AP2A2_MOUSE - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: AP2A2_MOUSE
• UniProt AC: P17427
• Protein Name: AP-2 complex subunit alpha-2
• Gene Name: Ap2a2
• Organism: Mus musculus (Mouse).
• Sequence Length: 938
• 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..
• Protein Sequence: MPAVSKGDGMRGLAVFISDIRNCKSKEAEIKRINKELANIRSKFKGDKALDGYSKKKYVCKLLFIFLLGHDIDFGHMEAVNLLSSNRYTEKQIGYLFISVLVNSNSELIRLINNAIKNDLASRNPTFMGLALHCIANVGSREMAEAFAGEIPKILVAGDTMDSVKQSAALCLLRLYRTSPDLVPMGDWTSRVVHLLNDQHLGVVTAATSLITTLAQKNPEEFKTSVSLAVSRLSRIVTSASTDLQDYTYYFVPAPWLSVKLLRLLQCYPPPDPAVRGRLTECLETILNKAQEPPKSKKVQHSNAKNAVLFEAISLIIHHDSEPNLLVRACNQLGQFLQHRETNLRYLALESMCTLASSEFSHEAVKTHIETVINALKTERDVSVRQRAVDLLYAMCDRSNAQQIVAEMLSYLETADYSIREEIVLKVAILAEKYAVDYTWYVDTILNLIRIAGDYVSEEVWYRVIQIVINRDDVQGYAAKTVFEALQAPACHENLVKVGGYILGEFGNLIAGDPRSSPLIQFNLLHSKFHLCSVPTRALLLSTYIKFVNLFPEVKATIQDVLRSDSQLKNADVELQQRAVEYLRLSTVASTDILATVLEEMPPFPERESSILAKLKKKKGPSTVTDLEETKRERSIDVNGGPEPVPASTSAASTPSPSADLLGLGAVPPAPTGPPPSSGGGLLVDVFSDSASAVAPLAPGSEDNFARFVCKNNGVLFENQLLQIGLKSEFRQNLGRMFIFYGNKTSTQFLNFTPTLICADDLQTNLNLQTKPVDPTVDGGAQVQQVVNIECISDFTEAPVLNIQFRYGGTFQNVSVKLPITLNKFFQPTEMASQDFFQRWKQLSNPQQEVQNIFKAKHPMDTEITKAKIIGFGSALLEEVDPNPANFVGAGIIHTKTTQIGCLLRLEPNLQAQMYRLTLRTSKDTVSQRLCELLSEQF

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
6	Malonylation	--MPAVSKGDGMRGL --CCCCCCCCCCHHH	55.19	26320211
6	Ubiquitination	--MPAVSKGDGMRGL --CCCCCCCCCCHHH	55.19	-
35	Malonylation	AEIKRINKELANIRS HHHHHHHHHHHHHHH	52.30	26320211
35	Ubiquitination	AEIKRINKELANIRS HHHHHHHHHHHHHHH	52.30	-
53	Phosphorylation	GDKALDGYSKKKYVC CCCCCCCCCHHHHHH	19.58	25195567
95	Phosphorylation	YTEKQIGYLFISVLV CCHHHCCCCEEEEEE	10.48	26643407
99	Phosphorylation	QIGYLFISVLVNSNS HCCCCEEEEEECCCH	11.32	26643407
104	Phosphorylation	FISVLVNSNSELIRL EEEEEECCCHHHHHH	33.96	26643407
106	Phosphorylation	SVLVNSNSELIRLIN EEEECCCHHHHHHHH	33.33	26643407
134	S-palmitoylation	FMGLALHCIANVGSR HHHHHHHHHHHCCCH	3.06	28680068
165	Ubiquitination	GDTMDSVKQSAALCL CCCHHHHHHHHHHHH	42.35	-
171	S-palmitoylation	VKQSAALCLLRLYRT HHHHHHHHHHHHHHH	2.63	28526873
231	Phosphorylation	TSVSLAVSRLSRIVT HHHHHHHHHHHHHHH	23.15	23737553
234	Phosphorylation	SLAVSRLSRIVTSAS HHHHHHHHHHHHHCC	20.89	23737553
282	S-palmitoylation	VRGRLTECLETILNK HHCHHHHHHHHHHHH	3.33	28526873
330	S-palmitoylation	PNLLVRACNQLGQFL CCHHHHHHHHHHHHH	2.03	28526873
330	S-nitrosylation	PNLLVRACNQLGQFL CCHHHHHHHHHHHHH	2.03	20925432
330	S-nitrosocysteine	PNLLVRACNQLGQFL CCHHHHHHHHHHHHH	2.03	-
353	S-palmitoylation	YLALESMCTLASSEF HHHHHHHHHHHCCCC	3.82	28526873
396	S-palmitoylation	VDLLYAMCDRSNAQQ HHHHHHHCCCCCHHH	2.75	28526873
532	S-palmitoylation	LHSKFHLCSVPTRAL CCCCHHHCCHHHHHH	2.64	28526873
564	Phosphorylation	TIQDVLRSDSQLKNA HHHHHHHCCHHHCCC	37.14	29899451
569	Ubiquitination	LRSDSQLKNADVELQ HHCCHHHCCCCHHHH	42.31	-
614	Ubiquitination	RESSILAKLKKKKGP HHHHHHHHHHHCCCC	58.35	-
619	Ubiquitination	LAKLKKKKGPSTVTD HHHHHHCCCCCCCCC	82.19	-
619	Malonylation	LAKLKKKKGPSTVTD HHHHHHCCCCCCCCC	82.19	26320211
622	Phosphorylation	LKKKKGPSTVTDLEE HHHCCCCCCCCCHHH	44.15	29899451
623	Phosphorylation	KKKKGPSTVTDLEET HHCCCCCCCCCHHHH	30.47	11758877
625	Phosphorylation	KKGPSTVTDLEETKR CCCCCCCCCHHHHHH	34.65	29899451
631	Ubiquitination	VTDLEETKRERSIDV CCCHHHHHHHCCCCC	56.38	-
635	Phosphorylation	EETKRERSIDVNGGP HHHHHHCCCCCCCCC	20.56	23649490
692	Phosphorylation	DVFSDSASAVAPLAP EEECCCCCCCCCCCC	27.51	23649490
807	Phosphorylation	VLNIQFRYGGTFQNV EEEEEEEECCEECCE	22.61	17203969
841	Ubiquitination	QDFFQRWKQLSNPQQ HHHHHHHHHCCCHHH	43.48	-
855	Ubiquitination	QEVQNIFKAKHPMDT HHHHHHHHCCCCCCC	53.37	-
902	S-palmitoylation	TKTTQIGCLLRLEPN ECCCEECEEEECCCC	3.27	28526873
922	Phosphorylation	YRLTLRTSKDTVSQR EHHHHHCCHHHHHHH	23.31	24719451
927	Phosphorylation	RTSKDTVSQRLCELL HCCHHHHHHHHHHHH	16.21	24719451

Upstream regulatory proteins (kinases for phosphorylation sites, E3 ubiquitin ligases of ubiquitination sites, ...)

Oops, there are no upstream regulatory protein records of AP2A2_MOUSE !!

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of AP2A2_MOUSE !!

Disease-associated PTM Sites based on SAP

* Distance = the distance between SAP position and PTM sites.

Oops, there are no SNP-PTM records of AP2A2_MOUSE !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
SPTN2_RAT	Sptbn2	physical	10477754
AAGAB_RAT	Aagab	physical	10477754
AP180_RAT	Snap91	physical	10430869
AMPH_RAT	Amph	physical	10430869
EPN1_RAT	Epn1	physical	10430869
DYN1_RAT	Dnm1	physical	10430869
BIN1_RAT	Bin1	physical	10430869

Drug and Disease Associations

• Kegg Drug
• DrugBank
• There are no disease associations of PTM sites.

Related Literatures of Post-Translational Modification

Phosphorylation

"Protein phosphorylation and expression profiling by Yin-yangmultidimensional liquid chromatography (Yin-yang MDLC) massspectrometry.";
Dai J., Jin W.-H., Sheng Q.-H., Shieh C.-H., Wu J.-R., Zeng R.;
J. Proteome Res. 6:250-262(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-807, AND MASSSPECTROMETRY.
PubMed: 17203969