AMOL2_MOUSE - dbPTM
AMOL2_MOUSE - PTM Information in dbPTM
Basic Information of Protein
UniProt ID AMOL2_MOUSE
UniProt AC Q8K371
Protein Name Angiomotin-like protein 2
Gene Name Amotl2
Organism Mus musculus (Mouse).
Sequence Length 772
Subcellular Localization Recycling endosome.
Protein Description Regulates the translocation of phosphorylated SRC to peripheral cell-matrix adhesion sites. Required for proper architecture of actin filaments. Inhibits the Wnt/beta-catenin signaling pathway, probably by recruiting CTNNB1 to recycling endosomes and hence preventing its translocation to the nucleus. Participates in angiogenesis. May play a role in the polarity, proliferation and migration of endothelial cells. Selectively promotes FGF-induced MAPK activation through SRC (By similarity)..
Protein Sequence MRTLEDSSGTVLHRLIQEQLRYGNLTETRTLLAIQQQALRGGAGAGGTGSPQASLEIGAPEDSQVLQQATRQEPQGQEHQGGETHLAENRLYRLCPQPSKGEELPTYEEAKAHSQYYAAQQAGSRPHVGDRDPRGGVSGGGRRQDEALRELRHGHVRSLSERLLQLSLERNGARVPSHMSSSHSFPQLARSQQGPQPRGPPAEGPEPRGPPPQYPHAVMAQETAAVTDPRYRPRSSPHFQHAEVRILQAQVPPVFLQQQQYQYLPQPQEHSPPLHPAALGHGPPSSFGPPAVEGPPSAQATLGSAHLAQMETVLRENARLQRDNERLQRELESTSEKAGRIEKLENEIQRLSEAHESLMRTSSKREALEKTMRNKMDGEMRRLQDFNRDLRERLESANRHLASKTQEAQAGSQDMVAKLLAQSYEQQQEQEKLEREMALLRGAIEDQRRHAELLEQALGNAQSRAARAEEELRKKQAYVEKVERLQQALGQLQAACEKREQLELRLRTRLEQELKALRAQQRQTGTLAGGGGSHGGSAELSALRLSEQLREKEEQILALEADMTKWEQKYLEERAMRQFAMDAAATAAAQRDTTLIRHSPQPSPSSSFNEGLLPGNHRHQEMESRLKVLHAQILEKDAVIKVLQQRSRKDPGKATQGTLRPAKSVPSIFAAAVGTQGWQGLVSSERQTDARPAGDRVPAEEPPATAPLPAHTKHGSRDGSTQTDGPADNTSACLASEPDGLLGCNSSQRTPSLDSIAATRVQDLSDMVEILI
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
48PhosphorylationGGAGAGGTGSPQASL
CCCCCCCCCCCCCEE		33.3025619855
50PhosphorylationAGAGGTGSPQASLEI
CCCCCCCCCCCEEEC		17.4225619855
54PhosphorylationGTGSPQASLEIGAPE
CCCCCCCEEECCCCC		22.6825619855
99PhosphorylationYRLCPQPSKGEELPT
HHHCCCCCCCCCCCC		48.3129514104
107PhosphorylationKGEELPTYEEAKAHS
CCCCCCCHHHHHHHH		15.16-
158PhosphorylationLRHGHVRSLSERLLQ
HHCCHHHHHHHHHHH		34.8581018307
160PhosphorylationHGHVRSLSERLLQLS
CCHHHHHHHHHHHHH		23.1626824392
167PhosphorylationSERLLQLSLERNGAR
HHHHHHHHHHHCCCC		18.4127180971
177PhosphorylationRNGARVPSHMSSSHS
HCCCCCCCCCCCCCC		29.0318846507
180PhosphorylationARVPSHMSSSHSFPQ
CCCCCCCCCCCCHHH		24.2226643407
181PhosphorylationRVPSHMSSSHSFPQL
CCCCCCCCCCCHHHH		25.2126643407
182PhosphorylationVPSHMSSSHSFPQLA
CCCCCCCCCCHHHHH		18.8226643407
184PhosphorylationSHMSSSHSFPQLARS
CCCCCCCCHHHHHHH		40.3428507225
223PhosphorylationHAVMAQETAAVTDPR
CCEECCCCCCCCCCC		14.0828576409
231PhosphorylationAAVTDPRYRPRSSPH
CCCCCCCCCCCCCCC		30.2926643407
235PhosphorylationDPRYRPRSSPHFQHA
CCCCCCCCCCCCCHH		51.4026643407
236PhosphorylationPRYRPRSSPHFQHAE
CCCCCCCCCCCCHHH		24.5525334469
381MethylationNKMDGEMRRLQDFNR
HHHHHHHHHHHHHCH		31.68-
382MethylationKMDGEMRRLQDFNRD
HHHHHHHHHHHHCHH		35.08-
388MethylationRRLQDFNRDLRERLE
HHHHHHCHHHHHHHH		44.31-
396PhosphorylationDLRERLESANRHLAS
HHHHHHHHHHHHHHH		35.1225338131
541PhosphorylationHGGSAELSALRLSEQ
CCCHHHHHHHHHHHH		19.4351459757
593PhosphorylationTAAAQRDTTLIRHSP
HHHHHCCCCEEECCC		26.2023984901
594PhosphorylationAAAQRDTTLIRHSPQ
HHHHCCCCEEECCCC		25.2063766299
599PhosphorylationDTTLIRHSPQPSPSS
CCCEEECCCCCCCCC		18.5121659605
603PhosphorylationIRHSPQPSPSSSFNE
EECCCCCCCCCCCCC		31.9726643407
605PhosphorylationHSPQPSPSSSFNEGL
CCCCCCCCCCCCCCC		42.8426643407
606PhosphorylationSPQPSPSSSFNEGLL
CCCCCCCCCCCCCCC		42.1926643407
607PhosphorylationPQPSPSSSFNEGLLP
CCCCCCCCCCCCCCC		36.1126643407
647PhosphorylationIKVLQQRSRKDPGKA
HHHHHHHCCCCCCCC		39.0737006805
655PhosphorylationRKDPGKATQGTLRPA
CCCCCCCCCCCCCCC		30.9037012337
664PhosphorylationGTLRPAKSVPSIFAA
CCCCCCCCCCHHHHH		41.1727180971
667PhosphorylationRPAKSVPSIFAAAVG
CCCCCCCHHHHHHHC		28.3423984901
675PhosphorylationIFAAAVGTQGWQGLV
HHHHHHCCCCCHHHH		19.8126643407
716PhosphorylationPAHTKHGSRDGSTQT
CCCCCCCCCCCCCCC		27.2421659605
720PhosphorylationKHGSRDGSTQTDGPA
CCCCCCCCCCCCCCC		22.9526160508
721PhosphorylationHGSRDGSTQTDGPAD
CCCCCCCCCCCCCCC		40.8026160508
723PhosphorylationSRDGSTQTDGPADNT
CCCCCCCCCCCCCCC		42.9126160508
730PhosphorylationTDGPADNTSACLASE
CCCCCCCCHHCCCCC		20.4626160508
731PhosphorylationDGPADNTSACLASEP
CCCCCCCHHCCCCCC		24.2026160508
736PhosphorylationNTSACLASEPDGLLG
CCHHCCCCCCCCCCC		36.3926160508
750PhosphorylationGCNSSQRTPSLDSIA
CCCCCCCCCCHHHHH		15.0225619855
752PhosphorylationNSSQRTPSLDSIAAT
CCCCCCCCHHHHHHH		44.1725521595
755PhosphorylationQRTPSLDSIAATRVQ
CCCCCHHHHHHHCCC		21.3025521595
759PhosphorylationSLDSIAATRVQDLSD
CHHHHHHHCCCCHHH		23.5025619855
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
107YPhosphorylationKinaseFGFR1P16092
Uniprot
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of AMOL2_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 AMOL2_MOUSE !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
MAGI1_HUMANMAGI1physical
16019084
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 AMOL2_MOUSE

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Related Literatures of Post-Translational Modification

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