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Q9UHG3

- PCYOX_HUMAN

UniProt

Q9UHG3 - PCYOX_HUMAN

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Protein

Prenylcysteine oxidase 1

Gene
PCYOX1, KIAA0908, PCL1, UNQ597/PRO1183
Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

Involved in the degradation of prenylated proteins. Cleaves the thioether bond of prenyl-L-cysteines, such as farnesylcysteine and geranylgeranylcysteine.

Catalytic activityi

An S-prenyl-L-cysteine + O2 + H2O = a prenal + L-cysteine + H2O2.

Cofactori

FAD.

GO - Molecular functioni

  1. chloride-transporting ATPase activity Source: Ensembl
  2. prenylcysteine oxidase activity Source: BHF-UCL

GO - Biological processi

  1. prenylated protein catabolic process Source: UniProtKB
  2. prenylcysteine catabolic process Source: Ensembl
  3. prenylcysteine metabolic process Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Ligandi

FAD, Flavoprotein

Names & Taxonomyi

Protein namesi
Recommended name:
Prenylcysteine oxidase 1 (EC:1.8.3.5)
Alternative name(s):
Prenylcysteine lyase
Gene namesi
Name:PCYOX1
Synonyms:KIAA0908, PCL1
ORF Names:UNQ597/PRO1183
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 2

Organism-specific databases

HGNCiHGNC:20588. PCYOX1.

Subcellular locationi

GO - Cellular componenti

  1. extracellular vesicular exosome Source: UniProt
  2. lysosome Source: BHF-UCL
  3. plasma membrane Source: Ensembl
  4. very-low-density lipoprotein particle Source: BHF-UCL
Complete GO annotation...

Keywords - Cellular componenti

Lysosome

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA134959852.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2727 Reviewed predictionAdd
BLAST
Chaini28 – 505478Prenylcysteine oxidase 1PRO_0000023298Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Cross-linki162 – 162Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)1 Publication
Glycosylationi196 – 1961N-linked (GlcNAc...)2 Publications
Glycosylationi323 – 3231N-linked (GlcNAc...)1 Publication
Glycosylationi353 – 3531N-linked (GlcNAc...)2 Publications

Post-translational modificationi

The protein is glycosylated at one or more potential N-glycosylation sites.

Keywords - PTMi

Glycoprotein, Isopeptide bond, Ubl conjugation

Proteomic databases

MaxQBiQ9UHG3.
PaxDbiQ9UHG3.
PeptideAtlasiQ9UHG3.
PRIDEiQ9UHG3.

PTM databases

PhosphoSiteiQ9UHG3.

Expressioni

Tissue specificityi

Ubiquitous.

Gene expression databases

ArrayExpressiQ9UHG3.
BgeeiQ9UHG3.
CleanExiHS_PCYOX1.
GenevestigatoriQ9UHG3.

Organism-specific databases

HPAiHPA035193.

Interactioni

Protein-protein interaction databases

BioGridi119547. 4 interactions.
IntActiQ9UHG3. 2 interactions.
STRINGi9606.ENSP00000387654.

Structurei

3D structure databases

ProteinModelPortaliQ9UHG3.
SMRiQ9UHG3. Positions 35-110.

Family & Domainsi

Sequence similaritiesi

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiNOG73316.
HOGENOMiHOG000241149.
HOVERGENiHBG053532.
InParanoidiQ9UHG3.
KOiK05906.
OMAiNGIECAA.
PhylomeDBiQ9UHG3.
TreeFamiTF329001.

Family and domain databases

InterProiIPR010795. Prenylcys_lyase.
IPR017046. Prenylcysteine_Oxase.
[Graphical view]
PfamiPF07156. Prenylcys_lyase. 1 hit.
[Graphical view]
PIRSFiPIRSF036292. Prenylcysteine_oxidase. 1 hit.

Sequencei

Sequence statusi: Complete.

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

Q9UHG3-1 [UniParc]FASTAAdd to Basket

« Hide

MGRVVAELVS SLLGLWLLLC SCGCPEGAEL RAPPDKIAII GAGIGGTSAA    50
YYLRQKFGKD VKIDLFEREE VGGRLATMMV QGQEYEAGGS VIHPLNLHMK 100
RFVKDLGLSA VQASGGLLGI YNGETLVFEE SNWFIINVIK LVWRYGFQSL 150
RMHMWVEDVL DKFMRIYRYQ SHDYAFSSVE KLLHALGGDD FLGMLNRTLL 200
ETLQKAGFSE KFLNEMIAPV MRVNYGQSTD INAFVGAVSL SCSDSGLWAV 250
EGGNKLVCSG LLQASKSNLI SGSVMYIEEK TKTKYTGNPT KMYEVVYQIG 300
TETRSDFYDI VLVATPLNRK MSNITFLNFD PPIEEFHQYY QHIVTTLVKG 350
ELNTSIFSSR PIDKFGLNTV LTTDNSDLFI NSIGIVPSVR EKEDPEPSTD 400
GTYVWKIFSQ ETLTKAQILK LFLSYDYAVK KPWLAYPHYK PPEKCPSIIL 450
HDRLYYLNGI ECAASAMEMS AIAAHNAALL AYHRWNGHTD MIDQDGLYEK 500
LKTEL 505
Length:505
Mass (Da):56,640
Last modified:September 19, 2006 - v3
Checksum:iFB388AF70AF229F5
GO

Sequence cautioni

The sequence BAA74931.1 differs from that shown. Reason: Erroneous initiation.

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti149 – 1491S → F.1 Publication
Corresponds to variant rs2706762 [ dbSNP | Ensembl ].
VAR_050469
Natural varianti414 – 4141T → S.
Corresponds to variant rs17005441 [ dbSNP | Ensembl ].
VAR_050470
Natural varianti465 – 4651S → G.
Corresponds to variant rs34041544 [ dbSNP | Ensembl ].
VAR_050471

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti341 – 3411Q → H in AAF16937. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AF181490 mRNA. Translation: AAF16937.1.
AB020715 mRNA. Translation: BAA74931.1. Different initiation.
AY359063 mRNA. Translation: AAQ89422.1.
AK314453 mRNA. Translation: BAG37061.1.
CH471053 Genomic DNA. Translation: EAW99819.1.
BC007029 mRNA. Translation: AAH07029.1.
BC033815 mRNA. Translation: AAH33815.1.
BC051891 mRNA. Translation: AAH51891.1.
CCDSiCCDS1902.1.
RefSeqiNP_057381.3. NM_016297.3.
UniGeneiHs.567502.

Genome annotation databases

EnsembliENST00000433351; ENSP00000387654; ENSG00000116005.
GeneIDi51449.
KEGGihsa:51449.
UCSCiuc002sgn.4. human.

Polymorphism databases

DMDMi115311617.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AF181490 mRNA. Translation: AAF16937.1 .
AB020715 mRNA. Translation: BAA74931.1 . Different initiation.
AY359063 mRNA. Translation: AAQ89422.1 .
AK314453 mRNA. Translation: BAG37061.1 .
CH471053 Genomic DNA. Translation: EAW99819.1 .
BC007029 mRNA. Translation: AAH07029.1 .
BC033815 mRNA. Translation: AAH33815.1 .
BC051891 mRNA. Translation: AAH51891.1 .
CCDSi CCDS1902.1.
RefSeqi NP_057381.3. NM_016297.3.
UniGenei Hs.567502.

3D structure databases

ProteinModelPortali Q9UHG3.
SMRi Q9UHG3. Positions 35-110.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 119547. 4 interactions.
IntActi Q9UHG3. 2 interactions.
STRINGi 9606.ENSP00000387654.

PTM databases

PhosphoSitei Q9UHG3.

Polymorphism databases

DMDMi 115311617.

Proteomic databases

MaxQBi Q9UHG3.
PaxDbi Q9UHG3.
PeptideAtlasi Q9UHG3.
PRIDEi Q9UHG3.

Protocols and materials databases

DNASUi 51449.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000433351 ; ENSP00000387654 ; ENSG00000116005 .
GeneIDi 51449.
KEGGi hsa:51449.
UCSCi uc002sgn.4. human.

Organism-specific databases

CTDi 51449.
GeneCardsi GC02P070484.
HGNCi HGNC:20588. PCYOX1.
HPAi HPA035193.
MIMi 610995. gene.
neXtProti NX_Q9UHG3.
PharmGKBi PA134959852.
HUGEi Search...
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG73316.
HOGENOMi HOG000241149.
HOVERGENi HBG053532.
InParanoidi Q9UHG3.
KOi K05906.
OMAi NGIECAA.
PhylomeDBi Q9UHG3.
TreeFami TF329001.

Miscellaneous databases

ChiTaRSi PCYOX1. human.
GeneWikii PCYOX1.
GenomeRNAii 51449.
NextBioi 55051.
PROi Q9UHG3.
SOURCEi Search...

Gene expression databases

ArrayExpressi Q9UHG3.
Bgeei Q9UHG3.
CleanExi HS_PCYOX1.
Genevestigatori Q9UHG3.

Family and domain databases

InterProi IPR010795. Prenylcys_lyase.
IPR017046. Prenylcysteine_Oxase.
[Graphical view ]
Pfami PF07156. Prenylcys_lyase. 1 hit.
[Graphical view ]
PIRSFi PIRSF036292. Prenylcysteine_oxidase. 1 hit.
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Cloning, expression, and cellular localization of a human prenylcysteine lyase."
    Tschantz W.R., Zhang L., Casey P.J.
    J. Biol. Chem. 274:35802-35808(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Tissue: Brain.
  2. "Prediction of the coding sequences of unidentified human genes. XII. The complete sequences of 100 new cDNA clones from brain which code for large proteins in vitro."
    Nagase T., Ishikawa K., Suyama M., Kikuno R., Hirosawa M., Miyajima N., Tanaka A., Kotani H., Nomura N., Ohara O.
    DNA Res. 5:355-364(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], VARIANT PHE-149.
    Tissue: Brain.
  3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
  4. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
    Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
    , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
    Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Placenta.
  5. 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].
    Tissue: Heart and Lung.
  7. Bienvenut W.V.
    Submitted (JUN-2005) to UniProtKB
    Cited for: PROTEIN SEQUENCE OF 37-54; 256-266 AND 421-430, IDENTIFICATION BY MASS SPECTROMETRY.
    Tissue: B-cell lymphoma.
  8. "Human plasma N-glycoproteome analysis by immunoaffinity subtraction, hydrazide chemistry, and mass spectrometry."
    Liu T., Qian W.-J., Gritsenko M.A., Camp D.G. II, Monroe M.E., Moore R.J., Smith R.D.
    J. Proteome Res. 4:2070-2080(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-196; ASN-323 AND ASN-353.
    Tissue: Plasma.
  9. "Tryptic digestion of ubiquitin standards reveals an improved strategy for identifying ubiquitinated proteins by mass spectrometry."
    Denis N.J., Vasilescu J., Lambert J.-P., Smith J.C., Figeys D.
    Proteomics 7:868-874(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: UBIQUITINATION [LARGE SCALE ANALYSIS] AT LYS-162.
    Tissue: Mammary cancer.
  10. "Glycoproteomics analysis of human liver tissue by combination of multiple enzyme digestion and hydrazide chemistry."
    Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.
    J. Proteome Res. 8:651-661(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-196 AND ASN-353.
    Tissue: Liver.
  11. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiPCYOX_HUMAN
AccessioniPrimary (citable) accession number: Q9UHG3
Secondary accession number(s): B2RB14
, O94982, Q8N4N5, Q96QM8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 1, 2000
Last sequence update: September 19, 2006
Last modified: July 9, 2014
This is version 132 of the entry and version 3 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

Caution

Was originally (1 Publication) thought to be a lyase and was therefore termed prenylcysteine lyase.

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 2
    Human chromosome 2: 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. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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