dbPTM

AP180_MOUSE - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	AP180_MOUSE
UniProt AC	Q61548
Protein Name	Clathrin coat assembly protein AP180
Gene Name	Snap91
Organism	Mus musculus (Mouse).
Sequence Length	901
Subcellular Localization	Cell membrane. Membrane, coated pit Peripheral membrane protein Cytoplasmic side. Component of the coat surrounding the cytoplasmic face of coated vesicles in the plasma membrane.
Protein Description	Adaptins are components of the adaptor complexes which link clathrin to receptors in coated vesicles. Clathrin-associated protein complexes are believed to interact with the cytoplasmic tails of membrane proteins, leading to their selection and concentration. Binding of AP180 to clathrin triskelia induces their assembly into 60-70 nm coats..
Protein Sequence	MSGQTLTDRIAAAQYSVTGSAVARAVCKATTHEVMGPKKKHLDYLIQATNETNVNIPQMADTLFERATNSSWVVVFKALVTTHHLMVHGNERFIQYLASRNTLFNLSNFLDKSGSHGYDMSTFIRRYSRYLNEKAFSYRQMAFDFARVKKGADGVMRTMVPEKLLKSMPILQGQIDALLEFDVHPNELTNGVINAAFMLLFKDLIKLFACYNDGVINLLEKFFEMKKGQCKDALEIYKRFLTRMTRVSEFLKVAEQVGIDKGDIPDLTQAPSSLMETLEQHLNTLEGKKPGNNEGSGAPSPLSKSSPATTVTSPNSTPAKTIDTSPPVDIFATASAAAPVSSAKPSSDLLDLQPDFSGAAAGAAAPVVPPSGGATAWGDLLGEDSLAALSSVPCEAPISDPFAPEPSPPTTTTEPASASASTTTAVTAVTTEVDLFGDAFAASPGEAPAASEGATAPATPAPVAAALDACSGNDPFAPSEGSAEAAPELDLFAMKPPETSAPVVTPTASTAPPVPATAPSPAPTAVAATAATTTAAAAATTTATTSAAAATTAAAPPALDIFGDLFDSAPEVAAAPKPDAAPSIDLFGTDAFSSPPRGASPVPESSLTADLLSVDAFAAPSPASTASPAKAESSGVIDLFGDAFGSGASETQPAPQAVSSSSASADLLAGFGGSFMAPSTTPVTPAQNNLLQPSFEAAFGTTPSTSSSSSFDPSVFDGLGDLLMPTMAPSGQPAPVSMVPPSPAMAASKGLGSDLDSSLASLVGNLGISGTTSKKGDLQWNAGEKKLTGGANWQPKVTPATWSAGVPPQGTVPPTSSVPPGAGAPSVGQPGAGFGMPPSGTGMTMMSQQPVMFAQPMMRPPFGAAAVPGTQLSPSPTPATQSPKKPPAKDPLADLNIKDFL

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
15	Phosphorylation	DRIAAAQYSVTGSAV HHHHHHHCCCHHHHH	10.61	22817900
16	Phosphorylation	RIAAAQYSVTGSAVA HHHHHHCCCHHHHHH	10.92	28066266
18	Phosphorylation	AAAQYSVTGSAVARA HHHHCCCHHHHHHHH	21.34	28066266
68	Phosphorylation	DTLFERATNSSWVVV HHHHHHHCCCCEEEE	41.68	20415495
70	Phosphorylation	LFERATNSSWVVVFK HHHHHCCCCEEEEEE	22.63	20415495
71	Phosphorylation	FERATNSSWVVVFKA HHHHCCCCEEEEEEH	26.43	29899451
96	Phosphorylation	GNERFIQYLASRNTL CCHHHHHHHHHCCCH	10.22	-
99	Phosphorylation	RFIQYLASRNTLFNL HHHHHHHHCCCHHHH	24.38	-
102	Phosphorylation	QYLASRNTLFNLSNF HHHHHCCCHHHHHHH	31.45	22817900
107	Phosphorylation	RNTLFNLSNFLDKSG CCCHHHHHHHHCCCC	27.00	22324799
113	Phosphorylation	LSNFLDKSGSHGYDM HHHHHCCCCCCCCCH	45.23	19060867
115	Phosphorylation	NFLDKSGSHGYDMST HHHCCCCCCCCCHHH	22.34	19060867
134	Ubiquitination	YSRYLNEKAFSYRQM HHHHHCHHCCHHHHH	54.37	22790023
248	Phosphorylation	LTRMTRVSEFLKVAE HHHHHHHHHHHHHHH	21.24	22817900
296	Phosphorylation	KPGNNEGSGAPSPLS CCCCCCCCCCCCCCC	26.13	25521595
300	Phosphorylation	NEGSGAPSPLSKSSP CCCCCCCCCCCCCCC	37.63	25521595
303	Phosphorylation	SGAPSPLSKSSPATT CCCCCCCCCCCCCCE	33.60	22324799
303	O-linked_Glycosylation	SGAPSPLSKSSPATT CCCCCCCCCCCCCCE	33.60	9460413
305	Phosphorylation	APSPLSKSSPATTVT CCCCCCCCCCCCEEC	37.87	25521595
306	Phosphorylation	PSPLSKSSPATTVTS CCCCCCCCCCCEECC	23.45	25521595
309	Phosphorylation	LSKSSPATTVTSPNS CCCCCCCCEECCCCC	25.78	25521595
309	O-linked_Glycosylation	LSKSSPATTVTSPNS CCCCCCCCEECCCCC	25.78	9460437
310	O-linked_Glycosylation	SKSSPATTVTSPNST CCCCCCCEECCCCCC	24.72	30059200
310	Phosphorylation	SKSSPATTVTSPNST CCCCCCCEECCCCCC	24.72	24925903
312	Phosphorylation	SSPATTVTSPNSTPA CCCCCEECCCCCCCC	36.05	25521595
313	Phosphorylation	SPATTVTSPNSTPAK CCCCEECCCCCCCCC	20.11	25521595
316	Phosphorylation	TTVTSPNSTPAKTID CEECCCCCCCCCCCC	38.87	25521595
317	Phosphorylation	TVTSPNSTPAKTIDT EECCCCCCCCCCCCC	33.63	25521595
321	Phosphorylation	PNSTPAKTIDTSPPV CCCCCCCCCCCCCCC	26.62	22817900
324	Phosphorylation	TPAKTIDTSPPVDIF CCCCCCCCCCCCEEE	39.00	19060867
325	Phosphorylation	PAKTIDTSPPVDIFA CCCCCCCCCCCEEEE	24.37	22817900
333	Phosphorylation	PPVDIFATASAAAPV CCCEEEEECCCCCCC	15.47	20415495
335	Phosphorylation	VDIFATASAAAPVSS CEEEEECCCCCCCCC	17.68	22817900
341	Phosphorylation	ASAAAPVSSAKPSSD CCCCCCCCCCCCCHH	24.42	20415495
342	Phosphorylation	SAAAPVSSAKPSSDL CCCCCCCCCCCCHHH	40.31	20415495
593	Phosphorylation	LFGTDAFSSPPRGAS CCCCCCCCCCCCCCC	43.59	20415495
594	Phosphorylation	FGTDAFSSPPRGASP CCCCCCCCCCCCCCC	32.25	22817900
600	Phosphorylation	SSPPRGASPVPESSL CCCCCCCCCCCHHHH	29.29	24925903
605	Phosphorylation	GASPVPESSLTADLL CCCCCCHHHHCCCEE	25.28	24925903
606	Phosphorylation	ASPVPESSLTADLLS CCCCCHHHHCCCEEC	28.25	28066266
608	Phosphorylation	PVPESSLTADLLSVD CCCHHHHCCCEECCC	21.77	24925903
613	Phosphorylation	SLTADLLSVDAFAAP HHCCCEECCCCCCCC	25.83	24925903
621	Phosphorylation	VDAFAAPSPASTASP CCCCCCCCCCCCCCH	28.50	28066266
624	Phosphorylation	FAAPSPASTASPAKA CCCCCCCCCCCHHHH	28.08	28066266
625	Phosphorylation	AAPSPASTASPAKAE CCCCCCCCCCHHHHH	33.01	28066266
627	Phosphorylation	PSPASTASPAKAESS CCCCCCCCHHHHHHC	26.02	24925903
753	Phosphorylation	AASKGLGSDLDSSLA HHHCCCCCCHHHHHH	39.79	29899451
757	Phosphorylation	GLGSDLDSSLASLVG CCCCCHHHHHHHHHH	34.25	22324799
758	Phosphorylation	LGSDLDSSLASLVGN CCCCHHHHHHHHHHH	27.85	22324799
761	Phosphorylation	DLDSSLASLVGNLGI CHHHHHHHHHHHCCC	28.96	29899451
773	Phosphorylation	LGISGTTSKKGDLQW CCCCCCCCCCCCCEE	32.01	29899451
859	Methylation	MFAQPMMRPPFGAAA EECCCCCCCCCCCCC	29.50	24129315
859	Asymmetric dimethylarginine	MFAQPMMRPPFGAAA EECCCCCCCCCCCCC	29.50	-
873	Phosphorylation	AVPGTQLSPSPTPAT CCCCCCCCCCCCCCC	17.32	21082442
882	Phosphorylation	SPTPATQSPKKPPAK CCCCCCCCCCCCCCC	34.04	21082442

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 AP180_MOUSE !!

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Reference
310	T	Phosphorylation	-
There is no evidence for direct Thr-310 phosphorylation (By similarity).
310	T	Phosphorylation	-
Thr-310 can be modified by the addition of N-acetylglucosamine which can be further phosphorylated.

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 AP180_MOUSE !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference	Domain-Domain Interactions
Oops, there are no PPI records of AP180_MOUSE !!

Drug and Disease Associations

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

Regulatory Network of AP180_MOUSE

Related Literatures of Post-Translational Modification

Phosphorylation
Reference	PubMed
"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 THR-312; SER-316 ANDSER-600, AND MASS SPECTROMETRY.	17114649 [Abstract]
"Phosphoproteomic analysis of the developing mouse brain."; Ballif B.A., Villen J., Beausoleil S.A., Schwartz D., Gygi S.P.; Mol. Cell. Proteomics 3:1093-1101(2004). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-313, AND MASSSPECTROMETRY.	15345747 [Abstract]

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