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Sep. 10, 2014:
A total of 174 experimentally verified S-nitrosylation sites on 94 S-nitrosylated proteins from individualized human colorectal cancer tissues using a label-free quantitation strategy.

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Protein Name: AP-2 complex subunit mu

UniprotKB/SwissProt ID: AP2M1_HUMAN (Q96CW1)

Gene Name: AP2M1

Synonyms: CLAPM1, KIAA0109

Organism: Homo sapiens (Human).

Function: 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 mu subunit binds to transmembrane cargo proteins; it recognizes the Y-X-X-Phi motifs. The surface region interacting with to the Y-X- X-Phi motif is inaccessible in cytosolic AP-2, but becomes accessible through a conformational change following phosphorylation of AP-2 mu subunit at 'Tyr-156' in membrane- associated AP-2. The membrane-specific phosphorylation event appears to involve assembled clathrin which activates the AP-2 mu kinase AAK1 (By similarity). Plays a role in endocytosis of frizzled family members upon Wnt signaling (By similarity).

Other Modifications: View all modification sites in dbPTM

Protein Subcellular Localization: Cell membrane. Membrane, coated pit; Peripheral membrane protein; Cytoplasmic side. Note=AP-2 appears to be excluded from internalizing CCVs and to disengage from sites of endocytosis seconds before internalization of the nascent CCV (By similarity).

PDB :
( If your security settings prevent Jmol from running, please register http://140.138.144.145/ as a safe location in your Java settings. )

Protein disease:
Disease database Database Entry Disease information
OMIM601024ADAPTOR-RELATED PROTEIN COMPLEX 2, MU-1 SUBUNIT; AP2M1 ;;CLATHRIN-ASSOCIATED/ASSEMBLY/ADAPTO
Network with metabolic pathway:
Kegg map ID Pathway Link
map04721Synaptic vesicle cycle
map04961Endocrine and other factor-regulated calcium reabsorption
map05016Huntington's disease
map04144Endocytosis
Graphical Visualization of S-nitrosylation Sites:
Overview of Protein S-nitrosylation Sites with Functional and Structural Information
InterPro ID Domain
IPR001392
IPR008968
IPR011012
IPR015629

The S-nitrosylation sites of AP2M1_HUMAN

No. Position S-nitrosylated Peptide Secondary Structure of S-nitrosylated Peptide Solvent Accessibility of nitrosylated Site Substrate Motifs PubMed ID Experiment
1212MKSYLSGMPE C KFGMNDKIVI EEEEECCCCE E EEEECCEEEE 3.49%HC102212679
(Cys210)
in vitro