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P40855 (PEX19_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 147. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Peroxisomal biogenesis factor 19
Alternative name(s):
33 kDa housekeeping protein
Peroxin-19
Peroxisomal farnesylated protein
Gene names
Name:PEX19
Synonyms:HK33, PXF
ORF Names:OK/SW-cl.22
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length299 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. Ref.3 Ref.10 Ref.11 Ref.13 Ref.14 Ref.15

Subunit structure

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. Ref.9 Ref.10 Ref.11 Ref.12 Ref.13 Ref.14 Ref.15 Ref.21 Ref.22

Subcellular location

Cytoplasm. Peroxisome membrane; Lipid-anchor; Cytoplasmic side. Note: Mainly cytoplasmic. Some fraction membrane-associated to the outer surface of peroxisomes. Ref.2 Ref.3 Ref.10 Ref.11 Ref.14

Tissue specificity

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

Involvement in disease

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).
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.17

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.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.3

Sequence similarities

Belongs to the peroxin-19 family.

Sequence caution

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

Ontologies

Keywords
   Biological processPeroxisome biogenesis
   Cellular componentCytoplasm
Membrane
Peroxisome
   Coding sequence diversityAlternative splicing
   DiseasePeroxisome biogenesis disorder
Zellweger syndrome
   PTMAcetylation
Lipoprotein
Methylation
Phosphoprotein
Prenylation
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processchaperone-mediated protein folding

Inferred from direct assay Ref.15. Source: UniProtKB

chaperone-mediated protein transport

Inferred from direct assay Ref.15. Source: UniProtKB

establishment of protein localization to peroxisome

Inferred from mutant phenotype PubMed 18782765. Source: UniProtKB

negative regulation of lipid binding

Inferred from direct assay PubMed 19715730. Source: UniProtKB

peroxisome fission

Inferred from mutant phenotype PubMed 18782765. Source: UniProtKB

peroxisome membrane biogenesis

Inferred from direct assay Ref.3. Source: UniProtKB

peroxisome organization

Inferred from mutant phenotype Ref.15Ref.13PubMed 12924628. Source: UniProtKB

protein import into peroxisome membrane

Inferred from direct assay Ref.15. Source: UniProtKB

protein stabilization

Inferred from direct assay Ref.15PubMed 16344115. Source: UniProtKB

protein targeting to peroxisome

Inferred from direct assay PubMed 16344115PubMed 16763195. Source: UniProtKB

transmembrane transport

Traceable author statement. Source: Reactome

   Cellular_componentbrush border membrane

Inferred from sequence or structural similarity. Source: UniProtKB

cytoplasm

Inferred from direct assay Ref.15PubMed 20171429Ref.3. Source: UniProtKB

cytosol

Inferred from direct assay PubMed 19114594. Source: UniProtKB

integral component of membrane

Inferred from direct assay Ref.3. Source: UniProtKB

intracellular membrane-bounded organelle

Inferred from direct assay. Source: HPA

nucleus

Inferred from direct assay. Source: HPA

peroxisomal membrane

Inferred from direct assay PubMed 21525035Ref.2PubMed 15713480. Source: UniProtKB

peroxisome

Inferred from direct assay PubMed 19114594. Source: UniProtKB

protein complex

Inferred from direct assay PubMed 18174172. Source: UniProtKB

   Molecular_functionATPase binding

Inferred from physical interaction PubMed 11453642. Source: UniProtKB

peroxisome membrane class-1 targeting sequence binding

Inferred from direct assay Ref.15. Source: UniProtKB

protein N-terminus binding

Inferred from physical interaction Ref.20. Source: UniProtKB

protein binding

Inferred from physical interaction Ref.10Ref.9PubMed 11590176Ref.15PubMed 16344115PubMed 16763195PubMed 18174172PubMed 18782765PubMed 19114594PubMed 19715730PubMed 20171429PubMed 21525035Ref.13PubMed 15713480. Source: UniProtKB

Complete GO annotation...

Alternative products

This entry describes 5 isoforms produced by alternative splicing. [Align] [Select]

Note: Experimental confirmation may be lacking for some isoforms.
Isoform 1 (identifier: P40855-1)

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.
Note: The two main transcripts are PXF-all and PXF-delta-2.
Isoform 2 (identifier: P40855-2)

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

The sequence of this isoform is not available.
Note: The two main transcripts are PXF-all and PXF-delta-2.
Isoform 3 (identifier: P40855-3)

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

The sequence of this isoform is not available.
Isoform 4 (identifier: P40855-4)

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

The sequence of this isoform is not available.
Isoform 5 (identifier: P40855-5)

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

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.19
Chain2 – 296295Peroxisomal biogenesis factor 19
PRO_0000218759
Propeptide297 – 2993Removed in mature form Probable
PRO_0000393944

Regions

Region2 – 9190Necessary for PEX19 function on peroxisome biogenesis
Region2 – 5655Docking to the peroxisome membrane and binding to PEX3

Amino acid modifications

Modified residue21N-acetylalanine Ref.19
Modified residue351Phosphoserine By similarity
Modified residue2961Cysteine methyl ester Probable
Lipidation2961S-farnesyl cysteine Ref.2 Ref.3

Natural variations

Alternative sequence1 – 5959MAAAE…PGDTA → PPLRKAVVSGPKRTGNWRSF W in isoform 5.
VSP_012649

Experimental info

Mutagenesis291F → A: Abolishes binding to PEX3. Ref.22
Mutagenesis296 – 2994Missing: Abolishes binding to PEX10, PEX11B, PEX12 and PEX13. Does not affect binding to PEX3 and PEX16. Ref.2 Ref.3 Ref.9 Ref.10 Ref.12
Mutagenesis2961C → A: Slightly inhibits PEX19 function on peroxisome biogenesis. Ref.2 Ref.3 Ref.9 Ref.10
Mutagenesis2961C → S: Abolishes farnesylation. Abolishes PEX19 function on peroxisome biogenesis. Does not affect binding to ABCD1, ABCD2 and ABCD3. Ref.2 Ref.3 Ref.9 Ref.10

Secondary structure

................... 299
Helix Strand Turn

Details...

Sequences

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

Last modified February 1, 1995. Version 1.
Checksum: 399AF6B79F219100

FASTA29932,807
        10         20         30         40         50         60 
MAAAEEGCSV GAEADRELEE LLESALDDFD KAKPSPAPPS TTTAPDASGP QKRSPGDTAK 

        70         80         90        100        110        120 
DALFASQEKF FQELFDSELA SQATAEFEKA MKELAEEEPH LVEQFQKLSE AAGRVGSDMT 

       130        140        150        160        170        180 
SQQEFTSCLK ETLSGLAKNA TDLQNSSMSE EELTKAMEGL GMDEGDGEGN ILPIMQSIMQ 

       190        200        210        220        230        240 
NLLSKDVLYP SLKEITEKYP EWLQSHRESL PPEQFEKYQE QHSVMCKICE QFEAETPTDS 

       250        260        270        280        290 
ETTQKARFEM VLDLMQQLQD LGHPPKELAG EMPPGLNFDL DALNLSGPPG ASGEQCLIM 

« Hide

Isoform 2 (PXF-delta-2) (PXF lacking exon 2) (Sequence not available).
Isoform 3 (PXF-delta-4) (PXF lacking exon 4) (Sequence not available).
Isoform 4 (PXF-delta-8) (PXF lacking part of exon 8) (Sequence not available).
Isoform 5 [UniParc].

Checksum: 5174D3C039E6A3B6
Show »

FASTA26129,259

References

« Hide 'large scale' references
[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. expand/collapse author list , 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]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].
[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]"A quantitative atlas of mitotic phosphorylation."
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract]
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]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[19]"N-terminal acetylome analyses and functional insights of the N-terminal acetyltransferase NatB."
Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A., Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012) [PubMed] [Europe PMC] [Abstract]
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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
CCDSCCDS1201.1. [P40855-1]
PIRI37468.
RefSeqNP_001180573.1. NM_001193644.1.
NP_002848.1. NM_002857.3. [P40855-1]
UniGeneHs.517232.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2W85NMR-B66-77[»]
2WL8X-ray2.05A/B/C/D161-283[»]
3AJBX-ray2.50B1-44[»]
3MK4X-ray2.42B14-33[»]
ProteinModelPortalP40855.
SMRP40855. Positions 171-280.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid111782. 37 interactions.
DIPDIP-24172N.
IntActP40855. 29 interactions.
MINTMINT-241394.
STRING9606.ENSP00000357051.

Protein family/group databases

TCDB9.A.17.1.2. the integral membrane peroxisomal protein importer-2 (ppi2) family.

PTM databases

PhosphoSiteP40855.

Polymorphism databases

DMDM729723.

Proteomic databases

MaxQBP40855.
PaxDbP40855.
PRIDEP40855.

Protocols and materials databases

DNASU5824.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000368072; ENSP00000357051; ENSG00000162735. [P40855-1]
GeneID5824.
KEGGhsa:5824.
UCSCuc001fvs.2. human. [P40855-1]

Organism-specific databases

CTD5824.
GeneCardsGC01M160246.
GeneReviewsPEX19.
HGNCHGNC:9713. PEX19.
HPAHPA044837.
HPA051966.
MIM600279. gene.
614886. phenotype.
neXtProtNX_P40855.
Orphanet772. Infantile Refsum disease.
44. Neonatal adrenoleukodystrophy.
912. Zellweger syndrome.
PharmGKBPA34058.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG133983.
HOGENOMHOG000038537.
HOVERGENHBG053573.
InParanoidP40855.
KOK13337.
OMANKAMEGL.
OrthoDBEOG7P5T1P.
PhylomeDBP40855.
TreeFamTF315082.

Enzyme and pathway databases

ReactomeREACT_15518. Transmembrane transport of small molecules.

Gene expression databases

ArrayExpressP40855.
BgeeP40855.
CleanExHS_PEX19.
GenevestigatorP40855.

Family and domain databases

InterProIPR006708. Pex19.
[Graphical view]
PANTHERPTHR12774. PTHR12774. 1 hit.
PfamPF04614. Pex19. 1 hit.
[Graphical view]
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EvolutionaryTraceP40855.
GeneWikiPEX19.
GenomeRNAi5824.
NextBio22685.
PROP40855.
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Entry information

Entry namePEX19_HUMAN
AccessionPrimary (citable) accession number: P40855
Secondary accession number(s): D3DVE7, Q5QNY4, Q8NI97
Entry history
Integrated into UniProtKB/Swiss-Prot: February 1, 1995
Last sequence update: February 1, 1995
Last modified: July 9, 2014
This is version 147 of the entry and version 1 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 chromosome 1

Human chromosome 1: entries, gene names and cross-references to MIM