SH3GLB1

Endophilin-B1 is a protein that in humans is encoded by the SH3GLB1 gene.^[5][6][7] Endophilin-B1 belongs to the Bin/Amphiphysin/Rvs167 (BAR) family of proteins and plays a critical role in mitochondrial fission and fusion, as well as in autophagy and apoptosis.^[8][9][10] Loss of functional endophilin-B1 is seen in many different forms of cancer.^[11][12][13] The link between carcinogenesis and dysregulation of cell death pathways suggests that endophilin-B1 serves a critical tumor suppressor role in the cell, although the underlying mechanisms are not known.

SH3GLB1
Available structures PDB Ortholog search: PDBe RCSB List of PDB id codes 1X43
Identifiers
Aliases	SH3GLB1, Bif-1, PPP1R70, dJ612B15.2, CGI-61, SH3 domain containing GRB2 like endophilin B1, SH3 domain containing GRB2 like, endophilin B1
External IDs	OMIM: 609287; MGI: 1859730; HomoloGene: 9337; GeneCards: SH3GLB1; OMA:SH3GLB1 - orthologs
Gene location (Human) Chr. Chromosome 1 (human)[1] Band 1p22.3 Start 86,704,570 bp[1] End 86,748,184 bp[1]
Gene location (Mouse) Chr. Chromosome 3 (mouse)[2] Band 3|3 H2 Start 144,389,439 bp[2] End 144,426,096 bp[2]
RNA expression pattern Bgee Human Mouse (ortholog) Top expressed in tibialis anterior muscle deltoid muscle right ventricle muscle of trunk Skeletal muscle tissue of rectus abdominis gastrocnemius muscle thoracic diaphragm oocyte muscle of arm biceps brachii Top expressed in blood seminiferous tubule ankle endothelial cell of lymphatic vessel temporal muscle digastric muscle sternocleidomastoid muscle triceps brachii muscle medial head of gastrocnemius muscle right ventricle More reference expression data BioGPS More reference expression data
Gene ontology Molecular function protein homodimerization activity protein binding identical protein binding lipid binding cadherin binding Cellular component cytoplasm Golgi apparatus membrane Golgi membrane mitochondrial outer membrane autophagosome membrane midbody mitochondrion extracellular exosome cytoplasmic vesicle cytosol Biological process cellular response to glucose starvation regulation of cytokinesis regulation of protein stability positive regulation of autophagosome assembly positive regulation of autophagy positive regulation of protein targeting to mitochondrion cellular response to amino acid starvation receptor catabolic process autophagy protein complex oligomerization membrane fission positive regulation of protein oligomerization positive regulation of membrane tubulation autophagic cell death regulation of macroautophagy protein localization to vacuolar membrane apoptotic process Sources:Amigo / QuickGO
Orthologs Species Human Mouse Entrez 51100 54673 Ensembl ENSG00000097033 ENSMUSG00000037062 UniProt Q9Y371 Q9JK48 RefSeq (mRNA) NM_001206651 NM_001206652 NM_001206653 NM_016009 NM_001282037 NM_001282042 NM_019464 NM_001379170 NM_001379171 NM_001379172 NM_001379173 NM_001379174 RefSeq (protein) NP_001193580 NP_001193581 NP_001193582 NP_057093 NP_001268966 NP_001268971 NP_062337 NP_001366099 NP_001366100 NP_001366101 NP_001366102 NP_001366103 Location (UCSC) Chr 1: 86.7 – 86.75 Mb Chr 3: 144.39 – 144.43 Mb PubMed search [3] [4]
Wikidata
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Structure

A pseudo-atomic model of helical scaffolds formed by a truncated form of endophilin-B1.^[14] Based on a ChimeraX^[15] rendering of 6UP6.

In the presence of model biological membranes, endophilin-B1 dimers assemble into helical scaffolds around the membrane and drive its tubulation.^[14]

Interactions

In addition to the membrane binding and remodeling properties endophilin-B1 shares with many other BAR proteins, endophilin-B1 interacts with the pro-apoptotic factor Bcl-2-associated X protein (Bax)^[5][6] and SH3GLB2.^[5] It has also been shown to interact with a wide variety of proteins through a canonical SH3 domain that enables PxxP motif-containing protein interactions, including Beclin-1, amphiphysin-1, amphiphysin-2, and huntingtin.^[16][17]