Q02962 (PAX2_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Paired box protein Pax-2

Gene names

Name:

PAX2

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	417 AA.
Sequence status	Complete.
Protein existence	Evidence 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 process	Differentiation Transcription Transcription regulation
Cellular component	Nucleus
Coding sequence diversity	Alternative splicing Polymorphism
Disease	Disease mutation
Domain	Paired box
Ligand	DNA-binding
Molecular function	Developmental protein
PTM	Phosphoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	aging Inferred from electronic annotation. Source: Compara 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 cell fate determination Inferred from sequence or structural similarity. Source: UniProtKB cellular response to epidermal growth factor stimulus Inferred from electronic annotation. Source: Compara 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: Compara 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 mesonephric duct development Inferred from electronic annotation. Source: Compara mesonephric tubule formation Inferred from electronic annotation. Source: Compara 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 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 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: Compara negative regulation of transcription, DNA-dependent 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 structural organization Inferred from sequence or structural similarity. Source: UniProtKB pancreas development Inferred from electronic annotation. Source: Compara paramesonephric duct development Inferred from electronic annotation. Source: Compara 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 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 PubMed 17513325. Source: UniProtKB response to nutrient levels Inferred from electronic annotation. Source: Compara 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 ureter maturation Inferred from sequence or structural similarity. Source: UniProtKB ureter morphogenesis Inferred from electronic annotation. Source: Compara vestibulocochlear nerve formation Inferred from sequence or structural similarity. Source: UniProtKB visual perception Traceable author statement PubMed 9106533. Source: ProtInc
Cellular_component	centriolar satellite Inferred from direct assay PubMed 18000879. Source: BHF-UCL lysosome Inferred from electronic annotation. Source: Compara 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_function	core promoter proximal region sequence-specific DNA binding Inferred from direct assay PubMed 19118900. 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 key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 417	417	Paired box protein Pax-2		PRO_0000050175
Regions
	Domain	16 – 142	127	Paired
Amino acid modifications
	Modified residue	226	1	Phosphothreonine Ref.7
Natural variations
	Alternative sequence	206 – 228	23	Missing in isoform 3 and isoform 4.		VSP_002345
	Alternative sequence	364 – 417	54	GSEFS…AYDRH → EAAVGPSSSLMSKPGRKLAE VPPCVQPTGASSPATRTATP STRPTTRLGDSATPPY in isoform 2 and isoform 4.		VSP_002346
	Natural variant	24	1	G → E Probable disease-associated mutation found in a patient with renal hypodysplasia. Ref.9		VAR_068079
	Natural variant	25	1	G → V in RCS. Ref.15		VAR_068080
	Natural variant	33	1	L → R in RCS. Ref.15		VAR_068081
	Natural variant	39 – 40	2	Missing in OMN; with bilateral coloboma.		VAR_012442
	Natural variant	61	1	S → I in RCS. Ref.15		VAR_068082
	Natural variant	61	1	S → N in RCS. Ref.15		VAR_068083
	Natural variant	62 – 66	5	Missing in RCS.		VAR_068084
	Natural variant	69	1	L → P in RCS. Ref.15		VAR_068085
	Natural variant	71	1	R → T in RCS. Ref.13		VAR_068086
	Natural variant	75	1	T → TET in RCS.		VAR_003788
	Natural variant	75	1	T → TT in RCS. Ref.15		VAR_068087
	Natural variant	76	1	G → S in RCS. Ref.10		VAR_003789
	Natural variant	84	1	G → GSIKPGVIG in RCS.		VAR_068088
	Natural variant	84	1	G → S in RCS. Ref.15		VAR_068089
	Natural variant	117	1	R → P in RCS. Ref.15		VAR_068090
	Natural variant	130	1	P → H in RCS. Ref.14		VAR_068091
	Natural variant	130	1	P → S in RCS. Ref.15		VAR_068092
	Natural variant	160	1	A → T. Ref.15		VAR_068093
	Natural variant	164	1	T → N. Ref.15		VAR_068094
	Natural variant	175	1	S → T. Ref.15		VAR_068095
	Natural variant	334	1	A → V. Ref.11 Ref.15 Corresponds to variant rs78738655 [ dbSNP | Ensembl ].		VAR_012443
	Natural variant	387	1	S → N Found in a patient with bilateral optic nerve colobomas; uncertain pathological significance. Ref.15		VAR_068096
Experimental info
	Sequence conflict	15 – 16	2	PG → R in AAC41711. Ref.6
	Sequence conflict	404	1	Missing in AAA60024. Ref.1
	Sequence conflict	404	1	Missing in AAC63385. Ref.3
	Sequence conflict	410	1	A → R in AAA60024. Ref.1
	Sequence conflict	410	1	A → R in AAC63385. Ref.3

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified February 10, 2009. Version 4. Checksum: 7EA24F9EB8C843F8	FASTA	417	44,706
	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
	Isoform 2 (Fetal kidney) [UniParc]. Checksum: 0FE028784294B10E	FASTA	419	44,485
	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 MVPEAAVGPS SSLMSKPGRK LAEVPPCVQP TGASSPATRT ATPSTRPTTR LGDSATPPY
	Isoform 3 [UniParc]. Checksum: B0CF2E31D3D09900	FASTA	394	42,177
	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 RKRDEDVSEG SVPNGDSQSG VDSLRKHLRA DTFTQQQLEA 250 260 270 280 290 300 LDRVFERPSY PDVFQASEHI KSEQGNEYSL PALTPGLDEV KSSLSASTNP ELGSNVSGTQ 310 320 330 340 350 360 TYPVVTGRDM ASTTLPGYPP HVPPTGQGSY PTSTLAGMVP GSEFSGNPYS HPQYTAYNEA 370 380 390 WRFSNPALLS SPYYYSAAPR GSAPAAAAAA YDRH
	Isoform 4 [UniParc]. Checksum: AE946615233BDA16	FASTA	396	41,956
	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 RKRDEDVSEG SVPNGDSQSG VDSLRKHLRA DTFTQQQLEA 250 260 270 280 290 300 LDRVFERPSY PDVFQASEHI KSEQGNEYSL PALTPGLDEV KSSLSASTNP ELGSNVSGTQ 310 320 330 340 350 360 TYPVVTGRDM ASTTLPGYPP HVPPTGQGSY PTSTLAGMVP EAAVGPSSSL MSKPGRKLAE 370 380 390 VPPCVQPTGA SSPATRTATP STRPTTRLGD SATPPY

References

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

Web resources

PAX2 mutation db

Atlas of Genetics and Cytogenetics in Oncology and Haematology

GeneReviews

PAX2 variant database paired box 2 (PAX2)

Leiden Open Variation Database (LOVD)

Cross-references

Sequence databases
EMBL GenBank DDBJ	M89470 mRNA. Translation: AAA60024.1. L25597 mRNA. Translation: AAA36417.1. U45255 , 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.
IPI	IPI00179609. IPI00220545. IPI00375134. IPI00395548.
PIR	A49008.
RefSeq	NP_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.
UniGene	Hs.155644.
3D structure databases
ProteinModelPortal	Q02962.
ModBase	Search...
Protein-protein interaction databases
IntAct	Q02962. 4 interactions.
STRING	9606.ENSP00000355069.
PTM databases
PhosphoSite	Q02962.
Polymorphism databases
DMDM	223590261.
Proteomic databases
PaxDb	Q02962.
PRIDE	Q02962.
Protocols and materials databases
DNASU	5076.
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000355243; ENSP00000347385; ENSG00000075891. ENST00000361791; ENSP00000355069; ENSG00000075891. ENST00000370296; ENSP00000359319; ENSG00000075891. ENST00000428433; ENSP00000396259; ENSG00000075891.
GeneID	5076.
KEGG	hsa:5076.
UCSC	uc001krk.4. human. uc001krl.4. human. uc001krm.4. human. uc001krn.4. human.
Organism-specific databases
CTD	5076.
GeneCards	GC10P102495.
HGNC	HGNC:8616. PAX2.
HPA	CAB013024.
MIM	120330. phenotype. 167409. gene.
neXtProt	NX_Q02962.
Orphanet	1475. Renal coloboma syndrome.
PharmGKB	PA32956.
GenAtlas	Search...
Phylogenomic databases
eggNOG	NOG326044.
HOGENOM	HOG000230938.
HOVERGEN	HBG009115.
KO	K15608.
OMA	TYPVVTX.
OrthoDB	EOG49S66H.
PhylomeDB	Q02962.
Enzyme and pathway databases
SignaLink	Q02962.
Gene expression databases
ArrayExpress	Q02962.
Bgee	Q02962.
CleanEx	HS_PAX2.
Genevestigator	Q02962.
GermOnline	ENSG00000075891. Homo sapiens.
Family and domain databases
Gene3D	1.10.10.10. 2 hits.
InterPro	IPR009057. Homeodomain-like. IPR001523. Paired_dom. IPR022130. Pax2_C. IPR011991. WHTH_DNA-bd_dom. [Graphical view]
Pfam	PF00292. PAX. 1 hit. PF12403. Pax2_C. 1 hit. [Graphical view]
PRINTS	PR00027. PAIREDBOX.
SMART	SM00351. PAX. 1 hit. [Graphical view]
SUPFAM	SSF46689. Homeodomain_like. 1 hit.
PROSITE	PS00034. PAIRED_1. 1 hit. PS51057. PAIRED_2. 1 hit. [Graphical view]
ProtoNet	Search...
Other
GenomeRNAi	5076.
NextBio	19560.
SOURCE	Search...

Entry information

Entry name

PAX2_HUMAN

Accession

Primary (citable) accession number: Q02962
Secondary accession number(s): Q15105 , Q15110, Q15837, Q5SZP2, Q5SZP3

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 1, 1993
Last sequence update:	February 10, 2009
Last modified:	May 29, 2013
This is version 143 of the entry and version 4 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.