AP2A2_HUMAN - dbPTM
AP2A2_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID AP2A2_HUMAN
UniProt AC O94973
Protein Name AP-2 complex subunit alpha-2
Gene Name AP2A2
Organism Homo sapiens (Human).
Sequence Length 939
Subcellular Localization Cell membrane
Peripheral membrane protein
Cytoplasmic side . 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 int
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 MPAVSKGDGMRGLAVFISDIRNCKSKEAEIKRINKELANIRSKFKGDKALDGYSKKKYVCKLLFIFLLGHDIDFGHMEAVNLLSSNRYTEKQIGYLFISVLVNSNSELIRLINNAIKNDLASRNPTFMGLALHCIASVGSREMAEAFAGEIPKVLVAGDTMDSVKQSAALCLLRLYRTSPDLVPMGDWTSRVVHLLNDQHLGVVTAATSLITTLAQKNPEEFKTSVSLAVSRLSRIVTSASTDLQDYTYYFVPAPWLSVKLLRLLQCYPPPDPAVRGRLTECLETILNKAQEPPKSKKVQHSNAKNAVLFEAISLIIHHDSEPNLLVRACNQLGQFLQHRETNLRYLALESMCTLASSEFSHEAVKTHIETVINALKTERDVSVRQRAVDLLYAMCDRSNAPQIVAEMLSYLETADYSIREEIVLKVAILAEKYAVDYTWYVDTILNLIRIAGDYVSEEVWYRVIQIVINRDDVQGYAAKTVFEALQAPACHENLVKVGGYILGEFGNLIAGDPRSSPLIQFHLLHSKFHLCSVPTRALLLSTYIKFVNLFPEVKPTIQDVLRSDSQLRNADVELQQRAVEYLRLSTVASTDILATVLEEMPPFPERESSILAKLKKKKGPSTVTDLEDTKRDRSVDVNGGPEPAPASTSAVSTPSPSADLLGLGAAPPAPAGPPPSSGGSGLLVDVFSDSASVVAPLAPGSEDNFARFVCKNNGVLFENQLLQIGLKSEFRQNLGRMFIFYGNKTSTQFLNFTPTLICSDDLQPNLNLQTKPVDPTVEGGAQVQQVVNIECVSDFTEAPVLNIQFRYGGTFQNVSVQLPITLNKFFQPTEMASQDFFQRWKQLSNPQQEVQNIFKAKHPMDTEVTKAKIIGFGSALLEEVDPNPANFVGAGIIHTKTTQIGCLLRLEPNLQAQMYRLTLRTSKEAVSQRLCELLSAQF
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-
31AcetylationKSKEAEIKRINKELA
CCCHHHHHHHHHHHH		38.4425953088
31UbiquitinationKSKEAEIKRINKELA
CCCHHHHHHHHHHHH		38.4424816145
35UbiquitinationAEIKRINKELANIRS
HHHHHHHHHHHHHHH		52.3027667366
35MalonylationAEIKRINKELANIRS
HHHHHHHHHHHHHHH		52.3026320211
35AcetylationAEIKRINKELANIRS
HHHHHHHHHHHHHHH		52.3019608861
41UbiquitinationNKELANIRSKFKGDK
HHHHHHHHHHCCCCC		33.3321890473
45UbiquitinationANIRSKFKGDKALDG
HHHHHHCCCCCCCCC		70.6833845483
48UbiquitinationRSKFKGDKALDGYSK
HHHCCCCCCCCCCCH		60.5633845483
53PhosphorylationGDKALDGYSKKKYVC
CCCCCCCCCHHHHHH		19.5828102081
54PhosphorylationDKALDGYSKKKYVCK
CCCCCCCCHHHHHHH		43.4528102081
55UbiquitinationKALDGYSKKKYVCKL
CCCCCCCHHHHHHHH		44.8129967540
84PhosphorylationMEAVNLLSSNRYTEK
HHHHHHHCCCCCCHH		28.8232142685
117 (in isoform 1)Ubiquitination-41.8321890473
117 (in isoform 3)Ubiquitination-41.8321890473
117 (in isoform 2)Ubiquitination-41.8321890473
117UbiquitinationRLINNAIKNDLASRN
HHHHHHHHHCHHHCC		41.8322817900
117MalonylationRLINNAIKNDLASRN
HHHHHHHHHCHHHCC		41.8326320211
161SulfoxidationVLVAGDTMDSVKQSA
EEEECCCHHHHHHHH		4.2621406390
167PhosphorylationTMDSVKQSAALCLLR
CHHHHHHHHHHHHHH		15.1421406692
227PhosphorylationEEFKTSVSLAVSRLS
HHHHHHHHHHHHHHH		15.4620068231
231PhosphorylationTSVSLAVSRLSRIVT
HHHHHHHHHHHHHHH		23.1520068231
234PhosphorylationSLAVSRLSRIVTSAS
HHHHHHHHHHHHHCC		20.8928355574
302UbiquitinationKSKKVQHSNAKNAVL
CCCCCCCCCHHHHHH		22.7622817900
357PhosphorylationESMCTLASSEFSHEA
HHHHHHHCCCCCHHH		33.259407517
377UbiquitinationETVINALKTERDVSV
HHHHHHHHCCCCCHH		46.0221906983
377 (in isoform 1)Ubiquitination-46.0221890473
378 (in isoform 3)Ubiquitination-36.7821890473
378UbiquitinationTVINALKTERDVSVR
HHHHHHHCCCCCHHH		36.7822817900
378 (in isoform 2)Ubiquitination-36.7821890473
383PhosphorylationLKTERDVSVRQRAVD
HHCCCCCHHHHHHHH		18.8318323811
410PhosphorylationQIVAEMLSYLETADY
HHHHHHHHHHHHCCC		26.7618323819
418PhosphorylationYLETADYSIREEIVL
HHHHCCCCCHHHHHH		18.7324719451
455PhosphorylationLIRIAGDYVSEEVWY
HHHHHCCCCCHHHHH		12.64110738137
480UbiquitinationDVQGYAAKTVFEALQ
CCCCHHHHHHHHHHC		36.7322817900
536PhosphorylationFHLCSVPTRALLLST
HHCCCHHHHHHHHHH		26.8150565787
539UbiquitinationCSVPTRALLLSTYIK
CCHHHHHHHHHHHHH		4.4522817900
541UbiquitinationVPTRALLLSTYIKFV
HHHHHHHHHHHHHHH		3.6022817900
542UbiquitinationPTRALLLSTYIKFVN
HHHHHHHHHHHHHHH		21.0922817900
542PhosphorylationPTRALLLSTYIKFVN
HHHHHHHHHHHHHHH		21.0921406692
543UbiquitinationTRALLLSTYIKFVNL
HHHHHHHHHHHHHHC		29.2722817900
543PhosphorylationTRALLLSTYIKFVNL
HHHHHHHHHHHHHHC		29.2721406692
544PhosphorylationRALLLSTYIKFVNLF
HHHHHHHHHHHHHCC		9.9521406692
544UbiquitinationRALLLSTYIKFVNLF
HHHHHHHHHHHHHCC		9.9522817900
555UbiquitinationVNLFPEVKPTIQDVL
HHCCCCCCCHHHHHH		34.4821906983
555 (in isoform 1)Ubiquitination-34.4821890473
556 (in isoform 2)Ubiquitination-39.6521890473
556 (in isoform 3)Ubiquitination-39.6521890473
556UbiquitinationNLFPEVKPTIQDVLR
HCCCCCCCHHHHHHH		39.6521963094
569MethylationLRSDSQLRNADVELQ
HHCCHHHHCCCHHHH		28.75-
609PhosphorylationPPFPERESSILAKLK
CCCCCHHHHHHHHHH		28.9723312004
610PhosphorylationPFPERESSILAKLKK
CCCCHHHHHHHHHHH		19.5023312004
614AcetylationRESSILAKLKKKKGP
HHHHHHHHHHHCCCC		58.3525953088
614UbiquitinationRESSILAKLKKKKGP
HHHHHHHHHHHCCCC		58.3522817900
615UbiquitinationESSILAKLKKKKGPS
HHHHHHHHHHCCCCC		9.0522817900
616UbiquitinationSSILAKLKKKKGPST
HHHHHHHHHCCCCCC		62.9422817900
617UbiquitinationSILAKLKKKKGPSTV
HHHHHHHHCCCCCCC		70.8822817900
618UbiquitinationILAKLKKKKGPSTVT
HHHHHHHCCCCCCCC		62.4722817900
619 (in isoform 1)Ubiquitination-82.1921890473
619UbiquitinationLAKLKKKKGPSTVTD
HHHHHHCCCCCCCCC		82.1921906983
620UbiquitinationAKLKKKKGPSTVTDL
HHHHHCCCCCCCCCH		30.2133845483
620 (in isoform 2)Ubiquitination-30.2121890473
620 (in isoform 3)Ubiquitination-30.2121890473
622PhosphorylationLKKKKGPSTVTDLED
HHHCCCCCCCCCHHH		44.1528857561
623PhosphorylationKKKKGPSTVTDLEDT
HHCCCCCCCCCHHHC		30.4728857561
625PhosphorylationKKGPSTVTDLEDTKR
CCCCCCCCCHHHCCC		34.6511758883
630PhosphorylationTVTDLEDTKRDRSVD
CCCCHHHCCCCCCCC		20.7111758893
631 (in isoform 1)Ubiquitination-65.7021890473
631UbiquitinationVTDLEDTKRDRSVDV
CCCHHHCCCCCCCCC		65.7021906983
632 (in isoform 2)Ubiquitination-46.8221890473
632 (in isoform 3)Ubiquitination-46.8221890473
632UbiquitinationTDLEDTKRDRSVDVN
CCHHHCCCCCCCCCC		46.8227667366
649 (in isoform 3)Phosphorylation-23.8622210691
650 (in isoform 3)Phosphorylation-24.9522210691
654PhosphorylationASTSAVSTPSPSADL
CCCCCCCCCCCCCCC		22.6126074081
656PhosphorylationTSAVSTPSPSADLLG
CCCCCCCCCCCCCCC		31.4126074081
658PhosphorylationAVSTPSPSADLLGLG
CCCCCCCCCCCCCCC		38.4626074081
712UbiquitinationNFARFVCKNNGVLFE
CHHHHHCCCCCEEEC		48.42-
713 (in isoform 2)Ubiquitination-45.41-
767UbiquitinationSDDLQPNLNLQTKPV
CCCCCCCCCCCCCCC		9.5921890473
808PhosphorylationVLNIQFRYGGTFQNV
EEEEEEEECCEECCE		22.6129052541
811PhosphorylationIQFRYGGTFQNVSVQ
EEEEECCEECCEEEE		20.0629052541
816PhosphorylationGGTFQNVSVQLPITL
CCEECCEEEEEEEEC		16.2229052541
822PhosphorylationVSVQLPITLNKFFQP
EEEEEEEECCCCCCC		23.4929052541
842 (in isoform 1)Ubiquitination-43.4821890473
842UbiquitinationQDFFQRWKQLSNPQQ
HHHHHHHHHCCCHHH		43.4822817900
843 (in isoform 2)Ubiquitination-43.0721890473
843UbiquitinationDFFQRWKQLSNPQQE
HHHHHHHHCCCHHHH		43.0721890473
845PhosphorylationFQRWKQLSNPQQEVQ
HHHHHHCCCHHHHHH		43.9327174698
858UbiquitinationVQNIFKAKHPMDTEV
HHHHHHCCCCCCCHH		49.1629967540
859UbiquitinationQNIFKAKHPMDTEVT
HHHHHCCCCCCCHHH		27.9829967540
861SulfoxidationIFKAKHPMDTEVTKA
HHHCCCCCCCHHHHH		11.2930846556
916PhosphorylationPNLQAQMYRLTLRTS
CCHHHHHHHHHHHCC		7.1524043423
919PhosphorylationQAQMYRLTLRTSKEA
HHHHHHHHHHCCHHH		12.7524043423
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 AP2A2_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of AP2A2_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 AP2A2_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
DAB2_HUMANDAB2physical
11247302
AMPH_HUMANAMPHphysical
9280305
EPS15_HUMANEPS15physical
18362181
A4_HUMANAPPphysical
21832049
PI51C_HUMANPIP5K1Cphysical
20435073
AT1A1_HUMANATP1A1physical
20435073
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 AP2A2_HUMAN

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Related Literatures of Post-Translational Modification
Acetylation
ReferencePubMed
"Lysine acetylation targets protein complexes and co-regulates majorcellular functions.";
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.,Olsen J.V., Mann M.;
Science 325:834-840(2009).
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-35, AND MASS SPECTROMETRY.

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