O35857 · TIM44_MOUSE

  • Protein
    Mitochondrial import inner membrane translocase subunit TIM44
  • Gene
    Timm44
  • Status
    UniProtKB reviewed (Swiss-Prot)
  • Amino acids
  • Protein existence
    Evidence at protein level
  • Annotation score
    4/5

Function

function

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 (PubMed:31618756).
Recruits mitochondrial HSP70 to drive protein translocation into the matrix using ATP as an energy source (By similarity).

Features

Showing features for binding site.

145250100150200250300350400450
TypeIDPosition(s)Description
Binding site166-173ATP (UniProtKB | ChEBI)

GO annotations

all annotationsall molecular functionvirus receptor activitydna bindingrna bindingcytoskeletal motor activitycatalytic activitygtpase activitystructural molecule activitytransporter activitycytoskeletal protein bindinglipid bindingcyclase activityantioxidant activityoxidoreductase activitytransferase activityhydrolase activitylyase activityisomerase activityligase activityprotein tag activitycargo receptor activityhistone bindingprotein folding chaperonetranslation regulator activitynutrient reservoir activityreceptor ligand activitymolecular transducer activitymolecular adaptor activitytoxin activitycell adhesion mediator activitymolecular function regulator activityvirus coreceptor activitycatalytic activity, acting on a proteincatalytic activity, acting on dnacatalytic activity, acting on rnamolecular carrier activitytranscription regulator activitygeneral transcription initiation factor activitymolecular sensor activitymolecular sequestering activityatp-dependent activityother molecular functionall biological processmitotic cell cyclecytokinesiscytoplasmic translationimmune system processmuscle system processcirculatory system processrenal system processrespiratory system processcarbohydrate metabolic processgeneration of precursor metabolites and energydna replicationdna repairdna recombinationchromatin organizationdna-templated transcriptionregulation of dna-templated transcriptiontrna metabolic processprotein foldingprotein glycosylationamino acid metabolic processmodified amino acid metabolic processlipid metabolic processvitamin metabolic processsulfur compound metabolic processintracellular protein transportnucleocytoplasmic transportautophagyinflammatory responsemitochondrion organizationcytoskeleton organizationmicrotubule-based movementperoxisome organizationlysosome organizationchromosome segregationcell adhesionestablishment or maintenance of cell polarityprogrammed cell deathphotosynthesismrna metabolic processsnrna metabolic processvesicle-mediated transportreproductive processdigestive system processsignalingcell differentiationprotein catabolic processextracellular matrix organizationregulatory ncrna-mediated gene silencingtelomere organizationcell junction organizationwound healingribosome biogenesiscilium organizationanatomical structure developmentcell motilitynervous system processendocrine processprotein maturationtransmembrane transportnucleobase-containing small molecule metabolic processhepaticobiliary system processmembrane organizationprotein-containing complex assemblycell wall organization or biogenesisnitrogen cycle metabolic processprotein localization to plasma membranedefense response to other organismdetoxificationmeiotic nuclear divisionmitotic nuclear divisionmitochondrial gene expressioncarbohydrate derivative metabolic processother biological processall cellular componentnuclear chromosomeextracellular regionextracellular spacecell wallnucleusnuclear envelopenucleoplasmchromosomenucleolusmitochondrionlysosomeendosomevacuoleperoxisomeendoplasmic reticulumgolgi apparatuslipid dropletmicrotubule organizing centercytosolribosomecytoskeletonplasma membraneciliumplastidthylakoidexternal encapsulating structureextracellular matrixcytoplasmic vesicleorganelleother cellular component
Cell color indicative of number of GO terms
AspectTerm
Cellular Componentfibrillar center
Cellular Componentmitochondrial inner membrane
Cellular Componentmitochondrial matrix
Cellular Componentmitochondrion
Cellular ComponentTIM23 mitochondrial import inner membrane translocase complex
Molecular FunctionATP binding
Molecular Functionprotein-folding chaperone binding
Biological Processprotein import into mitochondrial matrix

Keywords

Names & Taxonomy

Protein names

  • Recommended name
    Mitochondrial import inner membrane translocase subunit TIM44

Gene names

    • Name
      Timm44
    • Synonyms
      Mimt44, Tim44

Organism names

  • Taxonomic identifier
  • Strains
    • CD-1
    • NMRI
  • Taxonomic lineage
    Eukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Glires > Rodentia > Myomorpha > Muroidea > Muridae > Murinae > Mus > Mus

Accessions

  • Primary accession
    O35857
  • Secondary accessions
    • Q2NLC5

Proteomes

Organism-specific databases

Phenotypes & Variants

Features

Showing features for mutagenesis.

TypeIDPosition(s)Description
Mutagenesis282Abolished interaction with SLC25A4/ANT1.

Variants

We now provide the "Disease & Variants" viewer in its own tab.

The viewer provides 22 variants from UniProt as well as other sources including ClinVar and dbSNP.

Go to variant viewer

PTM/Processing

Features

Showing features for chain, transit peptide, modified residue.

TypeIDPosition(s)Description
ChainPRO_0000034315?-452Mitochondrial import inner membrane translocase subunit TIM44
Transit peptide1-?Mitochondrion
Modified residue128Phosphothreonine
Modified residue177N6-succinyllysine
Modified residue180Phosphoserine
Modified residue217N6-succinyllysine

Keywords

Proteomic databases

2D gel databases

PTM databases

Expression

Gene expression databases

Interaction

Subunit

Probable component of the PAM complex at least composed of a mitochondrial HSP70 protein, GRPEL1 or GRPEL2, TIMM44, TIMM16/PAM16 and TIMM14/DNAJC19 (By similarity).
The complex interacts with the TIMM23 component of the TIM23 complex (PubMed:31618756).
Interacts with SLC25A4/ANT1 and SLC25A5/ANT2; leading to inhibit the presequence translocase TIMM23, thereby promoting stabilization of PINK1 (PubMed:31618756).

Protein-protein interaction databases

Miscellaneous

Structure

Family & Domains

Sequence similarities

Belongs to the Tim44 family.

Keywords

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Sequence processing
    The displayed sequence is further processed into a mature form.
  • Length
    452
  • Mass (Da)
    51,091
  • Last updated
    2011-07-27 v2
  • Checksum
    DC3E5F4E43972D2F
MAAAALRGGWCRCPRRCLGSGIQFLSSHNLPHGSSYQISRPGRELTLTKSYSSGSRKGFLSGLLDNIKQELAKNKEMKESIKKFRDEAKKLEESDALQEARRKYKSIESETVRTSEAIKKKLGELTGTVKESLDEVSKSDLGRKIKEGVEEAARTAKQSAESVSKSGEKLGKTAAFKAISQGVESVKKELDESVLGQTGPYRRPERLRKRTEFAGAKFKESKVFEANEEALGVVLHKDSKWYQQWKDFKDNNVVFNRFFEMKMKYDESDNVLIRASRALTDKVTDLLGGLFSKTEMSEVLTEILRVDPTFDKDHFLHQCETDIIPNILEAMISGELDILKDWCYEATYSQLAHPIQQAKALGFQFHSRILDISNVDLAMGKMMEQGPVLIVTFQAQVVMVIKNSKGEVYDGDPDKVQRMLYVWALCRDQEELNPYAAWRLLDISASSTEQIL

Features

Showing features for sequence conflict.

TypeIDPosition(s)Description
Sequence conflict5in Ref. 1; AAB97624

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
U69898
EMBL· GenBank· DDBJ
AAB97624.1
EMBL· GenBank· DDBJ
mRNA
CH466566
EMBL· GenBank· DDBJ
EDL21992.1
EMBL· GenBank· DDBJ
Genomic DNA
BC110677
EMBL· GenBank· DDBJ
AAI10678.1
EMBL· GenBank· DDBJ
mRNA
BC117523
EMBL· GenBank· DDBJ
AAI17524.1
EMBL· GenBank· DDBJ
mRNA
BC117524
EMBL· GenBank· DDBJ
AAI17525.1
EMBL· GenBank· DDBJ
mRNA

Genome annotation databases

Similar Proteins

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. Our staff consists of biologists and biochemists that are not trained to give medical advice.
We'd like to inform you that we have updated our Privacy Notice to comply with Europe’s new General Data Protection Regulation (GDPR) that applies since 25 May 2018.
FeedbackHelp