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O75381 (PEX14_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 121. 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 membrane protein PEX14
Alternative name(s):
PTS1 receptor-docking protein
Peroxin-14
Peroxisomal membrane anchor protein PEX14
Gene names
Name:PEX14
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length377 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Component of the peroxisomal translocation machinery with PEX13 and PEX17. Interacts with both the PTS1 and PTS2 receptors. Binds directly to PEX17.

Subunit structure

Interacts with PEX5 and PEX19. Ref.9 Ref.17

Subcellular location

Peroxisome membrane; Peripheral membrane protein; Cytoplasmic side Ref.17.

Involvement in disease

Peroxisome biogenesis disorder complementation group K (PBD-CGK) [MIM:614887]: 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.10

Peroxisome biogenesis disorder 13A (PBD13A) [MIM:614887]: 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.10

Sequence similarities

Belongs to the peroxin-14 family.

Ontologies

Keywords
   Biological processProtein transport
Translocation
Transport
   Cellular componentMembrane
Peroxisome
   Coding sequence diversityAlternative splicing
Polymorphism
   DiseasePeroxisome biogenesis disorder
Zellweger syndrome
   PTMAcetylation
Phosphoprotein
   Technical term3D-structure
Complete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processmicrotubule anchoring

Inferred from direct assay PubMed 21525035. Source: UniProtKB

negative regulation of protein binding

Inferred from direct assay PubMed 21976670. Source: UniProtKB

negative regulation of protein homotetramerization

Inferred from direct assay PubMed 21976670. Source: UniProtKB

negative regulation of sequence-specific DNA binding transcription factor activity

Inferred from direct assay PubMed 11863372. Source: UniProtKB

negative regulation of transcription, DNA-templated

Inferred from direct assay PubMed 11863372. Source: UniProtKB

peroxisome organization

Inferred from sequence or structural similarity. Source: UniProtKB

peroxisome transport along microtubule

Inferred from direct assay PubMed 21525035. Source: UniProtKB

protein complex assembly

Inferred from direct assay PubMed 21525035. Source: UniProtKB

protein homooligomerization

Inferred from direct assay PubMed 12488033. Source: UniProtKB

protein import into peroxisome matrix

Inferred from mutant phenotype Ref.10. Source: UniProtKB

protein import into peroxisome matrix, substrate release

Inferred from direct assay PubMed 21976670. Source: UniProtKB

protein import into peroxisome matrix, translocation

Inferred from direct assay PubMed 21525035. Source: UniProtKB

   Cellular_componentintegral component of membrane

Inferred from sequence or structural similarity. Source: UniProtKB

intracellular

Inferred from direct assay PubMed 21976670. Source: UniProtKB

intracellular membrane-bounded organelle

Inferred from direct assay. Source: HPA

nucleolus

Inferred from direct assay. Source: HPA

nucleus

Non-traceable author statement PubMed 11863372. Source: UniProtKB

peroxisomal membrane

Inferred from direct assay PubMed 10022913PubMed 11669066PubMed 18346465PubMed 21525035. Source: UniProtKB

peroxisome

Inferred from direct assay PubMed 16449325PubMed 17881773Ref.17PubMed 21375735. Source: UniProtKB

protein complex

Inferred from direct assay PubMed 19584060. Source: UniProtKB

   Molecular_functionbeta-tubulin binding

Inferred from physical interaction PubMed 21525035. Source: UniProtKB

microtubule binding

Inferred from direct assay PubMed 21525035. Source: UniProtKB

protein N-terminus binding

Inferred from physical interaction PubMed 11863372. Source: UniProtKB

receptor binding

Inferred from physical interaction PubMed 10022913PubMed 21525035PubMed 21976670. Source: UniProtKB

transcription corepressor activity

Inferred from direct assay PubMed 11863372. Source: UniProtKB

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

PEX19P4085515EBI-594898,EBI-594747
PEX5P5054213EBI-594898,EBI-597835

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: O75381-1)

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: O75381-2)

The sequence of this isoform differs from the canonical sequence as follows:
     58-100: Missing.
Note: No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.8
Chain2 – 377376Peroxisomal membrane protein PEX14
PRO_0000058325

Amino acid modifications

Modified residue21N-acetylalanine Ref.8 Ref.12 Ref.16
Modified residue341N6-acetyllysine Ref.13
Modified residue3351Phosphoserine Ref.11

Natural variations

Alternative sequence58 – 10043Missing in isoform 2.
VSP_037021
Natural variant1171A → S.
Corresponds to variant rs12061667 [ dbSNP | Ensembl ].
VAR_051269
Natural variant1501A → S.
Corresponds to variant rs11539793 [ dbSNP | Ensembl ].
VAR_051270
Natural variant3201R → K.
Corresponds to variant rs12070353 [ dbSNP | Ensembl ].
VAR_051271

Experimental info

Mutagenesis521F → A or W: Reduced interaction with PEX19, minor effect on interaction with PEX5. Ref.17
Mutagenesis561K → A or E: Reduced interaction with PEX19, minor effect on interaction with PEX5. Ref.17
Sequence conflict3191K → E in BAG51028. Ref.3

Secondary structure

........... 377
Helix Strand Turn

Details...

Sequences

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

Last modified November 1, 1998. Version 1.
Checksum: FED28F62A0B94E7F

FASTA37741,237
        10         20         30         40         50         60 
MASSEQAEQP SQPSSTPGSE NVLPREPLIA TAVKFLQNSR VRQSPLATRR AFLKKKGLTD 

        70         80         90        100        110        120 
EEIDMAFQQS GTAADEPSSL GPATQVVPVQ PPHLISQPYS PAGSRWRDYG ALAIIMAGIA 

       130        140        150        160        170        180 
FGFHQLYKKY LLPLILGGRE DRKQLERMEA GLSELSGSVA QTVTQLQTTL ASVQELLIQQ 

       190        200        210        220        230        240 
QQKIQELAHE LAAAKATTST NWILESQNIN ELKSEINSLK GLLLNRRQFP PSPSAPKIPS 

       250        260        270        280        290        300 
WQIPVKSPSP SSPAAVNHHS SSDISPVSNE STSSSPGKEG HSPEGSTVTY HLLGPQEEGE 

       310        320        330        340        350        360 
GVVDVKGQVR MEVQGEEEKR EDKEDEEDEE DDDVSHVDEE DCLGVQREDR RGGDGQINEQ 

       370 
VEKLRRPEGA SNESERD 

« Hide

Isoform 2 [UniParc].

Checksum: 03B5FAF2B7892357
Show »

FASTA33436,702

References

« Hide 'large scale' references
[1]"Identification of a human PTS1 receptor docking protein directly required for peroxisomal protein import."
Fransen M., Terlecky S.R., Subramani S.
Proc. Natl. Acad. Sci. U.S.A. 95:8087-8092(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
[2]"The peroxin Pex14p. cDNA cloning by functional complementation on a Chinese hamster ovary cell mutant, characterization, and functional analysis."
Shimizu N., Itoh R., Hirono Y., Otera H., Ghaedi K., Tateishi K., Tamura S., Okumoto K., Harano T., Mukai S., Fujiki Y.
J. Biol. Chem. 274:12593-12604(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
[3]"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 AND 2).
Tissue: Brain, Cerebellum and Placenta.
[4]"Cloning of human full open reading frames in Gateway(TM) system entry vector (pDONR201)."
Halleck A., Ebert L., Mkoundinya M., Schick M., Eisenstein S., Neubert P., Kstrang K., Schatten R., Shen B., Henze S., Mar W., Korn B., Zuo D., Hu Y., LaBaer J.
Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
[5]"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].
[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 (JUL-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 1).
Tissue: Muscle.
[8]Bienvenut W.V., Lempens A., Norman J.C.
Submitted (OCT-2009) to UniProtKB
Cited for: PROTEIN SEQUENCE OF 2-34; 184-195 AND 352-363, CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY.
Tissue: Ovarian carcinoma.
[9]"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: INTERACTION WITH PEX19.
[10]"Identification of a new complementation group of the peroxisome biogenesis disorders and PEX14 as the mutated gene."
Shimozawa N., Tsukamoto T., Nagase T., Takemoto Y., Koyama N., Suzuki Y., Komori M., Osumi T., Jeannette G., Wanders R.J., Kondo N.
Hum. Mutat. 23:552-558(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: INVOLVEMENT IN PBD-CGK AND PBD13A.
[11]"Global, in vivo, and site-specific phosphorylation dynamics in signaling networks."
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.
Cell 127:635-648(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-335, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[12]"Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[13]"Lysine acetylation targets protein complexes and co-regulates major cellular functions."
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M.
Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-34, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[14]"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].
[15]"System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[16]"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].
[17]"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 16-80 IN COMPLEXES WITH PEX5 AND PEX19, MUTAGENESIS OF PHE-52 AND LYS-56, SUBCELLULAR LOCATION, INTERACTION WITH PEX5 AND PEX19.
+Additional computationally mapped references.

Web resources

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF045186 mRNA. Translation: AAC39843.1.
AB017546 mRNA. Translation: BAA36837.1.
AK002194 mRNA. Translation: BAG51028.1.
AK293684 mRNA. Translation: BAH11568.1.
AK313046 mRNA. Translation: BAG35878.1.
CR450321 mRNA. Translation: CAG29317.1.
CR542083 mRNA. Translation: CAG46880.1.
AL139423, AL354956, AL591403 Genomic DNA. Translation: CAD20149.2.
AL354956, AL139423, AL591403 Genomic DNA. Translation: CAI19198.1.
AL591403, AL139423, AL354956 Genomic DNA. Translation: CAH70044.1.
CH471130 Genomic DNA. Translation: EAW71661.1.
BC006327 mRNA. Translation: AAH06327.1.
RefSeqNP_004556.1. NM_004565.2.
UniGeneHs.149983.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2W84NMR-A16-80[»]
2W85NMR-A16-80[»]
4BXUNMR-A16-80[»]
ProteinModelPortalO75381.
SMRO75381. Positions 20-76.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid111218. 57 interactions.
IntActO75381. 62 interactions.
MINTMINT-241450.
STRING9606.ENSP00000349016.

Protein family/group databases

TCDB3.A.20.1.1. the peroxisomal protein importer (ppi) family.

PTM databases

PhosphoSiteO75381.

Proteomic databases

PaxDbO75381.
PeptideAtlasO75381.
PRIDEO75381.

Protocols and materials databases

DNASU5195.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000356607; ENSP00000349016; ENSG00000142655. [O75381-1]
GeneID5195.
KEGGhsa:5195.
UCSCuc001arn.3. human. [O75381-1]
uc010oan.2. human. [O75381-2]

Organism-specific databases

CTD5195.
GeneCardsGC01P010532.
HGNCHGNC:8856. PEX14.
HPAHPA046104.
HPA049231.
MIM601791. gene.
614887. phenotype.
neXtProtNX_O75381.
Orphanet772. Infantile Refsum disease.
44. Neonatal adrenoleukodystrophy.
912. Zellweger syndrome.
PharmGKBPA33198.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG136629.
HOGENOMHOG000220930.
HOVERGENHBG053571.
InParanoidO75381.
KOK13343.
OMAWQIPVKP.
OrthoDBEOG7DFXD4.
PhylomeDBO75381.
TreeFamTF323535.

Gene expression databases

ArrayExpressO75381.
BgeeO75381.
CleanExHS_PEX14.
GenevestigatorO75381.

Family and domain databases

InterProIPR025655. PEX14.
IPR006785. Pex14_N.
[Graphical view]
PANTHERPTHR23058. PTHR23058. 1 hit.
PfamPF04695. Pex14_N. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSPEX14. human.
EvolutionaryTraceO75381.
GeneWikiPEX14.
GenomeRNAi5195.
NextBio20094.
PROO75381.
SOURCESearch...

Entry information

Entry namePEX14_HUMAN
AccessionPrimary (citable) accession number: O75381
Secondary accession number(s): B2R7N1 expand/collapse secondary AC list , B3KML6, B7Z1N2, Q8WX51
Entry history
Integrated into UniProtKB/Swiss-Prot: May 30, 2000
Last sequence update: November 1, 1998
Last modified: April 16, 2014
This is version 121 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 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 1

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