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Q9Y5L4

- TIM13_HUMAN

UniProt

Q9Y5L4 - TIM13_HUMAN

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Protein

Mitochondrial import inner membrane translocase subunit Tim13

Gene

TIMM13

Organism
Homo sapiens (Human)
Status
Reviewed - 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

  1. zinc ion binding Source: ProtInc

GO - Biological processi

  1. cellular protein metabolic process Source: Reactome
  2. chaperone-mediated protein transport Source: BHF-UCL
  3. protein targeting to mitochondrion Source: Reactome
  4. 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: Chromosome 19

Organism-specific databases

HGNCiHGNC:11816. TIMM13.

Subcellular locationi

Mitochondrion inner membrane 1 Publication; Peripheral membrane protein 1 Publication; Intermembrane side 1 Publication

GO - Cellular componenti

  1. mitochondrial inner membrane Source: UniProtKB-KW
  2. mitochondrial intermembrane space protein transporter complex Source: BHF-UCL
  3. mitochondrion Source: HPA
  4. nucleolus Source: HPA
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.
GenevestigatoriQ9Y5L4.

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. 32 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.
OMAiGSEETCL.
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:
EMBL
GenBank
DDBJ
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:
EMBL
GenBank
DDBJ
Links Updated
AF144700 mRNA. Translation: AAD39951.1 .
AF152351 mRNA. Translation: AAF15101.1 .
AF152352 mRNA. Translation: AAF15102.1 .
BC008607 mRNA. Translation: AAH08607.1 .
CCDSi CCDS12089.1.
RefSeqi NP_036590.1. NM_012458.3.
UniGenei Hs.75056.

3D structure databases

ProteinModelPortali Q9Y5L4.
SMRi Q9Y5L4. Positions 35-89.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 117722. 32 interactions.
IntActi Q9Y5L4. 8 interactions.
MINTi MINT-3087260.
STRINGi 9606.ENSP00000215570.

PTM databases

PhosphoSitei Q9Y5L4.

Proteomic databases

MaxQBi Q9Y5L4.
PaxDbi Q9Y5L4.
PeptideAtlasi Q9Y5L4.
PRIDEi Q9Y5L4.

Protocols and materials databases

DNASUi 26517.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000215570 ; ENSP00000215570 ; ENSG00000099800 .
GeneIDi 26517.
KEGGi hsa:26517.
UCSCi uc002lvx.1. human.

Organism-specific databases

CTDi 26517.
GeneCardsi GC19M002425.
HGNCi HGNC:11816. TIMM13.
HPAi HPA048985.
MIMi 607383. gene.
neXtProti NX_Q9Y5L4.
PharmGKBi PA36522.
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG246901.
GeneTreei ENSGT00390000014000.
HOGENOMi HOG000115759.
HOVERGENi HBG079645.
InParanoidi Q9Y5L4.
KOi K17781.
OMAi GSEETCL.
OrthoDBi EOG7Q8CQP.
PhylomeDBi Q9Y5L4.
TreeFami TF106194.

Enzyme and pathway databases

Reactomei REACT_118595. Mitochondrial protein import.

Miscellaneous databases

GeneWikii TIMM13.
GenomeRNAii 26517.
NextBioi 48830.
PROi Q9Y5L4.
SOURCEi Search...

Gene expression databases

Bgeei Q9Y5L4.
CleanExi HS_TIMM13.
ExpressionAtlasi Q9Y5L4. baseline.
Genevestigatori Q9Y5L4.

Family and domain databases

Gene3Di 1.10.287.810. 1 hit.
InterProi IPR004217. Tim10/DDP_fam_Znf.
[Graphical view ]
Pfami PF02953. zf-Tim10_DDP. 1 hit.
[Graphical view ]
SUPFAMi SSF144122. SSF144122. 1 hit.
ProtoNeti Search...

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].

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: October 29, 2014
This is version 123 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