TIM8A_HUMAN
ID TIM8A_HUMAN Reviewed; 97 AA.
AC O60220; B2R5A6; Q6IRW6;
DT 15-JUL-1999, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1998, sequence version 1.
DT 03-AUG-2022, entry version 188.
DE RecName: Full=Mitochondrial import inner membrane translocase subunit Tim8 A;
DE AltName: Full=Deafness dystonia protein 1;
DE AltName: Full=X-linked deafness dystonia protein;
GN Name=TIMM8A; Synonyms=DDP, DDP1, TIM8A;
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=8841189; DOI=10.1038/ng1096-177;
RA Jin H., May M., Tranebjaerg L., Kendall E., Fontan G., Jackson J.,
RA Subramony S.H., Arena F., Lubs H., Smith S., Stevenson R., Schwartz C.,
RA Vetrie D.;
RT "A novel X-linked gene, DDP, shows mutations in families with deafness
RT (DFN-1), dystonia, mental deficiency and blindness.";
RL Nat. Genet. 14:177-180(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Tongue;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15772651; DOI=10.1038/nature03440;
RA Ross M.T., Grafham D.V., Coffey A.J., Scherer S., McLay K., Muzny D.,
RA Platzer M., Howell G.R., Burrows C., Bird C.P., Frankish A., Lovell F.L.,
RA Howe K.L., Ashurst J.L., Fulton R.S., Sudbrak R., Wen G., Jones M.C.,
RA Hurles M.E., Andrews T.D., Scott C.E., Searle S., Ramser J., Whittaker A.,
RA Deadman R., Carter N.P., Hunt S.E., Chen R., Cree A., Gunaratne P.,
RA Havlak P., Hodgson A., Metzker M.L., Richards S., Scott G., Steffen D.,
RA Sodergren E., Wheeler D.A., Worley K.C., Ainscough R., Ambrose K.D.,
RA Ansari-Lari M.A., Aradhya S., Ashwell R.I., Babbage A.K., Bagguley C.L.,
RA Ballabio A., Banerjee R., Barker G.E., Barlow K.F., Barrett I.P.,
RA Bates K.N., Beare D.M., Beasley H., Beasley O., Beck A., Bethel G.,
RA Blechschmidt K., Brady N., Bray-Allen S., Bridgeman A.M., Brown A.J.,
RA Brown M.J., Bonnin D., Bruford E.A., Buhay C., Burch P., Burford D.,
RA Burgess J., Burrill W., Burton J., Bye J.M., Carder C., Carrel L.,
RA Chako J., Chapman J.C., Chavez D., Chen E., Chen G., Chen Y., Chen Z.,
RA Chinault C., Ciccodicola A., Clark S.Y., Clarke G., Clee C.M., Clegg S.,
RA Clerc-Blankenburg K., Clifford K., Cobley V., Cole C.G., Conquer J.S.,
RA Corby N., Connor R.E., David R., Davies J., Davis C., Davis J., Delgado O.,
RA Deshazo D., Dhami P., Ding Y., Dinh H., Dodsworth S., Draper H.,
RA Dugan-Rocha S., Dunham A., Dunn M., Durbin K.J., Dutta I., Eades T.,
RA Ellwood M., Emery-Cohen A., Errington H., Evans K.L., Faulkner L.,
RA Francis F., Frankland J., Fraser A.E., Galgoczy P., Gilbert J., Gill R.,
RA Gloeckner G., Gregory S.G., Gribble S., Griffiths C., Grocock R., Gu Y.,
RA Gwilliam R., Hamilton C., Hart E.A., Hawes A., Heath P.D., Heitmann K.,
RA Hennig S., Hernandez J., Hinzmann B., Ho S., Hoffs M., Howden P.J.,
RA Huckle E.J., Hume J., Hunt P.J., Hunt A.R., Isherwood J., Jacob L.,
RA Johnson D., Jones S., de Jong P.J., Joseph S.S., Keenan S., Kelly S.,
RA Kershaw J.K., Khan Z., Kioschis P., Klages S., Knights A.J., Kosiura A.,
RA Kovar-Smith C., Laird G.K., Langford C., Lawlor S., Leversha M., Lewis L.,
RA Liu W., Lloyd C., Lloyd D.M., Loulseged H., Loveland J.E., Lovell J.D.,
RA Lozado R., Lu J., Lyne R., Ma J., Maheshwari M., Matthews L.H.,
RA McDowall J., McLaren S., McMurray A., Meidl P., Meitinger T., Milne S.,
RA Miner G., Mistry S.L., Morgan M., Morris S., Mueller I., Mullikin J.C.,
RA Nguyen N., Nordsiek G., Nyakatura G., O'dell C.N., Okwuonu G., Palmer S.,
RA Pandian R., Parker D., Parrish J., Pasternak S., Patel D., Pearce A.V.,
RA Pearson D.M., Pelan S.E., Perez L., Porter K.M., Ramsey Y., Reichwald K.,
RA Rhodes S., Ridler K.A., Schlessinger D., Schueler M.G., Sehra H.K.,
RA Shaw-Smith C., Shen H., Sheridan E.M., Shownkeen R., Skuce C.D.,
RA Smith M.L., Sotheran E.C., Steingruber H.E., Steward C.A., Storey R.,
RA Swann R.M., Swarbreck D., Tabor P.E., Taudien S., Taylor T., Teague B.,
RA Thomas K., Thorpe A., Timms K., Tracey A., Trevanion S., Tromans A.C.,
RA d'Urso M., Verduzco D., Villasana D., Waldron L., Wall M., Wang Q.,
RA Warren J., Warry G.L., Wei X., West A., Whitehead S.L., Whiteley M.N.,
RA Wilkinson J.E., Willey D.L., Williams G., Williams L., Williamson A.,
RA Williamson H., Wilming L., Woodmansey R.L., Wray P.W., Yen J., Zhang J.,
RA Zhou J., Zoghbi H., Zorilla S., Buck D., Reinhardt R., Poustka A.,
RA Rosenthal A., Lehrach H., Meindl A., Minx P.J., Hillier L.W., Willard H.F.,
RA Wilson R.K., Waterston R.H., Rice C.M., Vaudin M., Coulson A., Nelson D.L.,
RA Weinstock G., Sulston J.E., Durbin R.M., Hubbard T., Gibbs R.A., Beck S.,
RA Rogers J., Bentley D.R.;
RT "The DNA sequence of the human X chromosome.";
RL Nature 434:325-337(2005).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain, Kidney, and Urinary bladder;
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 [6]
RP PROBABLE FUNCTION.
RX PubMed=10051608; DOI=10.1073/pnas.96.5.2141;
RA Koehler C.M., Leuenberger D., Merchant S., Renold A., Junne T., Schatz G.;
RT "Human deafness dystonia syndrome is a mitochondrial disease.";
RL Proc. Natl. Acad. Sci. U.S.A. 96:2141-2146(1999).
RN [7]
RP PROBABLE FUNCTION.
RX PubMed=10051550; DOI=10.1073/pnas.96.5.1817;
RA Wallace D.C., Murdock D.G.;
RT "Mitochondria and dystonia: the movement disorder connection?";
RL Proc. Natl. Acad. Sci. U.S.A. 96:1817-1819(1999).
RN [8]
RP FUNCTION, SUBCELLULAR LOCATION, ZINC-BINDING, AND INTERACTION WITH TIMM13.
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 [9]
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 [10]
RP INVOLVEMENT IN MTS.
RX PubMed=11803487; DOI=10.1076/opge.22.4.207.2220;
RA Tranebjaerg L., Jensen P.K., Van Ghelue M., Vnencak-Jones C.L., Sund S.,
RA Elgjo K., Jakobsen J., Lindal S., Warburg M., Fuglsang-Frederiksen A.,
RA Skullerud K.;
RT "Neuronal cell death in the visual cortex is a prominent feature of the X-
RT linked recessive mitochondrial deafness-dystonia syndrome caused by
RT mutations in the TIMM8a gene.";
RL Ophthalmic Genet. 22:207-223(2001).
RN [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-94, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [12]
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 [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-96, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T.,
RA Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.;
RT "System-wide temporal characterization of the proteome and phosphoproteome
RT of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [14]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-96, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma, and 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 [15]
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 [16]
RP VARIANT MTS TRP-66.
RX PubMed=10878669; DOI=10.1038/sj.ejhg.5200483;
RA Tranebjaerg L., Hamel B.C.J., Gabreels F.J.M., Renier W.O., Van Ghelue M.;
RT "A de novo missense mutation in a critical domain of the X-linked DDP gene
RT causes the typical deafness-dystonia-optic atrophy syndrome.";
RL Eur. J. Hum. Genet. 8:464-467(2000).
RN [17]
RP VARIANT MTS TRP-66.
RX PubMed=11875042; DOI=10.1093/hmg/11.5.477;
RA Roesch K., Curran S.P., Tranebjaerg L., Koehler C.M.;
RT "Human deafness dystonia syndrome is caused by a defect in assembly of the
RT DDP1/TIMM8a-TIMM13 complex.";
RL Hum. Mol. Genet. 11:477-486(2002).
RN [18]
RP VARIANT MTS TRP-66.
RX PubMed=11956200; DOI=10.1074/jbc.m201154200;
RA Hofmann S., Rothbauer U., Muehlenbein N., Neupert W., Gerbitz K.-D.,
RA Brunner M., Bauer M.F.;
RT "The C66W mutation in the deafness dystonia peptide 1 (DDP1) affects the
RT formation of functional DDP1.TIM13 complexes in the mitochondrial
RT intermembrane space.";
RL J. Biol. Chem. 277:23287-23293(2002).
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 Probably necessary for normal neurologic development.
CC {ECO:0000269|PubMed:11489896, ECO:0000269|PubMed:15254020}.
CC -!- SUBUNIT: Heterohexamer; composed of 3 copies of TIMM8A and 3 copies of
CC TIMM13, named soluble 70 kDa complex. Associates with the TIM22
CC complex, whose core is composed of TIMM22.
CC -!- INTERACTION:
CC O60220; Q99856: ARID3A; NbExp=3; IntAct=EBI-1049822, EBI-5458244;
CC O60220; Q8WUW1: BRK1; NbExp=3; IntAct=EBI-1049822, EBI-2837444;
CC O60220; Q9BXJ5: C1QTNF2; NbExp=3; IntAct=EBI-1049822, EBI-2817707;
CC O60220; Q969G5: CAVIN3; NbExp=3; IntAct=EBI-1049822, EBI-3893101;
CC O60220; P48643: CCT5; NbExp=3; IntAct=EBI-1049822, EBI-355710;
CC O60220; Q53GS7: GLE1; NbExp=3; IntAct=EBI-1049822, EBI-1955541;
CC O60220; P42858: HTT; NbExp=15; IntAct=EBI-1049822, EBI-466029;
CC O60220; P19012: KRT15; NbExp=3; IntAct=EBI-1049822, EBI-739566;
CC O60220; O43482: OIP5; NbExp=3; IntAct=EBI-1049822, EBI-536879;
CC O60220; Q7Z699: SPRED1; NbExp=3; IntAct=EBI-1049822, EBI-5235340;
CC O60220; O75886: STAM2; NbExp=9; IntAct=EBI-1049822, EBI-373258;
CC O60220; Q9Y5L4: TIMM13; NbExp=2; IntAct=EBI-1049822, EBI-1057344;
CC O60220; O60220: TIMM8A; NbExp=6; IntAct=EBI-1049822, EBI-1049822;
CC O60220; O76024: WFS1; NbExp=3; IntAct=EBI-1049822, EBI-720609;
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: Highly expressed in fetal and adult brain, followed
CC by fetal lung, liver and kidney. Also expressed in heart, placenta,
CC lung, liver, kidney, pancreas, skeletal muscle and heart.
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 TIMM8A 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 -!- DISEASE: Mohr-Tranebjaerg syndrome (MTS) [MIM:304700]: An X-linked
CC recessive disorder characterized by postlingual sensorineural deafness
CC with onset in early childhood, dystonia, spasticity, dysphagia, mental
CC deterioration, paranoia and cortical blindness.
CC {ECO:0000269|PubMed:10878669, ECO:0000269|PubMed:11803487,
CC ECO:0000269|PubMed:11875042, ECO:0000269|PubMed:11956200}. Note=The
CC disease is caused by variants affecting the gene represented in this
CC entry.
CC -!- SIMILARITY: Belongs to the small Tim family. {ECO:0000305}.
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DR EMBL; U66035; AAC15946.1; -; mRNA.
DR EMBL; AK312117; BAG35053.1; -; mRNA.
DR EMBL; AL035422; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471115; EAX02854.1; -; Genomic_DNA.
DR EMBL; BC006994; AAH06994.1; -; mRNA.
DR EMBL; BC015093; AAH15093.1; -; mRNA.
DR EMBL; BC070284; AAH70284.1; -; mRNA.
DR CCDS; CCDS14481.1; -.
DR RefSeq; NP_004076.1; NM_004085.3.
DR AlphaFoldDB; O60220; -.
DR SMR; O60220; -.
DR BioGRID; 108042; 81.
DR ComplexPortal; CPX-6131; TIM8A-TIM13 mitochondrial intermembrane space protein transporter complex.
DR CORUM; O60220; -.
DR IntAct; O60220; 52.
DR MINT; O60220; -.
DR STRING; 9606.ENSP00000361993; -.
DR GlyGen; O60220; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; O60220; -.
DR PhosphoSitePlus; O60220; -.
DR BioMuta; TIMM8A; -.
DR EPD; O60220; -.
DR jPOST; O60220; -.
DR MassIVE; O60220; -.
DR MaxQB; O60220; -.
DR PaxDb; O60220; -.
DR PeptideAtlas; O60220; -.
DR PRIDE; O60220; -.
DR ProteomicsDB; 49248; -.
DR TopDownProteomics; O60220; -.
DR Antibodypedia; 584; 140 antibodies from 27 providers.
DR DNASU; 1678; -.
DR Ensembl; ENST00000372902.4; ENSP00000361993.3; ENSG00000126953.8.
DR GeneID; 1678; -.
DR KEGG; hsa:1678; -.
DR MANE-Select; ENST00000372902.4; ENSP00000361993.3; NM_004085.4; NP_004076.1.
DR UCSC; uc004ehd.3; human.
DR CTD; 1678; -.
DR DisGeNET; 1678; -.
DR GeneCards; TIMM8A; -.
DR GeneReviews; TIMM8A; -.
DR HGNC; HGNC:11817; TIMM8A.
DR HPA; ENSG00000126953; Low tissue specificity.
DR MalaCards; TIMM8A; -.
DR MIM; 300356; gene.
DR MIM; 304700; phenotype.
DR neXtProt; NX_O60220; -.
DR OpenTargets; ENSG00000126953; -.
DR Orphanet; 52368; Mohr-Tranebjaerg syndrome.
DR PharmGKB; PA36523; -.
DR VEuPathDB; HostDB:ENSG00000126953; -.
DR eggNOG; KOG3489; Eukaryota.
DR GeneTree; ENSGT00940000154661; -.
DR HOGENOM; CLU_141397_1_2_1; -.
DR InParanoid; O60220; -.
DR OMA; QATQVCL; -.
DR OrthoDB; 1593287at2759; -.
DR PhylomeDB; O60220; -.
DR TreeFam; TF106191; -.
DR PathwayCommons; O60220; -.
DR Reactome; R-HSA-1268020; Mitochondrial protein import.
DR SignaLink; O60220; -.
DR BioGRID-ORCS; 1678; 39 hits in 670 CRISPR screens.
DR ChiTaRS; TIMM8A; human.
DR GeneWiki; TIMM8A; -.
DR GenomeRNAi; 1678; -.
DR Pharos; O60220; Tbio.
DR PRO; PR:O60220; -.
DR Proteomes; UP000005640; Chromosome X.
DR RNAct; O60220; protein.
DR Bgee; ENSG00000126953; Expressed in endothelial cell and 129 other tissues.
DR ExpressionAtlas; O60220; baseline and differential.
DR Genevisible; O60220; HS.
DR GO; GO:0005743; C:mitochondrial inner membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005758; C:mitochondrial intermembrane space; IDA:BHF-UCL.
DR GO; GO:0042719; C:mitochondrial intermembrane space protein transporter complex; IPI:ComplexPortal.
DR GO; GO:0005739; C:mitochondrion; IDA:HPA.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0008270; F:zinc ion binding; IEA:Ensembl.
DR GO; GO:0007399; P:nervous system development; TAS:ProtInc.
DR GO; GO:0045039; P:protein insertion into mitochondrial inner membrane; TAS:BHF-UCL.
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 Chaperone; Deafness; Disease variant; Disulfide bond; Dystonia; Membrane;
KW Metal-binding; Mitochondrion; Mitochondrion inner membrane; Phosphoprotein;
KW Protein transport; Reference proteome; Translocation; Transport; Zinc.
FT CHAIN 1..97
FT /note="Mitochondrial import inner membrane translocase
FT subunit Tim8 A"
FT /id="PRO_0000193584"
FT MOTIF 43..66
FT /note="Twin CX3C motif"
FT MOD_RES 57
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9WVA2"
FT MOD_RES 87
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9WVA2"
FT MOD_RES 94
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 96
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21406692,
FT ECO:0007744|PubMed:23186163"
FT DISULFID 43..66
FT /evidence="ECO:0000250"
FT DISULFID 47..62
FT /evidence="ECO:0000250"
FT VARIANT 66
FT /note="C -> W (in MTS; disrupts the assembly of the
FT heterohexamer with TIMM13; dbSNP:rs80356560)"
FT /evidence="ECO:0000269|PubMed:10878669,
FT ECO:0000269|PubMed:11875042, ECO:0000269|PubMed:11956200"
FT /id="VAR_010237"
FT CONFLICT 62
FT /note="C -> R (in Ref. 5; AAH70284)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 97 AA; 10998 MW; CB72822290F20AB0 CRC64;
MDSSSSSSAA GLGAVDPQLQ HFIEVETQKQ RFQQLVHQMT ELCWEKCMDK PGPKLDSRAE
ACFVNCVERF IDTSQFILNR LEQTQKSKPV FSESLSD
