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Q15388

- TOM20_HUMAN

UniProt

Q15388 - TOM20_HUMAN

Protein

Mitochondrial import receptor subunit TOM20 homolog

Gene

TOMM20

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
  1. Functioni

    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.By similarity

    GO - Molecular functioni

    1. P-P-bond-hydrolysis-driven protein transmembrane transporter activity Source: HGNC
    2. protein binding Source: UniProtKB
    3. unfolded protein binding Source: HGNC

    GO - Biological processi

    1. cellular protein metabolic process Source: Reactome
    2. protein targeting to mitochondrion Source: HGNC
    3. protein transmembrane transport Source: GOC

    Keywords - Biological processi

    Protein transport, Transport

    Enzyme and pathway databases

    ReactomeiREACT_118595. Mitochondrial protein import.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Mitochondrial import receptor subunit TOM20 homolog
    Alternative name(s):
    Mitochondrial 20 kDa outer membrane protein
    Outer mitochondrial membrane receptor Tom20
    Gene namesi
    Name:TOMM20
    Synonyms:KIAA0016
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 1

    Organism-specific databases

    HGNCiHGNC:20947. TOMM20.

    Subcellular locationi

    GO - Cellular componenti

    1. integral component of membrane Source: UniProtKB-KW
    2. mitochondrial outer membrane translocase complex Source: UniProtKB
    3. mitochondrion Source: HPA

    Keywords - Cellular componenti

    Membrane, Mitochondrion, Mitochondrion outer membrane

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi56 – 561K → R: Defects in mitophagy; when associated with R-61 and R-68. 1 Publication
    Mutagenesisi61 – 611K → R: Defects in mitophagy; when associated with R-56 and R-68. 1 Publication
    Mutagenesisi68 – 681K → R: Defects in mitophagy; when associated with R-56 and R-61. 1 Publication

    Organism-specific databases

    PharmGKBiPA134964372.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 145145Mitochondrial import receptor subunit TOM20 homologPRO_0000051538Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Cross-linki56 – 56Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)1 Publication
    Cross-linki61 – 61Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)1 Publication
    Cross-linki68 – 68Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)1 Publication
    Modified residuei135 – 1351Phosphoserine3 Publications
    Modified residuei138 – 1381Phosphoserine5 Publications

    Post-translational modificationi

    Ubiquitinated at Lys-56, Lys-61 and Lys-68 by PARK2 during mitophagy, leading to its degradation and enhancement of mitophagy. Deubiquitinated by USP30.1 Publication

    Keywords - PTMi

    Isopeptide bond, Phosphoprotein, Ubl conjugation

    Proteomic databases

    MaxQBiQ15388.
    PaxDbiQ15388.
    PeptideAtlasiQ15388.
    PRIDEiQ15388.

    PTM databases

    PhosphoSiteiQ15388.

    Expressioni

    Gene expression databases

    BgeeiQ15388.
    CleanExiHS_TOMM20.
    GenevestigatoriQ15388.

    Organism-specific databases

    HPAiCAB005585.
    HPA011562.

    Interactioni

    Subunit structurei

    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 APEX1.2 Publications

    Protein-protein interaction databases

    BioGridi115144. 32 interactions.
    DIPiDIP-46735N.
    IntActiQ15388. 19 interactions.
    MINTiMINT-1403841.
    STRINGi9606.ENSP00000355566.

    Structurei

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    4APOX-ray1.90D/E140-145[»]
    ProteinModelPortaliQ15388.
    SMRiQ15388. Positions 59-126.
    ModBaseiSearch...
    MobiDBiSearch...

    Topological domain

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Topological domaini1 – 66Mitochondrial intermembraneSequence Analysis
    Topological domaini25 – 145121CytoplasmicSequence AnalysisAdd
    BLAST

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei7 – 2418HelicalSequence AnalysisAdd
    BLAST

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the Tom20 family.Curated

    Keywords - Domaini

    Transmembrane, Transmembrane helix

    Phylogenomic databases

    eggNOGiNOG307355.
    HOGENOMiHOG000006671.
    HOVERGENiHBG057315.
    InParanoidiQ15388.
    KOiK17770.
    OMAiKMVGRNS.
    OrthoDBiEOG790G2R.
    PhylomeDBiQ15388.
    TreeFamiTF106200.

    Family and domain databases

    Gene3Di1.20.960.10. 1 hit.
    InterProiIPR002056. MAS20_rcpt-related.
    IPR022422. MAS20_rcpt_metazoan.
    IPR023392. Tom20_dom.
    [Graphical view]
    PANTHERiPTHR12430. PTHR12430. 1 hit.
    PfamiPF02064. MAS20. 1 hit.
    [Graphical view]
    PIRSFiPIRSF037707. MAS20_rcpt. 1 hit.
    PRINTSiPR01989. EUOM20RECPTR.
    PR00351. OM20RECEPTOR.
    SUPFAMiSSF47157. SSF47157. 1 hit.
    TIGRFAMsiTIGR00985. 3a0801s04tom. 1 hit.

    Sequencei

    Sequence statusi: Complete.

    Q15388-1 [UniParc]FASTAAdd to Basket

    « Hide

    MVGRNSAIAA GVCGALFIGY CIYFDRKRRS DPNFKNRLRE RRKKQKLAKE    50
    RAGLSKLPDL KDAEAVQKFF LEEIQLGEEL LAQGEYEKGV DHLTNAIAVC 100
    GQPQQLLQVL QQTLPPPVFQ MLLTKLPTIS QRIVSAQSLA EDDVE 145
    Length:145
    Mass (Da):16,298
    Last modified:November 1, 1996 - v1
    Checksum:i5153BD25AC5D9B3A
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti145 – 1451E → D in CAG32999. 1 PublicationCurated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti117 – 1171P → L.
    Corresponds to variant rs16991984 [ dbSNP | Ensembl ].
    VAR_052366
    Natural varianti134 – 1341V → L.
    Corresponds to variant rs1049510 [ dbSNP | Ensembl ].
    VAR_052367

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF126962
    , AF126958, AF126959, AF126960, AF126961 Genomic DNA. Translation: AAF13354.1.
    D13641 mRNA. Translation: BAA02804.1.
    AK289810 mRNA. Translation: BAF82499.1.
    CR456718 mRNA. Translation: CAG32999.1.
    AL732292 Genomic DNA. Translation: CAI21937.1.
    CH471098 Genomic DNA. Translation: EAW70003.1.
    BC000882 mRNA. Translation: AAH00882.1.
    BC066335 mRNA. Translation: AAH66335.1.
    BC071994 mRNA. Translation: AAH71994.1.
    BC100286 mRNA. Translation: AAI00287.1.
    BC107851 mRNA. Translation: AAI07852.1.
    CCDSiCCDS1603.1.
    PIRiS68215.
    RefSeqiNP_055580.1. NM_014765.2.
    UniGeneiHs.533192.

    Genome annotation databases

    EnsembliENST00000366607; ENSP00000355566; ENSG00000173726.
    GeneIDi9804.
    KEGGihsa:9804.
    UCSCiuc001hwl.3. human.

    Polymorphism databases

    DMDMi2498697.

    Keywords - Coding sequence diversityi

    Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF126962
    , AF126958 , AF126959 , AF126960 , AF126961 Genomic DNA. Translation: AAF13354.1 .
    D13641 mRNA. Translation: BAA02804.1 .
    AK289810 mRNA. Translation: BAF82499.1 .
    CR456718 mRNA. Translation: CAG32999.1 .
    AL732292 Genomic DNA. Translation: CAI21937.1 .
    CH471098 Genomic DNA. Translation: EAW70003.1 .
    BC000882 mRNA. Translation: AAH00882.1 .
    BC066335 mRNA. Translation: AAH66335.1 .
    BC071994 mRNA. Translation: AAH71994.1 .
    BC100286 mRNA. Translation: AAI00287.1 .
    BC107851 mRNA. Translation: AAI07852.1 .
    CCDSi CCDS1603.1.
    PIRi S68215.
    RefSeqi NP_055580.1. NM_014765.2.
    UniGenei Hs.533192.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    4APO X-ray 1.90 D/E 140-145 [» ]
    ProteinModelPortali Q15388.
    SMRi Q15388. Positions 59-126.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 115144. 32 interactions.
    DIPi DIP-46735N.
    IntActi Q15388. 19 interactions.
    MINTi MINT-1403841.
    STRINGi 9606.ENSP00000355566.

    PTM databases

    PhosphoSitei Q15388.

    Polymorphism databases

    DMDMi 2498697.

    Proteomic databases

    MaxQBi Q15388.
    PaxDbi Q15388.
    PeptideAtlasi Q15388.
    PRIDEi Q15388.

    Protocols and materials databases

    DNASUi 9804.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000366607 ; ENSP00000355566 ; ENSG00000173726 .
    GeneIDi 9804.
    KEGGi hsa:9804.
    UCSCi uc001hwl.3. human.

    Organism-specific databases

    CTDi 9804.
    GeneCardsi GC01M235272.
    HGNCi HGNC:20947. TOMM20.
    HPAi CAB005585.
    HPA011562.
    MIMi 601848. gene.
    neXtProti NX_Q15388.
    PharmGKBi PA134964372.
    HUGEi Search...
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG307355.
    HOGENOMi HOG000006671.
    HOVERGENi HBG057315.
    InParanoidi Q15388.
    KOi K17770.
    OMAi KMVGRNS.
    OrthoDBi EOG790G2R.
    PhylomeDBi Q15388.
    TreeFami TF106200.

    Enzyme and pathway databases

    Reactomei REACT_118595. Mitochondrial protein import.

    Miscellaneous databases

    ChiTaRSi TOMM20. human.
    GeneWikii TOMM20.
    GenomeRNAii 9804.
    NextBioi 36912.
    PROi Q15388.
    SOURCEi Search...

    Gene expression databases

    Bgeei Q15388.
    CleanExi HS_TOMM20.
    Genevestigatori Q15388.

    Family and domain databases

    Gene3Di 1.20.960.10. 1 hit.
    InterProi IPR002056. MAS20_rcpt-related.
    IPR022422. MAS20_rcpt_metazoan.
    IPR023392. Tom20_dom.
    [Graphical view ]
    PANTHERi PTHR12430. PTHR12430. 1 hit.
    Pfami PF02064. MAS20. 1 hit.
    [Graphical view ]
    PIRSFi PIRSF037707. MAS20_rcpt. 1 hit.
    PRINTSi PR01989. EUOM20RECPTR.
    PR00351. OM20RECEPTOR.
    SUPFAMi SSF47157. SSF47157. 1 hit.
    TIGRFAMsi TIGR00985. 3a0801s04tom. 1 hit.
    ProtoNeti Search...

    Publicationsi

    1. "Identification of the human mitochondrial protein import receptor, huMas20p. Complementation of delta mas20 in yeast."
      Goping I.S., Millar D.G., Shore G.C.
      FEBS Lett. 373:45-50(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Tissue: Fibroblast.
    2. "A human homolog of the mitochondrial protein import receptor Mom19 can assemble with the yeast mitochondrial receptor complex."
      Seki N., Moczko M., Nagase T., Zufall N., Ehmann B., Dietmeier K., Schaefer E., Nomura N., Pfanner N.
      FEBS Lett. 375:307-310(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    3. "Gene structure of the human mitochondrial outer membrane receptor tom20 and evolutionary study of its family of processed pseudogenes."
      Hernandez J.M., Giner P., Hernandez-Yago J.
      Gene 239:283-291(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    4. "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."
      Nomura N., Miyajima N., Sazuka T., Tanaka A., Kawarabayasi Y., Sato S., Nagase T., Seki N., Ishikawa K., Tabata S.
      DNA Res. 1:27-35(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Tissue: Bone marrow.
    5. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
      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.
      Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Tissue: Brain.
    6. "Cloning of human full open reading frames in Gateway(TM) system entry vector (pDONR201)."
      Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.
      Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    7. "The DNA sequence and biological annotation of human chromosome 1."
      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.
      Nature 441:315-321(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    8. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    9. "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: Brain, Cervix, Eye and Pancreas.
    10. "Global, in vivo, and site-specific phosphorylation dynamics in signaling networks."
      Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.
      Cell 127:635-648(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-138, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    11. "Identification of Tom5 and Tom6 in the preprotein translocase complex of human mitochondrial outer membrane."
      Kato H., Mihara K.
      Biochem. Biophys. Res. Commun. 369:958-963(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION IN THE TOM COMPLEX.
    12. "Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle."
      Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., Greff Z., Keri G., Stemmann O., Mann M.
      Mol. Cell 31:438-448(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    13. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-138, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    14. "Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
      Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
      Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-135 AND SER-138, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Leukemic T-cell.
    15. "Identification and characterization of mitochondrial targeting sequence of human apurinic/apyrimidinic endonuclease 1."
      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.
      J. Biol. Chem. 285:14871-14881(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH APEX1.
    16. "Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
      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.
      Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-135 AND SER-138, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    17. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    18. "System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
      Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
      Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-135 AND SER-138, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    19. "The mitochondrial deubiquitinase USP30 opposes parkin-mediated mitophagy."
      Bingol B., Tea J.S., Phu L., Reichelt M., Bakalarski C.E., Song Q., Foreman O., Kirkpatrick D.S., Sheng M.
      Nature 0:0-0(2014) [PubMed] [Europe PMC] [Abstract]
      Cited for: UBIQUITINATION AT LYS-56; LYS-61 AND LYS-68, MUTAGENESIS OF LYS-56; LYS-61 AND LYS-68, DEUBIQUITINATION.

    Entry informationi

    Entry nameiTOM20_HUMAN
    AccessioniPrimary (citable) accession number: Q15388
    Secondary accession number(s): A8K195, Q498B3, Q6IBT4
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 1, 1997
    Last sequence update: November 1, 1996
    Last modified: October 1, 2014
    This is version 142 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program
    DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. Human chromosome 1
      Human chromosome 1: entries, gene names and cross-references to MIM
    2. Human entries with polymorphisms or disease mutations
      List of human entries with polymorphisms or disease mutations
    3. Human polymorphisms and disease mutations
      Index of human polymorphisms and disease mutations
    4. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    5. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    6. SIMILARITY comments
      Index of protein domains and families

    External Data

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