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P50542

- PEX5_HUMAN

UniProt

P50542 - PEX5_HUMAN

Protein

Peroxisomal targeting signal 1 receptor

Gene

PEX5

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 157 (01 Oct 2014)
      Sequence version 3 (12 Dec 2006)
      Previous versions | rss
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    Functioni

    Binds to the C-terminal PTS1-type tripeptide peroxisomal targeting signal (SKL-type) and plays an essential role in peroxisomal protein import.3 Publications

    GO - Molecular functioni

    1. enzyme binding Source: UniProtKB
    2. peroxisome matrix targeting signal-1 binding Source: UniProtKB
    3. peroxisome targeting sequence binding Source: UniProtKB
    4. protein binding Source: UniProtKB
    5. protein C-terminus binding Source: UniProtKB
    6. protein N-terminus binding Source: UniProtKB
    7. small GTPase binding Source: UniProtKB

    GO - Biological processi

    1. cell development Source: Ensembl
    2. cerebral cortex cell migration Source: Ensembl
    3. cerebral cortex neuron differentiation Source: Ensembl
    4. endoplasmic reticulum organization Source: Ensembl
    5. fatty acid beta-oxidation Source: Ensembl
    6. mitochondrial membrane organization Source: Ensembl
    7. negative regulation of protein homotetramerization Source: UniProtKB
    8. neuromuscular process Source: Ensembl
    9. neuron migration Source: Ensembl
    10. positive regulation of multicellular organism growth Source: Ensembl
    11. protein import into peroxisome matrix Source: UniProtKB
    12. protein import into peroxisome matrix, docking Source: UniProtKB
    13. protein import into peroxisome matrix, translocation Source: UniProtKB
    14. protein import into peroxisome membrane Source: UniProtKB
    15. protein targeting to peroxisome Source: UniProtKB
    16. protein tetramerization Source: UniProtKB
    17. very long-chain fatty acid metabolic process Source: Ensembl

    Keywords - Biological processi

    Protein transport, Transport

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Peroxisomal targeting signal 1 receptor
    Short name:
    PTS1 receptor
    Short name:
    PTS1R
    Alternative name(s):
    PTS1-BP
    Peroxin-5
    Peroxisomal C-terminal targeting signal import receptor
    Peroxisome receptor 1
    Gene namesi
    Name:PEX5
    Synonyms:PXR1
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 12

    Organism-specific databases

    HGNCiHGNC:9719. PEX5.

    Subcellular locationi

    Cytoplasm. Peroxisome membrane; Peripheral membrane protein
    Note: Its distribution appears to be dynamic. It is probably a cycling receptor found mainly in the cytoplasm and as well associated to the peroxisomal membrane through a docking factor (PEX13).

    GO - Cellular componenti

    1. cytoplasm Source: UniProtKB
    2. cytosol Source: UniProtKB
    3. Golgi apparatus Source: HPA
    4. intracellular Source: GOC
    5. membrane Source: UniProtKB
    6. mitochondrion Source: GOC
    7. peroxisomal matrix Source: UniProtKB
    8. peroxisomal membrane Source: UniProtKB
    9. peroxisome Source: UniProtKB
    10. protein complex Source: UniProtKB

    Keywords - Cellular componenti

    Cytoplasm, Membrane, Peroxisome

    Pathology & Biotechi

    Involvement in diseasei

    Peroxisome biogenesis disorder 2A (PBD2A) [MIM:214110]: A fatal peroxisome biogenesis disorder belonging to the Zellweger disease spectrum and characterized clinically 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.
    Peroxisome biogenesis disorder 2B (PBD2B) [MIM:202370]: A peroxisome biogenesis disorder that includes neonatal adrenoleukodystrophy (NALD) and infantile Refsum disease (IRD), two milder manifestations of the Zellweger disease spectrum. The clinical course of patients with the NALD and IRD presentation is variable and may include developmental delay, hypotonia, liver dysfunction, sensorineural hearing loss, retinal dystrophy and vision impairment. Children with the NALD presentation may reach their teens, while patients with the IRD presentation may reach adulthood. The clinical conditions are often slowly progressive in particular with respect to loss of hearing and vision. The biochemical abnormalities include accumulation of phytanic acid, very long chain fatty acids (VLCFA), di- and trihydroxycholestanoic acid and pipecolic acid.2 Publications
    Note: The disease is caused by mutations affecting the gene represented in this entry.
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti526 – 5261N → K in PBD2B; neonatal adrenoleukodystrophy; strongly affects peroxisomal protein import. 2 Publications
    VAR_007543
    Natural varianti600 – 6001S → W in PBD2B; infantile Refsum disease; mildly affects peroxisomal protein import. 1 Publication
    VAR_031328

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi118 – 1181W → A: Strongly reduced interaction with PEX14. 1 Publication
    Mutagenesisi122 – 1221F → A: Strongly reduced interaction with PEX14. 1 Publication

    Keywords - Diseasei

    Disease mutation, Peroxisome biogenesis disorder, Zellweger syndrome

    Organism-specific databases

    MIMi202370. phenotype.
    214110. phenotype.
    Orphaneti772. Infantile Refsum disease.
    44. Neonatal adrenoleukodystrophy.
    912. Zellweger syndrome.
    PharmGKBiPA34063.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 639639Peroxisomal targeting signal 1 receptorPRO_0000106305Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Cross-linki11 – 11Glycyl cysteine thioester (Cys-Gly) (interchain with G-Cter in ubiquitin)By similarity

    Post-translational modificationi

    Monoubiquitination at Cys-11 is required for proper export from peroxisomes and recycling.By similarity

    Keywords - PTMi

    Thioester bond, Ubl conjugation

    Proteomic databases

    MaxQBiP50542.
    PaxDbiP50542.
    PRIDEiP50542.

    PTM databases

    PhosphoSiteiP50542.

    Expressioni

    Tissue specificityi

    Detected in heart, brain, placenta, lung, liver, skeletal muscle, kidney and pancreas.3 Publications

    Gene expression databases

    ArrayExpressiP50542.
    BgeeiP50542.
    CleanExiHS_PEX5.
    GenevestigatoriP50542.

    Organism-specific databases

    HPAiHPA039259.
    HPA039260.

    Interactioni

    Subunit structurei

    Interacts with PEX7 and PEX13 By similarity. Interacts with PEX12 and PEX14. Interacts (Cys-linked ubiquitinated) with ZFAND6.By similarity6 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    PEX12O006234EBI-597835,EBI-594836
    PEX14O7538113EBI-597835,EBI-594898

    Protein-protein interaction databases

    BioGridi111788. 66 interactions.
    DIPiDIP-34654N.
    IntActiP50542. 18 interactions.
    MINTiMINT-241634.
    STRINGi9606.ENSP00000407401.

    Structurei

    Secondary structure

    1
    639
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi60 – 6910
    Helixi109 – 12416
    Helixi318 – 3214
    Turni331 – 3344
    Helixi338 – 34710
    Helixi351 – 36313
    Helixi369 – 38113
    Helixi385 – 39814
    Helixi403 – 41513
    Helixi419 – 43113
    Turni434 – 4363
    Helixi437 – 4393
    Helixi460 – 48122
    Helixi488 – 50013
    Helixi504 – 51714
    Helixi522 – 53413
    Helixi538 – 55114
    Helixi556 – 56914
    Helixi572 – 58716
    Beta strandi593 – 5953
    Helixi601 – 61414
    Helixi617 – 6193
    Helixi620 – 6245
    Helixi628 – 6347

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1FCHX-ray2.20A/B272-639[»]
    2C0LX-ray2.30A335-639[»]
    2C0MX-ray2.50A/B/C/F321-639[»]
    2J9QX-ray2.65A/B315-639[»]
    2W84NMR-B108-127[»]
    3R9AX-ray2.35B/D315-639[»]
    4BXUNMR-B57-71[»]
    DisProtiDP00472.
    ProteinModelPortaliP50542.
    SMRiP50542. Positions 335-639.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP50542.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Repeati335 – 36834TPR 1Add
    BLAST
    Repeati369 – 40234TPR 2Add
    BLAST
    Repeati403 – 43634TPR 3Add
    BLAST
    Repeati452 – 48534TPR 4Add
    BLAST
    Repeati488 – 52134TPR 5Add
    BLAST
    Repeati522 – 55534TPR 6Add
    BLAST
    Repeati556 – 58934TPR 7Add
    BLAST

    Sequence similaritiesi

    Contains 7 TPR repeats.PROSITE-ProRule annotation

    Keywords - Domaini

    Repeat, TPR repeat

    Phylogenomic databases

    eggNOGiCOG0457.
    HOGENOMiHOG000158146.
    HOVERGENiHBG053575.
    InParanoidiP50542.
    KOiK13342.
    OrthoDBiEOG793B77.
    PhylomeDBiP50542.
    TreeFamiTF315044.

    Family and domain databases

    Gene3Di1.25.40.10. 2 hits.
    InterProiIPR024111. PTS1R_family.
    IPR013026. TPR-contain_dom.
    IPR011990. TPR-like_helical.
    IPR001440. TPR_1.
    IPR019734. TPR_repeat.
    [Graphical view]
    PANTHERiPTHR10130. PTHR10130. 1 hit.
    PfamiPF00515. TPR_1. 3 hits.
    [Graphical view]
    SMARTiSM00028. TPR. 4 hits.
    [Graphical view]
    PROSITEiPS50005. TPR. 5 hits.
    PS50293. TPR_REGION. 1 hit.
    [Graphical view]

    Sequences (4)i

    Sequence statusi: Complete.

    This entry describes 4 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: P50542-1) [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

    MAMRELVEAE CGGANPLMKL AGHFTQDKAL RQEGLRPGPW PPGAPASEAA    50
    SKPLGVASED ELVAEFLQDQ NAPLVSRAPQ TFKMDDLLAE MQQIEQSNFR 100
    QAPQRAPGVA DLALSENWAQ EFLAAGDAVD VTQDYNETDW SQEFISEVTD 150
    PLSVSPARWA EEYLEQSEEK LWLGEPEGTA TDRWYDEYHP EEDLQHTASD 200
    FVAKVDDPKL ANSEFLKFVR QIGEGQVSLE SGAGSGRAQA EQWAAEFIQQ 250
    QGTSDAWVDQ FTRPVNTSAL DMEFERAKSA IESDVDFWDK LQAELEEMAK 300
    RDAEAHPWLS DYDDLTSATY DKGYQFEEEN PLRDHPQPFE EGLRRLQEGD 350
    LPNAVLLFEA AVQQDPKHME AWQYLGTTQA ENEQELLAIS ALRRCLELKP 400
    DNQTALMALA VSFTNESLQR QACETLRDWL RYTPAYAHLV TPAEEGAGGA 450
    GLGPSKRILG SLLSDSLFLE VKELFLAAVR LDPTSIDPDV QCGLGVLFNL 500
    SGEYDKAVDC FTAALSVRPN DYLLWNKLGA TLANGNQSEE AVAAYRRALE 550
    LQPGYIRSRY NLGISCINLG AHREAVEHFL EALNMQRKSR GPRGEGGAMS 600
    ENIWSTLRLA LSMLGQSDAY GAADARDLST LLTMFGLPQ 639
    Length:639
    Mass (Da):70,865
    Last modified:December 12, 2006 - v3
    Checksum:i9D6951F58AED31AC
    GO
    Isoform 2 (identifier: P50542-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         215-251: Missing.

    Show »
    Length:602
    Mass (Da):66,830
    Checksum:iEA4E6FAAF5E11C55
    GO
    Isoform 3 (identifier: P50542-3) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         283-290: Missing.

    Show »
    Length:631
    Mass (Da):69,872
    Checksum:i9F3B705D888C484B
    GO
    Isoform 4 (identifier: P50542-4) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         45-45: P → PASEAVSVLEVESPGA

    Note: No experimental confirmation available.

    Show »
    Length:654
    Mass (Da):72,291
    Checksum:iCF2055CBD6902BFE
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti425 – 4251T → I in AAC50103. (PubMed:7719337)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti526 – 5261N → K in PBD2B; neonatal adrenoleukodystrophy; strongly affects peroxisomal protein import. 2 Publications
    VAR_007543
    Natural varianti600 – 6001S → W in PBD2B; infantile Refsum disease; mildly affects peroxisomal protein import. 1 Publication
    VAR_031328

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei45 – 451P → PASEAVSVLEVESPGA in isoform 4. 1 PublicationVSP_043639
    Alternative sequencei215 – 25137Missing in isoform 2. 3 PublicationsVSP_021880Add
    BLAST
    Alternative sequencei283 – 2908Missing in isoform 3. 1 PublicationVSP_024106

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U19721 mRNA. Translation: AAC50103.1.
    Z48054 mRNA. Translation: CAA88131.1.
    X84899 mRNA. Translation: CAA59324.1.
    AK292256 mRNA. Translation: BAF84945.1.
    AK302742 mRNA. Translation: BAG63957.1.
    AK316250 mRNA. Translation: BAH14621.1.
    AC018653 Genomic DNA. No translation available.
    CH471116 Genomic DNA. Translation: EAW88671.1.
    CH471116 Genomic DNA. Translation: EAW88674.1.
    CH471116 Genomic DNA. Translation: EAW88672.1.
    BC010621 mRNA. Translation: AAH10621.1.
    CCDSiCCDS44822.1. [P50542-4]
    CCDS44823.1. [P50542-1]
    CCDS44824.1. [P50542-2]
    CCDS8576.1. [P50542-3]
    PIRiA56126.
    RefSeqiNP_000310.2. NM_000319.4. [P50542-3]
    NP_001124495.1. NM_001131023.1. [P50542-4]
    NP_001124496.1. NM_001131024.1. [P50542-2]
    NP_001124497.1. NM_001131025.1. [P50542-1]
    NP_001124498.1. NM_001131026.1. [P50542-1]
    XP_006719194.1. XM_006719131.1. [P50542-1]
    UniGeneiHs.567327.

    Genome annotation databases

    EnsembliENST00000266563; ENSP00000266563; ENSG00000139197. [P50542-2]
    ENST00000266564; ENSP00000266564; ENSG00000139197. [P50542-3]
    ENST00000420616; ENSP00000410159; ENSG00000139197. [P50542-1]
    ENST00000434354; ENSP00000407401; ENSG00000139197. [P50542-4]
    ENST00000455147; ENSP00000400647; ENSG00000139197. [P50542-1]
    GeneIDi5830.
    KEGGihsa:5830.
    UCSCiuc001qsu.3. human. [P50542-2]
    uc001qsv.3. human. [P50542-3]
    uc001qsw.3. human. [P50542-1]
    uc010sgc.2. human. [P50542-4]

    Polymorphism databases

    DMDMi119364633.

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U19721 mRNA. Translation: AAC50103.1 .
    Z48054 mRNA. Translation: CAA88131.1 .
    X84899 mRNA. Translation: CAA59324.1 .
    AK292256 mRNA. Translation: BAF84945.1 .
    AK302742 mRNA. Translation: BAG63957.1 .
    AK316250 mRNA. Translation: BAH14621.1 .
    AC018653 Genomic DNA. No translation available.
    CH471116 Genomic DNA. Translation: EAW88671.1 .
    CH471116 Genomic DNA. Translation: EAW88674.1 .
    CH471116 Genomic DNA. Translation: EAW88672.1 .
    BC010621 mRNA. Translation: AAH10621.1 .
    CCDSi CCDS44822.1. [P50542-4 ]
    CCDS44823.1. [P50542-1 ]
    CCDS44824.1. [P50542-2 ]
    CCDS8576.1. [P50542-3 ]
    PIRi A56126.
    RefSeqi NP_000310.2. NM_000319.4. [P50542-3 ]
    NP_001124495.1. NM_001131023.1. [P50542-4 ]
    NP_001124496.1. NM_001131024.1. [P50542-2 ]
    NP_001124497.1. NM_001131025.1. [P50542-1 ]
    NP_001124498.1. NM_001131026.1. [P50542-1 ]
    XP_006719194.1. XM_006719131.1. [P50542-1 ]
    UniGenei Hs.567327.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1FCH X-ray 2.20 A/B 272-639 [» ]
    2C0L X-ray 2.30 A 335-639 [» ]
    2C0M X-ray 2.50 A/B/C/F 321-639 [» ]
    2J9Q X-ray 2.65 A/B 315-639 [» ]
    2W84 NMR - B 108-127 [» ]
    3R9A X-ray 2.35 B/D 315-639 [» ]
    4BXU NMR - B 57-71 [» ]
    DisProti DP00472.
    ProteinModelPortali P50542.
    SMRi P50542. Positions 335-639.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 111788. 66 interactions.
    DIPi DIP-34654N.
    IntActi P50542. 18 interactions.
    MINTi MINT-241634.
    STRINGi 9606.ENSP00000407401.

    PTM databases

    PhosphoSitei P50542.

    Polymorphism databases

    DMDMi 119364633.

    Proteomic databases

    MaxQBi P50542.
    PaxDbi P50542.
    PRIDEi P50542.

    Protocols and materials databases

    DNASUi 5830.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000266563 ; ENSP00000266563 ; ENSG00000139197 . [P50542-2 ]
    ENST00000266564 ; ENSP00000266564 ; ENSG00000139197 . [P50542-3 ]
    ENST00000420616 ; ENSP00000410159 ; ENSG00000139197 . [P50542-1 ]
    ENST00000434354 ; ENSP00000407401 ; ENSG00000139197 . [P50542-4 ]
    ENST00000455147 ; ENSP00000400647 ; ENSG00000139197 . [P50542-1 ]
    GeneIDi 5830.
    KEGGi hsa:5830.
    UCSCi uc001qsu.3. human. [P50542-2 ]
    uc001qsv.3. human. [P50542-3 ]
    uc001qsw.3. human. [P50542-1 ]
    uc010sgc.2. human. [P50542-4 ]

    Organism-specific databases

    CTDi 5830.
    GeneCardsi GC12P007341.
    GeneReviewsi PEX5.
    HGNCi HGNC:9719. PEX5.
    HPAi HPA039259.
    HPA039260.
    MIMi 202370. phenotype.
    214110. phenotype.
    600414. gene.
    neXtProti NX_P50542.
    Orphaneti 772. Infantile Refsum disease.
    44. Neonatal adrenoleukodystrophy.
    912. Zellweger syndrome.
    PharmGKBi PA34063.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG0457.
    HOGENOMi HOG000158146.
    HOVERGENi HBG053575.
    InParanoidi P50542.
    KOi K13342.
    OrthoDBi EOG793B77.
    PhylomeDBi P50542.
    TreeFami TF315044.

    Miscellaneous databases

    ChiTaRSi PEX5. human.
    EvolutionaryTracei P50542.
    GeneWikii PEX5.
    GenomeRNAii 5830.
    NextBioi 22716.
    PROi P50542.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P50542.
    Bgeei P50542.
    CleanExi HS_PEX5.
    Genevestigatori P50542.

    Family and domain databases

    Gene3Di 1.25.40.10. 2 hits.
    InterProi IPR024111. PTS1R_family.
    IPR013026. TPR-contain_dom.
    IPR011990. TPR-like_helical.
    IPR001440. TPR_1.
    IPR019734. TPR_repeat.
    [Graphical view ]
    PANTHERi PTHR10130. PTHR10130. 1 hit.
    Pfami PF00515. TPR_1. 3 hits.
    [Graphical view ]
    SMARTi SM00028. TPR. 4 hits.
    [Graphical view ]
    PROSITEi PS50005. TPR. 5 hits.
    PS50293. TPR_REGION. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Mutations in the PTS1 receptor gene, PXR1, define complementation group 2 of the peroxisome biogenesis disorders."
      Dodt G., Braverman N., Wong C., Moser A., Moser H.W., Watkins P., Valle D., Gould S.J.
      Nat. Genet. 9:115-125(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), INVOLVEMENT IN PBD2A, VARIANT PBD2B LYS-526, FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
    2. "Human peroxisomal targeting signal-1 receptor restores peroxisomal protein import in cells from patients with fatal peroxisomal disorders."
      Wiemer E.A.C., Nuttley W.M., Bertolaet B.L., Li X., Francke U., Wheelock M.J., Anne U.K., Johnson K.R., Subramani S.
      J. Cell Biol. 130:51-65(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), FUNCTION, TISSUE SPECIFICITY.
      Tissue: Liver.
    3. "Identification and characterization of the putative human peroxisomal C-terminal targeting signal import receptor."
      Fransen M., Brees C., Baumgart E., Vanhooren J.C.T., Baes M., Mannaerts G.P., van Veldhoven P.P.
      J. Biol. Chem. 270:7731-7736(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, TISSUE SPECIFICITY, SUBCELLULAR LOCATION.
      Tissue: Liver.
    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; 2 AND 4).
      Tissue: Testis.
    5. "The finished DNA sequence of human chromosome 12."
      Scherer S.E., Muzny D.M., Buhay C.J., Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V., Hume J., Jackson A., Khan Z.M., Kovar-Smith C., Lewis L.R.
      , Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R., Montgomery K.T., Morgan M.B., Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D., Lovering R.C., Wheeler D.A., Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z., Clerc-Blankenburg K.P., Davis C., Delgado O., Dinh H.H., Draper H., Gonzalez-Garay M.L., Havlak P., Jackson L.R., Jacob L.S., Kelly S.H., Li L., Li Z., Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O., Pasternak S., Perez L.M., Plopper F.J.H., Santibanez J., Shen H., Tabor P.E., Verduzco D., Waldron L., Wang Q., Williams G.A., Zhang J., Zhou J., Allen C.C., Amin A.G., Anyalebechi V., Bailey M., Barbaria J.A., Bimage K.E., Bryant N.P., Burch P.E., Burkett C.E., Burrell K.L., Calderon E., Cardenas V., Carter K., Casias K., Cavazos I., Cavazos S.R., Ceasar H., Chacko J., Chan S.N., Chavez D., Christopoulos C., Chu J., Cockrell R., Cox C.D., Dang M., Dathorne S.R., David R., Davis C.M., Davy-Carroll L., Deshazo D.R., Donlin J.E., D'Souza L., Eaves K.A., Egan A., Emery-Cohen A.J., Escotto M., Flagg N., Forbes L.D., Gabisi A.M., Garza M., Hamilton C., Henderson N., Hernandez O., Hines S., Hogues M.E., Huang M., Idlebird D.G., Johnson R., Jolivet A., Jones S., Kagan R., King L.M., Leal B., Lebow H., Lee S., LeVan J.M., Lewis L.C., London P., Lorensuhewa L.M., Loulseged H., Lovett D.A., Lucier A., Lucier R.L., Ma J., Madu R.C., Mapua P., Martindale A.D., Martinez E., Massey E., Mawhiney S., Meador M.G., Mendez S., Mercado C., Mercado I.C., Merritt C.E., Miner Z.L., Minja E., Mitchell T., Mohabbat F., Mohabbat K., Montgomery B., Moore N., Morris S., Munidasa M., Ngo R.N., Nguyen N.B., Nickerson E., Nwaokelemeh O.O., Nwokenkwo S., Obregon M., Oguh M., Oragunye N., Oviedo R.J., Parish B.J., Parker D.N., Parrish J., Parks K.L., Paul H.A., Payton B.A., Perez A., Perrin W., Pickens A., Primus E.L., Pu L.-L., Puazo M., Quiles M.M., Quiroz J.B., Rabata D., Reeves K., Ruiz S.J., Shao H., Sisson I., Sonaike T., Sorelle R.P., Sutton A.E., Svatek A.F., Svetz L.A., Tamerisa K.S., Taylor T.R., Teague B., Thomas N., Thorn R.D., Trejos Z.Y., Trevino B.K., Ukegbu O.N., Urban J.B., Vasquez L.I., Vera V.A., Villasana D.M., Wang L., Ward-Moore S., Warren J.T., Wei X., White F., Williamson A.L., Wleczyk R., Wooden H.S., Wooden S.H., Yen J., Yoon L., Yoon V., Zorrilla S.E., Nelson D., Kucherlapati R., Weinstock G., Gibbs R.A.
      Nature 440:346-351(2006) [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 3).
      Tissue: Eye.
    8. "PEX12 interacts with PEX5 and PEX10 and acts downstream of receptor docking in peroxisomal matrix protein import."
      Chang C.C., Warren D.S., Sacksteder K.A., Gould S.J.
      J. Cell Biol. 147:761-774(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH PEX12.
    9. "The di-aromatic pentapeptide repeats of the human peroxisome import receptor PEX5 are separate high affinity binding sites for the peroxisomal membrane protein PEX14."
      Saidowsky J., Dodt G., Kirchberg K., Wegner A., Nastainczyk W., Kunau W.-H., Schliebs W.
      J. Biol. Chem. 276:34524-34529(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH PEX14, MUTAGENESIS OF TRP-118 AND PHE-122.
    10. "AWP1/ZFAND6 functions in Pex5 export by interacting with cys-monoubiquitinated Pex5 and Pex6 AAA ATPase."
      Miyata N., Okumoto K., Mukai S., Noguchi M., Fujiki Y.
      Traffic 13:168-183(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH ZFAND6.
    11. "Peroxisomal targeting signal-1 recognition by the TPR domains of human PEX5."
      Gatto G.J. Jr., Geisbrecht B.V., Gould S.J., Berg J.M.
      Nat. Struct. Biol. 7:1091-1095(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF 272-639 IN COMPLEX WITH TARGETING PEPTIDE.
    12. "Recognition of a functional peroxisome type 1 target by the dynamic import receptor Pex5p."
      Stanley W.A., Filipp F.V., Kursula P., Schueller N., Erdmann R., Schliebs W., Sattler M., Wilmanns M.
      Mol. Cell 24:653-663(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 321-639 IN COMPLEX WITH TARGETING PEPTIDE.
    13. "A previously unobserved conformation for the human Pex5p receptor suggests roles for intrinsic flexibility and rigid domain motions in ligand binding."
      Stanley W.A., Pursiainen N.V., Garman E.F., Juffer A.H., Wilmanns M., Kursula P.
      BMC Struct. Biol. 7:24-24(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.65 ANGSTROMS) OF 315-639, BINDING TO C-TERMINAL TARGETING PEPTIDES.
    14. "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 108-127 IN COMPLEX WITH PEX14.
    15. "Functional heterogeneity of C-terminal peroxisome targeting signal 1 in PEX5-defective patients."
      Shimozawa N., Zhang Z., Suzuki Y., Imamura A., Tsukamoto T., Osumi T., Fujiki Y., Orii T., Barth P.G., Wanders R.J., Kondo N.
      Biochem. Biophys. Res. Commun. 262:504-508(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANTS PBD2B LYS-526 AND TRP-600, CHARACTERIZATION OF VARIANTS PBD2B LYS-526 AND TRP-600.

    Entry informationi

    Entry nameiPEX5_HUMAN
    AccessioniPrimary (citable) accession number: P50542
    Secondary accession number(s): A8K891
    , B4DZ45, B7ZAD5, D3DUT8, Q15115, Q15266, Q96FN7
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: October 1, 1996
    Last sequence update: December 12, 2006
    Last modified: October 1, 2014
    This is version 157 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

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. Human chromosome 12
      Human chromosome 12: 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. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    6. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3