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Protein

Mitochondrial import inner membrane translocase subunit Tim9

Gene

TIMM9

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 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 homodimerization activity Source: BHF-UCL
  3. transporter activity Source: BHF-UCL
  4. 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
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 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
Complete GO annotation...

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

BgeeiQ9Y5J7.
CleanExiHS_TIMM9.
ExpressionAtlasiQ9Y5J7. baseline and differential.
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. 19 interactions.
IntActiQ9Y5J7. 4 interactions.
STRINGi9606.ENSP00000216463.

Structurei

Secondary structure

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

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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.
GeneTreeiENSGT00450000040278.
HOVERGENiHBG083156.
InParanoidiQ9Y5J7.
KOiK17777.
OMAiSNLVERC.
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

        10         20         30         40         50
MAAQIPESDQ IKQFKEFLGT YNKLTETCFL DCVKDFTTRE VKPEETTCSE
60 70 80
HCLQKYLKMT QRISMRFQEY HIQQNEALAA KAGLLGQPR
Length:89
Mass (Da):10,378
Last modified:November 1, 1999 - v1
Checksum:i00F17CF6332ABF48
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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:
EMBLi
GenBanki
DDBJi
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.

3D structure databases

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

Protein-protein interaction databases

BioGridi117724. 19 interactions.
IntActiQ9Y5J7. 4 interactions.
STRINGi9606.ENSP00000216463.

PTM databases

PhosphoSiteiQ9Y5J7.

Proteomic databases

MaxQBiQ9Y5J7.
PaxDbiQ9Y5J7.
PeptideAtlasiQ9Y5J7.
PRIDEiQ9Y5J7.

Protocols and materials databases

DNASUi26520.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

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

Organism-specific databases

CTDi26520.
GeneCardsiGC14M058875.
HGNCiHGNC:11819. TIMM9.
HPAiHPA002932.
MIMi607384. gene.
neXtProtiNX_Q9Y5J7.
PharmGKBiPA36525.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiNOG242543.
GeneTreeiENSGT00450000040278.
HOVERGENiHBG083156.
InParanoidiQ9Y5J7.
KOiK17777.
OMAiSNLVERC.
OrthoDBiEOG789CF4.
PhylomeDBiQ9Y5J7.
TreeFamiTF106192.

Enzyme and pathway databases

ReactomeiREACT_118595. Mitochondrial protein import.

Miscellaneous databases

ChiTaRSiTIMM9. human.
EvolutionaryTraceiQ9Y5J7.
GeneWikiiTIMM9.
GenomeRNAii26520.
NextBioi48838.
PROiQ9Y5J7.
SOURCEiSearch...

Gene expression databases

BgeeiQ9Y5J7.
CleanExiHS_TIMM9.
ExpressionAtlasiQ9Y5J7. baseline and differential.
GenevestigatoriQ9Y5J7.

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], 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: January 7, 2015
This is version 132 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

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.