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Q9NVS9

- PNPO_HUMAN

UniProt

Q9NVS9 - PNPO_HUMAN

Protein

Pyridoxine-5'-phosphate oxidase

Gene

PNPO

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 132 (01 Oct 2014)
      Sequence version 1 (01 Oct 2000)
      Previous versions | rss
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    Functioni

    Catalyzes the oxidation of either pyridoxine 5'-phosphate (PNP) or pyridoxamine 5'-phosphate (PMP) into pyridoxal 5'-phosphate (PLP).1 Publication

    Catalytic activityi

    Pyridoxamine 5'-phosphate + H2O + O2 = pyridoxal 5'-phosphate + NH3 + H2O2.
    Pyridoxine 5'-phosphate + O2 = pyridoxal 5'-phosphate + H2O2.

    Cofactori

    Binds 1 FMN per subunit.

    Pathwayi

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei95 – 951FMN1 Publication
    Binding sitei98 – 981FMN; via amide nitrogen1 Publication
    Binding sitei100 – 1001Substrate
    Binding sitei117 – 1171FMN1 Publication
    Binding sitei157 – 1571Substrate
    Binding sitei161 – 1611Substrate
    Binding sitei165 – 1651Substrate

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi110 – 1112FMN1 Publication
    Nucleotide bindingi174 – 1752FMN1 Publication

    GO - Molecular functioni

    1. FMN binding Source: InterPro
    2. pyridoxamine-phosphate oxidase activity Source: Reactome

    GO - Biological processi

    1. pyridoxine biosynthetic process Source: UniProtKB-KW
    2. small molecule metabolic process Source: Reactome
    3. vitamin B6 metabolic process Source: Reactome
    4. vitamin metabolic process Source: Reactome
    5. water-soluble vitamin metabolic process Source: Reactome

    Keywords - Molecular functioni

    Oxidoreductase

    Keywords - Biological processi

    Pyridoxine biosynthesis

    Keywords - Ligandi

    Flavoprotein, FMN, Pyridoxal phosphate

    Enzyme and pathway databases

    BioCyciMetaCyc:HS03105-MONOMER.
    ReactomeiREACT_25012. Vitamins B6 activation to pyridoxal phosphate.
    SABIO-RKQ9NVS9.
    UniPathwayiUPA00190; UER00304.
    UPA00190; UER00305.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Pyridoxine-5'-phosphate oxidase (EC:1.4.3.5)
    Alternative name(s):
    Pyridoxamine-phosphate oxidase
    Gene namesi
    Name:PNPO
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 17

    Organism-specific databases

    HGNCiHGNC:30260. PNPO.

    Subcellular locationi

    GO - Cellular componenti

    1. cytosol Source: Reactome
    2. extracellular vesicular exosome Source: UniProt

    Pathology & Biotechi

    Involvement in diseasei

    Pyridoxine-5'-phosphate oxidase deficiency (PNPO deficiency) [MIM:610090]: The main feature of neonatal epileptic encephalopathy is the onset within hours of birth of a severe seizure disorder that does not respond to anticonvulsant drugs and can be fatal. Seizures can cease with the administration of PLP, being resistant to treatment with pyridoxine,.1 Publication
    Note: The disease is caused by mutations affecting the gene represented in this entry.
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti229 – 2291R → W in PNPO deficiency; strong activity decrease. 1 Publication
    Corresponds to variant rs104894629 [ dbSNP | Ensembl ].
    VAR_029360

    Keywords - Diseasei

    Disease mutation, Epilepsy

    Organism-specific databases

    MIMi610090. phenotype.
    Orphaneti79096. Pyridoxal phosphate-responsive seizures.
    PharmGKBiPA134915565.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 261261Pyridoxine-5'-phosphate oxidasePRO_0000167783Add
    BLAST

    Proteomic databases

    MaxQBiQ9NVS9.
    PaxDbiQ9NVS9.
    PeptideAtlasiQ9NVS9.
    PRIDEiQ9NVS9.

    2D gel databases

    REPRODUCTION-2DPAGEIPI00018272.

    PTM databases

    PhosphoSiteiQ9NVS9.

    Expressioni

    Gene expression databases

    ArrayExpressiQ9NVS9.
    BgeeiQ9NVS9.
    CleanExiHS_PNPO.
    GenevestigatoriQ9NVS9.

    Organism-specific databases

    HPAiHPA023204.
    HPA027776.

    Interactioni

    Subunit structurei

    Homodimer.1 Publication

    Protein-protein interaction databases

    BioGridi120463. 4 interactions.
    STRINGi9606.ENSP00000225573.

    Structurei

    Secondary structure

    1
    261
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi58 – 7114
    Beta strandi80 – 867
    Beta strandi88 – 903
    Beta strandi92 – 987
    Beta strandi102 – 1054
    Beta strandi106 – 1127
    Helixi116 – 1238
    Beta strandi126 – 1338
    Helixi134 – 1363
    Beta strandi138 – 14811
    Helixi151 – 16010
    Helixi163 – 1719
    Helixi181 – 19414
    Turni195 – 1973
    Beta strandi206 – 2116
    Beta strandi214 – 2207
    Beta strandi228 – 2347
    Beta strandi254 – 2585

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1NRGX-ray1.95A1-261[»]
    3HY8X-ray2.50A1-261[»]
    DisProtiDP00168.
    ProteinModelPortaliQ9NVS9.
    SMRiQ9NVS9. Positions 49-261.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ9NVS9.

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni225 – 2273Substrate binding

    Sequence similaritiesi

    Phylogenomic databases

    eggNOGiCOG0259.
    HOGENOMiHOG000242755.
    HOVERGENiHBG045634.
    InParanoidiQ9NVS9.
    KOiK00275.
    OMAiNMGSRKA.
    PhylomeDBiQ9NVS9.
    TreeFamiTF313411.

    Family and domain databases

    Gene3Di2.30.110.10. 1 hit.
    HAMAPiMF_01629. PdxH.
    InterProiIPR000659. Pyridox_Oxase.
    IPR019740. Pyridox_Oxase_CS.
    IPR011576. Pyridox_Oxase_FMN-bd.
    IPR019576. Pyridoxamine_oxidase_dimer_C.
    IPR012349. Split_barrel_FMN-bd.
    [Graphical view]
    PANTHERiPTHR10851. PTHR10851. 1 hit.
    PfamiPF10590. PNPOx_C. 1 hit.
    PF01243. Pyridox_oxidase. 1 hit.
    [Graphical view]
    PIRSFiPIRSF000190. Pyd_amn-ph_oxd. 1 hit.
    SUPFAMiSSF50475. SSF50475. 1 hit.
    TIGRFAMsiTIGR00558. pdxH. 1 hit.
    PROSITEiPS01064. PYRIDOX_OXIDASE. 1 hit.
    [Graphical view]

    Sequences (4)i

    Sequence statusi: Complete.

    This entry describes 4 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: Q9NVS9-1) [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

    MTCWLRGVTA TFGRPAEWPG YLSHLCGRSA AMDLGPMRKS YRGDREAFEE    50
    THLTSLDPVK QFAAWFEEAV QCPDIGEANA MCLATCTRDG KPSARMLLLK 100
    GFGKDGFRFF TNFESRKGKE LDSNPFASLV FYWEPLNRQV RVEGPVKKLP 150
    EEEAECYFHS RPKSSQIGAV VSHQSSVIPD REYLRKKNEE LEQLYQDQEV 200
    PKPKSWGGYV LYPQVMEFWQ GQTNRLHDRI VFRRGLPTGD SPLGPMTHRG 250
    EEDWLYERLA P 261
    Length:261
    Mass (Da):29,988
    Last modified:October 1, 2000 - v1
    Checksum:i2C74E9F962FE2A95
    GO
    Isoform 2 (identifier: Q9NVS9-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-95: Missing.

    Note: No experimental confirmation available.

    Show »
    Length:166
    Mass (Da):19,478
    Checksum:i81A7843218C16A1D
    GO
    Isoform 3 (identifier: Q9NVS9-3) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         122-139: Missing.

    Note: No experimental confirmation available.

    Show »
    Length:243
    Mass (Da):27,823
    Checksum:i0E1F950A074A37D7
    GO
    Isoform 4 (identifier: Q9NVS9-4) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         140-182: Missing.

    Note: No experimental confirmation available.

    Show »
    Length:218
    Mass (Da):25,200
    Checksum:i710BED8B9D98115F
    GO

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti50 – 501E → K.1 Publication
    VAR_029358
    Natural varianti116 – 1161R → Q.
    Corresponds to variant rs17679445 [ dbSNP | Ensembl ].
    VAR_029359
    Natural varianti229 – 2291R → W in PNPO deficiency; strong activity decrease. 1 Publication
    Corresponds to variant rs104894629 [ dbSNP | Ensembl ].
    VAR_029360

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 9595Missing in isoform 2. 1 PublicationVSP_056409Add
    BLAST
    Alternative sequencei122 – 13918Missing in isoform 3. 1 PublicationVSP_056410Add
    BLAST
    Alternative sequencei140 – 18243Missing in isoform 4. 1 PublicationVSP_056411Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF468030 mRNA. Translation: AAM76918.1.
    AK001397 mRNA. Translation: BAA91668.1.
    AK303536 mRNA. Translation: BAG64562.1.
    AK303665 mRNA. Translation: BAG64664.1.
    AK303792 mRNA. Translation: BAG64749.1.
    CH471109 Genomic DNA. Translation: EAW94770.1.
    CH471109 Genomic DNA. Translation: EAW94771.1.
    BC006525 mRNA. Translation: AAH06525.1.
    CCDSiCCDS11522.1.
    RefSeqiNP_060599.1. NM_018129.3.
    UniGeneiHs.631742.

    Genome annotation databases

    EnsembliENST00000225573; ENSP00000225573; ENSG00000108439.
    ENST00000434554; ENSP00000399960; ENSG00000108439.
    ENST00000534893; ENSP00000437480; ENSG00000108439.
    ENST00000544840; ENSP00000446182; ENSG00000108439.
    GeneIDi55163.
    KEGGihsa:55163.
    UCSCiuc002imo.3. human.

    Polymorphism databases

    DMDMi37082126.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF468030 mRNA. Translation: AAM76918.1 .
    AK001397 mRNA. Translation: BAA91668.1 .
    AK303536 mRNA. Translation: BAG64562.1 .
    AK303665 mRNA. Translation: BAG64664.1 .
    AK303792 mRNA. Translation: BAG64749.1 .
    CH471109 Genomic DNA. Translation: EAW94770.1 .
    CH471109 Genomic DNA. Translation: EAW94771.1 .
    BC006525 mRNA. Translation: AAH06525.1 .
    CCDSi CCDS11522.1.
    RefSeqi NP_060599.1. NM_018129.3.
    UniGenei Hs.631742.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1NRG X-ray 1.95 A 1-261 [» ]
    3HY8 X-ray 2.50 A 1-261 [» ]
    DisProti DP00168.
    ProteinModelPortali Q9NVS9.
    SMRi Q9NVS9. Positions 49-261.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 120463. 4 interactions.
    STRINGi 9606.ENSP00000225573.

    Chemistry

    DrugBanki DB00114. Pyridoxal Phosphate.

    PTM databases

    PhosphoSitei Q9NVS9.

    Polymorphism databases

    DMDMi 37082126.

    2D gel databases

    REPRODUCTION-2DPAGE IPI00018272.

    Proteomic databases

    MaxQBi Q9NVS9.
    PaxDbi Q9NVS9.
    PeptideAtlasi Q9NVS9.
    PRIDEi Q9NVS9.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000225573 ; ENSP00000225573 ; ENSG00000108439 .
    ENST00000434554 ; ENSP00000399960 ; ENSG00000108439 .
    ENST00000534893 ; ENSP00000437480 ; ENSG00000108439 .
    ENST00000544840 ; ENSP00000446182 ; ENSG00000108439 .
    GeneIDi 55163.
    KEGGi hsa:55163.
    UCSCi uc002imo.3. human.

    Organism-specific databases

    CTDi 55163.
    GeneCardsi GC17P046018.
    HGNCi HGNC:30260. PNPO.
    HPAi HPA023204.
    HPA027776.
    MIMi 603287. gene.
    610090. phenotype.
    neXtProti NX_Q9NVS9.
    Orphaneti 79096. Pyridoxal phosphate-responsive seizures.
    PharmGKBi PA134915565.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG0259.
    HOGENOMi HOG000242755.
    HOVERGENi HBG045634.
    InParanoidi Q9NVS9.
    KOi K00275.
    OMAi NMGSRKA.
    PhylomeDBi Q9NVS9.
    TreeFami TF313411.

    Enzyme and pathway databases

    UniPathwayi UPA00190 ; UER00304 .
    UPA00190 ; UER00305 .
    BioCyci MetaCyc:HS03105-MONOMER.
    Reactomei REACT_25012. Vitamins B6 activation to pyridoxal phosphate.
    SABIO-RK Q9NVS9.

    Miscellaneous databases

    ChiTaRSi PNPO. human.
    EvolutionaryTracei Q9NVS9.
    GeneWikii PNPO.
    GenomeRNAii 55163.
    NextBioi 58925.
    PROi Q9NVS9.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q9NVS9.
    Bgeei Q9NVS9.
    CleanExi HS_PNPO.
    Genevestigatori Q9NVS9.

    Family and domain databases

    Gene3Di 2.30.110.10. 1 hit.
    HAMAPi MF_01629. PdxH.
    InterProi IPR000659. Pyridox_Oxase.
    IPR019740. Pyridox_Oxase_CS.
    IPR011576. Pyridox_Oxase_FMN-bd.
    IPR019576. Pyridoxamine_oxidase_dimer_C.
    IPR012349. Split_barrel_FMN-bd.
    [Graphical view ]
    PANTHERi PTHR10851. PTHR10851. 1 hit.
    Pfami PF10590. PNPOx_C. 1 hit.
    PF01243. Pyridox_oxidase. 1 hit.
    [Graphical view ]
    PIRSFi PIRSF000190. Pyd_amn-ph_oxd. 1 hit.
    SUPFAMi SSF50475. SSF50475. 1 hit.
    TIGRFAMsi TIGR00558. pdxH. 1 hit.
    PROSITEi PS01064. PYRIDOX_OXIDASE. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. Kwon O.-S.
      Submitted (JAN-2002) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
      Tissue: Brain.
    2. "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; 2; 3 AND 4).
      Tissue: Liver, Teratocarcinoma, Thymus and Thyroid.
    3. "DNA sequence of human chromosome 17 and analysis of rearrangement in the human lineage."
      Zody M.C., Garber M., Adams D.J., Sharpe T., Harrow J., Lupski J.R., Nicholson C., Searle S.M., Wilming L., Young S.K., Abouelleil A., Allen N.R., Bi W., Bloom T., Borowsky M.L., Bugalter B.E., Butler J., Chang J.L.
      , Chen C.-K., Cook A., Corum B., Cuomo C.A., de Jong P.J., DeCaprio D., Dewar K., FitzGerald M., Gilbert J., Gibson R., Gnerre S., Goldstein S., Grafham D.V., Grocock R., Hafez N., Hagopian D.S., Hart E., Norman C.H., Humphray S., Jaffe D.B., Jones M., Kamal M., Khodiyar V.K., LaButti K., Laird G., Lehoczky J., Liu X., Lokyitsang T., Loveland J., Lui A., Macdonald P., Major J.E., Matthews L., Mauceli E., McCarroll S.A., Mihalev A.H., Mudge J., Nguyen C., Nicol R., O'Leary S.B., Osoegawa K., Schwartz D.C., Shaw-Smith C., Stankiewicz P., Steward C., Swarbreck D., Venkataraman V., Whittaker C.A., Yang X., Zimmer A.R., Bradley A., Hubbard T., Birren B.W., Rogers J., Lander E.S., Nusbaum C.
      Nature 440:1045-1049(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    5. "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: Lymph.
    6. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    7. "Structure and properties of recombinant human pyridoxine 5'-phosphate oxidase."
      Musayev F.N., Di Salvo M.L., Ko T.-P., Schirch V., Safo M.K.
      Protein Sci. 12:1455-1463(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.95 ANGSTROMS) OF 49-161 IN COMPLEX WITH FMN AND PYRIDOXAL 5'-PHOSPHATE, PARTIAL PROTEIN SEQUENCE, SUBUNIT, ENZYME REGULATION, FUNCTION.
    8. "Neonatal epileptic encephalopathy caused by mutations in the PNPO gene encoding pyridox(am)ine 5'-phosphate oxidase."
      Mills P.B., Surtees R.A.H., Champion M.P., Beesley C.E., Dalton N., Scambler P.J., Heales S.J.R., Briddon A., Scheimberg I., Hoffmann G.F., Zschocke J., Clayton P.T.
      Hum. Mol. Genet. 14:1077-1086(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT PNPO DEFICIENCY TRP-229, VARIANT LYS-50.

    Entry informationi

    Entry nameiPNPO_HUMAN
    AccessioniPrimary (citable) accession number: Q9NVS9
    Secondary accession number(s): B4E0V0
    , B4E152, B4E1D7, D3DTT9
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: September 26, 2003
    Last sequence update: October 1, 2000
    Last modified: October 1, 2014
    This is version 132 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, Direct protein sequencing, Reference proteome

    Documents

    1. Human chromosome 17
      Human chromosome 17: 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