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Protein

Mitochondrial import inner membrane translocase subunit Tim13

Gene

TIMM13

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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. The TIMM8-TIMM13 complex mediates the import of proteins such as TIMM23, SLC25A12/ARALAR1 and SLC25A13/ARALAR2, while the predominant TIMM9-TIMM10 70 kDa complex mediates the import of much more proteins.2 Publications

GO - Molecular functioni

  • zinc ion binding Source: ProtInc

GO - Biological processi

  • cellular protein metabolic process Source: Reactome
  • chaperone-mediated protein transport Source: BHF-UCL
  • protein targeting to mitochondrion Source: Reactome
  • sensory perception of sound Source: ProtInc
Complete GO annotation...

Keywords - Molecular functioni

Chaperone

Keywords - Biological processi

Protein transport, Translocation, Transport

Keywords - Ligandi

Metal-binding, Zinc

Enzyme and pathway databases

ReactomeiREACT_118595. Mitochondrial protein import.

Names & Taxonomyi

Protein namesi
Recommended name:
Mitochondrial import inner membrane translocase subunit Tim13
Gene namesi
Name:TIMM13
Synonyms:TIM13B, TIMM13A, TIMM13B
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome 19

Organism-specific databases

HGNCiHGNC:11816. TIMM13.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Membrane, Mitochondrion, Mitochondrion inner membrane

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA36522.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 9595Mitochondrial import inner membrane translocase subunit Tim13PRO_0000193623Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei1 – 11N-acetylmethionine1 Publication
Disulfide bondi46 ↔ 69By similarity
Disulfide bondi50 ↔ 65By similarity
Modified residuei53 – 531N6-succinyllysineBy similarity

Keywords - PTMi

Acetylation, Disulfide bond

Proteomic databases

MaxQBiQ9Y5L4.
PaxDbiQ9Y5L4.
PeptideAtlasiQ9Y5L4.
PRIDEiQ9Y5L4.

PTM databases

PhosphoSiteiQ9Y5L4.

Expressioni

Tissue specificityi

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

Gene expression databases

BgeeiQ9Y5L4.
CleanExiHS_TIMM13.
ExpressionAtlasiQ9Y5L4. baseline.
GenevisibleiQ9Y5L4. HS.

Organism-specific databases

HPAiHPA048985.

Interactioni

Subunit structurei

Heterohexamer; composed of 3 copies of TIMM8 (TIMM8A or TIMM8B) and 3 copies of TIMM13, named soluble 70 kDa complex. Associates with the TIM22 complex, whose core is composed of TIMM22.

Protein-protein interaction databases

BioGridi117722. 30 interactions.
IntActiQ9Y5L4. 8 interactions.
MINTiMINT-3087260.
STRINGi9606.ENSP00000215570.

Structurei

3D structure databases

ProteinModelPortaliQ9Y5L4.
SMRiQ9Y5L4. Positions 35-89.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi46 – 6924Twin CX3C motifAdd
BLAST

Domaini

The twin CX3C motif contains 4 conserved Cys residues that form 2 disulfide bonds in the mitochondrial intermembrane space. However, during the transit of TIMM13 from cytoplasm into mitochondrion, the Cys residues probably coordinate zinc, thereby preventing folding and allowing its transfer across mitochondrial outer membrane (By similarity).By similarity

Sequence similaritiesi

Belongs to the small Tim family.Curated

Phylogenomic databases

eggNOGiNOG246901.
GeneTreeiENSGT00390000014000.
HOGENOMiHOG000115759.
HOVERGENiHBG079645.
InParanoidiQ9Y5L4.
KOiK17781.
OMAiETCLSRC.
OrthoDBiEOG7Q8CQP.
PhylomeDBiQ9Y5L4.
TreeFamiTF106194.

Family and domain databases

Gene3Di1.10.287.810. 1 hit.
InterProiIPR004217. Tim10/DDP_fam_Znf.
[Graphical view]
PfamiPF02953. zf-Tim10_DDP. 1 hit.
[Graphical view]
SUPFAMiSSF144122. SSF144122. 1 hit.

Sequencei

Sequence statusi: Complete.

Q9Y5L4-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MEGGFGSDFG GSGSGKLDPG LIMEQVKVQI AVANAQELLQ RMTDKCFRKC
60 70 80 90
IGKPGGSLDN SEQKCIAMCM DRYMDAWNTV SRAYNSRLQR ERANM
Length:95
Mass (Da):10,500
Last modified:November 1, 1999 - v1
Checksum:iE40E742C7CA55834
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti2 – 32EG → DS in AAF15101 (PubMed:10552927).Curated
Sequence conflicti12 – 143SGS → TGG in AAF15101 (PubMed:10552927).Curated
Sequence conflicti21 – 211L → A in AAF15101 (PubMed:10552927).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF144700 mRNA. Translation: AAD39951.1.
AF152351 mRNA. Translation: AAF15101.1.
AF152352 mRNA. Translation: AAF15102.1.
BC008607 mRNA. Translation: AAH08607.1.
CCDSiCCDS12089.1.
RefSeqiNP_036590.1. NM_012458.3.
UniGeneiHs.75056.

Genome annotation databases

EnsembliENST00000215570; ENSP00000215570; ENSG00000099800.
GeneIDi26517.
KEGGihsa:26517.
UCSCiuc002lvx.1. human.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF144700 mRNA. Translation: AAD39951.1.
AF152351 mRNA. Translation: AAF15101.1.
AF152352 mRNA. Translation: AAF15102.1.
BC008607 mRNA. Translation: AAH08607.1.
CCDSiCCDS12089.1.
RefSeqiNP_036590.1. NM_012458.3.
UniGeneiHs.75056.

3D structure databases

ProteinModelPortaliQ9Y5L4.
SMRiQ9Y5L4. Positions 35-89.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi117722. 30 interactions.
IntActiQ9Y5L4. 8 interactions.
MINTiMINT-3087260.
STRINGi9606.ENSP00000215570.

PTM databases

PhosphoSiteiQ9Y5L4.

Proteomic databases

MaxQBiQ9Y5L4.
PaxDbiQ9Y5L4.
PeptideAtlasiQ9Y5L4.
PRIDEiQ9Y5L4.

Protocols and materials databases

DNASUi26517.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000215570; ENSP00000215570; ENSG00000099800.
GeneIDi26517.
KEGGihsa:26517.
UCSCiuc002lvx.1. human.

Organism-specific databases

CTDi26517.
GeneCardsiGC19M002425.
HGNCiHGNC:11816. TIMM13.
HPAiHPA048985.
MIMi607383. gene.
neXtProtiNX_Q9Y5L4.
PharmGKBiPA36522.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiNOG246901.
GeneTreeiENSGT00390000014000.
HOGENOMiHOG000115759.
HOVERGENiHBG079645.
InParanoidiQ9Y5L4.
KOiK17781.
OMAiETCLSRC.
OrthoDBiEOG7Q8CQP.
PhylomeDBiQ9Y5L4.
TreeFamiTF106194.

Enzyme and pathway databases

ReactomeiREACT_118595. Mitochondrial protein import.

Miscellaneous databases

ChiTaRSiTIMM13. human.
GeneWikiiTIMM13.
GenomeRNAii26517.
NextBioi48830.
PROiQ9Y5L4.
SOURCEiSearch...

Gene expression databases

BgeeiQ9Y5L4.
CleanExiHS_TIMM13.
ExpressionAtlasiQ9Y5L4. baseline.
GenevisibleiQ9Y5L4. HS.

Family and domain databases

Gene3Di1.10.287.810. 1 hit.
InterProiIPR004217. Tim10/DDP_fam_Znf.
[Graphical view]
PfamiPF02953. zf-Tim10_DDP. 1 hit.
[Graphical view]
SUPFAMiSSF144122. SSF144122. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "The mitochondrial TIM22 preprotein translocase is highly conserved throughout the eukaryotic kingdom."
    Bauer M.F., Rothbauer U., Muehlenbein N., Smith R.J.H., Gerbitz K.-D., Neupert W., Brunner M., Hofmann S.
    FEBS Lett. 464:41-47(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  2. "The human family of deafness/dystonia peptide (DDP) related mitochondrial import proteins."
    Jin H., Kendall E., Freeman T.C., Roberts R.G., Vetrie D.L.P.
    Genomics 61:259-267(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  3. "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].
    Tissue: Placenta.
  4. "Role of the deafness dystonia peptide 1 (DDP1) in import of human Tim23 into the inner membrane of mitochondria."
    Rothbauer U., Hofmann S., Muehlenbein N., Paschen S.A., Gerbitz K.-D., Neupert W., Brunner M., Bauer M.F.
    J. Biol. Chem. 276:37327-37334(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION, ZINC-BINDING, INTERACTION WITH TIMM8A.
  5. "The calcium-binding aspartate/glutamate carriers, citrin and aralar1, are new substrates for the DDP1/TIMM8a-TIMM13 complex."
    Roesch K., Hynds P.J., Varga R., Tranebjaerg L., Koehler C.M.
    Hum. Mol. Genet. 13:2101-2111(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  6. "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 MET-1, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  7. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  8. "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome."
    Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., Ye M., Zou H.
    J. Proteomics 96:253-262(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.

Entry informationi

Entry nameiTIM13_HUMAN
AccessioniPrimary (citable) accession number: Q9Y5L4
Secondary accession number(s): P62206, Q9UHL8, Q9WTL1
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 11, 2001
Last sequence update: November 1, 1999
Last modified: July 22, 2015
This is version 129 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (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.

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Human chromosome 19
    Human chromosome 19: entries, gene names and cross-references to MIM
  2. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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 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.