UniProt functional annotation for O88339



	UniProt functional annotation for O88339

UniProt code: O88339.

Organism: Rattus norvegicus (Rat).

Taxonomy: Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae; Murinae; Rattus.

Function: Binds to membranes enriched in phosphatidylinositol 4,5- bisphosphate (PtdIns(4,5)P2) (PubMed:11161217). Modifies membrane curvature and facilitates the formation of clathrin-coated invaginations (PubMed:9723620, PubMed:12353027). Regulates receptor- mediated endocytosis (By similarity). {ECO:0000250|UniProtKB:Q9Y6I3, ECO:0000269|PubMed:11161217, ECO:0000269|PubMed:12353027, ECO:0000269|PubMed:9723620}.

Subunit: Monomer. Binds ITSN1 (By similarity). Binds clathrin, ZBTB16/ZNF145, AP2A1 and AP2A2. Binds ubiquitinated proteins. Interacts with RALBP1 in a complex also containing NUMB and TFAP2A during interphase and mitosis. Interacts with AP2B1. Interacts with UBQLN2 (By similarity). Interacts with REPS2; the interaction is direct (By similarity). Interacts with EPS15; the interaction is direct (By similarity). {ECO:0000250|UniProtKB:Q80VP1, ECO:0000250|UniProtKB:Q9Y6I3, ECO:0000269|PubMed:10380931, ECO:0000269|PubMed:10430869, ECO:0000269|PubMed:10692452, ECO:0000269|PubMed:10791968, ECO:0000269|PubMed:10944104, ECO:0000269|PubMed:11161217, ECO:0000269|PubMed:12057195, ECO:0000269|PubMed:12353027, ECO:0000269|PubMed:9723620, ECO:0000269|PubMed:9920862}.

Subcellular location: Cytoplasm. Cell membrane; Peripheral membrane protein. Nucleus. Membrane, clathrin-coated pit. Note=Associated with the cytoplasmic membrane at sites where clathrin-coated pits are forming. Colocalizes with clathrin and AP-2 in a punctate pattern on the plasma membrane. Colocalizes with clathrin at the Golgi complex. Detected in presynaptic nerve terminals and in synaptosomes. May shuttle to the nucleus when associated with ZBTB16/ZNF145.

Tissue specificity: Ubiquitously expressed (PubMed:9723620). Detected in liver, spleen and testis, and weakly in lung and thymus (at protein level) (PubMed:10393179). {ECO:0000269|PubMed:10393179, ECO:0000269|PubMed:9723620}.

Domain: The NPF repeat domain is involved in EPS15 binding.

Domain: The DPW repeat domain is involved in AP2A2 and clathrin binding.

Domain: The [DE]-X(1,2)-F-X-X-[FL]-X-X-X-R motif mediates interaction the AP-2 complex subunit AP2B1. {ECO:0000250}.

Ptm: Ubiquitinated. {ECO:0000269|PubMed:11919637}.

Ptm: Phosphorylated on serine and/or threonine residues in mitotic cells. Phosphorylation reduces interaction with REPS2, AP-2 and the membrane fraction. Depolarization of synaptosomes results in dephosphorylation. {ECO:0000269|PubMed:9920862}.

Similarity: Belongs to the epsin family. {ECO:0000305}.

Annotations taken from UniProtKB at the EBI.


Organism:		Rattus norvegicus (Rat).
Taxonomy:		Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae; Murinae; Rattus.



Function:		Binds to membranes enriched in phosphatidylinositol 4,5- bisphosphate (PtdIns(4,5)P2) (PubMed:11161217). Modifies membrane curvature and facilitates the formation of clathrin-coated invaginations (PubMed:9723620, PubMed:12353027). Regulates receptor- mediated endocytosis (By similarity). {ECO:0000250\|UniProtKB:Q9Y6I3, ECO:0000269\|PubMed:11161217, ECO:0000269\|PubMed:12353027, ECO:0000269\|PubMed:9723620}.


Subunit:		Monomer. Binds ITSN1 (By similarity). Binds clathrin, ZBTB16/ZNF145, AP2A1 and AP2A2. Binds ubiquitinated proteins. Interacts with RALBP1 in a complex also containing NUMB and TFAP2A during interphase and mitosis. Interacts with AP2B1. Interacts with UBQLN2 (By similarity). Interacts with REPS2; the interaction is direct (By similarity). Interacts with EPS15; the interaction is direct (By similarity). {ECO:0000250\|UniProtKB:Q80VP1, ECO:0000250\|UniProtKB:Q9Y6I3, ECO:0000269\|PubMed:10380931, ECO:0000269\|PubMed:10430869, ECO:0000269\|PubMed:10692452, ECO:0000269\|PubMed:10791968, ECO:0000269\|PubMed:10944104, ECO:0000269\|PubMed:11161217, ECO:0000269\|PubMed:12057195, ECO:0000269\|PubMed:12353027, ECO:0000269\|PubMed:9723620, ECO:0000269\|PubMed:9920862}.
Subcellular location:		Cytoplasm. Cell membrane; Peripheral membrane protein. Nucleus. Membrane, clathrin-coated pit. Note=Associated with the cytoplasmic membrane at sites where clathrin-coated pits are forming. Colocalizes with clathrin and AP-2 in a punctate pattern on the plasma membrane. Colocalizes with clathrin at the Golgi complex. Detected in presynaptic nerve terminals and in synaptosomes. May shuttle to the nucleus when associated with ZBTB16/ZNF145.
Tissue specificity:		Ubiquitously expressed (PubMed:9723620). Detected in liver, spleen and testis, and weakly in lung and thymus (at protein level) (PubMed:10393179). {ECO:0000269\|PubMed:10393179, ECO:0000269\|PubMed:9723620}.
Domain:		The NPF repeat domain is involved in EPS15 binding.
Domain:		The DPW repeat domain is involved in AP2A2 and clathrin binding.
Domain:		The [DE]-X(1,2)-F-X-X-[FL]-X-X-X-R motif mediates interaction the AP-2 complex subunit AP2B1. {ECO:0000250}.
Ptm:		Ubiquitinated. {ECO:0000269\|PubMed:11919637}.
Ptm:		Phosphorylated on serine and/or threonine residues in mitotic cells. Phosphorylation reduces interaction with REPS2, AP-2 and the membrane fraction. Depolarization of synaptosomes results in dephosphorylation. {ECO:0000269\|PubMed:9920862}.
Similarity:		Belongs to the epsin family. {ECO:0000305}.