TOM20_HUMAN
ID TOM20_HUMAN Reviewed; 145 AA.
AC Q15388; A8K195; Q498B3; Q6IBT4;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 199.
DE RecName: Full=Mitochondrial import receptor subunit TOM20 homolog;
DE AltName: Full=Mitochondrial 20 kDa outer membrane protein;
DE AltName: Full=Outer mitochondrial membrane receptor Tom20;
GN Name=TOMM20; Synonyms=KIAA0016;
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].
RC TISSUE=Fibroblast;
RX PubMed=7589431; DOI=10.1016/0014-5793(95)01010-c;
RA Goping I.S., Millar D.G., Shore G.C.;
RT "Identification of the human mitochondrial protein import receptor,
RT huMas20p. Complementation of delta mas20 in yeast.";
RL FEBS Lett. 373:45-50(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=7498524; DOI=10.1016/0014-5793(95)01229-8;
RA Seki N., Moczko M., Nagase T., Zufall N., Ehmann B., Dietmeier K.,
RA Schaefer E., Nomura N., Pfanner N.;
RT "A human homolog of the mitochondrial protein import receptor Mom19 can
RT assemble with the yeast mitochondrial receptor complex.";
RL FEBS Lett. 375:307-310(1995).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=10548729; DOI=10.1016/s0378-1119(99)00409-6;
RA Hernandez J.M., Giner P., Hernandez-Yago J.;
RT "Gene structure of the human mitochondrial outer membrane receptor tom20
RT and evolutionary study of its family of processed pseudogenes.";
RL Gene 239:283-291(1999).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Bone marrow;
RX PubMed=7584026; DOI=10.1093/dnares/1.1.27;
RA Nomura N., Miyajima N., Sazuka T., Tanaka A., Kawarabayasi Y., Sato S.,
RA Nagase T., Seki N., Ishikawa K., Tabata S.;
RT "Prediction of the coding sequences of unidentified human genes. I. The
RT coding sequences of 40 new genes (KIAA0001-KIAA0040) deduced by analysis of
RT randomly sampled cDNA clones from human immature myeloid cell line KG-1.";
RL DNA Res. 1:27-35(1994).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain;
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 [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.;
RT "Cloning of human full open reading frames in Gateway(TM) system entry
RT vector (pDONR201).";
RL Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16710414; DOI=10.1038/nature04727;
RA Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A.,
RA Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C.,
RA Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.,
RA Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C.,
RA Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W.,
RA Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J.,
RA Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J.,
RA Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y.,
RA Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J.,
RA Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
RA Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
RA Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
RA Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S.,
RA Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K.,
RA Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R.,
RA Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M.,
RA Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S.,
RA Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J.,
RA Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W.,
RA McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
RA Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
RA Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
RA Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
RA Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S.,
RA Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M.,
RA White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H.,
RA Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E.,
RA Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G.,
RA Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.;
RT "The DNA sequence and biological annotation of human chromosome 1.";
RL Nature 441:315-321(2006).
RN [8]
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 [9]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain, Cervix, Eye, and Pancreas;
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 [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-138, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
RA Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.;
RT "Global, in vivo, and site-specific phosphorylation dynamics in signaling
RT networks.";
RL Cell 127:635-648(2006).
RN [11]
RP IDENTIFICATION IN THE TOM COMPLEX.
RX PubMed=18331822; DOI=10.1016/j.bbrc.2008.02.150;
RA Kato H., Mihara K.;
RT "Identification of Tom5 and Tom6 in the preprotein translocase complex of
RT human mitochondrial outer membrane.";
RL Biochem. Biophys. Res. Commun. 369:958-963(2008).
RN [12]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007;
RA Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,
RA Greff Z., Keri G., Stemmann O., Mann M.;
RT "Kinase-selective enrichment enables quantitative phosphoproteomics of the
RT kinome across the cell cycle.";
RL Mol. Cell 31:438-448(2008).
RN [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-138, 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 [14]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-135 AND SER-138, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Leukemic T-cell;
RX PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA Rodionov V., Han D.K.;
RT "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT reveals system-wide modulation of protein-protein interactions.";
RL Sci. Signal. 2:RA46-RA46(2009).
RN [15]
RP SUBCELLULAR LOCATION.
RX PubMed=20628368; DOI=10.1038/cr.2010.103;
RA Liu X.Y., Wei B., Shi H.X., Shan Y.F., Wang C.;
RT "Tom70 mediates activation of interferon regulatory factor 3 on
RT mitochondria.";
RL Cell Res. 20:994-1011(2010).
RN [16]
RP INTERACTION WITH APEX1.
RX PubMed=20231292; DOI=10.1074/jbc.m109.069591;
RA Li M., Zhong Z., Zhu J., Xiang D., Dai N., Cao X., Qing Y., Yang Z.,
RA Xie J., Li Z., Baugh L., Wang G., Wang D.;
RT "Identification and characterization of mitochondrial targeting sequence of
RT human apurinic/apyrimidinic endonuclease 1.";
RL J. Biol. Chem. 285:14871-14881(2010).
RN [17]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-135 AND SER-138, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [18]
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 [19]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-135 AND SER-138, AND
RP IDENTIFICATION BY 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 [20]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-135, 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 [21]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-135, AND IDENTIFICATION BY
RP 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 [22]
RP UBIQUITINATION AT LYS-56; LYS-61 AND LYS-68, MUTAGENESIS OF LYS-56; LYS-61
RP AND LYS-68, AND DEUBIQUITINATION.
RX PubMed=24896179; DOI=10.1038/nature13418;
RA Bingol B., Tea J.S., Phu L., Reichelt M., Bakalarski C.E., Song Q.,
RA Foreman O., Kirkpatrick D.S., Sheng M.;
RT "The mitochondrial deubiquitinase USP30 opposes parkin-mediated
RT mitophagy.";
RL Nature 510:370-375(2014).
RN [23]
RP SUBCELLULAR LOCATION.
RX PubMed=25764979; DOI=10.1016/j.bbamcr.2015.03.004;
RA Koob S., Barrera M., Anand R., Reichert A.S.;
RT "The non-glycosylated isoform of MIC26 is a constituent of the mammalian
RT MICOS complex and promotes formation of crista junctions.";
RL Biochim. Biophys. Acta 1853:1551-1563(2015).
RN [24]
RP SUBCELLULAR LOCATION.
RX PubMed=25997101; DOI=10.7554/elife.06265;
RA Guarani V., McNeill E.M., Paulo J.A., Huttlin E.L., Froehlich F.,
RA Gygi S.P., Van Vactor D., Harper J.W.;
RT "QIL1 is a novel mitochondrial protein required for MICOS complex stability
RT and cristae morphology.";
RL Elife 4:0-0(2015).
RN [25]
RP UBIQUITINATION AT LYS-35; LYS-56 AND LYS-61.
RX PubMed=25621951; DOI=10.1038/ncb3097;
RA Cunningham C.N., Baughman J.M., Phu L., Tea J.S., Yu C., Coons M.,
RA Kirkpatrick D.S., Bingol B., Corn J.E.;
RT "USP30 and parkin homeostatically regulate atypical ubiquitin chains on
RT mitochondria.";
RL Nat. Cell Biol. 17:160-169(2015).
RN [26]
RP IDENTIFICATION BY MASS 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).
RN [27]
RP SUBCELLULAR LOCATION.
RX PubMed=31644573; DOI=10.1371/journal.pone.0218303;
RA Wagner F., Kunz T.C., Chowdhury S.R., Thiede B., Fraunholz M., Eger D.,
RA Kozjak-Pavlovic V.;
RT "Armadillo repeat-containing protein 1 is a dual localization protein
RT associated with mitochondrial intermembrane space bridging complex.";
RL PLoS ONE 14:e0218303-e0218303(2019).
CC -!- FUNCTION: Central component of the receptor complex responsible for the
CC recognition and translocation of cytosolically synthesized
CC mitochondrial preproteins. Together with TOM22 functions as the transit
CC peptide receptor at the surface of the mitochondrion outer membrane and
CC facilitates the movement of preproteins into the TOM40 translocation
CC pore (By similarity). Required for the translocation across the
CC mitochondrial outer membrane of cytochrome P450 monooxygenases.
CC {ECO:0000250, ECO:0000250|UniProtKB:Q62760}.
CC -!- SUBUNIT: Forms part of the preprotein translocase complex of the outer
CC mitochondrial membrane (TOM complex) which consists of at least 7
CC different proteins (TOMM5, TOMM6, TOMM7, TOMM20, TOMM22, TOMM40 and
CC TOMM70). Interacts with TOM22. Interacts with APEX1 (PubMed:20231292).
CC Interacts with TBC1D21 (By similarity). {ECO:0000250|UniProtKB:Q9DCC8,
CC ECO:0000269|PubMed:18331822, ECO:0000269|PubMed:20231292}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion outer membrane
CC {ECO:0000269|PubMed:20628368, ECO:0000269|PubMed:25764979,
CC ECO:0000269|PubMed:25997101, ECO:0000269|PubMed:31644573}; Single-pass
CC membrane protein {ECO:0000255}.
CC -!- PTM: Ubiquitinated by PRKN during mitophagy, leading to its degradation
CC and enhancement of mitophagy. Deubiquitinated by USP30.
CC {ECO:0000269|PubMed:24896179, ECO:0000269|PubMed:25621951}.
CC -!- SIMILARITY: Belongs to the Tom20 family. {ECO:0000305}.
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DR EMBL; AF126962; AAF13354.1; -; Genomic_DNA.
DR EMBL; AF126958; AAF13354.1; JOINED; Genomic_DNA.
DR EMBL; AF126959; AAF13354.1; JOINED; Genomic_DNA.
DR EMBL; AF126960; AAF13354.1; JOINED; Genomic_DNA.
DR EMBL; AF126961; AAF13354.1; JOINED; Genomic_DNA.
DR EMBL; D13641; BAA02804.1; -; mRNA.
DR EMBL; AK289810; BAF82499.1; -; mRNA.
DR EMBL; CR456718; CAG32999.1; -; mRNA.
DR EMBL; AL732292; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471098; EAW70003.1; -; Genomic_DNA.
DR EMBL; BC000882; AAH00882.1; -; mRNA.
DR EMBL; BC066335; AAH66335.1; -; mRNA.
DR EMBL; BC071994; AAH71994.1; -; mRNA.
DR EMBL; BC100286; AAI00287.1; -; mRNA.
DR EMBL; BC107851; AAI07852.1; -; mRNA.
DR CCDS; CCDS1603.1; -.
DR PIR; S68215; S68215.
DR RefSeq; NP_055580.1; NM_014765.2.
DR PDB; 4APO; X-ray; 1.90 A; D/E=140-145.
DR PDBsum; 4APO; -.
DR AlphaFoldDB; Q15388; -.
DR BMRB; Q15388; -.
DR SMR; Q15388; -.
DR BioGRID; 115144; 211.
DR ComplexPortal; CPX-6121; TOM40 mitochondrial outer membrane translocase complex.
DR CORUM; Q15388; -.
DR DIP; DIP-46735N; -.
DR IntAct; Q15388; 155.
DR MINT; Q15388; -.
DR STRING; 9606.ENSP00000355566; -.
DR iPTMnet; Q15388; -.
DR PhosphoSitePlus; Q15388; -.
DR BioMuta; TOMM20; -.
DR DMDM; 2498697; -.
DR EPD; Q15388; -.
DR jPOST; Q15388; -.
DR MassIVE; Q15388; -.
DR MaxQB; Q15388; -.
DR PaxDb; Q15388; -.
DR PeptideAtlas; Q15388; -.
DR PRIDE; Q15388; -.
DR ProteomicsDB; 60558; -.
DR TopDownProteomics; Q15388; -.
DR Antibodypedia; 2619; 234 antibodies from 34 providers.
DR DNASU; 9804; -.
DR Ensembl; ENST00000366607.5; ENSP00000355566.4; ENSG00000173726.11.
DR GeneID; 9804; -.
DR KEGG; hsa:9804; -.
DR MANE-Select; ENST00000366607.5; ENSP00000355566.4; NM_014765.3; NP_055580.1.
DR UCSC; uc001hwl.4; human.
DR CTD; 9804; -.
DR DisGeNET; 9804; -.
DR GeneCards; TOMM20; -.
DR HGNC; HGNC:20947; TOMM20.
DR HPA; ENSG00000173726; Low tissue specificity.
DR MIM; 601848; gene.
DR neXtProt; NX_Q15388; -.
DR OpenTargets; ENSG00000173726; -.
DR PharmGKB; PA134964372; -.
DR VEuPathDB; HostDB:ENSG00000173726; -.
DR eggNOG; KOG4056; Eukaryota.
DR GeneTree; ENSGT00390000011698; -.
DR HOGENOM; CLU_100000_0_0_1; -.
DR InParanoid; Q15388; -.
DR OMA; VGYCFYF; -.
DR OrthoDB; 1316067at2759; -.
DR PhylomeDB; Q15388; -.
DR TreeFam; TF106200; -.
DR PathwayCommons; Q15388; -.
DR Reactome; R-HSA-1268020; Mitochondrial protein import.
DR Reactome; R-HSA-5205685; PINK1-PRKN Mediated Mitophagy.
DR Reactome; R-HSA-5689880; Ub-specific processing proteases.
DR SignaLink; Q15388; -.
DR SIGNOR; Q15388; -.
DR BioGRID-ORCS; 9804; 599 hits in 1048 CRISPR screens.
DR ChiTaRS; TOMM20; human.
DR GeneWiki; TOMM20; -.
DR GenomeRNAi; 9804; -.
DR Pharos; Q15388; Tbio.
DR PRO; PR:Q15388; -.
DR Proteomes; UP000005640; Chromosome 1.
DR RNAct; Q15388; protein.
DR Bgee; ENSG00000173726; Expressed in parotid gland and 206 other tissues.
DR ExpressionAtlas; Q15388; baseline and differential.
DR Genevisible; Q15388; HS.
DR GO; GO:0031307; C:integral component of mitochondrial outer membrane; IBA:GO_Central.
DR GO; GO:0044233; C:mitochondria-associated endoplasmic reticulum membrane; IDA:MGI.
DR GO; GO:0005741; C:mitochondrial outer membrane; IDA:UniProtKB.
DR GO; GO:0005742; C:mitochondrial outer membrane translocase complex; IBA:GO_Central.
DR GO; GO:0005739; C:mitochondrion; IDA:UniProtKB.
DR GO; GO:0097225; C:sperm midpiece; ISS:UniProtKB.
DR GO; GO:0030943; F:mitochondrion targeting sequence binding; IBA:GO_Central.
DR GO; GO:0015450; F:protein-transporting ATPase activity; IDA:HGNC-UCL.
DR GO; GO:0051082; F:unfolded protein binding; IDA:HGNC-UCL.
DR GO; GO:0030150; P:protein import into mitochondrial matrix; IBA:GO_Central.
DR GO; GO:0045040; P:protein insertion into mitochondrial outer membrane; IC:ComplexPortal.
DR GO; GO:0006626; P:protein targeting to mitochondrion; IDA:HGNC-UCL.
DR GO; GO:0016031; P:tRNA import into mitochondrion; IBA:GO_Central.
DR Gene3D; 1.20.960.10; -; 1.
DR InterPro; IPR002056; MAS20.
DR InterPro; IPR022422; MAS20_rcpt_metazoan.
DR InterPro; IPR023392; Tom20_dom_sf.
DR PANTHER; PTHR12430; PTHR12430; 1.
DR Pfam; PF02064; MAS20; 1.
DR PIRSF; PIRSF037707; MAS20_rcpt; 1.
DR PRINTS; PR01989; EUOM20RECPTR.
DR PRINTS; PR00351; OM20RECEPTOR.
DR SUPFAM; SSF47157; SSF47157; 1.
DR TIGRFAMs; TIGR00985; 3a0801s04tom; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Isopeptide bond; Membrane; Mitochondrion;
KW Mitochondrion outer membrane; Phosphoprotein; Protein transport;
KW Reference proteome; Transmembrane; Transmembrane helix; Transport;
KW Ubl conjugation.
FT CHAIN 1..145
FT /note="Mitochondrial import receptor subunit TOM20 homolog"
FT /id="PRO_0000051538"
FT TOPO_DOM 1..6
FT /note="Mitochondrial intermembrane"
FT /evidence="ECO:0000255"
FT TRANSMEM 7..24
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 25..145
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT MOD_RES 135
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19690332,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
FT ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569"
FT MOD_RES 138
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17081983,
FT ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:19690332,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692"
FT CROSSLNK 35
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0000269|PubMed:25621951"
FT CROSSLNK 56
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0000269|PubMed:24896179,
FT ECO:0000269|PubMed:25621951"
FT CROSSLNK 61
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0000269|PubMed:24896179,
FT ECO:0000269|PubMed:25621951"
FT CROSSLNK 68
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0000269|PubMed:24896179"
FT VARIANT 117
FT /note="P -> L (in dbSNP:rs16991984)"
FT /id="VAR_052366"
FT VARIANT 134
FT /note="V -> L (in dbSNP:rs1049510)"
FT /id="VAR_052367"
FT MUTAGEN 56
FT /note="K->R: Defects in mitophagy; when associated with R-
FT 61 and R-68."
FT /evidence="ECO:0000269|PubMed:24896179"
FT MUTAGEN 61
FT /note="K->R: Defects in mitophagy; when associated with R-
FT 56 and R-68."
FT /evidence="ECO:0000269|PubMed:24896179"
FT MUTAGEN 68
FT /note="K->R: Defects in mitophagy; when associated with R-
FT 56 and R-61."
FT /evidence="ECO:0000269|PubMed:24896179"
FT CONFLICT 145
FT /note="E -> D (in Ref. 6; CAG32999)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 145 AA; 16298 MW; 5153BD25AC5D9B3A CRC64;
MVGRNSAIAA GVCGALFIGY CIYFDRKRRS DPNFKNRLRE RRKKQKLAKE RAGLSKLPDL
KDAEAVQKFF LEEIQLGEEL LAQGEYEKGV DHLTNAIAVC GQPQQLLQVL QQTLPPPVFQ
MLLTKLPTIS QRIVSAQSLA EDDVE
