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Q9Y5J7

- TIM9_HUMAN

UniProt

Q9Y5J7 - TIM9_HUMAN

Protein

Mitochondrial import inner membrane translocase subunit Tim9

Gene

TIMM9

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: ProtInc

    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: Reactome
    5. sensory perception of sound Source: ProtInc

    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 Tim9
    Gene namesi
    Name:TIMM9
    Synonyms:TIM9, TIM9A, TIMM9A
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 14

    Organism-specific databases

    HGNCiHGNC:11819. TIMM9.

    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 intermembrane space Source: BHF-UCL
    3. mitochondrial intermembrane space protein transporter complex Source: BHF-UCL
    4. mitochondrion Source: HPA

    Keywords - Cellular componenti

    Membrane, Mitochondrion, Mitochondrion inner membrane

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA36525.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed1 Publication
    Chaini2 – 8988Mitochondrial import inner membrane translocase subunit Tim9PRO_0000193595Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei2 – 21N-acetylalanine1 Publication
    Disulfide bondi28 ↔ 521 Publication
    Disulfide bondi32 ↔ 481 Publication

    Keywords - PTMi

    Acetylation, Disulfide bond

    Proteomic databases

    MaxQBiQ9Y5J7.
    PaxDbiQ9Y5J7.
    PeptideAtlasiQ9Y5J7.
    PRIDEiQ9Y5J7.

    PTM databases

    PhosphoSiteiQ9Y5J7.

    Expressioni

    Tissue specificityi

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

    Gene expression databases

    ArrayExpressiQ9Y5J7.
    BgeeiQ9Y5J7.
    CleanExiHS_TIMM9.
    GenevestigatoriQ9Y5J7.

    Organism-specific databases

    HPAiHPA002932.

    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
    TIMM10P620724EBI-1200370,EBI-1200391

    Protein-protein interaction databases

    BioGridi117724. 20 interactions.
    IntActiQ9Y5J7. 4 interactions.
    STRINGi9606.ENSP00000216463.

    Structurei

    Secondary structure

    1
    89
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi15 – 3218
    Beta strandi37 – 404
    Helixi43 – 7129
    Beta strandi72 – 754
    Helixi76 – 816

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2BSKX-ray3.30A/C/E1-89[»]
    ProteinModelPortaliQ9Y5J7.
    SMRiQ9Y5J7. Positions 9-87.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ9Y5J7.

    Family & Domainsi

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi28 – 5225Twin 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 TIMM9 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

    eggNOGiNOG242543.
    HOVERGENiHBG083156.
    InParanoidiQ9Y5J7.
    KOiK17777.
    OMAiCCNDFTS.
    OrthoDBiEOG789CF4.
    PhylomeDBiQ9Y5J7.
    TreeFamiTF106192.

    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.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    Q9Y5J7-1 [UniParc]FASTAAdd to Basket

    « Hide

    MAAQIPESDQ IKQFKEFLGT YNKLTETCFL DCVKDFTTRE VKPEETTCSE   50
    HCLQKYLKMT QRISMRFQEY HIQQNEALAA KAGLLGQPR 89
    Length:89
    Mass (Da):10,378
    Last modified:November 1, 1999 - v1
    Checksum:i00F17CF6332ABF48
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF150100 mRNA. Translation: AAD40006.1.
    AF152353 mRNA. Translation: AAF15103.1.
    AK312095 mRNA. Translation: BAG35031.1.
    CH471061 Genomic DNA. Translation: EAW80735.1.
    BC020213 mRNA. Translation: AAH20213.1.
    BC054875 mRNA. Translation: AAH54875.1.
    CCDSiCCDS9735.1.
    PIRiT51191.
    RefSeqiNP_036592.1. NM_012460.2.
    UniGeneiHs.440525.

    Genome annotation databases

    EnsembliENST00000395159; ENSP00000378588; ENSG00000100575.
    ENST00000555061; ENSP00000450638; ENSG00000100575.
    ENST00000555404; ENSP00000451198; ENSG00000100575.
    ENST00000555593; ENSP00000451006; ENSG00000100575.
    GeneIDi26520.
    KEGGihsa:26520.
    UCSCiuc001xds.3. human.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF150100 mRNA. Translation: AAD40006.1 .
    AF152353 mRNA. Translation: AAF15103.1 .
    AK312095 mRNA. Translation: BAG35031.1 .
    CH471061 Genomic DNA. Translation: EAW80735.1 .
    BC020213 mRNA. Translation: AAH20213.1 .
    BC054875 mRNA. Translation: AAH54875.1 .
    CCDSi CCDS9735.1.
    PIRi T51191.
    RefSeqi NP_036592.1. NM_012460.2.
    UniGenei Hs.440525.

    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 A/C/E 1-89 [» ]
    ProteinModelPortali Q9Y5J7.
    SMRi Q9Y5J7. Positions 9-87.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 117724. 20 interactions.
    IntActi Q9Y5J7. 4 interactions.
    STRINGi 9606.ENSP00000216463.

    PTM databases

    PhosphoSitei Q9Y5J7.

    Proteomic databases

    MaxQBi Q9Y5J7.
    PaxDbi Q9Y5J7.
    PeptideAtlasi Q9Y5J7.
    PRIDEi Q9Y5J7.

    Protocols and materials databases

    DNASUi 26520.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000395159 ; ENSP00000378588 ; ENSG00000100575 .
    ENST00000555061 ; ENSP00000450638 ; ENSG00000100575 .
    ENST00000555404 ; ENSP00000451198 ; ENSG00000100575 .
    ENST00000555593 ; ENSP00000451006 ; ENSG00000100575 .
    GeneIDi 26520.
    KEGGi hsa:26520.
    UCSCi uc001xds.3. human.

    Organism-specific databases

    CTDi 26520.
    GeneCardsi GC14M058875.
    HGNCi HGNC:11819. TIMM9.
    HPAi HPA002932.
    MIMi 607384. gene.
    neXtProti NX_Q9Y5J7.
    PharmGKBi PA36525.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG242543.
    HOVERGENi HBG083156.
    InParanoidi Q9Y5J7.
    KOi K17777.
    OMAi CCNDFTS.
    OrthoDBi EOG789CF4.
    PhylomeDBi Q9Y5J7.
    TreeFami TF106192.

    Enzyme and pathway databases

    Reactomei REACT_118595. Mitochondrial protein import.

    Miscellaneous databases

    EvolutionaryTracei Q9Y5J7.
    GeneWikii TIMM9.
    GenomeRNAii 26520.
    NextBioi 48838.
    PROi Q9Y5J7.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q9Y5J7.
    Bgeei Q9Y5J7.
    CleanExi HS_TIMM9.
    Genevestigatori Q9Y5J7.

    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

    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: Hippocampus.
    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: Placenta and Skin.
    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 TIMM10; TIMM22 AND FXC1.
    8. "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 ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
    9. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    10. "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 TIMM10, DISULFIDE BONDS.

    Entry informationi

    Entry nameiTIM9_HUMAN
    AccessioniPrimary (citable) accession number: Q9Y5J7
    Secondary accession number(s): B2R584
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: January 11, 2001
    Last sequence update: November 1, 1999
    Last modified: October 1, 2014
    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

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. Human chromosome 14
      Human chromosome 14: 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