P78562 (PHEX_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended 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

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	749 AA.
Sequence status	Complete.
Protein existence	Evidence 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 process	Biomineralization
Cellular component	Membrane
Disease	Disease mutation
Domain	Signal-anchor Transmembrane Transmembrane helix
Ligand	Metal-binding Zinc
Molecular function	Aminopeptidase Hydrolase Metalloprotease Protease
PTM	Glycoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	bone mineralization Inferred from electronic annotation. Source: Compara 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: Compara proteolysis Inferred from direct assay PubMed 11409890. Source: UniProtKB skeletal system development Traceable author statement Ref.4. Source: ProtInc
Cellular_component	Golgi apparatus Inferred from electronic annotation. Source: Compara endoplasmic reticulum Inferred from electronic annotation. Source: Compara integral to plasma membrane Traceable author statement PubMed 9593714. Source: ProtInc perinuclear region of cytoplasm Inferred from electronic annotation. Source: Compara
Molecular_function	aminopeptidase 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 key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 749	749	Phosphate-regulating neutral endopeptidase		PRO_0000078228
Regions
	Topological domain	1 – 20	20	Cytoplasmic Potential
	Transmembrane	21 – 41	21	Helical; Signal-anchor for type II membrane protein; Potential
	Topological domain	42 – 641	600	Extracellular Potential
Sites
	Active site	581	1	By similarity
	Active site	646	1	Proton donor Potential
	Metal binding	580	1	Zinc; catalytic By similarity
	Metal binding	584	1	Zinc; catalytic By similarity
	Metal binding	642	1	Zinc; catalytic By similarity
Amino acid modifications
	Glycosylation	71	1	N-linked (GlcNAc...) Potential
	Glycosylation	238	1	N-linked (GlcNAc...) Potential
	Glycosylation	263	1	N-linked (GlcNAc...) Potential
	Glycosylation	290	1	N-linked (GlcNAc...) Potential
	Glycosylation	301	1	N-linked (GlcNAc...) Potential
	Glycosylation	377	1	N-linked (GlcNAc...) Potential
	Glycosylation	484	1	N-linked (GlcNAc...) Potential
	Glycosylation	736	1	N-linked (GlcNAc...) Potential
Natural variations
	Natural variant	77	1	C → S in XLHR. Ref.10		VAR_006738
	Natural variant	80	1	F → S in XLHR; sporadic. Ref.13		VAR_010616
	Natural variant	85	1	C → F in XLHR; sporadic. Ref.14		VAR_010617
	Natural variant	85	1	C → R in XLHR. Ref.1		VAR_010618
	Natural variant	85	1	C → Y in XLHR. Ref.5		VAR_006739
	Natural variant	138	1	L → P in XLHR. Ref.10		VAR_006740
	Natural variant	141	1	S → P in XLHR; sporadic. Ref.14		VAR_010619
	Natural variant	142	1	C → F in XLHR. Ref.13		VAR_010620
	Natural variant	160	1	L → R in XLHR. Ref.15		VAR_010621
	Natural variant	166	1	R → C in XLHR. Ref.5		VAR_006741
	Natural variant	237	1	D → G in XLHR; sporadic. Ref.13		VAR_010622
	Natural variant	252	1	F → S in XLHR. Ref.5		VAR_006742
	Natural variant	253	1	M → I in XLHR. Ref.5		VAR_006743
	Natural variant	317	1	Y → F in XLHR. Ref.12		VAR_010623
	Natural variant	341	1	Missing in XLHR; sporadic. Ref.14		VAR_010624
	Natural variant	444	1	W → WN in XLHR. Ref.15		VAR_010625
	Natural variant	530	1	W → C in XLHR. Ref.13		VAR_010626
	Natural variant	534	1	P → L in XLHR. Ref.1 Ref.10 Ref.12		VAR_006744
	Natural variant	555	1	L → P in XLHR. Ref.11		VAR_010627
	Natural variant	567	1	R → P in XLHR; sporadic. Ref.14		VAR_010628
	Natural variant	573	1	A → D in XLHR; sporadic. Ref.13		VAR_010629
	Natural variant	579	1	G → R in XLHR. Ref.1 Ref.10 Ref.12		VAR_006745
	Natural variant	579	1	G → V in XLHR. Ref.5		VAR_006746
	Natural variant	621	1	Q → R in XLHR. Ref.12		VAR_010630
	Natural variant	651	1	R → P in XLHR. Ref.1		VAR_010631
	Natural variant	680	1	N → K in XLHR; sporadic. Ref.14		VAR_010633
	Natural variant	680	1	Missing in XLHR. Ref.12		VAR_010632
	Natural variant	693	1	C → Y in XLHR; sporadic. Ref.14		VAR_010634
	Natural variant	720	1	A → T in XLHR. Ref.12		VAR_010635
	Natural variant	731	1	F → Y in XLHR. Ref.12		VAR_010636
	Natural variant	733	1	C → S in XLHR; sporadic. Ref.13		VAR_010637
	Natural variant	746	1	C → W in XLHR; sporadic. Ref.13		VAR_010638
	Natural variant	749	1	W → R in XLHR. Ref.12		VAR_010639
Experimental info
	Sequence conflict	363	1	A → D in AAC50552. Ref.9
	Sequence conflict	403	1	W → R in AAC50552. Ref.9
	Sequence conflict	641	1	G → A in AAC50552. Ref.9

Sequences

	Sequence		Length	Mass (Da)
	P78562 [UniParc]. Last modified May 1, 1997. Version 1. Checksum: 7C4F9F3E2471C6A8	FASTA	749	86,474
	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

References

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

PHEXdb

GeneReviews

Cross-references

Sequence databases
EMBL GenBank DDBJ	Y08111 , 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.
IPI	IPI00020366.
RefSeq	NP_000435.3. NM_000444.4.
UniGene	Hs.495834.
3D structure databases
ProteinModelPortal	P78562.
ModBase	Search...
Protein-protein interaction databases
IntAct	P78562. 1 interaction.
STRING	9606.ENSP00000368682.
Protein family/group databases
MEROPS	M13.091.
PTM databases
PhosphoSite	P78562.
Polymorphism databases
DMDM	2499917.
Proteomic databases
PaxDb	P78562.
PRIDE	P78562.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000379374; ENSP00000368682; ENSG00000102174.
GeneID	5251.
KEGG	hsa:5251.
UCSC	uc004dah.3. human.
Organism-specific databases
CTD	5251.
GeneCards	GC0XP021960.
HGNC	HGNC:8918. PHEX.
HPA	HPA029582.
MIM	300550. gene. 307800. phenotype.
neXtProt	NX_P78562.
Orphanet	89936. X-linked hypophosphatemia.
PharmGKB	PA33258.
GenAtlas	Search...
Phylogenomic databases
eggNOG	COG3590.
HOGENOM	HOG000245574.
HOVERGEN	HBG005554.
InParanoid	P78562.
KO	K08636.
OMA	YSASTNQ.
OrthoDB	EOG4STS43.
PhylomeDB	P78562.
Gene expression databases
ArrayExpress	P78562.
Bgee	P78562.
CleanEx	HS_PHEX.
Genevestigator	P78562.
GermOnline	ENSG00000102174. Homo sapiens.
Family and domain databases
Gene3D	3.40.390.10. 2 hits.
InterPro	IPR024079. MetalloPept_cat_dom. IPR000718. Peptidase_M13. IPR018497. Peptidase_M13_C. IPR008753. Peptidase_M13_N. IPR015603. PHEX. [Graphical view]
PANTHER	PTHR11733. PTHR11733. 1 hit. PTHR11733:SF21. PTHR11733:SF21. 1 hit.
Pfam	PF01431. Peptidase_M13. 1 hit. PF05649. Peptidase_M13_N. 1 hit. [Graphical view]
PRINTS	PR00786. NEPRILYSIN.
PROSITE	PS00142. ZINC_PROTEASE. 1 hit. [Graphical view]
ProtoNet	Search...
Other
ChiTaRS	PHEX. human.
GenomeRNAi	5251.
NextBio	20286.
SOURCE	Search...

Entry information

Entry name

PHEX_HUMAN

Accession

Primary (citable) accession number: P78562
Secondary accession number(s): O00678 , Q13646, Q2M325, Q93032, Q99827

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1997
Last sequence update:	May 1, 1997
Last modified:	May 1, 2013
This is version 135 of the entry and version 1 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.