TOM70_MOUSE - dbPTM
TOM70_MOUSE - PTM Information in dbPTM
Basic Information of Protein
UniProt ID TOM70_MOUSE
UniProt AC Q9CZW5
Protein Name Mitochondrial import receptor subunit TOM70
Gene Name Tomm70 {ECO:0000250|UniProtKB:O94826}
Organism Mus musculus (Mouse).
Sequence Length 611
Subcellular Localization Mitochondrion outer membrane
Single-pass membrane protein.
Protein Description Receptor that accelerates the import of all mitochondrial precursor proteins..
Protein Sequence MAASKPIEAAMAAAAAPGSGNGVGGGGGTAGPGSGAGTLPRWHVALAIGAPLLLGAGAMYLWSRRRRRREAGGRGDASGLKRNSERKTPEGRASPALGSGHHDGSGDSLEMSSLDRAQAAKNKGNKYFKAGKYEQAIQCYTEAISLCPTEKNVDLSTFYQNRAAAFEQLQKWKEVAQDCTKAVELNPKYVKALFRRAKAHEKLDNKKECLEDVTAVCILEGFQNEQSMLLADKVLKLLGKENAKEKYKNREPLMPSPQFIKSYFSSFTDDIISQPMLKGEKSDEDKDKEGEALEVKENSGYLKAKQYMEEENYDKIISECSKEIDAQGKYMAEALLLRATFYLLIGSANAAKPDLDKVISLKEANVKLRANALIKRGTMCMQQQQPMLSTQDFNMAAEIDPMNSDVYHHRGQLKILLDLVEEAVADFDACIRLRPKFALAQAQKCFALYRQAYTANNSSQVQAAMKGFEEIIKKFPRCAEGYALYAQALTDQQQFGKADEMYDKCIDLEPDNATTYVHKGLLQLQWKQDLDKGLELISKAIEIDNKCDFAYETMGTIEVQRGNMEKAIDMFNKAINLAKSEMEMAHLYSLCDAAHAQTEVAKKYGLKPPTL
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 Orthologous
Protein Cluster
2Acetylation------MAASKPIEA
------CCCCHHHHH		22.05-
19PhosphorylationAAAAAPGSGNGVGGG
HHHHCCCCCCCCCCC		28.20-
74MethylationRRREAGGRGDASGLK
HHHHHCCCCCHHHCC		38.61-
84PhosphorylationASGLKRNSERKTPEG
HHHCCCCCCCCCCCC		42.6924704852
88PhosphorylationKRNSERKTPEGRASP
CCCCCCCCCCCCCCC		32.5626824392
94PhosphorylationKTPEGRASPALGSGH
CCCCCCCCCCCCCCC		14.8924925903
94O-linked_GlycosylationKTPEGRASPALGSGH
CCCCCCCCCCCCCCC		14.893966685
99PhosphorylationRASPALGSGHHDGSG
CCCCCCCCCCCCCCC		35.4824925903
105PhosphorylationGSGHHDGSGDSLEMS
CCCCCCCCCCCCCCC		45.5524925903
108PhosphorylationHHDGSGDSLEMSSLD
CCCCCCCCCCCCHHH		29.7424925903
112PhosphorylationSGDSLEMSSLDRAQA
CCCCCCCCHHHHHHH		20.5524925903
113AcetylationGDSLEMSSLDRAQAA
CCCCCCCHHHHHHHH		32.74-
113PhosphorylationGDSLEMSSLDRAQAA
CCCCCCCHHHHHHHH		32.7424925903
126MalonylationAAKNKGNKYFKAGKY
HHHHHCCCCHHCCHH		61.8126320211
126AcetylationAAKNKGNKYFKAGKY
HHHHHCCCCHHCCHH		61.8123201123
126UbiquitinationAAKNKGNKYFKAGKY
HHHHHCCCCHHCCHH		61.8127667366
151UbiquitinationISLCPTEKNVDLSTF
HHCCCCCCCCCHHHH		65.82-
171UbiquitinationAAFEQLQKWKEVAQD
HHHHHHHHHHHHHHH		69.6827667366
173MalonylationFEQLQKWKEVAQDCT
HHHHHHHHHHHHHHH		49.7126320211
179S-nitrosylationWKEVAQDCTKAVELN
HHHHHHHHHHHHHHC		2.5321278135
179S-nitrosocysteineWKEVAQDCTKAVELN
HHHHHHHHHHHHHHC		2.53-
181MalonylationEVAQDCTKAVELNPK
HHHHHHHHHHHHCHH		57.6826320211
188UbiquitinationKAVELNPKYVKALFR
HHHHHCHHHHHHHHH		62.70-
188AcetylationKAVELNPKYVKALFR
HHHHHCHHHHHHHHH		62.7023864654
188MalonylationKAVELNPKYVKALFR
HHHHHCHHHHHHHHH		62.7026320211
191MalonylationELNPKYVKALFRRAK
HHCHHHHHHHHHHHH		35.9626320211
236UbiquitinationLLADKVLKLLGKENA
HHHHHHHHHHCHHHH		44.6527667366
248UbiquitinationENAKEKYKNREPLMP
HHHHHHHCCCCCCCC		61.67-
256PhosphorylationNREPLMPSPQFIKSY
CCCCCCCCHHHHHHH		19.85-
262PhosphorylationPSPQFIKSYFSSFTD
CCHHHHHHHHHHCCC		26.9626643407
263PhosphorylationSPQFIKSYFSSFTDD
CHHHHHHHHHHCCCC		11.5026643407
265PhosphorylationQFIKSYFSSFTDDII
HHHHHHHHHCCCCHH		19.1326643407
266PhosphorylationFIKSYFSSFTDDIIS
HHHHHHHHCCCCHHC		23.4426643407
268PhosphorylationKSYFSSFTDDIISQP
HHHHHHCCCCHHCCC		34.4126643407
273PhosphorylationSFTDDIISQPMLKGE
HCCCCHHCCCHHCCC		28.6829899451
278UbiquitinationIISQPMLKGEKSDED
HHCCCHHCCCCCCCC		59.79-
282PhosphorylationPMLKGEKSDEDKDKE
CHHCCCCCCCCCCCC		41.7624899341
286AcetylationGEKSDEDKDKEGEAL
CCCCCCCCCCCCCCE		69.5223201123
288AcetylationKSDEDKDKEGEALEV
CCCCCCCCCCCCEEH		73.6623954790
296UbiquitinationEGEALEVKENSGYLK
CCCCEEHHHHCCCHH		41.63-
305UbiquitinationNSGYLKAKQYMEEEN
HCCCHHHHHHHHHHC		40.13-
307PhosphorylationGYLKAKQYMEEENYD
CCHHHHHHHHHHCHH		13.0425195567
313PhosphorylationQYMEEENYDKIISEC
HHHHHHCHHHHHHHH		23.1525195567
315AcetylationMEEENYDKIISECSK
HHHHCHHHHHHHHHH		31.4223864654
322MalonylationKIISECSKEIDAQGK
HHHHHHHHHHCCCCH		71.0526320211
362UbiquitinationLDKVISLKEANVKLR
HHHCCCHHHHHHHHH		48.2527667366
436AcetylationACIRLRPKFALAQAQ
HHHHHCHHHHHHHHH		36.5123864654
436MalonylationACIRLRPKFALAQAQ
HHHHHCHHHHHHHHH		36.5126320211
436UbiquitinationACIRLRPKFALAQAQ
HHHHHCHHHHHHHHH		36.5127667366
444UbiquitinationFALAQAQKCFALYRQ
HHHHHHHHHHHHHHH		34.04-
466UbiquitinationSQVQAAMKGFEEIIK
HHHHHHHHCHHHHHH		56.58-
473MalonylationKGFEEIIKKFPRCAE
HCHHHHHHHCCCHHH		54.7626320211
519AcetylationNATTYVHKGLLQLQW
CCHHHHHHHHHHHHH		41.0123864654
532UbiquitinationQWKQDLDKGLELISK
HHHHCHHHHHHHHHH		73.0927667366
566UbiquitinationVQRGNMEKAIDMFNK
EECCCHHHHHHHHHH		39.61-
573UbiquitinationKAIDMFNKAINLAKS
HHHHHHHHHHHHHHH		39.10-
607UbiquitinationVAKKYGLKPPTL---
HHHHHCCCCCCC---		44.5827667366
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 TOM70_MOUSE !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of TOM70_MOUSE !!
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 TOM70_MOUSE !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions

Oops, there are no PPI records of TOM70_MOUSE !!
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of TOM70_MOUSE

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Large scale localization of protein phosphorylation by use ofelectron capture dissociation mass spectrometry.";
Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.;
Mol. Cell. Proteomics 8:904-912(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-94, AND MASSSPECTROMETRY.
"The phagosomal proteome in interferon-gamma-activated macrophages.";
Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,Thibault P.;
Immunity 30:143-154(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-94, AND MASSSPECTROMETRY.
"Solid tumor proteome and phosphoproteome analysis by high resolutionmass spectrometry.";
Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J.,Faessler R., Mann M.;
J. Proteome Res. 7:5314-5326(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-94, AND MASSSPECTROMETRY.
"Specific phosphopeptide enrichment with immobilized titanium ionaffinity chromatography adsorbent for phosphoproteome analysis.";
Zhou H., Ye M., Dong J., Han G., Jiang X., Wu R., Zou H.;
J. Proteome Res. 7:3957-3967(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-94, AND MASSSPECTROMETRY.
"Mitochondrial phosphoproteome revealed by an improved IMAC method andMS/MS/MS.";
Lee J., Xu Y., Chen Y., Sprung R., Kim S.C., Xie S., Zhao Y.;
Mol. Cell. Proteomics 6:669-676(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-88 AND SER-94, AND MASSSPECTROMETRY.

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