true
1999-07-15
2024-01-24
214
PAHX_HUMAN
Identification of PAHX, a Refsum disease gene.
Mihalik S.J.
Morrell J.C.
Kim D.
Sachsteder K.A.
Watkins P.A.
Gould S.J.
doi:10.1038/ng1097-185
1997
Nat. Genet.
17
185-189
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1)
VARIANT RD TRP-275
CHARACTERIZATION OF VARIANT RD TRP-275
FUNCTION
CATALYTIC ACTIVITY
SUBCELLULAR LOCATION
COFACTOR
Refsum disease is caused by mutations in the phytanoyl-CoA hydroxylase gene.
Jansen G.A.
Ofman R.
Ferdinandusse S.
Ijlst L.
Muijsers A.O.
Skjeldal O.H.
Stokke O.
Jakobs C.
Besley G.T.N.
Wraith J.E.
Wanders R.J.A.
doi:10.1038/ng1097-190
1997
Nat. Genet.
17
190-193
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1)
VARIANT RD HIS-269
Immunophilins, Refsum disease, and lupus nephritis: the peroxisomal enzyme phytanoyl-CoA alpha-hydroxylase is a new FKBP-associated protein.
Chambraud B.
Radanyi C.
Camonis J.H.
Rajkowski K.
Schumacher M.
Baulieu E.-E.
doi:10.1073/pnas.96.5.2104
1999
Proc. Natl. Acad. Sci. U.S.A.
96
2104-2109
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1)
INTERACTION WITH FKBP52
Leukemia
Human phytanoyl-CoA hydroxylase: resolution of the gene structure and the molecular basis of Refsum's disease.
Jansen G.A.
Hogenhout E.M.
Ferdinandusse S.
Waterham H.R.
Ofman R.
Jakobs C.
Skjeldal O.H.
Wanders R.J.A.
doi:10.1093/hmg/9.8.1195
2000
Hum. Mol. Genet.
9
1195-1200
NUCLEOTIDE SEQUENCE [GENOMIC DNA]
VARIANTS RD SER-173; LYS-176; GLY-177; ALA-192 INS; ARG-193; GLN-197; PHE-199; SER-204; TYR-220; SER-257; HIS-269; GLN-275 AND TRP-275
VARIANTS SER-29 AND GLN-245
CHARACTERIZATION OF VARIANTS RD GLY-177; SER-204; GLN-275 AND TRP-275
CATALYTIC ACTIVITY
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.
doi:10.1038/nature02462
2004
Nature
429
375-381
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]
The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).
The MGC Project Team
doi:10.1101/gr.2596504
2004
Genome Res.
14
2121-2127
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1)
Brain
Identification of a brain specific protein that associates with a Refsum disease gene product, phytanoyl-CoA alpha-hydroxylase.
Lee Z.H.
Kim H.-H.
Ahn K.Y.
Seo K.H.
Kim J.K.
Bae C.S.
Kim K.K.
doi:10.1016/s0169-328x(99)00304-6
2000
Brain Res. Mol. Brain Res.
75
237-247
INTERACTION WITH PHYHIP
Phytanoyl-CoA hydroxylase: recognition of 3-methyl-branched acyl-coAs and requirement for GTP or ATP and Mg(2+) in addition to its known hydroxylation cofactors.
Croes K.
Foulon V.
Casteels M.
Van Veldhoven P.P.
Mannaerts G.P.
2000
J. Lipid Res.
41
629-636
FUNCTION
CATALYTIC ACTIVITY
COFACTOR
Utilization of sterol carrier protein-2 by phytanoyl-CoA 2-hydroxylase in the peroxisomal alpha oxidation of phytanic acid.
Mukherji M.
Kershaw N.J.
Schofield C.J.
Wierzbicki A.S.
Lloyd M.D.
doi:10.1016/s1074-5521(02)00139-4
2002
Chem. Biol.
9
597-605
FUNCTION
CATALYTIC ACTIVITY
BIOPHYSICOCHEMICAL PROPERTIES
Further studies on the substrate spectrum of phytanoyl-CoA hydroxylase: implications for Refsum disease?
Foulon V.
Asselberghs S.
Geens W.
Mannaerts G.P.
Casteels M.
Van Veldhoven P.P.
doi:10.1194/jlr.m300230-jlr200
2003
J. Lipid Res.
44
2349-2355
FUNCTION
CATALYTIC ACTIVITY
BIOPHYSICOCHEMICAL PROPERTIES
An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome.
Bian Y.
Song C.
Cheng K.
Dong M.
Wang F.
Huang J.
Sun D.
Wang L.
Ye M.
Zou H.
doi:10.1016/j.jprot.2013.11.014
2014
J. Proteomics
96
253-262
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-317
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]
Liver
N-terminome analysis of the human mitochondrial proteome.
Vaca Jacome A.S.
Rabilloud T.
Schaeffer-Reiss C.
Rompais M.
Ayoub D.
Lane L.
Bairoch A.
Van Dorsselaer A.
Carapito C.
doi:10.1002/pmic.201400617
2015
Proteomics
15
2519-2524
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]
Structure of human phytanoyl-CoA 2-hydroxylase identifies molecular mechanisms of Refsum disease.
McDonough M.A.
Kavanagh K.L.
Butler D.
Searls T.
Oppermann U.
Schofield C.J.
doi:10.1074/jbc.m507528200
2005
J. Biol. Chem.
280
41101-41110
X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 31-338 IN COMPLEX WITH IRON AND ALPHA-KETOGLUTARATE
COFACTOR
SUBSTRATE-BINDING SITES
METAL-BINDING SITES
Molecular basis of Refsum disease: sequence variations in phytanoyl-CoA hydroxylase (PHYH) and the PTS2 receptor (PEX7).
Jansen G.A.
Waterham H.R.
Wanders R.J.A.
doi:10.1002/humu.10315
2004
Hum. Mutat.
23
209-218
REVIEW
VARIANTS RD TYR-83 AND ARG-175
Phytanoyl-CoA hydroxylase deficiency. Enzymological and molecular basis of classical Refsum disease.
Jansen G.A.
Ferdinandusse S.
Hogenhout E.M.
Verhoeven N.M.
Jakobs C.
Wanders R.J.A.
1999
Adv. Exp. Med. Biol.
466
371-376
VARIANT RD SER-204
Analysis of protein-coding genetic variation in 60,706 humans.
Lek M.
Karczewski K.J.
Minikel E.V.
Samocha K.E.
Banks E.
Fennell T.
O'Donnell-Luria A.H.
Ware J.S.
Hill A.J.
Cummings B.B.
Tukiainen T.
Birnbaum D.P.
Kosmicki J.A.
Duncan L.E.
Estrada K.
Zhao F.
Zou J.
Pierce-Hoffman E.
Berghout J.
Cooper D.N.
Deflaux N.
DePristo M.
Do R.
Flannick J.
Fromer M.
Gauthier L.
Goldstein J.
Gupta N.
Howrigan D.
Kiezun A.
Kurki M.I.
Moonshine A.L.
Natarajan P.
Orozco L.
Peloso G.M.
Poplin R.
Rivas M.A.
Ruano-Rubio V.
Rose S.A.
Ruderfer D.M.
Shakir K.
Stenson P.D.
Stevens C.
Thomas B.P.
Tiao G.
Tusie-Luna M.T.
Weisburd B.
Won H.H.
Yu D.
Altshuler D.M.
Ardissino D.
Boehnke M.
Danesh J.
Donnelly S.
Elosua R.
Florez J.C.
Gabriel S.B.
Getz G.
Glatt S.J.
Hultman C.M.
Kathiresan S.
Laakso M.
McCarroll S.
McCarthy M.I.
McGovern D.
McPherson R.
Neale B.M.
Palotie A.
Purcell S.M.
Saleheen D.
Scharf J.M.
Sklar P.
Sullivan P.F.
Tuomilehto J.
Tsuang M.T.
Watkins H.C.
Wilson J.G.
Daly M.J.
MacArthur D.G.
Exome Aggregation Consortium
doi:10.1038/nature19057
2016
Nature
536
285-291
VARIANT GLN-245
2.50
A=31-338
25
22
Antihemophilic factor, human recombinant
Ascorbic acid
Lonoctocog alfa
Moroctocog alfa
1 sequenced antibody
482 antibodies from 33 providers
human
PHYH
Tissue enhanced (liver, skeletal muscle, tongue)
phenotype
gene
Refsum disease
Eukaryota
2681
Alpha-oxidation of phytanate
Peroxisomal protein import
TYSND1 cleaves peroxisomal proteins
13 hits in 1162 CRISPR screens
human
Tbio
Protein
Expressed in vastus lateralis and 205 other cell types or tissues
baseline and differential
HS
q2cbj1_9rhob like domain
PhyH
Phytyl_CoA_dOase-like
PHYTANOYL-COA ALPHA-HYDROXYLASE
PHYTANOYL-COA DIOXYGENASE, PEROXISOMAL
PhyH
Clavaminate synthase-like
Phytanoyl-CoA dioxygenase, peroxisomal
1.14.11.18
Phytanic acid oxidase
Phytanoyl-CoA alpha-hydroxylase
PhyH
PHYH
PAHX
Catalyzes the 2-hydroxylation of not only racemic phytanoyl-CoA and the isomers of 3-methylhexadecanoyl-CoA, but also a variety of other mono-branched 3-methylacyl-CoA esters (with a chain length of at least seven carbon atoms) and straight-chain acyl-CoA esters (with a chain length longer than four carbon atoms) (PubMed:9326939, PubMed:10744784, PubMed:12031666, PubMed:12923223). Does not hydroxylate long and very long straight chain acyl-CoAs or 2-methyl- and 4-methyl-branched acyl-CoAs (PubMed:10744784, PubMed:12923223).
40.8 uM for 3-methylhexadecanoyl-CoA
29.5 uM for phytanoyl-CoA (in presence of SCP2)
29.1 uM for hexadecanoyl-CoA (in presence of SCP2)
Interacts with FKBP52 (PubMed:10051602). Interacts with PHYHIP.
Expressed in liver, kidney, and T-cells, but not in spleen, brain, heart, lung and skeletal muscle.
The disease is caused by variants affecting the gene represented in this entry.
Belongs to the PhyH family.
Peroxisome
1
30
Phytanoyl-CoA dioxygenase, peroxisomal
35436
31
338
120
157
175
177
193
264
266
275
N6-succinyllysine
59
N6-succinyllysine
108
N6-succinyllysine
231
N6-succinyllysine
252
Phosphoserine
317
In isoform 2.
100
S
29
In RD.
Y
83
In RD.
S
173
In RD.
R
In RD.
K
176
In RD; total loss of activity.
G
In RD.
AA
192
In RD.
R
In RD.
Q
197
In RD.
F
199
In RD; total loss of activity.
S
204
S
215
In RD.
Y
220
Q
245
In RD.
S
257
In RD.
H
269
In RD; total loss of activity.
Q
In RD; total loss of activity.
W
57
64
65
69
75
89
99
101
104
106
115
117
122
128
135
137
147
149
161
180
186
188
189
206
208
212
214
246
248
255
258
271
273
284
296
301
320
327
329
333
false
3
false
3
false
3
false
3
false
3
false
3
false
3
false
7
false
3
false
3
false
3
false
4
false
3
false
3
false
3
false
3
false
3
false
3
false
3
ABHD17C
ASIC4
CDC23
COPS3
CRLF3
EDRF1
EPHB2
FAM9B
INADL
KLHL20
LHX6
MAGEA11
MALT1
OTUD7B
PIAS1
RNF112
SPMIP4
TRAF5
TRIM74
1998-01-01
1
true
38538
2adeb321a56a9946b74b3f34c3e444a6
1
MEQLRAAARLQIVLGHLGRPSAGAVVAHPTSGTISSASFHPQQFQYTLDNNVLTLEQRKFYEENGFLVIKNLVPDADIQRFRNEFEKICRKEVKPLGLTVMRDVTISKSEYAPSEKMITKVQDFQEDKELFRYCTLPEILKYVECFTGPNIMAMHTMLINKPPDSGKKTSRHPLHQDLHYFPFRPSDLIVCAWTAMEHISRNNGCLVVLPGTHKGSLKPHDYPKWEGGVNKMFHGIQDYEENKARVHLVMEKGDTVFFHPLLIHGSGQNKTQGFRKAISCHFASADCHYIDVKGTSQENIEKEVVGIAHKFFGAENSVNLKDIWMFRARLVKGERTNL
2
MRDVTISKSEYAPSEKMITKVQDFQEDKELFRYCTLPEILKYVECFTGPNIMAMHTMLINKPPDSGKKTSRHPLHQDLHYFPFRPSDLIVCAWTAMEHISRNNGCLVVLPGTHKGSLKPHDYPKWEGGVNKMFHGIQDYEENKARVHLVMEKGDTVFFHPLLIHGSGQNKTQGFRKAISCHFASADCHYIDVKGTSQENIEKEVVGIAHKFFGAENSVNLKDIWMFRARLVKGERTNL
true
true
true
true
true
true
true
true
true
true
true
true
true
true
true
true
true
true
true
true
true
true
true
true