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Protein

Mitochondrial import receptor subunit TOM20 homolog

Gene

Tomm20

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 4 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

GO - Biological processi

Complete GO annotation...

Keywords - Biological processi

Protein transport, Transport

Enzyme and pathway databases

ReactomeiR-MMU-5205685. Pink/Parkin Mediated Mitophagy.

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
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 8

Organism-specific databases

MGIiMGI:1915202. 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

Complete GO annotation...

Keywords - Cellular componenti

Membrane, Mitochondrion, Mitochondrion outer membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 145145Mitochondrial import receptor subunit TOM20 homologPRO_0000051539Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Cross-linki35 – 35Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)By similarity
Cross-linki56 – 56Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)By similarity
Cross-linki61 – 61Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)By similarity
Cross-linki68 – 68Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)By similarity
Modified residuei135 – 1351PhosphoserineCombined sources
Modified residuei138 – 1381PhosphoserineCombined sources

Post-translational modificationi

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

Keywords - PTMi

Isopeptide bond, Phosphoprotein, Ubl conjugation

Proteomic databases

EPDiQ9DCC8.
MaxQBiQ9DCC8.
PaxDbiQ9DCC8.
PRIDEiQ9DCC8.

PTM databases

iPTMnetiQ9DCC8.
PhosphoSiteiQ9DCC8.

Expressioni

Gene expression databases

BgeeiQ9DCC8.
ExpressionAtlasiQ9DCC8. baseline and differential.
GenevisibleiQ9DCC8. MM.

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 (By similarity).By similarity

GO - Molecular functioni

Protein-protein interaction databases

BioGridi212562. 2 interactions.
DIPiDIP-60017N.
IntActiQ9DCC8. 1 interaction.
MINTiMINT-4616302.
STRINGi10090.ENSMUSP00000136493.

Structurei

3D structure databases

ProteinModelPortaliQ9DCC8.
SMRiQ9DCC8. Positions 59-126.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the Tom20 family.Curated

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiKOG4056. Eukaryota.
ENOG4111NAH. LUCA.
GeneTreeiENSGT00390000011698.
HOGENOMiHOG000006671.
HOVERGENiHBG057315.
InParanoidiQ9DCC8.
KOiK17770.
OMAiAMLIIKM.
OrthoDBiEOG790G2R.
PhylomeDBiQ9DCC8.
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.

Q9DCC8-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MVGRNSAIAA GVCGALFIGY CIYFDRKRRS DPNFKNRLRE RRKKQKLAKE
60 70 80 90 100
RAGLSKLPDL KDAEAVQKFF LEEIQLGEEL LAQGDYEKGV DHLTNAIAVC
110 120 130 140
GQPQQLLQVL QQTLPPPVFQ MLLTKLPTIS QRIVSAQSLA EDDVE
Length:145
Mass (Da):16,284
Last modified:June 1, 2001 - v1
Checksum:i50E3BD25AD5C9B3B
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK002902 mRNA. Translation: BAB22444.1.
BC002087 mRNA. Translation: AAH02087.1.
CCDSiCCDS22786.1.
RefSeqiNP_077176.1. NM_024214.2.
UniGeneiMm.372086.
Mm.489811.
Mm.6932.

Genome annotation databases

EnsembliENSMUST00000179857; ENSMUSP00000136493; ENSMUSG00000093904.
GeneIDi67952.
KEGGimmu:67952.
UCSCiuc009nza.2. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK002902 mRNA. Translation: BAB22444.1.
BC002087 mRNA. Translation: AAH02087.1.
CCDSiCCDS22786.1.
RefSeqiNP_077176.1. NM_024214.2.
UniGeneiMm.372086.
Mm.489811.
Mm.6932.

3D structure databases

ProteinModelPortaliQ9DCC8.
SMRiQ9DCC8. Positions 59-126.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi212562. 2 interactions.
DIPiDIP-60017N.
IntActiQ9DCC8. 1 interaction.
MINTiMINT-4616302.
STRINGi10090.ENSMUSP00000136493.

PTM databases

iPTMnetiQ9DCC8.
PhosphoSiteiQ9DCC8.

Proteomic databases

EPDiQ9DCC8.
MaxQBiQ9DCC8.
PaxDbiQ9DCC8.
PRIDEiQ9DCC8.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000179857; ENSMUSP00000136493; ENSMUSG00000093904.
GeneIDi67952.
KEGGimmu:67952.
UCSCiuc009nza.2. mouse.

Organism-specific databases

CTDi9804.
MGIiMGI:1915202. Tomm20.

Phylogenomic databases

eggNOGiKOG4056. Eukaryota.
ENOG4111NAH. LUCA.
GeneTreeiENSGT00390000011698.
HOGENOMiHOG000006671.
HOVERGENiHBG057315.
InParanoidiQ9DCC8.
KOiK17770.
OMAiAMLIIKM.
OrthoDBiEOG790G2R.
PhylomeDBiQ9DCC8.
TreeFamiTF106200.

Enzyme and pathway databases

ReactomeiR-MMU-5205685. Pink/Parkin Mediated Mitophagy.

Miscellaneous databases

ChiTaRSiTomm20. mouse.
PROiQ9DCC8.
SOURCEiSearch...

Gene expression databases

BgeeiQ9DCC8.
ExpressionAtlasiQ9DCC8. baseline and differential.
GenevisibleiQ9DCC8. MM.

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. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: C57BL/6J.
    Tissue: Kidney.
  2. "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].
    Strain: FVB/N.
    Tissue: Mammary tumor.
  3. Lubec G., Kang S.U.
    Submitted (APR-2007) to UniProtKB
    Cited for: PROTEIN SEQUENCE OF 126-132, IDENTIFICATION BY MASS SPECTROMETRY.
    Strain: C57BL/6J.
    Tissue: Brain.
  4. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-135 AND SER-138, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas, Spleen and Testis.

Entry informationi

Entry nameiTOM20_MOUSE
AccessioniPrimary (citable) accession number: Q9DCC8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: September 27, 2004
Last sequence update: June 1, 2001
Last modified: July 6, 2016
This is version 134 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. SIMILARITY comments
    Index of protein domains and families

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 one 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.