Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Basket 0
(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

O94826

- TOM70_HUMAN

UniProt

O94826 - TOM70_HUMAN

Protein

Mitochondrial import receptor subunit TOM70

Gene

TOMM70A

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 133 (01 Oct 2014)
      Sequence version 1 (01 May 1999)
      Previous versions | rss
    • Help video
    • Feedback
    • Comment

    Functioni

    Receptor that accelerates the import of all mitochondrial precursor proteins.By similarity

    GO - Molecular functioni

    1. protein binding Source: UniProtKB
    2. protein transmembrane transporter activity Source: BHF-UCL

    GO - Biological processi

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

    Enzyme and pathway databases

    ReactomeiREACT_118595. Mitochondrial protein import.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Mitochondrial import receptor subunit TOM70
    Alternative name(s):
    Mitochondrial precursor proteins import receptor
    Translocase of outer membrane 70 kDa subunit
    Gene namesi
    Name:TOMM70A
    Synonyms:KIAA0719, TOM70
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 3

    Organism-specific databases

    HGNCiHGNC:11985. TOMM70A.

    Subcellular locationi

    GO - Cellular componenti

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

    Keywords - Cellular componenti

    Membrane, Mitochondrion, Mitochondrion outer membrane

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA36669.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed3 Publications
    Chaini2 – 608607Mitochondrial import receptor subunit TOM70PRO_0000106336Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei2 – 21N-acetylalanine3 Publications
    Modified residuei91 – 911Phosphoserine4 Publications
    Modified residuei185 – 1851N6-acetyllysine1 Publication

    Keywords - PTMi

    Acetylation, Phosphoprotein

    Proteomic databases

    MaxQBiO94826.
    PaxDbiO94826.
    PeptideAtlasiO94826.
    PRIDEiO94826.

    PTM databases

    PhosphoSiteiO94826.

    Expressioni

    Gene expression databases

    ArrayExpressiO94826.
    BgeeiO94826.
    CleanExiHS_TOMM70A.
    GenevestigatoriO94826.

    Organism-specific databases

    HPAiCAB017156.
    HPA014589.
    HPA048020.

    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 CAPN8 By similarity.By similarity

    Protein-protein interaction databases

    BioGridi115201. 28 interactions.
    IntActiO94826. 7 interactions.
    MINTiMINT-3002394.
    STRINGi9606.ENSP00000284320.

    Structurei

    3D structure databases

    ProteinModelPortaliO94826.
    SMRiO94826. Positions 81-586.
    ModBaseiSearch...
    MobiDBiSearch...

    Topological domain

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Topological domaini2 – 3837Mitochondrial intermembraneSequence AnalysisAdd
    BLAST
    Topological domaini60 – 608549CytoplasmicSequence AnalysisAdd
    BLAST

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei39 – 5921HelicalSequence AnalysisAdd
    BLAST

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Repeati114 – 14734TPR 1Add
    BLAST
    Repeati153 – 18634TPR 2Add
    BLAST
    Repeati294 – 32734TPR 3Add
    BLAST
    Repeati329 – 36234TPR 4Add
    BLAST
    Repeati367 – 40034TPR 5Add
    BLAST
    Repeati401 – 43434TPR 6Add
    BLAST
    Repeati440 – 47536TPR 7Add
    BLAST
    Repeati476 – 50934TPR 8Add
    BLAST
    Repeati511 – 54434TPR 9Add
    BLAST
    Repeati545 – 57834TPR 10Add
    BLAST

    Sequence similaritiesi

    Belongs to the Tom70 family.Curated
    Contains 10 TPR repeats.PROSITE-ProRule annotation

    Keywords - Domaini

    Repeat, TPR repeat, Transmembrane, Transmembrane helix

    Phylogenomic databases

    eggNOGiCOG0457.
    HOGENOMiHOG000264237.
    HOVERGENiHBG062335.
    InParanoidiO94826.
    KOiK17768.
    OMAiCILEAFQ.
    OrthoDBiEOG7DVD9R.
    PhylomeDBiO94826.
    TreeFamiTF106203.

    Family and domain databases

    Gene3Di1.25.40.10. 2 hits.
    InterProiIPR013026. TPR-contain_dom.
    IPR011990. TPR-like_helical.
    IPR001440. TPR_1.
    IPR019734. TPR_repeat.
    [Graphical view]
    PfamiPF00515. TPR_1. 2 hits.
    PF13181. TPR_8. 1 hit.
    [Graphical view]
    SMARTiSM00028. TPR. 8 hits.
    [Graphical view]
    PROSITEiPS50005. TPR. 7 hits.
    PS50293. TPR_REGION. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    O94826-1 [UniParc]FASTAAdd to Basket

    « Hide

    MAASKPVEAA VVAAAVPSSG SGVGGGGTAG PGTGGLPRWQ LALAVGAPLL    50
    LGAGAIYLWS RQQRRREARG RGDASGLKRN SERKTPEGRA SPAPGSGHPE 100
    GPGAHLDMNS LDRAQAAKNK GNKYFKAGKY EQAIQCYTEA ISLCPTEKNV 150
    DLSTFYQNRA AAFEQLQKWK EVAQDCTKAV ELNPKYVKAL FRRAKAHEKL 200
    DNKKECLEDV TAVCILEGFQ NQQSMLLADK VLKLLGKEKA KEKYKNREPL 250
    MPSPQFIKSY FSSFTDDIIS QPMLKGEKSD EDKDKEGEAL EVKENSGYLK 300
    AKQYMEEENY DKIISECSKE IDAEGKYMAE ALLLRATFYL LIGNANAAKP 350
    DLDKVISLKE ANVKLRANAL IKRGSMYMQQ QQPLLSTQDF NMAADIDPQN 400
    ADVYHHRGQL KILLDQVEEA VADFDECIRL RPESALAQAQ KCFALYRQAY 450
    TGNNSSQIQA AMKGFEEVIK KFPRCAEGYA LYAQALTDQQ QFGKADEMYD 500
    KCIDLEPDNA TTYVHKGLLQ LQWKQDLDRG LELISKAIEI DNKCDFAYET 550
    MGTIEVQRGN MEKAIDMFNK AINLAKSEME MAHLYSLCDA AHAQTEVAKK 600
    YGLKPPTL 608
    Length:608
    Mass (Da):67,455
    Last modified:May 1, 1999 - v1
    Checksum:i5AAF5CAAA8582480
    GO

    Sequence cautioni

    The sequence BAA34439.2 differs from that shown. Reason: Erroneous initiation.

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AB018262 mRNA. Translation: BAA34439.2. Different initiation.
    CH471052 Genomic DNA. Translation: EAW79822.1.
    CH471052 Genomic DNA. Translation: EAW79823.1.
    BC003633 mRNA. Translation: AAH03633.1.
    BC052994 mRNA. Translation: AAH52994.1.
    CCDSiCCDS33807.1.
    RefSeqiNP_055635.3. NM_014820.4.
    UniGeneiHs.227253.

    Genome annotation databases

    EnsembliENST00000284320; ENSP00000284320; ENSG00000154174.
    GeneIDi9868.
    KEGGihsa:9868.
    UCSCiuc003dtw.3. human.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AB018262 mRNA. Translation: BAA34439.2 . Different initiation.
    CH471052 Genomic DNA. Translation: EAW79822.1 .
    CH471052 Genomic DNA. Translation: EAW79823.1 .
    BC003633 mRNA. Translation: AAH03633.1 .
    BC052994 mRNA. Translation: AAH52994.1 .
    CCDSi CCDS33807.1.
    RefSeqi NP_055635.3. NM_014820.4.
    UniGenei Hs.227253.

    3D structure databases

    ProteinModelPortali O94826.
    SMRi O94826. Positions 81-586.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 115201. 28 interactions.
    IntActi O94826. 7 interactions.
    MINTi MINT-3002394.
    STRINGi 9606.ENSP00000284320.

    PTM databases

    PhosphoSitei O94826.

    Proteomic databases

    MaxQBi O94826.
    PaxDbi O94826.
    PeptideAtlasi O94826.
    PRIDEi O94826.

    Protocols and materials databases

    DNASUi 9868.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000284320 ; ENSP00000284320 ; ENSG00000154174 .
    GeneIDi 9868.
    KEGGi hsa:9868.
    UCSCi uc003dtw.3. human.

    Organism-specific databases

    CTDi 9868.
    GeneCardsi GC03M100082.
    HGNCi HGNC:11985. TOMM70A.
    HPAi CAB017156.
    HPA014589.
    HPA048020.
    MIMi 606081. gene.
    neXtProti NX_O94826.
    PharmGKBi PA36669.
    HUGEi Search...
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG0457.
    HOGENOMi HOG000264237.
    HOVERGENi HBG062335.
    InParanoidi O94826.
    KOi K17768.
    OMAi CILEAFQ.
    OrthoDBi EOG7DVD9R.
    PhylomeDBi O94826.
    TreeFami TF106203.

    Enzyme and pathway databases

    Reactomei REACT_118595. Mitochondrial protein import.

    Miscellaneous databases

    ChiTaRSi TOMM70A. human.
    GeneWikii TOMM70A.
    GenomeRNAii 9868.
    NextBioi 37199.
    PROi O94826.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi O94826.
    Bgeei O94826.
    CleanExi HS_TOMM70A.
    Genevestigatori O94826.

    Family and domain databases

    Gene3Di 1.25.40.10. 2 hits.
    InterProi IPR013026. TPR-contain_dom.
    IPR011990. TPR-like_helical.
    IPR001440. TPR_1.
    IPR019734. TPR_repeat.
    [Graphical view ]
    Pfami PF00515. TPR_1. 2 hits.
    PF13181. TPR_8. 1 hit.
    [Graphical view ]
    SMARTi SM00028. TPR. 8 hits.
    [Graphical view ]
    PROSITEi PS50005. TPR. 7 hits.
    PS50293. TPR_REGION. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Prediction of the coding sequences of unidentified human genes. XI. The complete sequences of 100 new cDNA clones from brain which code for large proteins in vitro."
      Nagase T., Ishikawa K., Suyama M., Kikuno R., Miyajima N., Tanaka A., Kotani H., Nomura N., Ohara O.
      DNA Res. 5:277-286(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Tissue: Brain.
    2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    3. "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: Skin and Uterus.
    4. "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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    5. "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.
    6. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-91, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Platelet.
    7. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-91, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    8. "Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
      Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
      Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
    9. "Lysine acetylation targets protein complexes and co-regulates major cellular functions."
      Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M.
      Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-185, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    10. "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-91, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    11. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    12. "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-91, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    13. "Comparative large-scale characterisation of plant vs. mammal proteins reveals similar and idiosyncratic N-alpha acetylation features."
      Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T., Giglione C.
      Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    14. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

    Entry informationi

    Entry nameiTOM70_HUMAN
    AccessioniPrimary (citable) accession number: O94826
    Secondary accession number(s): D3DN48
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: June 1, 2001
    Last sequence update: May 1, 1999
    Last modified: October 1, 2014
    This is version 133 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

    Complete proteome, Reference proteome

    Documents

    1. Human chromosome 3
      Human chromosome 3: entries, gene names and cross-references to MIM
    2. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    3. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3