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Q9Y5J7 (TIM9_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 127. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Mitochondrial import inner membrane translocase subunit Tim9
Gene names
Name:TIMM9
Synonyms:TIM9, TIM9A, TIMM9A
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length89 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. Ref.7

Subunit structure

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. Ref.7

Subcellular location

Mitochondrion inner membrane; Peripheral membrane protein; Intermembrane side Ref.6 Ref.7.

Tissue specificity

Ubiquitous, with highest expression in heart, kidney, liver and skeletal muscle. Ref.1 Ref.2

Domain

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.

Sequence similarities

Belongs to the small Tim family.

Ontologies

Keywords
   Biological processProtein transport
Translocation
Transport
   Cellular componentMembrane
Mitochondrion
Mitochondrion inner membrane
   LigandMetal-binding
Zinc
   Molecular functionChaperone
   PTMAcetylation
Disulfide bond
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processcellular protein metabolic process

Traceable author statement. Source: Reactome

chaperone-mediated protein transport

Inferred from direct assay Ref.10. Source: BHF-UCL

protein import into mitochondrial inner membrane

Inferred from direct assay Ref.10. Source: BHF-UCL

protein targeting to mitochondrion

Traceable author statement. Source: Reactome

sensory perception of sound

Traceable author statement Ref.2. Source: ProtInc

   Cellular_componentmitochondrial inner membrane

Inferred from direct assay Ref.7. Source: BHF-UCL

mitochondrial intermembrane space

Traceable author statement Ref.7. Source: BHF-UCL

mitochondrial intermembrane space protein transporter complex

Inferred from direct assay Ref.7. Source: BHF-UCL

mitochondrion

Inferred from direct assay. Source: HPA

   Molecular_functionchaperone binding

Inferred from physical interaction Ref.10. Source: BHF-UCL

protein binding

Inferred from physical interaction Ref.7. Source: IntAct

protein homodimerization activity

Inferred from physical interaction Ref.10. Source: BHF-UCL

transporter activity

Inferred from direct assay Ref.10. Source: BHF-UCL

zinc ion binding

Traceable author statement Ref.2. Source: ProtInc

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

TIMM10P620724EBI-1200370,EBI-1200391

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.8
Chain2 – 8988Mitochondrial import inner membrane translocase subunit Tim9
PRO_0000193595

Regions

Motif28 – 5225Twin CX3C motif

Amino acid modifications

Modified residue21N-acetylalanine Ref.8
Disulfide bond28 ↔ 52 Ref.10
Disulfide bond32 ↔ 48 Ref.10

Secondary structure

......... 89
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q9Y5J7 [UniParc].

Last modified November 1, 1999. Version 1.
Checksum: 00F17CF6332ABF48

FASTA8910,378
        10         20         30         40         50         60 
MAAQIPESDQ IKQFKEFLGT YNKLTETCFL DCVKDFTTRE VKPEETTCSE HCLQKYLKMT 

        70         80 
QRISMRFQEY HIQQNEALAA KAGLLGQPR 

« Hide

References

« Hide 'large scale' references
[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. expand/collapse author list , 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]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
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]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
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.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
CCDSCCDS9735.1.
PIRT51191.
RefSeqNP_036592.1. NM_012460.2.
UniGeneHs.440525.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2BSKX-ray3.30A/C/E1-89[»]
ProteinModelPortalQ9Y5J7.
SMRQ9Y5J7. Positions 9-87.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid117724. 20 interactions.
IntActQ9Y5J7. 4 interactions.
STRING9606.ENSP00000216463.

PTM databases

PhosphoSiteQ9Y5J7.

Proteomic databases

MaxQBQ9Y5J7.
PaxDbQ9Y5J7.
PeptideAtlasQ9Y5J7.
PRIDEQ9Y5J7.

Protocols and materials databases

DNASU26520.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000395159; ENSP00000378588; ENSG00000100575.
ENST00000555061; ENSP00000450638; ENSG00000100575.
ENST00000555404; ENSP00000451198; ENSG00000100575.
ENST00000555593; ENSP00000451006; ENSG00000100575.
GeneID26520.
KEGGhsa:26520.
UCSCuc001xds.3. human.

Organism-specific databases

CTD26520.
GeneCardsGC14M058875.
HGNCHGNC:11819. TIMM9.
HPAHPA002932.
MIM607384. gene.
neXtProtNX_Q9Y5J7.
PharmGKBPA36525.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG242543.
HOVERGENHBG083156.
InParanoidQ9Y5J7.
KOK17777.
OMACCNDFTS.
OrthoDBEOG789CF4.
PhylomeDBQ9Y5J7.
TreeFamTF106192.

Enzyme and pathway databases

ReactomeREACT_17015. Metabolism of proteins.

Gene expression databases

ArrayExpressQ9Y5J7.
BgeeQ9Y5J7.
CleanExHS_TIMM9.
GenevestigatorQ9Y5J7.

Family and domain databases

Gene3D1.10.287.810. 1 hit.
InterProIPR004217. Tim10/DDP_fam_Znf.
[Graphical view]
PfamPF02953. zf-Tim10_DDP. 1 hit.
[Graphical view]
SUPFAMSSF144122. SSF144122. 1 hit.
ProtoNetSearch...

Other

EvolutionaryTraceQ9Y5J7.
GeneWikiTIMM9.
GenomeRNAi26520.
NextBio48838.
PROQ9Y5J7.
SOURCESearch...

Entry information

Entry nameTIM9_HUMAN
AccessionPrimary (citable) accession number: Q9Y5J7
Secondary accession number(s): B2R584
Entry history
Integrated into UniProtKB/Swiss-Prot: January 11, 2001
Last sequence update: November 1, 1999
Last modified: July 9, 2014
This is version 127 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human chromosome 14

Human chromosome 14: entries, gene names and cross-references to MIM