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Protein

Mitochondrial import inner membrane translocase subunit TIM14

Gene

PAM18

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

Essential component of the PAM complex, a complex required for the translocation of transit peptide-containing proteins from the inner membrane into the mitochondrial matrix in an ATP-dependent manner. In the complex, it is required to stimulate activity of mtHSP70 (SSC1).3 Publications

GO - Molecular functioni

  • ATPase activator activity Source: SGD

GO - Biological processi

  • protein import into mitochondrial matrix Source: SGD
  • protein targeting to mitochondrion Source: Reactome
Complete GO annotation...

Keywords - Molecular functioni

Chaperone

Keywords - Biological processi

Protein transport, Translocation, Transport

Enzyme and pathway databases

BioCyciYEAST:G3O-32169-MONOMER.
ReactomeiR-SCE-1268020. Mitochondrial protein import.

Protein family/group databases

TCDBi3.A.8.1.1. the mitochondrial protein translocase (mpt) family.

Names & Taxonomyi

Protein namesi
Recommended name:
Mitochondrial import inner membrane translocase subunit TIM14
Alternative name(s):
Presequence translocated-associated motor subunit PAM18
Gene namesi
Name:PAM18
Synonyms:TIM14
Ordered Locus Names:YLR008C
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
Proteomesi
  • UP000002311 Componenti: Chromosome XII

Organism-specific databases

EuPathDBiFungiDB:YLR008C.
SGDiS000003998. PAM18.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 6565Mitochondrial intermembraneSequence analysisAdd
BLAST
Transmembranei66 – 8318HelicalSequence analysisAdd
BLAST
Topological domaini84 – 16885Mitochondrial matrixSequence analysisAdd
BLAST

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Membrane, Mitochondrion, Mitochondrion inner membrane

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi141 – 1433HPD → AAA: Induces lethality. 1 Publication
Mutagenesisi141 – 1411H → Q: Induces lethality. 2 Publications
Mutagenesisi142 – 1421P → A: Induces a strong reduction in ability to stimulate mtHSP70 activity but does not affect import of proteins into mitochondrial matrix. 1 Publication
Mutagenesisi143 – 1431D → N: Induces lethality. 1 Publication
Mutagenesisi144 – 1441K → Q: Induces a strong reduction in ability to stimulate mtHSP70 activity but does not affect import of proteins into mitochondrial matrix. 1 Publication
Mutagenesisi150 – 1501L → W: Temperature-sensitive mutant that impairs heterodimerization with PAM16 and import of proteins into mitochondrial matrix when incubated at 37 degrees Celsius. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 168168Mitochondrial import inner membrane translocase subunit TIM14PRO_0000071118Add
BLAST

Proteomic databases

MaxQBiQ07914.

Interactioni

Subunit structurei

Homodimer and heterodimer with PAM16/TIM16. Homodimerization may not be relevant in vivo, while heterodimerization is essential for activity regulation of mtHSP70. Component of the PAM complex, at least composed of mtHsp70, MGE1, TIM44, PAM16, PAM17 and PAM18/TIM14. Interacts directly with mtHsp70. Interacts directly with TIM17 subunit of the TIM23 complex.6 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
PAM16P429495EBI-31963,EBI-26019
TIM17P395153EBI-31963,EBI-9127

Protein-protein interaction databases

BioGridi31281. 65 interactions.
DIPiDIP-2125N.
IntActiQ07914. 24 interactions.
MINTiMINT-516352.

Structurei

Secondary structure

1
168
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi110 – 1167Combined sources
Turni121 – 1233Combined sources
Helixi126 – 14015Combined sources
Helixi142 – 1443Combined sources
Helixi148 – 16417Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2GUZX-ray2.00A/C/E/G/I/K/M/O99-168[»]
ProteinModelPortaliQ07914.
SMRiQ07914. Positions 98-168.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ07914.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini112 – 16857JPROSITE-ProRule annotationAdd
BLAST

Domaini

The J domain is essential for co-chaperone activity and mediates the heterodimerization with the J-like domain of PAM16.1 Publication

Sequence similaritiesi

Belongs to the TIM14 family.Curated
Contains 1 J domain.PROSITE-ProRule annotation

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

GeneTreeiENSGT00390000017303.
HOGENOMiHOG000115841.
InParanoidiQ07914.
KOiK09539.
OMAiEGSAEWY.
OrthoDBiEOG7FFN55.

Family and domain databases

Gene3Di1.10.287.110. 1 hit.
InterProiIPR001623. DnaJ_domain.
[Graphical view]
SMARTiSM00271. DnaJ. 1 hit.
[Graphical view]
SUPFAMiSSF46565. SSF46565. 1 hit.
PROSITEiPS50076. DNAJ_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q07914-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSSQSNTGNS IEAPQLPIPG QTNGSANVTV DGAGVNVGIQ NGSQGQKTGM
60 70 80 90 100
DLYFDQALNY MGEHPVITGF GAFLTLYFTA GAYKSISKGL NGGKSTTAFL
110 120 130 140 150
KGGFDPKMNS KEALQILNLT ENTLTKKKLK EVHRKIMLAN HPDKGGSPFL
160
ATKINEAKDF LEKRGISK
Length:168
Mass (Da):17,910
Last modified:November 1, 1996 - v1
Checksum:i9CBF71CA50A0F341
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Z73180 Genomic DNA. Translation: CAA97530.1.
AY558196 Genomic DNA. Translation: AAS56522.1.
BK006945 Genomic DNA. Translation: DAA09326.1.
PIRiS64830.
RefSeqiNP_013108.1. NM_001181895.1.

Genome annotation databases

EnsemblFungiiYLR008C; YLR008C; YLR008C.
GeneIDi850694.
KEGGisce:YLR008C.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Z73180 Genomic DNA. Translation: CAA97530.1.
AY558196 Genomic DNA. Translation: AAS56522.1.
BK006945 Genomic DNA. Translation: DAA09326.1.
PIRiS64830.
RefSeqiNP_013108.1. NM_001181895.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2GUZX-ray2.00A/C/E/G/I/K/M/O99-168[»]
ProteinModelPortaliQ07914.
SMRiQ07914. Positions 98-168.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi31281. 65 interactions.
DIPiDIP-2125N.
IntActiQ07914. 24 interactions.
MINTiMINT-516352.

Protein family/group databases

TCDBi3.A.8.1.1. the mitochondrial protein translocase (mpt) family.

Proteomic databases

MaxQBiQ07914.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiYLR008C; YLR008C; YLR008C.
GeneIDi850694.
KEGGisce:YLR008C.

Organism-specific databases

EuPathDBiFungiDB:YLR008C.
SGDiS000003998. PAM18.

Phylogenomic databases

GeneTreeiENSGT00390000017303.
HOGENOMiHOG000115841.
InParanoidiQ07914.
KOiK09539.
OMAiEGSAEWY.
OrthoDBiEOG7FFN55.

Enzyme and pathway databases

BioCyciYEAST:G3O-32169-MONOMER.
ReactomeiR-SCE-1268020. Mitochondrial protein import.

Miscellaneous databases

EvolutionaryTraceiQ07914.
PROiQ07914.

Family and domain databases

Gene3Di1.10.287.110. 1 hit.
InterProiIPR001623. DnaJ_domain.
[Graphical view]
SMARTiSM00271. DnaJ. 1 hit.
[Graphical view]
SUPFAMiSSF46565. SSF46565. 1 hit.
PROSITEiPS50076. DNAJ_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "The nucleotide sequence of Saccharomyces cerevisiae chromosome XII."
    Johnston M., Hillier L.W., Riles L., Albermann K., Andre B., Ansorge W., Benes V., Brueckner M., Delius H., Dubois E., Duesterhoeft A., Entian K.-D., Floeth M., Goffeau A., Hebling U., Heumann K., Heuss-Neitzel D., Hilbert H.
    , Hilger F., Kleine K., Koetter P., Louis E.J., Messenguy F., Mewes H.-W., Miosga T., Moestl D., Mueller-Auer S., Nentwich U., Obermaier B., Piravandi E., Pohl T.M., Portetelle D., Purnelle B., Rechmann S., Rieger M., Rinke M., Rose M., Scharfe M., Scherens B., Scholler P., Schwager C., Schwarz S., Underwood A.P., Urrestarazu L.A., Vandenbol M., Verhasselt P., Vierendeels F., Voet M., Volckaert G., Voss H., Wambutt R., Wedler E., Wedler H., Zimmermann F.K., Zollner A., Hani J., Hoheisel J.D.
    Nature 387:87-90(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 204508 / S288c.
  2. Cited for: GENOME REANNOTATION.
    Strain: ATCC 204508 / S288c.
  3. Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: ATCC 204508 / S288c.
  4. "Tim14, a novel key component of the import motor of the TIM23 protein translocase of mitochondria."
    Mokranjac D., Sichting M., Neupert W., Hell K.
    EMBO J. 22:4945-4956(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION, TOPOLOGY, IDENTIFICATION IN THE PAM COMPLEX, INTERACTION WITH SSC1 AND TIM17, MUTAGENESIS OF HIS-141.
  5. "A J-protein is an essential subunit of the presequence translocase-associated protein import motor of mitochondria."
    Truscott K.N., Voos W., Frazier A.E., Lind M., Li Y., Geissler A., Dudek J., Mueller H., Sickmann A., Meyer H.E., Meisinger C., Guiard B., Rehling P., Pfanner N.
    J. Cell Biol. 163:707-713(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY, IDENTIFICATION IN THE PAM COMPLEX, FUNCTION, SUBCELLULAR LOCATION, TOPOLOGY.
  6. "J protein cochaperone of the mitochondrial inner membrane required for protein import into the mitochondrial matrix."
    D'Silva P.D., Schilke B., Walter W., Andrew A., Craig E.A.
    Proc. Natl. Acad. Sci. U.S.A. 100:13839-13844(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION, TOPOLOGY, MUTAGENESIS OF 141-HIS--ASP-143 AND HIS-141.
  7. "The presequence translocase-associated protein import motor of mitochondria. Pam16 functions in an antagonistic manner to Pam18."
    Li Y., Dudek J., Guiard B., Pfanner N., Rehling P., Voos W.
    J. Biol. Chem. 279:38047-38054(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH PAM16.
  8. Cited for: INTERACTION WITH PAM16.
  9. "Pam17 is required for architecture and translocation activity of the mitochondrial protein import motor."
    van der Laan M., Chacinska A., Lind M., Perschil I., Sickmann A., Meyer H.E., Guiard B., Meisinger C., Pfanner N., Rehling P.
    Mol. Cell. Biol. 25:7449-7458(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION IN THE PAM COMPLEX WITH PAM16; PAM17; TIM44; SSC1 AND MGE1.
  10. "Role of Pam16's degenerate J domain in protein import across the mitochondrial inner membrane."
    D'Silva P.R., Schilke B., Walter W., Craig E.A.
    Proc. Natl. Acad. Sci. U.S.A. 102:12419-12424(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBUNIT, INTERACTION WITH PAM16, DOMAIN, MUTAGENESIS OF PRO-142; ASP-143; LYS-144 AND LEU-150.

Entry informationi

Entry nameiTIM14_YEAST
AccessioniPrimary (citable) accession number: Q07914
Secondary accession number(s): D6VY10
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 6, 2005
Last sequence update: November 1, 1996
Last modified: July 6, 2016
This is version 113 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

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 XII
    Yeast (Saccharomyces cerevisiae) chromosome XII: 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.