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P62075

- TIM13_MOUSE

UniProt

P62075 - TIM13_MOUSE

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Protein

Mitochondrial import inner membrane translocase subunit Tim13

Gene

Timm13

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 3 out of 5- Experimental evidence at protein leveli

Functioni

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. The TIMM8-TIMM13 complex mediates the import of proteins such as TIMM23, SLC25A12/ARALAR1 and SLC25A13/ARALAR2, while the predominant TIMM9-TIMM10 70 kDa complex mediates the import of much more proteins (By similarity).By similarity

GO - Molecular functioni

  1. metal ion binding Source: UniProtKB-KW

GO - Biological processi

  1. protein transport Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Chaperone

Keywords - Biological processi

Protein transport, Translocation, Transport

Keywords - Ligandi

Metal-binding, Zinc

Enzyme and pathway databases

ReactomeiREACT_199101. Mitochondrial protein import.

Names & Taxonomyi

Protein namesi
Recommended name:
Mitochondrial import inner membrane translocase subunit Tim13
Gene namesi
Name:Timm13
Synonyms:Tim13a, Timm13a
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Chromosome 10

Organism-specific databases

MGIiMGI:1353432. Timm13.

Subcellular locationi

GO - Cellular componenti

  1. mitochondrial inner membrane Source: UniProtKB-KW
  2. mitochondrion Source: MGI
  3. nucleolus Source: Ensembl
Complete GO annotation...

Keywords - Cellular componenti

Membrane, Mitochondrion, Mitochondrion inner membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 9595Mitochondrial import inner membrane translocase subunit Tim13PRO_0000193624Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei1 – 11N-acetylmethionineBy similarity
Disulfide bondi46 ↔ 69By similarity
Disulfide bondi50 ↔ 65By similarity
Modified residuei53 – 531N6-succinyllysine1 Publication

Keywords - PTMi

Acetylation, Disulfide bond

Proteomic databases

MaxQBiP62075.
PaxDbiP62075.
PRIDEiP62075.

PTM databases

PhosphoSiteiP62075.

Expressioni

Tissue specificityi

Present at high level in liver and brain, and at lower level in muscle and heart. In CNS sections, it is predominantly present in the soma and the dendritic portion of the Purkinje cells of the cerebellum, but not in the glial cells. Scattered expression also is also detected in the brain stem, olfactory bulb, substantia nigra, hippocampus and striatum (at protein level).1 Publication

Gene expression databases

BgeeiP62075.
GenevestigatoriP62075.

Interactioni

Subunit structurei

Heterohexamer; composed of 3 copies of TIMM8 (TIMM8A or TIMM8B) and 3 copies of TIMM13, named soluble 70 kDa complex. Associates with the TIM22 complex, whose core is composed of TIMM22 (By similarity).By similarity

Protein-protein interaction databases

IntActiP62075. 2 interactions.
MINTiMINT-4996911.

Structurei

3D structure databases

ProteinModelPortaliP62075.
SMRiP62075. Positions 35-89.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi46 – 6924Twin 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 TIMM13 from cytoplasm into mitochondrion, the Cys residues probably coordinate zinc, thereby preventing folding and allowing its transfer across mitochondrial outer membrane (By similarity).By similarity

Sequence similaritiesi

Belongs to the small Tim family.Curated

Phylogenomic databases

eggNOGiNOG246901.
GeneTreeiENSGT00390000014000.
HOGENOMiHOG000115759.
HOVERGENiHBG079645.
InParanoidiP62075.
KOiK17781.
OMAiGSEETCL.
OrthoDBiEOG7Q8CQP.
PhylomeDBiP62075.
TreeFamiTF106194.

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.

P62075-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MDSGFGSDFG GTGGGKLDPG AIMEQVKVQI AVANAQELLQ RMTDKCFRKC
60 70 80 90
IGKPGGSLDN SEQKCIAMCM DRYMDAWNTV SRAYNSRLQR ERANM
Length:95
Mass (Da):10,458
Last modified:June 21, 2004 - v1
Checksum:iF9A50A2E7F6E64C8
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti3 – 31S → G in BAB22536. (PubMed:16141072)Curated
Sequence conflicti18 – 181D → S in AAH11436. (PubMed:15489334)Curated

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AF144702 mRNA. Translation: AAD39953.1.
AK003054 mRNA. Translation: BAB22536.1.
AK009041 mRNA. Translation: BAB26042.1.
AK009152 mRNA. Translation: BAB26109.1.
AK013230 mRNA. Translation: BAB28728.1.
AK088984 mRNA. Translation: BAC40687.1.
BC011436 mRNA. Translation: AAH11436.1.
CCDSiCCDS35989.1.
RefSeqiNP_038923.1. NM_013895.4.
UniGeneiMm.142132.

Genome annotation databases

EnsembliENSMUST00000020440; ENSMUSP00000020440; ENSMUSG00000020219.
GeneIDi30055.
KEGGimmu:30055.
UCSCiuc007gfi.2. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AF144702 mRNA. Translation: AAD39953.1 .
AK003054 mRNA. Translation: BAB22536.1 .
AK009041 mRNA. Translation: BAB26042.1 .
AK009152 mRNA. Translation: BAB26109.1 .
AK013230 mRNA. Translation: BAB28728.1 .
AK088984 mRNA. Translation: BAC40687.1 .
BC011436 mRNA. Translation: AAH11436.1 .
CCDSi CCDS35989.1.
RefSeqi NP_038923.1. NM_013895.4.
UniGenei Mm.142132.

3D structure databases

ProteinModelPortali P62075.
SMRi P62075. Positions 35-89.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

IntActi P62075. 2 interactions.
MINTi MINT-4996911.

PTM databases

PhosphoSitei P62075.

Proteomic databases

MaxQBi P62075.
PaxDbi P62075.
PRIDEi P62075.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSMUST00000020440 ; ENSMUSP00000020440 ; ENSMUSG00000020219 .
GeneIDi 30055.
KEGGi mmu:30055.
UCSCi uc007gfi.2. mouse.

Organism-specific databases

CTDi 26517.
MGIi MGI:1353432. Timm13.

Phylogenomic databases

eggNOGi NOG246901.
GeneTreei ENSGT00390000014000.
HOGENOMi HOG000115759.
HOVERGENi HBG079645.
InParanoidi P62075.
KOi K17781.
OMAi GSEETCL.
OrthoDBi EOG7Q8CQP.
PhylomeDBi P62075.
TreeFami TF106194.

Enzyme and pathway databases

Reactomei REACT_199101. Mitochondrial protein import.

Miscellaneous databases

NextBioi 307174.
PROi P62075.
SOURCEi Search...

Gene expression databases

Bgeei P62075.
Genevestigatori P62075.

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

« 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].
  2. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: C57BL/6J and NOD.
    Tissue: Brain, Thymus and Tongue.
  3. "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: Mammary tumor.
  4. Lubec G., Kang S.U.
    Submitted (APR-2007) to UniProtKB
    Cited for: PROTEIN SEQUENCE OF 28-41 AND 50-64, IDENTIFICATION BY MASS SPECTROMETRY.
    Strain: C57BL/6.
    Tissue: Brain.
  5. "The calcium-binding aspartate/glutamate carriers, citrin and aralar1, are new substrates for the DDP1/TIMM8a-TIMM13 complex."
    Roesch K., Hynds P.J., Varga R., Tranebjaerg L., Koehler C.M.
    Hum. Mol. Genet. 13:2101-2111(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: TISSUE SPECIFICITY.
  6. "SIRT5-mediated lysine desuccinylation impacts diverse metabolic pathways."
    Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y., Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.
    Mol. Cell 50:919-930(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUCCINYLATION [LARGE SCALE ANALYSIS] AT LYS-53, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.

Entry informationi

Entry nameiTIM13_MOUSE
AccessioniPrimary (citable) accession number: P62075
Secondary accession number(s): Q91VM6
, Q9DC89, Q9UHL8, Q9WTL1
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 21, 2004
Last sequence update: June 21, 2004
Last modified: October 29, 2014
This is version 96 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3