CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-001658
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 AP-2 complex subunit alpha-1 
Protein Synonyms/Alias
 100 kDa coated vesicle protein A; Adapter-related protein complex 2 alpha-1 subunit; Adaptor protein complex AP-2 subunit alpha-1; Alpha-adaptin A; Alpha1-adaptin; Clathrin assembly protein complex 2 alpha-A large chain; Plasma membrane adaptor HA2/AP2 adaptin alpha A subunit 
Gene Name
 AP2A1 
Gene Synonyms/Alias
 ADTAA; CLAPA1 
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
6**MPAVSKGDGMRGLubiquitination[1]
35AEIKRINKELANIRSubiquitination[1]
117RLINNAIKNDLASRNubiquitination[2]
165GDSMDSVKQSAALCLubiquitination[3]
177LCLLRLYKASPDLVPacetylation[3, 4]
378DTVINALKTERDVSVubiquitination[1]
810TQLAVQTKRVAAQVDubiquitination[1]
856APQALTLKLPVTINKubiquitination[1]
880QDFFQRWKQLSLPQQubiquitination[1, 2, 5]
891LPQQEAQKIFKANHPubiquitination[2, 5]
894QEAQKIFKANHPMDAubiquitination[1]
905PMDAEVTKAKLLGFGubiquitination[1]
907DAEVTKAKLLGFGSAubiquitination[6]
Reference
 [1] Refined preparation and use of anti-diglycine remnant (K-ε-GG) antibody enables routine quantification of 10,000s of ubiquitination sites in single proteomics experiments.
 Udeshi ND, Svinkina T, Mertins P, Kuhn E, Mani DR, Qiao JW, Carr SA.
 Mol Cell Proteomics. 2013 Mar;12(3):825-31. [PMID: 23266961]
 [2] hCKSAAP_UbSite: improved prediction of human ubiquitination sites by exploiting amino acid pattern and properties.
 Chen Z, Zhou Y, Song J, Zhang Z.
 Biochim Biophys Acta. 2013 Aug;1834(8):1461-7. [PMID: 23603789]
 [3] Integrated proteomic analysis of post-translational modifications by serial enrichment.
 Mertins P, Qiao JW, Patel J, Udeshi ND, Clauser KR, Mani DR, Burgess MW, Gillette MA, Jaffe JD, Carr SA.
 Nat Methods. 2013 Jul;10(7):634-7. [PMID: 23749302]
 [4] Proteomic investigations of lysine acetylation identify diverse substrates of mitochondrial deacetylase sirt3.
 Sol EM, Wagner SA, Weinert BT, Kumar A, Kim HS, Deng CX, Choudhary C.
 PLoS One. 2012;7(12):e50545. [PMID: 23236377]
 [5] A proteome-wide, quantitative survey of in vivo ubiquitylation sites reveals widespread regulatory roles.
 Wagner SA, Beli P, Weinert BT, Nielsen ML, Cox J, Mann M, Choudhary C.
 Mol Cell Proteomics. 2011 Oct;10(10):M111.013284. [PMID: 21890473]
 [6] Systematic and quantitative assessment of the ubiquitin-modified proteome.
 Kim W, Bennett EJ, Huttlin EL, Guo A, Li J, Possemato A, Sowa ME, Rad R, Rush J, Comb MJ, Harper JW, Gygi SP.
 Mol Cell. 2011 Oct 21;44(2):325-40. [PMID: 21906983] 
Functional 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 subunit binds polyphosphoinositide-containing lipids, positioning AP-2 on the membrane. The AP-2 alpha subunit acts via its C- terminal appendage domain as a scaffolding platform for endocytic accessory proteins. 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). 
Sequence Annotation
 MOD_RES 626 626 Phosphoserine.
 MOD_RES 650 650 Phosphothreonine (By similarity).
 MOD_RES 652 652 Phosphoserine.
 MOD_RES 653 653 Phosphothreonine.
 MOD_RES 655 655 Phosphoserine.  
Keyword
 Alternative splicing; Cell membrane; Coated pit; Complete proteome; Endocytosis; Membrane; Phosphoprotein; Polymorphism; Protein transport; Reference proteome; Transport. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 977 AA 
Protein Sequence
MPAVSKGDGM RGLAVFISDI RNCKSKEAEI KRINKELANI RSKFKGDKAL DGYSKKKYVC 60
KLLFIFLLGH DIDFGHMEAV NLLSSNKYTE KQIGYLFISV LVNSNSELIR LINNAIKNDL 120
ASRNPTFMCL ALHCIANVGS REMGEAFAAD IPRILVAGDS MDSVKQSAAL CLLRLYKASP 180
DLVPMGEWTA RVVHLLNDQH MGVVTAAVSL ITCLCKKNPD DFKTCVSLAV SRLSRIVSSA 240
STDLQDYTYY FVPAPWLSVK LLRLLQCYPP PEDAAVKGRL VECLETVLNK AQEPPKSKKV 300
QHSNAKNAIL FETISLIIHY DSEPNLLVRA CNQLGQFLQH RETNLRYLAL ESMCTLASSE 360
FSHEAVKTHI DTVINALKTE RDVSVRQRAA DLLYAMCDRS NAKQIVSEML RYLETADYAI 420
REEIVLKVAI LAEKYAVDYS WYVDTILNLI RIAGDYVSEE VWYRVLQIVT NRDDVQGYAA 480
KTVFEALQAP ACHENMVKVG GYILGEFGNL IAGDPRSSPP VQFSLLHSKF HLCSVATRAL 540
LLSTYIKFIN LFPETKATIQ GVLRAGSQLR NADVELQQRA VEYLTLSSVA STDVLATVLE 600
EMPPFPERES SILAKLKRKK GPGAGSALDD GRRDPSSNDI NGGMEPTPST VSTPSPSADL 660
LGLRAAPPPA APPASAGAGN LLVDVFDGPA AQPSLGPTPE EAFLSELEPP APESPMALLA 720
DPAPAADPGP EDIGPPIPEA DELLNKFVCK NNGVLFENQL LQIGVKSEFR QNLGRMYLFY 780
GNKTSVQFQN FSPTVVHPGD LQTQLAVQTK RVAAQVDGGA QVQQVLNIEC LRDFLTPPLL 840
SVRFRYGGAP QALTLKLPVT INKFFQPTEM AAQDFFQRWK QLSLPQQEAQ KIFKANHPMD 900
AEVTKAKLLG FGSALLDNVD PNPENFVGAG IIQTKALQVG CLLRLEPNAQ AQMYRLTLRT 960
SKEPVSRHLC ELLAQQF 977 
Gene Ontology
 GO:0030122; C:AP-2 adaptor complex; NAS:UniProtKB.
 GO:0016324; C:apical plasma membrane; IEA:Compara.
 GO:0016323; C:basolateral plasma membrane; IEA:Compara.
 GO:0030130; C:clathrin coat of trans-Golgi network vesicle; NAS:UniProtKB.
 GO:0005829; C:cytosol; TAS:Reactome.
 GO:0008565; F:protein transporter activity; IEA:InterPro.
 GO:0019886; P:antigen processing and presentation of exogenous peptide antigen via MHC class II; TAS:Reactome.
 GO:0007411; P:axon guidance; TAS:Reactome.
 GO:0006897; P:endocytosis; NAS:UniProtKB.
 GO:0007173; P:epidermal growth factor receptor signaling pathway; TAS:Reactome.
 GO:0006895; P:Golgi to endosome transport; NAS:UniProtKB.
 GO:0006886; P:intracellular protein transport; NAS:UniProtKB.
 GO:0042059; P:negative regulation of epidermal growth factor receptor signaling pathway; TAS:Reactome.
 GO:0048011; P:neurotrophin TRK receptor signaling pathway; TAS:Reactome.
 GO:0050690; P:regulation of defense response to virus by virus; TAS:Reactome.
 GO:0007268; P:synaptic transmission; TAS:Reactome.
 GO:0016032; P:viral reproduction; TAS:Reactome. 
Interpro
 IPR017104; AP2_complex_asu.
 IPR011989; ARM-like.
 IPR016024; ARM-type_fold.
 IPR002553; Clathrin/coatomer_adapt-like_N.
 IPR013038; Clathrin_a-adaptin_app_Ig-like.
 IPR003164; Clathrin_a-adaptin_app_sub_C.
 IPR008152; Clathrin_a/b/g-adaptin_app_Ig.
 IPR015873; Clathrin_a/coatomer_app_sub_C.
 IPR009028; Coatomer/calthrin_app_sub_C.
 IPR013041; Coatomer/clathrin_app_Ig-like. 
Pfam
 PF01602; Adaptin_N
 PF02296; Alpha_adaptin_C
 PF02883; Alpha_adaptinC2 
SMART
 SM00809; Alpha_adaptinC2 
PROSITE
  
PRINTS