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P50542 (PEX5_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 153. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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 names
Name:PEX5
Synonyms:PXR1
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length639 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Binds to the C-terminal PTS1-type tripeptide peroxisomal targeting signal (SKL-type) and plays an essential role in peroxisomal protein import. Ref.1 Ref.2 Ref.3

Subunit structure

Interacts with PEX7 and PEX13 By similarity. Interacts with PEX12 and PEX14. Interacts (Cys-linked ubiquitinated) with ZFAND6. Ref.8 Ref.9 Ref.10

Subcellular location

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). Ref.1 Ref.3

Tissue specificity

Detected in heart, brain, placenta, lung, liver, skeletal muscle, kidney and pancreas. Ref.1 Ref.2 Ref.3

Post-translational modification

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

Involvement in disease

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.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.1

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.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.1 Ref.15

Sequence similarities

Belongs to the peroxisomal targeting signal receptor family.

Contains 7 TPR repeats.

Ontologies

Keywords
   Biological processProtein transport
Transport
   Cellular componentCytoplasm
Membrane
Peroxisome
   Coding sequence diversityAlternative splicing
   DiseaseDisease mutation
Peroxisome biogenesis disorder
Zellweger syndrome
   DomainRepeat
TPR repeat
   PTMThioester bond
Ubl conjugation
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processcell development

Inferred from electronic annotation. Source: Ensembl

cerebral cortex cell migration

Inferred from electronic annotation. Source: Ensembl

cerebral cortex neuron differentiation

Inferred from electronic annotation. Source: Ensembl

endoplasmic reticulum organization

Inferred from electronic annotation. Source: Ensembl

fatty acid beta-oxidation

Inferred from electronic annotation. Source: Ensembl

mitochondrial membrane organization

Inferred from electronic annotation. Source: Ensembl

negative regulation of protein homotetramerization

Inferred from direct assay PubMed 21976670. Source: UniProtKB

neuromuscular process

Inferred from electronic annotation. Source: Ensembl

neuron migration

Inferred from electronic annotation. Source: Ensembl

positive regulation of multicellular organism growth

Inferred from electronic annotation. Source: Ensembl

protein import into peroxisome matrix

Inferred from genetic interaction PubMed 11931631. Source: UniProtKB

protein import into peroxisome matrix, docking

Inferred from direct assay PubMed 21976670. Source: UniProtKB

protein import into peroxisome matrix, translocation

Inferred from direct assay PubMed 11336669Ref.1. Source: UniProtKB

protein import into peroxisome membrane

Inferred from mutant phenotype PubMed 14709540. Source: UniProtKB

protein targeting to peroxisome

Inferred from direct assay PubMed 21375735. Source: UniProtKB

protein tetramerization

Inferred from direct assay PubMed 12456682. Source: UniProtKB

very long-chain fatty acid metabolic process

Inferred from electronic annotation. Source: Ensembl

   Cellular_componentGolgi apparatus

Inferred from direct assay. Source: HPA

cytoplasm

Inferred from direct assay PubMed 10514471. Source: UniProtKB

cytosol

Inferred from direct assay PubMed 11336669Ref.1. Source: UniProtKB

intracellular

Inferred from genetic interaction PubMed 11931631. Source: GOC

membrane

Inferred from direct assay PubMed 10514471. Source: UniProtKB

mitochondrion

Inferred from electronic annotation. Source: GOC

peroxisomal matrix

Inferred from direct assay PubMed 11336669. Source: UniProtKB

peroxisomal membrane

Inferred from direct assay PubMed 21525035PubMed 21525035. Source: UniProtKB

peroxisome

Inferred from direct assay PubMed 21375735Ref.1. Source: UniProtKB

protein complex

Inferred from direct assay PubMed 19584060. Source: UniProtKB

   Molecular_functionenzyme binding

Inferred from physical interaction PubMed 11060344PubMed 11669066PubMed 21976670. Source: UniProtKB

peroxisome matrix targeting signal-1 binding

Inferred from direct assay PubMed 10514471PubMed 11463335PubMed 12456682Ref.1. Source: UniProtKB

peroxisome targeting sequence binding

Inferred from direct assay PubMed 18346465. Source: UniProtKB

protein C-terminus binding

Inferred from physical interaction Ref.8. Source: UniProtKB

protein N-terminus binding

Inferred from physical interaction Ref.14. Source: UniProtKB

small GTPase binding

Inferred from physical interaction PubMed 18346465. Source: UniProtKB

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

PEX12O006234EBI-597835,EBI-594836
PEX14O7538113EBI-597835,EBI-594898

Alternative products

This entry describes 4 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: P50542-1)

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.
Isoform 2 (identifier: P50542-2)

The sequence of this isoform differs from the canonical sequence as follows:
     215-251: Missing.
Isoform 3 (identifier: P50542-3)

The sequence of this isoform differs from the canonical sequence as follows:
     283-290: Missing.
Isoform 4 (identifier: P50542-4)

The sequence of this isoform differs from the canonical sequence as follows:
     45-45: P → PASEAVSVLEVESPGA
Note: No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 639639Peroxisomal targeting signal 1 receptor
PRO_0000106305

Regions

Repeat335 – 36834TPR 1
Repeat369 – 40234TPR 2
Repeat403 – 43634TPR 3
Repeat452 – 48534TPR 4
Repeat488 – 52134TPR 5
Repeat522 – 55534TPR 6
Repeat556 – 58934TPR 7

Amino acid modifications

Cross-link11Glycyl cysteine thioester (Cys-Gly) (interchain with G-Cter in ubiquitin) By similarity

Natural variations

Alternative sequence451P → PASEAVSVLEVESPGA in isoform 4.
VSP_043639
Alternative sequence215 – 25137Missing in isoform 2.
VSP_021880
Alternative sequence283 – 2908Missing in isoform 3.
VSP_024106
Natural variant5261N → K in PBD2B; neonatal adrenoleukodystrophy; strongly affects peroxisomal protein import. Ref.1 Ref.15
VAR_007543
Natural variant6001S → W in PBD2B; infantile Refsum disease; mildly affects peroxisomal protein import. Ref.15
VAR_031328

Experimental info

Mutagenesis1181W → A: Strongly reduced interaction with PEX14. Ref.9
Mutagenesis1221F → A: Strongly reduced interaction with PEX14. Ref.9
Sequence conflict4251T → I in AAC50103. Ref.1

Secondary structure

............................................... 639
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified December 12, 2006. Version 3.
Checksum: 9D6951F58AED31AC

FASTA63970,865
        10         20         30         40         50         60 
MAMRELVEAE CGGANPLMKL AGHFTQDKAL RQEGLRPGPW PPGAPASEAA SKPLGVASED 

        70         80         90        100        110        120 
ELVAEFLQDQ NAPLVSRAPQ TFKMDDLLAE MQQIEQSNFR QAPQRAPGVA DLALSENWAQ 

       130        140        150        160        170        180 
EFLAAGDAVD VTQDYNETDW SQEFISEVTD PLSVSPARWA EEYLEQSEEK LWLGEPEGTA 

       190        200        210        220        230        240 
TDRWYDEYHP EEDLQHTASD FVAKVDDPKL ANSEFLKFVR QIGEGQVSLE SGAGSGRAQA 

       250        260        270        280        290        300 
EQWAAEFIQQ QGTSDAWVDQ FTRPVNTSAL DMEFERAKSA IESDVDFWDK LQAELEEMAK 

       310        320        330        340        350        360 
RDAEAHPWLS DYDDLTSATY DKGYQFEEEN PLRDHPQPFE EGLRRLQEGD LPNAVLLFEA 

       370        380        390        400        410        420 
AVQQDPKHME AWQYLGTTQA ENEQELLAIS ALRRCLELKP DNQTALMALA VSFTNESLQR 

       430        440        450        460        470        480 
QACETLRDWL RYTPAYAHLV TPAEEGAGGA GLGPSKRILG SLLSDSLFLE VKELFLAAVR 

       490        500        510        520        530        540 
LDPTSIDPDV QCGLGVLFNL SGEYDKAVDC FTAALSVRPN DYLLWNKLGA TLANGNQSEE 

       550        560        570        580        590        600 
AVAAYRRALE LQPGYIRSRY NLGISCINLG AHREAVEHFL EALNMQRKSR GPRGEGGAMS 

       610        620        630 
ENIWSTLRLA LSMLGQSDAY GAADARDLST LLTMFGLPQ 

« Hide

Isoform 2 [UniParc].

Checksum: EA4E6FAAF5E11C55
Show »

FASTA60266,830
Isoform 3 [UniParc].

Checksum: 9F3B705D888C484B
Show »

FASTA63169,872
Isoform 4 [UniParc].

Checksum: CF2055CBD6902BFE
Show »

FASTA65472,291

References

« Hide 'large scale' references
[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. expand/collapse author list , 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. expand/collapse author list , 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]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases
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.
+Additional computationally mapped references.

Web resources

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
PIRA56126.
RefSeqNP_000310.2. NM_000319.4.
NP_001124495.1. NM_001131023.1.
NP_001124496.1. NM_001131024.1.
NP_001124497.1. NM_001131025.1.
NP_001124498.1. NM_001131026.1.
UniGeneHs.567327.

3D structure databases

PDBe
RCSB PDB
PDBj
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[»]
DisProtDP00472.
ProteinModelPortalP50542.
SMRP50542. Positions 335-639.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid111788. 66 interactions.
DIPDIP-34654N.
IntActP50542. 18 interactions.
MINTMINT-241634.
STRING9606.ENSP00000407401.

PTM databases

PhosphoSiteP50542.

Polymorphism databases

DMDM119364633.

Proteomic databases

PaxDbP50542.
PRIDEP50542.

Protocols and materials databases

DNASU5830.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000266563; ENSP00000266563; ENSG00000139197. [P50542-2]
ENST00000266564; ENSP00000266564; ENSG00000139197. [P50542-3]
ENST00000420616; ENSP00000410159; ENSG00000139197. [P50542-1]
ENST00000434354; ENSP00000407401; ENSG00000139197. [P50542-4]
ENST00000455147; ENSP00000400647; ENSG00000139197. [P50542-1]
GeneID5830.
KEGGhsa:5830.
UCSCuc001qsu.3. human. [P50542-2]
uc001qsv.3. human. [P50542-3]
uc001qsw.3. human. [P50542-1]
uc010sgc.2. human. [P50542-4]

Organism-specific databases

CTD5830.
GeneCardsGC12P007341.
HGNCHGNC:9719. PEX5.
HPAHPA039259.
HPA039260.
MIM202370. phenotype.
214110. phenotype.
600414. gene.
neXtProtNX_P50542.
Orphanet772. Infantile Refsum disease.
44. Neonatal adrenoleukodystrophy.
912. Zellweger syndrome.
PharmGKBPA34063.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG0457.
HOGENOMHOG000158146.
HOVERGENHBG053575.
InParanoidP50542.
KOK13342.
OrthoDBEOG793B77.
PhylomeDBP50542.
TreeFamTF315044.

Gene expression databases

ArrayExpressP50542.
BgeeP50542.
CleanExHS_PEX5.
GenevestigatorP50542.

Family and domain databases

Gene3D1.25.40.10. 2 hits.
InterProIPR024111. PTS1R_family.
IPR013026. TPR-contain_dom.
IPR011990. TPR-like_helical.
IPR001440. TPR_1.
IPR019734. TPR_repeat.
[Graphical view]
PANTHERPTHR10130. PTHR10130. 1 hit.
PfamPF00515. TPR_1. 3 hits.
[Graphical view]
SMARTSM00028. TPR. 4 hits.
[Graphical view]
PROSITEPS50005. TPR. 5 hits.
PS50293. TPR_REGION. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSPEX5. human.
EvolutionaryTraceP50542.
GeneWikiPEX5.
GenomeRNAi5830.
NextBio22716.
PROP50542.
SOURCESearch...

Entry information

Entry namePEX5_HUMAN
AccessionPrimary (citable) accession number: P50542
Secondary accession number(s): A8K891 expand/collapse secondary AC list , B4DZ45, B7ZAD5, D3DUT8, Q15115, Q15266, Q96FN7
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: December 12, 2006
Last modified: April 16, 2014
This is version 153 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 12

Human chromosome 12: entries, gene names and cross-references to MIM