UniProt functional annotation for Q99962



	UniProt functional annotation for Q99962

UniProt code: Q99962.

Organism: Homo sapiens (Human).

Taxonomy: Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; Homo.

Function: Implicated in synaptic vesicle endocytosis. May recruit other proteins to membranes with high curvature. Required for BDNF-dependent dendrite outgrowth. Cooperates with SH3GL2 to mediate BDNF-NTRK2 early endocytic trafficking and signaling from early endosomes. {ECO:0000250|UniProtKB:Q62420}.

Subunit: Monomer; in cytoplasm. Homodimer; when associated with membranes (By similarity). Interacts with OPHN1 (By similarity). Interacts with SYNJ1 (PubMed:10542231). Interacts with DNM1 (By similarity). Interacts with MAP4K3; the interaction appears to regulate MAP4K3-mediated JNK activation (By similarity). Interacts with PDCD6IP (PubMed:17350572). Interacts with ATXN2 (PubMed:18602463). Interacts with ADAM9 and ADAM15 cytoplasmic tails (PubMed:10531379). Interacts with BIN2 (PubMed:23285027). Interacts with TMEM108 (By similarity). Interacts with ADGRB2 (PubMed:28891236). {ECO:0000250|UniProtKB:Q62420, ECO:0000250|UniProtKB:Q62910, ECO:0000269|PubMed:10531379, ECO:0000269|PubMed:10542231, ECO:0000269|PubMed:17350572, ECO:0000269|PubMed:18602463, ECO:0000269|PubMed:23285027, ECO:0000269|PubMed:28891236}.

Subcellular location: Cytoplasm {ECO:0000250|UniProtKB:O35179}. Membrane {ECO:0000250|UniProtKB:O35179}; Peripheral membrane protein {ECO:0000250|UniProtKB:O35179}. Early endosome {ECO:0000250|UniProtKB:Q62420}. Cell junction, synapse, presynapse {ECO:0000250|UniProtKB:O35179}.

Tissue specificity: Brain, mostly in frontal cortex. Expressed at high level in fetal cerebellum.

Domain: An N-terminal amphipathic helix, the BAR domain and a second amphipathic helix inserted into helix 1 of the BAR domain (N-BAR domain) induce membrane curvature and bind curved membranes. The BAR domain dimer forms a rigid crescent shaped bundle of helices with the pair of second amphipathic helices protruding towards the membrane- binding surface. {ECO:0000269|PubMed:16763557}.

Miscellaneous: HeLa cells expressing the N-BAR domain of SH3GL2 show tubulation of the plasma membrane. The N-BAR domain binds liposomes and induces formation of tubules from liposomes. The N-terminal amphipathic helix is required for liposome binding. The second amphipathic helix enhances liposome tubulation.

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

Annotations taken from UniProtKB at the EBI.


Organism:		Homo sapiens (Human).
Taxonomy:		Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; Homo.



Function:		Implicated in synaptic vesicle endocytosis. May recruit other proteins to membranes with high curvature. Required for BDNF-dependent dendrite outgrowth. Cooperates with SH3GL2 to mediate BDNF-NTRK2 early endocytic trafficking and signaling from early endosomes. {ECO:0000250\|UniProtKB:Q62420}.


Subunit:		Monomer; in cytoplasm. Homodimer; when associated with membranes (By similarity). Interacts with OPHN1 (By similarity). Interacts with SYNJ1 (PubMed:10542231). Interacts with DNM1 (By similarity). Interacts with MAP4K3; the interaction appears to regulate MAP4K3-mediated JNK activation (By similarity). Interacts with PDCD6IP (PubMed:17350572). Interacts with ATXN2 (PubMed:18602463). Interacts with ADAM9 and ADAM15 cytoplasmic tails (PubMed:10531379). Interacts with BIN2 (PubMed:23285027). Interacts with TMEM108 (By similarity). Interacts with ADGRB2 (PubMed:28891236). {ECO:0000250\|UniProtKB:Q62420, ECO:0000250\|UniProtKB:Q62910, ECO:0000269\|PubMed:10531379, ECO:0000269\|PubMed:10542231, ECO:0000269\|PubMed:17350572, ECO:0000269\|PubMed:18602463, ECO:0000269\|PubMed:23285027, ECO:0000269\|PubMed:28891236}.
Subcellular location:		Cytoplasm {ECO:0000250\|UniProtKB:O35179}. Membrane {ECO:0000250\|UniProtKB:O35179}; Peripheral membrane protein {ECO:0000250\|UniProtKB:O35179}. Early endosome {ECO:0000250\|UniProtKB:Q62420}. Cell junction, synapse, presynapse {ECO:0000250\|UniProtKB:O35179}.
Tissue specificity:		Brain, mostly in frontal cortex. Expressed at high level in fetal cerebellum.
Domain:		An N-terminal amphipathic helix, the BAR domain and a second amphipathic helix inserted into helix 1 of the BAR domain (N-BAR domain) induce membrane curvature and bind curved membranes. The BAR domain dimer forms a rigid crescent shaped bundle of helices with the pair of second amphipathic helices protruding towards the membrane- binding surface. {ECO:0000269\|PubMed:16763557}.
Miscellaneous:		HeLa cells expressing the N-BAR domain of SH3GL2 show tubulation of the plasma membrane. The N-BAR domain binds liposomes and induces formation of tubules from liposomes. The N-terminal amphipathic helix is required for liposome binding. The second amphipathic helix enhances liposome tubulation.
Similarity:		Belongs to the endophilin family. {ECO:0000305}.