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Q9NS69

- TOM22_HUMAN

UniProt

Q9NS69 - TOM22_HUMAN

Protein

Mitochondrial import receptor subunit TOM22 homolog

Gene

TOMM22

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

    Central receptor component of the translocase of the outer membrane of mitochondria (TOM complex) responsible for the recognition and translocation of cytosolically synthesized mitochondrial preproteins. Together with the peripheral receptor TOM20 functions as the transit peptide receptor and facilitates the movement of preproteins into the translocation pore.1 Publication

    GO - Molecular functioni

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

    GO - Biological processi

    1. cellular protein metabolic process Source: Reactome
    2. protein import into mitochondrial outer membrane Source: BHF-UCL
    3. protein targeting to mitochondrion Source: HGNC

    Keywords - Molecular functioni

    Receptor

    Keywords - Biological processi

    Protein transport, Translocation, Transport

    Enzyme and pathway databases

    ReactomeiREACT_118595. Mitochondrial protein import.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Mitochondrial import receptor subunit TOM22 homolog
    Short name:
    hTom22
    Alternative name(s):
    1C9-2
    Translocase of outer membrane 22 kDa subunit homolog
    Gene namesi
    Name:TOMM22
    Synonyms:TOM22
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 22

    Organism-specific databases

    HGNCiHGNC:18002. TOMM22.

    Subcellular locationi

    GO - Cellular componenti

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

    Keywords - Cellular componenti

    Membrane, Mitochondrion, Mitochondrion outer membrane

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA38275.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed5 Publications
    Chaini2 – 142141Mitochondrial import receptor subunit TOM22 homologPRO_0000076106Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei2 – 21N-acetylalanine5 Publications
    Modified residuei15 – 151Phosphoserine3 Publications
    Modified residuei43 – 431Phosphothreonine1 Publication

    Keywords - PTMi

    Acetylation, Phosphoprotein

    Proteomic databases

    MaxQBiQ9NS69.
    PaxDbiQ9NS69.
    PeptideAtlasiQ9NS69.
    PRIDEiQ9NS69.

    PTM databases

    PhosphoSiteiQ9NS69.

    Expressioni

    Tissue specificityi

    Ubiquitous.

    Gene expression databases

    ArrayExpressiQ9NS69.
    BgeeiQ9NS69.
    CleanExiHS_TOMM22.
    GenevestigatoriQ9NS69.

    Organism-specific databases

    HPAiHPA003037.

    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 TOMM40. Interacts with PPP2R2B By similarity.By similarity

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    TOMM7Q9P0U12EBI-1047508,EBI-1180558

    Protein-protein interaction databases

    BioGridi121308. 24 interactions.
    IntActiQ9NS69. 3 interactions.
    STRINGi9606.ENSP00000216034.

    Structurei

    3D structure databases

    ProteinModelPortaliQ9NS69.
    ModBaseiSearch...
    MobiDBiSearch...

    Topological domain

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Topological domaini2 – 8382CytoplasmicSequence AnalysisAdd
    BLAST
    Topological domaini104 – 14239Mitochondrial intermembraneSequence AnalysisAdd
    BLAST

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei84 – 10320HelicalSequence AnalysisAdd
    BLAST

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni41 – 5010Import sequence; necessary for mitochondrion outer membrane localization and integration in the TOM complexBy similarity
    Regioni83 – 10321TMD; necessary for mitochondrion outer membrane localization and integration in the TOM complexBy similarityAdd
    BLAST
    Regioni123 – 14220C-tail signal; necessary for mitochondrion outer membrane localization and integration in the TOM complexBy similarityAdd
    BLAST

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi110 – 1189Poly-Gln

    Domaini

    Requires the transmembrane domain (TMD), a short segment (the import sequence) in the cytoplasmic domain localizing separately from the TMD and the C-tail signal in the C-terminal domain for efficient targeting and integration into the TOM complex By similarity. The N-terminal domain (residues 1-62) is important for binding to the unfolded mature imported proteins. Residues (49-71) of the cytoplasmic domain interacts with TOMM20 while the C-terminal segment (residues 63-82) binds presequence of preproteins.By similarity

    Sequence similaritiesi

    Belongs to the Tom22 family.Curated

    Keywords - Domaini

    Transmembrane, Transmembrane helix

    Phylogenomic databases

    eggNOGiNOG310729.
    HOGENOMiHOG000067816.
    HOVERGENiHBG061819.
    InParanoidiQ9NS69.
    KOiK17769.
    OMAiMMPPAPG.
    OrthoDBiEOG7KWSKG.
    PhylomeDBiQ9NS69.
    TreeFamiTF106201.

    Family and domain databases

    InterProiIPR005683. Tom22.
    [Graphical view]
    PfamiPF04281. Tom22. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

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

    Q9NS69-1 [UniParc]FASTAAdd to Basket

    « Hide

    MAAAVAAAGA GEPQSPDELL PKGDAEKPEE ELEEDDDEEL DETLSERLWG    50
    LTEMFPERVR SAAGATFDLS LFVAQKMYRF SRAALWIGTT SFMILVLPVV 100
    FETEKLQMEQ QQQLQQRQIL LGPNTGLSGG MPGALPSLPG KI 142
    Length:142
    Mass (Da):15,522
    Last modified:January 23, 2007 - v3
    Checksum:iC957232F8420F34D
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AB040119 mRNA. Translation: BAB03306.1.
    AB041906 mRNA. Translation: BAB16408.1.
    AK024731 mRNA. Translation: BAB14979.1.
    CR456475 mRNA. Translation: CAG30361.1.
    BC009363 mRNA. Translation: AAH09363.1.
    CCDSiCCDS13975.1.
    RefSeqiNP_064628.1. NM_020243.4.
    UniGeneiHs.595072.

    Genome annotation databases

    EnsembliENST00000216034; ENSP00000216034; ENSG00000100216.
    GeneIDi56993.
    KEGGihsa:56993.
    UCSCiuc003awe.3. human.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AB040119 mRNA. Translation: BAB03306.1 .
    AB041906 mRNA. Translation: BAB16408.1 .
    AK024731 mRNA. Translation: BAB14979.1 .
    CR456475 mRNA. Translation: CAG30361.1 .
    BC009363 mRNA. Translation: AAH09363.1 .
    CCDSi CCDS13975.1.
    RefSeqi NP_064628.1. NM_020243.4.
    UniGenei Hs.595072.

    3D structure databases

    ProteinModelPortali Q9NS69.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 121308. 24 interactions.
    IntActi Q9NS69. 3 interactions.
    STRINGi 9606.ENSP00000216034.

    PTM databases

    PhosphoSitei Q9NS69.

    Proteomic databases

    MaxQBi Q9NS69.
    PaxDbi Q9NS69.
    PeptideAtlasi Q9NS69.
    PRIDEi Q9NS69.

    Protocols and materials databases

    DNASUi 56993.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000216034 ; ENSP00000216034 ; ENSG00000100216 .
    GeneIDi 56993.
    KEGGi hsa:56993.
    UCSCi uc003awe.3. human.

    Organism-specific databases

    CTDi 56993.
    GeneCardsi GC22P039077.
    HGNCi HGNC:18002. TOMM22.
    HPAi HPA003037.
    MIMi 607046. gene.
    neXtProti NX_Q9NS69.
    PharmGKBi PA38275.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG310729.
    HOGENOMi HOG000067816.
    HOVERGENi HBG061819.
    InParanoidi Q9NS69.
    KOi K17769.
    OMAi MMPPAPG.
    OrthoDBi EOG7KWSKG.
    PhylomeDBi Q9NS69.
    TreeFami TF106201.

    Enzyme and pathway databases

    Reactomei REACT_118595. Mitochondrial protein import.

    Miscellaneous databases

    ChiTaRSi TOMM22. human.
    GeneWikii TOMM22.
    GenomeRNAii 56993.
    NextBioi 62693.
    PROi Q9NS69.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q9NS69.
    Bgeei Q9NS69.
    CleanExi HS_TOMM22.
    Genevestigatori Q9NS69.

    Family and domain databases

    InterProi IPR005683. Tom22.
    [Graphical view ]
    Pfami PF04281. Tom22. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Identification and functional analysis of human Tom22 for protein import into mitochondria."
      Yano M., Hoogenraad N., Terada K., Mori M.
      Mol. Cell. Biol. 20:7205-7213(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION.
      Tissue: Liver.
    2. "Identification of mammalian Tom22 as a subunit of the preprotein translocase of the mitochondrial outer membrane."
      Saeki K., Suzuki H., Tsuneoka M., Maeda M., Iwamoto R., Hasuwa H., Shida S., Takahashi T., Sakaguchi M., Endo T., Miura Y., Mekada E., Mihara K.
      J. Biol. Chem. 275:31996-32002(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 24-31; 48-58; 61-76 AND 107-135.
      Tissue: Myeloid leukemia cell.
    3. "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].
    4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    5. "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: Uterus.
    6. Bienvenut W.V.
      Submitted (JUN-2005) to UniProtKB
      Cited for: PROTEIN SEQUENCE OF 2-22; 48-58 AND 61-76, CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY.
      Tissue: B-cell lymphoma.
    7. "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-15, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    8. "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.
    9. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-43, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    10. "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].
    11. "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: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-15, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    12. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    13. "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: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-15, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    14. "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].

    Entry informationi

    Entry nameiTOM22_HUMAN
    AccessioniPrimary (citable) accession number: Q9NS69
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: October 19, 2002
    Last sequence update: January 23, 2007
    Last modified: October 1, 2014
    This is version 121 of the entry and version 3 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, Direct protein sequencing, Reference proteome

    Documents

    1. Human chromosome 22
      Human chromosome 22: 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