AMER1_HUMAN - dbPTM
AMER1_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID AMER1_HUMAN
UniProt AC Q5JTC6
Protein Name APC membrane recruitment protein 1
Gene Name AMER1
Organism Homo sapiens (Human).
Sequence Length 1135
Subcellular Localization Cytoplasm. Cell membrane
Peripheral membrane protein
Cytoplasmic side. Nucleus. Shuttles between nucleus and cytoplasm. Detected in nuclear paraspeckles that are found close to splicing speckles. Translocates to the cell membrane following binding
Protein Description Regulator of the canonical Wnt signaling pathway. Acts by specifically binding phosphatidylinositol 4,5-bisphosphate (PtdIns(4,5)P2), translocating to the cell membrane and interacting with key regulators of the canonical Wnt signaling pathway, such as components of the beta-catenin destruction complex. Acts both as a positive and negative regulator of the Wnt signaling pathway, depending on the context: acts as a positive regulator by promoting LRP6 phosphorylation. Also acts as a negative regulator by acting as a scaffold protein for the beta-catenin destruction complex and promoting stabilization of Axin at the cell membrane. Promotes CTNNB1 ubiquitination and degradation. Involved in kidney development..
Protein Sequence METQKDEAAQAKGAAASGSTREQTAEKGAKNKAAEATEGPTSEPSSSGPGRLKKTAMKLFGGKKGICTLPSFFGGGRSKGSGKGSSKKGLSKSKTHDGLSEAAHGPEDVVSEGTGFSLPLPELPCQFPSSQSAHGALETGSRCKTSVAGATEKAVAEKFPSMPKPKKGLKGFFSSIRRHRKSKVTGAEQSEPGAKGPERVRARPHEHVSSAPQVPCFEETFQAPRKENANPQDAPGPKVSPTPEPSPPATEKMACKDPEKPMEACASAHVQPKPAPEASSLEEPHSPETGEKVVAGEVNPPNGPVGDPLSLLFGDVTSLKSFDSLTGCGDIIAEQDMDSMTDSMASGGQRANRDGTKRSSCLVTYQGGGEEMALPDDDDEEEEEEEEVELEEEEEEVKEEEEDDDLEYLWETAQMYPRPNMNLGYHPTTSPGHHGYMLLDPVRSYPGLAPGELLTPQSDQQESAPNSDEGYYDSTTPGFEDDSGEALGLVRRDCLPRDSYSGDALYEFYEPDDSLENSPPGDDCLYDLHGRSSEMFDPFLNFEPFLSSRPPGAMETEEERLVTIQKQLLYWELRREQLEAQEARAREAHAREAHAREAYTREAYGREAYAREAHTWEAHGREARTREAQAREVRCRETQVRETQARQEKPVLEYQMRPLGPSVMGLAAGVSGTSQISHRGITSAFPTTASSEPDWRDFRPLEKRYEGTCSKKDQSTCLMQLFQSDAMFEPDMQEANFGGSPRRAYPTYSPPEDPEEEEVEKEGNATVSFSQALVEFTSNGNLFSSMSCSSDSDSSFTQNLPELPPMVTFDIADVERDGEGKCEENPEFHNDEDLAASLEAFELGYYHKHAFNNYHSRFYQGLPWGVSSLPRYLGLPGLHPRPPPAAMALNRRSRSLDTAETLEMELSNSHLVQGYLESDELQAQQEDSDEEDEEEEEGEWSRDSPLSLYTEPPGAYDWPAWAPCPLPVGPGPAWISPNQLDRPSSQSPYRQATCCIPPMTMSISLSVPESRAPGESGPQLARPSHLHLPMGPCYNLQPQASQSMRARPRDVLLPVDEPSCSSSSGGFSPSPLPQAKPVGITHGIPQLPRVRPEHPQPQPTHYGPSSLDLSKERAEQGASLATSYSSTAMNGNLAK
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
1Acetylation-------METQKDEA
-------CCCHHHHH
50.4622814378
19PhosphorylationKGAAASGSTREQTAE
HHHHHCCCHHHHHHH
23.0725627689
37PhosphorylationKNKAAEATEGPTSEP
HHHHHHHCCCCCCCC
32.7422210691
41PhosphorylationAEATEGPTSEPSSSG
HHHCCCCCCCCCCCC
57.49-
42PhosphorylationEATEGPTSEPSSSGP
HHCCCCCCCCCCCCC
51.1222210691
45PhosphorylationEGPTSEPSSSGPGRL
CCCCCCCCCCCCCHH
32.8425627689
46PhosphorylationGPTSEPSSSGPGRLK
CCCCCCCCCCCCHHH
50.4522210691
47PhosphorylationPTSEPSSSGPGRLKK
CCCCCCCCCCCHHHH
54.0325627689
53UbiquitinationSSGPGRLKKTAMKLF
CCCCCHHHHHHHHHH
46.8723000965
54UbiquitinationSGPGRLKKTAMKLFG
CCCCHHHHHHHHHHC
46.2223000965
58UbiquitinationRLKKTAMKLFGGKKG
HHHHHHHHHHCCCCC
37.8923000965
63UbiquitinationAMKLFGGKKGICTLP
HHHHHCCCCCEEECC
48.4823000965
64UbiquitinationMKLFGGKKGICTLPS
HHHHCCCCCEEECCC
57.7023000965
91PhosphorylationGSSKKGLSKSKTHDG
CCCCCCCCCCCCCCC
43.48-
161PhosphorylationAVAEKFPSMPKPKKG
HHHHHCCCCCCCCCC
51.3418452278
174PhosphorylationKGLKGFFSSIRRHRK
CCHHHHHHHHHHHHH
23.6929978859
175PhosphorylationGLKGFFSSIRRHRKS
CHHHHHHHHHHHHHH
18.2429978859
185PhosphorylationRHRKSKVTGAEQSEP
HHHHHCCCCCCCCCC
34.1228857561
190PhosphorylationKVTGAEQSEPGAKGP
CCCCCCCCCCCCCCC
36.9528857561
195AcetylationEQSEPGAKGPERVRA
CCCCCCCCCCHHHCC
79.5019824281
240PhosphorylationDAPGPKVSPTPEPSP
CCCCCCCCCCCCCCC
29.2325159151
242PhosphorylationPGPKVSPTPEPSPPA
CCCCCCCCCCCCCCC
32.5530266825
246PhosphorylationVSPTPEPSPPATEKM
CCCCCCCCCCCCCCC
41.6830266825
250PhosphorylationPEPSPPATEKMACKD
CCCCCCCCCCCCCCC
41.7430266825
267PhosphorylationKPMEACASAHVQPKP
CCHHHHHHCCCCCCC
20.84-
279PhosphorylationPKPAPEASSLEEPHS
CCCCCCCCCCCCCCC
33.5229255136
280PhosphorylationKPAPEASSLEEPHSP
CCCCCCCCCCCCCCC
47.0129255136
286PhosphorylationSSLEEPHSPETGEKV
CCCCCCCCCCCCCCE
34.8429255136
289PhosphorylationEEPHSPETGEKVVAG
CCCCCCCCCCCEEEC
54.7623663014
317PhosphorylationSLLFGDVTSLKSFDS
HHHHCCCCCCCCCCC
32.8429523821
318PhosphorylationLLFGDVTSLKSFDSL
HHHCCCCCCCCCCCC
33.3825159151
324PhosphorylationTSLKSFDSLTGCGDI
CCCCCCCCCCCCCCE
26.31-
326PhosphorylationLKSFDSLTGCGDIIA
CCCCCCCCCCCCEEE
34.08-
429PhosphorylationNLGYHPTTSPGHHGY
CCCCCCCCCCCCCCE
37.06-
430PhosphorylationLGYHPTTSPGHHGYM
CCCCCCCCCCCCCEE
31.22-
518PhosphorylationPDDSLENSPPGDDCL
CCCCCCCCCCCCCCC
24.09-
526PhosphorylationPPGDDCLYDLHGRSS
CCCCCCCEECCCCCH
23.8427642862
548PhosphorylationNFEPFLSSRPPGAME
CCHHHHHCCCCCCCC
51.45-
556PhosphorylationRPPGAMETEEERLVT
CCCCCCCCHHHHHHH
35.30-
570PhosphorylationTIQKQLLYWELRREQ
HHHHHHHHHHHHHHH
12.8727642862
615PhosphorylationAYAREAHTWEAHGRE
HHHHHHHHHHHCCHH
31.8627251275
683PhosphorylationISHRGITSAFPTTAS
CCCCCCCCCCCCCCC
26.45-
690PhosphorylationSAFPTTASSEPDWRD
CCCCCCCCCCCCHHH
32.8924719451
740PhosphorylationQEANFGGSPRRAYPT
CCCCCCCCCCCCCCC
18.6628348404
745PhosphorylationGGSPRRAYPTYSPPE
CCCCCCCCCCCCCCC
8.3626471730
747PhosphorylationSPRRAYPTYSPPEDP
CCCCCCCCCCCCCCC
24.7721815630
748PhosphorylationPRRAYPTYSPPEDPE
CCCCCCCCCCCCCCC
18.0625159151
749PhosphorylationRRAYPTYSPPEDPEE
CCCCCCCCCCCCCCH
36.1321815630
768 (in isoform 2)Phosphorylation-18.1522210691
777 (in isoform 2)Phosphorylation-14.0522210691
784 (in isoform 2)Phosphorylation-28.4422210691
803 (in isoform 2)Phosphorylation-5.65-
854PhosphorylationHKHAFNNYHSRFYQG
CHHCCCCHHHHHHCC
11.41-
867PhosphorylationQGLPWGVSSLPRYLG
CCCCCCHHHCCHHHC
23.4028348404
868PhosphorylationGLPWGVSSLPRYLGL
CCCCCHHHCCHHHCC
39.7322617229
872PhosphorylationGVSSLPRYLGLPGLH
CHHHCCHHHCCCCCC
11.8126074081
895PhosphorylationALNRRSRSLDTAETL
HHCCCCCCCCHHHHH
31.6624275569
898PhosphorylationRRSRSLDTAETLEME
CCCCCCCHHHHHHHH
31.5224275569
1006PhosphorylationMTMSISLSVPESRAP
CEEEEEEECCCCCCC
28.92-
1059PhosphorylationLLPVDEPSCSSSSGG
EEECCCCCCCCCCCC
25.2829978859
1061PhosphorylationPVDEPSCSSSSGGFS
ECCCCCCCCCCCCCC
37.2829978859
1062PhosphorylationVDEPSCSSSSGGFSP
CCCCCCCCCCCCCCC
32.6129978859
1063PhosphorylationDEPSCSSSSGGFSPS
CCCCCCCCCCCCCCC
19.3929978859
1064PhosphorylationEPSCSSSSGGFSPSP
CCCCCCCCCCCCCCC
44.9029978859
1068PhosphorylationSSSSGGFSPSPLPQA
CCCCCCCCCCCCCCC
27.9529978859
1070PhosphorylationSSGGFSPSPLPQAKP
CCCCCCCCCCCCCCC
37.5629978859
1081PhosphorylationQAKPVGITHGIPQLP
CCCCCCCCCCCCCCC
14.2329978859
1091MethylationIPQLPRVRPEHPQPQ
CCCCCCCCCCCCCCC
31.97115920101
1100PhosphorylationEHPQPQPTHYGPSSL
CCCCCCCCCCCCCCC
23.6029978859
1102PhosphorylationPQPQPTHYGPSSLDL
CCCCCCCCCCCCCCC
32.9627642862
1105PhosphorylationQPTHYGPSSLDLSKE
CCCCCCCCCCCCCHH
38.8929978859
1106PhosphorylationPTHYGPSSLDLSKER
CCCCCCCCCCCCHHH
29.0929978859
1110PhosphorylationGPSSLDLSKERAEQG
CCCCCCCCHHHHHHH
31.9429978859
1123PhosphorylationQGASLATSYSSTAMN
HHHCHHHHHCCCCCC
19.8730576142
1125PhosphorylationASLATSYSSTAMNGN
HCHHHHHCCCCCCCC
22.45-
1126PhosphorylationSLATSYSSTAMNGNL
CHHHHHCCCCCCCCC
16.3830576142
1127PhosphorylationLATSYSSTAMNGNLA
HHHHHCCCCCCCCCC
24.80-

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 AMER1_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of AMER1_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 AMER1_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
CTNB1_HUMANCTNNB1physical
17510365
AXIN1_HUMANAXIN1physical
17510365
FBW1A_HUMANBTRCphysical
17510365
FBW1B_HUMANFBXW11physical
17510365
KEAP1_HUMANKEAP1physical
17510365
KEAP1_HUMANKEAP1physical
22215675
RAF1_HUMANRAF1physical
27173435
FBW1B_HUMANFBXW11physical
22215675

Drug and Disease Associations
Kegg Disease
H00444 Osteopathia striata with cranial sclerosis
OMIM Disease
300373Osteopathia striata with cranial sclerosis (OSCS)
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of AMER1_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Lys-N and trypsin cover complementary parts of the phosphoproteome ina refined SCX-based approach.";
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,Mohammed S.;
Anal. Chem. 81:4493-4501(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-242; SER-246 ANDTHR-250, AND MASS SPECTROMETRY.
"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 THR-242 AND SER-246, ANDMASS SPECTROMETRY.

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