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Q9UHG3

- PCYOX_HUMAN

UniProt

Q9UHG3 - PCYOX_HUMAN

Protein

Prenylcysteine oxidase 1

Gene

PCYOX1

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 133 (01 Oct 2014)
      Sequence version 3 (19 Sep 2006)
      Previous versions | rss
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    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

    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

    Keywords - Cellular componenti

    Lysosome

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA134959852.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 2727Sequence AnalysisAdd
    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.2 Publications

    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.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the prenylcysteine oxidase family.Curated

    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.

    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: Q9UHG3-1) [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

    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
    Isoform 2 (identifier: Q9UHG3-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-77: Missing.

    Note: No experimental confirmation available.

    Show »
    Length:428
    Mass (Da):48,507
    Checksum:i353962C00F7703DC
    GO

    Sequence cautioni

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

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti341 – 3411Q → H in AAF16937. (PubMed:10585463)Curated

    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

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 7777Missing in isoform 2. 1 PublicationVSP_056701Add
    BLAST

    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.
    AK316013 mRNA. Translation: BAH14384.1.
    AC016700 Genomic DNA. No translation available.
    AC079338 Genomic DNA. No translation available.
    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.
    ENST00000505044; ENSP00000441566; ENSG00000116005.
    GeneIDi51449.
    KEGGihsa:51449.
    UCSCiuc002sgn.4. human.

    Polymorphism databases

    DMDMi115311617.

    Keywords - Coding sequence diversityi

    Alternative splicing, 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 .
    AK316013 mRNA. Translation: BAH14384.1 .
    AC016700 Genomic DNA. No translation available.
    AC079338 Genomic DNA. No translation available.
    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 .
    ENST00000505044 ; ENSP00000441566 ; 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

    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] (ISOFORM 1).
      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] (ISOFORM 1), VARIANT PHE-149.
      Tissue: Brain.
    3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    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] (ISOFORMS 1 AND 2).
      Tissue: Brain and Placenta.
    5. "Generation and annotation of the DNA sequences of human chromosomes 2 and 4."
      Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L., Du H.
      , Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K., McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C., Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S., Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H., Wilson R.K.
      Nature 434:724-731(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    6. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    7. "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: Heart and Lung.
    8. 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.
    9. "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.
    10. "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.
    11. "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.
    12. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

    Entry informationi

    Entry nameiPCYOX_HUMAN
    AccessioniPrimary (citable) accession number: Q9UHG3
    Secondary accession number(s): B2RB14
    , B7Z9P8, O94982, Q8N4N5, Q96QM8
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: December 1, 2000
    Last sequence update: September 19, 2006
    Last modified: October 1, 2014
    This is version 133 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

    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