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Q9Y5J9 (TIM8B_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 119. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Mitochondrial import inner membrane translocase subunit Tim8 B
Alternative name(s):
DDP-like protein
Deafness dystonia protein 2
Gene names
Name:TIMM8B
Synonyms:DDP2, DDPL, TIM8B
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length83 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Probable 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 By similarity.

Subunit structure

Heterohexamer; possibly composed of 3 copies of TIMM8B and 3 copies of TIMM13, named soluble 70 kDa complex. Associates with the TIM22 complex, whose core is composed of TIMM22 By similarity.

Subcellular location

Mitochondrion inner membrane; Peripheral membrane protein; Intermembrane side By similarity.

Tissue specificity

Ubiquitous, with highest expression in heart, kidney, liver and skeletal muscle. 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 TIMM8B from cytoplasm into mitochondrion, the Cys residues probably coordinate zinc, thereby preventing folding and allowing its transfer across mitochondrial outer membrane By similarity.

Sequence similarities

Belongs to the small Tim family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.7
Chain2 – 8382Mitochondrial import inner membrane translocase subunit Tim8 B
PRO_0000193587

Regions

Motif36 – 5924Twin CX3C motif

Amino acid modifications

Modified residue21N-acetylalanine Ref.7 Ref.9 Ref.10
Disulfide bond36 ↔ 59 By similarity
Disulfide bond40 ↔ 55 By similarity

Sequences

Sequence LengthMass (Da)Tools
Q9Y5J9 [UniParc].

Last modified November 1, 1999. Version 1.
Checksum: 9DC47BB475DB8692

FASTA839,344
        10         20         30         40         50         60 
MAELGEADEA ELQRLVAAEQ QKAQFTAQVH HFMELCWDKC VEKPGNRLDS RTENCLSSCV 

        70         80 
DRFIDTTLAI TSRFAQIVQK GGQ 

« Hide

References

« Hide 'large scale' references
[1]"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].
[2]"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.
[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: Brain.
[4]NHLBI resequencing and genotyping service (RS&G)
Submitted (FEB-2007) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [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: Lung, Mammary gland and Testis.
[6]"Molecular cloning of DDP-like gene."
Xia J.-H., He Y.-G., Yu K.-P., Zheng Z.-H., Tan S.
Submitted (JUL-1999) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 33-83.
Tissue: Heart.
[7]"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].
[8]"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].
[9]"Comparative large-scale characterisation of plant vs. mammal proteins reveals similar and idiosyncratic N-alpha acetylation features."
Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T., Giglione C.
Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[10]"N-terminal acetylome analyses and functional insights of the N-terminal acetyltransferase NatB."
Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A., Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF152350 mRNA. Translation: AAF15100.1.
AF150087 mRNA. Translation: AAD39994.1.
AK312169 mRNA. Translation: BAG35103.1.
EF445036 Genomic DNA. Translation: ACA06083.1.
BC000711 mRNA. Translation: AAH00711.1.
BC105986 mRNA. Translation: AAI05987.1.
BC106067 mRNA. Translation: AAI06068.1.
AF165967 mRNA. Translation: AAD51801.1.
RefSeqNP_036591.2. NM_012459.2.
UniGeneHs.279915.

3D structure databases

ProteinModelPortalQ9Y5J9.
SMRQ9Y5J9. Positions 20-72.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid117725. 6 interactions.
IntActQ9Y5J9. 3 interactions.
STRING9606.ENSP00000280354.

PTM databases

PhosphoSiteQ9Y5J9.

Proteomic databases

MaxQBQ9Y5J9.
PaxDbQ9Y5J9.
PeptideAtlasQ9Y5J9.
PRIDEQ9Y5J9.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000504148; ENSP00000422122; ENSG00000150779.
GeneID26521.
KEGGhsa:26521.

Organism-specific databases

CTD26521.
GeneCardsGC11M111989.
H-InvDBHIX0201613.
HGNCHGNC:11818. TIMM8B.
HPAHPA041173.
MIM606659. gene.
neXtProtNX_Q9Y5J9.
PharmGKBPA36524.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG238740.
HOGENOMHOG000115758.
HOVERGENHBG060492.
InParanoidQ9Y5J9.
KOK17780.
OrthoDBEOG79W97P.
PhylomeDBQ9Y5J9.

Enzyme and pathway databases

ReactomeREACT_17015. Metabolism of proteins.

Gene expression databases

ArrayExpressQ9Y5J9.
BgeeQ9Y5J9.
CleanExHS_TIMM8B.
GenevestigatorQ9Y5J9.

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

GenomeRNAi26521.
NextBio48842.
PROQ9Y5J9.
SOURCESearch...

Entry information

Entry nameTIM8B_HUMAN
AccessionPrimary (citable) accession number: Q9Y5J9
Secondary accession number(s): B0YJA5, Q3KQS9, Q9UN04
Entry history
Integrated into UniProtKB/Swiss-Prot: January 11, 2001
Last sequence update: November 1, 1999
Last modified: May 14, 2014
This is version 119 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

MIM cross-references

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

Human chromosome 11

Human chromosome 11: entries, gene names and cross-references to MIM