ID SHLB1_HUMAN Reviewed; 365 AA. AC Q9Y371; B4E182; Q5H8U5; Q9H3Z0; Q9NR47; Q9NYA9; DT 16-JAN-2004, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1999, sequence version 1. DT 28-JAN-2026, entry version 206. DE RecName: Full=Endophilin-B1; DE AltName: Full=Bax-interacting factor 1; DE Short=Bif-1; DE AltName: Full=SH3 domain-containing GRB2-like protein B1; GN Name=SH3GLB1; Synonyms=KIAA0491; ORFNames=CGI-61; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; OC Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), MUTAGENESIS OF VAL-8, INTERACTION RP WITH BAX AND SH3GLB2, AND TISSUE SPECIFICITY. RC TISSUE=Skeletal muscle; RX PubMed=11161816; DOI=10.1006/geno.2000.6378; RA Pierrat B., Simonen M., Cueto M., Mestan J., Ferrigno P., Heim J.; RT "SH3GLB, a new endophilin-related protein family featuring an SH3 domain."; RL Genomics 71:222-234(2001). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), INTERACTION WITH BAX, AND TISSUE RP SPECIFICITY. RC TISSUE=Fetal brain; RX PubMed=11259440; DOI=10.1074/jbc.m101527200; RA Cuddeback S.M., Yamaguchi H., Komatsu K., Miyashita T., Yamada M., Wu C., RA Singh S., Wang H.-G.; RT "Molecular cloning and characterization of Bif-1. A novel Src homology 3 RT domain-containing protein that associates with Bax."; RL J. Biol. Chem. 276:20559-20565(2001). RN [3] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2). RC TISSUE=Lung; RX PubMed=12456676; DOI=10.1074/jbc.m208568200; RA Modregger J., Schmidt A.A., Ritter B., Huttner W.B., Plomann M.; RT "Characterization of endophilin B1b, a brain-specific membrane-associated RT lysophosphatidic acid acyl transferase with properties distinct from RT endophilin A1."; RL J. Biol. Chem. 278:4160-4167(2003). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RC TISSUE=Brain; RX PubMed=9455484; DOI=10.1093/dnares/4.5.345; RA Seki N., Ohira M., Nagase T., Ishikawa K., Miyajima N., Nakajima D., RA Nomura N., Ohara O.; RT "Characterization of cDNA clones in size-fractionated cDNA libraries from RT human brain."; RL DNA Res. 4:345-349(1997). RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RX PubMed=10810093; DOI=10.1101/gr.10.5.703; RA Lai C.-H., Chou C.-Y., Ch'ang L.-Y., Liu C.-S., Lin W.-C.; RT "Identification of novel human genes evolutionarily conserved in RT Caenorhabditis elegans by comparative proteomics."; RL Genome Res. 10:703-713(2000). RN [6] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 3). RC TISSUE=Kidney, and Placenta; RX PubMed=14702039; DOI=10.1038/ng1285; RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S., RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., RA Isogai T., Sugano S.; RT "Complete sequencing and characterization of 21,243 full-length human RT cDNAs."; RL Nat. Genet. 36:40-45(2004). RN [7] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=16710414; DOI=10.1038/nature04727; RA Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., RA Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., RA Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K., RA Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., RA Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., RA Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., RA Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., RA Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., RA Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., RA Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., RA Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., RA Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., RA Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., RA Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., RA Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., RA Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., RA Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., RA Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., RA Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., RA McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., RA Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., RA Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., RA Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., RA Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., RA Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., RA White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., RA Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., RA Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., RA Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.; RT "The DNA sequence and biological annotation of human chromosome 1."; RL Nature 441:315-321(2006). RN [8] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RC TISSUE=Skin; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA project: RT the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [9] RP FUNCTION, AND DOMAIN. RX PubMed=11604418; DOI=10.1083/jcb.200107075; RA Farsad K., Ringstad N., Takei K., Floyd S.R., Rose K., De Camilli P.; RT "Generation of high curvature membranes mediated by direct endophilin RT bilayer interactions."; RL J. Cell Biol. 155:193-200(2001). RN [10] RP FUNCTION, AND SUBCELLULAR LOCATION. RX PubMed=15452144; DOI=10.1083/jcb.200407046; RA Karbowski M., Jeong S.-Y., Youle R.J.; RT "Endophilin B1 is required for the maintenance of mitochondrial RT morphology."; RL J. Cell Biol. 166:1027-1039(2004). RN [11] RP FUNCTION. RX PubMed=16227588; DOI=10.1128/mcb.25.21.9369-9382.2005; RA Takahashi Y., Karbowski M., Yamaguchi H., Kazi A., Wu J., Sebti S.M., RA Youle R.J., Wang H.G.; RT "Loss of Bif-1 suppresses Bax/Bak conformational change and mitochondrial RT apoptosis."; RL Mol. Cell. Biol. 25:9369-9382(2005). RN [12] RP FUNCTION, INTERACTION WITH UVRAG AND BECN1, SUBCELLULAR LOCATION, AND RP DOMAIN. RX PubMed=17891140; DOI=10.1038/ncb1634; RA Takahashi Y., Coppola D., Matsushita N., Cualing H.D., Sun M., Sato Y., RA Liang C., Jung J.U., Cheng J.Q., Mule J.J., Pledger W.J., Wang H.G.; RT "Bif-1 interacts with Beclin 1 through UVRAG and regulates autophagy and RT tumorigenesis."; RL Nat. Cell Biol. 9:1142-1151(2007). RN [13] RP FUNCTION, SUBUNIT, AND SUBCELLULAR LOCATION. RX PubMed=20643123; DOI=10.1016/j.yexcr.2010.07.008; RA Thoresen S.B., Pedersen N.M., Liestol K., Stenmark H.; RT "A phosphatidylinositol 3-kinase class III sub-complex containing VPS15, RT VPS34, Beclin 1, UVRAG and BIF-1 regulates cytokinesis and degradative RT endocytic traffic."; RL Exp. Cell Res. 316:3368-3378(2010). RN [14] RP FUNCTION, AND SUBCELLULAR LOCATION. RX PubMed=21068542; DOI=10.4161/auto.7.1.14015; RA Takahashi Y., Meyerkord C.L., Hori T., Runkle K., Fox T.E., Kester M., RA Loughran T.P., Wang H.G.; RT "Bif-1 regulates Atg9 trafficking by mediating the fission of Golgi RT membranes during autophagy."; RL Autophagy 7:61-73(2011). RN [15] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=21269460; DOI=10.1186/1752-0509-5-17; RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., RA Bennett K.L., Superti-Furga G., Colinge J.; RT "Initial characterization of the human central proteome."; RL BMC Syst. Biol. 5:17-17(2011). RN [16] RP PHOSPHORYLATION AT THR-145, AND MUTAGENESIS OF THR-145. RX PubMed=21499257; DOI=10.1038/ncb2217; RA Wong A.S., Lee R.H., Cheung A.Y., Yeung P.K., Chung S.K., Cheung Z.H., RA Ip N.Y.; RT "Cdk5-mediated phosphorylation of endophilin B1 is required for induced RT autophagy in models of Parkinson's disease."; RL Nat. Cell Biol. 13:568-579(2011). RN [17] RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND IDENTIFICATION BY MASS RP SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=22814378; DOI=10.1073/pnas.1210303109; RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A., RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E., RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.; RT "N-terminal acetylome analyses and functional insights of the N-terminal RT acetyltransferase NatB."; RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012). RN [18] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=25944712; DOI=10.1002/pmic.201400617; RA Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., Ayoub D., RA Lane L., Bairoch A., Van Dorsselaer A., Carapito C.; RT "N-terminome analysis of the human mitochondrial proteome."; RL Proteomics 15:2519-2524(2015). CC -!- FUNCTION: May be required for normal outer mitochondrial membrane CC dynamics (PubMed:15452144). Required for coatomer-mediated retrograde CC transport in certain cells (By similarity). May recruit other proteins CC to membranes with high curvature. May promote membrane fusion CC (PubMed:11604418). Involved in activation of caspase-dependent CC apoptosis by promoting BAX/BAK1 activation (PubMed:16227588). Isoform 1 CC acts proapoptotic in fibroblasts (By similarity). Involved in caspase- CC independent apoptosis during nutrition starvation and involved in the CC regulation of autophagy. Activates lipid kinase activity of PIK3C3 CC during autophagy probably by associating with the PI3K complex II CC (PI3KC3-C2) (PubMed:17891140). Associated with PI3KC3-C2 during CC autophagy may regulate the trafficking of ATG9A from the Golgi complex CC to the peripheral cytoplasm for the formation of autophagosomes by CC inducing Golgi membrane tubulation and fragmentation (PubMed:21068542). CC Involved in regulation of degradative endocytic trafficking and CC cytokinesis, probably in the context of PI3KC3-C2 (PubMed:20643123). CC Isoform 2 acts antiapoptotic in neuronal cells; involved in maintenance CC of mitochondrial morphology and promotes neuronal viability (By CC similarity). {ECO:0000250|UniProtKB:Q9JK48, CC ECO:0000269|PubMed:11604418, ECO:0000269|PubMed:15452144, CC ECO:0000269|PubMed:17891140, ECO:0000269|PubMed:20643123, CC ECO:0000269|PubMed:21068542}. CC -!- SUBUNIT: Homodimer, and heterodimer with SH3GLB2 (PubMed:11161816). CC Binds BAX; induction of apoptosis augments BAX binding CC (PubMed:11161816, PubMed:11259440). Binds DNM1, HTT, AMPH, BIN1 and CC ARFGAP1 (By similarity). Interacts with UVRAG; UVRAG bridges the CC interaction to BECN1 indicative for an association with the PI3K CC complex II (PI3KC3-C2) (PubMed:17891140, PubMed:20643123). CC {ECO:0000250|UniProtKB:Q9JK48, ECO:0000269|PubMed:11161816, CC ECO:0000269|PubMed:11259440, ECO:0000269|PubMed:17891140}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:15452144}. Golgi CC apparatus membrane {ECO:0000269|PubMed:21068542}; Peripheral membrane CC protein {ECO:0000250}. Mitochondrion outer membrane CC {ECO:0000269|PubMed:15452144}; Peripheral membrane protein CC {ECO:0000269|PubMed:15452144}. Cytoplasmic vesicle, autophagosome CC membrane {ECO:0000269|PubMed:17891140}. Midbody CC {ECO:0000269|PubMed:20643123}. Note=Association with the Golgi CC apparatus depends on the cell type (By similarity). Following CC starvation colocalizes with ATG5 and LC3 autophagy-related protein(s)on CC autophagosomal membranes (PubMed:17891140). {ECO:0000250, CC ECO:0000269|PubMed:17891140}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=3; CC Comment=Additional isoforms seem to exist.; CC Name=1; CC IsoId=Q9Y371-1; Sequence=Displayed; CC Name=2; CC IsoId=Q9Y371-2; Sequence=VSP_009276; CC Name=3; CC IsoId=Q9Y371-3; Sequence=VSP_044895; CC -!- TISSUE SPECIFICITY: Highly expressed in heart, skeletal muscle, kidney CC and placenta. Detected at lower levels in brain, colon, thymus, spleen, CC liver, small intestine, lung and peripheral blood leukocytes. CC {ECO:0000269|PubMed:11161816, ECO:0000269|PubMed:11259440}. CC -!- DOMAIN: An N-terminal amphipathic helix, the BAR domain and a second CC amphipathic helix inserted into helix 1 of the BAR domain (N-BAR CC domain) induce membrane curvature and bind curved membranes. CC {ECO:0000269|PubMed:11604418}. CC -!- DOMAIN: The SH3 domain is required and sufficient for the interaction CC with UVRAG. {ECO:0000269|PubMed:17891140}. CC -!- PTM: Phosphorylated at Thr-145 by CDK5; this phosphorylation is CC required for autophagy induction in starved neurons and facilitates CC homodimerization. {ECO:0000269|PubMed:21499257}. CC -!- MISCELLANEOUS: HeLa cells lacking SH3GLB1 show dissociation of outer CC and inner mitochondrial membrane as well as abnormal mitochondrial CC morphology. Cells overexpressing SH3GLB1 lacking an N-terminal CC amphipathic helix show a similar phenotype. CC -!- MISCELLANEOUS: SH3GLB1 binds liposomes and induces formation of tubules CC from liposomes. SH3GLB1 lacking the N-terminal amphipathic helix fails CC to induce liposome tubulation. CC -!- SIMILARITY: Belongs to the endophilin family. {ECO:0000305}. CC -!- CAUTION: It is uncertain whether Met-1 or Met-4 is the initiator. CC {ECO:0000305}. CC -!- CAUTION: Was originally thought to have lysophosphatidic acid CC acyltransferase activity, but by homology with SH3GL2/endophilin A1 is CC unlikely to have this activity. {ECO:0000305|PubMed:12456676}. CC -!- SEQUENCE CAUTION: CC Sequence=AAF81225.1; Type=Erroneous initiation; Evidence={ECO:0000305}; CC Sequence=BAD88797.1; Type=Erroneous initiation; Evidence={ECO:0000305}; CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AF257318; AAF81225.1; ALT_INIT; mRNA. DR EMBL; AF350371; AAK27365.1; -; mRNA. DR EMBL; AF263293; AAF73017.1; -; mRNA. DR EMBL; AB007960; BAD88797.1; ALT_INIT; mRNA. DR EMBL; AF151819; AAD34056.1; -; mRNA. DR EMBL; AK001954; BAA91999.1; -; mRNA. DR EMBL; AK303710; BAG64694.1; -; mRNA. DR EMBL; AL049597; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; BC007455; AAH07455.1; -; mRNA. DR CCDS; CCDS55612.1; -. [Q9Y371-2] DR CCDS; CCDS55613.1; -. [Q9Y371-3] DR CCDS; CCDS710.1; -. [Q9Y371-1] DR RefSeq; NP_001193580.1; NM_001206651.1. DR RefSeq; NP_001193581.1; NM_001206652.2. [Q9Y371-2] DR RefSeq; NP_001193582.1; NM_001206653.2. [Q9Y371-3] DR RefSeq; NP_057093.1; NM_016009.5. [Q9Y371-1] DR PDB; 6UP6; EM; 9.00 A; A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P/Q/R/S/T/V/W/a/b/c/d/e/f/g/h=1-365. DR PDB; 6UPN; EM; 10.00 A; A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P/Q/R/S/T/V/W/X/Y/a/b/c/d/e/f=1-365. DR PDB; 9G2R; EM; 3.88 A; A/B/C/D/E/F/G/H/I/J/K/L=1-365. DR PDB; 9G2U; EM; 3.45 A; A/B=1-365. DR PDB; 9G2W; EM; 3.60 A; A/B=1-365. DR PDBsum; 6UP6; -. DR PDBsum; 6UPN; -. DR PDBsum; 9G2R; -. DR PDBsum; 9G2U; -. DR PDBsum; 9G2W; -. DR AlphaFoldDB; Q9Y371; -. DR EMDB; EMD-20835; -. DR EMDB; EMD-20842; -. DR EMDB; EMD-50981; -. DR EMDB; EMD-50984; -. DR EMDB; EMD-50986; -. DR SASBDB; Q9Y371; -. DR SMR; Q9Y371; -. DR BioGRID; 119289; 128. DR CORUM; Q9Y371; -. DR DIP; DIP-41970N; -. DR FunCoup; Q9Y371; 2461. DR MINT; Q9Y371; -. DR STRING; 9606.ENSP00000479919; -. DR TCDB; 8.A.34.1.4; the endophilin (endophilin) family. DR GlyGen; Q9Y371; 2 sites, 1 N-linked glycan (1 site), 1 O-linked glycan (1 site). DR iPTMnet; Q9Y371; -. DR PhosphoSitePlus; Q9Y371; -. DR BioMuta; SH3GLB1; -. DR DMDM; 41018158; -. DR REPRODUCTION-2DPAGE; IPI00006558; -. DR jPOST; Q9Y371; -. DR MassIVE; Q9Y371; -. DR PaxDb; 9606-ENSP00000479919; -. DR PeptideAtlas; Q9Y371; -. DR ProteomicsDB; 5734; -. DR ProteomicsDB; 85978; -. [Q9Y371-1] DR ProteomicsDB; 85979; -. [Q9Y371-2] DR Pumba; Q9Y371; -. DR Antibodypedia; 2824; 553 antibodies from 36 providers. DR DNASU; 51100; -. DR Ensembl; ENST00000370558.8; ENSP00000473267.1; ENSG00000097033.16. [Q9Y371-1] DR Ensembl; ENST00000482504.1; ENSP00000418744.1; ENSG00000097033.16. [Q9Y371-2] DR Ensembl; ENST00000535010.5; ENSP00000441355.1; ENSG00000097033.16. [Q9Y371-3] DR GeneID; 51100; -. DR KEGG; hsa:51100; -. DR MANE-Select; ENST00000370558.8; ENSP00000473267.1; NM_016009.5; NP_057093.1. DR UCSC; uc001dlw.4; human. [Q9Y371-1] DR AGR; HGNC:10833; -. DR ClinPGx; PA35739; -. DR CTD; 51100; -. DR DisGeNET; 51100; -. DR GeneCards; SH3GLB1; -. DR HGNC; HGNC:10833; SH3GLB1. DR HPA; ENSG00000097033; Low tissue specificity. DR MIM; 609287; gene. DR OpenTargets; ENSG00000097033; -. DR VEuPathDB; HostDB:ENSG00000097033; -. DR eggNOG; KOG3725; Eukaryota. DR GeneTree; ENSGT00940000155667; -. DR HOGENOM; CLU_043817_1_0_1; -. DR InParanoid; Q9Y371; -. DR OMA; ETTYYAQ; -. DR OrthoDB; 14167at2759; -. DR PAN-GO; Q9Y371; 2 GO annotations based on evolutionary models. DR PhylomeDB; Q9Y371; -. DR PathwayCommons; Q9Y371; -. DR SignaLink; Q9Y371; -. DR SIGNOR; Q9Y371; -. DR Agora; ENSG00000097033; -. DR BioGRID-ORCS; 51100; 14 hits in 1159 CRISPR screens. DR CD-CODE; 91857CE7; Nucleolus. DR ChiTaRS; SH3GLB1; human. DR GeneWiki; SH3GLB1; -. DR GenomeRNAi; 51100; -. DR Pharos; Q9Y371; Tbio. DR PRO; PR:Q9Y371; -. DR Proteomes; UP000005640; Chromosome 1. DR RNAct; Q9Y371; protein. DR Bgee; ENSG00000097033; Expressed in tibialis anterior and 209 other cell types or tissues. DR ExpressionAtlas; Q9Y371; baseline and differential. DR GO; GO:0000421; C:autophagosome membrane; IDA:UniProtKB. DR GO; GO:0005737; C:cytoplasm; IDA:HGNC-UCL. DR GO; GO:0031410; C:cytoplasmic vesicle; IEA:UniProtKB-KW. DR GO; GO:0005829; C:cytosol; IDA:HPA. DR GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell. DR GO; GO:0016020; C:membrane; IBA:GO_Central. DR GO; GO:0030496; C:midbody; IDA:UniProtKB. DR GO; GO:0005741; C:mitochondrial outer membrane; IEA:UniProtKB-SubCell. DR GO; GO:0016604; C:nuclear body; IDA:HPA. DR GO; GO:0032991; C:protein-containing complex; IDA:UniProtKB. DR GO; GO:0045296; F:cadherin binding; HDA:BHF-UCL. DR GO; GO:0005504; F:fatty acid binding; IEA:Ensembl. DR GO; GO:0042802; F:identical protein binding; IPI:IntAct. DR GO; GO:0042171; F:lysophosphatidic acid acyltransferase activity; IEA:Ensembl. DR GO; GO:0141038; F:phosphatidylinositol 3-kinase activator activity; IEA:Ensembl. DR GO; GO:0042803; F:protein homodimerization activity; IPI:HGNC-UCL. DR GO; GO:0051084; P:'de novo' post-translational protein folding; IEA:Ensembl. DR GO; GO:0006915; P:apoptotic process; IEA:UniProtKB-KW. DR GO; GO:0048102; P:autophagic cell death; IMP:UniProtKB. DR GO; GO:0006914; P:autophagy; IEA:UniProtKB-KW. DR GO; GO:0034198; P:cellular response to amino acid starvation; IMP:UniProtKB. DR GO; GO:0042149; P:cellular response to glucose starvation; IMP:UniProtKB. DR GO; GO:0090148; P:membrane fission; IMP:UniProtKB. DR GO; GO:0061024; P:membrane organization; IBA:GO_Central. DR GO; GO:0006654; P:phosphatidic acid biosynthetic process; IEA:Ensembl. DR GO; GO:2000786; P:positive regulation of autophagosome assembly; IMP:UniProtKB. DR GO; GO:0010508; P:positive regulation of autophagy; IMP:UniProtKB. DR GO; GO:1903527; P:positive regulation of membrane tubulation; IMP:UniProtKB. DR GO; GO:1903955; P:positive regulation of protein targeting to mitochondrion; HMP:ParkinsonsUK-UCL. DR GO; GO:0031334; P:positive regulation of protein-containing complex assembly; IDA:UniProtKB. DR GO; GO:1903778; P:protein localization to vacuolar membrane; IMP:UniProtKB. DR GO; GO:0032801; P:receptor catabolic process; IMP:UniProtKB. DR GO; GO:0032465; P:regulation of cytokinesis; IMP:UniProtKB. DR GO; GO:0016241; P:regulation of macroautophagy; TAS:ParkinsonsUK-UCL. DR GO; GO:0031647; P:regulation of protein stability; HMP:ParkinsonsUK-UCL. DR CDD; cd07616; BAR_Endophilin_B1; 1. DR CDD; cd11945; SH3_Endophilin_B1; 1. DR FunFam; 1.20.1270.60:FF:000017; endophilin-B2 isoform X1; 1. DR FunFam; 2.30.30.40:FF:000028; endophilin-B2 isoform X1; 1. DR Gene3D; 1.20.1270.60; Arfaptin homology (AH) domain/BAR domain; 1. DR Gene3D; 2.30.30.40; SH3 Domains; 1. DR InterPro; IPR027267; AH/BAR_dom_sf. DR InterPro; IPR004148; BAR_dom. DR InterPro; IPR050384; Endophilin_SH3RF. DR InterPro; IPR036028; SH3-like_dom_sf. DR InterPro; IPR001452; SH3_domain. DR InterPro; IPR035695; SH3GLB1_BAR. DR InterPro; IPR028503; SH3GLB_SH3. DR PANTHER; PTHR14167:SF52; ENDOPHILIN-B1; 1. DR PANTHER; PTHR14167; SH3 DOMAIN-CONTAINING; 1. DR Pfam; PF03114; BAR; 1. DR Pfam; PF14604; SH3_9; 1. DR SMART; SM00721; BAR; 1. DR SMART; SM00326; SH3; 1. DR SUPFAM; SSF103657; BAR/IMD domain-like; 1. DR SUPFAM; SSF50044; SH3-domain; 1. DR PROSITE; PS51021; BAR; 1. DR PROSITE; PS50002; SH3; 1. PE 1: Evidence at protein level; KW 3D-structure; Acetylation; Alternative splicing; Apoptosis; Autophagy; KW Coiled coil; Cytoplasm; Cytoplasmic vesicle; Golgi apparatus; KW Lipid-binding; Membrane; Mitochondrion; Mitochondrion outer membrane; KW Phosphoprotein; Proteomics identification; Reference proteome; SH3 domain. FT CHAIN 1..365 FT /note="Endophilin-B1" FT /id="PRO_0000146753" FT DOMAIN 27..261 FT /note="BAR" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00361" FT DOMAIN 305..365 FT /note="SH3" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00192" FT REGION 1..37 FT /note="Required for membrane binding" FT /evidence="ECO:0000269|PubMed:21068542" FT REGION 1..30 FT /note="Membrane-binding amphipathic helix" FT COILED 155..195 FT /evidence="ECO:0000255" FT MOD_RES 1 FT /note="N-acetylmethionine" FT /evidence="ECO:0007744|PubMed:22814378" FT MOD_RES 145 FT /note="Phosphothreonine; by CDK5" FT /evidence="ECO:0000269|PubMed:21499257" FT VAR_SEQ 1..100 FT /note="Missing (in isoform 3)" FT /evidence="ECO:0000303|PubMed:14702039" FT /id="VSP_044895" FT VAR_SEQ 190 FT /note="S -> SQLNSARLEGDNIMIWAEEVTK (in isoform 2)" FT /evidence="ECO:0000303|PubMed:12456676" FT /id="VSP_009276" FT MUTAGEN 8 FT /note="V->M: Abolishes interaction with BAX." FT /evidence="ECO:0000269|PubMed:11161816" FT MUTAGEN 145 FT /note="T->A: Reduced CDK5-mediated phosphorylation and FT impaired dimerization." FT /evidence="ECO:0000269|PubMed:21499257" FT MUTAGEN 145 FT /note="T->E: Spontaneous dimerization." FT /evidence="ECO:0000269|PubMed:21499257" FT HELIX 12..30 FT /evidence="ECO:0007829|PDB:9G2U" FT STRAND 31..33 FT /evidence="ECO:0007829|PDB:9G2U" FT HELIX 40..67 FT /evidence="ECO:0007829|PDB:9G2U" FT HELIX 71..75 FT /evidence="ECO:0007829|PDB:9G2U" FT HELIX 93..108 FT /evidence="ECO:0007829|PDB:9G2U" FT STRAND 110..112 FT /evidence="ECO:0007829|PDB:9G2U" FT HELIX 113..142 FT /evidence="ECO:0007829|PDB:9G2U" FT HELIX 144..153 FT /evidence="ECO:0007829|PDB:9G2U" FT HELIX 155..180 FT /evidence="ECO:0007829|PDB:9G2U" FT HELIX 185..251 FT /evidence="ECO:0007829|PDB:9G2U" SQ SEQUENCE 365 AA; 40796 MW; 42C2AEA57A0B350E CRC64; MNIMDFNVKK LAADAGTFLS RAVQFTEEKL GQAEKTELDA HLENLLSKAE CTKIWTEKIM KQTEVLLQPN PNARIEEFVY EKLDRKAPSR INNPELLGQY MIDAGTEFGP GTAYGNALIK CGETQKRIGT ADRELIQTSA LNFLTPLRNF IEGDYKTIAK ERKLLQNKRL DLDAAKTRLK KAKAAETRNS SEQELRITQS EFDRQAEITR LLLEGISSTH AHHLRCLNDF VEAQMTYYAQ CYQYMLDLQK QLGSFPSNYL SNNNQTSVTP VPSVLPNAIG SSAMASTSGL VITSPSNLSD LKECSGSRKA RVLYDYDAAN STELSLLADE VITVFSVVGM DSDWLMGERG NQKGKVPITY LELLN //