Q9Y5J9 · TIM8B_HUMAN

  • Protein
    Mitochondrial import inner membrane translocase subunit Tim8 B
  • Gene
    TIMM8B
  • Status
    UniProtKB reviewed (Swiss-Prot)
  • Amino acids
  • Protein existence
    Evidence at protein level
  • Annotation score
    4/5

Function

function

Probable mitochondrial intermembrane chaperone that participates in the import and insertion of some multi-pass transmembrane proteins into the mitochondrial inner membrane. Also required for the transfer of beta-barrel precursors from the TOM complex to the sorting and assembly machinery (SAM complex) of the outer membrane. Acts as a chaperone-like protein that protects the hydrophobic precursors from aggregation and guide them through the mitochondrial intermembrane space (By similarity).

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 Componentextracellular space
Cellular Componentmitochondrial inner membrane
Cellular Componentmitochondrial intermembrane space
Cellular Componentmitochondrial intermembrane space protein transporter complex
Molecular Functionprotein transporter activity
Molecular Functionzinc ion binding
Biological Processprotein insertion into mitochondrial inner membrane
Biological Processprotein targeting to mitochondrion
Biological Processsensory perception of sound

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    Mitochondrial import inner membrane translocase subunit Tim8 B
  • Alternative names
    • DDP-like protein
    • Deafness dystonia protein 2

Gene names

    • Name
      TIMM8B
    • Synonyms
      DDP2, DDPL, TIM8B

Organism names

  • Taxonomic identifier
  • Taxonomic lineage
    Eukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Primates > Haplorrhini > Catarrhini > Hominidae > Homo

Accessions

  • Primary accession
    Q9Y5J9
  • Secondary accessions
    • B0YJA5
    • Q3KQS9
    • Q9UN04

Proteomes

Organism-specific databases

Disease & Variants

Variants

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

The viewer provides 116 variants from UniProt as well as other sources including ClinVar and dbSNP.

Go to variant viewer

Organism-specific databases

Miscellaneous

Genetic variation databases

PTM/Processing

Features

Showing features for initiator methionine, modified residue, chain, disulfide bond.

TypeIDPosition(s)Description
Initiator methionine1Removed
Modified residue2N-acetylalanine
ChainPRO_00001935872-83Mitochondrial import inner membrane translocase subunit Tim8 B
Disulfide bond36↔59
Disulfide bond40↔55

Keywords

Proteomic databases

PTM databases

Expression

Tissue specificity

Ubiquitous, with highest expression in heart, kidney, liver and skeletal muscle.

Gene expression databases

Organism-specific databases

Interaction

Subunit

Heterohexamer; possibly composed of 3 copies of TIMM8B and 3 copies of TIMM13, named soluble 70 kDa complex. Associates with the TIM22 complex, whose core is composed of TIMM22 (By similarity).
View interactors in UniProtKB
View CPX-6132 in Complex Portal

Protein-protein interaction databases

Miscellaneous

Structure

Family & Domains

Features

Showing features for motif.

TypeIDPosition(s)Description
Motif36-59Twin CX3C motif

Domain

The twin CX3C motif contains 4 conserved Cys residues that form 2 disulfide bonds in the mitochondrial intermembrane space. However, during the transit of TIMM8B from cytoplasm into mitochondrion, the Cys residues probably coordinate zinc, thereby preventing folding and allowing its transfer across mitochondrial outer membrane (By similarity).

Sequence similarities

Belongs to the small Tim family.

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    83
  • Mass (Da)
    9,344
  • Last updated
    1999-11-01 v1
  • Checksum
    9DC47BB475DB8692
MAELGEADEAELQRLVAAEQQKAQFTAQVHHFMELCWDKCVEKPGNRLDSRTENCLSSCVDRFIDTTLAITSRFAQIVQKGGQ

Computationally mapped potential isoform sequences

There are 2 potential isoforms mapped to this entry

View all
EntryEntry nameGene nameLength
E9PIR3E9PIR3_HUMANTIMM8B32
G3XAN8G3XAN8_HUMANTIMM8B98

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
AF152350
EMBL· GenBank· DDBJ
AAF15100.1
EMBL· GenBank· DDBJ
mRNA
AF150087
EMBL· GenBank· DDBJ
AAD39994.1
EMBL· GenBank· DDBJ
mRNA
AK312169
EMBL· GenBank· DDBJ
BAG35103.1
EMBL· GenBank· DDBJ
mRNA
EF445036
EMBL· GenBank· DDBJ
ACA06083.1
EMBL· GenBank· DDBJ
Genomic DNA
BC000711
EMBL· GenBank· DDBJ
AAH00711.1
EMBL· GenBank· DDBJ
mRNA
BC105986
EMBL· GenBank· DDBJ
AAI05987.1
EMBL· GenBank· DDBJ
mRNA
BC106067
EMBL· GenBank· DDBJ
AAI06068.1
EMBL· GenBank· DDBJ
mRNA
AF165967
EMBL· GenBank· DDBJ
AAD51801.1
EMBL· GenBank· DDBJ
mRNA

Genome annotation databases

Similar Proteins

Disclaimer

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