P40855 (PEX19_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended 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

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	299 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence 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.20 Ref.21
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 process	Peroxisome biogenesis
Cellular component	Cytoplasm Membrane Peroxisome
Coding sequence diversity	Alternative splicing
Disease	Peroxisome biogenesis disorder Zellweger syndrome
PTM	Lipoprotein Methylation Prenylation
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	chaperone-mediated protein folding Inferred from direct assay Ref.15. Source: UniProtKB chaperone-mediated protein transport Inferred from direct assay Ref.15. 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.13. 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
Cellular_component	brush border membrane Inferred from sequence or structural similarity. Source: UniProtKB cytosol Inferred from direct assay PubMed 19114594. Source: UniProtKB integral to membrane Inferred from direct assay Ref.3. Source: UniProtKB nucleus Inferred from mutant phenotype PubMed 12924628. Source: UniProtKB peroxisomal membrane Inferred from direct assay PubMed 21525035Ref.2PubMed 15713480. Source: UniProtKB protein complex Inferred from direct assay PubMed 18174172. Source: UniProtKB
Molecular_function	peroxisome membrane class-1 targeting sequence binding Inferred from direct assay Ref.15. Source: UniProtKB
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
ABCD3	P28288	2	EBI-594747,EBI-80992
PEX11B	O96011	2	EBI-594747,EBI-594824
PEX12	O00623	2	EBI-594747,EBI-594836
PEX13	Q92968	2	EBI-594747,EBI-594849
PEX14	O75381	4	EBI-594747,EBI-594898
PEX3	P56589	4	EBI-594747,EBI-594885
SLC25A17	O43808	4	EBI-594747,EBI-594912

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 key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 296

296

Peroxisomal biogenesis factor 19

PRO_0000218759

Propeptide

297 – 299

3

Removed in mature form Probable

PRO_0000393944

Regions

Region

1 – 91

91

Necessary for PEX19 function on peroxisome biogenesis

Region

1 – 56

56

Docking to the peroxisome membrane and binding to PEX3

Amino acid modifications

Modified residue

296

1

Cysteine methyl ester Probable

Lipidation

296

1

S-farnesyl cysteine Ref.2 Ref.3

Natural variations

Alternative sequence

1 – 59

59

MAAAE…PGDTA → PPLRKAVVSGPKRTGNWRSF W in isoform 5.

VSP_012649

Experimental info

Mutagenesis

29

1

F → A: Abolishes binding to PEX3. Ref.21

Mutagenesis

296 – 299

4

Missing: 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

Mutagenesis

296

1

C → A: Slightly inhibits PEX19 function on peroxisome biogenesis. Ref.2 Ref.3 Ref.9 Ref.10

Mutagenesis

296

1

C → 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

1

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

299

Helix Strand Turn

Details...

Helix

16 – 27

12

Helix

28 – 31

4

Helix

67 – 76

10

Helix

172 – 182

11

Helix

185 – 196

12

Helix

199 – 206

8

Helix

207 – 209

3

Helix

212 – 234

23

Helix

241 – 260

20

Helix

266 – 268

3

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 (PXF-all) [UniParc]. Last modified February 1, 1995. Version 1. Checksum: 399AF6B79F219100	FASTA	299	32,807
	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
	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	FASTA	261	29,259
	10 20 30 40 50 60 PPLRKAVVSG PKRTGNWRSF WKDALFASQE KFFQELFDSE LASQATAEFE KAMKELAEEE 70 80 90 100 110 120 PHLVEQFQKL SEAAGRVGSD MTSQQEFTSC LKETLSGLAK NATDLQNSSM SEEELTKAME 130 140 150 160 170 180 GLGMDEGDGE GNILPIMQSI MQNLLSKDVL YPSLKEITEK YPEWLQSHRE SLPPEQFEKY 190 200 210 220 230 240 QEQHSVMCKI CEQFEAETPT DSETTQKARF EMVLDLMQQL QDLGHPPKEL AGEMPPGLNF 250 260 DLDALNLSGP PGASGEQCLI M

References

	« Hide 'large scale' referencesShow '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. , 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. , 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]	"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.
[20]	"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.
[21]	"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.

Web resources

GeneReviews

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.

IPI

IPI00441867.
IPI00939321.

PIR

I37468.

RefSeq

NP_001180573.1. NM_001193644.1.
NP_002848.1. NM_002857.3.

UniGene

Hs.517232.

3D structure databases

PDBe
RCSB PDB
PDBj

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	[»]

ProteinModelPortal

P40855.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-24172N.

IntAct

P40855. 25 interactions.

MINT

MINT-241394.

STRING

9606.ENSP00000357051.

Protein family/group databases

TCDB

9.A.17.1.2. integral membrane peroxisomal protein importer-2 (PPI2) family.

PTM databases

PhosphoSite

P40855.

Polymorphism databases

DMDM

729723.

Proteomic databases

PaxDb

P40855.

PRIDE

P40855.

Protocols and materials databases

DNASU

5824.

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000368072; ENSP00000357051; ENSG00000162735.

GeneID

5824.

KEGG

hsa:5824.

UCSC

uc001fvs.2. human.

Organism-specific databases

CTD

5824.

GeneCards

GC01M160246.

HGNC

HGNC:9713. PEX19.

HPA

HPA044837.

MIM

600279. gene.
614886. phenotype.

neXtProt

NX_P40855.

Orphanet

772. Infantile Refsum disease.
44. Neonatal adrenoleukodystrophy.
912. Zellweger syndrome.

PharmGKB

PA34058.

GenAtlas

Search...

Phylogenomic databases

eggNOG

NOG133983.

HOGENOM

HOG000038537.

HOVERGEN

HBG053573.

InParanoid

P40855.

KO

K13337.

OMA

DAFFIEQ.

OrthoDB

EOG40K80Z.

PhylomeDB

P40855.

Enzyme and pathway databases

Reactome

REACT_15518. Transmembrane transport of small molecules.

Gene expression databases

ArrayExpress

P40855.

Bgee

P40855.

CleanEx

HS_PEX19.

Genevestigator

P40855.

GermOnline

ENSG00000162735. Homo sapiens.

Family and domain databases

InterPro

IPR006708. Pex19.
[Graphical view]

PANTHER

PTHR12774. PTHR12774. 1 hit.

Pfam

PF04614. Pex19. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

EvolutionaryTrace

P40855.

GenomeRNAi

5824.

NextBio

22685.

SOURCE

Search...

Entry information

Entry name

PEX19_HUMAN

Accession

Primary (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:	May 1, 2013
This is version 135 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.