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IID50122
UniprotP84092
ProteinAP-2 complex subunit mu
GeneAp2m1
OrganismRattus norvegicus
Sequence LLPS PhaSepDB
PhaSePro
LLPSDB
DrLLPS
Network xml rdf
Structure
Experiment
  :order   disorder   conflict   PDB cluster   ProS   Pfam Domain   SEG
435
 order/disorder by at least rule
     disorder by at least rule
     order by at least rule
 order/disorder by majority rule
Seq 1-435 Hetero dimer : IID00615Complex
 Evidence X-RAY 5fpi A Reference
       Region 5fpi A 1-158 disorder
       Region 5fpi A 159-221 order
       Region 5fpi A 222-237 disorder
       Region 5fpi A 238-256 order
       Region 5fpi A 257-259 disorder
       Region 5fpi A 260-435 order
 Evidence X-RAY 5c7z A Reference
       Region 5c7z A 159-221 order
       Region 5c7z A 222-237 disorder
       Region 5c7z A 238-256 order
       Region 5c7z A 257-259 disorder
       Region 5c7z A 260-435 order
Seq 1-435 Hetero tetramer : IID50124Complex,IID50129Complex,P63010
 Evidence X-RAY 2vgl M Reference
       Region 2vgl M 1-141 order
       Region 2vgl M 142-158 disorder
       Region 2vgl M 159-222 order
       Region 2vgl M 223-239 disorder
       Region 2vgl M 240-255 order
       Region 2vgl M 256-260 disorder
       Region 2vgl M 261-435 order
 Evidence X-RAY 4uqi M Reference
       Region 4uqi M 1-141 order
       Region 4uqi M 142-158 disorder
       Region 4uqi M 159-222 order
       Region 4uqi M 223-239 disorder
       Region 4uqi M 240-255 order
       Region 4uqi M 256-260 disorder
       Region 4uqi M 261-435 order
Seq 1-435 Hetero pentamer : IID50124Complex,P17427,P63010
 Evidence X-RAY 2jkt U Reference
       Region 2jkt U 1-141 order
       Region 2jkt U 142-158 disorder
       Region 2jkt U 159-222 order
       Region 2jkt U 223-231 disorder
       Region 2jkt U 232-435 order
 Evidence X-RAY 2jkt M Reference
       Region 2jkt M 1-141 order
       Region 2jkt M 142-158 disorder
       Region 2jkt M 159-222 order
       Region 2jkt M 223-231 disorder
       Region 2jkt M 232-435 order
 Evidence X-RAY 2jkr U Reference
       Region 2jkr U 1-141 order
       Region 2jkr U 142-158 disorder
       Region 2jkr U 159-222 order
       Region 2jkr U 223-231 disorder
       Region 2jkr U 232-435 order
 Evidence X-RAY 2jkr M Reference
       Region 2jkr M 1-141 order
       Region 2jkr M 142-158 disorder
       Region 2jkr M 159-222 order
       Region 2jkr M 223-231 disorder
       Region 2jkr M 232-435 order
Seq 1-435 Hetero pentamer : IID50129Complex,P63010
 Evidence X-RAY 2xa7 M Reference
       Region 2xa7 M 1-135 order
       Region 2xa7 M 136-141 disorder
       Region 2xa7 M 142-223 order
       Region 2xa7 M 224-235 disorder
       Region 2xa7 M 236-435 order
Seq 1-435 Hetero tetramer : IID50129Complex,P63010
 Evidence X-RAY 2xa7 M Reference
       Region 2xa7 M 1-135 order
       Region 2xa7 M 136-141 disorder
       Region 2xa7 M 142-223 order
       Region 2xa7 M 224-235 disorder
       Region 2xa7 M 236-435 order
Seq 1-435 Hetero dimer : IID50123Complex
 Evidence X-RAY 2bp5 M Reference
       Region 2bp5 M 1-158 disorder
       Region 2bp5 M 159-219 order
       Region 2bp5 M 220-239 disorder
       Region 2bp5 M 240-255 order
       Region 2bp5 M 256-259 disorder
       Region 2bp5 M 260-435 order
Seq 122-435 Hetero dimer : A8IP97
 Evidence X-RAY 1i31 A Reference
       Region 1i31 A 122-158 disorder
       Region 1i31 A 159-220 order
       Region 1i31 A 221-237 disorder
       Region 1i31 A 238-255 order
       Region 1i31 A 256-259 disorder
       Region 1i31 A 260-435 order
 Evidence X-RAY 1bw8 A Reference
       Region 1bw8 A 122-158 disorder
       Region 1bw8 A 159-220 order
       Region 1bw8 A 221-237 disorder
       Region 1bw8 A 238-255 order
       Region 1bw8 A 256-259 disorder
       Region 1bw8 A 260-435 order
Seq 158-435 Hetero dimer :
 Evidence X-RAY 1bxx A Reference
       Region 1bxx A 158-158 disorder
       Region 1bxx A 159-220 order
       Region 1bxx A 221-237 disorder
       Region 1bxx A 238-255 order
       Region 1bxx A 256-259 disorder
       Region 1bxx A 260-435 order
Seq 158-435 Hetero dimer : P35570
 Evidence X-RAY 5wrl A Reference
       Region 5wrl A 158-158 disorder
       Region 5wrl A 159-219 order
       Region 5wrl A 220-237 disorder
       Region 5wrl A 238-435 order
Seq 158-435 Hetero dimer : P35570
 Evidence X-RAY 5wrk A Reference
       Region 5wrk A 158-158 disorder
       Region 5wrk A 159-435 order
Seq 158-435 Hetero dimer : IID00359Complex
 Evidence X-RAY 3h85 A Reference
       Region 3h85 A 158-158 disorder
       Region 3h85 A 159-220 order
       Region 3h85 A 221-239 disorder
       Region 3h85 A 240-255 order
       Region 3h85 A 256-260 disorder
       Region 3h85 A 261-435 order
Seq 158-435 Hetero dimer : IID50125Complex
 Evidence X-RAY 2pr9 A Reference
       Region 2pr9 A 158-158 disorder
       Region 2pr9 A 159-219 order
       Region 2pr9 A 220-237 disorder
       Region 2pr9 A 238-255 order
       Region 2pr9 A 256-260 disorder
       Region 2pr9 A 261-435 order
Seq 158-435 Hetero dimer : IID00353Complex
 Evidence X-RAY 1hes A Reference
       Region 1hes A 158-158 disorder
       Region 1hes A 159-220 order
       Region 1hes A 221-237 disorder
       Region 1hes A 238-255 order
       Region 1hes A 256-259 disorder
       Region 1hes A 260-435 order
Seq 158-435 Hetero dimer : P35570
 Evidence X-RAY 5wrm A Reference
       Region 5wrm A 158-158 disorder
       Region 5wrm A 159-219 order
       Region 5wrm A 220-237 disorder
       Region 5wrm A 238-435 order
Seq 170-435 Monomer : IID50127Complex
 Evidence X-RAY 3ml6 B Reference
       Region 3ml6 B 170-217 order
       Region 3ml6 B 218-244 disorder
       Region 3ml6 B 245-255 order
       Region 3ml6 B 256-260 disorder
       Region 3ml6 B 261-435 order
Seq 170-435 Monomer : IID50127Complex
 Evidence X-RAY 3ml6 C Reference
       Region 3ml6 C 170-217 order
       Region 3ml6 C 218-240 disorder
       Region 3ml6 C 241-435 order
Seq 170-435 Monomer : IID50127Complex
 Evidence X-RAY 3ml6 F Reference
       Region 3ml6 F 170-218 order
       Region 3ml6 F 219-244 disorder
       Region 3ml6 F 245-255 order
       Region 3ml6 F 256-260 disorder
       Region 3ml6 F 261-435 order
Seq 170-435 Monomer : IID50127Complex
 Evidence X-RAY 3ml6 D Reference
       Region 3ml6 D 170-217 order
       Region 3ml6 D 218-244 disorder
       Region 3ml6 D 245-255 order
       Region 3ml6 D 256-260 disorder
       Region 3ml6 D 261-375 order
       Region 3ml6 D 376-380 disorder
       Region 3ml6 D 381-435 order
Seq 170-435 Monomer : IID50127Complex
 Evidence X-RAY 3ml6 E Reference
       Region 3ml6 E 170-218 order
       Region 3ml6 E 219-244 disorder
       Region 3ml6 E 245-255 order
       Region 3ml6 E 256-259 disorder
       Region 3ml6 E 260-376 order
       Region 3ml6 E 377-379 disorder
       Region 3ml6 E 380-435 order
Seq 170-435 Monomer : IID50127Complex
 Evidence X-RAY 3ml6 A Reference
       Region 3ml6 A 170-218 order
       Region 3ml6 A 219-240 disorder
       Region 3ml6 A 241-435 order
Seqphosphorylation
    156-156 Phosphothreonine
    45-45 Phosphoserine
 
Prediction
NeProc
Disorder 141-166,228-234
Order 1-140,167-227,236-435
ProS 158-166
AlphaFold
Disorder 136-143,225-239
Order 1-135,144-224,240-435
Pfam Hmmer
PF00928 159-435 3.1e-131
Function
Function in SwissProt
Component of the adaptor protein complex 2 (AP-2) (PubMed:14745134, PubMed:15473838). Adaptor protein complexes function in protein transport via transport vesicles in different membrane traffic pathways (PubMed:14745134, PubMed:15473838). Adaptor protein complexes are vesicle coat components and appear to be involved in cargo selection and vesicle formation (PubMed:14745134, PubMed:15473838). 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 (PubMed:14745134, PubMed:15473838). The clathrin lattice serves as a mechanical scaffold but is itself unable to bind directly to membrane components (PubMed:14745134, PubMed:15473838). 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 (PubMed:14745134, PubMed:15473838). AP-2 also serves as a cargo receptor to selectively sort the membrane proteins involved in receptor-mediated endocytosis (PubMed:14745134, PubMed:15473838). AP-2 seems to play a role in the recycling of synaptic vesicle membranes from the presynaptic surface (By similarity). 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 (PubMed:15985462). AP-2 may also play a role in maintaining normal post-endocytic trafficking through the ARF6-regulated, non-clathrin pathway (By similarity). During long-term potentiation in hippocampal neurons, AP-2 is responsible for the endocytosis of ADAM10 (By similarity). The AP-2 mu (AP2M1) subunit binds to transmembrane cargo proteins; it recognizes the Y-X-X-Phi motifs (PubMed:15985462). 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 Thr-156 in membrane-associated AP-2 (PubMed:15985462, PubMed:11516654). 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 (PubMed:20947020).
Biological Process
See also
Diagram with PDB data
ITGA4/Ap2m1Mu2 adaptin subunit of the AP2 adaptor (C-terminal domain) complexed with Integrin alpha4 internalisation peptide QYKSILQE