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Q9NS69 (TOM22_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 119. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Mitochondrial import receptor subunit TOM22 homolog

Short name=hTom22
Alternative name(s):
1C9-2
Translocase of outer membrane 22 kDa subunit homolog
Gene names
Name:TOMM22
Synonyms:TOM22
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length142 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. Ref.1

Subunit structure

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. Ref.8

Subcellular location

Mitochondrion outer membrane; Single-pass membrane protein By similarity.

Tissue specificity

Ubiquitous.

Domain

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.

Sequence similarities

Belongs to the Tom22 family.

Binary interactions

With

Entry

#Exp.

IntAct

Notes

TOMM7Q9P0U12EBI-1047508,EBI-1180558

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.6
Chain2 – 142141Mitochondrial import receptor subunit TOM22 homolog
PRO_0000076106

Regions

Topological domain2 – 8382Cytoplasmic Potential
Transmembrane84 – 10320Helical; Potential
Topological domain104 – 14239Mitochondrial intermembrane Potential
Region41 – 5010Import sequence; necessary for mitochondrion outer membrane localization and integration in the TOM complex By similarity
Region83 – 10321TMD; necessary for mitochondrion outer membrane localization and integration in the TOM complex By similarity
Region123 – 14220C-tail signal; necessary for mitochondrion outer membrane localization and integration in the TOM complex By similarity
Compositional bias110 – 1189Poly-Gln

Amino acid modifications

Modified residue21N-acetylalanine Ref.6 Ref.10 Ref.11 Ref.13 Ref.14
Modified residue151Phosphoserine Ref.7 Ref.11 Ref.13
Modified residue431Phosphothreonine Ref.9

Sequences

Sequence LengthMass (Da)Tools
Q9NS69 [UniParc].

Last modified January 23, 2007. Version 3.
Checksum: C957232F8420F34D

FASTA14215,522
        10         20         30         40         50         60 
MAAAVAAAGA GEPQSPDELL PKGDAEKPEE ELEEDDDEEL DETLSERLWG LTEMFPERVR 

        70         80         90        100        110        120 
SAAGATFDLS LFVAQKMYRF SRAALWIGTT SFMILVLPVV FETEKLQMEQ QQQLQQRQIL 

       130        140 
LGPNTGLSGG MPGALPSLPG KI 

« Hide

References

« Hide 'large scale' references
[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. expand/collapse author list , 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]"A genome annotation-driven approach to cloning the human ORFeome."
Collins J.E., Wright C.L., Edwards C.A., Davis M.P., Grinham J.A., Cole C.G., Goward M.E., Aguado B., Mallya M., Mokrab Y., Huckle E.J., Beare D.M., Dunham I.
Genome Biol. 5:R84.1-R84.11(2004) [PubMed] [Europe PMC] [Abstract]
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]"A quantitative atlas of mitotic phosphorylation."
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract]
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]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
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].
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
CCDSCCDS13975.1.
RefSeqNP_064628.1. NM_020243.4.
UniGeneHs.595072.

3D structure databases

ProteinModelPortalQ9NS69.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid121308. 24 interactions.
IntActQ9NS69. 3 interactions.
STRING9606.ENSP00000216034.

PTM databases

PhosphoSiteQ9NS69.

Proteomic databases

MaxQBQ9NS69.
PaxDbQ9NS69.
PeptideAtlasQ9NS69.
PRIDEQ9NS69.

Protocols and materials databases

DNASU56993.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000216034; ENSP00000216034; ENSG00000100216.
GeneID56993.
KEGGhsa:56993.
UCSCuc003awe.3. human.

Organism-specific databases

CTD56993.
GeneCardsGC22P039077.
HGNCHGNC:18002. TOMM22.
HPAHPA003037.
MIM607046. gene.
neXtProtNX_Q9NS69.
PharmGKBPA38275.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG310729.
HOGENOMHOG000067816.
HOVERGENHBG061819.
InParanoidQ9NS69.
KOK17769.
OMAMMPPAPG.
OrthoDBEOG7KWSKG.
PhylomeDBQ9NS69.
TreeFamTF106201.

Enzyme and pathway databases

ReactomeREACT_17015. Metabolism of proteins.

Gene expression databases

ArrayExpressQ9NS69.
BgeeQ9NS69.
CleanExHS_TOMM22.
GenevestigatorQ9NS69.

Family and domain databases

InterProIPR005683. Tom22.
[Graphical view]
PfamPF04281. Tom22. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSTOMM22. human.
GeneWikiTOMM22.
GenomeRNAi56993.
NextBio62693.
PROQ9NS69.
SOURCESearch...

Entry information

Entry nameTOM22_HUMAN
AccessionPrimary (citable) accession number: Q9NS69
Entry history
Integrated into UniProtKB/Swiss-Prot: October 19, 2002
Last sequence update: January 23, 2007
Last modified: July 9, 2014
This is version 119 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human chromosome 22

Human chromosome 22: entries, gene names and cross-references to MIM