterProIPR009057. Homeodomain-like.
IPR001523. Paired_dom.
IPR022130. Pax2_C.
IPR011991. WHTH_DNA-bd_dom.
[Graphical view]
PfamPF00292. PAX. 1 hit.
PF12403. Pax2_C. 1 hit.
[Graphical view]
PRINTSPR00027. PAIREDBOX.
SMARTSM00351. PAX. 1 hit.
[Graphical view]
SUPFAMSSF46689. SSF46689. 1 hit.
PROSITEPS00034. PAIRED_1. 1 hit.
PS51057. PAIRED_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

GeneWikiPAX2.
GenomeRNAi5076.
NextBio19560.
PROQ02962.
SOURCESearch...

Entry information

Entry namePAX2_HUMAN
AccessionPrimary (citable) accession number: Q02962
Secondary accession number(s): Q15105 expand/collapse secondary AC list , Q15110, Q15837, Q5SZP2, Q5SZP3
Entry history
Integrated into UniProtKB/Swiss-Prot: July 1, 1993
Last sequence update: February 10, 2009
Last modified: July 9, 2014
This is version 154 of the entry and version 4 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

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 10

Human chromosome 10: entries, gene names and cross-references to MIM