Basic Information | Overview of PTM Sites | Experimental PTM Sites | Protein-Protein Interactions | Drug and Disease Associations | Related Literatures
Basic Information
Protein Name :  AP-2 complex subunit beta  

UniProtKB / Swiss-Prot ID :  AP2B1_HUMAN

Gene Name (Synonyms) : 
AP2B1, ADTB2, CLAPB1  

Species :  Homo sapiens (Human). 

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. 

Protein 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 surrrounded 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 beta subunit acts via its C-terminal appendage domain as a scaffolding platform for endocytic accessory proteins; at least some clathrin- associated sorting proteins (CLASPs) are recognized by their [DE]- X(1,2)-F-X-X-[FL]-X-X-X-R motif. The AP-2 beta subunit binds to clathrin heavy chain, promoting clathrin lattice assembly; clathrin displaces at least some CLASPs from AP2B1 which probably then can be positioned for further coat assembly. 

Protein Sequence MTDSKYFTTNKKGEIFELKAELNNEKKEKRKEAVKKVIAAMTVGKDVSSLFPDVVNCMQTDNLELKKLVY...
Predicted Secondary Structure CCCCCHHHHHCCCHHHHHHHHHCCCCHHHHHHHHHHHHHHHHCCCCCHHHHHHHHHHHCCCCHHHHHHHH...
Protein Variant -
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Overview of Protein Modification Sites with Functional and Structural Information
Accessible Surface Area (ASA)
Pred. Secondary
Real Secondary
Disorder Prediction
Protein Domain
&
Experimental PTM Sites
Predicted PTM Sites
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Experimental Post-Translational Modification Sites Download
Locations
Modification
Substrate Sites
&
Secondary Structure
Accessible Surface Area (%)
Resource
Reference
Structural Characterization
Orthologous
Protein Cluster
2Phosphothreonine---MTDSKY
---CCCCCH
49.32HPRD
Link-
2Phosphothreonine---MTDSKY
---CCCCCH
49.32Phosphositeplus
Link-
2Phosphothreonine.---MTDSKY
---CCCCCH
49.32UniProtKB
Link-
4Phosphoserine-MTDSKYFT
-CCCCCHHH
21.79HPRD
Link-
4Phosphoserine-MTDSKYFT
-CCCCCHHH
21.79Phosphositeplus
Link-
4Phosphoserine.-MTDSKYFT
-CCCCCHHH
21.79UniProtKB
Link-
6PhosphotyrosineTDSKYFTTN
CCCCHHHHH
15.31HPRD
Link-
6PhosphotyrosineTDSKYFTTN
CCCCHHHHH
15.31PhosphoELM
Link-
6PhosphotyrosineTDSKYFTTN
CCCCHHHHH
15.31Phosphositeplus
Link-
19N6-acetyllysineIFELKAELN
HHHHHHHHC
32.39Phosphositeplus
Link-
26N6-acetyllysineLNNEKKEKR
HCCCCHHHH
69.25Phosphositeplus
Link-
79PhosphoserineNYAKSQPDM
HHCCCCHHH
38.48HPRD
Link-
136PhosphotyrosineDEDPYVRKT
CCCHHHHHH
25.80Phosphositeplus
Link-
265N6-acetyllysineKVLMKFLEL
HHHHHHHCC
42.51HPRD
Link-
265N6-acetyllysineKVLMKFLEL
HHHHHHHCC
42.51Phosphositeplus
Link-
265N6-acetyllysine.KVLMKFLEL
HHHHHHHCC
42.51UniProtKB
Link-
272Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)ELLPKDSDY
CCCCCCHHH
70.59Phosphositeplus
Link-
276PhosphotyrosineKDSDYYNML
CCHHHHHHH
10.74Phosphositeplus
Link-
276Phosphotyrosine.KDSDYYNML
CCHHHHHHH
10.74UniProtKB
Link-
277PhosphotyrosineDSDYYNMLL
CHHHHHHHH
10.09Phosphositeplus
Link-
318N6-acetyllysinePEILKQEIK
CHHHHHCCC
52.09HPRD
Link-
318N6-acetyllysinePEILKQEIK
CHHHHHCCC
52.09Phosphositeplus
Link-
318N6-acetyllysine.PEILKQEIK
CHHHHHCCC
52.09UniProtKB
Link-
361PhosphotyrosineELKEYATEV
HHHHHHHCC
19.75HPRD
Link-
497PhosphoserineLKKPSETQE
CCCCHHHHH
63.25HPRD
Link-
538Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)PVTAKEVVL
HHHHHHHHC
41.50Phosphositeplus
Link-
680PhosphoserineTFAPSPTPA
CCCCCCCCC
37.67HPRD
Link-
680PhosphoserineTFAPSPTPA
CCCCCCCCC
37.67Phosphositeplus
Link-
737PhosphotyrosineQGHIYMEMN
CCCEEEEEE
4.95HPRD
Link
737PhosphotyrosineQGHIYMEMN
CCCEEEEEE
4.95HPRD
Link
737PhosphotyrosineQGHIYMEMN
CCCEEEEEE
4.95PhosphoELM
Link
737PhosphotyrosineQGHIYMEMN
CCCEEEEEE
4.95Phosphositeplus
Link
737Phosphotyrosine; by SRC.QGHIYMEMN
CCCEEEEEE
4.95UniProtKB
Link
878Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)YTIAKRNVE
EEEEECCCC
40.43Phosphositeplus
Link
888PhosphotyrosineQDMLYQSLK
HHHHHHHHH
6.87PhosphoELM
Link
888PhosphotyrosineQDMLYQSLK
HHHHHHHHH
6.87Phosphositeplus
Link
888Phosphotyrosine.QDMLYQSLK
HHHHHHHHH
6.87UniProtKB
Link
917Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)TLSLKCRAP
EEEEEECCC
20.49Phosphositeplus
Link
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Protein-Protein Interactions
      Interacting Protein      
Interaction type
Source ID
      Resource      
      Pubmed ID      
Domain-Domain Interactions
MLH1_HUMANphysical interactionMINT-66474MINT16189514
MEA1_HUMANphysical interactionMINT-66587MINT16189514
K0408_HUMANphysical interactionMINT-66266MINT16189514
Q9H7R8_HUMANphysical interactionMINT-67135MINT16189514
TE2IP_HUMANphysical interactionMINT-67704MINT16189514
GCP4_HUMANphysical interactionMINT-66991MINT16189514
PO121_HUMANphysical interactionMINT-67325MINT16189514
AP1M2_HUMANphysical interactionMINT-68428MINT16189514
BUB1B_HUMANphysical interaction
physical interaction
physical interaction
DIP:40090EDIP12419313
12419313
12419313
BUB1_HUMANphysical interactionDIP:40092EDIP12419313
NUP54_HUMANphysical interactionEBI-757762
intact16189514
Q9BVR6_HUMANphysical interactionEBI-755599
intact16189514
DHX58_HUMANphysical interactionEBI-753868
intact16189514
MLH1_HUMANphysical interactionEBI-753892
intact16189514
AP1M1_HUMANphysical interaction
physical interaction
EBI-753982
EBI-540750
intact16189514
9341158
TE2IP_HUMANphysical interactionEBI-757942
intact16189514
ARH_HUMANphysical interactionEBI-756082
intact16189514
THAP1_HUMANphysical interactionEBI-756658
intact16189514
Q96HA1_HUMANphysical interactionEBI-756691
intact16189514
NECP2_HUMANphysical interactionEBI-757093
intact16189514
MEA1_HUMANphysical interaction
physical interaction
EBI-754261
EBI-760798
intact16189514
16189514
VATG1_HUMANphysical interactionEBI-757510
intact16189514
AP2M1_HUMANphysical interactionEBI-760465
intact16189514
FA46C_HUMANphysical interactionEBI-759334
intact16189514
RIBC2_HUMANphysical interactionEBI-760183
intact16189514
AP1M2_HUMANphysical interactionEBI-760285
intact16189514
NECP2_HUMANyeast 2-hybridHPRD:03015HPRD16189514
PO121_HUMANyeast 2-hybridHPRD:03015HPRD16189514
RIBC2_HUMANyeast 2-hybridHPRD:03015HPRD16189514
DHX58_HUMANyeast 2-hybridHPRD:03015HPRD16189514
FA46C_HUMANyeast 2-hybridHPRD:03015HPRD16189514
THAP1_HUMANyeast 2-hybridHPRD:03015HPRD16189514
K0408_HUMANyeast 2-hybridHPRD:03015HPRD16189514
AP1M1_HUMANyeast 2-hybridHPRD:03015HPRD16189514
TE2IP_HUMANyeast 2-hybridHPRD:03015HPRD16189514
ARH_HUMANyeast 2-hybridHPRD:03015HPRD16189514
NUP54_HUMANyeast 2-hybridHPRD:03015HPRD16189514
VATG1_HUMANyeast 2-hybridHPRD:03015HPRD16189514
ARRB1_HUMANin vitro
yeast 2-hybrid
HPRD:03015HPRD11777907
TGFR1_HUMANin vitro
in vivo
yeast 2-hybrid
HPRD:03015HPRD12429842
SMAD4_HUMANin vivoHPRD:03015HPRD15761153
SMUF1_HUMANin vivoHPRD:03015HPRD15761153
AP2M1_HUMANin vitroHPRD:03015HPRD12086608
BUB1_HUMANyeast 2-hybridHPRD:03015HPRD12419313
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Disease Reference
Kegg disease
There are no disease associations of PTM sites.
Drug Reference
There are no disease associations of PTM sites.
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Related Literatures of Post-Translational Modification
Acetylation
ReferencePubMed
"Lysine acetylation targets protein complexes and co-regulates majorcellular functions.";
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.,Olsen J.V., Mann M.;
Science 325:834-840(2009).
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-265 AND LYS-318, AND MASSSPECTROMETRY.
Phosphorylation
ReferencePubMed
"Immunoaffinity profiling of tyrosine phosphorylation in cancercells.";
Rush J., Moritz A., Lee K.A., Guo A., Goss V.L., Spek E.J., Zhang H.,Zha X.-M., Polakiewicz R.D., Comb M.J.;
Nat. Biotechnol. 23:94-101(2005).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-737, AND MASSSPECTROMETRY.
"Global survey of phosphotyrosine signaling identifies oncogenickinases in lung cancer.";
Rikova K., Guo A., Zeng Q., Possemato A., Yu J., Haack H., Nardone J.,Lee K., Reeves C., Li Y., Hu Y., Tan Z., Stokes M., Sullivan L.,Mitchell J., Wetzel R., Macneill J., Ren J.M., Yuan J.,Bakalarski C.E., Villen J., Kornhauser J.M., Smith B., Li D., Zhou X.,Gygi S.P., Gu T.-L., Polakiewicz R.D., Rush J., Comb M.J.;
Cell 131:1190-1203(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-737 AND TYR-888, ANDMASS SPECTROMETRY.
"Src-dependent phosphorylation of beta2-adaptin dissociates the beta-arrestin-AP-2 complex.";
Fessart D., Simaan M., Zimmerman B., Comeau J., Hamdan F.F.,Wiseman P.W., Bouvier M., Laporte S.A.;
J. Cell Sci. 120:1723-1732(2007).
Cited for: PHOSPHORYLATION AT TYR-737, AND INTERACTION WITH ARRB1.
"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 THR-2 AND SER-4, AND MASSSPECTROMETRY.
"c-Src-mediated phosphorylation of AP-2 reveals a general mechanismfor receptors internalizing through the clathrin pathway.";
Zimmerman B., Simaan M., Lee M.-H., Luttrell L.M., Laporte S.A.;
Cell. Signal. 21:103-110(2009).
Cited for: PHOSPHORYLATION AT TYR-737.
"An extensive survey of tyrosine phosphorylation revealing new sitesin human mammary epithelial cells.";
Heibeck T.H., Ding S.-J., Opresko L.K., Zhao R., Schepmoes A.A.,Yang F., Tolmachev A.V., Monroe M.E., Camp D.G. II, Smith R.D.,Wiley H.S., Qian W.-J.;
J. Proteome Res. 8:3852-3861(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-276, AND MASSSPECTROMETRY.
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Basic Information | Overview of PTM Sites | Experimental PTM Sites | Protein-Protein Interactions | Drug and Disease Associations | Related Literatures