Q9Y5J9 (TIM8B_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended 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

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	83 AA.
Sequence status	Complete.
Protein existence	Evidence 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.

Ontologies

Keywords
Biological process	Protein transport Translocation Transport
Cellular component	Membrane Mitochondrion Mitochondrion inner membrane
Ligand	Metal-binding Zinc
Molecular function	Chaperone
PTM	Disulfide bond
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	cellular protein metabolic process Traceable author statement. Source: Reactome chaperone-mediated protein transport Traceable author statement PubMed 16387659. Source: BHF-UCL protein targeting to mitochondrion Traceable author statement. Source: Reactome sensory perception of sound Traceable author statement Ref.1. Source: ProtInc
Cellular_component	mitochondrial inner membrane Inferred from electronic annotation. Source: UniProtKB-SubCell mitochondrial intermembrane space protein transporter complex Traceable author statement Ref.1. Source: BHF-UCL
Molecular_function	zinc ion binding Traceable author statement Ref.1. Source: ProtInc
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 83	83	Mitochondrial import inner membrane translocase subunit Tim8 B		PRO_0000193587
Regions
	Motif	36 – 59	24	Twin CX3C motif
Amino acid modifications
	Disulfide bond	36 ↔ 59		By similarity
	Disulfide bond	40 ↔ 55		By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q9Y5J9 [UniParc]. Last modified November 1, 1999. Version 1. Checksum: 9DC47BB475DB8692	FASTA	83	9,344
	10 20 30 40 50 60 MAELGEADEA ELQRLVAAEQ QKAQFTAQVH HFMELCWDKC VEKPGNRLDS RTENCLSSCV 70 80 DRFIDTTLAI TSRFAQIVQK GGQ

References

	« Hide 'large scale' referencesShow '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. , 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]	"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].
+	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.
IPI	IPI01015642.
RefSeq	NP_036591.2. NM_012459.2.
UniGene	Hs.279915.
3D structure databases
ProteinModelPortal	Q9Y5J9.
ModBase	Search...
Protein-protein interaction databases
IntAct	Q9Y5J9. 3 interactions.
STRING	9606.ENSP00000280354.
PTM databases
PhosphoSite	Q9Y5J9.
Polymorphism databases
DMDM	12643955.
Proteomic databases
PaxDb	Q9Y5J9.
PeptideAtlas	Q9Y5J9.
PRIDE	Q9Y5J9.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000504148; ENSP00000422122; ENSG00000150779.
GeneID	26521.
KEGG	hsa:26521.
UCSC	uc001pmx.3. human.
Organism-specific databases
CTD	26521.
GeneCards	GC11M111989.
H-InvDB	HIX0201613.
HGNC	HGNC:11818. TIMM8B.
HPA	HPA041173.
MIM	606659. gene.
neXtProt	NX_Q9Y5J9.
PharmGKB	PA36524.
GenAtlas	Search...
Phylogenomic databases
eggNOG	NOG238740.
HOGENOM	HOG000115758.
HOVERGEN	HBG060492.
InParanoid	Q9Y5J9.
OrthoDB	EOG4ZCT65.
PhylomeDB	Q9Y5J9.
Enzyme and pathway databases
Reactome	REACT_17015. Metabolism of proteins.
Gene expression databases
ArrayExpress	Q9Y5J9.
Bgee	Q9Y5J9.
CleanEx	HS_TIMM8B.
Genevestigator	Q9Y5J9.
GermOnline	ENSG00000150779. Homo sapiens.
Family and domain databases
Gene3D	1.10.287.810. 1 hit.
InterPro	IPR004217. Tim10/DDP_fam_Znf. [Graphical view]
Pfam	PF02953. zf-Tim10_DDP. 1 hit. [Graphical view]
SUPFAM	SSF144122. SSF144122. 1 hit.
ProtoNet	Search...
Other
GenomeRNAi	26521.
NextBio	48842.
SOURCE	Search...

Entry information

Entry name

TIM8B_HUMAN

Accession

Primary (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 1, 2013
This is version 110 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.