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P78562

- PHEX_HUMAN

UniProt

P78562 - PHEX_HUMAN

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Protein
Phosphate-regulating neutral endopeptidase
Gene
PHEX, PEX
Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

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

Cofactori

Binds 1 zinc ion per subunit By similarity.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi580 – 5801Zinc; catalytic By similarity
Active sitei581 – 5811 By similarity
Metal bindingi584 – 5841Zinc; catalytic By similarity
Metal bindingi642 – 6421Zinc; catalytic By similarity
Active sitei646 – 6461Proton donor Reviewed prediction

GO - Molecular functioni

  1. aminopeptidase activity Source: UniProtKB-KW
  2. metalloendopeptidase activity Source: ProtInc
  3. zinc ion binding Source: ProtInc
Complete GO annotation...

GO - Biological processi

  1. bone mineralization Source: Ensembl
  2. cell-cell signaling Source: ProtInc
  3. cellular protein modification process Source: ProtInc
  4. organophosphate metabolic process Source: Ensembl
  5. proteolysis Source: UniProtKB
  6. skeletal system development Source: ProtInc
Complete GO annotation...

Keywords - Molecular functioni

Aminopeptidase, Hydrolase, Metalloprotease, Protease

Keywords - Biological processi

Biomineralization

Keywords - Ligandi

Metal-binding, Zinc

Protein family/group databases

MEROPSiM13.091.

Names & Taxonomyi

Protein namesi
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 namesi
Name:PHEX
Synonyms:PEX
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome X

Organism-specific databases

HGNCiHGNC:8918. PHEX.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 2020Cytoplasmic Reviewed prediction
Add
BLAST
Transmembranei21 – 4121Helical; Signal-anchor for type II membrane protein; Reviewed prediction
Add
BLAST
Topological domaini42 – 641600Extracellular Reviewed prediction
Add
BLAST

GO - Cellular componenti

  1. Golgi apparatus Source: Ensembl
  2. endoplasmic reticulum Source: Ensembl
  3. integral component of plasma membrane Source: ProtInc
  4. perinuclear region of cytoplasm Source: Ensembl
  5. plasma membrane Source: ProtInc
Complete GO annotation...

Keywords - Cellular componenti

Membrane

Pathology & Biotechi

Involvement in diseasei

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.8 Publications
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti77 – 771C → S in XLHR. 1 Publication
VAR_006738
Natural varianti80 – 801F → S in XLHR; sporadic. 1 Publication
VAR_010616
Natural varianti85 – 851C → F in XLHR; sporadic. 1 Publication
VAR_010617
Natural varianti85 – 851C → R in XLHR. 1 Publication
VAR_010618
Natural varianti85 – 851C → Y in XLHR. 1 Publication
VAR_006739
Natural varianti138 – 1381L → P in XLHR. 1 Publication
VAR_006740
Natural varianti141 – 1411S → P in XLHR; sporadic. 1 Publication
VAR_010619
Natural varianti142 – 1421C → F in XLHR. 1 Publication
VAR_010620
Natural varianti160 – 1601L → R in XLHR. 1 Publication
VAR_010621
Natural varianti166 – 1661R → C in XLHR. 1 Publication
VAR_006741
Natural varianti237 – 2371D → G in XLHR; sporadic. 1 Publication
VAR_010622
Natural varianti252 – 2521F → S in XLHR. 1 Publication
VAR_006742
Natural varianti253 – 2531M → I in XLHR. 1 Publication
VAR_006743
Natural varianti317 – 3171Y → F in XLHR. 1 Publication
VAR_010623
Natural varianti341 – 3411Missing in XLHR; sporadic. 1 Publication
VAR_010624
Natural varianti444 – 4441W → WN in XLHR. 1 Publication
VAR_010625
Natural varianti530 – 5301W → C in XLHR. 1 Publication
VAR_010626
Natural varianti534 – 5341P → L in XLHR. 3 Publications
VAR_006744
Natural varianti555 – 5551L → P in XLHR. 1 Publication
VAR_010627
Natural varianti567 – 5671R → P in XLHR; sporadic. 1 Publication
VAR_010628
Natural varianti573 – 5731A → D in XLHR; sporadic. 1 Publication
VAR_010629
Natural varianti579 – 5791G → R in XLHR. 3 Publications
VAR_006745
Natural varianti579 – 5791G → V in XLHR. 1 Publication
VAR_006746
Natural varianti621 – 6211Q → R in XLHR. 1 Publication
VAR_010630
Natural varianti651 – 6511R → P in XLHR. 1 Publication
VAR_010631
Natural varianti680 – 6801N → K in XLHR; sporadic. 1 Publication
VAR_010633
Natural varianti680 – 6801Missing in XLHR. 1 Publication
VAR_010632
Natural varianti693 – 6931C → Y in XLHR; sporadic. 1 Publication
VAR_010634
Natural varianti720 – 7201A → T in XLHR. 1 Publication
VAR_010635
Natural varianti731 – 7311F → Y in XLHR. 1 Publication
VAR_010636
Natural varianti733 – 7331C → S in XLHR; sporadic. 1 Publication
VAR_010637
Natural varianti746 – 7461C → W in XLHR; sporadic. 1 Publication
VAR_010638
Natural varianti749 – 7491W → R in XLHR. 1 Publication
VAR_010639

Keywords - Diseasei

Disease mutation

Organism-specific databases

MIMi307800. phenotype.
Orphaneti89936. X-linked hypophosphatemia.
PharmGKBiPA33258.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 749749Phosphate-regulating neutral endopeptidase
PRO_0000078228Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi71 – 711N-linked (GlcNAc...) Reviewed prediction
Glycosylationi238 – 2381N-linked (GlcNAc...) Reviewed prediction
Glycosylationi263 – 2631N-linked (GlcNAc...) Reviewed prediction
Glycosylationi290 – 2901N-linked (GlcNAc...) Reviewed prediction
Glycosylationi301 – 3011N-linked (GlcNAc...) Reviewed prediction
Glycosylationi377 – 3771N-linked (GlcNAc...) Reviewed prediction
Glycosylationi484 – 4841N-linked (GlcNAc...) Reviewed prediction
Glycosylationi736 – 7361N-linked (GlcNAc...) Reviewed prediction

Keywords - PTMi

Glycoprotein

Proteomic databases

PaxDbiP78562.
PRIDEiP78562.

PTM databases

PhosphoSiteiP78562.

Expressioni

Tissue specificityi

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

Gene expression databases

ArrayExpressiP78562.
BgeeiP78562.
CleanExiHS_PHEX.
GenevestigatoriP78562.

Organism-specific databases

HPAiHPA029582.

Interactioni

Protein-protein interaction databases

BioGridi111270. 1 interaction.
IntActiP78562. 1 interaction.
STRINGi9606.ENSP00000368682.

Structurei

3D structure databases

ProteinModelPortaliP78562.
SMRiP78562. Positions 59-749.

Family & Domainsi

Sequence similaritiesi

Belongs to the peptidase M13 family.

Keywords - Domaini

Signal-anchor, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiCOG3590.
HOGENOMiHOG000245574.
HOVERGENiHBG005554.
InParanoidiP78562.
KOiK08636.
OMAiKVGYPEF.
OrthoDBiEOG7PZRWQ.
PhylomeDBiP78562.
TreeFamiTF315192.

Family and domain databases

Gene3Di3.40.390.10. 2 hits.
InterProiIPR024079. MetalloPept_cat_dom.
IPR000718. Peptidase_M13.
IPR018497. Peptidase_M13_C.
IPR008753. Peptidase_M13_N.
[Graphical view]
PANTHERiPTHR11733. PTHR11733. 1 hit.
PfamiPF01431. Peptidase_M13. 1 hit.
PF05649. Peptidase_M13_N. 1 hit.
[Graphical view]
PRINTSiPR00786. NEPRILYSIN.
PROSITEiPS00142. ZINC_PROTEASE. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P78562-1 [UniParc]FASTAAdd to Basket

« Hide

MEAETGSSVE TGKKANRGTR IALVVFVGGT LVLGTILFLV SQGLLSLQAK    50
QEYCLKPECI EAAAAILSKV NLSVDPCDNF FRFACDGWIS NNPIPEDMPS 100
YGVYPWLRHN VDLKLKELLE KSISRRRDTE AIQKAKILYS SCMNEKAIEK 150
ADAKPLLHIL RHSPFRWPVL ESNIGPEGVW SERKFSLLQT LATFRGQYSN 200
SVFIRLYVSP DDKASNEHIL KLDQATLSLA VREDYLDNST EAKSYRDALY 250
KFMVDTAVLL GANSSRAEHD MKSVLRLEIK IAEIMIPHEN RTSEAMYNKM 300
NISELSAMIP QFDWLGYIKK VIDTRLYPHL KDISPSENVV VRVPQYFKDL 350
FRILGSERKK TIANYLVWRM VYSRIPNLSR RFQYRWLEFS RVIQGTTTLL 400
PQWDKCVNFI ESALPYVVGK MFVDVYFQED KKEMMEELVE GVRWAFIDML 450
EKENEWMDAG TKRKAKEKAR AVLAKVGYPE FIMNDTHVNE DLKAIKFSEA 500
DYFGNVLQTR KYLAQSDFFW LRKAVPKTEW FTNPTTVNAF YSASTNQIRF 550
PAGELQKPFF WGTEYPRSLS YGAIGVIVGH EFTHGFDNNG RKYDKNGNLD 600
PWWSTESEEK FKEKTKCMIN QYSNYYWKKA GLNVKGKRTL GENIADNGGL 650
REAFRAYRKW INDRRQGLEE PLLPGITFTN NQLFFLSYAH VRCNSYRPEA 700
AREQVQIGAH SPPQFRVNGA ISNFEEFQKA FNCPPNSTMN RGMDSCRLW 749
Length:749
Mass (Da):86,474
Last modified:May 1, 1997 - v1
Checksum:i7C4F9F3E2471C6A8
GO

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti77 – 771C → S in XLHR. 1 Publication
VAR_006738
Natural varianti80 – 801F → S in XLHR; sporadic. 1 Publication
VAR_010616
Natural varianti85 – 851C → F in XLHR; sporadic. 1 Publication
VAR_010617
Natural varianti85 – 851C → R in XLHR. 1 Publication
VAR_010618
Natural varianti85 – 851C → Y in XLHR. 1 Publication
VAR_006739
Natural varianti138 – 1381L → P in XLHR. 1 Publication
VAR_006740
Natural varianti141 – 1411S → P in XLHR; sporadic. 1 Publication
VAR_010619
Natural varianti142 – 1421C → F in XLHR. 1 Publication
VAR_010620
Natural varianti160 – 1601L → R in XLHR. 1 Publication
VAR_010621
Natural varianti166 – 1661R → C in XLHR. 1 Publication
VAR_006741
Natural varianti237 – 2371D → G in XLHR; sporadic. 1 Publication
VAR_010622
Natural varianti252 – 2521F → S in XLHR. 1 Publication
VAR_006742
Natural varianti253 – 2531M → I in XLHR. 1 Publication
VAR_006743
Natural varianti317 – 3171Y → F in XLHR. 1 Publication
VAR_010623
Natural varianti341 – 3411Missing in XLHR; sporadic. 1 Publication
VAR_010624
Natural varianti444 – 4441W → WN in XLHR. 1 Publication
VAR_010625
Natural varianti530 – 5301W → C in XLHR. 1 Publication
VAR_010626
Natural varianti534 – 5341P → L in XLHR. 3 Publications
VAR_006744
Natural varianti555 – 5551L → P in XLHR. 1 Publication
VAR_010627
Natural varianti567 – 5671R → P in XLHR; sporadic. 1 Publication
VAR_010628
Natural varianti573 – 5731A → D in XLHR; sporadic. 1 Publication
VAR_010629
Natural varianti579 – 5791G → R in XLHR. 3 Publications
VAR_006745
Natural varianti579 – 5791G → V in XLHR. 1 Publication
VAR_006746
Natural varianti621 – 6211Q → R in XLHR. 1 Publication
VAR_010630
Natural varianti651 – 6511R → P in XLHR. 1 Publication
VAR_010631
Natural varianti680 – 6801N → K in XLHR; sporadic. 1 Publication
VAR_010633
Natural varianti680 – 6801Missing in XLHR. 1 Publication
VAR_010632
Natural varianti693 – 6931C → Y in XLHR; sporadic. 1 Publication
VAR_010634
Natural varianti720 – 7201A → T in XLHR. 1 Publication
VAR_010635
Natural varianti731 – 7311F → Y in XLHR. 1 Publication
VAR_010636
Natural varianti733 – 7331C → S in XLHR; sporadic. 1 Publication
VAR_010637
Natural varianti746 – 7461C → W in XLHR; sporadic. 1 Publication
VAR_010638
Natural varianti749 – 7491W → R in XLHR. 1 Publication
VAR_010639

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti363 – 3631A → D in AAC50552. 1 Publication
Sequence conflicti403 – 4031W → R in AAC50552. 1 Publication
Sequence conflicti641 – 6411G → A in AAC50552. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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.
CCDSiCCDS14204.1.
RefSeqiNP_000435.3. NM_000444.5.
NP_001269683.1. NM_001282754.1.
UniGeneiHs.495834.

Genome annotation databases

EnsembliENST00000379374; ENSP00000368682; ENSG00000102174.
GeneIDi5251.
KEGGihsa:5251.
UCSCiuc004dah.3. human.

Polymorphism databases

DMDMi2499917.

Cross-referencesi

Web resourcesi

PHEXdb

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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 .
CCDSi CCDS14204.1.
RefSeqi NP_000435.3. NM_000444.5.
NP_001269683.1. NM_001282754.1.
UniGenei Hs.495834.

3D structure databases

ProteinModelPortali P78562.
SMRi P78562. Positions 59-749.
ModBasei Search...

Protein-protein interaction databases

BioGridi 111270. 1 interaction.
IntActi P78562. 1 interaction.
STRINGi 9606.ENSP00000368682.

Protein family/group databases

MEROPSi M13.091.

PTM databases

PhosphoSitei P78562.

Polymorphism databases

DMDMi 2499917.

Proteomic databases

PaxDbi P78562.
PRIDEi P78562.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000379374 ; ENSP00000368682 ; ENSG00000102174 .
GeneIDi 5251.
KEGGi hsa:5251.
UCSCi uc004dah.3. human.

Organism-specific databases

CTDi 5251.
GeneCardsi GC0XP021960.
GeneReviewsi PHEX.
HGNCi HGNC:8918. PHEX.
HPAi HPA029582.
MIMi 300550. gene.
307800. phenotype.
neXtProti NX_P78562.
Orphaneti 89936. X-linked hypophosphatemia.
PharmGKBi PA33258.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG3590.
HOGENOMi HOG000245574.
HOVERGENi HBG005554.
InParanoidi P78562.
KOi K08636.
OMAi KVGYPEF.
OrthoDBi EOG7PZRWQ.
PhylomeDBi P78562.
TreeFami TF315192.

Miscellaneous databases

ChiTaRSi PHEX. human.
GeneWikii PHEX.
GenomeRNAii 5251.
NextBioi 20286.
PROi P78562.
SOURCEi Search...

Gene expression databases

ArrayExpressi P78562.
Bgeei P78562.
CleanExi HS_PHEX.
Genevestigatori P78562.

Family and domain databases

Gene3Di 3.40.390.10. 2 hits.
InterProi IPR024079. MetalloPept_cat_dom.
IPR000718. Peptidase_M13.
IPR018497. Peptidase_M13_C.
IPR008753. Peptidase_M13_N.
[Graphical view ]
PANTHERi PTHR11733. PTHR11733. 1 hit.
Pfami PF01431. Peptidase_M13. 1 hit.
PF05649. Peptidase_M13_N. 1 hit.
[Graphical view ]
PRINTSi PR00786. NEPRILYSIN.
PROSITEi PS00142. ZINC_PROTEASE. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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. 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. Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 4-641.
  10. 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. 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. Cited for: VARIANTS XLHR ARG-160 AND ASN-444 INS.

Entry informationi

Entry nameiPHEX_HUMAN
AccessioniPrimary (citable) accession number: P78562
Secondary accession number(s): O00678
, Q13646, Q2M325, Q93032, Q99827
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: May 1, 1997
Last modified: July 9, 2014
This is version 145 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (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.

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Human chromosome X
    Human chromosome X: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. Peptidase families
    Classification of peptidase families and list of entries
  6. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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