TOM70_HUMAN - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: TOM70_HUMAN
• UniProt AC: O94826
• Protein Name: Mitochondrial import receptor subunit TOM70
• Gene Name: TOMM70 {ECO:0000312|HGNC:HGNC:11985}
• Organism: Homo sapiens (Human).
• Sequence Length: 608
• Subcellular Localization: Mitochondrion outer membrane; Single-pass membrane protein.
• Protein Description: Receptor that accelerates the import of all mitochondrial precursor proteins..
• Protein Sequence: MAASKPVEAAVVAAAVPSSGSGVGGGGTAGPGTGGLPRWQLALAVGAPLLLGAGAIYLWSRQQRRREARGRGDASGLKRNSERKTPEGRASPAPGSGHPEGPGAHLDMNSLDRAQAAKNKGNKYFKAGKYEQAIQCYTEAISLCPTEKNVDLSTFYQNRAAAFEQLQKWKEVAQDCTKAVELNPKYVKALFRRAKAHEKLDNKKECLEDVTAVCILEGFQNQQSMLLADKVLKLLGKEKAKEKYKNREPLMPSPQFIKSYFSSFTDDIISQPMLKGEKSDEDKDKEGEALEVKENSGYLKAKQYMEEENYDKIISECSKEIDAEGKYMAEALLLRATFYLLIGNANAAKPDLDKVISLKEANVKLRANALIKRGSMYMQQQQPLLSTQDFNMAADIDPQNADVYHHRGQLKILLDQVEEAVADFDECIRLRPESALAQAQKCFALYRQAYTGNNSSQIQAAMKGFEEVIKKFPRCAEGYALYAQALTDQQQFGKADEMYDKCIDLEPDNATTYVHKGLLQLQWKQDLDRGLELISKAIEIDNKCDFAYETMGTIEVQRGNMEKAIDMFNKAINLAKSEMEMAHLYSLCDAAHAQTEVAKKYGLKPPTL

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
2	Acetylation	------MAASKPVEA ------CCCCCCCEE	22.05	19413330
4	Phosphorylation	----MAASKPVEAAV ----CCCCCCCEEEE	28.14	20068231
18	Phosphorylation	VVAAAVPSSGSGVGG EEEEECCCCCCCCCC	40.51	20068231
18	O-linked_Glycosylation	VVAAAVPSSGSGVGG EEEEECCCCCCCCCC	40.51	OGP
19	Phosphorylation	VAAAVPSSGSGVGGG EEEECCCCCCCCCCC	30.79	20068231
21	Phosphorylation	AAVPSSGSGVGGGGT EECCCCCCCCCCCCC	32.05	20068231
28	Phosphorylation	SGVGGGGTAGPGTGG CCCCCCCCCCCCCCC	31.54	30387612
33	Phosphorylation	GGTAGPGTGGLPRWQ CCCCCCCCCCCCHHH	31.07	20068231
69	Methylation	QQRRREARGRGDASG HHHHHHHCCCCCCCC	30.50	115918721
71	Methylation	RRREARGRGDASGLK HHHHHCCCCCCCCCC	33.98	24129315
75	Phosphorylation	ARGRGDASGLKRNSE HCCCCCCCCCCCCCC	49.77	20068231
78	Ubiquitination	RGDASGLKRNSERKT CCCCCCCCCCCCCCC	53.73	27667366
81	Phosphorylation	ASGLKRNSERKTPEG CCCCCCCCCCCCCCC	42.69	26074081
84	Ubiquitination	LKRNSERKTPEGRAS CCCCCCCCCCCCCCC	65.46	23503661
85	Phosphorylation	KRNSERKTPEGRASP CCCCCCCCCCCCCCC	32.56	20201521
89	Methylation	ERKTPEGRASPAPGS CCCCCCCCCCCCCCC	30.17	97812419
91	Phosphorylation	KTPEGRASPAPGSGH CCCCCCCCCCCCCCC	21.89	29255136
96	Phosphorylation	RASPAPGSGHPEGPG CCCCCCCCCCCCCCC	32.63	29255136
110	Phosphorylation	GAHLDMNSLDRAQAA CCCCCCCHHHHHHHH	25.63	29255136
118	Ubiquitination	LDRAQAAKNKGNKYF HHHHHHHHHCCCCCH	63.31	32142685
120	Ubiquitination	RAQAAKNKGNKYFKA HHHHHHHCCCCCHHC	64.25	32142685
123	Ubiquitination	AAKNKGNKYFKAGKY HHHHCCCCCHHCCHH	61.81	32142685
123	Acetylation	AAKNKGNKYFKAGKY HHHHCCCCCHHCCHH	61.81	26051181
126	Ubiquitination	NKGNKYFKAGKYEQA HCCCCCHHCCHHHHH	53.81	23503661
126	Acetylation	NKGNKYFKAGKYEQA HCCCCCHHCCHHHHH	53.81	26051181
129	Ubiquitination	NKYFKAGKYEQAIQC CCCHHCCHHHHHHHH	50.93	33845483
129	Acetylation	NKYFKAGKYEQAIQC CCCHHCCHHHHHHHH	50.93	25953088
130	Phosphorylation	KYFKAGKYEQAIQCY CCHHCCHHHHHHHHH	16.62	28152594
148	Ubiquitination	ISLCPTEKNVDLSTF HHCCCCCCCCCHHHH	65.82	23503661
153	Phosphorylation	TEKNVDLSTFYQNRA CCCCCCHHHHHHHHH	16.41	28152594
154	Phosphorylation	EKNVDLSTFYQNRAA CCCCCHHHHHHHHHH	33.39	28152594
156	Phosphorylation	NVDLSTFYQNRAAAF CCCHHHHHHHHHHHH	12.64	28152594
168	Ubiquitination	AAFEQLQKWKEVAQD HHHHHHHHHHHHHHH	69.68	23000965
168	2-Hydroxyisobutyrylation	AAFEQLQKWKEVAQD HHHHHHHHHHHHHHH	69.68	-
168	Acetylation	AAFEQLQKWKEVAQD HHHHHHHHHHHHHHH	69.68	26051181
170	Ubiquitination	FEQLQKWKEVAQDCT HHHHHHHHHHHHHHH	49.71	23000965
170	2-Hydroxyisobutyrylation	FEQLQKWKEVAQDCT HHHHHHHHHHHHHHH	49.71	-
170	Malonylation	FEQLQKWKEVAQDCT HHHHHHHHHHHHHHH	49.71	26320211
178	Acetylation	EVAQDCTKAVELNPK HHHHHHHHHHHHCHH	57.68	26051181
178	Ubiquitination	EVAQDCTKAVELNPK HHHHHHHHHHHHCHH	57.68	32015554
185	Acetylation	KAVELNPKYVKALFR HHHHHCHHHHHHHHH	62.70	19608861
185	Ubiquitination	KAVELNPKYVKALFR HHHHHCHHHHHHHHH	62.70	19608861
185	Malonylation	KAVELNPKYVKALFR HHHHHCHHHHHHHHH	62.70	26320211
188	Acetylation	ELNPKYVKALFRRAK HHCHHHHHHHHHHHH	35.96	26051181
188	Ubiquitination	ELNPKYVKALFRRAK HHCHHHHHHHHHHHH	35.96	23503661
188	2-Hydroxyisobutyrylation	ELNPKYVKALFRRAK HHCHHHHHHHHHHHH	35.96	-
188	Malonylation	ELNPKYVKALFRRAK HHCHHHHHHHHHHHH	35.96	26320211
199	2-Hydroxyisobutyrylation	RRAKAHEKLDNKKEC HHHHHHHHHCCHHHH	51.80	-
204	Ubiquitination	HEKLDNKKECLEDVT HHHHCCHHHHHHHHH	60.97	-
230	Ubiquitination	QSMLLADKVLKLLGK HHHHHHHHHHHHHCH	43.81	22817900
233	Ubiquitination	LLADKVLKLLGKEKA HHHHHHHHHHCHHHH	44.65	27667366
233	Malonylation	LLADKVLKLLGKEKA HHHHHHHHHHCHHHH	44.65	26320211
233	Acetylation	LLADKVLKLLGKEKA HHHHHHHHHHCHHHH	44.65	25953088
237	Ubiquitination	KVLKLLGKEKAKEKY HHHHHHCHHHHHHHH	56.88	22817900
239	Ubiquitination	LKLLGKEKAKEKYKN HHHHCHHHHHHHHCC	69.14	23000965
241	Ubiquitination	LLGKEKAKEKYKNRE HHCHHHHHHHHCCCC	66.85	23000965
243	Ubiquitination	GKEKAKEKYKNREPL CHHHHHHHHCCCCCC	61.90	23000965
245	Ubiquitination	EKAKEKYKNREPLMP HHHHHHHCCCCCCCC	61.67	23000965
253	Phosphorylation	NREPLMPSPQFIKSY CCCCCCCCHHHHHHH	19.85	25159151
258	Ubiquitination	MPSPQFIKSYFSSFT CCCHHHHHHHHHHCC	40.15	23503661
259	Phosphorylation	PSPQFIKSYFSSFTD CCHHHHHHHHHHCCC	26.96	22210691
260	Phosphorylation	SPQFIKSYFSSFTDD CHHHHHHHHHHCCCC	11.50	22210691
263	Phosphorylation	FIKSYFSSFTDDIIS HHHHHHHHCCCCHHC	23.44	20860994
265	Phosphorylation	KSYFSSFTDDIISQP HHHHHHCCCCHHCCC	34.41	20860994
270	Phosphorylation	SFTDDIISQPMLKGE HCCCCHHCCCHHCCC	28.68	29759185
275	Ubiquitination	IISQPMLKGEKSDED HHCCCHHCCCCCCCC	59.79	21906983
275	Neddylation	IISQPMLKGEKSDED HHCCCHHCCCCCCCC	59.79	32015554
275	Sumoylation	IISQPMLKGEKSDED HHCCCHHCCCCCCCC	59.79	28112733
278	Ubiquitination	QPMLKGEKSDEDKDK CCHHCCCCCCCCCCC	72.39	22817900
279	Phosphorylation	PMLKGEKSDEDKDKE CHHCCCCCCCCCCCC	41.76	21082442
283	Ubiquitination	GEKSDEDKDKEGEAL CCCCCCCCCCCCCCE	69.52	23503661
285	Ubiquitination	KSDEDKDKEGEALEV CCCCCCCCCCCCEEH	73.66	33845483
293	Ubiquitination	EGEALEVKENSGYLK CCCCEEHHHHCCCHH	41.63	21906983
300	Ubiquitination	KENSGYLKAKQYMEE HHHCCCHHHHHHHHH	45.08	22817900
302	Ubiquitination	NSGYLKAKQYMEEEN HCCCHHHHHHHHHHC	40.13	21906983
302	Acetylation	NSGYLKAKQYMEEEN HCCCHHHHHHHHHHC	40.13	27452117
310	Phosphorylation	QYMEEENYDKIISEC HHHHHHCHHHHHHHH	23.15	-
312	Ubiquitination	MEEENYDKIISECSK HHHHCHHHHHHHHHH	31.42	32015554
315	Phosphorylation	ENYDKIISECSKEID HCHHHHHHHHHHHCC	35.70	27174698
318	Phosphorylation	DKIISECSKEIDAEG HHHHHHHHHHCCCCC	29.31	27174698
319	Ubiquitination	KIISECSKEIDAEGK HHHHHHHHHCCCCCH	71.05	33845483
319	2-Hydroxyisobutyrylation	KIISECSKEIDAEGK HHHHHHHHHCCCCCH	71.05	-
319	Acetylation	KIISECSKEIDAEGK HHHHHHHHHCCCCCH	71.05	26051181
326	Ubiquitination	KEIDAEGKYMAEALL HHCCCCCHHHHHHHH	24.29	33845483
326	2-Hydroxyisobutyrylation	KEIDAEGKYMAEALL HHCCCCCHHHHHHHH	24.29	-
327	Phosphorylation	EIDAEGKYMAEALLL HCCCCCHHHHHHHHH	16.65	22817900
337	Phosphorylation	EALLLRATFYLLIGN HHHHHHHHHHHHHCC	13.33	22817900
339	Phosphorylation	LLLRATFYLLIGNAN HHHHHHHHHHHCCCC	9.02	18083107
349	Ubiquitination	IGNANAAKPDLDKVI HCCCCCCCCCHHHCC	36.33	23503661
354	Ubiquitination	AAKPDLDKVISLKEA CCCCCHHHCCCHHHH	49.09	23503661
357	Phosphorylation	PDLDKVISLKEANVK CCHHHCCCHHHHHHH	36.05	24719451
359	Acetylation	LDKVISLKEANVKLR HHHCCCHHHHHHHHH	48.25	30593047
359	Ubiquitination	LDKVISLKEANVKLR HHHCCCHHHHHHHHH	48.25	33845483
359	2-Hydroxyisobutyrylation	LDKVISLKEANVKLR HHHCCCHHHHHHHHH	48.25	-
364	Ubiquitination	SLKEANVKLRANALI CHHHHHHHHHHHHHH	31.87	23503661
364	2-Hydroxyisobutyrylation	SLKEANVKLRANALI CHHHHHHHHHHHHHH	31.87	-
372	Ubiquitination	LRANALIKRGSMYMQ HHHHHHHHHCCHHHH	52.11	24816145
372	2-Hydroxyisobutyrylation	LRANALIKRGSMYMQ HHHHHHHHHCCHHHH	52.11	-
427	Glutathionylation	AVADFDECIRLRPES HHCCHHHHHHHCHHH	2.06	22555962
434	Phosphorylation	CIRLRPESALAQAQK HHHHCHHHHHHHHHH	31.12	30266825
441	Acetylation	SALAQAQKCFALYRQ HHHHHHHHHHHHHHH	34.04	26051181
441	Ubiquitination	SALAQAQKCFALYRQ HHHHHHHHHHHHHHH	34.04	22053931
442	Glutathionylation	ALAQAQKCFALYRQA HHHHHHHHHHHHHHH	1.28	22555962
462	Sulfoxidation	SSQIQAAMKGFEEVI HHHHHHHHHCHHHHH	4.97	28465586
463	Ubiquitination	SQIQAAMKGFEEVIK HHHHHHHHCHHHHHH	56.58	23503661
470	Acetylation	KGFEEVIKKFPRCAE HCHHHHHHHCCCHHH	54.24	19608861
470	Ubiquitination	KGFEEVIKKFPRCAE HCHHHHHHHCCCHHH	54.24	32142685
470	Succinylation	KGFEEVIKKFPRCAE HCHHHHHHHCCCHHH	54.24	23954790
471	Ubiquitination	GFEEVIKKFPRCAEG CHHHHHHHCCCHHHH	49.86	23503661
475	Glutathionylation	VIKKFPRCAEGYALY HHHHCCCHHHHHHHH	4.04	22555962
501	2-Hydroxyisobutyrylation	KADEMYDKCIDLEPD CHHHHHHHHCCCCCC	18.66	-
501	Acetylation	KADEMYDKCIDLEPD CHHHHHHHHCCCCCC	18.66	26051181
502	Glutathionylation	ADEMYDKCIDLEPDN HHHHHHHHCCCCCCC	2.40	22555962
516	Ubiquitination	NATTYVHKGLLQLQW CCHHHHHHHHHHHHH	41.01	29967540
524	Ubiquitination	GLLQLQWKQDLDRGL HHHHHHHHCHHHHHH	22.45	32142685
524	2-Hydroxyisobutyrylation	GLLQLQWKQDLDRGL HHHHHHHHCHHHHHH	22.45	-
536	Ubiquitination	RGLELISKAIEIDNK HHHHHHHHHHHHCCC	46.52	32015554
536	2-Hydroxyisobutyrylation	RGLELISKAIEIDNK HHHHHHHHHHHHCCC	46.52	-
544	Glutathionylation	AIEIDNKCDFAYETM HHHHCCCCCCCHHHC	6.97	22555962
563	Ubiquitination	VQRGNMEKAIDMFNK EECCCHHHHHHHHHH	39.61	23503661
563	2-Hydroxyisobutyrylation	VQRGNMEKAIDMFNK EECCCHHHHHHHHHH	39.61	-
570	Ubiquitination	KAIDMFNKAINLAKS HHHHHHHHHHHHHHH	39.10	32142685
570	2-Hydroxyisobutyrylation	KAIDMFNKAINLAKS HHHHHHHHHHHHHHH	39.10	-
570	Acetylation	KAIDMFNKAINLAKS HHHHHHHHHHHHHHH	39.10	26051181
576	Ubiquitination	NKAINLAKSEMEMAH HHHHHHHHHHHHHHH	50.55	23503661
601	Phosphorylation	QTEVAKKYGLKPPTL HHHHHHHHCCCCCCC	27.30	-
604	Ubiquitination	VAKKYGLKPPTL--- HHHHHCCCCCCC---	44.58	33845483
607	Phosphorylation	KYGLKPPTL------ HHCCCCCCC------	54.34	-

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

Oops, there are no upstream regulatory protein records of TOM70_HUMAN !!

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of TOM70_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 TOM70_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
TOM7_HUMAN	TOMM7	physical	22939629
TRADD_HUMAN	TRADD	physical	20628368
TRAF6_HUMAN	TRAF6	physical	20628368
STING_HUMAN	TMEM173	physical	20628368
MAVS_HUMAN	MAVS	physical	20628368
HS90A_HUMAN	HSP90AA1	physical	20628368
IRF3_HUMAN	IRF3	physical	20628368
TBK1_HUMAN	TBK1	physical	20628368
PRKN_HUMAN	PARK2	physical	24149440
RAB1A_HUMAN	RAB1A	physical	26344197
PRKN_HUMAN	PARK2	physical	25591737

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

Acetylation

"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 THR-85 AND SER-91, AND MASS SPECTROMETRY.
PubMed: 19413330

"Lysine acetylation targets protein complexes and co-regulates majorcellular functions.";
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.,Olsen J.V., Mann M.;
Science 325:834-840(2009).
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-185 AND LYS-470, AND MASSSPECTROMETRY.
PubMed: 19608861

Phosphorylation

"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 THR-85 AND SER-91, AND MASS SPECTROMETRY.
PubMed: 19413330

"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-91, AND MASSSPECTROMETRY.
PubMed: 18669648

"Kinase-selective enrichment enables quantitative phosphoproteomics ofthe kinome across the cell cycle.";
Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,Greff Z., Keri G., Stemmann O., Mann M.;
Mol. Cell 31:438-448(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-91, AND MASSSPECTROMETRY.
PubMed: 18691976

"Phosphoproteome of resting human platelets.";
Zahedi R.P., Lewandrowski U., Wiesner J., Wortelkamp S., Moebius J.,Schuetz C., Walter U., Gambaryan S., Sickmann A.;
J. Proteome Res. 7:526-534(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-91, AND MASSSPECTROMETRY.
PubMed: 18088087

"Improved titanium dioxide enrichment of phosphopeptides from HeLacells and high confident phosphopeptide identification by cross-validation of MS/MS and MS/MS/MS spectra.";
Yu L.-R., Zhu Z., Chan K.C., Issaq H.J., Dimitrov D.S., Veenstra T.D.;
J. Proteome Res. 6:4150-4162(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-91, AND MASSSPECTROMETRY.
PubMed: 17924679