AP18A_YEAST - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: AP18A_YEAST
• UniProt AC: P38856
• Protein Name: Clathrin coat assembly protein AP180A
• Gene Name: YAP1801
• Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
• Sequence Length: 637
• Subcellular Localization: Bud . Bud neck . Cell membrane ; Peripheral membrane protein ; Cytoplasmic side . Cytoplasm .
• Protein Description: Involved in endocytosis and clathrin cage assembly..
• Protein Sequence: MTTYFKLVKGATKIKSAPPKQKYLDPILLGTSNEEDFYEIVKGLDSRINDTAWTIVYKSLLVVHLMIREGSKDVALRYYSRNLEFFDIENIRGSNGSASGDMRALDRYDNYLKVRCREFGKIKKDYVRDGYRTLKLNSGNYGSSRNKQHSINIALDHVESLEVQIQALIKNKYTQYDLSNELIIFGFKLLIQDLLALYNALNEGIITLLESFFELSHHNAERTLDLYKTFVDLTEHVVRYLKSGKTAGLKIPVIKHITTKLVRSLEEHLIEDDKTHNTFVPVDSSQGSAGAVVAKSTAQERLEQIREQKRILEAQLKNEQVAISPALTTVTAAQSYNPFGTDSSMHTNIPMAVANQTQQIANNPFVSQTQPQVMNTPTAHTEPANLNVPEYAAVQHTVNFNPVQDAGVSAQQTGYYSINNHLTPTFTGAGFGGYSVSQDTTAASNQQVSHSQTGSNNPFALHNAATIATGNPAHENVLNNPFSRPNFDEQNTNMPLQQQIISNPFQNQTYNQQQFQQQKMPLSSINSVMTTPTSMQGSMNIPQRFDKMEFQAHYTQNHLQQQQQQQQQQQQQQQQQPQQGYYVPATAGANPVTNITGTVQPQNFPFYPQQQPQPEQSQTQQPVLGNQYANNLNLIDM

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
22	Acetylation	KSAPPKQKYLDPILL CCCCCCCCCCCCEEC	54.64	24489116
135	Ubiquitination	RDGYRTLKLNSGNYG HCCEEEEEECCCCCC	45.04	23749301
138	Phosphorylation	YRTLKLNSGNYGSSR EEEEEECCCCCCCCC	38.56	30377154
274	Ubiquitination	EHLIEDDKTHNTFVP HHHCCCCCCCCEEEE	65.10	23749301
275	Phosphorylation	HLIEDDKTHNTFVPV HHCCCCCCCCEEEEC	27.61	19823750
278	Phosphorylation	EDDKTHNTFVPVDSS CCCCCCCEEEECCCC	20.57	19823750
284	Phosphorylation	NTFVPVDSSQGSAGA CEEEECCCCCCCHHH	25.46	19823750
285	Phosphorylation	TFVPVDSSQGSAGAV EEEECCCCCCCHHHH	33.81	21440633
288	Phosphorylation	PVDSSQGSAGAVVAK ECCCCCCCHHHHEEH	18.85	20377248
295	Ubiquitination	SAGAVVAKSTAQERL CHHHHEEHHHHHHHH	36.41	19722269
324	Phosphorylation	KNEQVAISPALTTVT HCCCCCCCCCCCHHH	8.38	28889911
413	Phosphorylation	AGVSAQQTGYYSINN CCCCCHHHCEEEECC	18.31	28889911
427	Phosphorylation	NHLTPTFTGAGFGGY CCCCCCCCCCCCCCE	28.71	28889911
453	Phosphorylation	QQVSHSQTGSNNPFA CCCCCCCCCCCCCCH	45.66	28889911
530	Phosphorylation	SSINSVMTTPTSMQG HHHCCCCCCCCCCCC	27.71	24961812
531	Phosphorylation	SINSVMTTPTSMQGS HHCCCCCCCCCCCCC	13.38	25752575
533	Phosphorylation	NSVMTTPTSMQGSMN CCCCCCCCCCCCCCC	34.44	21440633
534	Phosphorylation	SVMTTPTSMQGSMNI CCCCCCCCCCCCCCC	15.43	21440633

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

Oops, there are no upstream regulatory protein records of AP18A_YEAST !!

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of AP18A_YEAST !!

Disease-associated PTM Sites based on SAP

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

Oops, there are no SNP-PTM records of AP18A_YEAST !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
SLA2_YEAST	SLA2	genetic	14704157
BMH2_YEAST	BMH2	physical	16554755
PPN1_YEAST	PPN1	physical	16554755
SNU13_YEAST	SNU13	physical	16554755
MDN1_YEAST	MDN1	physical	16554755
AP18A_YEAST	YAP1801	physical	19345193
TPM1_YEAST	TPM1	genetic	23891562
PAN1_YEAST	PAN1	physical	9531549
CLH_YEAST	CHC1	physical	9531549
CLC1_YEAST	CLC1	physical	9531549

Drug and Disease Associations

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

Related Literatures of Post-Translational Modification

Phosphorylation

"A multidimensional chromatography technology for in-depthphosphoproteome analysis.";
Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.;
Mol. Cell. Proteomics 7:1389-1396(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-324, AND MASSSPECTROMETRY.
PubMed: 18407956