AP-2 complex subunit beta (Protein name
), AP2B1_HUMAN from NCBI database.
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General Annotation
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Antigen Annotation
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Gene name:
AP2B1(ADTB2;CLAPB1);
Protein name:
AP-2 complex subunit beta;
Alternative:
Adapter-related protein complex 2 beta subunit;AP105B;Beta-2-adaptin;Adaptor protein complex AP-2 subunit beta;Clathrin assembly protein complex 2 beta large chain;Beta-adaptin;Plasma membrane adaptor HA2/AP2 adaptin beta subunit;
Organism:
Human (Homo sapiens).
General Annotation
Sub Unit:
Adaptor protein complex 2 (AP-2) is an heterotetramer composed of two large adaptins (alpha-type subunit AP2A1 or AP2A2 and beta-type subunit AP2B1), a medium adaptin (mu-type subunit AP2M1) and a small adaptin (sigma-type subunit AP2S1). Interacts with EPN1. Interacts with EPS15; clathrin competes with EPS15. Interacts with SNAP91; clathrin competes with SNAP91. Interacts with CLTC; clathrin competes with EPS15, SNAP91 and PIP5K1C. Interacts with LDLRAP1. Interacts with AMPH and BIN1. Interacts with ARF6 (GDP-bound). Interacts (dephosphorylated at Tyr-737) with ARRB1; phosphorylation of AP2B1 at Tyr-737 disrupts the interaction. Interacts with SLC2A8. Interacts with SCYL1 and SCYL2. Interacts with TGFBR1 and TGFBR2. Interacts with PIP5K1C; clathrin competes with PIP5K1C (By similarity). Interacts with DENND1B, but not with DENND1A, nor DENND1C.
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.
Subcellular Location:
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.
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Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3);ALTERNATIVE SPLICING
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Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2)
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Cited for: INTERACTION WITH ARRB1;MUTAGENESIS OF GLU-849 AND GLU-902
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Cited for: FUNCTION OF THE AP-2 COMPLEX IN CLATHRIN-MEDIATED ENDOCYTOSIS
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Cited for: FUNCTION OF THE AP-2 COMPLEX IN CLATHRIN-MEDIATED ENDOCYTOSIS
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Cited for: INTERACTION WITH LDLRAP1;MUTAGENESIS OF TRP-841 AND TYR-888
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Cited for: PHOSPHORYLATION AT TYR-737;INTERACTION WITH ARRB1
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Cited for: FUNCTION OF THE AP-2 COMPLEX IN NON-CLATHRIN-DEPENDENT ENDOCYTOSIS
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Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]
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Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-265;IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]
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Cited for: INTERACTION WITH DENND1B;MUTAGENESIS OF TRP-841; GLU-849; TYR-888 AND GLU-902
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Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]
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Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT THR-2;IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS];CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS]
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Cited for: X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS) OF 701-937;MUTAGENESIS OF ARG-879; TYR-888 AND LYS-917;INTERACTION WITH EPN1; EPS15; SNAP91 AND CLTC
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Cited for: X-RAY CRYSTALLOGRAPHY (2.59 ANGSTROMS) OF 1-591 IN COMPLEX WITH AP2A2; AP2M1; AP2S1 AND AN INOSITOL POLYPHOSPHATE HEADGROUP
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Cited for: X-RAY CRYSTALLOGRAPHY (1.60 ANGSTROMS) OF 701-937 IN COMPLEX WITH LDLRAP1;INTERACTION WITH ARRB1; EPN1; SNAP91; AMPH AND BIN1;MUTAGENESIS OF TYR-815; TRP-841; GLU-849; TYR-888 AND GLU-902
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Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 700-937 IN COMPLEX WITH EPS15;X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 700-937 IN COMPLEX WITH ARRB1;INTERACTION WITH SCYL1; SCYL2; EPS15; AMPH; SNAP91; ARRB1 AND LDLRAP1;MUTAGENESIS OF TYR-815; TRP-841; LYS-842; GLN-851; ARG-879 AND TYR-888
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Cited for: X-RAY CRYSTALLOGRAPHY (1.60 ANGSTROMS) OF 1-591 IN COMPLEX WITH AP2A2; AP2M1; AP2S1 AND CD4 INTERNALIZATION SIGNAL
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