TIM13_HUMAN
ID TIM13_HUMAN Reviewed; 95 AA.
AC Q9Y5L4; P62206; Q9UHL8; Q9WTL1;
DT 11-JAN-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1999, sequence version 1.
DT 03-AUG-2022, entry version 181.
DE RecName: Full=Mitochondrial import inner membrane translocase subunit Tim13;
GN Name=TIMM13; Synonyms=TIM13B, TIMM13A, TIMM13B;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=10611480; DOI=10.1016/s0014-5793(99)01665-8;
RA Bauer M.F., Rothbauer U., Muehlenbein N., Smith R.J.H., Gerbitz K.-D.,
RA Neupert W., Brunner M., Hofmann S.;
RT "The mitochondrial TIM22 preprotein translocase is highly conserved
RT throughout the eukaryotic kingdom.";
RL FEBS Lett. 464:41-47(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=10552927; DOI=10.1006/geno.1999.5966;
RA Jin H., Kendall E., Freeman T.C., Roberts R.G., Vetrie D.L.P.;
RT "The human family of deafness/dystonia peptide (DDP) related mitochondrial
RT import proteins.";
RL Genomics 61:259-267(1999).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Placenta;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [4]
RP FUNCTION, SUBCELLULAR LOCATION, ZINC-BINDING, AND INTERACTION WITH TIMM8A.
RX PubMed=11489896; DOI=10.1074/jbc.m105313200;
RA Rothbauer U., Hofmann S., Muehlenbein N., Paschen S.A., Gerbitz K.-D.,
RA Neupert W., Brunner M., Bauer M.F.;
RT "Role of the deafness dystonia peptide 1 (DDP1) in import of human Tim23
RT into the inner membrane of mitochondria.";
RL J. Biol. Chem. 276:37327-37334(2001).
RN [5]
RP FUNCTION.
RX PubMed=15254020; DOI=10.1093/hmg/ddh217;
RA Roesch K., Hynds P.J., Varga R., Tranebjaerg L., Koehler C.M.;
RT "The calcium-binding aspartate/glutamate carriers, citrin and aralar1, are
RT new substrates for the DDP1/TIMM8a-TIMM13 complex.";
RL Hum. Mol. Genet. 13:2101-2111(2004).
RN [6]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a
RT refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [7]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-7, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [9]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [10]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25944712; DOI=10.1002/pmic.201400617;
RA Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., Ayoub D.,
RA Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
RT "N-terminome analysis of the human mitochondrial proteome.";
RL Proteomics 15:2519-2524(2015).
CC -!- FUNCTION: Mitochondrial intermembrane chaperone that participates in
CC the import and insertion of some multi-pass transmembrane proteins into
CC the mitochondrial inner membrane. Also required for the transfer of
CC beta-barrel precursors from the TOM complex to the sorting and assembly
CC machinery (SAM complex) of the outer membrane. Acts as a chaperone-like
CC protein that protects the hydrophobic precursors from aggregation and
CC guide them through the mitochondrial intermembrane space. The TIMM8-
CC TIMM13 complex mediates the import of proteins such as TIMM23,
CC SLC25A12/ARALAR1 and SLC25A13/ARALAR2, while the predominant TIMM9-
CC TIMM10 70 kDa complex mediates the import of much more proteins.
CC {ECO:0000269|PubMed:11489896, ECO:0000269|PubMed:15254020}.
CC -!- SUBUNIT: Heterohexamer; composed of 3 copies of TIMM8 (TIMM8A or
CC TIMM8B) and 3 copies of TIMM13, named soluble 70 kDa complex.
CC Associates with the TIM22 complex, whose core is composed of TIMM22.
CC -!- INTERACTION:
CC Q9Y5L4; O60220: TIMM8A; NbExp=2; IntAct=EBI-1057344, EBI-1049822;
CC Q9Y5L4; Q8N6Y0: USHBP1; NbExp=3; IntAct=EBI-1057344, EBI-739895;
CC -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane
CC {ECO:0000269|PubMed:11489896}; Peripheral membrane protein
CC {ECO:0000269|PubMed:11489896}; Intermembrane side
CC {ECO:0000269|PubMed:11489896}.
CC -!- TISSUE SPECIFICITY: Ubiquitous, with highest expression in heart,
CC kidney, liver and skeletal muscle.
CC -!- DOMAIN: The twin CX3C motif contains 4 conserved Cys residues that form
CC 2 disulfide bonds in the mitochondrial intermembrane space. However,
CC during the transit of TIMM13 from cytoplasm into mitochondrion, the Cys
CC residues probably coordinate zinc, thereby preventing folding and
CC allowing its transfer across mitochondrial outer membrane (By
CC similarity). {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the small Tim family. {ECO:0000305}.
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DR EMBL; AF144700; AAD39951.1; -; mRNA.
DR EMBL; AF152351; AAF15101.1; -; mRNA.
DR EMBL; AF152352; AAF15102.1; -; mRNA.
DR EMBL; BC008607; AAH08607.1; -; mRNA.
DR CCDS; CCDS12089.1; -.
DR RefSeq; NP_036590.1; NM_012458.3.
DR AlphaFoldDB; Q9Y5L4; -.
DR SMR; Q9Y5L4; -.
DR BioGRID; 117722; 154.
DR ComplexPortal; CPX-6131; TIM8A-TIM13 mitochondrial intermembrane space protein transporter complex.
DR ComplexPortal; CPX-6132; TIM8B-TIM13 mitochondrial intermembrane space protein transporter complex.
DR CORUM; Q9Y5L4; -.
DR IntAct; Q9Y5L4; 102.
DR MINT; Q9Y5L4; -.
DR STRING; 9606.ENSP00000215570; -.
DR iPTMnet; Q9Y5L4; -.
DR MetOSite; Q9Y5L4; -.
DR PhosphoSitePlus; Q9Y5L4; -.
DR BioMuta; TIMM13; -.
DR EPD; Q9Y5L4; -.
DR jPOST; Q9Y5L4; -.
DR MassIVE; Q9Y5L4; -.
DR MaxQB; Q9Y5L4; -.
DR PaxDb; Q9Y5L4; -.
DR PeptideAtlas; Q9Y5L4; -.
DR PRIDE; Q9Y5L4; -.
DR ProteomicsDB; 86442; -.
DR TopDownProteomics; Q9Y5L4; -.
DR Antibodypedia; 23013; 52 antibodies from 18 providers.
DR DNASU; 26517; -.
DR Ensembl; ENST00000215570.8; ENSP00000215570.2; ENSG00000099800.8.
DR GeneID; 26517; -.
DR KEGG; hsa:26517; -.
DR MANE-Select; ENST00000215570.8; ENSP00000215570.2; NM_012458.4; NP_036590.1.
DR UCSC; uc002lvx.3; human.
DR CTD; 26517; -.
DR DisGeNET; 26517; -.
DR GeneCards; TIMM13; -.
DR HGNC; HGNC:11816; TIMM13.
DR HPA; ENSG00000099800; Low tissue specificity.
DR MIM; 607383; gene.
DR neXtProt; NX_Q9Y5L4; -.
DR OpenTargets; ENSG00000099800; -.
DR PharmGKB; PA36522; -.
DR VEuPathDB; HostDB:ENSG00000099800; -.
DR eggNOG; KOG1733; Eukaryota.
DR GeneTree; ENSGT00390000014000; -.
DR HOGENOM; CLU_141397_0_2_1; -.
DR InParanoid; Q9Y5L4; -.
DR OMA; MAAWNQV; -.
DR OrthoDB; 1566384at2759; -.
DR PhylomeDB; Q9Y5L4; -.
DR TreeFam; TF106194; -.
DR PathwayCommons; Q9Y5L4; -.
DR Reactome; R-HSA-1268020; Mitochondrial protein import.
DR SignaLink; Q9Y5L4; -.
DR BioGRID-ORCS; 26517; 693 hits in 1087 CRISPR screens.
DR ChiTaRS; TIMM13; human.
DR GeneWiki; TIMM13; -.
DR GenomeRNAi; 26517; -.
DR Pharos; Q9Y5L4; Tdark.
DR PRO; PR:Q9Y5L4; -.
DR Proteomes; UP000005640; Chromosome 19.
DR RNAct; Q9Y5L4; protein.
DR Bgee; ENSG00000099800; Expressed in mucosa of transverse colon and 98 other tissues.
DR ExpressionAtlas; Q9Y5L4; baseline and differential.
DR Genevisible; Q9Y5L4; HS.
DR GO; GO:0001650; C:fibrillar center; IDA:HPA.
DR GO; GO:0005743; C:mitochondrial inner membrane; IDA:CAFA.
DR GO; GO:0005758; C:mitochondrial intermembrane space; IC:ComplexPortal.
DR GO; GO:0042719; C:mitochondrial intermembrane space protein transporter complex; IPI:ComplexPortal.
DR GO; GO:0005739; C:mitochondrion; IDA:HPA.
DR GO; GO:0008270; F:zinc ion binding; TAS:ProtInc.
DR GO; GO:0045039; P:protein insertion into mitochondrial inner membrane; IBA:GO_Central.
DR GO; GO:0006626; P:protein targeting to mitochondrion; TAS:ProtInc.
DR GO; GO:0007605; P:sensory perception of sound; TAS:ProtInc.
DR Gene3D; 1.10.287.810; -; 1.
DR InterPro; IPR004217; Tim10-like.
DR InterPro; IPR035427; Tim10-like_dom_sf.
DR InterPro; IPR039238; Tim8/13.
DR PANTHER; PTHR19338; PTHR19338; 1.
DR Pfam; PF02953; zf-Tim10_DDP; 1.
DR SUPFAM; SSF144122; SSF144122; 1.
PE 1: Evidence at protein level;
KW Acetylation; Chaperone; Disulfide bond; Membrane; Metal-binding;
KW Mitochondrion; Mitochondrion inner membrane; Phosphoprotein;
KW Protein transport; Reference proteome; Translocation; Transport; Zinc.
FT CHAIN 1..95
FT /note="Mitochondrial import inner membrane translocase
FT subunit Tim13"
FT /id="PRO_0000193623"
FT MOTIF 46..69
FT /note="Twin CX3C motif"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0007744|PubMed:19413330,
FT ECO:0007744|PubMed:25944712"
FT MOD_RES 7
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 53
FT /note="N6-succinyllysine"
FT /evidence="ECO:0000250|UniProtKB:P62075"
FT DISULFID 46..69
FT /evidence="ECO:0000250"
FT DISULFID 50..65
FT /evidence="ECO:0000250"
FT CONFLICT 2..3
FT /note="EG -> DS (in Ref. 2; AAF15101)"
FT /evidence="ECO:0000305"
FT CONFLICT 12..14
FT /note="SGS -> TGG (in Ref. 2; AAF15101)"
FT /evidence="ECO:0000305"
FT CONFLICT 21
FT /note="L -> A (in Ref. 2; AAF15101)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 95 AA; 10500 MW; E40E742C7CA55834 CRC64;
MEGGFGSDFG GSGSGKLDPG LIMEQVKVQI AVANAQELLQ RMTDKCFRKC IGKPGGSLDN
SEQKCIAMCM DRYMDAWNTV SRAYNSRLQR ERANM
