AP2A1_MOUSE - dbPTM
AP2A1_MOUSE - PTM Information in dbPTM
Basic Information of Protein
UniProt ID AP2A1_MOUSE
UniProt AC P17426
Protein Name AP-2 complex subunit alpha-1
Gene Name Ap2a1
Organism Mus musculus (Mouse).
Sequence Length 977
Subcellular Localization Cell membrane. Membrane, coated pit
Peripheral membrane protein
Cytoplasmic side. AP-2 appears to be excluded from internalizing CCVs and to disengage from sites of endocytosis seconds before internalization of the nascent CCV..
Protein Description Component of the adaptor protein complex 2 (AP-2). Adaptor protein complexes function in protein transport via transport vesicles in different membrane traffic pathways. Adaptor protein complexes are vesicle coat components and appear to be involved in cargo selection and vesicle formation. AP-2 is involved in clathrin-dependent endocytosis in which cargo proteins are incorporated into vesicles surrounded by clathrin (clathrin-coated vesicles, CCVs) which are destined for fusion with the early endosome. The clathrin lattice serves as a mechanical scaffold but is itself unable to bind directly to membrane components. Clathrin-associated adaptor protein (AP) complexes which can bind directly to both the clathrin lattice and to the lipid and protein components of membranes are considered to be the major clathrin adaptors contributing the CCV formation. AP-2 also serves as a cargo receptor to selectively sort the membrane proteins involved in receptor-mediated endocytosis. AP-2 seems to play a role in the recycling of synaptic vesicle membranes from the presynaptic surface. AP-2 recognizes Y-X-X-[FILMV] (Y-X-X-Phi) and [ED]-X-X-X-L-[LI] endocytosis signal motifs within the cytosolic tails of transmembrane cargo molecules. AP-2 may also play a role in maintaining normal post-endocytic trafficking through the ARF6-regulated, non-clathrin pathway. The AP-2 alpha subunit binds polyphosphoinositide-containing lipids, positioning AP-2 on the membrane. The AP-2 alpha subunit acts via its C-terminal appendage domain as a scaffolding platform for endocytic accessory proteins. The AP-2 alpha and AP-2 sigma subunits are thought to contribute to the recognition of the [ED]-X-X-X-L-[LI] motif (By similarity)..
Protein Sequence MPAVSKGDGMRGLAVFISDIRNCKSKEAEIKRINKELANIRSKFKGDKALDGYSKKKYVCKLLFIFLLGHDIDFGHMEAVNLLSSNKYTEKQIGYLFISVLVNSNSELIRLINNAIKNDLASRNPTFMCLALHCIANVGSREMGEAFAADIPRILVAGDSMDSVKQSAALCLLRLYKASPDLVPMGEWTARVVHLLNDQHMGVVTAAVSLITCLCKKNPDDFKTCISLAVSRLSRIVSSASTDLQDYTYYFVPAPWLSVKLLRLLQCYPPPEDAAVKGRLVECLETVLNKAQEPPKSKKVQHSNAKNAILFETISLIIHYDSEPNLLVRACNQLGQFLQHRETNLRYLALESMCTLASSEFSHEAVKTHIDTVINALKTERDVSVRQRAADLLYAMCDRSNAKQIVSEMLRYLETADYAIREEIVLKVAILAEKYAVDYSWYVDTILNLIRIAGDYVSEEVWYRVLQIVTNRDDVQGYAAKTVFEALQAPACHENMVKVGGYILGEFGNLIAGDPRSSPPVQFSLLHSKFHLCSVATRALLLSTYIKFINLFPETKATIQGVLRAGSQLRNADVELQQRAVEYLTLSSVASTDVLATVLEEMPPFPERESSILAKLKRKKGPGAASALDDSRRDTSSNDINGGVEPTPSTVSTPSPSADLLGLRAAPPPAAPPAPVGGNLLVDVFSDGPTAQPSLGPTPEEAFLSELEPPAPESPMALLADPAPAADPGPEDIGPPIPEADELLNKFVCKNSGVLFENQLLQIGVKSEFRQNLGRMYLFYGNKTSVQFQNFLPTVVHPGDLQTQLAVQTKRVAAQVDGGAQVQQVLNIECLRDFLTPPLLSVRFRYGGTAQSLTLKLPVTINKFFQPTEMAAQDFFQRWKQLSLPLQEAQKIFKANHPMDAEVTKAKLLGFGSALLDNVDPNPENFVGAGIIQTKALQVGCLLRLEPNAQAQMYRLTLRTSKEPVSRHLCELLAQQF
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
6Ubiquitination--MPAVSKGDGMRGL
--CCCCCCCCCCHHH		55.19-
6Malonylation--MPAVSKGDGMRGL
--CCCCCCCCCCHHH		55.1926320211
26UbiquitinationDIRNCKSKEAEIKRI
CHHCCCCCHHHHHHH		46.5727667366
31UbiquitinationKSKEAEIKRINKELA
CCCHHHHHHHHHHHH		38.4427667366
35AcetylationAEIKRINKELANIRS
HHHHHHHHHHHHHHH		52.3022826441
35UbiquitinationAEIKRINKELANIRS
HHHHHHHHHHHHHHH		52.3027667366
35MalonylationAEIKRINKELANIRS
HHHHHHHHHHHHHHH		52.3026320211
48UbiquitinationRSKFKGDKALDGYSK
HHHCCCCCCCCCCCH		60.5627667366
53PhosphorylationGDKALDGYSKKKYVC
CCCCCCCCCHHHHHH		19.5825195567
95PhosphorylationYTEKQIGYLFISVLV
CCHHHCCCCEEEEEE		10.4826643407
99PhosphorylationQIGYLFISVLVNSNS
HCCCCEEEEEECCCH		11.3226643407
104PhosphorylationFISVLVNSNSELIRL
EEEEEECCCHHHHHH		33.9626643407
106PhosphorylationSVLVNSNSELIRLIN
EEEECCCHHHHHHHH		33.3326643407
134S-palmitoylationFMCLALHCIANVGSR
HHHHHHHHHHHHCCH		3.0628680068
165UbiquitinationGDSMDSVKQSAALCL
CCCCHHHHHHHHHHH		42.3522790023
177AcetylationLCLLRLYKASPDLVP
HHHHHHHHHCCCCCC		47.1622826441
177MalonylationLCLLRLYKASPDLVP
HHHHHHHHHCCCCCC		47.1626320211
231PhosphorylationTCISLAVSRLSRIVS
HHHHHHHHHHHHHHH		23.1523737553
234PhosphorylationSLAVSRLSRIVSSAS
HHHHHHHHHHHHHCC		20.8923737553
263UbiquitinationWLSVKLLRLLQCYPP
HHHHHHHHHHHCCCC		43.7327667366
268UbiquitinationLLRLLQCYPPPEDAA
HHHHHHCCCCCCHHH		13.0527667366
277UbiquitinationPPEDAAVKGRLVECL
CCCHHHHCCHHHHHH		33.3222790023
283GlutathionylationVKGRLVECLETVLNK
HCCHHHHHHHHHHHH		3.0324333276
283S-nitrosylationVKGRLVECLETVLNK
HCCHHHHHHHHHHHH		3.0324895380
400PhosphorylationLYAMCDRSNAKQIVS
HHHHCCCCCHHHHHH		28.0829899451
403UbiquitinationMCDRSNAKQIVSEML
HCCCCCHHHHHHHHH		44.8222790023
517PhosphorylationLIAGDPRSSPPVQFS
CCCCCCCCCCCCCHH		53.2125521595
518PhosphorylationIAGDPRSSPPVQFSL
CCCCCCCCCCCCHHH		34.2124899341
524PhosphorylationSSPPVQFSLLHSKFH
CCCCCCHHHHCCHHH		16.9626643407
528PhosphorylationVQFSLLHSKFHLCSV
CCHHHHCCHHHHHHH		36.6726643407
528UbiquitinationVQFSLLHSKFHLCSV
CCHHHHCCHHHHHHH		36.6727667366
539UbiquitinationLCSVATRALLLSTYI
HHHHHHHHHHHHHHH		9.7527667366
544UbiquitinationTRALLLSTYIKFINL
HHHHHHHHHHHHHHH		29.2727667366
610UbiquitinationPPFPERESSILAKLK
CCCCCHHHHHHHHHH		28.9727667366
615UbiquitinationRESSILAKLKRKKGP
HHHHHHHHHHHCCCC		51.6127667366
620MalonylationLAKLKRKKGPGAASA
HHHHHHCCCCCHHHH		74.5026320211
620UbiquitinationLAKLKRKKGPGAASA
HHHHHHCCCCCHHHH		74.5027667366
626PhosphorylationKKGPGAASALDDSRR
CCCCCHHHHCCCCCC		28.918570555
631PhosphorylationAASALDDSRRDTSSN
HHHHCCCCCCCCCCC		28.9628066266
635PhosphorylationLDDSRRDTSSNDING
CCCCCCCCCCCCCCC		32.0424925903
636PhosphorylationDDSRRDTSSNDINGG
CCCCCCCCCCCCCCC		31.2818388127
637PhosphorylationDSRRDTSSNDINGGV
CCCCCCCCCCCCCCC		40.3824925903
647PhosphorylationINGGVEPTPSTVSTP
CCCCCCCCCCCCCCC		19.1618388127
649PhosphorylationGGVEPTPSTVSTPSP
CCCCCCCCCCCCCCC		43.8725521595
650PhosphorylationGVEPTPSTVSTPSPS
CCCCCCCCCCCCCCC		21.4918388127
652PhosphorylationEPTPSTVSTPSPSAD
CCCCCCCCCCCCCCC		34.3918388127
653PhosphorylationPTPSTVSTPSPSADL
CCCCCCCCCCCCCCC		24.3725521595
655PhosphorylationPSTVSTPSPSADLLG
CCCCCCCCCCCCCCC		31.4125521595
657PhosphorylationTVSTPSPSADLLGLR
CCCCCCCCCCCCCCC		38.4624925903
777PhosphorylationRQNLGRMYLFYGNKT
HHHCCCEEEEECCCC		7.72141285
804UbiquitinationHPGDLQTQLAVQTKR
CCCCHHHHHHHCCCC		17.9227667366
810UbiquitinationTQLAVQTKRVAAQVD
HHHHHCCCCCEEECC		27.9922790023
836PhosphorylationECLRDFLTPPLLSVR
HHHHHHCCCCEEEEE		23.8922817900
858UbiquitinationQSLTLKLPVTINKFF
CEEEEECCEEEHHHC		21.4427667366
880UbiquitinationQDFFQRWKQLSLPLQ
HHHHHHHHHCCCCHH		43.4822790023
886UbiquitinationWKQLSLPLQEAQKIF
HHHCCCCHHHHHHHH		9.7227667366
891UbiquitinationLPLQEAQKIFKANHP
CCHHHHHHHHHCCCC		58.1022790023
940UbiquitinationQTKALQVGCLLRLEP
CCCCEEECCEEEECC		5.3827667366
941S-nitrosocysteineTKALQVGCLLRLEPN
CCCEEECCEEEECCC		3.21-
941S-nitrosylationTKALQVGCLLRLEPN
CCCEEECCEEEECCC		3.2124895380
962UbiquitinationRLTLRTSKEPVSRHL
EEHHHCCCCCHHHHH		66.4827667366
970S-nitrosylationEPVSRHLCELLAQQF
CCHHHHHHHHHHHHC		2.5724895380
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 AP2A1_MOUSE !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of AP2A1_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 AP2A1_MOUSE !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions

Oops, there are no PPI records of AP2A1_MOUSE !!
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of AP2A1_MOUSE

loading...

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-655, AND MASSSPECTROMETRY.
"Proteomic analysis of in vivo phosphorylated synaptic proteins.";
Collins M.O., Yu L., Coba M.P., Husi H., Campuzano I.,Blackstock W.P., Choudhary J.S., Grant S.G.;
J. Biol. Chem. 280:5972-5982(2005).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-650; SER-652; THR-653AND SER-655, AND MASS SPECTROMETRY.

TOP
© 2024 Institute of Bioinformatics and Systems Biology, NYCU | Designed by : BiOmics Laboratory