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P78562 (PHEX_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 142. 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·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Phosphate-regulating neutral endopeptidase

EC=3.4.24.-
Alternative name(s):
Metalloendopeptidase homolog PEX
Vitamin D-resistant hypophosphatemic rickets protein
X-linked hypophosphatemia protein
Short name=HYP
Gene names
Name:PHEX
Synonyms:PEX
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length749 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Probably involved in bone and dentin mineralization and renal phosphate reabsorption.

Cofactor

Binds 1 zinc ion per subunit By similarity.

Subcellular location

Membrane; Single-pass type II membrane protein Potential.

Tissue specificity

Lymphocytes and fetal brain; not in adult brain, placenta, skeletal muscle and pancreas; not in adult and fetal heart, lung, liver and kidney.

Involvement in disease

Hypophosphatemic rickets, X-linked dominant (XLHR) [MIM:307800]: A disorder characterized by impaired phosphate uptake in the kidney, which is likely to be caused by abnormal regulation of sodium phosphate cotransport in the proximal tubules. Clinical manifestations include skeletal deformities, growth failure, craniosynostosis, paravertebral calcifications, pseudofractures in lower extremities, and muscular hypotonia with onset in early childhood. X-linked hypophosphatemic rickets is the most common form of hypophosphatemia with an incidence of 1 in 20000.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.1 Ref.5 Ref.10 Ref.11 Ref.12 Ref.13 Ref.14 Ref.15

Sequence similarities

Belongs to the peptidase M13 family.

Ontologies

Keywords
   Biological processBiomineralization
   Cellular componentMembrane
   DiseaseDisease mutation
   DomainSignal-anchor
Transmembrane
Transmembrane helix
   LigandMetal-binding
Zinc
   Molecular functionAminopeptidase
Hydrolase
Metalloprotease
Protease
   PTMGlycoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processbone mineralization

Inferred from electronic annotation. Source: Ensembl

cell-cell signaling

Traceable author statement Ref.9. Source: ProtInc

cellular protein modification process

Traceable author statement Ref.9. Source: ProtInc

organophosphate metabolic process

Inferred from electronic annotation. Source: Ensembl

proteolysis

Inferred from direct assay PubMed 11409890. Source: UniProtKB

skeletal system development

Traceable author statement Ref.4. Source: ProtInc

   Cellular_componentGolgi apparatus

Inferred from electronic annotation. Source: Ensembl

endoplasmic reticulum

Inferred from electronic annotation. Source: Ensembl

integral component of plasma membrane

Traceable author statement PubMed 9593714. Source: ProtInc

perinuclear region of cytoplasm

Inferred from electronic annotation. Source: Ensembl

plasma membrane

Traceable author statement PubMed 9593714. Source: ProtInc

   Molecular_functionaminopeptidase activity

Inferred from electronic annotation. Source: UniProtKB-KW

metalloendopeptidase activity

Traceable author statement PubMed 9593714. Source: ProtInc

zinc ion binding

Traceable author statement Ref.4. Source: ProtInc

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 749749Phosphate-regulating neutral endopeptidase
PRO_0000078228

Regions

Topological domain1 – 2020Cytoplasmic Potential
Transmembrane21 – 4121Helical; Signal-anchor for type II membrane protein; Potential
Topological domain42 – 641600Extracellular Potential

Sites

Active site5811 By similarity
Active site6461Proton donor Potential
Metal binding5801Zinc; catalytic By similarity
Metal binding5841Zinc; catalytic By similarity
Metal binding6421Zinc; catalytic By similarity

Amino acid modifications

Glycosylation711N-linked (GlcNAc...) Potential
Glycosylation2381N-linked (GlcNAc...) Potential
Glycosylation2631N-linked (GlcNAc...) Potential
Glycosylation2901N-linked (GlcNAc...) Potential
Glycosylation3011N-linked (GlcNAc...) Potential
Glycosylation3771N-linked (GlcNAc...) Potential
Glycosylation4841N-linked (GlcNAc...) Potential
Glycosylation7361N-linked (GlcNAc...) Potential

Natural variations

Natural variant771C → S in XLHR. Ref.10
VAR_006738
Natural variant801F → S in XLHR; sporadic. Ref.13
VAR_010616
Natural variant851C → F in XLHR; sporadic. Ref.14
VAR_010617
Natural variant851C → R in XLHR. Ref.1
VAR_010618
Natural variant851C → Y in XLHR. Ref.5
VAR_006739
Natural variant1381L → P in XLHR. Ref.10
VAR_006740
Natural variant1411S → P in XLHR; sporadic. Ref.14
VAR_010619
Natural variant1421C → F in XLHR. Ref.13
VAR_010620
Natural variant1601L → R in XLHR. Ref.15
VAR_010621
Natural variant1661R → C in XLHR. Ref.5
VAR_006741
Natural variant2371D → G in XLHR; sporadic. Ref.13
VAR_010622
Natural variant2521F → S in XLHR. Ref.5
VAR_006742
Natural variant2531M → I in XLHR. Ref.5
VAR_006743
Natural variant3171Y → F in XLHR. Ref.12
VAR_010623
Natural variant3411Missing in XLHR; sporadic. Ref.14
VAR_010624
Natural variant4441W → WN in XLHR. Ref.15
VAR_010625
Natural variant5301W → C in XLHR. Ref.13
VAR_010626
Natural variant5341P → L in XLHR. Ref.1 Ref.10 Ref.12
VAR_006744
Natural variant5551L → P in XLHR. Ref.11
VAR_010627
Natural variant5671R → P in XLHR; sporadic. Ref.14
VAR_010628
Natural variant5731A → D in XLHR; sporadic. Ref.13
VAR_010629
Natural variant5791G → R in XLHR. Ref.1 Ref.10 Ref.12
VAR_006745
Natural variant5791G → V in XLHR. Ref.5
VAR_006746
Natural variant6211Q → R in XLHR. Ref.12
VAR_010630
Natural variant6511R → P in XLHR. Ref.1
VAR_010631
Natural variant6801N → K in XLHR; sporadic. Ref.14
VAR_010633
Natural variant6801Missing in XLHR. Ref.12
VAR_010632
Natural variant6931C → Y in XLHR; sporadic. Ref.14
VAR_010634
Natural variant7201A → T in XLHR. Ref.12
VAR_010635
Natural variant7311F → Y in XLHR. Ref.12
VAR_010636
Natural variant7331C → S in XLHR; sporadic. Ref.13
VAR_010637
Natural variant7461C → W in XLHR; sporadic. Ref.13
VAR_010638
Natural variant7491W → R in XLHR. Ref.12
VAR_010639

Experimental info

Sequence conflict3631A → D in AAC50552. Ref.9
Sequence conflict4031W → R in AAC50552. Ref.9
Sequence conflict6411G → A in AAC50552. Ref.9

Sequences

Sequence LengthMass (Da)Tools
P78562 [UniParc].

Last modified May 1, 1997. Version 1.
Checksum: 7C4F9F3E2471C6A8

FASTA74986,474
        10         20         30         40         50         60 
MEAETGSSVE TGKKANRGTR IALVVFVGGT LVLGTILFLV SQGLLSLQAK QEYCLKPECI 

        70         80         90        100        110        120 
EAAAAILSKV NLSVDPCDNF FRFACDGWIS NNPIPEDMPS YGVYPWLRHN VDLKLKELLE 

       130        140        150        160        170        180 
KSISRRRDTE AIQKAKILYS SCMNEKAIEK ADAKPLLHIL RHSPFRWPVL ESNIGPEGVW 

       190        200        210        220        230        240 
SERKFSLLQT LATFRGQYSN SVFIRLYVSP DDKASNEHIL KLDQATLSLA VREDYLDNST 

       250        260        270        280        290        300 
EAKSYRDALY KFMVDTAVLL GANSSRAEHD MKSVLRLEIK IAEIMIPHEN RTSEAMYNKM 

       310        320        330        340        350        360 
NISELSAMIP QFDWLGYIKK VIDTRLYPHL KDISPSENVV VRVPQYFKDL FRILGSERKK 

       370        380        390        400        410        420 
TIANYLVWRM VYSRIPNLSR RFQYRWLEFS RVIQGTTTLL PQWDKCVNFI ESALPYVVGK 

       430        440        450        460        470        480 
MFVDVYFQED KKEMMEELVE GVRWAFIDML EKENEWMDAG TKRKAKEKAR AVLAKVGYPE 

       490        500        510        520        530        540 
FIMNDTHVNE DLKAIKFSEA DYFGNVLQTR KYLAQSDFFW LRKAVPKTEW FTNPTTVNAF 

       550        560        570        580        590        600 
YSASTNQIRF PAGELQKPFF WGTEYPRSLS YGAIGVIVGH EFTHGFDNNG RKYDKNGNLD 

       610        620        630        640        650        660 
PWWSTESEEK FKEKTKCMIN QYSNYYWKKA GLNVKGKRTL GENIADNGGL REAFRAYRKW 

       670        680        690        700        710        720 
INDRRQGLEE PLLPGITFTN NQLFFLSYAH VRCNSYRPEA AREQVQIGAH SPPQFRVNGA 

       730        740 
ISNFEEFQKA FNCPPNSTMN RGMDSCRLW 

« Hide

References

« Hide 'large scale' references
[1]"Genomic organization of the human PEX gene mutated in X-linked dominant hypophosphatemic rickets."
Francis F., Strom T.M., Hennig S., Boeddrich A., Lorenz B., Brandau O., Mohnike K.L., Cagnoli M., Steffens C., Klages S., Borzym K., Pohl T., Oudet C.L., Econs M.J., Rowe P.S.N., Reinhardt R., Meitinger T., Lehrach H.
Genome Res. 7:573-585(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANTS XLHR ARG-85; LEU-534; ARG-579 AND PRO-651.
[2]"Pex/PEX tissue distribution and evidence for a deletion in the 3' region of the Pex gene in X-linked hypophosphatemic mice."
Beck L., Soumounou Y., Martel J., Krishnamurthy G., Gauthier C., Goodyer C.G., Tenenhouse H.S.
J. Clin. Invest. 99:1200-1209(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[3]"Cloning and sequencing of human PEX from a bone cDNA library: evidence for its developmental stage-specific regulation in osteoblasts."
Guo R., Quarles L.D.
J. Bone Miner. Res. 12:1009-1017(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Bone.
[4]"Expression and cloning of the human X-linked hypophosphatemia gene cDNA."
Grieff M., Mumm S., Waeltz P., Mazzarella R., Whyte M.P., Thakker R.V., Schlessinger D.
Biochem. Biophys. Res. Commun. 231:635-639(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[5]"Mutational analysis of the PEX gene in patients with X-linked hypophosphatemic rickets."
Holm I.A., Huang X., Kunkel L.M.
Am. J. Hum. Genet. 60:790-797(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANTS XLHR TYR-85; CYS-166; SER-252; ILE-253 AND VAL-579.
[6]Lipman M.L., Panda D., Henderson J.E., Shen Y., Goltzman D., Karaplis A.C.
Submitted (JAN-1997) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[7]"The DNA sequence of the human X chromosome."
Ross M.T., Grafham D.V., Coffey A.J., Scherer S., McLay K., Muzny D., Platzer M., Howell G.R., Burrows C., Bird C.P., Frankish A., Lovell F.L., Howe K.L., Ashurst J.L., Fulton R.S., Sudbrak R., Wen G., Jones M.C. expand/collapse author list , Hurles M.E., Andrews T.D., Scott C.E., Searle S., Ramser J., Whittaker A., Deadman R., Carter N.P., Hunt S.E., Chen R., Cree A., Gunaratne P., Havlak P., Hodgson A., Metzker M.L., Richards S., Scott G., Steffen D., Sodergren E., Wheeler D.A., Worley K.C., Ainscough R., Ambrose K.D., Ansari-Lari M.A., Aradhya S., Ashwell R.I., Babbage A.K., Bagguley C.L., Ballabio A., Banerjee R., Barker G.E., Barlow K.F., Barrett I.P., Bates K.N., Beare D.M., Beasley H., Beasley O., Beck A., Bethel G., Blechschmidt K., Brady N., Bray-Allen S., Bridgeman A.M., Brown A.J., Brown M.J., Bonnin D., Bruford E.A., Buhay C., Burch P., Burford D., Burgess J., Burrill W., Burton J., Bye J.M., Carder C., Carrel L., Chako J., Chapman J.C., Chavez D., Chen E., Chen G., Chen Y., Chen Z., Chinault C., Ciccodicola A., Clark S.Y., Clarke G., Clee C.M., Clegg S., Clerc-Blankenburg K., Clifford K., Cobley V., Cole C.G., Conquer J.S., Corby N., Connor R.E., David R., Davies J., Davis C., Davis J., Delgado O., Deshazo D., Dhami P., Ding Y., Dinh H., Dodsworth S., Draper H., Dugan-Rocha S., Dunham A., Dunn M., Durbin K.J., Dutta I., Eades T., Ellwood M., Emery-Cohen A., Errington H., Evans K.L., Faulkner L., Francis F., Frankland J., Fraser A.E., Galgoczy P., Gilbert J., Gill R., Gloeckner G., Gregory S.G., Gribble S., Griffiths C., Grocock R., Gu Y., Gwilliam R., Hamilton C., Hart E.A., Hawes A., Heath P.D., Heitmann K., Hennig S., Hernandez J., Hinzmann B., Ho S., Hoffs M., Howden P.J., Huckle E.J., Hume J., Hunt P.J., Hunt A.R., Isherwood J., Jacob L., Johnson D., Jones S., de Jong P.J., Joseph S.S., Keenan S., Kelly S., Kershaw J.K., Khan Z., Kioschis P., Klages S., Knights A.J., Kosiura A., Kovar-Smith C., Laird G.K., Langford C., Lawlor S., Leversha M., Lewis L., Liu W., Lloyd C., Lloyd D.M., Loulseged H., Loveland J.E., Lovell J.D., Lozado R., Lu J., Lyne R., Ma J., Maheshwari M., Matthews L.H., McDowall J., McLaren S., McMurray A., Meidl P., Meitinger T., Milne S., Miner G., Mistry S.L., Morgan M., Morris S., Mueller I., Mullikin J.C., Nguyen N., Nordsiek G., Nyakatura G., O'dell C.N., Okwuonu G., Palmer S., Pandian R., Parker D., Parrish J., Pasternak S., Patel D., Pearce A.V., Pearson D.M., Pelan S.E., Perez L., Porter K.M., Ramsey Y., Reichwald K., Rhodes S., Ridler K.A., Schlessinger D., Schueler M.G., Sehra H.K., Shaw-Smith C., Shen H., Sheridan E.M., Shownkeen R., Skuce C.D., Smith M.L., Sotheran E.C., Steingruber H.E., Steward C.A., Storey R., Swann R.M., Swarbreck D., Tabor P.E., Taudien S., Taylor T., Teague B., Thomas K., Thorpe A., Timms K., Tracey A., Trevanion S., Tromans A.C., d'Urso M., Verduzco D., Villasana D., Waldron L., Wall M., Wang Q., Warren J., Warry G.L., Wei X., West A., Whitehead S.L., Whiteley M.N., Wilkinson J.E., Willey D.L., Williams G., Williams L., Williamson A., Williamson H., Wilming L., Woodmansey R.L., Wray P.W., Yen J., Zhang J., Zhou J., Zoghbi H., Zorilla S., Buck D., Reinhardt R., Poustka A., Rosenthal A., Lehrach H., Meindl A., Minx P.J., Hillier L.W., Willard H.F., Wilson R.K., Waterston R.H., Rice C.M., Vaudin M., Coulson A., Nelson D.L., Weinstock G., Sulston J.E., Durbin R.M., Hubbard T., Gibbs R.A., Beck S., Rogers J., Bentley D.R.
Nature 434:325-337(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[8]"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].
Tissue: Brain.
[9]"A gene (PEX) with homologies to endopeptidases is mutated in patients with X-linked hypophosphatemic rickets."
The HYP consortium
Francis F., Hennig S., Korn B., Reinhardt R., de Jong P., Poustka A., Lehrach H., Rowe P.S.N., Goulding J.N., Summerfield T., Mountford R., Read A.P., Popowska E., Pronicka E., Davies K.E., Oriordan J.L.H., Econs M.J., Nesbitt T. expand/collapse author list , Drezner M.K., Oudet C.L., Pannetier S., Hanauer A., Strom T.M., Meindl A., Lorenz B., Cagnoli M., Mohnike K.L., Murken J., Meitinger T.
Nat. Genet. 11:130-136(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 4-641.
[10]"Distribution of mutations in the PEX gene in families with X-linked hypophosphataemic rickets (HYP)."
Rowe P.S.N., Oudet C.L., Francis F., Sinding C., Pannetier S., Econs M.J., Strom T.M., Meitinger T., Garabedian M., David A., Macher M.-A., Questiaux E., Popowska E., Pronicka E., Read A.P., Mokrzycki A., Glorieux F.H., Drezner M.K. expand/collapse author list , Hanauer A., Lehrach H., Goulding J.N., O'Riordan J.L.H.
Hum. Mol. Genet. 6:539-549(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS XLHR SER-77; PRO-138; LEU-534 AND ARG-579.
[11]"A PHEX gene mutation is responsible for adult-onset vitamin D-resistant hypophosphatemic osteomalacia: evidence that the disorder is not a distinct entity from X-linked hypophosphatemic rickets."
Econs M.J., Friedman N.E., Rowe P.S.N., Speer M.C., Francis F., Strom T.M., Oudet C.L., Smith J.A., Ninomiya J.T., Lee B.E., Bergen H.
J. Clin. Endocrinol. Metab. 83:3459-3462(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT XLHR PRO-555.
[12]"Mutational analysis of PHEX gene in X-linked hypophosphatemia."
Dixon P.H., Christie P.T., Wooding C., Trump D., Grieff M., Holm I.A., Gertner J.M., Schmidtke J., Shah B., Shaw N., Smith C., Tau C., Schlessinger D., Whyte M.P., Thakker R.V.
J. Clin. Endocrinol. Metab. 83:3615-3623(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS XLHR PHE-317; LEU-534; ARG-579; ARG-621; ASN-680 DEL; THR-720; TYR-731 AND ARG-749.
[13]"Non-random distribution of mutations in the PHEX gene, and under-detected missense mutations at non-conserved residues."
Filisetti D., Ostermann G., von Bredow M., Strom T.M., Filler G., Ehrich J., Pannetier S., Garnier J.-M., Rowe P.S.N., Francis F., Julienne A., Hanauer A., Econs M.J., Oudet C.L.
Eur. J. Hum. Genet. 7:615-619(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS XLHR SER-80; PHE-142; GLY-237; CYS-530; ASP-573; SER-733 AND TRP-746.
[14]"Identification of fifteen novel PHEX gene mutations in Finnish patients with hypophosphatemic rickets."
Tyynismaa H., Kaitila I., Naentoe-Salonen K., Ala-Houhala M., Alitalo T.
Hum. Mutat. 15:383-384(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS XLHR PHE-85; PRO-141; VAL-341 DEL; PRO-567; LYS-680 AND TYR-693.
[15]"Three novel PHEX gene mutations in Japanese patients with X-linked hypophosphatemic rickets."
Sato K., Tajima T., Nakae J., Adachi M., Asakura Y., Tachibana K., Suwa S., Katsumata N., Tanaka T., Hayashi Y., Abe S., Murashita M., Okuhara K., Shinohara N., Fujieda K.
Pediatr. Res. 48:536-540(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS XLHR ARG-160 AND ASN-444 INS.
+Additional computationally mapped references.

Web resources

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
Y08111 expand/collapse EMBL AC list , Y08112, Y08113, Y08114, Y08115, Y08116, Y08117, Y08118, Y08119, Y08120, Y08121, Y08122, Y08123, Y08124, Y08125, Y08126, Y08127, Y08128, Y08129, Y08130, Y08131, Y08132 Genomic DNA. Translation: CAA69326.1.
U75645 mRNA. Translation: AAB47749.1.
U87284 mRNA. Translation: AAB47562.1.
AD000712 mRNA. Translation: AAB51604.1.
AH004966 Genomic DNA. Translation: AAB42219.1.
U82970 mRNA. Translation: AAC24487.1.
U73024 Genomic DNA. Translation: AAD08630.1.
Y10196 Genomic DNA. Translation: CAA71258.1.
BC105057 mRNA. Translation: AAI05058.1.
BC105059 mRNA. Translation: AAI05060.1.
U60475 mRNA. Translation: AAC50552.1.
RefSeqNP_000435.3. NM_000444.5.
NP_001269683.1. NM_001282754.1.
UniGeneHs.495834.

3D structure databases

ProteinModelPortalP78562.
SMRP78562. Positions 59-749.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid111270. 1 interaction.
IntActP78562. 1 interaction.
STRING9606.ENSP00000368682.

Protein family/group databases

MEROPSM13.091.

PTM databases

PhosphoSiteP78562.

Polymorphism databases

DMDM2499917.

Proteomic databases

PaxDbP78562.
PRIDEP78562.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000379374; ENSP00000368682; ENSG00000102174.
GeneID5251.
KEGGhsa:5251.
UCSCuc004dah.3. human.

Organism-specific databases

CTD5251.
GeneCardsGC0XP021960.
HGNCHGNC:8918. PHEX.
HPAHPA029582.
MIM300550. gene.
307800. phenotype.
neXtProtNX_P78562.
Orphanet89936. X-linked hypophosphatemia.
PharmGKBPA33258.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG3590.
HOGENOMHOG000245574.
HOVERGENHBG005554.
InParanoidP78562.
KOK08636.
OMAKVGYPEF.
OrthoDBEOG7PZRWQ.
PhylomeDBP78562.
TreeFamTF315192.

Gene expression databases

ArrayExpressP78562.
BgeeP78562.
CleanExHS_PHEX.
GenevestigatorP78562.

Family and domain databases

Gene3D3.40.390.10. 2 hits.
InterProIPR024079. MetalloPept_cat_dom.
IPR000718. Peptidase_M13.
IPR018497. Peptidase_M13_C.
IPR008753. Peptidase_M13_N.
IPR015603. PHEX.
[Graphical view]
PANTHERPTHR11733. PTHR11733. 1 hit.
PTHR11733:SF21. PTHR11733:SF21. 1 hit.
PfamPF01431. Peptidase_M13. 1 hit.
PF05649. Peptidase_M13_N. 1 hit.
[Graphical view]
PRINTSPR00786. NEPRILYSIN.
PROSITEPS00142. ZINC_PROTEASE. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSPHEX. human.
GeneWikiPHEX.
GenomeRNAi5251.
NextBio20286.
PROP78562.
SOURCESearch...

Entry information

Entry namePHEX_HUMAN
AccessionPrimary (citable) accession number: P78562
Secondary accession number(s): O00678 expand/collapse secondary AC list , Q13646, Q2M325, Q93032, Q99827
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: May 1, 1997
Last modified: April 16, 2014
This is version 142 of the entry and version 1 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

Peptidase families

Classification of peptidase families and list of entries

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 X

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