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Mitochondrial import receptor subunit TOM20 homolog (Mitochondrial 20 kDa outer membrane protein) (Outer mitochondrial membrane receptor Tom20)

 TOM20_HUMAN             Reviewed;         145 AA.
Q15388; A8K195; Q498B3; Q6IBT4;
01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
01-NOV-1996, sequence version 1.
28-MAR-2018, entry version 171.
RecName: Full=Mitochondrial import receptor subunit TOM20 homolog;
AltName: Full=Mitochondrial 20 kDa outer membrane protein;
AltName: Full=Outer mitochondrial membrane receptor Tom20;
Name=TOMM20; Synonyms=KIAA0016;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Fibroblast;
PubMed=7589431; DOI=10.1016/0014-5793(95)01010-C;
Goping I.S., Millar D.G., Shore G.C.;
"Identification of the human mitochondrial protein import receptor,
huMas20p. Complementation of delta mas20 in yeast.";
FEBS Lett. 373:45-50(1995).
[2]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=7498524; DOI=10.1016/0014-5793(95)01229-8;
Seki N., Moczko M., Nagase T., Zufall N., Ehmann B., Dietmeier K.,
Schaefer E., Nomura N., Pfanner N.;
"A human homolog of the mitochondrial protein import receptor Mom19
can assemble with the yeast mitochondrial receptor complex.";
FEBS Lett. 375:307-310(1995).
[3]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=10548729; DOI=10.1016/S0378-1119(99)00409-6;
Hernandez J.M., Giner P., Hernandez-Yago J.;
"Gene structure of the human mitochondrial outer membrane receptor
tom20 and evolutionary study of its family of processed pseudogenes.";
Gene 239:283-291(1999).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Bone marrow;
PubMed=7584026; DOI=10.1093/dnares/1.1.27;
Nomura N., Miyajima N., Sazuka T., Tanaka A., Kawarabayasi Y.,
Sato S., Nagase T., Seki N., Ishikawa K., Tabata S.;
"Prediction of the coding sequences of unidentified human genes. I.
The coding sequences of 40 new genes (KIAA0001-KIAA0040) deduced by
analysis of randomly sampled cDNA clones from human immature myeloid
cell line KG-1.";
DNA Res. 1:27-35(1994).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Brain;
PubMed=14702039; DOI=10.1038/ng1285;
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.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.;
"Cloning of human full open reading frames in Gateway(TM) system entry
vector (pDONR201).";
Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=16710414; DOI=10.1038/nature04727;
Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D.,
Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A.,
Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F.,
McDonald L., Evans R., Phillips K., Atkinson A., Cooper R., Jones C.,
Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P.,
Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K.,
Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G.,
Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D.,
Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G.,
Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J.,
Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R.,
Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D.,
Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G.,
Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M.,
Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J.,
Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M.,
Loveland J., Lovell J., Lush M.J., Lyne R., Martin S.,
Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S.,
Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C.,
Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z.,
Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E.,
Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A.,
Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R.,
Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V.,
Beck S., Rogers J., Bentley D.R.;
"The DNA sequence and biological annotation of human chromosome 1.";
Nature 441:315-321(2006).
[8]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
[9]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Brain, Cervix, Eye, and Pancreas;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[10]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-138, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,
Mann M.;
"Global, in vivo, and site-specific phosphorylation dynamics in
signaling networks.";
Cell 127:635-648(2006).
[11]
IDENTIFICATION IN THE TOM COMPLEX.
PubMed=18331822; DOI=10.1016/j.bbrc.2008.02.150;
Kato H., Mihara K.;
"Identification of Tom5 and Tom6 in the preprotein translocase complex
of human mitochondrial outer membrane.";
Biochem. Biophys. Res. Commun. 369:958-963(2008).
[12]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007;
Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,
Greff Z., Keri G., Stemmann O., Mann M.;
"Kinase-selective enrichment enables quantitative phosphoproteomics of
the kinome across the cell cycle.";
Mol. Cell 31:438-448(2008).
[13]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-138, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18669648; DOI=10.1073/pnas.0805139105;
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
Elledge S.J., Gygi S.P.;
"A quantitative atlas of mitotic phosphorylation.";
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
[14]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-135 AND SER-138, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Leukemic T-cell;
PubMed=19690332; DOI=10.1126/scisignal.2000007;
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
Rodionov V., Han D.K.;
"Quantitative phosphoproteomic analysis of T cell receptor signaling
reveals system-wide modulation of protein-protein interactions.";
Sci. Signal. 2:RA46-RA46(2009).
[15]
INTERACTION WITH APEX1.
PubMed=20231292; DOI=10.1074/jbc.M109.069591;
Li M., Zhong Z., Zhu J., Xiang D., Dai N., Cao X., Qing Y., Yang Z.,
Xie J., Li Z., Baugh L., Wang G., Wang D.;
"Identification and characterization of mitochondrial targeting
sequence of human apurinic/apyrimidinic endonuclease 1.";
J. Biol. Chem. 285:14871-14881(2010).
[16]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-135 AND SER-138, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=20068231; DOI=10.1126/scisignal.2000475;
Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S.,
Mann M.;
"Quantitative phosphoproteomics reveals widespread full
phosphorylation site occupancy during mitosis.";
Sci. Signal. 3:RA3-RA3(2010).
[17]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21269460; DOI=10.1186/1752-0509-5-17;
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
"Initial characterization of the human central proteome.";
BMC Syst. Biol. 5:17-17(2011).
[18]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-135 AND SER-138, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21406692; DOI=10.1126/scisignal.2001570;
Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J.,
Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V.,
Blagoev B.;
"System-wide temporal characterization of the proteome and
phosphoproteome of human embryonic stem cell differentiation.";
Sci. Signal. 4:RS3-RS3(2011).
[19]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-135, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma, and Erythroleukemia;
PubMed=23186163; DOI=10.1021/pr300630k;
Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
Mohammed S.;
"Toward a comprehensive characterization of a human cancer cell
phosphoproteome.";
J. Proteome Res. 12:260-271(2013).
[20]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-135, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D.,
Wang L., Ye M., Zou H.;
"An enzyme assisted RP-RPLC approach for in-depth analysis of human
liver phosphoproteome.";
J. Proteomics 96:253-262(2014).
[21]
UBIQUITINATION AT LYS-56; LYS-61 AND LYS-68, MUTAGENESIS OF LYS-56;
LYS-61 AND LYS-68, AND DEUBIQUITINATION.
PubMed=24896179; DOI=10.1038/nature13418;
Bingol B., Tea J.S., Phu L., Reichelt M., Bakalarski C.E., Song Q.,
Foreman O., Kirkpatrick D.S., Sheng M.;
"The mitochondrial deubiquitinase USP30 opposes parkin-mediated
mitophagy.";
Nature 510:370-375(2014).
[22]
SUBCELLULAR LOCATION.
PubMed=25764979; DOI=10.1016/j.bbamcr.2015.03.004;
Koob S., Barrera M., Anand R., Reichert A.S.;
"The non-glycosylated isoform of MIC26 is a constituent of the
mammalian MICOS complex and promotes formation of crista junctions.";
Biochim. Biophys. Acta 1853:1551-1563(2015).
[23]
SUBCELLULAR LOCATION.
PubMed=25997101; DOI=10.7554/eLife.06265;
Guarani V., McNeill E.M., Paulo J.A., Huttlin E.L., Froehlich F.,
Gygi S.P., Van Vactor D., Harper J.W.;
"QIL1 is a novel mitochondrial protein required for MICOS complex
stability and cristae morphology.";
Elife 4:0-0(2015).
[24]
UBIQUITINATION AT LYS-35; LYS-56 AND LYS-61.
PubMed=25621951; DOI=10.1038/ncb3097;
Cunningham C.N., Baughman J.M., Phu L., Tea J.S., Yu C., Coons M.,
Kirkpatrick D.S., Bingol B., Corn J.E.;
"USP30 and parkin homeostatically regulate atypical ubiquitin chains
on mitochondria.";
Nat. Cell Biol. 17:160-169(2015).
[25]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=25944712; DOI=10.1002/pmic.201400617;
Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M.,
Ayoub D., Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
"N-terminome analysis of the human mitochondrial proteome.";
Proteomics 15:2519-2524(2015).
-!- FUNCTION: Central component of the receptor complex responsible
for the recognition and translocation of cytosolically synthesized
mitochondrial preproteins. Together with TOM22 functions as the
transit peptide receptor at the surface of the mitochondrion outer
membrane and facilitates the movement of preproteins into the
TOM40 translocation pore (By similarity). {ECO:0000250}.
-!- SUBUNIT: Forms part of the preprotein translocase complex of the
outer mitochondrial membrane (TOM complex) which consists of at
least 7 different proteins (TOMM5, TOMM6, TOMM7, TOMM20, TOMM22,
TOMM40 and TOMM70). Interacts with TOM22. Interacts with APEX1.
{ECO:0000269|PubMed:18331822, ECO:0000269|PubMed:20231292}.
-!- SUBCELLULAR LOCATION: Mitochondrion outer membrane
{ECO:0000269|PubMed:25764979, ECO:0000269|PubMed:25997101};
Single-pass membrane protein {ECO:0000255}.
-!- PTM: Ubiquitinated by PRKN during mitophagy, leading to its
degradation and enhancement of mitophagy. Deubiquitinated by
USP30. {ECO:0000269|PubMed:24896179, ECO:0000269|PubMed:25621951}.
-!- SIMILARITY: Belongs to the Tom20 family. {ECO:0000305}.
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EMBL; AF126962; AAF13354.1; -; Genomic_DNA.
EMBL; AF126958; AAF13354.1; JOINED; Genomic_DNA.
EMBL; AF126959; AAF13354.1; JOINED; Genomic_DNA.
EMBL; AF126960; AAF13354.1; JOINED; Genomic_DNA.
EMBL; AF126961; AAF13354.1; JOINED; Genomic_DNA.
EMBL; D13641; BAA02804.1; -; mRNA.
EMBL; AK289810; BAF82499.1; -; mRNA.
EMBL; CR456718; CAG32999.1; -; mRNA.
EMBL; AL732292; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; CH471098; EAW70003.1; -; Genomic_DNA.
EMBL; BC000882; AAH00882.1; -; mRNA.
EMBL; BC066335; AAH66335.1; -; mRNA.
EMBL; BC071994; AAH71994.1; -; mRNA.
EMBL; BC100286; AAI00287.1; -; mRNA.
EMBL; BC107851; AAI07852.1; -; mRNA.
CCDS; CCDS1603.1; -.
PIR; S68215; S68215.
RefSeq; NP_055580.1; NM_014765.2.
UniGene; Hs.533192; -.
PDB; 4APO; X-ray; 1.90 A; D/E=140-145.
PDBsum; 4APO; -.
ProteinModelPortal; Q15388; -.
SMR; Q15388; -.
BioGrid; 115144; 47.
CORUM; Q15388; -.
DIP; DIP-46735N; -.
IntAct; Q15388; 28.
MINT; Q15388; -.
STRING; 9606.ENSP00000355566; -.
iPTMnet; Q15388; -.
PhosphoSitePlus; Q15388; -.
BioMuta; TOMM20; -.
DMDM; 2498697; -.
EPD; Q15388; -.
MaxQB; Q15388; -.
PaxDb; Q15388; -.
PeptideAtlas; Q15388; -.
PRIDE; Q15388; -.
TopDownProteomics; Q15388; -.
DNASU; 9804; -.
Ensembl; ENST00000366607; ENSP00000355566; ENSG00000173726.
GeneID; 9804; -.
KEGG; hsa:9804; -.
UCSC; uc001hwl.4; human.
CTD; 9804; -.
EuPathDB; HostDB:ENSG00000173726.10; -.
GeneCards; TOMM20; -.
HGNC; HGNC:20947; TOMM20.
HPA; CAB005585; -.
HPA; HPA011562; -.
MIM; 601848; gene.
neXtProt; NX_Q15388; -.
OpenTargets; ENSG00000173726; -.
PharmGKB; PA134964372; -.
eggNOG; KOG4056; Eukaryota.
eggNOG; ENOG4111NAH; LUCA.
GeneTree; ENSGT00390000011698; -.
HOGENOM; HOG000006671; -.
HOVERGEN; HBG057315; -.
InParanoid; Q15388; -.
KO; K17770; -.
OMA; FVGYCFY; -.
OrthoDB; EOG091G0Z80; -.
PhylomeDB; Q15388; -.
TreeFam; TF106200; -.
Reactome; R-HSA-1268020; Mitochondrial protein import.
Reactome; R-HSA-5205685; Pink/Parkin Mediated Mitophagy.
Reactome; R-HSA-5689880; Ub-specific processing proteases.
ChiTaRS; TOMM20; human.
GeneWiki; TOMM20; -.
GenomeRNAi; 9804; -.
PRO; PR:Q15388; -.
Proteomes; UP000005640; Chromosome 1.
Bgee; ENSG00000173726; -.
CleanEx; HS_TOMM20; -.
ExpressionAtlas; Q15388; baseline and differential.
Genevisible; Q15388; HS.
GO; GO:0044233; C:ER-mitochondrion membrane contact site; IDA:MGI.
GO; GO:0031012; C:extracellular matrix; HDA:BHF-UCL.
GO; GO:0031307; C:integral component of mitochondrial outer membrane; IBA:GO_Central.
GO; GO:0005741; C:mitochondrial outer membrane; IDA:UniProtKB.
GO; GO:0005742; C:mitochondrial outer membrane translocase complex; TAS:HGNC.
GO; GO:0005739; C:mitochondrion; IDA:HPA.
GO; GO:0030943; F:mitochondrion targeting sequence binding; IBA:GO_Central.
GO; GO:0015450; F:P-P-bond-hydrolysis-driven protein transmembrane transporter activity; IDA:HGNC.
GO; GO:0051082; F:unfolded protein binding; IDA:HGNC.
GO; GO:0016236; P:macroautophagy; TAS:Reactome.
GO; GO:0070096; P:mitochondrial outer membrane translocase complex assembly; IBA:GO_Central.
GO; GO:0016579; P:protein deubiquitination; TAS:Reactome.
GO; GO:0030150; P:protein import into mitochondrial matrix; IBA:GO_Central.
GO; GO:0006626; P:protein targeting to mitochondrion; IDA:HGNC.
GO; GO:1905242; P:response to 3,3',5-triiodo-L-thyronine; IEA:Ensembl.
GO; GO:0014850; P:response to muscle activity; IEA:Ensembl.
GO; GO:0016031; P:tRNA import into mitochondrion; IBA:GO_Central.
Gene3D; 1.20.960.10; -; 1.
InterPro; IPR002056; MAS20.
InterPro; IPR022422; MAS20_rcpt_metazoan.
InterPro; IPR023392; Tom20_dom_sf.
PANTHER; PTHR12430; PTHR12430; 1.
Pfam; PF02064; MAS20; 1.
PIRSF; PIRSF037707; MAS20_rcpt; 1.
PRINTS; PR01989; EUOM20RECPTR.
PRINTS; PR00351; OM20RECEPTOR.
SUPFAM; SSF47157; SSF47157; 1.
TIGRFAMs; TIGR00985; 3a0801s04tom; 1.
1: Evidence at protein level;
3D-structure; Complete proteome; Isopeptide bond; Membrane;
Mitochondrion; Mitochondrion outer membrane; Phosphoprotein;
Polymorphism; Protein transport; Reference proteome; Transmembrane;
Transmembrane helix; Transport; Ubl conjugation.
CHAIN 1 145 Mitochondrial import receptor subunit
TOM20 homolog.
/FTId=PRO_0000051538.
TOPO_DOM 1 6 Mitochondrial intermembrane.
{ECO:0000255}.
TRANSMEM 7 24 Helical. {ECO:0000255}.
TOPO_DOM 25 145 Cytoplasmic. {ECO:0000255}.
MOD_RES 135 135 Phosphoserine.
{ECO:0000244|PubMed:19690332,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:21406692,
ECO:0000244|PubMed:23186163,
ECO:0000244|PubMed:24275569}.
MOD_RES 138 138 Phosphoserine.
{ECO:0000244|PubMed:17081983,
ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:19690332,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:21406692}.
CROSSLNK 35 35 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in ubiquitin).
{ECO:0000269|PubMed:25621951}.
CROSSLNK 56 56 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in ubiquitin).
{ECO:0000269|PubMed:24896179,
ECO:0000269|PubMed:25621951}.
CROSSLNK 61 61 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in ubiquitin).
{ECO:0000269|PubMed:24896179,
ECO:0000269|PubMed:25621951}.
CROSSLNK 68 68 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in ubiquitin).
{ECO:0000269|PubMed:24896179}.
VARIANT 117 117 P -> L (in dbSNP:rs16991984).
/FTId=VAR_052366.
VARIANT 134 134 V -> L (in dbSNP:rs1049510).
/FTId=VAR_052367.
MUTAGEN 56 56 K->R: Defects in mitophagy; when
associated with R-61 and R-68.
{ECO:0000269|PubMed:24896179}.
MUTAGEN 61 61 K->R: Defects in mitophagy; when
associated with R-56 and R-68.
{ECO:0000269|PubMed:24896179}.
MUTAGEN 68 68 K->R: Defects in mitophagy; when
associated with R-56 and R-61.
{ECO:0000269|PubMed:24896179}.
CONFLICT 145 145 E -> D (in Ref. 6; CAG32999).
{ECO:0000305}.
SEQUENCE 145 AA; 16298 MW; 5153BD25AC5D9B3A CRC64;
MVGRNSAIAA GVCGALFIGY CIYFDRKRRS DPNFKNRLRE RRKKQKLAKE RAGLSKLPDL
KDAEAVQKFF LEEIQLGEEL LAQGEYEKGV DHLTNAIAVC GQPQQLLQVL QQTLPPPVFQ
MLLTKLPTIS QRIVSAQSLA EDDVE


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