AMOL1_MOUSE - dbPTM
AMOL1_MOUSE - PTM Information in dbPTM
Basic Information of Protein
UniProt ID AMOL1_MOUSE
UniProt AC Q9D4H4
Protein Name Angiomotin-like protein 1
Gene Name Amotl1
Organism Mus musculus (Mouse).
Sequence Length 968
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 MRRAKSRRGPCEPVLRAPPPICYSPSSPVQILEDPAYFYPDLQLYSGRHEASTLTVEASGGLRGKSVEDPLSSFHSPNFLRTPEVEMRGSEDVASGRVLQRLIQEQLRYGTPTENMNLLAIQHQATGSAGPAHATTNFSSTETLTQEDPQMVYQSARQEPQGQEHQGDNTVMEKQVRSTQPQQNNEELPTYEEAKAQSQFFRGQQQQQQQQQQQQQQQQQQGQGPLSHTYYMAGGTSQKSRTEGRPTVNRANSGQAHKDEALKELKQGHVRSLSERIMQLSLERNGAKQHLPSSGNGKSFKAGGEPSPAQPVCKALDPRGPPPEYPFKTKPMKSPVSKNQDHGLYYNDQHPGVLHEMVKPYPAPQPARTEVAVLRYQPPPEYGVTSRPCQLPFPSTVQQHSPMSSQTSSIGGTLHSVSLPLPLPISLAASQPLPASPNQQLGPDAFAIVERAQQMVEILTEENRVLHQELQGCYDNADKLHKFEKELQSISEAYESLVKSTTKRESLDKAMRTKLEGEIRRLHDFNRDLRDRLETANRQLSSREYDGHEDKAAESHYVSQNKEFLKEKEKLEMELAAVRTASEDHRRHIEILDQALSNAQARVIKLEEELREKQAYVEKVEKLQQALTQLQSACEKRGQMERRLRTWLERELDALRTQQKHGTGPPVSLPECNAPALMELVREKEERILALEADMTKWEQKYLEESTIRHFAMSAAAAATAERDTTISNHSRNGSYGESSLEAHIWPEEEEVVQANRRCQDMEYTIKNLHAKIIEKDAMIKVLQQRSRKDAGKTDSASLRPARSVPSIAAATGTHSRQTSLTSSQLTEEKKEEKTTWKGSIGFLLGKEHQGQASAPLLPTTPASALSLPASTTSASSTHAKTGSKDSSTQTDKSTELFWPSMASLPSRGRLSTAPSNSPILKHPAAKGAVEKQENSPGHGKASEHRGRVSNLLHKPEFPDGEMMEVLI
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
195UbiquitinationLPTYEEAKAQSQFFR
CCCHHHHHHHHHHHH		15.9922790023
195UbiquitinationLPTYEEAKAQSQFFR
CCCHHHHHHHHHHHH		15.9922790023
253PhosphorylationPTVNRANSGQAHKDE
CCCCCCCCCCCCHHH		45.0336013191
281PhosphorylationSERIMQLSLERNGAK
HHHHHHHHHHHCCCC		26.2746162993
298AcetylationLPSSGNGKSFKAGGE
CCCCCCCCCCCCCCC		4.2619857989
301AcetylationSGNGKSFKAGGEPSP
CCCCCCCCCCCCCCC		27.0119857997
307PhosphorylationFKAGGEPSPAQPVCK
CCCCCCCCCCCCCHH		11.53-
334PhosphorylationFKTKPMKSPVSKNQD
CCCCCCCCCCCCCCC		25.1554886881
485UbiquitinationDKLHKFEKELQSISE
HHHHHHHHHHHHHHH		8.7522790023
485UbiquitinationDKLHKFEKELQSISE
HHHHHHHHHHHHHHH		8.7522790023
496PhosphorylationSISEAYESLVKSTTK
HHHHHHHHHHHHHHC		42.8320139300
500PhosphorylationAYESLVKSTTKRESL
HHHHHHHHHHCHHHH		44.1620139300
501PhosphorylationYESLVKSTTKRESLD
HHHHHHHHHCHHHHH		31.5437009437
502PhosphorylationESLVKSTTKRESLDK
HHHHHHHHCHHHHHH		23.2220139300
725PhosphorylationAATAERDTTISNHSR
HHHHHCCCCCCCCCC		9.5023684622
726PhosphorylationATAERDTTISNHSRN
HHHHCCCCCCCCCCC		37.5823684622
728PhosphorylationAERDTTISNHSRNGS
HHCCCCCCCCCCCCC		16.6023684622
731PhosphorylationDTTISNHSRNGSYGE
CCCCCCCCCCCCCCC		35.8723684622
735PhosphorylationSNHSRNGSYGESSLE
CCCCCCCCCCCCCCC		6.469550943
736PhosphorylationNHSRNGSYGESSLEA
CCCCCCCCCCCCCCE		26.5426160508
739PhosphorylationRNGSYGESSLEAHIW
CCCCCCCCCCCEEEC		52.7726160508
740PhosphorylationNGSYGESSLEAHIWP
CCCCCCCCCCEEECC		7.6126160508
796PhosphorylationKDAGKTDSASLRPAR
CCCCCCCCCCCCCCC		47.6981018275
804PhosphorylationASLRPARSVPSIAAA
CCCCCCCCCCCHHHH		50.0426824392
807PhosphorylationRPARSVPSIAAATGT
CCCCCCCCHHHHCCC		63.7723737553
812PhosphorylationVPSIAAATGTHSRQT
CCCHHHHCCCCCCCC		7.9923737553
814PhosphorylationSIAAATGTHSRQTSL
CHHHHCCCCCCCCCC		13.5923737553
816PhosphorylationAAATGTHSRQTSLTS
HHHCCCCCCCCCCCH		2.2928507225
819PhosphorylationTGTHSRQTSLTSSQL
CCCCCCCCCCCHHHC		3.0325619855
820PhosphorylationGTHSRQTSLTSSQLT
CCCCCCCCCCHHHCC		21.3425619855
822PhosphorylationHSRQTSLTSSQLTEE
CCCCCCCCHHHCCHH		32.1025619855
823PhosphorylationSRQTSLTSSQLTEEK
CCCCCCCHHHCCHHH		38.9425619855
824PhosphorylationRQTSLTSSQLTEEKK
CCCCCCHHHCCHHHH		25.1025619855
835PhosphorylationEEKKEEKTTWKGSIG
HHHHHHHCCCCCHHH		4.7826745281
836PhosphorylationEKKEEKTTWKGSIGF
HHHHHHCCCCCHHHH		48.5426745281
840PhosphorylationEKTTWKGSIGFLLGK
HHCCCCCHHHHHCCC		18.4425521595
854PhosphorylationKEHQGQASAPLLPTT
CCCCCCCCCCCCCCC		32.8981018291
912PhosphorylationLPSRGRLSTAPSNSP
CCCCCCCCCCCCCCC		29472430
913PhosphorylationPSRGRLSTAPSNSPI
CCCCCCCCCCCCCCC		4095063
916PhosphorylationGRLSTAPSNSPILKH
CCCCCCCCCCCCCCC		81018299
918PhosphorylationLSTAPSNSPILKHPA
CCCCCCCCCCCCCHH		26824392
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 AMOL1_MOUSE !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of AMOL1_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 AMOL1_MOUSE !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
MPP5_MOUSEMpp5physical
18824598
MPDZ_MOUSEMpdzphysical
18824598
LIN7C_MOUSELin7cphysical
18824598
PKHG5_MOUSEPlekhg5physical
18824598
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of AMOL1_MOUSE

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"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-645; SER-718 ANDSER-730, AND MASS SPECTROMETRY.

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