P27351 · AP2B_YEAST
- ProteinAP-2 complex subunit beta
- GeneAPL1
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids700 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Adaptins are components of the adaptor complexes which link clathrin to receptors in coated vesicles. Clathrin-associated protein complexes are believed to interact with the cytoplasmic tails of membrane proteins, leading to their selection and concentration. Beta adaptin is a subunit of the plasma membrane adaptor.
Miscellaneous
Present with 1670 molecules/cell in log phase SD medium.
GO annotations
all annotations | all molecular function | virus receptor activity | dna binding | rna binding | cytoskeletal motor activity | catalytic activity | gtpase activity | structural molecule activity | transporter activity | cytoskeletal protein binding | lipid binding | cyclase activity | antioxidant activity | oxidoreductase activity | transferase activity | hydrolase activity | lyase activity | isomerase activity | ligase activity | protein tag activity | cargo receptor activity | histone binding | protein folding chaperone | translation regulator activity | nutrient reservoir activity | receptor ligand activity | molecular transducer activity | molecular adaptor activity | toxin activity | cell adhesion mediator activity | molecular function regulator activity | virus coreceptor activity | catalytic activity, acting on a protein | catalytic activity, acting on dna | catalytic activity, acting on rna | molecular carrier activity | transcription regulator activity | general transcription initiation factor activity | molecular sensor activity | molecular sequestering activity | atp-dependent activity | other molecular function | all biological process | mitotic cell cycle | cytokinesis | cytoplasmic translation | immune system process | muscle system process | circulatory system process | renal system process | respiratory system process | carbohydrate metabolic process | generation of precursor metabolites and energy | dna replication | dna repair | dna recombination | chromatin organization | dna-templated transcription | regulation of dna-templated transcription | trna metabolic process | protein folding | protein glycosylation | amino acid metabolic process | modified amino acid metabolic process | lipid metabolic process | vitamin metabolic process | sulfur compound metabolic process | intracellular protein transport | nucleocytoplasmic transport | autophagy | inflammatory response | mitochondrion organization | cytoskeleton organization | microtubule-based movement | peroxisome organization | lysosome organization | chromosome segregation | cell adhesion | establishment or maintenance of cell polarity | programmed cell death | photosynthesis | mrna metabolic process | snrna metabolic process | vesicle-mediated transport | reproductive process | digestive system process | signaling | cell differentiation | protein catabolic process | extracellular matrix organization | regulatory ncrna-mediated gene silencing | telomere organization | cell junction organization | wound healing | ribosome biogenesis | cilium organization | anatomical structure development | cell motility | nervous system process | endocrine process | protein maturation | transmembrane transport | nucleobase-containing small molecule metabolic process | hepaticobiliary system process | membrane organization | protein-containing complex assembly | cell wall organization or biogenesis | nitrogen cycle metabolic process | protein localization to plasma membrane | defense response to other organism | detoxification | meiotic nuclear division | mitotic nuclear division | mitochondrial gene expression | carbohydrate derivative metabolic process | other biological process | all cellular component | nuclear chromosome | extracellular region | extracellular space | cell wall | nucleus | nuclear envelope | nucleoplasm | chromosome | nucleolus | mitochondrion | lysosome | endosome | vacuole | peroxisome | endoplasmic reticulum | golgi apparatus | lipid droplet | microtubule organizing center | cytosol | ribosome | cytoskeleton | plasma membrane | cilium | plastid | thylakoid | external encapsulating structure | extracellular matrix | cytoplasmic vesicle | organelle | other cellular component | |||
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Aspect | Term | |
---|---|---|
Cellular Component | AP-2 adaptor complex | |
Cellular Component | cellular bud neck | |
Cellular Component | endocytic vesicle | |
Molecular Function | clathrin binding | |
Biological Process | endocytosis | |
Biological Process | intracellular protein transport | |
Biological Process | vesicle-mediated transport |
Keywords
- Biological process
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameAP-2 complex subunit beta
- Alternative names
Gene names
Organism names
- Strain
- Taxonomic lineageEukaryota > Fungi > Dikarya > Ascomycota > Saccharomycotina > Saccharomycetes > Saccharomycetales > Saccharomycetaceae > Saccharomyces
Accessions
- Primary accessionP27351
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
UniProt Annotation
GO Annotation
Membrane, coated pit ; Peripheral membrane protein
Note: Component of the coat surrounding the cytoplasmic face of coated vesicles in the plasma membrane.
Keywords
- Cellular component
PTM/Processing
Features
Showing features for chain, modified residue.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000193755 | 1-700 | AP-2 complex subunit beta | |||
Sequence: MSDQKVFARYKANEIVTDLQHFGVKKFKSNITRRKNALRKIIANLVLGNYGEMSVLFSELLKFWQIEDDLEVKRICHEYIRVIGALKPQQAREALPFIMDDFKSRDEKLQIMALRTLVLVPVKELSDQAFDCIISLVNHKSPPEQVTRTAIYALLDLDEIDHERVLGLSSILHDIVKAQSSSPEVIVAALHTLYSIHEKNANMEPFRIPLELAFDMLELLPELNEWNKATVLEVLTTSVVPQHYLDTHEMIELALPYLQQVNTYVVLNSLKFIMYLLNYVDVIKETLAEKLSNSVIALLDKPPELQFLVLRNVILLLLSRESSLLRLDISYFFIEYNDPIYIKDTKLECLYLLANKETLPRILEELEQYATDIDIQMSRKSVRAIGNLAVKLDEDSVHDCVAVLLDLLEFGVDYVVQEIISVFRNILRKYPNNFKANVTELVKHTEVVQEPESKNAMIWIITQYSDVIPNYLELFRVFSSNMFSETLEVQFSILNSAIKFFIRSPTKETEELCMDLLKGCIDHENNPDLRDKTLMYWRLLSLTKTSRISNAITFESLKSVLDGELPLIEMNTKLDPTVLEELELNIGTIVSIYLKPVSHIFRLNKTKLLPQSPILNPNKDLLPVVGNSFPPTGANRDRQNSESQSSTKSRKTAMMDDYDKPAEKINQLKGKRKSSSNNPSKLSRKPSTLLRKLSMKRPFS | ||||||
Modified residue | 649 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 652 | Phosphothreonine | ||||
Sequence: T | ||||||
Modified residue | 683 | Phosphoserine | ||||
Sequence: S |
Keywords
- PTM
Proteomic databases
PTM databases
Interaction
Subunit
Adaptor protein complex 2 (AP-2) is a heterotetramer composed of two large adaptins (alpha-type subunit APL3 and beta-type subunit APL1), a medium chain (mu-type subunit APM4) and a small adaptin (sigma-type subunit APS2). Interacts with APS2.
Protein-protein interaction databases
Miscellaneous
Structure
Family & Domains
Features
Showing features for region, compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Region | 625-700 | Disordered | ||||
Sequence: VGNSFPPTGANRDRQNSESQSSTKSRKTAMMDDYDKPAEKINQLKGKRKSSSNNPSKLSRKPSTLLRKLSMKRPFS | ||||||
Compositional bias | 632-651 | Polar residues | ||||
Sequence: TGANRDRQNSESQSSTKSRK | ||||||
Compositional bias | 652-670 | Basic and acidic residues | ||||
Sequence: TAMMDDYDKPAEKINQLKG | ||||||
Compositional bias | 671-687 | Polar residues | ||||
Sequence: KRKSSSNNPSKLSRKPS |
Sequence similarities
Belongs to the adaptor complexes large subunit family.
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length700
- Mass (Da)80,453
- Last updated1995-11-01 v2
- Checksum556A8F3EF8B3930F
Features
Showing features for sequence conflict, compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Sequence conflict | 55 | in Ref. 1; AAA35226 | ||||
Sequence: V → L | ||||||
Sequence conflict | 484 | in Ref. 1; AAA35226 | ||||
Sequence: S → N | ||||||
Sequence conflict | 504 | in Ref. 1; AAA35226 | ||||
Sequence: S → N | ||||||
Sequence conflict | 521 | in Ref. 1; AAA35226 | ||||
Sequence: I → T | ||||||
Sequence conflict | 629 | in Ref. 1; AAA35226 | ||||
Sequence: F → I | ||||||
Compositional bias | 632-651 | Polar residues | ||||
Sequence: TGANRDRQNSESQSSTKSRK | ||||||
Compositional bias | 652-670 | Basic and acidic residues | ||||
Sequence: TAMMDDYDKPAEKINQLKG | ||||||
Compositional bias | 671-687 | Polar residues | ||||
Sequence: KRKSSSNNPSKLSRKPS |
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
M64998 EMBL· GenBank· DDBJ | AAA35226.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
X87611 EMBL· GenBank· DDBJ | CAA60927.1 EMBL· GenBank· DDBJ | Genomic DNA | Sequence problems. | |
Z49505 EMBL· GenBank· DDBJ | CAA89527.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
BK006943 EMBL· GenBank· DDBJ | DAA08795.1 EMBL· GenBank· DDBJ | Genomic DNA |