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Protein

Mitochondrial import receptor subunit TOM22 homolog

Gene

TOMM22

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

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 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
Complete GO annotation...

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 Componenti: Chromosome 22

Organism-specific databases

HGNCiHGNC:18002. TOMM22.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini2 – 8382CytoplasmicSequence AnalysisAdd
BLAST
Transmembranei84 – 10320HelicalSequence AnalysisAdd
BLAST
Topological domaini104 – 14239Mitochondrial intermembraneSequence AnalysisAdd
BLAST

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
Complete GO annotation...

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

BgeeiQ9NS69.
CleanExiHS_TOMM22.
ExpressionAtlasiQ9NS69. baseline and differential.
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. 25 interactions.
IntActiQ9NS69. 3 interactions.
STRINGi9606.ENSP00000216034.

Structurei

3D structure databases

ProteinModelPortaliQ9NS69.
ModBaseiSearch...
MobiDBiSearch...

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.
GeneTreeiENSGT00390000016475.
HOGENOMiHOG000067816.
HOVERGENiHBG061819.
InParanoidiQ9NS69.
KOiK17769.
OMAiLGPNTGM.
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

        10         20         30         40         50
MAAAVAAAGA GEPQSPDELL PKGDAEKPEE ELEEDDDEEL DETLSERLWG
60 70 80 90 100
LTEMFPERVR SAAGATFDLS LFVAQKMYRF SRAALWIGTT SFMILVLPVV
110 120 130 140
FETEKLQMEQ QQQLQQRQIL LGPNTGLSGG MPGALPSLPG KI
Length:142
Mass (Da):15,522
Last modified:January 23, 2007 - v3
Checksum:iC957232F8420F34D
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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:
EMBLi
GenBanki
DDBJi
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.

3D structure databases

ProteinModelPortaliQ9NS69.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi121308. 25 interactions.
IntActiQ9NS69. 3 interactions.
STRINGi9606.ENSP00000216034.

PTM databases

PhosphoSiteiQ9NS69.

Proteomic databases

MaxQBiQ9NS69.
PaxDbiQ9NS69.
PeptideAtlasiQ9NS69.
PRIDEiQ9NS69.

Protocols and materials databases

DNASUi56993.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

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

Organism-specific databases

CTDi56993.
GeneCardsiGC22P039077.
HGNCiHGNC:18002. TOMM22.
HPAiHPA003037.
MIMi607046. gene.
neXtProtiNX_Q9NS69.
PharmGKBiPA38275.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiNOG310729.
GeneTreeiENSGT00390000016475.
HOGENOMiHOG000067816.
HOVERGENiHBG061819.
InParanoidiQ9NS69.
KOiK17769.
OMAiLGPNTGM.
OrthoDBiEOG7KWSKG.
PhylomeDBiQ9NS69.
TreeFamiTF106201.

Enzyme and pathway databases

ReactomeiREACT_118595. Mitochondrial protein import.

Miscellaneous databases

ChiTaRSiTOMM22. human.
GeneWikiiTOMM22.
GenomeRNAii56993.
NextBioi62693.
PROiQ9NS69.
SOURCEiSearch...

Gene expression databases

BgeeiQ9NS69.
CleanExiHS_TOMM22.
ExpressionAtlasiQ9NS69. baseline and differential.
GenevestigatoriQ9NS69.

Family and domain databases

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

Publicationsi

« Hide 'large scale' publications
  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(1999) [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(1999) [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(2003) [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(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Uterus.
  6. Bienvenut W.V.
    Submitted (MAY-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(2005) [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(2007) [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(2008) [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].
  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(2009) [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], CLEAVAGE OF INITIATOR METHIONINE [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(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], CLEAVAGE OF INITIATOR METHIONINE [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(2011) [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].

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: March 4, 2015
This is version 125 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

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.