AP2A1_HUMAN - dbPTM
AP2A1_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID AP2A1_HUMAN
UniProt AC O95782
Protein Name AP-2 complex subunit alpha-1
Gene Name AP2A1
Organism Homo sapiens (Human).
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 MPAVSKGDGMRGLAVFISDIRNCKSKEAEIKRINKELANIRSKFKGDKALDGYSKKKYVCKLLFIFLLGHDIDFGHMEAVNLLSSNKYTEKQIGYLFISVLVNSNSELIRLINNAIKNDLASRNPTFMCLALHCIANVGSREMGEAFAADIPRILVAGDSMDSVKQSAALCLLRLYKASPDLVPMGEWTARVVHLLNDQHMGVVTAAVSLITCLCKKNPDDFKTCVSLAVSRLSRIVSSASTDLQDYTYYFVPAPWLSVKLLRLLQCYPPPEDAAVKGRLVECLETVLNKAQEPPKSKKVQHSNAKNAILFETISLIIHYDSEPNLLVRACNQLGQFLQHRETNLRYLALESMCTLASSEFSHEAVKTHIDTVINALKTERDVSVRQRAADLLYAMCDRSNAKQIVSEMLRYLETADYAIREEIVLKVAILAEKYAVDYSWYVDTILNLIRIAGDYVSEEVWYRVLQIVTNRDDVQGYAAKTVFEALQAPACHENMVKVGGYILGEFGNLIAGDPRSSPPVQFSLLHSKFHLCSVATRALLLSTYIKFINLFPETKATIQGVLRAGSQLRNADVELQQRAVEYLTLSSVASTDVLATVLEEMPPFPERESSILAKLKRKKGPGAGSALDDGRRDPSSNDINGGMEPTPSTVSTPSPSADLLGLRAAPPPAAPPASAGAGNLLVDVFDGPAAQPSLGPTPEEAFLSELEPPAPESPMALLADPAPAADPGPEDIGPPIPEADELLNKFVCKNNGVLFENQLLQIGVKSEFRQNLGRMYLFYGNKTSVQFQNFSPTVVHPGDLQTQLAVQTKRVAAQVDGGAQVQQVLNIECLRDFLTPPLLSVRFRYGGAPQALTLKLPVTINKFFQPTEMAAQDFFQRWKQLSLPQQEAQKIFKANHPMDAEVTKAKLLGFGSALLDNVDPNPENFVGAGIIQTKALQVGCLLRLEPNAQAQMYRLTLRTSKEPVSRHLCELLAQQF
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
5Phosphorylation---MPAVSKGDGMRG
---CCCCCCCCCCHH		32.7827251275
6Ubiquitination--MPAVSKGDGMRGL
--CCCCCCCCCCHHH		55.1933845483
18PhosphorylationRGLAVFISDIRNCKS
HHHHHHHHCHHCCCC		18.6024719451
21MethylationAVFISDIRNCKSKEA
HHHHHCHHCCCCCHH		47.70-
31UbiquitinationKSKEAEIKRINKELA
CCCHHHHHHHHHHHH		38.4424816145
35AcetylationAEIKRINKELANIRS
HHHHHHHHHHHHHHH		52.3022645915
35MalonylationAEIKRINKELANIRS
HHHHHHHHHHHHHHH		52.3026320211
35UbiquitinationAEIKRINKELANIRS
HHHHHHHHHHHHHHH		52.3033845483
45UbiquitinationANIRSKFKGDKALDG
HHHHHHCCCCHHCCC		70.6833845483
48MalonylationRSKFKGDKALDGYSK
HHHCCCCHHCCCCCH		60.5630639696
48UbiquitinationRSKFKGDKALDGYSK
HHHCCCCHHCCCCCH		60.5633845483
52UbiquitinationKGDKALDGYSKKKYV
CCCHHCCCCCHHHHH		29.4824816145
53PhosphorylationGDKALDGYSKKKYVC
CCHHCCCCCHHHHHH		19.5828102081
54PhosphorylationDKALDGYSKKKYVCK
CHHCCCCCHHHHHHH		43.4528102081
55UbiquitinationKALDGYSKKKYVCKL
HHCCCCCHHHHHHHH		44.8129967540
62UbiquitinationKKKYVCKLLFIFLLG
HHHHHHHHHHHHHHC		3.9027667366
65UbiquitinationYVCKLLFIFLLGHDI
HHHHHHHHHHHCCCC		2.1027667366
85PhosphorylationEAVNLLSSNKYTEKQ
HHHHHHHCCCCCHHH		36.9922210691
117MalonylationRLINNAIKNDLASRN
HHHHHHHHHCHHHCC		41.8326320211
117UbiquitinationRLINNAIKNDLASRN
HHHHHHHHHCHHHCC		41.8322817900
117 (in isoform 1)Ubiquitination-41.8321890473
117 (in isoform 2)Ubiquitination-41.8321890473
134UbiquitinationFMCLALHCIANVGSR
HHHHHHHHHHHHCCH		3.0621890473
143SulfoxidationANVGSREMGEAFAAD
HHHCCHHHHHHHHCC		5.9721406390
161SulfoxidationILVAGDSMDSVKQSA
EEEECCCCHHHHHHH		5.4621406390
165AcetylationGDSMDSVKQSAALCL
CCCCHHHHHHHHHHH		42.357664285
165UbiquitinationGDSMDSVKQSAALCL
CCCCHHHHHHHHHHH		42.3532015554
167PhosphorylationSMDSVKQSAALCLLR
CCHHHHHHHHHHHHH		15.1421406692
177AcetylationLCLLRLYKASPDLVP
HHHHHHHHHCCCCCC		47.1623954790
177MalonylationLCLLRLYKASPDLVP
HHHHHHHHHCCCCCC		47.1626320211
179PhosphorylationLLRLYKASPDLVPMG
HHHHHHHCCCCCCCC		18.1346164979
185SulfoxidationASPDLVPMGEWTARV
HCCCCCCCCHHHHHH		6.2330846556
189PhosphorylationLVPMGEWTARVVHLL
CCCCCHHHHHHHHHH		10.5724719451
231PhosphorylationTCVSLAVSRLSRIVS
HHHHHHHHHHHHHHH		23.1521406692
234PhosphorylationSLAVSRLSRIVSSAS
HHHHHHHHHHHHHCC		20.8928355574
277UbiquitinationPPEDAAVKGRLVECL
CCCHHHHCCHHHHHH		33.3224816145
290UbiquitinationCLETVLNKAQEPPKS
HHHHHHHHCCCCCCC		47.4929967540
294UbiquitinationVLNKAQEPPKSKKVQ
HHHHCCCCCCCCCCC		29.5524816145
358PhosphorylationESMCTLASSEFSHEA
HHHHHHHCCCCCHHH		33.259407517
378UbiquitinationDTVINALKTERDVSV
HHHHHHHHCCCCHHH		46.0222817900
394PhosphorylationQRAADLLYAMCDRSN
HHHHHHHHHHCCCCC		10.2925147952
395UbiquitinationRAADLLYAMCDRSNA
HHHHHHHHHCCCCCH		7.6622817900
403MalonylationMCDRSNAKQIVSEML
HCCCCCHHHHHHHHH		44.8226320211
403UbiquitinationMCDRSNAKQIVSEML
HCCCCCHHHHHHHHH		44.8230230243
412PhosphorylationIVSEMLRYLETADYA
HHHHHHHHHHHCCHH		12.62141279
418PhosphorylationRYLETADYAIREEIV
HHHHHCCHHHHHHHH		11.06141287
456PhosphorylationLIRIAGDYVSEEVWY
HHHHHCHHCCHHHHH		12.64110738433
470PhosphorylationYRVLQIVTNRDDVQG
HHHHHHHCCCCCCCH		26.6022985185
478PhosphorylationNRDDVQGYAAKTVFE
CCCCCCHHHHHHHHH		6.0620068231
517PhosphorylationLIAGDPRSSPPVQFS
CCCCCCCCCCCCCHH		53.2125159151
517 (in isoform 2)Phosphorylation-53.21-
518PhosphorylationIAGDPRSSPPVQFSL
CCCCCCCCCCCCHHH		34.2125159151
524PhosphorylationSSPPVQFSLLHSKFH
CCCCCCHHHHCCHHH		16.9628060719
528PhosphorylationVQFSLLHSKFHLCSV
CCHHHHCCHHHHHHH		36.6728060719
543PhosphorylationATRALLLSTYIKFIN
HHHHHHHHHHHHHHH		21.0921406692
544PhosphorylationTRALLLSTYIKFINL
HHHHHHHHHHHHHHH		29.2721406692
545PhosphorylationRALLLSTYIKFINLF
HHHHHHHHHHHHHHC		9.9521406692
556UbiquitinationINLFPETKATIQGVL
HHHCCCCHHHHHHHH		41.7033845483
558PhosphorylationLFPETKATIQGVLRA
HCCCCHHHHHHHHHH		18.5223612710
567PhosphorylationQGVLRAGSQLRNADV
HHHHHHCHHHHCCCH		25.6726437602
570MethylationLRAGSQLRNADVELQ
HHHCHHHHCCCHHHH		28.75-
610PhosphorylationPPFPERESSILAKLK
CCCCCHHHHHHHHHH		28.9723312004
611PhosphorylationPFPERESSILAKLKR
CCCCHHHHHHHHHHH		19.5023312004
615UbiquitinationRESSILAKLKRKKGP
HHHHHHHHHHHCCCC		51.6133845483
620AcetylationLAKLKRKKGPGAGSA
HHHHHHCCCCCCCCC		74.5026051181
620UbiquitinationLAKLKRKKGPGAGSA
HHHHHHCCCCCCCCC		74.5033845483
626PhosphorylationKKGPGAGSALDDGRR
CCCCCCCCCCCCCCC		25.7321082442
626 (in isoform 2)Phosphorylation-25.73-
632UbiquitinationGSALDDGRRDPSSND
CCCCCCCCCCCCCCC		46.9924816145
636PhosphorylationDDGRRDPSSNDINGG
CCCCCCCCCCCCCCC		46.177185937
636 (in isoform 2)Phosphorylation-46.17-
637PhosphorylationDGRRDPSSNDINGGM
CCCCCCCCCCCCCCC		43.8623927012
637UbiquitinationDGRRDPSSNDINGGM
CCCCCCCCCCCCCCC		43.8624816145
637 (in isoform 2)Phosphorylation-43.86-
647PhosphorylationINGGMEPTPSTVSTP
CCCCCCCCCCCCCCC		19.3029255136
649PhosphorylationGGMEPTPSTVSTPSP
CCCCCCCCCCCCCCC		43.8729255136
649 (in isoform 2)Phosphorylation-43.87-
650PhosphorylationGMEPTPSTVSTPSPS
CCCCCCCCCCCCCCC		21.4929255136
650 (in isoform 2)Phosphorylation-21.49-
652PhosphorylationEPTPSTVSTPSPSAD
CCCCCCCCCCCCCCC		34.3929255136
652 (in isoform 2)Phosphorylation-34.39-
653O-linked_GlycosylationPTPSTVSTPSPSADL
CCCCCCCCCCCCCCC		24.37OGP
653PhosphorylationPTPSTVSTPSPSADL
CCCCCCCCCCCCCCC		24.3729255136
653 (in isoform 2)Phosphorylation-24.37-
655PhosphorylationPSTVSTPSPSADLLG
CCCCCCCCCCCCCCC		31.4129255136
655 (in isoform 2)Phosphorylation-31.41-
657PhosphorylationTVSTPSPSADLLGLR
CCCCCCCCCCCCCCC		38.4629255136
657 (in isoform 2)Phosphorylation-38.46-
728UbiquitinationDPAPAADPGPEDIGP
CCCCCCCCCCCCCCC		56.3529967540
744UbiquitinationIPEADELLNKFVCKN
CCCHHHHHHHHHHCC		6.5332015554
750AcetylationLLNKFVCKNNGVLFE
HHHHHHHCCCCEEEC		48.4226051181
750UbiquitinationLLNKFVCKNNGVLFE
HHHHHHHCCCCEEEC		48.4229967540
766AcetylationQLLQIGVKSEFRQNL
CHHHHCCCHHHHHHC		38.7726051181
766UbiquitinationQLLQIGVKSEFRQNL
CHHHHCCCHHHHHHC		38.7732015554
777PhosphorylationRQNLGRMYLFYGNKT
HHHCCCEEEEECCCC		7.7228152594
792PhosphorylationSVQFQNFSPTVVHPG
EEEEECCCCCEECCC		27.4924076635
794PhosphorylationQFQNFSPTVVHPGDL
EEECCCCCEECCCCH		33.6825307156
810MalonylationTQLAVQTKRVAAQVD
HHHHHCCCCCEEECC		27.9926320211
810UbiquitinationTQLAVQTKRVAAQVD
HHHHHCCCCCEEECC		27.99-
836PhosphorylationECLRDFLTPPLLSVR
HHHHHHCCCCEEEEE		23.8925850435
856UbiquitinationAPQALTLKLPVTINK
CCCEEEEEECEEEHH		45.57-
858UbiquitinationQALTLKLPVTINKFF
CEEEEEECEEEHHHC		21.4433845483
858 (in isoform 2)Ubiquitination-21.4421890473
869UbiquitinationNKFFQPTEMAAQDFF
HHHCCCHHHHHHHHH		33.2421890473
869 (in isoform 2)Ubiquitination-33.2421890473
872UbiquitinationFQPTEMAAQDFFQRW
CCCHHHHHHHHHHHH		14.2522817900
875UbiquitinationTEMAAQDFFQRWKQL
HHHHHHHHHHHHHHC		3.6021890473
880UbiquitinationQDFFQRWKQLSLPQQ
HHHHHHHHHCCCCHH		43.4822817900
880 (in isoform 1)Ubiquitination-43.4821890473
883UbiquitinationFQRWKQLSLPQQEAQ
HHHHHHCCCCHHHHH		35.1929967540
885UbiquitinationRWKQLSLPQQEAQKI
HHHHCCCCHHHHHHH		30.3630230243
885 (in isoform 2)Ubiquitination-30.3621890473
886UbiquitinationWKQLSLPQQEAQKIF
HHHCCCCHHHHHHHH		60.0721890473
889UbiquitinationLSLPQQEAQKIFKAN
CCCCHHHHHHHHHCC		16.1922817900
891UbiquitinationLPQQEAQKIFKANHP
CCHHHHHHHHHCCCC		58.1022817900
891 (in isoform 1)Ubiquitination-58.1021890473
894AcetylationQEAQKIFKANHPMDA
HHHHHHHHCCCCCCH		52.3225953088
894UbiquitinationQEAQKIFKANHPMDA
HHHHHHHHCCCCCCH		52.3222817900
897UbiquitinationQKIFKANHPMDAEVT
HHHHHCCCCCCHHHH		24.7521890473
899SulfoxidationIFKANHPMDAEVTKA
HHHCCCCCCHHHHHH		6.2430846556
905UbiquitinationPMDAEVTKAKLLGFG
CCCHHHHHHHHHCCH		49.0129967540
907UbiquitinationDAEVTKAKLLGFGSA
CHHHHHHHHHCCHHH		45.892190698
907 (in isoform 1)Ubiquitination-45.8921890473
908UbiquitinationAEVTKAKLLGFGSAL
HHHHHHHHHCCHHHH		7.2621890473
911UbiquitinationTKAKLLGFGSALLDN
HHHHHHCCHHHHHHC		7.6322817900
953SulfoxidationEPNAQAQMYRLTLRT
CCCHHHHEEEEHHHC		2.0521406390
954PhosphorylationPNAQAQMYRLTLRTS
CCHHHHEEEEHHHCC		7.1523401153
960PhosphorylationMYRLTLRTSKEPVSR
EEEEHHHCCCCCHHH		47.4623401153
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_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of AP2A1_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 AP2A1_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
RFIP2_HUMANRAB11FIP2physical
12364336
EPS15_HUMANEPS15physical
10764745
RBP1_HUMANRALBP1physical
10764745
REPS2_HUMANREPS2physical
10764745
EPN1_HUMANEPN1physical
10764745
EPS15_MOUSEEps15physical
12057195
EPN1_RATEpn1physical
12057195
AMPH_HUMANAMPHphysical
12057195
SYNJ1_HUMANSYNJ1physical
12057195
AP2A2_HUMANAP2A2physical
22939629
PICAL_HUMANPICALMphysical
22939629
AP1B1_HUMANAP1B1physical
26344197
AP2B1_HUMANAP2B1physical
26344197
EI2BA_HUMANEIF2B1physical
26344197
OCRL_HUMANOCRLphysical
27173435
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 AP2A1_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Large-scale proteomics analysis of the human kinome.";
Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G.,Mann M., Daub H.;
Mol. Cell. Proteomics 8:1751-1764(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-655, AND MASSSPECTROMETRY.
"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-652; THR-653 ANDSER-655, AND MASS SPECTROMETRY.
"Kinase-selective enrichment enables quantitative phosphoproteomics ofthe kinome across the cell cycle.";
Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,Greff Z., Keri G., Stemmann O., Mann M.;
Mol. Cell 31:438-448(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-626; SER-652; THR-653;SER-655 AND SER-657, AND MASS SPECTROMETRY.

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