TM1L2_MOUSE - dbPTM
TM1L2_MOUSE - PTM Information in dbPTM
Basic Information of Protein
UniProt ID TM1L2_MOUSE
UniProt AC Q5SRX1
Protein Name TOM1-like protein 2
Gene Name Tom1l2
Organism Mus musculus (Mouse).
Sequence Length 507
Subcellular Localization
Protein Description Probable role in protein transport. May regulate growth factor-induced mitogenic signaling (By similarity)..
Protein Sequence MEFLLGNPFSTPVGQCLEKATDGSLQSEDWTLNMEICDIINETEEGPKDAIRALKKRLSGNRNYREVMLALTVLETCVKNCGHRFHLLVANRDFIDSVLVKIISPKNNPPTIVQDKVLALIQAWADAFRSSPDLTGVVHIYEELKRRGIEFPMADLDALSPIHTPQRSVPEMDPAATIPRSQTQPRTTAGTYSSPPPASYSTLQAPALSVTGPITANSEQIARLRSELDIVRGNTKVMSEMLTEMVPGQEDSSDLELLQELNRTCRAMQHRIVELISRVSNEEVTEELLHVNDDLNNVFLRYERFERYRSGRSVQNASNGVLSEVTEDNLIDLGPGSPAVVSPMVGSTAPPSSLSSQLAGLDLGTESVSGTLSSLQQCKPQDGFDMFAQTRGNSLAEQRKTVTYEDPQAVGGLASALDNRKQNSEMIPVAQPSVMDDIEVWLRTDLKGDDLEEGVTSEEFDKFLEERAKAAETVPDLPSPPTEAPAPASNTSTRKKPERSDDALFAL
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
73UbiquitinationEVMLALTVLETCVKN
HHHHHHHHHHHHHHH
4.7727667366
101UbiquitinationFIDSVLVKIISPKNN
HHCEEEEEHHCCCCC
30.1122790023
106UbiquitinationLVKIISPKNNPPTIV
EEEHHCCCCCCCCHH
63.6722790023
145UbiquitinationVHIYEELKRRGIEFP
HHHHHHHHHCCCCCC
43.2422790023
160PhosphorylationMADLDALSPIHTPQR
CCCHHHCCCCCCCCC
24.4325521595
164PhosphorylationDALSPIHTPQRSVPE
HHCCCCCCCCCCCCC
23.1025521595
168PhosphorylationPIHTPQRSVPEMDPA
CCCCCCCCCCCCCCC
36.4629899451
177PhosphorylationPEMDPAATIPRSQTQ
CCCCCCCCCCCCCCC
33.3529514104
187PhosphorylationRSQTQPRTTAGTYSS
CCCCCCCCCCCCCCC
27.9025777480
187O-linked_GlycosylationRSQTQPRTTAGTYSS
CCCCCCCCCCCCCCC
27.9022517741
188O-linked_GlycosylationSQTQPRTTAGTYSSP
CCCCCCCCCCCCCCC
25.1122517741
188PhosphorylationSQTQPRTTAGTYSSP
CCCCCCCCCCCCCCC
25.1125777480
191PhosphorylationQPRTTAGTYSSPPPA
CCCCCCCCCCCCCCC
20.1225777480
192PhosphorylationPRTTAGTYSSPPPAS
CCCCCCCCCCCCCCC
13.2622817900
193PhosphorylationRTTAGTYSSPPPASY
CCCCCCCCCCCCCCC
35.8925777480
194PhosphorylationTTAGTYSSPPPASYS
CCCCCCCCCCCCCCC
30.8925777480
199PhosphorylationYSSPPPASYSTLQAP
CCCCCCCCCCCCCCC
25.9525777480
200PhosphorylationSSPPPASYSTLQAPA
CCCCCCCCCCCCCCC
14.0522817900
201PhosphorylationSPPPASYSTLQAPAL
CCCCCCCCCCCCCCE
21.8325777480
202PhosphorylationPPPASYSTLQAPALS
CCCCCCCCCCCCCEE
18.0425777480
209PhosphorylationTLQAPALSVTGPITA
CCCCCCEEECCCCCC
21.5325777480
211PhosphorylationQAPALSVTGPITANS
CCCCEEECCCCCCCH
33.5925777480
215PhosphorylationLSVTGPITANSEQIA
EEECCCCCCCHHHHH
23.9525777480
218PhosphorylationTGPITANSEQIARLR
CCCCCCCHHHHHHHH
28.5425777480
236UbiquitinationDIVRGNTKVMSEMLT
HHHHCCHHHHHHHHH
39.6822790023
367UbiquitinationGLDLGTESVSGTLSS
CCCCCCCCCCCHHHH
22.7827667366
394PhosphorylationFAQTRGNSLAEQRKT
CCHHCCCCHHHHHCC
31.6125521595
400UbiquitinationNSLAEQRKTVTYEDP
CCHHHHHCCEECCCH
47.2222790023
401PhosphorylationSLAEQRKTVTYEDPQ
CHHHHHCCEECCCHH
21.9218846507
403PhosphorylationAEQRKTVTYEDPQAV
HHHHCCEECCCHHHH
26.8229899451
404PhosphorylationEQRKTVTYEDPQAVG
HHHCCEECCCHHHHH
17.6322817900
424 (in isoform 2)Phosphorylation-26.5029899451
424PhosphorylationLDNRKQNSEMIPVAQ
HHCCCCCCCCCCCCC
26.5026643407
433PhosphorylationMIPVAQPSVMDDIEV
CCCCCCCCHHHCHHH
20.2826643407
435UbiquitinationPVAQPSVMDDIEVWL
CCCCCCHHHCHHHHH
4.4927667366
436 (in isoform 2)Phosphorylation-52.1329899451
437 (in isoform 2)Phosphorylation-22.3529899451
447UbiquitinationVWLRTDLKGDDLEEG
HHHHCCCCCCCHHCC
64.2022790023
449UbiquitinationLRTDLKGDDLEEGVT
HHCCCCCCCHHCCCC
56.5927667366
456PhosphorylationDDLEEGVTSEEFDKF
CCHHCCCCHHHHHHH
41.0830635358
457PhosphorylationDLEEGVTSEEFDKFL
CHHCCCCHHHHHHHH
32.4925521595
457UbiquitinationDLEEGVTSEEFDKFL
CHHCCCCHHHHHHHH
32.4927667366
462UbiquitinationVTSEEFDKFLEERAK
CCHHHHHHHHHHHHH
58.1122790023
468UbiquitinationDKFLEERAKAAETVP
HHHHHHHHHHHCCCC
14.7627667366
469UbiquitinationKFLEERAKAAETVPD
HHHHHHHHHHCCCCC
55.1122790023
473PhosphorylationERAKAAETVPDLPSP
HHHHHHCCCCCCCCC
32.3925619855
479PhosphorylationETVPDLPSPPTEAPA
CCCCCCCCCCCCCCC
51.3025521595
482PhosphorylationPDLPSPPTEAPAPAS
CCCCCCCCCCCCCCC
48.4325619855
489PhosphorylationTEAPAPASNTSTRKK
CCCCCCCCCCCCCCC
39.3125619855
490UbiquitinationEAPAPASNTSTRKKP
CCCCCCCCCCCCCCC
39.9127667366
491PhosphorylationAPAPASNTSTRKKPE
CCCCCCCCCCCCCCC
29.0425619855
492PhosphorylationPAPASNTSTRKKPER
CCCCCCCCCCCCCCC
30.3925619855
493PhosphorylationAPASNTSTRKKPERS
CCCCCCCCCCCCCCC
44.4625619855
500PhosphorylationTRKKPERSDDALFAL
CCCCCCCCCCCCCCC
37.8722324799

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 TM1L2_MOUSE !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of TM1L2_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 TM1L2_MOUSE !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions

Oops, there are no PPI records of TM1L2_MOUSE !!

Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of TM1L2_MOUSE

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Qualitative and quantitative analyses of protein phosphorylation innaive and stimulated mouse synaptosomal preparations.";
Munton R.P., Tweedie-Cullen R., Livingstone-Zatchej M., Weinandy F.,Waidelich M., Longo D., Gehrig P., Potthast F., Rutishauser D.,Gerrits B., Panse C., Schlapbach R., Mansuy I.M.;
Mol. Cell. Proteomics 6:283-293(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-479, AND MASSSPECTROMETRY.

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