AP2B1_MOUSE - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: AP2B1_MOUSE
• UniProt AC: Q9DBG3
• Protein Name: AP-2 complex subunit beta
• Gene Name: Ap2b1
• Organism: Mus musculus (Mouse).
• Sequence Length: 937
• 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 beta subunit acts via its C-terminal appendage domain as a scaffolding platform for endocytic accessory proteins; at least some clathrin-associated sorting proteins (CLASPs) are recognized by their [DE]-X(1,2)-F-X-X-[FL]-X-X-X-R motif. The AP-2 beta subunit binds to clathrin heavy chain, promoting clathrin lattice assembly; clathrin displaces at least some CLASPs from AP2B1 which probably then can be positioned for further coat assembly (By similarity)..
• Protein Sequence: MTDSKYFTTNKKGEIFELKAELNNEKKEKRKEAVKKVIAAMTVGKDVSSLFPDVVNCMQTDNLELKKLVYLYLMNYAKSQPDMAIMAVNSFVKDCEDPNPLIRALAVRTMGCIRVDKITEYLCEPLRKCLKDEDPYVRKTAAVCVAKLHDINAQMVEDQGFLDSLRDLIADSNPMVVANAVAALSEISESHPNSNLLDLNPQNINKLLTALNECTEWGQIFILDCLSNYNPKDDREAQSICERVTPRLSHANSAVVLSAVKVLMKFLELLPKDSDYYNMLLKKLAPPLVTLLSGEPEVQYVALRNINLIVQKRPEILKQEIKVFFVKYNDPIYVKLEKLDIMIRLASQANIAQVLAELKEYATEVDVDFVRKAVRAIGRCAIKVEQSAERCVSTLLDLIQTKVNYVVQEAIVVIRDIFRKYPNKYESIIATLCENLDSLDEPDARAAMIWIVGEYAERIDNADELLESFLEGFHDESTQVQLTLLTAIVKLFLKKPSETQELVQQVLSLATQDSDNPDLRDRGYIYWRLLSTDPVTAKEVVLSEKPLISEETDLIEPTLLDELICHIGSLASVYHKPPNAFVEGSHGIHRKHLPIHHGSTDAGDSPVGTTTTTNLEQPQVIPSQGDLLGDLLNLDLGPPVNVPQVSSMQMGAVDLLGGGLDSLVGQSFIPSSVPATFAPSPTPAVVSSGLNDLFELSTGIGMAPGGYVAPKAVWLPAVKAKGLEISGTFTHRQGHIYMEMNFTNKALQHMTDFAIQFNKNSFGVIPSTPLAIHTPLMPNQSIDVSLPLNTLGPVMKMEPLNNLQVAVKNNIDVFYFSCLIPLNVLFVEDGKMERQVFLATWKDIPNENELQFQIKECHLNADTVSSKLQNNNVYTIAKRNVEGQDMLYQSLKLTNGIWILAELRIQPGNPNYTLSLKCRAPEVSQYIYQVYDSILKN

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
2	Phosphorylation	------MTDSKYFTT ------CCCCCCCCC	49.32	8571751
2	Acetylation	------MTDSKYFTT ------CCCCCCCCC	49.32	-
4	Phosphorylation	----MTDSKYFTTNK ----CCCCCCCCCCC	21.79	26487105
5	Acetylation	---MTDSKYFTTNKK ---CCCCCCCCCCCC	47.39	66700873
5	Malonylation	---MTDSKYFTTNKK ---CCCCCCCCCCCC	47.39	26320211
6	Phosphorylation	--MTDSKYFTTNKKG --CCCCCCCCCCCCC	15.31	29514104
8	Phosphorylation	MTDSKYFTTNKKGEI CCCCCCCCCCCCCCE	26.77	29514104
11	Malonylation	SKYFTTNKKGEIFEL CCCCCCCCCCCEEEH	61.12	26320211
12	Ubiquitination	KYFTTNKKGEIFELK CCCCCCCCCCEEEHH	64.94	-
42	Phosphorylation	KKVIAAMTVGKDVSS HHHHHHHHCCCCHHH	22.75	51460325
70	Phosphorylation	LELKKLVYLYLMNYA HHHHHHHHHHHHHHH	10.48	26643407
72	Phosphorylation	LKKLVYLYLMNYAKS HHHHHHHHHHHHHHC	6.04	26643407
76	Phosphorylation	VYLYLMNYAKSQPDM HHHHHHHHHHCCCCH	11.05	26643407
79	Phosphorylation	YLMNYAKSQPDMAIM HHHHHHHCCCCHHHH	38.48	26643407
117	Ubiquitination	MGCIRVDKITEYLCE CCCEEHHHHHHHHHH	48.98	-
123	S-palmitoylation	DKITEYLCEPLRKCL HHHHHHHHHHHHHHC	5.04	28526873
131	Ubiquitination	EPLRKCLKDEDPYVR HHHHHHCCCCCHHHH	69.42	-
136	Phosphorylation	CLKDEDPYVRKTAAV HCCCCCHHHHHHHHH	25.80	82611
239	Phosphorylation	KDDREAQSICERVTP CCHHHHHHHHHHHCC	35.93	29899451
249	Phosphorylation	ERVTPRLSHANSAVV HHHCCCCCCCCHHHH	23.10	15994067
253	Phosphorylation	PRLSHANSAVVLSAV CCCCCCCHHHHHHHH	24.19	22807455
258	Phosphorylation	ANSAVVLSAVKVLMK CCHHHHHHHHHHHHH	21.29	-
265	Acetylation	SAVKVLMKFLELLPK HHHHHHHHHHHHCCC	42.51	22826441
265	Ubiquitination	SAVKVLMKFLELLPK HHHHHHHHHHHHCCC	42.51	-
272	Ubiquitination	KFLELLPKDSDYYNM HHHHHCCCCCHHHHH	70.59	-
276	Phosphorylation	LLPKDSDYYNMLLKK HCCCCCHHHHHHHHH	10.74	25338131
277	Phosphorylation	LPKDSDYYNMLLKKL CCCCCHHHHHHHHHH	10.09	25338131
282	Acetylation	DYYNMLLKKLAPPLV HHHHHHHHHHCCCCC	41.60	23954790
283	Ubiquitination	YYNMLLKKLAPPLVT HHHHHHHHHCCCCCH	50.26	-
318	Acetylation	QKRPEILKQEIKVFF ECCHHHHHHHEEEEE	52.09	22826441
322	Acetylation	EILKQEIKVFFVKYN HHHHHHEEEEEEECC	32.03	22826441
327	Acetylation	EIKVFFVKYNDPIYV HEEEEEEECCCCEEE	32.93	22826441
347	Phosphorylation	DIMIRLASQANIAQV HHHHHHHCCCCHHHH	34.12	20415495
380	S-palmitoylation	AVRAIGRCAIKVEQS HHHHHHHHEEEHHHH	3.75	26165157
393	Phosphorylation	QSAERCVSTLLDLIQ HHHHHHHHHHHHHHH	19.57	30993257
394	Phosphorylation	SAERCVSTLLDLIQT HHHHHHHHHHHHHHH	15.79	29899451
433	Glutathionylation	ESIIATLCENLDSLD HHHHHHHHHCHHCCC	2.57	24333276
497	Phosphorylation	KLFLKKPSETQELVQ HHHCCCCHHHHHHHH	63.25	29899451
499	Phosphorylation	FLKKPSETQELVQQV HCCCCHHHHHHHHHH	31.51	29899451
508	Phosphorylation	ELVQQVLSLATQDSD HHHHHHHHHHHCCCC	19.66	20415495
538	Ubiquitination	STDPVTAKEVVLSEK CCCCCCHHHHHHCCC	41.50	-
599	Phosphorylation	HLPIHHGSTDAGDSP CCCCCCCCCCCCCCC	20.82	51460333
605	Phosphorylation	GSTDAGDSPVGTTTT CCCCCCCCCCCCCCC	22.14	30815403
609	Phosphorylation	AGDSPVGTTTTTNLE CCCCCCCCCCCCCCC	22.62	51460341
707	Nitration	IGMAPGGYVAPKAVW CCCCCCCEECCCEEE	10.19	-
719	Ubiquitination	AVWLPAVKAKGLEIS EEEECCCCCCCEEEE	46.62	-
726	Phosphorylation	KAKGLEISGTFTHRQ CCCCEEEEEEEEECC	23.54	19854140
737	Phosphorylation	THRQGHIYMEMNFTN EECCCEEEEEEECCH	4.95	25367039
743	Phosphorylation	IYMEMNFTNKALQHM EEEEEECCHHHHHHH	30.70	25367039
751	Phosphorylation	NKALQHMTDFAIQFN HHHHHHHHHHHHHCC	26.32	19854140
768	Phosphorylation	SFGVIPSTPLAIHTP CCCCCCCCCEEECCC	19.57	16181353
842	Acetylation	QVFLATWKDIPNENE EEEEEECCCCCCCCC	41.23	23954790
857	S-nitrosylation	LQFQIKECHLNADTV EEEEEEEEECCCHHH	3.62	20925432
857	S-nitrosocysteine	LQFQIKECHLNADTV EEEEEEEEECCCHHH	3.62	-
878	Ubiquitination	NNVYTIAKRNVEGQD CCEEEEEECCCCCHH	40.43	-
878	Acetylation	NNVYTIAKRNVEGQD CCEEEEEECCCCCHH	40.43	22826441
888	Phosphorylation	VEGQDMLYQSLKLTN CCCHHHHHHHHHCCC	6.87	75177
915	Phosphorylation	GNPNYTLSLKCRAPE CCCCEEEEEEECCHH	20.27	23649490
926	Phosphorylation	RAPEVSQYIYQVYDS CCHHHHHHHHHHHHH	8.29	20415495
928	Phosphorylation	PEVSQYIYQVYDSIL HHHHHHHHHHHHHHH	6.23	75181
931	Phosphorylation	SQYIYQVYDSILKN- HHHHHHHHHHHHCC-	6.61	15546519

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

Oops, there are no upstream regulatory protein records of AP2B1_MOUSE !!

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of AP2B1_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 AP2B1_MOUSE !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
EPS15_MOUSE	Eps15	physical	9182572

Drug and Disease Associations

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

Related Literatures of Post-Translational Modification

Phosphorylation

"Large-scale identification and evolution indexing of tyrosinephosphorylation sites from murine brain.";
Ballif B.A., Carey G.R., Sunyaev S.R., Gygi S.P.;
J. Proteome Res. 7:311-318(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-737 AND TYR-888, ANDMASS SPECTROMETRY.
PubMed: 18034455