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Q15388

- TOM20_HUMAN

UniProt

Q15388 - TOM20_HUMAN

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Protein
Mitochondrial import receptor subunit TOM20 homolog
Gene
TOMM20, KIAA0016
Organism
Homo sapiens (Human)
Status
Reviewed - 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.

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
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: Chromosome 1

Organism-specific databases

HGNCiHGNC:20947. TOMM20.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 66Mitochondrial intermembrane Reviewed prediction
Transmembranei7 – 2418Helical; Reviewed prediction
Add
BLAST
Topological domaini25 – 145121Cytoplasmic Reviewed prediction
Add
BLAST

GO - Cellular componenti

  1. integral component of membrane Source: UniProtKB-KW
  2. mitochondrial outer membrane translocase complex Source: UniProtKB
  3. 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.
Mutagenesisi61 – 611K → R: Defects in mitophagy; when associated with R-56 and R-68.
Mutagenesisi68 – 681K → R: Defects in mitophagy; when associated with R-56 and R-61.

Organism-specific databases

PharmGKBiPA134964372.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 145145Mitochondrial import receptor subunit TOM20 homolog
PRO_0000051538Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Cross-linki56 – 56Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)
Cross-linki61 – 61Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)
Cross-linki68 – 68Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)
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.

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.
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.

Family & Domainsi

Sequence similaritiesi

Belongs to the Tom20 family.

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

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 conflict

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

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.
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

« 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. "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: September 3, 2014
This is version 141 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

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