TOM1_HUMAN - dbPTM
TOM1_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID TOM1_HUMAN
UniProt AC O60784
Protein Name Target of Myb protein 1
Gene Name TOM1
Organism Homo sapiens (Human).
Sequence Length 492
Subcellular Localization Cytoplasm . Membrane
Peripheral membrane protein .
Protein Description May be involved in intracellular trafficking. Probable association with membranes..
Protein Sequence MDFLLGNPFSSPVGQRIEKATDGSLQSEDWALNMEICDIINETEEGPKDALRAVKKRIVGNKNFHEVMLALTVLETCVKNCGHRFHVLVASQDFVESVLVRTILPKNNPPTIVHDKVLNLIQSWADAFRSSPDLTGVVTIYEDLRRKGLEFPMTDLDMLSPIHTPQRTVFNSETQSGQDSVGTDSSQQEDSGQHAAPLPAPPILSGDTPIAPTPEQIGKLRSELEMVSGNVRVMSEMLTELVPTQAEPADLELLQELNRTCRAMQQRVLELIPQIANEQLTEELLIVNDNLNNVFLRHERFERFRTGQTTKAPSEAEPAADLIDMGPDPAATGNLSSQLAGMNLGSSSVRAGLQSLEASGRLEDEFDMFALTRGSSLADQRKEVKYEAPQATDGLAGALDARQQSTGAIPVTQACLMEDIEQWLSTDVGNDAEEPKGVTSEEFDKFLEERAKAADRLPNLSSPSAEGPPGPPSGPAPRKKTQEKDDDMLFAL
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
1Acetylation-------MDFLLGNP
-------CCCCCCCC		8.0922223895
10PhosphorylationFLLGNPFSSPVGQRI
CCCCCCCCCCCHHHH		34.6823663014
11PhosphorylationLLGNPFSSPVGQRIE
CCCCCCCCCCHHHHH		24.8023663014
11 (in isoform 2)Phosphorylation-24.8024719451
73 (in isoform 4)Ubiquitination-4.7721890473
106UbiquitinationLVRTILPKNNPPTIV
HHHHHCCCCCCCCCH		66.95-
106 (in isoform 2)Ubiquitination-66.9521890473
106MalonylationLVRTILPKNNPPTIV
HHHHHCCCCCCCCCH		66.9526320211
106AcetylationLVRTILPKNNPPTIV
HHHHHCCCCCCCCCH		66.9523236377
106 (in isoform 1)Ubiquitination-66.9521890473
106 (in isoform 3)Ubiquitination-66.9521890473
114 (in isoform 4)Ubiquitination-25.8921890473
116UbiquitinationPPTIVHDKVLNLIQS
CCCCHHHHHHHHHHH		33.47-
130PhosphorylationSWADAFRSSPDLTGV
HHHHHHHHCCCCCCE		39.5119060867
131PhosphorylationWADAFRSSPDLTGVV
HHHHHHHCCCCCCEE		20.4119060867
131 (in isoform 2)Phosphorylation-20.4127251275
135PhosphorylationFRSSPDLTGVVTIYE
HHHCCCCCCEEEEHH		35.00-
139PhosphorylationPDLTGVVTIYEDLRR
CCCCCEEEEHHHHHH		18.5528152594
141 (in isoform 2)Phosphorylation-8.2727642862
141PhosphorylationLTGVVTIYEDLRRKG
CCCEEEEHHHHHHCC		8.2728152594
147UbiquitinationIYEDLRRKGLEFPMT
EHHHHHHCCCCCCCC		62.5021906983
147 (in isoform 2)Ubiquitination-62.5021890473
147 (in isoform 1)Ubiquitination-62.5021890473
147UbiquitinationIYEDLRRKGLEFPMT
EHHHHHHCCCCCCCC		62.5022053931
154PhosphorylationKGLEFPMTDLDMLSP
CCCCCCCCCHHHCCC		33.3829255136
160PhosphorylationMTDLDMLSPIHTPQR
CCCHHHCCCCCCCCC		18.3829255136
160 (in isoform 2)Phosphorylation-18.3824719451
164PhosphorylationDMLSPIHTPQRTVFN
HHCCCCCCCCCEEEE		23.1029255136
164 (in isoform 2)Phosphorylation-23.1024719451
168PhosphorylationPIHTPQRTVFNSETQ
CCCCCCCEEEECCCC		24.9726074081
172PhosphorylationPQRTVFNSETQSGQD
CCCEEEECCCCCCCC		30.4726074081
174PhosphorylationRTVFNSETQSGQDSV
CEEEECCCCCCCCCC		28.0526074081
176PhosphorylationVFNSETQSGQDSVGT
EEECCCCCCCCCCCC		45.9326074081
180PhosphorylationETQSGQDSVGTDSSQ
CCCCCCCCCCCCCCC		17.9828348404
183PhosphorylationSGQDSVGTDSSQQED
CCCCCCCCCCCCCCC		30.4728348404
185 (in isoform 2)Phosphorylation-29.8627251275
185PhosphorylationQDSVGTDSSQQEDSG
CCCCCCCCCCCCCCC		29.8628348404
186PhosphorylationDSVGTDSSQQEDSGQ
CCCCCCCCCCCCCCC		38.4028348404
191PhosphorylationDSSQQEDSGQHAAPL
CCCCCCCCCCCCCCC		39.3328348404
219 (in isoform 2)Ubiquitination-42.21-
222PhosphorylationEQIGKLRSELEMVSG
HHHHHHHHHHHHHHC		57.9021406692
228PhosphorylationRSELEMVSGNVRVMS
HHHHHHHHCCHHHHH		24.2826074081
235PhosphorylationSGNVRVMSEMLTELV
HCCHHHHHHHHHHHC		19.5926074081
239PhosphorylationRVMSEMLTELVPTQA
HHHHHHHHHHCCCCC		26.4326074081
244PhosphorylationMLTELVPTQAEPADL
HHHHHCCCCCCCCHH		32.6926074081
260PhosphorylationLLQELNRTCRAMQQR
HHHHHHHHHHHHHHH		12.7930257219
311UbiquitinationFRTGQTTKAPSEAEP
HHCCCCCCCCCCCCC		62.7821906983
311 (in isoform 2)Ubiquitination-62.78-
314 (in isoform 2)Phosphorylation-55.0627251275
314PhosphorylationGQTTKAPSEAEPAAD
CCCCCCCCCCCCHHH		55.0628348404
332PhosphorylationMGPDPAATGNLSSQL
CCCCHHHCCCHHHHH		28.8028102081
336PhosphorylationPAATGNLSSQLAGMN
HHHCCCHHHHHCCCC		21.7528102081
337PhosphorylationAATGNLSSQLAGMNL
HHCCCHHHHHCCCCC		32.1728102081
337 (in isoform 3)Ubiquitination-32.1721890473
340 (in isoform 3)Ubiquitination-13.9321890473
346PhosphorylationLAGMNLGSSSVRAGL
HCCCCCCCHHHHHHH		23.7028348404
347 (in isoform 2)Phosphorylation-30.9327251275
347PhosphorylationAGMNLGSSSVRAGLQ
CCCCCCCHHHHHHHH		30.9328348404
348PhosphorylationGMNLGSSSVRAGLQS
CCCCCCHHHHHHHHH		19.8122210691
349 (in isoform 4)Ubiquitination-5.4121890473
352 (in isoform 4)Ubiquitination-17.4321890473
355PhosphorylationSVRAGLQSLEASGRL
HHHHHHHHHHHHCCC		32.9729255136
355 (in isoform 2)Phosphorylation-32.9724719451
359PhosphorylationGLQSLEASGRLEDEF
HHHHHHHHCCCCCCH		18.3119664994
359 (in isoform 2)Phosphorylation-18.3124719451
375PhosphorylationMFALTRGSSLADQRK
HHHHHCCCCHHHHHH		20.9129396449
376PhosphorylationFALTRGSSLADQRKE
HHHHCCCCHHHHHHH		30.3323911959
376 (in isoform 2)Phosphorylation-30.3324719451
382UbiquitinationSSLADQRKEVKYEAP
CCHHHHHHHHCCCCC		62.3121906983
382 (in isoform 2)Ubiquitination-62.3121890473
382 (in isoform 1)Ubiquitination-62.3121890473
385UbiquitinationADQRKEVKYEAPQAT
HHHHHHHCCCCCCCC		38.1621906983
385 (in isoform 2)Ubiquitination-38.1621890473
385SumoylationADQRKEVKYEAPQAT
HHHHHHHCCCCCCCC		38.1628112733
385 (in isoform 1)Ubiquitination-38.1621890473
385UbiquitinationADQRKEVKYEAPQAT
HHHHHHHCCCCCCCC		38.1622053931
386PhosphorylationDQRKEVKYEAPQATD
HHHHHHCCCCCCCCC		23.6221945579
386 (in isoform 2)Phosphorylation-23.6227642862
392PhosphorylationKYEAPQATDGLAGAL
CCCCCCCCCCHHHHH		25.9221945579
405PhosphorylationALDARQQSTGAIPVT
HHCHHHHCCCCCCHH		22.0722798277
406PhosphorylationLDARQQSTGAIPVTQ
HCHHHHCCCCCCHHH		26.7127251275
410 (in isoform 4)Ubiquitination-23.6721890473
413 (in isoform 4)Ubiquitination-30.2521890473
425PhosphorylationEDIEQWLSTDVGNDA
HHHHHHHCCCCCCCC		21.4327251275
426PhosphorylationDIEQWLSTDVGNDAE
HHHHHHCCCCCCCCC		32.3127251275
439PhosphorylationAEEPKGVTSEEFDKF
CCCCCCCCHHHHHHH		38.8029514088
440PhosphorylationEEPKGVTSEEFDKFL
CCCCCCCHHHHHHHH		32.4929514088
443 (in isoform 2)Ubiquitination-12.4321890473
445UbiquitinationVTSEEFDKFLEERAK
CCHHHHHHHHHHHHH		58.11-
446 (in isoform 2)Ubiquitination-12.8121890473
452UbiquitinationKFLEERAKAADRLPN
HHHHHHHHHHHCCCC		50.78-
453 (in isoform 2)Ubiquitination-17.38-
461PhosphorylationADRLPNLSSPSAEGP
HHCCCCCCCCCCCCC		47.0129255136
462PhosphorylationDRLPNLSSPSAEGPP
HCCCCCCCCCCCCCC		26.4929255136
463 (in isoform 2)Phosphorylation-33.9024719451
464PhosphorylationLPNLSSPSAEGPPGP
CCCCCCCCCCCCCCC		40.6829255136
465 (in isoform 2)Phosphorylation-29.2027251275
473PhosphorylationEGPPGPPSGPAPRKK
CCCCCCCCCCCCCCC		61.6229255136
474 (in isoform 2)Phosphorylation-28.3227251275
481PhosphorylationGPAPRKKTQEKDDDM
CCCCCCCCCCCCCCC		45.0229214152
482 (in isoform 2)Phosphorylation-65.7024719451
484UbiquitinationPRKKTQEKDDDMLFA
CCCCCCCCCCCCCCC		57.5521906983
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
-KUbiquitinationE3 ubiquitin ligaseSMURF1Q9HCE7
PMID:20804422
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of TOM1_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 TOM1_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
TOLIP_HUMANTOLLIPphysical
14563850
ZFY16_HUMANZFYVE16physical
14613930
CLH1_HUMANCLTCphysical
14563850
TS101_HUMANTSG101physical
18367816
UBC_HUMANUBCphysical
16199040
TOLIP_HUMANTOLLIPphysical
16412388
CLH1_HUMANCLTCphysical
16412388
CLH1_HUMANCLTCphysical
15657082
UB2D1_HUMANUBE2D1physical
19578373
A4_HUMANAPPphysical
21832049
UBC_BOVINUBCphysical
20150893
MAOX_HUMANME1physical
22863883
YAP1_HUMANYAP1physical
22863883
TOLIP_HUMANTOLLIPphysical
25416956
TOLIP_HUMANTOLLIPphysical
15047686
DOHH_HUMANDOHHphysical
26344197
TOLIP_HUMANTOLLIPphysical
26320582
UBC_HUMANUBCphysical
26320582
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 TOM1_HUMAN

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Related Literatures of Post-Translational Modification
Acetylation
ReferencePubMed
"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 MET-1, AND MASS SPECTROMETRY.
Phosphorylation
ReferencePubMed
"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-160 AND THR-164, ANDMASS SPECTROMETRY.
"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-160; THR-164; SER-355AND SER-462, AND MASS SPECTROMETRY.
"Automated phosphoproteome analysis for cultured cancer cells by two-dimensional nanoLC-MS using a calcined titania/C18 biphasic column.";
Imami K., Sugiyama N., Kyono Y., Tomita M., Ishihama Y.;
Anal. Sci. 24:161-166(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-130; SER-131 ANDTHR-139, AND MASS SPECTROMETRY.
"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-461 AND SER-464, ANDMASS SPECTROMETRY.
"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-462, AND MASSSPECTROMETRY.
"An extensive survey of tyrosine phosphorylation revealing new sitesin human mammary epithelial cells.";
Heibeck T.H., Ding S.-J., Opresko L.K., Zhao R., Schepmoes A.A.,Yang F., Tolmachev A.V., Monroe M.E., Camp D.G. II, Smith R.D.,Wiley H.S., Qian W.-J.;
J. Proteome Res. 8:3852-3861(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-386, AND MASSSPECTROMETRY.

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