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O14832

- PAHX_HUMAN

UniProt

O14832 - PAHX_HUMAN

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Protein
Phytanoyl-CoA dioxygenase, peroxisomal
Gene
PHYH, PAHX
Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

Converts phytanoyl-CoA to 2-hydroxyphytanoyl-CoA.

Catalytic activityi

Phytanoyl-CoA + 2-oxoglutarate + O2 = 2-hydroxyphytanoyl-CoA + succinate + CO2.

Cofactori

Iron.1 Publication
Ascorbate.1 Publication

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei120 – 1201Alpha-ketoglutarate
Binding sitei157 – 1571Alpha-ketoglutarate
Metal bindingi175 – 1751Iron
Metal bindingi177 – 1771Iron
Binding sitei193 – 1931Alpha-ketoglutarate
Metal bindingi264 – 2641Iron
Binding sitei266 – 2661Alpha-ketoglutarate
Binding sitei275 – 2751Alpha-ketoglutarate

GO - Molecular functioni

  1. L-ascorbic acid binding Source: UniProtKB-KW
  2. cofactor binding Source: UniProtKB
  3. electron carrier activity Source: UniProtKB
  4. metal ion binding Source: UniProtKB-KW
  5. phytanoyl-CoA dioxygenase activity Source: UniProtKB
  6. protein binding Source: UniProtKB

GO - Biological processi

  1. cellular lipid metabolic process Source: Reactome
  2. fatty acid alpha-oxidation Source: UniProtKB
  3. isoprenoid metabolic process Source: UniProtKB
  4. methyl-branched fatty acid metabolic process Source: UniProtKB
  5. small molecule metabolic process Source: Reactome
Complete GO annotation...

Keywords - Molecular functioni

Dioxygenase, Oxidoreductase

Keywords - Ligandi

Iron, Metal-binding, Vitamin C

Enzyme and pathway databases

BioCyciMetaCyc:HS03003-MONOMER.
ReactomeiREACT_17003. Alpha-oxidation of phytanate.
UniPathwayiUPA00199.

Names & Taxonomyi

Protein namesi
Recommended name:
Phytanoyl-CoA dioxygenase, peroxisomal (EC:1.14.11.18)
Alternative name(s):
Phytanic acid oxidase
Phytanoyl-CoA alpha-hydroxylase
Short name:
PhyH
Gene namesi
Name:PHYH
Synonyms:PAHX
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 10

Organism-specific databases

HGNCiHGNC:8940. PHYH.

Subcellular locationi

GO - Cellular componenti

  1. mitochondrion Source: Ensembl
  2. peroxisomal matrix Source: Reactome
  3. peroxisome Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Peroxisome

Pathology & Biotechi

Involvement in diseasei

Refsum disease (RD) [MIM:266500]: A rare autosomal recessive peroxisomal disorder characterized by the accumulation of the branched-chain fatty acid, phytanic acid, in blood and tissues. Cardinal clinical features are retinitis pigmentosa, peripheral neuropathy, cerebellar ataxia, and elevated protein levels in the cerebrospinal fluid (CSF). Half of all patients exhibit generalized, mild to moderate ichthyosis resembling ichthyosis vulgaris. Less constant features are nerve deafness, anosmia, skeletal abnormalities, cataracts and cardiac impairment.
Note: The disease is caused by mutations affecting the gene represented in this entry.4 Publications
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti29 – 291P → S in RD; unknown pathological significance. 1 Publication
Corresponds to variant rs28938169 [ dbSNP | Ensembl ].
VAR_017482
Natural varianti83 – 831N → Y in RD.
VAR_018619
Natural varianti173 – 1731P → S in RD. 1 Publication
VAR_017483
Natural varianti175 – 1751H → R in RD.
VAR_018631
Natural varianti176 – 1761Q → K in RD. 1 Publication
Corresponds to variant rs28939672 [ dbSNP | Ensembl ].
VAR_017484
Natural varianti177 – 1771D → G in RD; total loss of activity. 1 Publication
VAR_017485
Natural varianti192 – 1921A → AA in RD. 1 Publication
VAR_012980
Natural varianti193 – 1931W → R in RD. 1 Publication
VAR_017486
Natural varianti197 – 1971E → Q in RD. 1 Publication
VAR_017487
Natural varianti199 – 1991I → F in RD. 1 Publication
VAR_017488
Natural varianti204 – 2041G → S in RD; total loss of activity. 2 Publications
Corresponds to variant rs28939673 [ dbSNP | Ensembl ].
VAR_017489
Natural varianti220 – 2201H → Y in RD. 1 Publication
VAR_017490
Natural varianti245 – 2451R → Q in RD; partial loss of activity. 1 Publication
Corresponds to variant rs62619919 [ dbSNP | Ensembl ].
VAR_017491
Natural varianti257 – 2571F → S in RD. 1 Publication
VAR_017492
Natural varianti269 – 2691N → H in RD. 2 Publications
VAR_005525
Natural varianti275 – 2751R → Q in RD; total loss of activity. 1 Publication
Corresponds to variant rs28939674 [ dbSNP | Ensembl ].
VAR_017493
Natural varianti275 – 2751R → W in RD; total loss of activity. 2 Publications
Corresponds to variant rs28939671 [ dbSNP | Ensembl ].
VAR_005526

Keywords - Diseasei

Cataract, Deafness, Disease mutation, Ichthyosis, Peroxisome biogenesis disorder, Retinitis pigmentosa

Organism-specific databases

MIMi266500. phenotype.
Orphaneti773. Refsum disease.
PharmGKBiPA33280.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transit peptidei1 – 3030Peroxisome By similarity
Add
BLAST
Chaini31 – 338308Phytanoyl-CoA dioxygenase, peroxisomal
PRO_0000024053Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei59 – 591N6-succinyllysine By similarity
Modified residuei108 – 1081N6-succinyllysine By similarity
Modified residuei231 – 2311N6-succinyllysine By similarity
Modified residuei252 – 2521N6-succinyllysine By similarity

Proteomic databases

MaxQBiO14832.
PaxDbiO14832.
PRIDEiO14832.

PTM databases

PhosphoSiteiO14832.

Expressioni

Tissue specificityi

Expressed in liver, kidney, and T-cells, but not in spleen, brain, heart, lung and skeletal muscle.

Gene expression databases

ArrayExpressiO14832.
BgeeiO14832.
CleanExiHS_PHYH.
GenevestigatoriO14832.

Organism-specific databases

HPAiHPA007598.
HPA011796.

Interactioni

Subunit structurei

Interacts specifically with the immunophilin FKBP52 and PHYHIP.1 Publication

Binary interactionsi

WithEntry#Exp.IntActNotes
COPS3Q9UNS21EBI-721853,EBI-350590
WDR8Q9P2S51EBI-721853,EBI-1054904

Protein-protein interaction databases

BioGridi111282. 10 interactions.
IntActiO14832. 2 interactions.
MINTiMINT-1411634.
STRINGi9606.ENSP00000263038.

Structurei

Secondary structure

Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi57 – 648
Beta strandi65 – 695
Helixi75 – 8915
Beta strandi99 – 1013
Beta strandi104 – 1063
Beta strandi115 – 1173
Beta strandi120 – 1223
Helixi128 – 1358
Helixi137 – 14711
Beta strandi149 – 16113
Helixi177 – 1804
Helixi186 – 1883
Beta strandi189 – 1979
Beta strandi206 – 2083
Helixi212 – 2143
Beta strandi246 – 2483
Beta strandi255 – 2584
Beta strandi264 – 2663
Beta strandi271 – 2733
Beta strandi275 – 28410
Helixi296 – 3016
Helixi320 – 3278
Beta strandi329 – 3335

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2A1XX-ray2.50A31-338[»]
DisProtiDP00327.
ProteinModelPortaliO14832.
SMRiO14832. Positions 44-338.

Miscellaneous databases

EvolutionaryTraceiO14832.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni175 – 1773Alpha-ketoglutarate binding

Sequence similaritiesi

Belongs to the PhyH family.

Keywords - Domaini

Transit peptide

Phylogenomic databases

eggNOGiCOG5285.
HOGENOMiHOG000007341.
HOVERGENiHBG000392.
KOiK00477.
OMAiRKSISCH.
OrthoDBiEOG7NGQC7.
PhylomeDBiO14832.
TreeFamiTF313667.

Family and domain databases

InterProiIPR008775. Phytyl_CoA_dOase.
[Graphical view]
PfamiPF05721. PhyH. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

This entry describes 2 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: O14832-1) [UniParc]FASTAAdd to Basket

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.

« Hide

MEQLRAAARL QIVLGHLGRP SAGAVVAHPT SGTISSASFH PQQFQYTLDN    50
NVLTLEQRKF YEENGFLVIK NLVPDADIQR FRNEFEKICR KEVKPLGLTV 100
MRDVTISKSE YAPSEKMITK VQDFQEDKEL FRYCTLPEIL KYVECFTGPN 150
IMAMHTMLIN KPPDSGKKTS RHPLHQDLHY FPFRPSDLIV CAWTAMEHIS 200
RNNGCLVVLP GTHKGSLKPH DYPKWEGGVN KMFHGIQDYE ENKARVHLVM 250
EKGDTVFFHP LLIHGSGQNK TQGFRKAISC HFASADCHYI DVKGTSQENI 300
EKEVVGIAHK FFGAENSVNL KDIWMFRARL VKGERTNL 338
Length:338
Mass (Da):38,538
Last modified:January 1, 1998 - v1
Checksum:iFBF9639E7C79A6B0
GO
Isoform 2 (identifier: O14832-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-100: Missing.

Note: No experimental confirmation available. Gene prediction based on EST data.

Show »
Length:238
Mass (Da):27,291
Checksum:iBB9006A60F16E0C6
GO

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti29 – 291P → S in RD; unknown pathological significance. 1 Publication
Corresponds to variant rs28938169 [ dbSNP | Ensembl ].
VAR_017482
Natural varianti83 – 831N → Y in RD.
VAR_018619
Natural varianti173 – 1731P → S in RD. 1 Publication
VAR_017483
Natural varianti175 – 1751H → R in RD.
VAR_018631
Natural varianti176 – 1761Q → K in RD. 1 Publication
Corresponds to variant rs28939672 [ dbSNP | Ensembl ].
VAR_017484
Natural varianti177 – 1771D → G in RD; total loss of activity. 1 Publication
VAR_017485
Natural varianti192 – 1921A → AA in RD. 1 Publication
VAR_012980
Natural varianti193 – 1931W → R in RD. 1 Publication
VAR_017486
Natural varianti197 – 1971E → Q in RD. 1 Publication
VAR_017487
Natural varianti199 – 1991I → F in RD. 1 Publication
VAR_017488
Natural varianti204 – 2041G → S in RD; total loss of activity. 2 Publications
Corresponds to variant rs28939673 [ dbSNP | Ensembl ].
VAR_017489
Natural varianti215 – 2151G → S.
Corresponds to variant rs7901902 [ dbSNP | Ensembl ].
VAR_050528
Natural varianti220 – 2201H → Y in RD. 1 Publication
VAR_017490
Natural varianti245 – 2451R → Q in RD; partial loss of activity. 1 Publication
Corresponds to variant rs62619919 [ dbSNP | Ensembl ].
VAR_017491
Natural varianti257 – 2571F → S in RD. 1 Publication
VAR_017492
Natural varianti269 – 2691N → H in RD. 2 Publications
VAR_005525
Natural varianti275 – 2751R → Q in RD; total loss of activity. 1 Publication
Corresponds to variant rs28939674 [ dbSNP | Ensembl ].
VAR_017493
Natural varianti275 – 2751R → W in RD; total loss of activity. 2 Publications
Corresponds to variant rs28939671 [ dbSNP | Ensembl ].
VAR_005526

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 100100Missing in isoform 2.
VSP_046289Add
BLAST

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AF023462 mRNA. Translation: AAB81834.1.
AF112977 mRNA. Translation: AAD20602.1.
AF242386
, AF242379, AF242380, AF242381, AF242382, AF242383, AF242384, AF242385 Genomic DNA. Translation: AAF74123.1.
AL138764 Genomic DNA. Translation: CAI12911.2.
BC029512 mRNA. Translation: AAH29512.1.
CCDSiCCDS41489.1. [O14832-2]
CCDS7097.1. [O14832-1]
RefSeqiNP_001032626.1. NM_001037537.1. [O14832-2]
NP_006205.1. NM_006214.3. [O14832-1]
UniGeneiHs.498732.

Genome annotation databases

EnsembliENST00000263038; ENSP00000263038; ENSG00000107537. [O14832-1]
ENST00000396913; ENSP00000380121; ENSG00000107537. [O14832-2]
GeneIDi5264.
KEGGihsa:5264.
UCSCiuc001ime.3. human. [O14832-1]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AF023462 mRNA. Translation: AAB81834.1 .
AF112977 mRNA. Translation: AAD20602.1 .
AF242386
, AF242379 , AF242380 , AF242381 , AF242382 , AF242383 , AF242384 , AF242385 Genomic DNA. Translation: AAF74123.1 .
AL138764 Genomic DNA. Translation: CAI12911.2 .
BC029512 mRNA. Translation: AAH29512.1 .
CCDSi CCDS41489.1. [O14832-2 ]
CCDS7097.1. [O14832-1 ]
RefSeqi NP_001032626.1. NM_001037537.1. [O14832-2 ]
NP_006205.1. NM_006214.3. [O14832-1 ]
UniGenei Hs.498732.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
2A1X X-ray 2.50 A 31-338 [» ]
DisProti DP00327.
ProteinModelPortali O14832.
SMRi O14832. Positions 44-338.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 111282. 10 interactions.
IntActi O14832. 2 interactions.
MINTi MINT-1411634.
STRINGi 9606.ENSP00000263038.

Chemistry

DrugBanki DB00025. Antihemophilic Factor.
DB00126. Vitamin C.

PTM databases

PhosphoSitei O14832.

Proteomic databases

MaxQBi O14832.
PaxDbi O14832.
PRIDEi O14832.

Protocols and materials databases

DNASUi 5264.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000263038 ; ENSP00000263038 ; ENSG00000107537 . [O14832-1 ]
ENST00000396913 ; ENSP00000380121 ; ENSG00000107537 . [O14832-2 ]
GeneIDi 5264.
KEGGi hsa:5264.
UCSCi uc001ime.3. human. [O14832-1 ]

Organism-specific databases

CTDi 5264.
GeneCardsi GC10M013319.
GeneReviewsi PHYH.
HGNCi HGNC:8940. PHYH.
HPAi HPA007598.
HPA011796.
MIMi 266500. phenotype.
602026. gene.
neXtProti NX_O14832.
Orphaneti 773. Refsum disease.
PharmGKBi PA33280.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG5285.
HOGENOMi HOG000007341.
HOVERGENi HBG000392.
KOi K00477.
OMAi RKSISCH.
OrthoDBi EOG7NGQC7.
PhylomeDBi O14832.
TreeFami TF313667.

Enzyme and pathway databases

UniPathwayi UPA00199 .
BioCyci MetaCyc:HS03003-MONOMER.
Reactomei REACT_17003. Alpha-oxidation of phytanate.

Miscellaneous databases

EvolutionaryTracei O14832.
GenomeRNAii 5264.
NextBioi 20330.
PROi O14832.
SOURCEi Search...

Gene expression databases

ArrayExpressi O14832.
Bgeei O14832.
CleanExi HS_PHYH.
Genevestigatori O14832.

Family and domain databases

InterProi IPR008775. Phytyl_CoA_dOase.
[Graphical view ]
Pfami PF05721. PhyH. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), VARIANT RD TRP-275.
  2. Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), VARIANT RD HIS-269.
  3. "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.
    Proc. Natl. Acad. Sci. U.S.A. 96:2104-2109(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    Tissue: Leukemia.
  4. "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.
    Hum. Mol. Genet. 9:1195-1200(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANTS RD SER-29; SER-173; LYS-176; GLY-177; ALA-192 INS; ARG-193; GLN-197; PHE-199; SER-204; TYR-220; GLN-245; SER-257; HIS-269; GLN-275 AND TRP-275.
  5. "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].
  6. "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] (ISOFORM 1).
    Tissue: Brain.
  7. "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.
    Brain Res. Mol. Brain Res. 75:237-247(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH PHYHIP.
  8. "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.
    J. Biol. Chem. 280:41101-41110(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 31-338 IN COMPLEX WITH IRON AND ALPHA-KETOGLUTARATE, COFACTOR.
  9. "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.
    Hum. Mutat. 23:209-218(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: REVIEW ON VARIANTS RD.
  10. "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.
    Adv. Exp. Med. Biol. 466:371-376(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANT RD SER-204.

Entry informationi

Entry nameiPAHX_HUMAN
AccessioniPrimary (citable) accession number: O14832
Secondary accession number(s): A8MTS8, B1ALH5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 15, 1999
Last sequence update: January 1, 1998
Last modified: September 3, 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

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 10
    Human chromosome 10: 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. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  6. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  7. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi