AP2S1_HUMAN - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: AP2S1_HUMAN
• UniProt AC: P53680
• Protein Name: AP-2 complex subunit sigma
• Gene Name: AP2S1
• Organism: Homo sapiens (Human).
• Sequence Length: 142
• 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 alpha and AP-2 sigma subunits are thought to contribute to the recognition of the [ED]-X-X-X-L-[LI] motif (By similarity). May also play a role in extracellular calcium homeostasis..
• Protein Sequence: MIRFILIQNRAGKTRLAKWYMQFDDDEKQKLIEEVHAVVTVRDAKHTNFVEFRNFKIIYRRYAGLYFCICVDVNDNNLAYLEAIHNFVEVLNEYFHNVCELDLVFNFYKVYTVVDEMFLAGEIRETSQTKVLKQLLMLQSLE

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
18	Ubiquitination	AGKTRLAKWYMQFDD CCCCCHHHHHHCCCH	43.37	21890473
18 (in isoform 2)	Ubiquitination	-	43.37	21890473
18 (in isoform 1)	Ubiquitination	-	43.37	21890473
18	Acetylation	AGKTRLAKWYMQFDD CCCCCHHHHHHCCCH	43.37	26822725
20	Phosphorylation	KTRLAKWYMQFDDDE CCCHHHHHHCCCHHH	4.74	29496907
28	Ubiquitination	MQFDDDEKQKLIEEV HCCCHHHHHHHHHEE	60.78	21890473
28 (in isoform 2)	Ubiquitination	-	60.78	21890473
28 (in isoform 1)	Ubiquitination	-	60.78	21890473
30	Ubiquitination	FDDDEKQKLIEEVHA CCHHHHHHHHHEECE	63.60	-
45	Ubiquitination	VVTVRDAKHTNFVEF EEEEECCCCCCCEEE	56.08	21906983
45	Malonylation	VVTVRDAKHTNFVEF EEEEECCCCCCCEEE	56.08	33225896
45	Acetylation	VVTVRDAKHTNFVEF EEEEECCCCCCCEEE	56.08	26051181
45 (in isoform 1)	Ubiquitination	-	56.08	21890473
56	Ubiquitination	FVEFRNFKIIYRRYA CEEECCCEEEEHHCC	31.57	21890473
56	Acetylation	FVEFRNFKIIYRRYA CEEECCCEEEEHHCC	31.57	26051181
56 (in isoform 1)	Ubiquitination	-	31.57	21890473
92 (in isoform 2)	Ubiquitination	-	47.28	21890473
95 (in isoform 2)	Ubiquitination	-	2.49	21890473
112	Phosphorylation	FNFYKVYTVVDEMFL EEEEEHHHHHHHHHH	19.62	25690035
127	Phosphorylation	AGEIRETSQTKVLKQ HCCCCHHHHHHHHHH	30.97	46165003
129	Phosphorylation	EIRETSQTKVLKQLL CCCHHHHHHHHHHHH	23.92	46165009
130 (in isoform 1)	Ubiquitination	-	37.62	21890473
130	Ubiquitination	IRETSQTKVLKQLLM CCHHHHHHHHHHHHH	37.62	21890473
133 (in isoform 1)	Ubiquitination	-	41.72	21890473
133	Ubiquitination	TSQTKVLKQLLMLQS HHHHHHHHHHHHHHC	41.72	21890473
140	Phosphorylation	KQLLMLQSLE----- HHHHHHHCCC-----	30.42	21082442

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

Oops, there are no upstream regulatory protein records of AP2S1_HUMAN !!

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of AP2S1_HUMAN !!

Disease-associated PTM Sites based on SAP

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

Oops, there are no SNP-PTM records of AP2S1_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
KHK_HUMAN	KHK	physical	17353931
DPOLQ_HUMAN	POLQ	physical	17353931
TDGF1_HUMAN	TDGF1	physical	21988832
AAGAB_HUMAN	AAGAB	physical	25416956
AP2A1_HUMAN	AP2A1	physical	26344197
AP2A2_HUMAN	AP2A2	physical	26344197
AP2M1_HUMAN	AP2M1	physical	26344197
AP2M1_HUMAN	AP2M1	physical	28514442
CCD32_HUMAN	C15orf57	physical	28514442
AAK1_HUMAN	AAK1	physical	28514442
AAGAB_HUMAN	AAGAB	physical	28514442
STON2_HUMAN	STON2	physical	28514442
ITSN1_HUMAN	ITSN1	physical	28514442
EPS15_HUMAN	EPS15	physical	28514442
FCHO2_HUMAN	FCHO2	physical	28514442
NECP2_HUMAN	NECAP2	physical	28514442
BMP2K_HUMAN	BMP2K	physical	28514442
AP2A1_HUMAN	AP2A1	physical	28514442
AP2A2_HUMAN	AP2A2	physical	28514442
EP15R_HUMAN	EPS15L1	physical	28514442
REPS1_HUMAN	REPS1	physical	28514442
AP1B1_HUMAN	AP1B1	physical	28514442
RBP1_HUMAN	RALBP1	physical	28514442
AP2B1_HUMAN	AP2B1	physical	28514442
ITSN2_HUMAN	ITSN2	physical	28514442
UBB_HUMAN	UBB	physical	28514442
IKIP_HUMAN	IKBIP	physical	28514442

Drug and Disease Associations

• Kegg Disease
• There are no disease associations of PTM sites.
• OMIM Disease
• 600740: Hypocalciuric hypercalcemia, familial 3 (HHC3)
• Kegg Drug
• There are no disease associations of PTM sites.
• DrugBank
• There are no disease associations of PTM sites.

Related Literatures of Post-Translational Modification

Phosphorylation

"Kinase-selective enrichment enables quantitative phosphoproteomics ofthe kinome across the cell cycle.";
Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,Greff Z., Keri G., Stemmann O., Mann M.;
Mol. Cell 31:438-448(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-140, AND MASSSPECTROMETRY.
PubMed: 18691976