TOM20_HUMAN - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: TOM20_HUMAN
• UniProt AC: Q15388
• Protein Name: Mitochondrial import receptor subunit TOM20 homolog
• Gene Name: TOMM20
• Organism: Homo sapiens (Human).
• Sequence Length: 145
• Subcellular Localization: Mitochondrion outer membrane ; Single-pass membrane protein .
• Protein Description: Central component of the receptor complex responsible for the recognition and translocation of cytosolically synthesized mitochondrial preproteins. Together with TOM22 functions as the transit peptide receptor at the surface of the mitochondrion outer membrane and facilitates the movement of preproteins into the TOM40 translocation pore (By similarity)..
• Protein Sequence: MVGRNSAIAAGVCGALFIGYCIYFDRKRRSDPNFKNRLRERRKKQKLAKERAGLSKLPDLKDAEAVQKFFLEEIQLGEELLAQGEYEKGVDHLTNAIAVCGQPQQLLQVLQQTLPPPVFQMLLTKLPTISQRIVSAQSLAEDDVE

Overview of Protein Modification Sites with Functional and Structural Information

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
30	Phosphorylation	YFDRKRRSDPNFKNR HHCCCCCCCCCHHHH	62.54	28555341
35	Ubiquitination	RRSDPNFKNRLRERR CCCCCCHHHHHHHHH	48.04	25621951
55	Phosphorylation	AKERAGLSKLPDLKD HHHHHCHHCCCCCCC	31.09	21712546
56	Acetylation	KERAGLSKLPDLKDA HHHHCHHCCCCCCCH	69.91	26051181
56	Ubiquitination	KERAGLSKLPDLKDA HHHHCHHCCCCCCCH	69.91	21890473
56	2-Hydroxyisobutyrylation	KERAGLSKLPDLKDA HHHHCHHCCCCCCCH	69.91	-
61	Ubiquitination	LSKLPDLKDAEAVQK HHCCCCCCCHHHHHH	63.37	21890473
68	Ubiquitination	KDAEAVQKFFLEEIQ CCHHHHHHHHHHHHH	31.33	24896179
128	Phosphorylation	MLLTKLPTISQRIVS HHHHHCCCHHHHHHH	43.63	29514088
130	Phosphorylation	LTKLPTISQRIVSAQ HHHCCCHHHHHHHHH	18.84	29514088
135	Phosphorylation	TISQRIVSAQSLAED CHHHHHHHHHHHHHC	20.44	30266825
138	Phosphorylation	QRIVSAQSLAEDDVE HHHHHHHHHHHCCCC	29.30	25159151

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
-	K	Ubiquitination	E3 ubiquitin ligase	PRKN	O60260	PMID:22199232

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of TOM20_HUMAN !!

Disease-associated PTM Sites based on SAP

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

Oops, there are no SNP-PTM records of TOM20_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
APOA1_HUMAN	APOA1	physical	16169070
PPHLN_HUMAN	PPHLN1	physical	16169070
FEZ1_HUMAN	FEZ1	physical	16169070
HAP1_HUMAN	HAP1	physical	16169070
CE126_HUMAN	KIAA1377	physical	16169070
PTN_HUMAN	PTN	physical	16169070
BAG6_HUMAN	BAG6	physical	16169070
OTC_HUMAN	OTC	physical	9756929
UCP1_HUMAN	UCP1	physical	9119086
VDAC1_HUMAN	VDAC1	physical	9119086
BCL2_HUMAN	BCL2	physical	9119086
PINK1_HUMAN	PINK1	physical	22280891
TOM40_HUMAN	TOMM40	physical	22280891
TOM22_HUMAN	TOMM22	physical	22939629
TOM70_HUMAN	TOMM70A	physical	22939629
TOM40_HUMAN	TOMM40	physical	22939629
TOM7_HUMAN	TOMM7	physical	22939629
PINK1_HUMAN	PINK1	physical	23885119
TRAF6_HUMAN	TRAF6	physical	23885119
SARM1_HUMAN	SARM1	physical	23885119
ADT2_HUMAN	SLC25A5	physical	26344197
ADT3_HUMAN	SLC25A6	physical	26344197
HCD2_HUMAN	HSD17B10	physical	25591737
BIRC2_HUMAN	BIRC2	physical	27693792

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.

Related Literatures of Post-Translational Modification

Phosphorylation

"Quantitative phosphoproteomic analysis of T cell receptor signalingreveals system-wide modulation of protein-protein interactions.";
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,Rodionov V., Han D.K.;
Sci. Signal. 2:RA46-RA46(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-135 AND SER-138, ANDMASS SPECTROMETRY.
PubMed: 19690332

"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 SER-138, AND MASSSPECTROMETRY.
PubMed: 18669648

"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-138, AND MASSSPECTROMETRY.
PubMed: 17081983