AMOL1_HUMAN - dbPTM
AMOL1_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID AMOL1_HUMAN
UniProt AC Q8IY63
Protein Name Angiomotin-like protein 1
Gene Name AMOTL1
Organism Homo sapiens (Human).
Sequence Length 956
Subcellular Localization Cell junction, tight junction.
Protein Description Inhibits the Wnt/beta-catenin signaling pathway, probably by recruiting CTNNB1 to recycling endosomes and hence preventing its translocation to the nucleus..
Protein Sequence MWRAKLRRGTCEPAVKGSPSACYSPSSPVQVLEDSTYFSPDFQLYSGRHETSALTVEATSSIREKVVEDPLCNFHSPNFLRISEVEMRGSEDAAAGTVLQRLIQEQLRYGTPTENMNLLAIQHQATGSAGPAHPTNNFSSTENLTQEDPQMVYQSARQEPQGQEHQVDNTVMEKQVRSTQPQQNNEELPTYEEAKAQSQFFRGQQQQQQQQGAVGHGYYMAGGTSQKSRTEGRPTVNRANSGQAHKDEALKELKQGHVRSLSERIMQLSLERNGAKQHLPGSGNGKGFKVGGGPSPAQPAGKVLDPRGPPPEYPFKTKQMMSPVSKTQEHGLFYGDQHPGMLHEMVKPYPAPQPVRTDVAVLRYQPPPEYGVTSRPCQLPFPSTMQQHSPMSSQTSSASGPLHSVSLPLPLPMALGAPQPPPAASPSQQLGPDAFAIVERAQQMVEILTEENRVLHQELQGYYDNADKLHKFEKELQRISEAYESLVKSTTKRESLDKAMRNKLEGEIRRLHDFNRDLRDRLETANRQLSSREYEGHEDKAAEGHYASQNKEFLKEKEKLEMELAAVRTASEDHRRHIEILDQALSNAQARVIKLEEELREKQAYVEKVEKLQQALTQLQSACEKREQMERRLRTWLERELDALRTQQKHGNGQPANMPEYNAPALLELVREKEERILALEADMTKWEQKYLEESTIRHFAMNAAATAAAERDTTIINHSRNGSYGESSLEAHIWQEEEEVVQANRRCQDMEYTIKNLHAKIIEKDAMIKVLQQRSRKDAGKTDSSSLRPARSVPSIAAATGTHSRQTSLTSSQLAEEKKEEKTWKGSIGLLLGKEHHEHASAPLLPPPPTSALSSIASTTAASSAHAKTGSKDSSTQTDKSAELFWPSMASLPSRGRLSTTPAHSPVLKHPAAKGTAEKLENSPGHGKSPDHRGRVSSLLHKPEFPDGEMMEVLI
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
16UbiquitinationGTCEPAVKGSPSACY
CCCCCCCCCCCCCCC
56.64-
51PhosphorylationLYSGRHETSALTVEA
EECCCCCCCCEEEEE
17.1172500125
52PhosphorylationYSGRHETSALTVEAT
ECCCCCCCCEEEEEC
20.4972500131
61PhosphorylationLTVEATSSIREKVVE
EEEEECHHHHHHHCC
22.7017924679
76PhosphorylationDPLCNFHSPNFLRIS
CCCCCCCCCCEEEEE
19.8729449344
135PhosphorylationSAGPAHPTNNFSSTE
CCCCCCCCCCCCCCC
32.6928348404
139PhosphorylationAHPTNNFSSTENLTQ
CCCCCCCCCCCCCCC
38.1728348404
140PhosphorylationHPTNNFSSTENLTQE
CCCCCCCCCCCCCCC
35.2928348404
141PhosphorylationPTNNFSSTENLTQED
CCCCCCCCCCCCCCC
27.9128348404
145PhosphorylationFSSTENLTQEDPQMV
CCCCCCCCCCCHHHH
41.3028348404
145 (in isoform 2)Ubiquitination-41.3021890473
174UbiquitinationVDNTVMEKQVRSTQP
CCCHHHHHHHHHCCC
35.68-
177 (in isoform 2)Ubiquitination-31.3421890473
190PhosphorylationQNNEELPTYEEAKAQ
CCCCCCCCHHHHHHH
57.0728796482
191PhosphorylationNNEELPTYEEAKAQS
CCCCCCCHHHHHHHH
15.1628796482
195UbiquitinationLPTYEEAKAQSQFFR
CCCHHHHHHHHHHHH
50.6821906983
195 (in isoform 1)Ubiquitination-50.6821890473
198PhosphorylationYEEAKAQSQFFRGQQ
HHHHHHHHHHHHHHH
33.5468724781
218PhosphorylationQGAVGHGYYMAGGTS
CCCCCCCCCCCCCCC
5.6128796482
219PhosphorylationGAVGHGYYMAGGTSQ
CCCCCCCCCCCCCCC
5.7728796482
224PhosphorylationGYYMAGGTSQKSRTE
CCCCCCCCCCCCCCC
27.3723401153
225PhosphorylationYYMAGGTSQKSRTEG
CCCCCCCCCCCCCCC
38.6028796482
227UbiquitinationMAGGTSQKSRTEGRP
CCCCCCCCCCCCCCC
41.4921906983
227 (in isoform 1)Ubiquitination-41.4921890473
239 (in isoform 2)Ubiquitination-14.88-
241PhosphorylationPTVNRANSGQAHKDE
CCCCCCCCCCCCHHH
31.1523927012
251UbiquitinationAHKDEALKELKQGHV
CCHHHHHHHHHHHHH
68.96-
252 (in isoform 2)Ubiquitination-63.1521890473
260PhosphorylationLKQGHVRSLSERIMQ
HHHHHHHHHHHHHHH
34.8523403867
262PhosphorylationQGHVRSLSERIMQLS
HHHHHHHHHHHHHHH
26.5223403867
269PhosphorylationSERIMQLSLERNGAK
HHHHHHHHHHHCCCC
15.9929255136
289UbiquitinationSGNGKGFKVGGGPSP
CCCCCCCCCCCCCCC
48.95-
295PhosphorylationFKVGGGPSPAQPAGK
CCCCCCCCCCCCCCC
35.8225159151
302AcetylationSPAQPAGKVLDPRGP
CCCCCCCCCCCCCCC
41.5526051181
302UbiquitinationSPAQPAGKVLDPRGP
CCCCCCCCCCCCCCC
41.552189047
302 (in isoform 1)Ubiquitination-41.5521890473
302UbiquitinationSPAQPAGKVLDPRGP
CCCCCCCCCCCCCCC
41.5521890473
316MethylationPPPEYPFKTKQMMSP
CCCCCCCCCCCCCCC
50.76-
316UbiquitinationPPPEYPFKTKQMMSP
CCCCCCCCCCCCCCC
50.76-
318MethylationPEYPFKTKQMMSPVS
CCCCCCCCCCCCCCC
36.47-
318UbiquitinationPEYPFKTKQMMSPVS
CCCCCCCCCCCCCCC
36.47-
322PhosphorylationFKTKQMMSPVSKTQE
CCCCCCCCCCCCHHH
19.4654886879
325PhosphorylationKQMMSPVSKTQEHGL
CCCCCCCCCHHHCCC
33.1122199227
347UbiquitinationGMLHEMVKPYPAPQP
CHHHHHCCCCCCCCC
37.21-
373PhosphorylationPPPEYGVTSRPCQLP
CCCCCCCCCCCCCCC
18.047899741
374PhosphorylationPPEYGVTSRPCQLPF
CCCCCCCCCCCCCCC
31.6411763373
425PhosphorylationPQPPPAASPSQQLGP
CCCCCCCCHHHHCCC
27.4726657352
471UbiquitinationDNADKLHKFEKELQR
CCHHHHHHHHHHHHH
66.70-
474UbiquitinationDKLHKFEKELQRISE
HHHHHHHHHHHHHHH
67.85-
480PhosphorylationEKELQRISEAYESLV
HHHHHHHHHHHHHHH
20.5429083192
483PhosphorylationLQRISEAYESLVKST
HHHHHHHHHHHHHHH
11.2929083192
485PhosphorylationRISEAYESLVKSTTK
HHHHHHHHHHHHHHC
26.2825850435
489PhosphorylationAYESLVKSTTKRESL
HHHHHHHHHHCHHHH
33.5529083192
490PhosphorylationYESLVKSTTKRESLD
HHHHHHHHHCHHHHH
30.5329083192
491PhosphorylationESLVKSTTKRESLDK
HHHHHHHHCHHHHHH
34.8829083192
503UbiquitinationLDKAMRNKLEGEIRR
HHHHHHHHHHHHHHH
37.23-
534PhosphorylationRQLSSREYEGHEDKA
HHHHHCHHCCCCCHH
26.5428796482
540UbiquitinationEYEGHEDKAAEGHYA
HHCCCCCHHHHCCHH
46.65-
546PhosphorylationDKAAEGHYASQNKEF
CHHHHCCHHHHCHHH
20.8528796482
548PhosphorylationAAEGHYASQNKEFLK
HHHCCHHHHCHHHHH
27.4128796482
551UbiquitinationGHYASQNKEFLKEKE
CCHHHHCHHHHHHHH
42.05-
594UbiquitinationNAQARVIKLEEELRE
HHHHHHHHHHHHHHH
47.17-
611UbiquitinationAYVEKVEKLQQALTQ
HHHHHHHHHHHHHHH
55.36-
625UbiquitinationQLQSACEKREQMERR
HHHHHHHHHHHHHHH
62.21-
649UbiquitinationDALRTQQKHGNGQPA
HHHHHHHHCCCCCCC
43.60-
661PhosphorylationQPANMPEYNAPALLE
CCCCCCCCCHHHHHH
15.6830835315
686UbiquitinationALEADMTKWEQKYLE
HHHCCCHHHHHHHHH
41.94-
690UbiquitinationDMTKWEQKYLEESTI
CCHHHHHHHHHHHHH
40.04-
691PhosphorylationMTKWEQKYLEESTIR
CHHHHHHHHHHHHHH
21.0227642862
707PhosphorylationFAMNAAATAAAERDT
HHHHHHHHHHHHCCC
16.47113326225
714PhosphorylationTAAAERDTTIINHSR
HHHHHCCCEEEECCC
26.5629255136
715PhosphorylationAAAERDTTIINHSRN
HHHHCCCEEEECCCC
24.9329255136
720PhosphorylationDTTIINHSRNGSYGE
CCEEEECCCCCCCCC
23.9729255136
724PhosphorylationINHSRNGSYGESSLE
EECCCCCCCCCCHHH
33.2522617229
725PhosphorylationNHSRNGSYGESSLEA
ECCCCCCCCCCHHHH
26.7223663014
728PhosphorylationRNGSYGESSLEAHIW
CCCCCCCCHHHHEEC
35.5423663014
729PhosphorylationNGSYGESSLEAHIWQ
CCCCCCCHHHHEECH
26.4023663014
756UbiquitinationQDMEYTIKNLHAKII
HCHHHHHHHHHHHHH
45.73-
761UbiquitinationTIKNLHAKIIEKDAM
HHHHHHHHHHHHHHH
33.21-
765UbiquitinationLHAKIIEKDAMIKVL
HHHHHHHHHHHHHHH
40.14-
782UbiquitinationRSRKDAGKTDSSSLR
HHHHCCCCCCCCCCC
51.37-
783PhosphorylationSRKDAGKTDSSSLRP
HHHCCCCCCCCCCCC
39.9523186163
785PhosphorylationKDAGKTDSSSLRPAR
HCCCCCCCCCCCCCC
27.3626074081
786PhosphorylationDAGKTDSSSLRPARS
CCCCCCCCCCCCCCC
35.8830576142
787PhosphorylationAGKTDSSSLRPARSV
CCCCCCCCCCCCCCC
32.1430576142
793PhosphorylationSSLRPARSVPSIAAA
CCCCCCCCCCCHHHH
40.2529255136
796PhosphorylationRPARSVPSIAAATGT
CCCCCCCCHHHHCCC
23.7829255136
801PhosphorylationVPSIAAATGTHSRQT
CCCHHHHCCCCHHHC
37.5823927012
803PhosphorylationSIAAATGTHSRQTSL
CHHHHCCCCHHHCCC
16.6023927012
805PhosphorylationAAATGTHSRQTSLTS
HHHCCCCHHHCCCCH
26.3919276368
808PhosphorylationTGTHSRQTSLTSSQL
CCCCHHHCCCCHHHH
25.2929255136
809PhosphorylationGTHSRQTSLTSSQLA
CCCHHHCCCCHHHHH
22.7029255136
811PhosphorylationHSRQTSLTSSQLAEE
CHHHCCCCHHHHHHH
26.5427794612
812PhosphorylationSRQTSLTSSQLAEEK
HHHCCCCHHHHHHHH
22.7519691289
813PhosphorylationRQTSLTSSQLAEEKK
HHCCCCHHHHHHHHH
24.7919691289
823UbiquitinationAEEKKEEKTWKGSIG
HHHHHHHHCCHHHHH
61.86-
824PhosphorylationEEKKEEKTWKGSIGL
HHHHHHHCCHHHHHH
35.3723186163
828PhosphorylationEEKTWKGSIGLLLGK
HHHCCHHHHHHHHCC
15.1222617229
842PhosphorylationKEHHEHASAPLLPPP
CCCCCCCCCCCCCCC
32.1222468782
851PhosphorylationPLLPPPPTSALSSIA
CCCCCCCCCHHHHHH
32.1922468782
852PhosphorylationLLPPPPTSALSSIAS
CCCCCCCCHHHHHHH
32.7422468782
860PhosphorylationALSSIASTTAASSAH
HHHHHHHHHHHHHHH
16.0722468782
861PhosphorylationLSSIASTTAASSAHA
HHHHHHHHHHHHHHH
20.1022468782
872PhosphorylationSAHAKTGSKDSSTQT
HHHHHCCCCCCCCCC
38.2224719451
875PhosphorylationAKTGSKDSSTQTDKS
HHCCCCCCCCCCHHH
38.7328985074
876PhosphorylationKTGSKDSSTQTDKSA
HCCCCCCCCCCHHHH
34.3710394463
877PhosphorylationTGSKDSSTQTDKSAE
CCCCCCCCCCHHHHH
39.1710394473
879PhosphorylationSKDSSTQTDKSAELF
CCCCCCCCHHHHHHH
45.5422269353
882PhosphorylationSSTQTDKSAELFWPS
CCCCCHHHHHHHCHH
29.7723090842
889PhosphorylationSAELFWPSMASLPSR
HHHHHCHHHCCCCCC
19.9925850435
892PhosphorylationLFWPSMASLPSRGRL
HHCHHHCCCCCCCCC
31.9725850435
895PhosphorylationPSMASLPSRGRLSTT
HHHCCCCCCCCCCCC
53.3025850435
900PhosphorylationLPSRGRLSTTPAHSP
CCCCCCCCCCCCCCC
28.9529255136
901PhosphorylationPSRGRLSTTPAHSPV
CCCCCCCCCCCCCCC
41.2029255136
902PhosphorylationSRGRLSTTPAHSPVL
CCCCCCCCCCCCCCC
18.3323401153
906PhosphorylationLSTTPAHSPVLKHPA
CCCCCCCCCCCCCCC
20.8623401153
917PhosphorylationKHPAAKGTAEKLENS
CCCCCCCCHHHHHCC
30.8220068231
924PhosphorylationTAEKLENSPGHGKSP
CHHHHHCCCCCCCCC
23.9223898821
930PhosphorylationNSPGHGKSPDHRGRV
CCCCCCCCCCCCCCH
39.9021712546
938PhosphorylationPDHRGRVSSLLHKPE
CCCCCCHHHHHCCCC
17.5728122231
939PhosphorylationDHRGRVSSLLHKPEF
CCCCCHHHHHCCCCC
31.9021984501

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
793SPhosphorylationKinaseAMPKA1Q13131
PSP

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of AMOL1_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 AMOL1_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
NED4L_HUMANNEDD4Lphysical
22558212
CDAC1_HUMANCDADC1physical
27173435
SCML1_HUMANSCML1physical
27173435
DDHD1_HUMANDDHD1physical
27173435
UH1BL_HUMANUHRF1BP1Lphysical
27173435
HECW2_HUMANHECW2physical
27498087
USP9X_HUMANUSP9Xphysical
28720576

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 AMOL1_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-295, AND MASSSPECTROMETRY.
"Combining protein-based IMAC, peptide-based IMAC, and MudPIT forefficient phosphoproteomic analysis.";
Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D.,Yates J.R. III;
J. Proteome Res. 7:1346-1351(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-803 AND SER-805, ANDMASS SPECTROMETRY.
"Evaluation of the low-specificity protease elastase for large-scalephosphoproteome analysis.";
Wang B., Malik R., Nigg E.A., Korner R.;
Anal. Chem. 80:9526-9533(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-425; SER-720 ANDSER-809, 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 THR-51; SER-52 AND SER-61,AND MASS SPECTROMETRY.

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