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P40855

- PEX19_HUMAN

UniProt

P40855 - PEX19_HUMAN

Protein

Peroxisomal biogenesis factor 19

Gene

PEX19

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 149 (01 Oct 2014)
      Sequence version 1 (01 Feb 1995)
      Previous versions | rss
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    Functioni

    Necessary for early peroxisomal biogenesis. Acts both as a cytosolic chaperone and as an import receptor for peroxisomal membrane proteins (PMPs). Binds and stabilizes newly synthesized PMPs in the cytoplasm by interacting with their hydrophobic membrane-spanning domains, and targets them to the peroxisome membrane by binding to the integral membrane protein PEX3. Excludes CDKN2A from the nucleus and prevents its interaction with MDM2, which results in active degradation of TP53.6 Publications

    GO - Molecular functioni

    1. ATPase binding Source: UniProtKB
    2. peroxisome membrane class-1 targeting sequence binding Source: UniProtKB
    3. protein binding Source: UniProtKB
    4. protein N-terminus binding Source: UniProtKB

    GO - Biological processi

    1. chaperone-mediated protein folding Source: UniProtKB
    2. chaperone-mediated protein transport Source: UniProtKB
    3. establishment of protein localization to peroxisome Source: UniProtKB
    4. negative regulation of lipid binding Source: UniProtKB
    5. peroxisome fission Source: UniProtKB
    6. peroxisome membrane biogenesis Source: UniProtKB
    7. peroxisome organization Source: UniProtKB
    8. protein import into peroxisome membrane Source: UniProtKB
    9. protein stabilization Source: UniProtKB
    10. protein targeting to peroxisome Source: UniProtKB
    11. transmembrane transport Source: Reactome

    Keywords - Biological processi

    Peroxisome biogenesis

    Enzyme and pathway databases

    ReactomeiREACT_111158. ABCA transporters in lipid homeostasis.

    Protein family/group databases

    TCDBi9.A.17.1.2. the integral membrane peroxisomal protein importer-2 (ppi2) family.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Peroxisomal biogenesis factor 19
    Alternative name(s):
    33 kDa housekeeping protein
    Peroxin-19
    Peroxisomal farnesylated protein
    Gene namesi
    Name:PEX19
    Synonyms:HK33, PXF
    ORF Names:OK/SW-cl.22
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 1

    Organism-specific databases

    HGNCiHGNC:9713. PEX19.

    Subcellular locationi

    Cytoplasm. Peroxisome membrane; Lipid-anchor; Cytoplasmic side
    Note: Mainly cytoplasmic. Some fraction membrane-associated to the outer surface of peroxisomes.

    GO - Cellular componenti

    1. brush border membrane Source: UniProtKB
    2. cytoplasm Source: UniProtKB
    3. cytosol Source: UniProtKB
    4. integral component of membrane Source: UniProtKB
    5. intracellular membrane-bounded organelle Source: HPA
    6. nucleus Source: HPA
    7. peroxisomal membrane Source: UniProtKB
    8. peroxisome Source: UniProtKB
    9. protein complex Source: UniProtKB

    Keywords - Cellular componenti

    Cytoplasm, Membrane, Peroxisome

    Pathology & Biotechi

    Involvement in diseasei

    Peroxisome biogenesis disorder complementation group 14 (PBD-CG14) [MIM:614886]: A peroxisomal disorder arising from a failure of protein import into the peroxisomal membrane or matrix. The peroxisome biogenesis disorders (PBD group) are genetically heterogeneous with at least 14 distinct genetic groups as concluded from complementation studies. Include disorders are: Zellweger syndrome (ZWS), neonatal adrenoleukodystrophy (NALD), infantile Refsum disease (IRD), and classical rhizomelic chondrodysplasia punctata (RCDP). ZWS, NALD and IRD are distinct from RCDP and constitute a clinical continuum of overlapping phenotypes known as the Zellweger spectrum (PBD-ZSS).1 Publication
    Note: The disease is caused by mutations affecting the gene represented in this entry.
    Peroxisome biogenesis disorder 12A (PBD12A) [MIM:614886]: A fatal peroxisome biogenesis disorder belonging to the Zellweger disease spectrum and clinically characterized by severe neurologic dysfunction with profound psychomotor retardation, severe hypotonia and neonatal seizures, craniofacial abnormalities, liver dysfunction, and biochemically by the absence of peroxisomes. Additional features include cardiovascular and skeletal defects, renal cysts, ocular abnormalities, and hearing impairment. Most severely affected individuals with the classic form of the disease (classic Zellweger syndrome) die within the first year of life.1 Publication
    Note: The disease is caused by mutations affecting the gene represented in this entry.

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi29 – 291F → A: Abolishes binding to PEX3. 2 Publications
    Mutagenesisi296 – 2994Missing: Abolishes binding to PEX10, PEX11B, PEX12 and PEX13. Does not affect binding to PEX3 and PEX16. 5 Publications
    Mutagenesisi296 – 2961C → A: Slightly inhibits PEX19 function on peroxisome biogenesis. 5 Publications
    Mutagenesisi296 – 2961C → S: Abolishes farnesylation. Abolishes PEX19 function on peroxisome biogenesis. Does not affect binding to ABCD1, ABCD2 and ABCD3. 5 Publications

    Keywords - Diseasei

    Peroxisome biogenesis disorder, Zellweger syndrome

    Organism-specific databases

    MIMi614886. phenotype.
    Orphaneti772. Infantile Refsum disease.
    44. Neonatal adrenoleukodystrophy.
    912. Zellweger syndrome.
    PharmGKBiPA34058.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed1 Publication
    Chaini2 – 296295Peroxisomal biogenesis factor 19PRO_0000218759Add
    BLAST
    Propeptidei297 – 2993Removed in mature formCuratedPRO_0000393944

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei2 – 21N-acetylalanine1 Publication
    Modified residuei35 – 351PhosphoserineBy similarity
    Modified residuei296 – 2961Cysteine methyl esterCurated
    Lipidationi296 – 2961S-farnesyl cysteine2 Publications

    Keywords - PTMi

    Acetylation, Lipoprotein, Methylation, Phosphoprotein, Prenylation

    Proteomic databases

    MaxQBiP40855.
    PaxDbiP40855.
    PRIDEiP40855.

    PTM databases

    PhosphoSiteiP40855.

    Expressioni

    Tissue specificityi

    Ubiquitously expressed. Isoform 1 is strongly predominant in all tissues except in utero where isoform 2 is the main form.1 Publication

    Gene expression databases

    ArrayExpressiP40855.
    BgeeiP40855.
    CleanExiHS_PEX19.
    GenevestigatoriP40855.

    Organism-specific databases

    HPAiHPA044837.
    HPA051966.

    Interactioni

    Subunit structurei

    Interacts with a broad range of peroxisomal membrane proteins, including PEX3, PEX10, PEX11A, PEX11B, PEX12, PEX13, PEX14 and PEX16, PXMP2/PMP22, PXMP4/PMP24, SLC25A17/PMP34, ABCD1/ALDP, ABCD2/ALDRP, and ABCD3/PMP70. Also interacts with the tumor suppressor CDKN2A/p19ARF.10 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    ABCD1P338973EBI-594747,EBI-81045
    ABCD3P282884EBI-594747,EBI-80992
    PEX11BO9601111EBI-594747,EBI-594824
    PEX12O006232EBI-594747,EBI-594836
    PEX13Q9296812EBI-594747,EBI-594849
    PEX14O7538115EBI-594747,EBI-594898
    PEX16Q9Y5Y56EBI-594747,EBI-981985
    PEX2P283283EBI-594747,EBI-713978
    PEX26Q7Z4126EBI-594747,EBI-752057
    PEX3P5658920EBI-594747,EBI-594885
    PXMP2Q9NR772EBI-594747,EBI-1392944
    SLC25A17O438084EBI-594747,EBI-594912

    Protein-protein interaction databases

    BioGridi111782. 37 interactions.
    DIPiDIP-24172N.
    IntActiP40855. 30 interactions.
    MINTiMINT-241394.
    STRINGi9606.ENSP00000357051.

    Structurei

    Secondary structure

    1
    299
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi16 – 2712
    Helixi28 – 314
    Helixi67 – 7610
    Helixi172 – 18211
    Helixi185 – 19612
    Helixi199 – 2068
    Helixi207 – 2093
    Helixi212 – 23423
    Helixi241 – 26020
    Helixi266 – 2683

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2W85NMR-B66-77[»]
    2WL8X-ray2.05A/B/C/D161-283[»]
    3AJBX-ray2.50B1-44[»]
    3MK4X-ray2.42B14-33[»]
    ProteinModelPortaliP40855.
    SMRiP40855. Positions 171-280.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP40855.

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni2 – 9190Necessary for PEX19 function on peroxisome biogenesisAdd
    BLAST
    Regioni2 – 5655Docking to the peroxisome membrane and binding to PEX3Add
    BLAST

    Sequence similaritiesi

    Belongs to the peroxin-19 family.Curated

    Phylogenomic databases

    eggNOGiNOG133983.
    HOGENOMiHOG000038537.
    HOVERGENiHBG053573.
    InParanoidiP40855.
    KOiK13337.
    OMAiNKAMEGL.
    OrthoDBiEOG7P5T1P.
    PhylomeDBiP40855.
    TreeFamiTF315082.

    Family and domain databases

    InterProiIPR006708. Pex19.
    [Graphical view]
    PANTHERiPTHR12774. PTHR12774. 1 hit.
    PfamiPF04614. Pex19. 1 hit.
    [Graphical view]

    Sequences (5)i

    Sequence statusi: Complete.

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

    This entry describes 5 isoformsi produced by alternative splicing. Align

    Note: Experimental confirmation may be lacking for some isoforms.

    Isoform 1 (identifier: P40855-1) [UniParc]FASTAAdd to Basket

    Also known as: PXF-all

    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

    MAAAEEGCSV GAEADRELEE LLESALDDFD KAKPSPAPPS TTTAPDASGP    50
    QKRSPGDTAK DALFASQEKF FQELFDSELA SQATAEFEKA MKELAEEEPH 100
    LVEQFQKLSE AAGRVGSDMT SQQEFTSCLK ETLSGLAKNA TDLQNSSMSE 150
    EELTKAMEGL GMDEGDGEGN ILPIMQSIMQ NLLSKDVLYP SLKEITEKYP 200
    EWLQSHRESL PPEQFEKYQE QHSVMCKICE QFEAETPTDS ETTQKARFEM 250
    VLDLMQQLQD LGHPPKELAG EMPPGLNFDL DALNLSGPPG ASGEQCLIM 299

    Note: The two main transcripts are PXF-all and PXF-delta-2.

    Length:299
    Mass (Da):32,807
    Last modified:February 1, 1995 - v1
    Checksum:i399AF6B79F219100
    GO
    Isoform 2 (identifier: P40855-2)

    Also known as: PXF-delta-2, PXF lacking exon 2

    Sequence is not available

    Note: The two main transcripts are PXF-all and PXF-delta-2.

    Length:
    Mass (Da):
    Isoform 3 (identifier: P40855-3)

    Also known as: PXF-delta-4, PXF lacking exon 4

    Sequence is not available
    Length:
    Mass (Da):
    Isoform 4 (identifier: P40855-4)

    Also known as: PXF-delta-8, PXF lacking part of exon 8

    Sequence is not available
    Length:
    Mass (Da):
    Isoform 5 (identifier: P40855-5) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-59: MAAAEEGCSV...PQKRSPGDTA → PPLRKAVVSGPKRTGNWRSFW

    Note: Incomplete sequence.

    Show »
    Length:261
    Mass (Da):29,259
    Checksum:i5174D3C039E6A3B6
    GO

    Sequence cautioni

    The sequence BAB93469.1 differs from that shown. Reason: Erroneous initiation.

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 5959MAAAE…PGDTA → PPLRKAVVSGPKRTGNWRSF W in isoform 5. 1 PublicationVSP_012649Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X75535 mRNA. Translation: CAA53225.1.
    Y09048 Genomic DNA. Translation: CAA70257.1.
    AB018541 mRNA. Translation: BAA76291.1.
    AB062286 mRNA. Translation: BAB93469.1. Different initiation.
    BT006879 mRNA. Translation: AAP35525.1.
    AL513282 Genomic DNA. Translation: CAI12457.1.
    CH471121 Genomic DNA. Translation: EAW52728.1.
    CH471121 Genomic DNA. Translation: EAW52729.1.
    BC000496 mRNA. Translation: AAH00496.1.
    CCDSiCCDS1201.1. [P40855-1]
    PIRiI37468.
    RefSeqiNP_001180573.1. NM_001193644.1.
    NP_002848.1. NM_002857.3. [P40855-1]
    UniGeneiHs.517232.

    Genome annotation databases

    EnsembliENST00000368072; ENSP00000357051; ENSG00000162735. [P40855-1]
    GeneIDi5824.
    KEGGihsa:5824.
    UCSCiuc001fvs.2. human. [P40855-1]

    Polymorphism databases

    DMDMi729723.

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X75535 mRNA. Translation: CAA53225.1 .
    Y09048 Genomic DNA. Translation: CAA70257.1 .
    AB018541 mRNA. Translation: BAA76291.1 .
    AB062286 mRNA. Translation: BAB93469.1 . Different initiation.
    BT006879 mRNA. Translation: AAP35525.1 .
    AL513282 Genomic DNA. Translation: CAI12457.1 .
    CH471121 Genomic DNA. Translation: EAW52728.1 .
    CH471121 Genomic DNA. Translation: EAW52729.1 .
    BC000496 mRNA. Translation: AAH00496.1 .
    CCDSi CCDS1201.1. [P40855-1 ]
    PIRi I37468.
    RefSeqi NP_001180573.1. NM_001193644.1.
    NP_002848.1. NM_002857.3. [P40855-1 ]
    UniGenei Hs.517232.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2W85 NMR - B 66-77 [» ]
    2WL8 X-ray 2.05 A/B/C/D 161-283 [» ]
    3AJB X-ray 2.50 B 1-44 [» ]
    3MK4 X-ray 2.42 B 14-33 [» ]
    ProteinModelPortali P40855.
    SMRi P40855. Positions 171-280.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 111782. 37 interactions.
    DIPi DIP-24172N.
    IntActi P40855. 30 interactions.
    MINTi MINT-241394.
    STRINGi 9606.ENSP00000357051.

    Protein family/group databases

    TCDBi 9.A.17.1.2. the integral membrane peroxisomal protein importer-2 (ppi2) family.

    PTM databases

    PhosphoSitei P40855.

    Polymorphism databases

    DMDMi 729723.

    Proteomic databases

    MaxQBi P40855.
    PaxDbi P40855.
    PRIDEi P40855.

    Protocols and materials databases

    DNASUi 5824.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000368072 ; ENSP00000357051 ; ENSG00000162735 . [P40855-1 ]
    GeneIDi 5824.
    KEGGi hsa:5824.
    UCSCi uc001fvs.2. human. [P40855-1 ]

    Organism-specific databases

    CTDi 5824.
    GeneCardsi GC01M160246.
    GeneReviewsi PEX19.
    HGNCi HGNC:9713. PEX19.
    HPAi HPA044837.
    HPA051966.
    MIMi 600279. gene.
    614886. phenotype.
    neXtProti NX_P40855.
    Orphaneti 772. Infantile Refsum disease.
    44. Neonatal adrenoleukodystrophy.
    912. Zellweger syndrome.
    PharmGKBi PA34058.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG133983.
    HOGENOMi HOG000038537.
    HOVERGENi HBG053573.
    InParanoidi P40855.
    KOi K13337.
    OMAi NKAMEGL.
    OrthoDBi EOG7P5T1P.
    PhylomeDBi P40855.
    TreeFami TF315082.

    Enzyme and pathway databases

    Reactomei REACT_111158. ABCA transporters in lipid homeostasis.

    Miscellaneous databases

    EvolutionaryTracei P40855.
    GeneWikii PEX19.
    GenomeRNAii 5824.
    NextBioi 22685.
    PROi P40855.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P40855.
    Bgeei P40855.
    CleanExi HS_PEX19.
    Genevestigatori P40855.

    Family and domain databases

    InterProi IPR006708. Pex19.
    [Graphical view ]
    PANTHERi PTHR12774. PTHR12774. 1 hit.
    Pfami PF04614. Pex19. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Sequence of a putative human housekeeping gene (HK33) localized on chromosome 1."
      Braun A., Kammerer S., Weissenhorn W., Weiss E.H., Cleve H.
      Gene 146:291-295(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
      Tissue: Ovary and Placenta.
    2. "Genomic organization and molecular characterization of a gene encoding HsPXF, a human peroxisomal farnesylated protein."
      Kammerer S., Arnold N., Gutensohn W., Mewes H.-W., Kunau W.-H., Hoefler G., Roscher A.A., Braun A.
      Genomics 45:200-210(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], ALTERNATIVE SPLICING, TISSUE SPECIFICITY, SUBCELLULAR LOCATION, ISOPRENYLATION AT CYS-296, MUTAGENESIS OF CYS-296.
      Tissue: Leukocyte and Placenta.
    3. "Human PEX19: cDNA cloning by functional complementation, mutation analysis in a patient with Zellweger syndrome, and potential role in peroxisomal membrane assembly."
      Matsuzono Y., Kinoshita N., Tamura S., Shimozawa N., Hamasaki M., Ghaedi K., Wanders R.J.A., Suzuki Y., Kondo N., Fujiki Y.
      Proc. Natl. Acad. Sci. U.S.A. 96:2116-2121(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), ISOPRENYLATION AT CYS-296, MUTAGENESIS OF CYS-296, SUBCELLULAR LOCATION, FUNCTION, INVOLVEMENT IN PBD12A.
      Tissue: Liver.
    4. "Identification of immuno-peptidmics that are recognized by tumor-reactive CTL generated from TIL of colon cancer patients."
      Shichijo S., Itoh K.
      Submitted (MAY-2001) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 5).
      Tissue: Colon adenocarcinoma.
    5. "Cloning of human full-length CDSs in BD Creator(TM) system donor vector."
      Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., Phelan M., Farmer A.
      Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    6. "The DNA sequence and biological annotation of human chromosome 1."
      Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.
      , Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.
      Nature 441:315-321(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    7. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    8. "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: Lung.
    9. "Human adrenoleukodystrophy protein and related peroxisomal ABC transporters interact with the peroxisomal assembly protein PEX19p."
      Gloeckner C.J., Mayerhofer P.U., Landgraf P., Muntau A.C., Holzinger A., Gerber J.-K., Kammerer S., Adamski J., Roscher A.A.
      Biochem. Biophys. Res. Commun. 271:144-150(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH ABCD1; ABCD2 AND ABCD3, MUTAGENESIS OF CYS-296.
      Tissue: Brain.
    10. "PEX19 binds multiple peroxisomal membrane proteins, is predominantly cytoplasmic, and is required for peroxisome membrane synthesis."
      Sacksteder K.A., Jones J.M., South S.T., Li X., Liu Y., Gould S.J.
      J. Cell Biol. 148:931-944(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, MUTAGENESIS OF CYS-296, SUBCELLULAR LOCATION, INTERACTION WITH ABCD1; ABCD2; ABCD3; PEX3; PEX10; PEX11A; PEX11B; PEX12; PEX13; PEX14; PEX16; PXMP2; PXMP4 AND SLC25A17.
    11. "Pex19p dampens the p19ARF-p53-p21WAF1 tumor suppressor pathway."
      Sugihara T., Kaul S.C., Kato J.-Y., Reddel R.R., Nomura H., Wadhwa R.
      J. Biol. Chem. 276:18649-18652(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH CDKN2A.
      Tissue: Testis.
    12. "Human pex19p binds peroxisomal integral membrane proteins at regions distinct from their sorting sequences."
      Fransen M., Wylin T., Brees C., Mannaerts G.P., Van Veldhoven P.P.
      Mol. Cell. Biol. 21:4413-4424(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH PEX3; PEX10; PEX11B; PEX12; PEX13 AND PEX16, MUTAGENESIS OF 296-CYS--MET-299.
    13. "Two splice variants of human PEX19 exhibit distinct functions in peroxisomal assembly."
      Mayerhofer P.U., Kattenfeld T., Roscher A.A., Muntau A.C.
      Biochem. Biophys. Res. Commun. 291:1180-1186(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH ABCD1; ABCD2; ABCD3 AND PEX3.
    14. "PEX3 functions as a PEX19 docking factor in the import of class I peroxisomal membrane proteins."
      Fang Y., Morrell J.C., Jones J.M., Gould S.J.
      J. Cell Biol. 164:863-875(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH PEX3, SUBCELLULAR LOCATION.
    15. "PEX19 is a predominantly cytosolic chaperone and import receptor for class 1 peroxisomal membrane proteins."
      Jones J.M., Morrell J.C., Gould S.J.
      J. Cell Biol. 164:57-67(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH PEX11B; PEX16; PXMP2; PXMP4; SLC25A17 AND ABCD3.
    16. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    17. "A mutation in PEX19 causes a severe clinical phenotype in a patient with peroxisomal biogenesis disorder."
      Mohamed S., El-Meleagy E., Nasr A., Ebberink M.S., Wanders R.J., Waterham H.R.
      Am. J. Med. Genet. A 152:2318-2321(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: INVOLVEMENT IN PBD-CG14.
    18. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    19. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
    20. "Structural basis for competitive interactions of Pex14 with the import receptors Pex5 and Pex19."
      Neufeld C., Filipp F.V., Simon B., Neuhaus A., Schueller N., David C., Kooshapur H., Madl T., Erdmann R., Schliebs W., Wilmanns M., Sattler M.
      EMBO J. 28:745-754(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: STRUCTURE BY NMR OF 66-77 IN COMPLEX WITH PEX14.
    21. "Structural basis for docking of peroxisomal membrane protein carrier Pex19p onto its receptor Pex3p."
      Sato Y., Shibata H., Nakatsu T., Nakano H., Kashiwayama Y., Imanaka T., Kato H.
      EMBO J. 29:4083-4093(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.50 ANGSTROMS) OF 1-44 IN COMPLEX WITH PEX3, SUBUNIT.
    22. "Insights into peroxisome function from the structure of PEX3 in complex with a soluble fragment of PEX19."
      Schmidt F., Treiber N., Zocher G., Bjelic S., Steinmetz M.O., Kalbacher H., Stehle T., Dodt G.
      J. Biol. Chem. 285:25410-25417(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.42 ANGSTROMS) OF 13-33 IN COMPLEX WITH PEX3, SUBUNIT, MUTAGENESIS OF PHE-29.

    Entry informationi

    Entry nameiPEX19_HUMAN
    AccessioniPrimary (citable) accession number: P40855
    Secondary accession number(s): D3DVE7, Q5QNY4, Q8NI97
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: February 1, 1995
    Last sequence update: February 1, 1995
    Last modified: October 1, 2014
    This is version 149 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 1
      Human chromosome 1: entries, gene names and cross-references to MIM
    2. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    3. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    4. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3