dbPTM

TOM22_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	TOM22_HUMAN
UniProt AC	Q9NS69
Protein Name	Mitochondrial import receptor subunit TOM22 homolog
Gene Name	TOMM22
Organism	Homo sapiens (Human).
Sequence Length	142
Subcellular Localization	Mitochondrion outer membrane Single-pass membrane protein .
Protein Description	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..
Protein Sequence	MAAAVAAAGAGEPQSPDELLPKGDAEKPEEELEEDDDEELDETLSERLWGLTEMFPERVRSAAGATFDLSLFVAQKMYRFSRAALWIGTTSFMILVLPVVFETEKLQMEQQQQLQQRQILLGPNTGLSGGMPGALPSLPGKI

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
2	Acetylation	------MAAAVAAAG ------CHHHHHHCC	12.25	20068231
15	Phosphorylation	AGAGEPQSPDELLPK CCCCCCCCHHHCCCC	45.06	29255136
27	Ubiquitination	LPKGDAEKPEEELEE CCCCCCCCCHHHHCC	60.49	21890473
27	Acetylation	LPKGDAEKPEEELEE CCCCCCCCCHHHHCC	60.49	26051181
43	Phosphorylation	DDEELDETLSERLWG CHHHHHHHHHHHHHH	34.94	21955146
45	Phosphorylation	EELDETLSERLWGLT HHHHHHHHHHHHHHH	28.26	30278072
76	Ubiquitination	LSLFVAQKMYRFSRA HHHHHHHHHHHHHHH	28.32	-
108	Sulfoxidation	FETEKLQMEQQQQLQ HHHHHHHHHHHHHHH	7.91	28465586
125	Phosphorylation	QILLGPNTGLSGGMP HHHHCCCCCCCCCCC	42.50	28348404
128	Phosphorylation	LGPNTGLSGGMPGAL HCCCCCCCCCCCCCC	34.35	28348404
141	Ubiquitination	ALPSLPGKI------ CCCCCCCCC------	43.21	21890473

Upstream regulatory proteins (kinases for phosphorylation sites, E3 ubiquitin ligases of ubiquitination sites, ...)

Modified Location	Modified Residue	Modification	Type of Upstream Proteins	Gene Name of Upstream Proteins	UniProt AC of Upstream Proteins	Sources
Oops, there are no upstream regulatory protein records of TOM22_HUMAN !!

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of TOM22_HUMAN !!

Disease-associated PTM Sites based on SAP

* Distance = the distance between SAP position and PTM sites.

Modified Location	Modification	Variant Position (Distance <= 10)	Residue Change	SAP	Related Disease	Reference
Oops, there are no SNP-PTM records of TOM22_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
TOM20_HUMAN	TOMM20	physical	10982837
TOM40_HUMAN	TOMM40	physical	17635912
BAX_HUMAN	BAX	physical	17635912
TOM40_HUMAN	TOMM40	physical	22280891
TOM40_HUMAN	TOMM40	physical	22939629
TOM7_HUMAN	TOMM7	physical	22939629
TOM70_HUMAN	TOMM70A	physical	22939629
CLH1_HUMAN	CLTC	physical	26344197
EHD1_HUMAN	EHD1	physical	26344197
DHB12_HUMAN	HSD17B12	physical	26344197
ODPA_HUMAN	PDHA1	physical	26344197
SSRG_HUMAN	SSR3	physical	26344197
SSRD_HUMAN	SSR4	physical	26344197
QCR8_HUMAN	UQCRQ	physical	26344197
HCD2_HUMAN	HSD17B10	physical	25591737
MFN1_HUMAN	MFN1	physical	28514442
TOM40_HUMAN	TOMM40	physical	28514442
SC11C_HUMAN	SEC11C	physical	28514442
TM40L_HUMAN	TOMM40L	physical	28514442
MTG2_HUMAN	MTG2	physical	28514442
SFXN3_HUMAN	SFXN3	physical	28514442
S35B2_HUMAN	SLC35B2	physical	28514442
DDX11_HUMAN	DDX11	physical	28514442
SCMC1_HUMAN	SLC25A24	physical	28514442
STK39_HUMAN	STK39	physical	28514442
RB39B_HUMAN	RAB39B	physical	28514442
RA51D_HUMAN	RAD51D	physical	28514442
TBA4A_HUMAN	TUBA4A	physical	28514442
HSDL1_HUMAN	HSDL1	physical	28514442
XRCC3_HUMAN	XRCC3	physical	28514442
TBB3_HUMAN	TUBB3	physical	28514442
FEM1B_HUMAN	FEM1B	physical	28514442
SPCS2_HUMAN	SPCS2	physical	28514442
INT5_HUMAN	INTS5	physical	28514442
TIM29_HUMAN	C19orf52	physical	28514442
ADT3_HUMAN	SLC25A6	physical	28514442
STOM_HUMAN	STOM	physical	27173435

Drug and Disease Associations

Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
There are no disease associations of PTM sites.
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.

Regulatory Network of TOM22_HUMAN

Related Literatures of Post-Translational Modification

Acetylation
Reference	PubMed
"Lys-N and trypsin cover complementary parts of the phosphoproteome ina refined SCX-based approach."; Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,Mohammed S.; Anal. Chem. 81:4493-4501(2009). Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, PHOSPHORYLATION [LARGESCALE ANALYSIS] AT SER-15, AND MASS SPECTROMETRY.	19413330 [Abstract]
Phosphorylation
Reference	PubMed
"Lys-N and trypsin cover complementary parts of the phosphoproteome ina refined SCX-based approach."; Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,Mohammed S.; Anal. Chem. 81:4493-4501(2009). Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, PHOSPHORYLATION [LARGESCALE ANALYSIS] AT SER-15, AND MASS SPECTROMETRY.	19413330 [Abstract]
"Global, in vivo, and site-specific phosphorylation dynamics insignaling networks."; Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,Mann M.; Cell 127:635-648(2006). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-15, AND MASSSPECTROMETRY.	17081983 [Abstract]
"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). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-43, AND MASSSPECTROMETRY.	18669648 [Abstract]