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Q02962 (PAX2_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 128. 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)
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

Defects in PAX2 are the cause of renal-coloboma syndrome (RCS) [MIM:120330]; also known as papillorenal syndrome or optic nerve coloboma with renal disease. RCS is an autosomal dominant disease characterized by the association of renal hypoplasia, vesicoureteral reflux and dysplasia of the retina and optic disk. Ref.9

Note=Defects in PAX2 may be responsible for isolated renal hypoplasia as observed in oligomeganephronia, a rare congenital and usually sporadic anomaly characterized by bilateral renal hypoplasia, with a reduced number of enlarged nephrons and without urinary tract abnormalities.

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 processanti-apoptosis

Inferred from mutant phenotype. Source: UniProtKB

axonogenesis

Traceable author statement. Source: ProtInc

brain morphogenesis

Inferred from sequence or structural similarity. Source: UniProtKB

branching involved in ureteric bud morphogenesis

Inferred from expression pattern. Source: UniProtKB

cell fate determination

Inferred from sequence or structural similarity. Source: UniProtKB

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 retinoic acid

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

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

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 mesenchymal cell differentiation

Inferred from sequence or structural similarity. Source: UniProtKB

metanephric nephron tubule formation

Inferred from sequence or structural similarity. Source: UniProtKB

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

Inferred from direct assay. Source: UniProtKB

negative regulation of cytolysis

Inferred from mutant phenotype. Source: UniProtKB

negative regulation of mesenchymal stem cell apoptosis involved in metanephric nephron morphogenesis

Inferred from sequence or structural similarity. Source: UniProtKB

negative regulation of reactive oxygen species metabolic process

Inferred from direct assay. Source: UniProtKB

negative regulation of transcription, DNA-dependent

Inferred from mutant phenotype. 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 structural organization

Inferred from sequence or structural similarity. Source: UniProtKB

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. 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. Source: UniProtKB

pronephric field specification

Inferred from sequence or structural similarity. Source: UniProtKB

protein kinase B signaling cascade

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. Source: UniProtKB

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. Source: ProtInc

ureter maturation

Inferred from sequence or structural similarity. Source: UniProtKB

vestibulocochlear nerve formation

Inferred from sequence or structural similarity. Source: UniProtKB

visual perception

Traceable author statement. Source: ProtInc

   Cellular componentcentriolar satellite

Inferred from direct assay. Source: BHF-UCL

nucleus

Inferred from direct assay. Source: UniProtKB

protein complex

Inferred from sequence or structural similarity. Source: UniProtKB

protein-DNA complex

Inferred from sequence or structural similarity. Source: UniProtKB

   Molecular functioncore promoter proximal region sequence-specific DNA binding

Inferred from direct assay. Source: UniProtKB

superoxide-generating NADPH oxidase activity

Inferred from sequence or structural similarity. 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 variant39 – 402Missing in OMN; with bilateral coloboma.
VAR_012442
Natural variant751T → TET in RCS.
VAR_003788
Natural variant761G → S in RCS. Ref.9
VAR_003789
Natural variant3341A → V. Ref.10
VAR_012443

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: 1378753] [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: 7819127] [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: 8661132] [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: 15164054] [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: 7981748] [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: 19690332] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-226, MASS SPECTROMETRY.
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: 21575608] [Abstract]
Cited for: INTERACTION WITH EGLN3.
[9]"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: 9760197] [Abstract]
Cited for: VARIANTS RCS GLU-THR-75 INS AND SER-76.
[10]"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: 11180607] [Abstract]
Cited for: VARIANT VAL-334.
[11]"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: 11168927] [Abstract]
Cited for: VARIANT OMN 39-GLN-ARG-40 DEL.
+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.
IPIIPI00179609.
IPI00220545.
IPI00375134.
IPI00395548.
PIRA49008.
RefSeqNP_000269.2. NM_000278.3.
NP_003978.2. NM_003987.3.
NP_003979.2. NM_003988.3.
NP_003980.2. NM_003989.3.
NP_003981.2. NM_003990.3.
UniGeneHs.155644.

3D structure databases

ProteinModelPortalQ02962.
SMRQ02962. Positions 19-142, 250-311.
ModBaseSearch...

Protein-protein interaction databases

IntActQ02962. 4 interactions.
STRINGQ02962.

PTM databases

PhosphoSiteQ02962.

Polymorphism databases

DMDM223590261.

Proteomic databases

PRIDEQ02962.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000370294; ENSP00000359317; ENSG00000075891.
ENST00000428433; ENSP00000396259; ENSG00000075891.
GeneID5076.
KEGGhsa:5076.
UCSCuc001krk.2. human.

Organism-specific databases

CTD5076.
GeneCardsGC10P102495.
HGNCHGNC:8616. PAX2.
HPACAB013024.
MIM120330. phenotype.
167409. gene.
neXtProtNX_Q02962.
Orphanet2260. Oligomeganephronia.
1475. Papillo-renal syndrome.
PharmGKBPA32956.
GenAtlasSearch...

Phylogenomic databases

eggNOGprNOG08685.
HOVERGENHBG009115.
OMAFSAMHRH.
OrthoDBEOG49S66H.
PhylomeDBQ02962.

Gene expression databases

ArrayExpressQ02962.
BgeeQ02962.
CleanExHS_PAX2.
GenevestigatorQ02962.
GermOnlineENSG00000075891. Homo sapiens.

Family and domain databases

InterProIPR009057. Homeodomain-like.
IPR012287. Homeodomain-rel.
IPR001523. Paired_box_N.
IPR022130. Pax2_C.
IPR011991. WHTH_trsnscrt_rep_DNA-bd.
[Graphical view]
Gene3DG3DSA:1.10.10.60. Homeodomain-rel. 1 hit.
G3DSA:1.10.10.10. Wing_hlx_DNA_bd. 2 hits.
KOK15608.
PfamPF00292. PAX. 1 hit.
PF12403. Pax2_C. 1 hit.
[Graphical view]
PRINTSPR00027. PAIREDBOX.
SMARTSM00351. PAX. 1 hit.
[Graphical view]
SUPFAMSSF46689. Homeodomain_like. 1 hit.
PROSITEPS00034. PAIRED_1. 1 hit.
PS51057. PAIRED_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio19560.
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: January 25, 2012
This is version 128 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

Human chromosome 10

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

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

MIM cross-references

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

SIMILARITY comments

Index of protein domains and families