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Protein

Mitochondrial import receptor subunit TOM20 homolog

Gene

TOMM20

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

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

  • P-P-bond-hydrolysis-driven protein transmembrane transporter activity Source: HGNC
  • unfolded protein binding Source: HGNC

GO - Biological processi

  • cellular protein metabolic process Source: Reactome
  • protein targeting to mitochondrion Source: HGNC
  • protein transmembrane transport Source: GOC
Complete GO annotation...

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 Componenti: Chromosome 1

Organism-specific databases

HGNCiHGNC:20947. TOMM20.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 66Mitochondrial intermembraneSequence Analysis
Transmembranei7 – 2418HelicalSequence AnalysisAdd
BLAST
Topological domaini25 – 145121CytoplasmicSequence AnalysisAdd
BLAST

GO - Cellular componenti

  • ER-mitochondrion membrane contact site Source: MGI
  • integral component of membrane Source: UniProtKB-KW
  • mitochondrial outer membrane translocase complex Source: UniProtKB
  • mitochondrion Source: HPA
Complete GO annotation...

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.

Polymorphism and mutation databases

BioMutaiTOMM20.
DMDMi2498697.

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-linki35 – 35Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)1 Publication
Cross-linki56 – 56Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)2 Publications
Cross-linki61 – 61Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)2 Publications
Cross-linki68 – 68Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)1 Publication
Modified residuei135 – 1351Phosphoserine4 Publications
Modified residuei138 – 1381Phosphoserine5 Publications

Post-translational modificationi

Ubiquitinated by PARK2 during mitophagy, leading to its degradation and enhancement of mitophagy. Deubiquitinated by USP30.2 Publications

Keywords - PTMi

Isopeptide bond, Phosphoprotein, Ubl conjugation

Proteomic databases

MaxQBiQ15388.
PaxDbiQ15388.
PeptideAtlasiQ15388.
PRIDEiQ15388.

PTM databases

PhosphoSiteiQ15388.

Expressioni

Gene expression databases

BgeeiQ15388.
CleanExiHS_TOMM20.
ExpressionAtlasiQ15388. baseline and differential.
GenevisibleiQ15388. HS.

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

Structurei

3D structure databases

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

Family & Domainsi

Sequence similaritiesi

Belongs to the Tom20 family.Curated

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiNOG307355.
GeneTreeiENSGT00390000011698.
HOGENOMiHOG000006671.
HOVERGENiHBG057315.
InParanoidiQ15388.
KOiK17770.
OMAiAMLIIKM.
OrthoDBiEOG790G2R.
PhylomeDBiQ15388.
TreeFamiTF106200.

Family and domain databases

Gene3Di1.20.960.10. 1 hit.
InterProiIPR002056. MAS20.
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

        10         20         30         40         50
MVGRNSAIAA GVCGALFIGY CIYFDRKRRS DPNFKNRLRE RRKKQKLAKE
60 70 80 90 100
RAGLSKLPDL KDAEAVQKFF LEEIQLGEEL LAQGEYEKGV DHLTNAIAVC
110 120 130 140
GQPQQLLQVL QQTLPPPVFQ MLLTKLPTIS QRIVSAQSLA EDDVE
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 (Ref. 6) Curated

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:
EMBLi
GenBanki
DDBJi
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.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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.

3D structure databases

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

Protein-protein interaction databases

BioGridi115144. 33 interactions.
DIPiDIP-46735N.
IntActiQ15388. 19 interactions.
MINTiMINT-1403841.
STRINGi9606.ENSP00000355566.

PTM databases

PhosphoSiteiQ15388.

Polymorphism and mutation databases

BioMutaiTOMM20.
DMDMi2498697.

Proteomic databases

MaxQBiQ15388.
PaxDbiQ15388.
PeptideAtlasiQ15388.
PRIDEiQ15388.

Protocols and materials databases

DNASUi9804.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

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

Organism-specific databases

CTDi9804.
GeneCardsiGC01M235272.
HGNCiHGNC:20947. TOMM20.
HPAiCAB005585.
HPA011562.
MIMi601848. gene.
neXtProtiNX_Q15388.
PharmGKBiPA134964372.
HUGEiSearch...
GenAtlasiSearch...

Phylogenomic databases

eggNOGiNOG307355.
GeneTreeiENSGT00390000011698.
HOGENOMiHOG000006671.
HOVERGENiHBG057315.
InParanoidiQ15388.
KOiK17770.
OMAiAMLIIKM.
OrthoDBiEOG790G2R.
PhylomeDBiQ15388.
TreeFamiTF106200.

Enzyme and pathway databases

ReactomeiREACT_118595. Mitochondrial protein import.

Miscellaneous databases

ChiTaRSiTOMM20. human.
GeneWikiiTOMM20.
GenomeRNAii9804.
NextBioi36912.
PROiQ15388.
SOURCEiSearch...

Gene expression databases

BgeeiQ15388.
CleanExiHS_TOMM20.
ExpressionAtlasiQ15388. baseline and differential.
GenevisibleiQ15388. HS.

Family and domain databases

Gene3Di1.20.960.10. 1 hit.
InterProiIPR002056. MAS20.
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.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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. "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome."
    Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., Ye M., Zou H.
    J. Proteomics 96:253-262(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-135, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  20. "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 510:370-375(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.
  21. "The non-glycosylated isoform of MIC26 is a constituent of the mammalian MICOS complex and promotes formation of crista junctions."
    Koob S., Barrera M., Anand R., Reichert A.S.
    Biochim. Biophys. Acta 1853:1551-1563(2015) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION.
  22. "QIL1 is a novel mitochondrial protein required for MICOS complex stability and cristae morphology."
    Guarani V., McNeill E.M., Paulo J.A., Huttlin E.L., Froehlich F., Gygi S.P., Van Vactor D., Harper J.W.
    Elife 4:0-0(2015) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION.
  23. "USP30 and parkin homeostatically regulate atypical ubiquitin chains on mitochondria."
    Cunningham C.N., Baughman J.M., Phu L., Tea J.S., Yu C., Coons M., Kirkpatrick D.S., Bingol B., Corn J.E.
    Nat. Cell Biol. 17:160-169(2015) [PubMed] [Europe PMC] [Abstract]
    Cited for: UBIQUITINATION AT LYS-35; LYS-56 AND LYS-61.

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: July 22, 2015
This is version 149 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

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.