TM1L2_HUMAN - dbPTM
TM1L2_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID TM1L2_HUMAN
UniProt AC Q6ZVM7
Protein Name TOM1-like protein 2
Gene Name TOM1L2
Organism Homo sapiens (Human).
Sequence Length 507
Subcellular Localization
Protein Description Probable role in protein transport. May regulate growth factor-induced mitogenic signaling..
Protein Sequence MEFLLGNPFSTPVGQCLEKATDGSLQSEDWTLNMEICDIINETEEGPKDAIRALKKRLNGNRNYREVMLALTVLETCVKNCGHRFHILVANRDFIDSVLVKIISPKNNPPTIVQDKVLALIQAWADAFRSSPDLTGVVHIYEELKRKGVEFPMADLDALSPIHTPQRSVPEVDPAATMPRSQSQQRTSAGSYSSPPPAPYSAPQAPALSVTGPITANSEQIARLRSELDVVRGNTKVMSEMLTEMVPGQEDSSDLELLQELNRTCRAMQQRIVELISRVSNEEVTEELLHVNDDLNNVFLRYERFERYRSGRSVQNASNGVLNEVTEDNLIDLGPGSPAVVSPMVGNTAPPSSLSSQLAGLDLGTESVSGTLSSLQQCNPRDGFDMFAQTRGNSLAEQRKTVTYEDPQAVGGLASALDNRKQSSEGIPVAQPSVMDDIEVWLRTDLKGDDLEEGVTSEEFDKFLEERAKAAEMVPDLPSPPMEAPAPASNPSGRKKPERSEDALFAL
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
48UbiquitinationNETEEGPKDAIRALK
HCCCCCHHHHHHHHH		71.32-
95 (in isoform 2)Ubiquitination-4.5221890473
101 (in isoform 3)Ubiquitination-30.1121890473
101UbiquitinationFIDSVLVKIISPKNN
HHCEEEEEHHCCCCC		30.1121890473
101 (in isoform 1)Ubiquitination-30.1121890473
101UbiquitinationFIDSVLVKIISPKNN
HHCEEEEEHHCCCCC		30.1121890473
104PhosphorylationSVLVKIISPKNNPPT
EEEEEHHCCCCCCCC		33.0424719451
106UbiquitinationLVKIISPKNNPPTIV
EEEHHCCCCCCCCHH		63.6721890473
106 (in isoform 3)Ubiquitination-63.6721890473
106 (in isoform 1)Ubiquitination-63.6721890473
106UbiquitinationLVKIISPKNNPPTIV
EEEHHCCCCCCCCHH		63.6721890473
110PhosphorylationISPKNNPPTIVQDKV
HCCCCCCCCHHHHHH		36.56-
114PhosphorylationNNPPTIVQDKVLALI
CCCCCHHHHHHHHHH		40.74-
127PhosphorylationLIQAWADAFRSSPDL
HHHHHHHHHHHCCCC		8.26-
131PhosphorylationWADAFRSSPDLTGVV
HHHHHHHCCCCCHHH		20.41-
133 (in isoform 4)Ubiquitination-59.8321890473
141PhosphorylationLTGVVHIYEELKRKG
CCHHHHHHHHHHHCC		6.6228152594
145 (in isoform 1)Ubiquitination-56.1721890473
145UbiquitinationVHIYEELKRKGVEFP
HHHHHHHHHCCCCCC		56.1721890473
145UbiquitinationVHIYEELKRKGVEFP
HHHHHHHHHCCCCCC		56.1721890473
147 (in isoform 1)Ubiquitination-66.7621890473
147UbiquitinationIYEELKRKGVEFPMA
HHHHHHHCCCCCCCC		66.7621890473
147UbiquitinationIYEELKRKGVEFPMA
HHHHHHHCCCCCCCC		66.7621890473
150PhosphorylationELKRKGVEFPMADLD
HHHHCCCCCCCCCHH		53.34-
154 (in isoform 4)Ubiquitination-17.9121890473
160 (in isoform 5)Phosphorylation-24.4325159151
160PhosphorylationMADLDALSPIHTPQR
CCCHHHCCCCCCCCC		24.4325159151
164 (in isoform 5)Phosphorylation-23.1025159151
164PhosphorylationDALSPIHTPQRSVPE
HHCCCCCCCCCCCCC		23.1025159151
168PhosphorylationPIHTPQRSVPEVDPA
CCCCCCCCCCCCCHH		36.4628060719
177PhosphorylationPEVDPAATMPRSQSQ
CCCCHHHCCCCCCCC		29.7918212344
180 (in isoform 4)Ubiquitination-36.1821890473
183UbiquitinationATMPRSQSQQRTSAG
HCCCCCCCCCCCCCC		29.5321890473
186 (in isoform 2)Ubiquitination-24.0221890473
187PhosphorylationRSQSQQRTSAGSYSS
CCCCCCCCCCCCCCC		20.7021945579
188PhosphorylationSQSQQRTSAGSYSSP
CCCCCCCCCCCCCCC		32.5921945579
191PhosphorylationQQRTSAGSYSSPPPA
CCCCCCCCCCCCCCC		22.8921945579
191 (in isoform 3)Ubiquitination-22.8921890473
192PhosphorylationQRTSAGSYSSPPPAP
CCCCCCCCCCCCCCC		16.5521945579
193PhosphorylationRTSAGSYSSPPPAPY
CCCCCCCCCCCCCCC		37.7621945579
194PhosphorylationTSAGSYSSPPPAPYS
CCCCCCCCCCCCCCC		32.9421945579
195 (in isoform 4)Ubiquitination-32.7121890473
200PhosphorylationSSPPPAPYSAPQAPA
CCCCCCCCCCCCCCC		21.4121945579
201PhosphorylationSPPPAPYSAPQAPAL
CCCCCCCCCCCCCCE		32.2021945579
202 (in isoform 4)Ubiquitination-8.3821890473
209PhosphorylationAPQAPALSVTGPITA
CCCCCCEEECCCCCC		21.5321945579
211PhosphorylationQAPALSVTGPITANS
CCCCEEECCCCCCCH		33.5921945579
226PhosphorylationEQIARLRSELDVVRG
HHHHHHHHHHHHHHC		47.2928857561
236UbiquitinationDVVRGNTKVMSEMLT
HHHHCCHHHHHHHHH		39.6821906983
236 (in isoform 1)Ubiquitination-39.6821890473
264PhosphorylationLLQELNRTCRAMQQR
HHHHHHHHHHHHHHH		12.7926074081
277PhosphorylationQRIVELISRVSNEEV
HHHHHHHHHCCCHHH		38.9726074081
280PhosphorylationVELISRVSNEEVTEE
HHHHHHCCCHHHHHH		37.1026074081
347UbiquitinationVVSPMVGNTAPPSSL
CCCCCCCCCCCCCHH		22.9721890473
350 (in isoform 2)Ubiquitination-27.5421890473
354PhosphorylationNTAPPSSLSSQLAGL
CCCCCCHHHHHHCCC		7.1917389395
355 (in isoform 3)Ubiquitination-20.2721890473
370 (in isoform 5)Phosphorylation-28.6426657352
371 (in isoform 5)Phosphorylation-18.8929978859
371PhosphorylationGTESVSGTLSSLQQC
CCCCCCCHHHHHHHC		18.8929759185
371 (in isoform 2)Ubiquitination-18.8921890473
373PhosphorylationESVSGTLSSLQQCNP
CCCCCHHHHHHHCCC		28.9220068231
374 (in isoform 5)Phosphorylation-33.0525159151
376 (in isoform 3)Ubiquitination-47.9621890473
377 (in isoform 5)Phosphorylation-33.9629978859
378 (in isoform 5)Phosphorylation-4.9625627689
394PhosphorylationFAQTRGNSLAEQRKT
CHHHCCCCHHHHHCC		31.6120068231
397 (in isoform 2)Ubiquitination-57.1021890473
400UbiquitinationNSLAEQRKTVTYEDP
CCHHHHHCCEECCCH		47.2221890473
400 (in isoform 1)Ubiquitination-47.2221890473
401PhosphorylationSLAEQRKTVTYEDPQ
CHHHHHCCEECCCHH		21.9221945579
402 (in isoform 3)Ubiquitination-6.3521890473
403PhosphorylationAEQRKTVTYEDPQAV
HHHHCCEECCCHHHH		26.8221945579
404PhosphorylationEQRKTVTYEDPQAVG
HHHCCEECCCHHHHH		17.6321945579
412 (in isoform 2)Ubiquitination-16.0921890473
415PhosphorylationQAVGGLASALDNRKQ
HHHHHHHHHHHHCCC		34.1125072903
417 (in isoform 3)Ubiquitination-5.7821890473
419 (in isoform 2)Ubiquitination-54.6321890473
421 (in isoform 1)Ubiquitination-61.8721890473
421UbiquitinationASALDNRKQSSEGIP
HHHHHHCCCCCCCCC		61.8721906983
423UbiquitinationALDNRKQSSEGIPVA
HHHHCCCCCCCCCCC		33.1321890473
423PhosphorylationALDNRKQSSEGIPVA
HHHHCCCCCCCCCCC		33.1325159151
424PhosphorylationLDNRKQSSEGIPVAQ
HHHCCCCCCCCCCCC		37.0325159151
424 (in isoform 3)Ubiquitination-37.0321890473
433PhosphorylationGIPVAQPSVMDDIEV
CCCCCCCCHHHCEEH		20.2828060719
438UbiquitinationQPSVMDDIEVWLRTD
CCCHHHCEEHHHHCC		3.9221890473
445UbiquitinationIEVWLRTDLKGDDLE
EEHHHHCCCCCCCHH		39.6921890473
447 (in isoform 1)Ubiquitination-64.2021890473
447UbiquitinationVWLRTDLKGDDLEEG
HHHHCCCCCCCHHCC		64.2021906983
456PhosphorylationDDLEEGVTSEEFDKF
CCHHCCCCHHHHHHH		41.0825849741
457PhosphorylationDLEEGVTSEEFDKFL
CHHCCCCHHHHHHHH		32.4925849741
462 (in isoform 1)Ubiquitination-58.1121890473
462UbiquitinationVTSEEFDKFLEERAK
CCHHHHHHHHHHHHH		58.1121890473
469 (in isoform 1)Ubiquitination-55.1121890473
469UbiquitinationKFLEERAKAAEMVPD
HHHHHHHHHHHCCCC		55.112190698
479PhosphorylationEMVPDLPSPPMEAPA
HCCCCCCCCCCCCCC		49.2729255136
489PhosphorylationMEAPAPASNPSGRKK
CCCCCCCCCCCCCCC		48.4929514088
492PhosphorylationPAPASNPSGRKKPER
CCCCCCCCCCCCCCC		56.3229514088
500PhosphorylationGRKKPERSEDALFAL
CCCCCCCCHHHHHCC		37.8627134283
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 TM1L2_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 TM1L2_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
TOLIP_HUMANTOLLIPphysical
16412388
CLH1_HUMANCLTCphysical
16412388
A4_HUMANAPPphysical
21832049
GDE_HUMANAGLphysical
26344197
CUED1_HUMANCUEDC1physical
28514442
SZRD1_HUMANSZRD1physical
28514442
NDUA6_HUMANNDUFA6physical
28514442
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 TM1L2_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"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 AND THR-164, ANDMASS SPECTROMETRY.
"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-192; TYR-200 ANDTYR-404, AND MASS SPECTROMETRY.
"Multiple reaction monitoring for robust quantitative proteomicanalysis of cellular signaling networks.";
Wolf-Yadlin A., Hautaniemi S., Lauffenburger D.A., White F.M.;
Proc. Natl. Acad. Sci. U.S.A. 104:5860-5865(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-404, AND MASSSPECTROMETRY.
"Time-resolved mass spectrometry of tyrosine phosphorylation sites inthe epidermal growth factor receptor signaling network reveals dynamicmodules.";
Zhang Y., Wolf-Yadlin A., Ross P.L., Pappin D.J., Rush J.,Lauffenburger D.A., White F.M.;
Mol. Cell. Proteomics 4:1240-1250(2005).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-192 AND TYR-200, ANDMASS SPECTROMETRY.

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