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Protein

Peroxisomal membrane protein PEX14

Gene

PEX14

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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

GO - Molecular functioni

  • protein binding, bridging Source: SGD

GO - Biological processi

  • protein import into peroxisome matrix, docking Source: SGD
Complete GO annotation...

Keywords - Biological processi

Protein transport, Translocation, Transport

Enzyme and pathway databases

BioCyciYEAST:G3O-30644-MONOMER.

Protein family/group databases

TCDBi3.A.20.1.5. the peroxisomal protein importer (ppi) family.

Names & Taxonomyi

Protein namesi
Recommended name:
Peroxisomal membrane protein PEX14
Alternative name(s):
Peroxin-14
Gene namesi
Name:PEX14
Ordered Locus Names:YGL153W
ORF Names:G1870
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
Proteomesi
  • UP000002311 Componenti: Chromosome VII

Organism-specific databases

EuPathDBiFungiDB:YGL153W.
SGDiS000003121. PEX14.

Subcellular locationi

GO - Cellular componenti

  • peroxisomal importomer complex Source: SGD
  • peroxisomal membrane Source: SGD
  • Pex17p-Pex14p docking complex Source: SGD
Complete GO annotation...

Keywords - Cellular componenti

Membrane, Peroxisome

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi87 – 904PTLP → ATLA: Loss of interaction with SH3 domain of PEX13. No effect on membrane association. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methionineiRemovedCombined sources
Chaini2 – 341340Peroxisomal membrane protein PEX14PRO_0000058329Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylserineCombined sources
Modified residuei313 – 3131PhosphoserineCombined sources

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

MaxQBiP53112.

PTM databases

iPTMnetiP53112.

Interactioni

Subunit structurei

Interacts with the SH3 domain of PEX13.1 Publication

Binary interactionsi

WithEntry#Exp.IntActNotes
FRQ1Q063893EBI-13212,EBI-11946
PEX13P8066717EBI-13212,EBI-13206
PEX17P4015514EBI-13212,EBI-13218
PEX2P3280010EBI-13212,EBI-13160
PEX5P350568EBI-13212,EBI-13170
PEX6P337606EBI-13212,EBI-13178

GO - Molecular functioni

  • protein binding, bridging Source: SGD

Protein-protein interaction databases

BioGridi33101. 88 interactions.
DIPiDIP-1749N.
IntActiP53112. 33 interactions.
MINTiMINT-407068.

Structurei

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1N5ZX-ray2.70P/Q83-96[»]
2V1RX-ray2.10P/Q/R83-96[»]
ProteinModelPortaliP53112.
SMRiP53112. Positions 7-58.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP53112.

Family & Domainsi

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi86 – 949SH3-binding

Sequence similaritiesi

Belongs to the peroxin-14 family.Curated

Phylogenomic databases

GeneTreeiENSGT00390000015047.
HOGENOMiHOG000000921.
InParanoidiP53112.
KOiK13343.
OMAiQAESTIN.
OrthoDBiEOG7JX3GH.

Family and domain databases

InterProiIPR025655. PEX14.
IPR006785. Pex14_N.
[Graphical view]
PANTHERiPTHR23058. PTHR23058. 2 hits.
PfamiPF04695. Pex14_N. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P53112-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSDVVSKDRK ALFDSAVSFL KDESIKDAPL LKKIEFLKSK GLTEKEIEIA
60 70 80 90 100
MKEPKKDGIV GDEVSKKIGS TENRASQDMY LYEAMPPTLP HRDWKDYFVM
110 120 130 140 150
ATATAGLLYG AYEVTRRYVI PNILPEAKSK LEGDKKEIDD QFSKIDTVLN
160 170 180 190 200
AIEAEQAEFR KKESETLKEL SDTIAELKQA LVQTTRSREK IEDEFRIVKL
210 220 230 240 250
EVVNMQNTID KFVSDNDGMQ ELNNIQKEME SLKSLMNNRM ESGNAQDNRL
260 270 280 290 300
FSISPNGIPG IDTIPSASEI LAKMGMQEES DKEKENGSDA NKDDNAVPAW
310 320 330 340
KKAREQTIDS NASIPEWQKN TAANEISVPD WQNGQVEDSI P
Length:341
Mass (Da):38,420
Last modified:October 1, 1996 - v1
Checksum:iB714D7DA045E2DCB
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Z48618 Genomic DNA. No translation available.
Z72675 Genomic DNA. Translation: CAA96864.1.
AY558503 Genomic DNA. Translation: AAS56829.1.
BK006941 Genomic DNA. Translation: DAA07959.1.
PIRiS60431.
RefSeqiNP_011362.3. NM_001181018.3.

Genome annotation databases

EnsemblFungiiYGL153W; YGL153W; YGL153W.
GeneIDi852724.
KEGGisce:YGL153W.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Z48618 Genomic DNA. No translation available.
Z72675 Genomic DNA. Translation: CAA96864.1.
AY558503 Genomic DNA. Translation: AAS56829.1.
BK006941 Genomic DNA. Translation: DAA07959.1.
PIRiS60431.
RefSeqiNP_011362.3. NM_001181018.3.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1N5ZX-ray2.70P/Q83-96[»]
2V1RX-ray2.10P/Q/R83-96[»]
ProteinModelPortaliP53112.
SMRiP53112. Positions 7-58.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi33101. 88 interactions.
DIPiDIP-1749N.
IntActiP53112. 33 interactions.
MINTiMINT-407068.

Protein family/group databases

TCDBi3.A.20.1.5. the peroxisomal protein importer (ppi) family.

PTM databases

iPTMnetiP53112.

Proteomic databases

MaxQBiP53112.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiYGL153W; YGL153W; YGL153W.
GeneIDi852724.
KEGGisce:YGL153W.

Organism-specific databases

EuPathDBiFungiDB:YGL153W.
SGDiS000003121. PEX14.

Phylogenomic databases

GeneTreeiENSGT00390000015047.
HOGENOMiHOG000000921.
InParanoidiP53112.
KOiK13343.
OMAiQAESTIN.
OrthoDBiEOG7JX3GH.

Enzyme and pathway databases

BioCyciYEAST:G3O-30644-MONOMER.

Miscellaneous databases

EvolutionaryTraceiP53112.
PROiP53112.

Family and domain databases

InterProiIPR025655. PEX14.
IPR006785. Pex14_N.
[Graphical view]
PANTHERiPTHR23058. PTHR23058. 2 hits.
PfamiPF04695. Pex14_N. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "DNA sequence analysis of a 35 kb segment from Saccharomyces cerevisiae chromosome VII reveals 19 open reading frames including RAD54, ACE1/CUP2, PMR1, RCK1, AMS1 and CAL1/CDC43."
    James C.M., Indge K.J., Oliver S.G.
    Yeast 11:1413-1419(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  2. "The nucleotide sequence of Saccharomyces cerevisiae chromosome VII."
    Tettelin H., Agostoni-Carbone M.L., Albermann K., Albers M., Arroyo J., Backes U., Barreiros T., Bertani I., Bjourson A.J., Brueckner M., Bruschi C.V., Carignani G., Castagnoli L., Cerdan E., Clemente M.L., Coblenz A., Coglievina M., Coissac E.
    , Defoor E., Del Bino S., Delius H., Delneri D., de Wergifosse P., Dujon B., Durand P., Entian K.-D., Eraso P., Escribano V., Fabiani L., Fartmann B., Feroli F., Feuermann M., Frontali L., Garcia-Gonzalez M., Garcia-Saez M.I., Goffeau A., Guerreiro P., Hani J., Hansen M., Hebling U., Hernandez K., Heumann K., Hilger F., Hofmann B., Indge K.J., James C.M., Klima R., Koetter P., Kramer B., Kramer W., Lauquin G., Leuther H., Louis E.J., Maillier E., Marconi A., Martegani E., Mazon M.J., Mazzoni C., McReynolds A.D.K., Melchioretto P., Mewes H.-W., Minenkova O., Mueller-Auer S., Nawrocki A., Netter P., Neu R., Nombela C., Oliver S.G., Panzeri L., Paoluzi S., Plevani P., Portetelle D., Portillo F., Potier S., Purnelle B., Rieger M., Riles L., Rinaldi T., Robben J., Rodrigues-Pousada C., Rodriguez-Belmonte E., Rodriguez-Torres A.M., Rose M., Ruzzi M., Saliola M., Sanchez-Perez M., Schaefer B., Schaefer M., Scharfe M., Schmidheini T., Schreer A., Skala J., Souciet J.-L., Steensma H.Y., Talla E., Thierry A., Vandenbol M., van der Aart Q.J.M., Van Dyck L., Vanoni M., Verhasselt P., Voet M., Volckaert G., Wambutt R., Watson M.D., Weber N., Wedler E., Wedler H., Wipfli P., Wolf K., Wright L.F., Zaccaria P., Zimmermann M., Zollner A., Kleine K.
    Nature 387:81-84(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 204508 / S288c.
  3. Cited for: GENOME REANNOTATION.
    Strain: ATCC 204508 / S288c.
  4. Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: ATCC 204508 / S288c.
  5. "Pex14p, a peroxisomal membrane protein binding both receptors of the two PTS-dependent import pathways."
    Albertini M., Rehling P., Erdmann R., Girzalsky W., Kiel J.A.K.W., Veenhuis M., Kunau W.-H.
    Cell 89:83-92(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: CHARACTERIZATION.
  6. "Involvement of Pex13p in Pex14p localization and peroxisomal targeting signal 2-dependent protein import into peroxisomes."
    Girzalsky W., Rehling P., Stein K., Kipper J., Blank L., Kunau W.-H., Erdmann R.
    J. Cell Biol. 144:1151-1162(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: MUTAGENESIS OF 87-PRO--PRO-90, INTERACTION WITH PEX13.
  7. Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
  8. "A multidimensional chromatography technology for in-depth phosphoproteome analysis."
    Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.
    Mol. Cell. Proteomics 7:1389-1396(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  9. "Global analysis of Cdk1 substrate phosphorylation sites provides insights into evolution."
    Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.
    Science 325:1682-1686(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-313, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  10. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS], IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiPEX14_YEAST
AccessioniPrimary (citable) accession number: P53112
Secondary accession number(s): D6VTZ8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: October 1, 1996
Last modified: June 8, 2016
This is version 138 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Miscellaneous

Present with 2570 molecules/cell in log phase SD medium.1 Publication

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families
  3. Yeast
    Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD
  4. Yeast chromosome VII
    Yeast (Saccharomyces cerevisiae) chromosome VII: entries and gene names

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.