Q9NS69 (TOM22_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

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 names

Name:	TOMM22
Synonyms:	TOM22

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	142 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence 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.

Ontologies

Keywords
Biological process	Protein transport Translocation Transport
Cellular component	Membrane Mitochondrion Mitochondrion outer membrane
Domain	Transmembrane Transmembrane helix
Molecular function	Receptor
PTM	Acetylation Phosphoprotein
Technical term	Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	cellular protein metabolic process Traceable author statement. Source: Reactome protein import into mitochondrial outer membrane Inferred from direct assay PubMed 15644312. Source: BHF-UCL
Cellular_component	integral to membrane Inferred from direct assay PubMed 15644312. Source: BHF-UCL mitochondrial inner membrane Inferred from electronic annotation. Source: Compara mitochondrial outer membrane translocase complex Inferred from direct assay PubMed 12198123PubMed 15644312. Source: BHF-UCL
Molecular_function	protein transmembrane transporter activity Inferred from sequence or structural similarity. Source: BHF-UCL
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
TOMM7	Q9P0U1	2	EBI-1047508,EBI-1180558

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Initiator methionine	1	1	Removed Ref.6
	Chain	2 – 142	141	Mitochondrial import receptor subunit TOM22 homolog		PRO_0000076106
Regions
	Topological domain	2 – 83	82	Cytoplasmic Potential
	Transmembrane	84 – 103	20	Helical; Potential
	Topological domain	104 – 142	39	Mitochondrial intermembrane Potential
	Region	41 – 50	10	Import sequence; necessary for mitochondrion outer membrane localization and integration in the TOM complex By similarity
	Region	83 – 103	21	TMD; necessary for mitochondrion outer membrane localization and integration in the TOM complex By similarity
	Region	123 – 142	20	C-tail signal; necessary for mitochondrion outer membrane localization and integration in the TOM complex By similarity
	Compositional bias	110 – 118	9	Poly-Gln
Amino acid modifications
	Modified residue	2	1	N-acetylalanine Ref.6 Ref.10 Ref.12
	Modified residue	15	1	Phosphoserine Ref.7 Ref.10 Ref.12
	Modified residue	43	1	Phosphothreonine Ref.9

Sequences

	Sequence		Length	Mass (Da)
	Q9NS69 [UniParc]. Last modified January 23, 2007. Version 3. Checksum: C957232F8420F34D	FASTA	142	15,522
	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

References

	« Hide 'large scale' referencesShow '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. , 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, 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, MASS SPECTROMETRY. 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 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, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[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: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-15, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[11]	"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].
[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: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-15, MASS SPECTROMETRY.
+	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.
IPI	IPI00024976.
RefSeq	NP_064628.1. NM_020243.4.
UniGene	Hs.595072.
3D structure databases
ProteinModelPortal	Q9NS69.
ModBase	Search...
Protein-protein interaction databases
IntAct	Q9NS69. 3 interactions.
STRING	9606.ENSP00000216034.
PTM databases
PhosphoSite	Q9NS69.
Polymorphism databases
DMDM	24212074.
Proteomic databases
PaxDb	Q9NS69.
PeptideAtlas	Q9NS69.
PRIDE	Q9NS69.
Protocols and materials databases
DNASU	56993.
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000216034; ENSP00000216034; ENSG00000100216.
GeneID	56993.
KEGG	hsa:56993.
UCSC	uc003awe.3. human.
Organism-specific databases
CTD	56993.
GeneCards	GC22P039077.
HGNC	HGNC:18002. TOMM22.
HPA	HPA003037.
MIM	607046. gene.
neXtProt	NX_Q9NS69.
PharmGKB	PA38275.
GenAtlas	Search...
Phylogenomic databases
eggNOG	NOG310729.
HOGENOM	HOG000067816.
HOVERGEN	HBG061819.
InParanoid	Q9NS69.
OMA	MMPPAPG.
OrthoDB	EOG441QD4.
PhylomeDB	Q9NS69.
Enzyme and pathway databases
Reactome	REACT_17015. Metabolism of proteins.
Gene expression databases
ArrayExpress	Q9NS69.
Bgee	Q9NS69.
CleanEx	HS_TOMM22.
Genevestigator	Q9NS69.
GermOnline	ENSG00000100216. Homo sapiens.
Family and domain databases
InterPro	IPR005683. Tom22. [Graphical view]
Pfam	PF04281. Tom22. 1 hit. [Graphical view]
ProtoNet	Search...
Other
ChiTaRS	TOMM22. human.
GenomeRNAi	56993.
NextBio	62693.
SOURCE	Search...

Entry information

Entry name

TOM22_HUMAN

Accession

Primary (citable) accession number: Q9NS69

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 19, 2002
Last sequence update:	January 23, 2007
Last modified:	May 1, 2013
This is version 108 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.