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P62072

- TIM10_HUMAN

UniProt

P62072 - TIM10_HUMAN

Protein

Mitochondrial import inner membrane translocase subunit Tim10

Gene

TIMM10

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

    Mitochondrial intermembrane chaperone that participates in the import and insertion of multi-pass transmembrane proteins into the mitochondrial inner membrane. May also be 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.1 Publication

    GO - Molecular functioni

    1. chaperone binding Source: BHF-UCL
    2. protein binding Source: IntAct
    3. protein homodimerization activity Source: BHF-UCL
    4. transporter activity Source: BHF-UCL
    5. zinc ion binding Source: UniProtKB

    GO - Biological processi

    1. cellular protein metabolic process Source: Reactome
    2. chaperone-mediated protein transport Source: BHF-UCL
    3. protein import into mitochondrial inner membrane Source: BHF-UCL
    4. protein targeting to mitochondrion Source: UniProtKB
    5. sensory perception of sound Source: UniProtKB

    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 Tim10
    Gene namesi
    Name:TIMM10
    Synonyms:TIM10
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 11

    Organism-specific databases

    HGNCiHGNC:11814. TIMM10.

    Subcellular locationi

    Mitochondrion inner membrane 2 Publications; Peripheral membrane protein 2 Publications; Intermembrane side 2 Publications

    GO - Cellular componenti

    1. mitochondrial inner membrane Source: BHF-UCL
    2. mitochondrial inner membrane presequence translocase complex Source: UniProtKB
    3. mitochondrial intermembrane space Source: BHF-UCL
    4. mitochondrial intermembrane space protein transporter complex Source: BHF-UCL
    5. mitochondrion Source: HPA

    Keywords - Cellular componenti

    Membrane, Mitochondrion, Mitochondrion inner membrane

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA36521.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 9090Mitochondrial import inner membrane translocase subunit Tim10PRO_0000193612Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Disulfide bondi29 ↔ 541 Publication
    Disulfide bondi33 ↔ 501 Publication

    Keywords - PTMi

    Disulfide bond

    Proteomic databases

    MaxQBiP62072.
    PaxDbiP62072.
    PeptideAtlasiP62072.
    PRIDEiP62072.

    PTM databases

    PhosphoSiteiP62072.

    Expressioni

    Tissue specificityi

    Ubiquitous, with highest expression in heart, kidney, liver and skeletal muscle.2 Publications

    Gene expression databases

    BgeeiP62072.
    CleanExiHS_TIMM10.
    GenevestigatoriP62072.

    Organism-specific databases

    HPAiHPA039946.

    Interactioni

    Subunit structurei

    Heterohexamer; composed of 3 copies of TIMM9 and 3 copies of TIMM10/TIM10A, named soluble 70 kDa complex. The complex forms a 6-bladed alpha-propeller structure and associates with the TIMM22 component of the TIM22 complex. Interacts with multi-pass transmembrane proteins in transit. Also forms a complex composed of TIMM9, TIMM10/TIM10A and FXC1/TIM10B.2 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    TIMM9Q9Y5J74EBI-1200391,EBI-1200370

    Protein-protein interaction databases

    BioGridi117723. 16 interactions.
    IntActiP62072. 4 interactions.
    STRINGi9606.ENSP00000257245.

    Structurei

    Secondary structure

    1
    90
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Turni14 – 185
    Helixi19 – 3315
    Beta strandi40 – 423
    Helixi45 – 7430

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2BSKX-ray3.30B/D/F1-90[»]
    ProteinModelPortaliP62072.
    SMRiP62072. Positions 1-90.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP62072.

    Family & Domainsi

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi29 – 5426Twin 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 TIMM10 from cytoplasm into mitochondrion, the Cys residues probably coordinate zinc, thereby preventing folding and allowing its transfer across mitochondrial outer membrane Probable.Curated

    Sequence similaritiesi

    Belongs to the small Tim family.Curated

    Phylogenomic databases

    eggNOGiNOG297225.
    HOGENOMiHOG000211421.
    HOVERGENiHBG055029.
    InParanoidiP62072.
    KOiK17778.
    OMAiKCIPPKY.
    OrthoDBiEOG7N37GD.
    PhylomeDBiP62072.
    TreeFamiTF106193.

    Family and domain databases

    Gene3Di1.10.287.810. 1 hit.
    InterProiIPR004217. Tim10/DDP_fam_Znf.
    IPR027247. Tim10/Tim12.
    [Graphical view]
    PANTHERiPTHR11038. PTHR11038. 1 hit.
    PfamiPF02953. zf-Tim10_DDP. 1 hit.
    [Graphical view]
    SUPFAMiSSF144122. SSF144122. 1 hit.

    Sequencei

    Sequence statusi: Complete.

    P62072-1 [UniParc]FASTAAdd to Basket

    « Hide

    MDPLRAQQLA AELEVEMMAD MYNRMTSACH RKCVPPHYKE AELSKGESVC   50
    LDRCVSKYLD IHERMGKKLT ELSMQDEELM KRVQQSSGPA 90
    Length:90
    Mass (Da):10,333
    Last modified:June 21, 2004 - v1
    Checksum:iD20EFAE694D14BAB
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF150089 mRNA. Translation: AAD39995.1.
    AF152354 mRNA. Translation: AAF15104.1.
    AK289751 mRNA. Translation: BAF82440.1.
    CH471076 Genomic DNA. Translation: EAW73753.1.
    BC032133 mRNA. Translation: AAH32133.1.
    CCDSiCCDS7959.1.
    RefSeqiNP_036588.1. NM_012456.2.
    UniGeneiHs.235750.

    Genome annotation databases

    EnsembliENST00000257245; ENSP00000257245; ENSG00000134809.
    ENST00000525158; ENSP00000433627; ENSG00000134809.
    ENST00000525587; ENSP00000435678; ENSG00000134809.
    GeneIDi26519.
    KEGGihsa:26519.
    UCSCiuc001nkm.1. human.

    Polymorphism databases

    DMDMi49065657.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF150089 mRNA. Translation: AAD39995.1 .
    AF152354 mRNA. Translation: AAF15104.1 .
    AK289751 mRNA. Translation: BAF82440.1 .
    CH471076 Genomic DNA. Translation: EAW73753.1 .
    BC032133 mRNA. Translation: AAH32133.1 .
    CCDSi CCDS7959.1.
    RefSeqi NP_036588.1. NM_012456.2.
    UniGenei Hs.235750.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2BSK X-ray 3.30 B/D/F 1-90 [» ]
    ProteinModelPortali P62072.
    SMRi P62072. Positions 1-90.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 117723. 16 interactions.
    IntActi P62072. 4 interactions.
    STRINGi 9606.ENSP00000257245.

    PTM databases

    PhosphoSitei P62072.

    Polymorphism databases

    DMDMi 49065657.

    Proteomic databases

    MaxQBi P62072.
    PaxDbi P62072.
    PeptideAtlasi P62072.
    PRIDEi P62072.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000257245 ; ENSP00000257245 ; ENSG00000134809 .
    ENST00000525158 ; ENSP00000433627 ; ENSG00000134809 .
    ENST00000525587 ; ENSP00000435678 ; ENSG00000134809 .
    GeneIDi 26519.
    KEGGi hsa:26519.
    UCSCi uc001nkm.1. human.

    Organism-specific databases

    CTDi 26519.
    GeneCardsi GC11M057299.
    HGNCi HGNC:11814. TIMM10.
    HPAi HPA039946.
    MIMi 602251. gene.
    neXtProti NX_P62072.
    PharmGKBi PA36521.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG297225.
    HOGENOMi HOG000211421.
    HOVERGENi HBG055029.
    InParanoidi P62072.
    KOi K17778.
    OMAi KCIPPKY.
    OrthoDBi EOG7N37GD.
    PhylomeDBi P62072.
    TreeFami TF106193.

    Enzyme and pathway databases

    Reactomei REACT_118595. Mitochondrial protein import.

    Miscellaneous databases

    EvolutionaryTracei P62072.
    GeneWikii TIMM10.
    GenomeRNAii 26519.
    NextBioi 48834.
    PROi P62072.
    SOURCEi Search...

    Gene expression databases

    Bgeei P62072.
    CleanExi HS_TIMM10.
    Genevestigatori P62072.

    Family and domain databases

    Gene3Di 1.10.287.810. 1 hit.
    InterProi IPR004217. Tim10/DDP_fam_Znf.
    IPR027247. Tim10/Tim12.
    [Graphical view ]
    PANTHERi PTHR11038. PTHR11038. 1 hit.
    Pfami PF02953. zf-Tim10_DDP. 1 hit.
    [Graphical view ]
    SUPFAMi SSF144122. SSF144122. 1 hit.
    ProtoNeti Search...

    Publicationsi

    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], TISSUE SPECIFICITY.
    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], TISSUE SPECIFICITY.
    3. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
      Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
      , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
      Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Tissue: Brain.
    4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    5. "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: Brain.
    6. "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: SUBCELLULAR LOCATION.
    7. "Organization and function of the small Tim complexes acting along the import pathway of metabolite carriers into mammalian mitochondria."
      Muehlenbein N., Hofmann S., Rothbauer U., Bauer M.F.
      J. Biol. Chem. 279:13540-13546(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH TIMM9; TIMM22 AND FXC1.
    8. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    9. "Crystal structure of the mitochondrial chaperone TIM9.10 reveals a six-bladed alpha-propeller."
      Webb C.T., Gorman M.A., Lazarou M., Ryan M.T., Gulbis J.M.
      Mol. Cell 21:123-133(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (3.3 ANGSTROMS) IN COMPLEX WITH TIMM9, DISULFIDE BONDS.

    Entry informationi

    Entry nameiTIM10_HUMAN
    AccessioniPrimary (citable) accession number: P62072
    Secondary accession number(s): A8K136
    , Q9WV99, Q9WVA0, Q9Y5J8
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: June 21, 2004
    Last sequence update: June 21, 2004
    Last modified: October 1, 2014
    This is version 99 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

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. Human chromosome 11
      Human chromosome 11: 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. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    4. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3