Full text data of SH3GLB1
SH3GLB1
(KIAA0491)
[Confidence: low (only semi-automatic identification from reviews)]
Endophilin-B1 (Bax-interacting factor 1; Bif-1; SH3 domain-containing GRB2-like protein B1)
Endophilin-B1 (Bax-interacting factor 1; Bif-1; SH3 domain-containing GRB2-like protein B1)
UniProt
Q9Y371
ID SHLB1_HUMAN Reviewed; 365 AA.
AC Q9Y371; B4E182; Q5H8U5; Q9H3Z0; Q9NR47; Q9NYA9;
DT 16-JAN-2004, integrated into UniProtKB/Swiss-Prot.
read moreDT 01-NOV-1999, sequence version 1.
DT 22-JAN-2014, entry version 120.
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;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, MUTAGENESIS OF
RP VAL-8, INTERACTION 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
RT domain.";
RL Genomics 71:222-234(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), INTERACTION WITH BAX, AND
RP TISSUE 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.,
RA Wu C., Singh S., Wang H.-G.;
RT "Molecular cloning and characterization of Bif-1. A novel Src homology
RT 3 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-
RT associated lysophosphatidic acid acyl transferase with properties
RT distinct from 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
RT from 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.,
RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA 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.,
RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA Nakai K., Yada T., Nakamura Y., Ohara O., 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.,
RA Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A.,
RA Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F.,
RA McDonald L., Evans R., Phillips K., Atkinson A., Cooper R., Jones C.,
RA Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P.,
RA Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K.,
RA Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G.,
RA Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D.,
RA Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G.,
RA Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J.,
RA 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.,
RA Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D.,
RA Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G.,
RA Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M.,
RA Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J.,
RA Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M.,
RA Loveland J., Lovell J., Lush M.J., Lyne R., Martin S.,
RA Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S.,
RA 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.,
RA Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z.,
RA Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E.,
RA Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A.,
RA Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R.,
RA Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V.,
RA 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
RT project: 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 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.,
RA Buerckstuemmer T., 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 [12]
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
RT induced autophagy in models of Parkinson's disease.";
RL Nat. Cell Biol. 13:568-579(2011).
RN [13]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND MASS SPECTROMETRY.
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.,
RA Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K.,
RA Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-
RT terminal acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
CC -!- FUNCTION: May be required for normal outer mitochondrial membrane
CC dynamics. Required for coatomer-mediated retrograde transport in
CC certain cells. May recruit other proteins to membranes with high
CC curvature. May promote membrane fusion.
CC -!- SUBUNIT: Binds DNM1, HTT, AMPH, BIN1 and ARFGAP1 (By similarity).
CC Homodimer, and heterodimer with SH3GLB2. Binds BAX. Induction of
CC apoptosis augments BAX binding.
CC -!- INTERACTION:
CC Self; NbExp=4; IntAct=EBI-2623095, EBI-2623095;
CC Q07812:BAX; NbExp=2; IntAct=EBI-5291808, EBI-516580;
CC P24522:GADD45A; NbExp=2; IntAct=EBI-2623095, EBI-448167;
CC Q9NR46:SH3GLB2; NbExp=5; IntAct=EBI-2623095, EBI-749607;
CC Q9P2Y5:UVRAG; NbExp=2; IntAct=EBI-2623095, EBI-2952704;
CC -!- SUBCELLULAR LOCATION: Cytoplasm. Golgi apparatus membrane;
CC Peripheral membrane protein (By similarity). Mitochondrion outer
CC membrane; Peripheral membrane protein. Note=Association with the
CC Golgi apparatus depends on the cell type (By similarity).
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 Note=No experimental confirmation available;
CC -!- TISSUE SPECIFICITY: Highly expressed in heart, skeletal muscle,
CC kidney and placenta. Detected at lower levels in brain, colon,
CC thymus, spleen, liver, small intestine, lung and peripheral blood
CC leukocytes.
CC -!- DOMAIN: An N-terminal amphipathic helix, the BAR domain and a
CC second amphipathic helix inserted into helix 1 of the BAR domain
CC (N-BAR domain) induce membrane curvature and bind curved
CC membranes.
CC -!- PTM: Phosphorylated at Thr-145 by CDK5; this phosphorylation is
CC required for autophagy induction in starved neurons and
CC facilitates homodimerization.
CC -!- MISCELLANEOUS: HeLa cells lacking SH3GLB1 show dissociation of
CC outer and inner mitochondrial membrane as well as abnormal
CC mitochondrial morphology. Cells overexpressing SH3GLB1 lacking an
CC N-terminal amphipathic helix show a similar phenotype.
CC -!- MISCELLANEOUS: SH3GLB1 binds liposomes and induces formation of
CC tubules from liposomes. SH3GLB1 lacking the N-terminal amphipathic
CC helix fails to induce liposome tubulation.
CC -!- SIMILARITY: Belongs to the endophilin family.
CC -!- SIMILARITY: Contains 1 BAR domain.
CC -!- SIMILARITY: Contains 1 SH3 domain.
CC -!- CAUTION: It is uncertain whether Met-1 or Met-4 is the initiator.
CC -!- CAUTION: Was originally (PubMed:12456676) thought to have
CC lysophosphatidic acid acyltransferase activity, but by homology
CC with SH3GL2/endophilin A1 is unlikely to have this activity.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAF81225.1; Type=Erroneous initiation;
CC Sequence=BAD88797.1; Type=Erroneous initiation;
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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; CAC10394.1; -; Genomic_DNA.
DR EMBL; AL049597; CAC10395.1; -; Genomic_DNA.
DR EMBL; BC007455; AAH07455.1; -; mRNA.
DR RefSeq; NP_001193580.1; NM_001206651.1.
DR RefSeq; NP_001193581.1; NM_001206652.1.
DR RefSeq; NP_001193582.1; NM_001206653.1.
DR RefSeq; NP_057093.1; NM_016009.4.
DR UniGene; Hs.136309; -.
DR ProteinModelPortal; Q9Y371; -.
DR SMR; Q9Y371; 21-252, 293-365.
DR IntAct; Q9Y371; 38.
DR MINT; MINT-192077; -.
DR STRING; 9606.ENSP00000212369; -.
DR PhosphoSite; Q9Y371; -.
DR DMDM; 41018158; -.
DR REPRODUCTION-2DPAGE; IPI00006558; -.
DR PaxDb; Q9Y371; -.
DR PRIDE; Q9Y371; -.
DR DNASU; 51100; -.
DR Ensembl; ENST00000370558; ENSP00000473267; ENSG00000097033.
DR Ensembl; ENST00000482504; ENSP00000418744; ENSG00000097033.
DR Ensembl; ENST00000535010; ENSP00000441355; ENSG00000097033.
DR GeneID; 51100; -.
DR KEGG; hsa:51100; -.
DR UCSC; uc001dlw.3; human.
DR CTD; 51100; -.
DR GeneCards; GC01P087170; -.
DR HGNC; HGNC:10833; SH3GLB1.
DR HPA; CAB004650; -.
DR HPA; HPA015608; -.
DR HPA; HPA019900; -.
DR MIM; 609287; gene.
DR neXtProt; NX_Q9Y371; -.
DR PharmGKB; PA35739; -.
DR eggNOG; NOG309804; -.
DR HOGENOM; HOG000232056; -.
DR HOVERGEN; HBG054448; -.
DR KO; K11248; -.
DR OMA; RITQSEF; -.
DR OrthoDB; EOG744T9N; -.
DR SignaLink; Q9Y371; -.
DR ChiTaRS; SH3GLB1; human.
DR GeneWiki; SH3GLB1; -.
DR GenomeRNAi; 51100; -.
DR NextBio; 53809; -.
DR PRO; PR:Q9Y371; -.
DR Bgee; Q9Y371; -.
DR CleanEx; HS_SH3GLB1; -.
DR Genevestigator; Q9Y371; -.
DR GO; GO:0005737; C:cytoplasm; IDA:HGNC.
DR GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005741; C:mitochondrial outer membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0043234; C:protein complex; IEA:Ensembl.
DR GO; GO:0005504; F:fatty acid binding; IEA:Ensembl.
DR GO; GO:0042171; F:lysophosphatidic acid acyltransferase activity; IEA:Ensembl.
DR GO; GO:0051084; P:'de novo' posttranslational protein folding; IEA:Ensembl.
DR GO; GO:0006915; P:apoptotic process; IEA:UniProtKB-KW.
DR GO; GO:0006654; P:phosphatidic acid biosynthetic process; IEA:Ensembl.
DR GO; GO:1900740; P:positive regulation of protein insertion into mitochondrial membrane involved in apoptotic signaling pathway; IEA:Ensembl.
DR GO; GO:0032461; P:positive regulation of protein oligomerization; IDA:UniProtKB.
DR GO; GO:0051259; P:protein oligomerization; IDA:UniProtKB.
DR Gene3D; 1.20.1270.60; -; 1.
DR InterPro; IPR027267; AH/BAR-dom.
DR InterPro; IPR004148; BAR_dom.
DR InterPro; IPR001452; SH3_domain.
DR InterPro; IPR028503; SH3GLB1.
DR PANTHER; PTHR10661:SF15; PTHR10661:SF15; 1.
DR Pfam; PF03114; BAR; 1.
DR SMART; SM00721; BAR; 1.
DR SMART; SM00326; SH3; 1.
DR SUPFAM; SSF50044; SSF50044; 2.
DR PROSITE; PS51021; BAR; 1.
DR PROSITE; PS50002; SH3; 1.
PE 1: Evidence at protein level;
KW Acetylation; Alternative splicing; Apoptosis; Coiled coil;
KW Complete proteome; Cytoplasm; Golgi apparatus; Lipid-binding;
KW Membrane; Mitochondrion; Mitochondrion outer membrane; Phosphoprotein;
KW Reference proteome; SH3 domain.
FT CHAIN 1 365 Endophilin-B1.
FT /FTId=PRO_0000146753.
FT DOMAIN 27 261 BAR.
FT DOMAIN 305 365 SH3.
FT REGION 1 30 Membrane-binding amphipathic helix.
FT COILED 155 195 Potential.
FT MOD_RES 1 1 N-acetylmethionine.
FT MOD_RES 145 145 Phosphothreonine; by CDK5.
FT VAR_SEQ 1 100 Missing (in isoform 3).
FT /FTId=VSP_044895.
FT VAR_SEQ 190 190 S -> SQLNSARLEGDNIMIWAEEVTK (in isoform
FT 2).
FT /FTId=VSP_009276.
FT MUTAGEN 8 8 V->M: Abolishes interaction with BAX.
FT MUTAGEN 145 145 T->A: Reduced CDK5-mediated
FT phosphorylation and impaired
FT dimerization.
FT MUTAGEN 145 145 T->E: Spontaneous dimerization.
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
//
ID SHLB1_HUMAN Reviewed; 365 AA.
AC Q9Y371; B4E182; Q5H8U5; Q9H3Z0; Q9NR47; Q9NYA9;
DT 16-JAN-2004, integrated into UniProtKB/Swiss-Prot.
read moreDT 01-NOV-1999, sequence version 1.
DT 22-JAN-2014, entry version 120.
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;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, MUTAGENESIS OF
RP VAL-8, INTERACTION 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
RT domain.";
RL Genomics 71:222-234(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), INTERACTION WITH BAX, AND
RP TISSUE 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.,
RA Wu C., Singh S., Wang H.-G.;
RT "Molecular cloning and characterization of Bif-1. A novel Src homology
RT 3 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-
RT associated lysophosphatidic acid acyl transferase with properties
RT distinct from 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
RT from 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.,
RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA 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.,
RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA Nakai K., Yada T., Nakamura Y., Ohara O., 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.,
RA Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A.,
RA Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F.,
RA McDonald L., Evans R., Phillips K., Atkinson A., Cooper R., Jones C.,
RA Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P.,
RA Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K.,
RA Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G.,
RA Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D.,
RA Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G.,
RA Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J.,
RA 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.,
RA Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D.,
RA Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G.,
RA Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M.,
RA Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J.,
RA Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M.,
RA Loveland J., Lovell J., Lush M.J., Lyne R., Martin S.,
RA Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S.,
RA 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.,
RA Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z.,
RA Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E.,
RA Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A.,
RA Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R.,
RA Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V.,
RA 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
RT project: 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 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.,
RA Buerckstuemmer T., 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 [12]
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
RT induced autophagy in models of Parkinson's disease.";
RL Nat. Cell Biol. 13:568-579(2011).
RN [13]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND MASS SPECTROMETRY.
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.,
RA Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K.,
RA Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-
RT terminal acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
CC -!- FUNCTION: May be required for normal outer mitochondrial membrane
CC dynamics. Required for coatomer-mediated retrograde transport in
CC certain cells. May recruit other proteins to membranes with high
CC curvature. May promote membrane fusion.
CC -!- SUBUNIT: Binds DNM1, HTT, AMPH, BIN1 and ARFGAP1 (By similarity).
CC Homodimer, and heterodimer with SH3GLB2. Binds BAX. Induction of
CC apoptosis augments BAX binding.
CC -!- INTERACTION:
CC Self; NbExp=4; IntAct=EBI-2623095, EBI-2623095;
CC Q07812:BAX; NbExp=2; IntAct=EBI-5291808, EBI-516580;
CC P24522:GADD45A; NbExp=2; IntAct=EBI-2623095, EBI-448167;
CC Q9NR46:SH3GLB2; NbExp=5; IntAct=EBI-2623095, EBI-749607;
CC Q9P2Y5:UVRAG; NbExp=2; IntAct=EBI-2623095, EBI-2952704;
CC -!- SUBCELLULAR LOCATION: Cytoplasm. Golgi apparatus membrane;
CC Peripheral membrane protein (By similarity). Mitochondrion outer
CC membrane; Peripheral membrane protein. Note=Association with the
CC Golgi apparatus depends on the cell type (By similarity).
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 Note=No experimental confirmation available;
CC -!- TISSUE SPECIFICITY: Highly expressed in heart, skeletal muscle,
CC kidney and placenta. Detected at lower levels in brain, colon,
CC thymus, spleen, liver, small intestine, lung and peripheral blood
CC leukocytes.
CC -!- DOMAIN: An N-terminal amphipathic helix, the BAR domain and a
CC second amphipathic helix inserted into helix 1 of the BAR domain
CC (N-BAR domain) induce membrane curvature and bind curved
CC membranes.
CC -!- PTM: Phosphorylated at Thr-145 by CDK5; this phosphorylation is
CC required for autophagy induction in starved neurons and
CC facilitates homodimerization.
CC -!- MISCELLANEOUS: HeLa cells lacking SH3GLB1 show dissociation of
CC outer and inner mitochondrial membrane as well as abnormal
CC mitochondrial morphology. Cells overexpressing SH3GLB1 lacking an
CC N-terminal amphipathic helix show a similar phenotype.
CC -!- MISCELLANEOUS: SH3GLB1 binds liposomes and induces formation of
CC tubules from liposomes. SH3GLB1 lacking the N-terminal amphipathic
CC helix fails to induce liposome tubulation.
CC -!- SIMILARITY: Belongs to the endophilin family.
CC -!- SIMILARITY: Contains 1 BAR domain.
CC -!- SIMILARITY: Contains 1 SH3 domain.
CC -!- CAUTION: It is uncertain whether Met-1 or Met-4 is the initiator.
CC -!- CAUTION: Was originally (PubMed:12456676) thought to have
CC lysophosphatidic acid acyltransferase activity, but by homology
CC with SH3GL2/endophilin A1 is unlikely to have this activity.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAF81225.1; Type=Erroneous initiation;
CC Sequence=BAD88797.1; Type=Erroneous initiation;
CC -----------------------------------------------------------------------
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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; CAC10394.1; -; Genomic_DNA.
DR EMBL; AL049597; CAC10395.1; -; Genomic_DNA.
DR EMBL; BC007455; AAH07455.1; -; mRNA.
DR RefSeq; NP_001193580.1; NM_001206651.1.
DR RefSeq; NP_001193581.1; NM_001206652.1.
DR RefSeq; NP_001193582.1; NM_001206653.1.
DR RefSeq; NP_057093.1; NM_016009.4.
DR UniGene; Hs.136309; -.
DR ProteinModelPortal; Q9Y371; -.
DR SMR; Q9Y371; 21-252, 293-365.
DR IntAct; Q9Y371; 38.
DR MINT; MINT-192077; -.
DR STRING; 9606.ENSP00000212369; -.
DR PhosphoSite; Q9Y371; -.
DR DMDM; 41018158; -.
DR REPRODUCTION-2DPAGE; IPI00006558; -.
DR PaxDb; Q9Y371; -.
DR PRIDE; Q9Y371; -.
DR DNASU; 51100; -.
DR Ensembl; ENST00000370558; ENSP00000473267; ENSG00000097033.
DR Ensembl; ENST00000482504; ENSP00000418744; ENSG00000097033.
DR Ensembl; ENST00000535010; ENSP00000441355; ENSG00000097033.
DR GeneID; 51100; -.
DR KEGG; hsa:51100; -.
DR UCSC; uc001dlw.3; human.
DR CTD; 51100; -.
DR GeneCards; GC01P087170; -.
DR HGNC; HGNC:10833; SH3GLB1.
DR HPA; CAB004650; -.
DR HPA; HPA015608; -.
DR HPA; HPA019900; -.
DR MIM; 609287; gene.
DR neXtProt; NX_Q9Y371; -.
DR PharmGKB; PA35739; -.
DR eggNOG; NOG309804; -.
DR HOGENOM; HOG000232056; -.
DR HOVERGEN; HBG054448; -.
DR KO; K11248; -.
DR OMA; RITQSEF; -.
DR OrthoDB; EOG744T9N; -.
DR SignaLink; Q9Y371; -.
DR ChiTaRS; SH3GLB1; human.
DR GeneWiki; SH3GLB1; -.
DR GenomeRNAi; 51100; -.
DR NextBio; 53809; -.
DR PRO; PR:Q9Y371; -.
DR Bgee; Q9Y371; -.
DR CleanEx; HS_SH3GLB1; -.
DR Genevestigator; Q9Y371; -.
DR GO; GO:0005737; C:cytoplasm; IDA:HGNC.
DR GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005741; C:mitochondrial outer membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0043234; C:protein complex; IEA:Ensembl.
DR GO; GO:0005504; F:fatty acid binding; IEA:Ensembl.
DR GO; GO:0042171; F:lysophosphatidic acid acyltransferase activity; IEA:Ensembl.
DR GO; GO:0051084; P:'de novo' posttranslational protein folding; IEA:Ensembl.
DR GO; GO:0006915; P:apoptotic process; IEA:UniProtKB-KW.
DR GO; GO:0006654; P:phosphatidic acid biosynthetic process; IEA:Ensembl.
DR GO; GO:1900740; P:positive regulation of protein insertion into mitochondrial membrane involved in apoptotic signaling pathway; IEA:Ensembl.
DR GO; GO:0032461; P:positive regulation of protein oligomerization; IDA:UniProtKB.
DR GO; GO:0051259; P:protein oligomerization; IDA:UniProtKB.
DR Gene3D; 1.20.1270.60; -; 1.
DR InterPro; IPR027267; AH/BAR-dom.
DR InterPro; IPR004148; BAR_dom.
DR InterPro; IPR001452; SH3_domain.
DR InterPro; IPR028503; SH3GLB1.
DR PANTHER; PTHR10661:SF15; PTHR10661:SF15; 1.
DR Pfam; PF03114; BAR; 1.
DR SMART; SM00721; BAR; 1.
DR SMART; SM00326; SH3; 1.
DR SUPFAM; SSF50044; SSF50044; 2.
DR PROSITE; PS51021; BAR; 1.
DR PROSITE; PS50002; SH3; 1.
PE 1: Evidence at protein level;
KW Acetylation; Alternative splicing; Apoptosis; Coiled coil;
KW Complete proteome; Cytoplasm; Golgi apparatus; Lipid-binding;
KW Membrane; Mitochondrion; Mitochondrion outer membrane; Phosphoprotein;
KW Reference proteome; SH3 domain.
FT CHAIN 1 365 Endophilin-B1.
FT /FTId=PRO_0000146753.
FT DOMAIN 27 261 BAR.
FT DOMAIN 305 365 SH3.
FT REGION 1 30 Membrane-binding amphipathic helix.
FT COILED 155 195 Potential.
FT MOD_RES 1 1 N-acetylmethionine.
FT MOD_RES 145 145 Phosphothreonine; by CDK5.
FT VAR_SEQ 1 100 Missing (in isoform 3).
FT /FTId=VSP_044895.
FT VAR_SEQ 190 190 S -> SQLNSARLEGDNIMIWAEEVTK (in isoform
FT 2).
FT /FTId=VSP_009276.
FT MUTAGEN 8 8 V->M: Abolishes interaction with BAX.
FT MUTAGEN 145 145 T->A: Reduced CDK5-mediated
FT phosphorylation and impaired
FT dimerization.
FT MUTAGEN 145 145 T->E: Spontaneous dimerization.
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
//
MIM
609287
*RECORD*
*FIELD* NO
609287
*FIELD* TI
*609287 SH3 DOMAIN, GRB2-LIKE, ENDOPHILIN B1; SH3GLB1
;;ENDOPHILIN B1;;
BAX-INTERACTING FACTOR 1; BIF1;;
read moreKIAA0491
*FIELD* TX
CLONING
Using BAX (600040) as bait in a yeast 2-hybrid screen of a skeletal
muscle cDNA library, Pierrat et al. (2001) cloned SH3GLB1. The deduced
362-amino acid protein contains an N-terminal domain, a central
coiled-coil region, and a C-terminal SH3 domain. SH3GLB1 shares 65%
amino acid identity with SH3GLB2 (609288). Northern blot analysis
detected a major 1.9-kb transcript and a minor 1.7-kb transcript in most
tissues examined, with higher levels in heart, placenta, and skeletal
muscle. Osteosarcoma and HeLa cells transfected with SH3GLB1 expressed
the protein in the cytoplasm, but it was excluded from the nucleus.
Cuddeback et al. (2001) cloned SH3GLB1, which they called BIF1, using
BAX as bait in a yeast 2-hybrid screen of a brain cDNA library. The
deduced protein contains 365 amino acids. Northern blot analysis
revealed abundant expression in heart, skeletal muscle, kidney, and
placenta. Transcripts of 1.5, 2.0, and 6.0 kb were detected.
Fluorescence-tagged SH3GLB1 showed a cytoplasmic distribution, and a
proportion of the protein associated with mitochondria.
Modregger et al. (2003) cloned several variants of mouse Sh3glb1, which
they called endophilin B1. The deduced proteins range from 365 to 386
residues in length. The N-terminal domain of endophilin B1 shares
highest similarity with the lipid-binding and -modifying (LBM) domain of
class A endophilins (see SH3GL2; 604465), which mediates
lysophosphatidic acid (LPA) acyltransferase activity, liposome binding,
and tubulation. Northern blot analysis detected transcripts of 2.6, 5.0,
6.5, and 8.0 kb that were generated by alternative splicing and the use
of alternate polyadenylation signals. Two brain-specific transcripts,
designated endophilins B1b and B1c, differ in the 3-prime exon 6 splice
site. The ubiquitously expressed transcript, endophilin B1a, lacks exons
6 and 7. Western blot analysis detected a 40-kD protein in most mouse
tissues, a 42-kD protein in brain only, and a 43-kD protein in lung and
spleen only. Confocal microscopy detected epitope-tagged endophilin B1b
in a reticular pattern throughout the cytoplasm. Endophilin B1b
associated with membranes in fractionated mouse brain homogenates.
GENE FUNCTION
Using SH3GLB1 truncation mutants, Pierrat et al. (2001) determined that
the first 42 N-terminal amino acids of SH3GLB1, and not the SH3 domain,
were required for its interaction with BAX, and a point mutation at val5
of SH3GLB1 abrogated the interaction. SH3GLB1 could form homodimers and
heterodimers with SH3GLB2. Mutation analysis indicated that the
coiled-coil region between amino acids 153 and 183 was required for
homo- and heterodimer formation. SH3GLB1 overexpression in HeLa and
human embryonic kidney cells had a general weak protective effect (5 to
10%) against cell death induced by BAX overexpression, FAS ligand
(TNFSF6; 134638), and chemical agents.
By yeast 2-hybrid analysis, Cuddeback et al. (2001) confirmed a direct
interaction between SH3GLB1 and BAX. Immunoprecipitation analysis
detected an endogenous interaction between Sh3glb1 and Bax in a mouse
hematopoietic cell line. Induction of apoptosis by interleukin-3 (IL3;
147740) withdrawal increased the association of Bax with Sh3glb1, and
this was accompanied by a conformational change in the Bax protein.
Overexpression of Sh3glb1 promoted Bax conformational change, caspase
activation, and apoptotic cell death in mouse hematopoietic cells
following IL3 deprivation.
Modregger et al. (2003) found that immobilized mouse endophilin B1 bound
dynamin (see 602378), huntingtin (HTT; 613004), and 2 amphiphysins (see
600418) in mouse brain detergent extracts. It did not bind
synaptojanin-1 (SYNJ1; 604297). Yeast 2-hybrid analysis confirmed that
endophilin B1b interacts with dynamin and huntingtin, and the SH3 domain
of endophilin B1b was sufficient for these interactions. Endophilin B1b
also interacted with itself, and this self-interaction required the
N-terminal LBM domain and the coiled-coil region. Endophilin B1b
expressed in mouse fibroblasts bound palmitoyl-CoA.
Gallop et al. (2005) found that the LPA acyltransferase, or LPAAT,
activity associated with endophilin (e.g., Modregger et al., 2003) is a
contaminant of the purification procedure and could also be found
associated with the pleckstrin homology domain of dynamin.
Karbowski et al. (2004) found that knockdown of endophilin B1 in HeLa
cells by RNA interference led to changes in mitochondrial shape,
formation of vesicular structures continuous with mitochondria, and a
separation of the outer and inner mitochondrial membrane compartments.
Overexpression of endophilin B1 lacking the N-terminal LBM domain caused
similar changes. Endophilin B1 translocated to mitochondria during
synchronous remodeling of the mitochondrial network during apoptosis.
Double knockdown of endophilin B1 and DRP1 (DNM1L; 602462) led to a
mitochondrial phenotype identical to that of DRP1 single knockdown.
Karbowski et al. (2004) concluded that endophilin B1 is required for the
maintenance of mitochondria and that DRP1 acts upstream of endophilin
B1.
GENE STRUCTURE
Modregger et al. (2003) determined that the SH3GLB1 gene contains 11
exons.
MAPPING
By genomic sequence analysis, Modregger et al. (2003) mapped the SH3GLB1
gene to chromosome 1p31.1-p22.2.
MOLECULAR GENETICS
Kim et al. (2008) detected only 1 somatic mutation in the BIF1 gene
among 284 human cancer tissues of various origin. They concluded that
BIF1 mutation is rare in cancers.
*FIELD* RF
1. Cuddeback, S. M.; Yamaguchi, H.; Komatsu, K.; Miyashita, T.; Yamada,
M.; Wu, C.; Singh, S.; Wang, H.-G.: Molecular cloning and characterization
of Bif-1: a novel Src homology 3 domain-containing protein that associates
with Bax. J. Biol. Chem. 276: 20559-20565, 2001.
2. Gallop, J. L.; Butler, P. J. G.; McMahon, H. T.: Endophilin and
CtBP/BARS are not acyl transferases in endocytosis or Golgi fission. Nature 438:
675-678, 2005.
3. Karbowski, M.; Jeong, S.-Y.; Youle, R. J.: Endophilin B1 is required
for the maintenance of mitochondrial morphology. J. Cell Biol. 166:
1027-1039, 2004.
4. Kim, M. S.; Yoo, N. J.; Lee, S. H.: Somatic mutation of pro-cell
death Bif-1 gene is rare in common human cancers. (Letter) APMIS 116:
939-940, 2008.
5. Modregger, J.; Schmidt, A. A.; Ritter, B.; Huttner, W. B.; Plomann,
M.: Characterization of endophilin B1b, a brain-specific membrane-associated
lysophosphatidic acid acyl transferase with properties distinct from
endophilin A1. J. Biol. Chem. 278: 4160-4167, 2003.
6. Pierrat, B.; Simonen, M.; Cueto, M.; Mestan, J.; Ferrigno, P.;
Heim, J.: SH3GLB, a new endophilin-related protein family featuring
an SH3 domain. Genomics 71: 222-234, 2001.
*FIELD* CN
Matthew B. Gross - updated: 06/28/2011
*FIELD* CD
Patricia A. Hartz: 3/31/2005
*FIELD* ED
mgross: 06/28/2011
wwang: 9/15/2009
alopez: 2/1/2006
mgross: 3/31/2005
*RECORD*
*FIELD* NO
609287
*FIELD* TI
*609287 SH3 DOMAIN, GRB2-LIKE, ENDOPHILIN B1; SH3GLB1
;;ENDOPHILIN B1;;
BAX-INTERACTING FACTOR 1; BIF1;;
read moreKIAA0491
*FIELD* TX
CLONING
Using BAX (600040) as bait in a yeast 2-hybrid screen of a skeletal
muscle cDNA library, Pierrat et al. (2001) cloned SH3GLB1. The deduced
362-amino acid protein contains an N-terminal domain, a central
coiled-coil region, and a C-terminal SH3 domain. SH3GLB1 shares 65%
amino acid identity with SH3GLB2 (609288). Northern blot analysis
detected a major 1.9-kb transcript and a minor 1.7-kb transcript in most
tissues examined, with higher levels in heart, placenta, and skeletal
muscle. Osteosarcoma and HeLa cells transfected with SH3GLB1 expressed
the protein in the cytoplasm, but it was excluded from the nucleus.
Cuddeback et al. (2001) cloned SH3GLB1, which they called BIF1, using
BAX as bait in a yeast 2-hybrid screen of a brain cDNA library. The
deduced protein contains 365 amino acids. Northern blot analysis
revealed abundant expression in heart, skeletal muscle, kidney, and
placenta. Transcripts of 1.5, 2.0, and 6.0 kb were detected.
Fluorescence-tagged SH3GLB1 showed a cytoplasmic distribution, and a
proportion of the protein associated with mitochondria.
Modregger et al. (2003) cloned several variants of mouse Sh3glb1, which
they called endophilin B1. The deduced proteins range from 365 to 386
residues in length. The N-terminal domain of endophilin B1 shares
highest similarity with the lipid-binding and -modifying (LBM) domain of
class A endophilins (see SH3GL2; 604465), which mediates
lysophosphatidic acid (LPA) acyltransferase activity, liposome binding,
and tubulation. Northern blot analysis detected transcripts of 2.6, 5.0,
6.5, and 8.0 kb that were generated by alternative splicing and the use
of alternate polyadenylation signals. Two brain-specific transcripts,
designated endophilins B1b and B1c, differ in the 3-prime exon 6 splice
site. The ubiquitously expressed transcript, endophilin B1a, lacks exons
6 and 7. Western blot analysis detected a 40-kD protein in most mouse
tissues, a 42-kD protein in brain only, and a 43-kD protein in lung and
spleen only. Confocal microscopy detected epitope-tagged endophilin B1b
in a reticular pattern throughout the cytoplasm. Endophilin B1b
associated with membranes in fractionated mouse brain homogenates.
GENE FUNCTION
Using SH3GLB1 truncation mutants, Pierrat et al. (2001) determined that
the first 42 N-terminal amino acids of SH3GLB1, and not the SH3 domain,
were required for its interaction with BAX, and a point mutation at val5
of SH3GLB1 abrogated the interaction. SH3GLB1 could form homodimers and
heterodimers with SH3GLB2. Mutation analysis indicated that the
coiled-coil region between amino acids 153 and 183 was required for
homo- and heterodimer formation. SH3GLB1 overexpression in HeLa and
human embryonic kidney cells had a general weak protective effect (5 to
10%) against cell death induced by BAX overexpression, FAS ligand
(TNFSF6; 134638), and chemical agents.
By yeast 2-hybrid analysis, Cuddeback et al. (2001) confirmed a direct
interaction between SH3GLB1 and BAX. Immunoprecipitation analysis
detected an endogenous interaction between Sh3glb1 and Bax in a mouse
hematopoietic cell line. Induction of apoptosis by interleukin-3 (IL3;
147740) withdrawal increased the association of Bax with Sh3glb1, and
this was accompanied by a conformational change in the Bax protein.
Overexpression of Sh3glb1 promoted Bax conformational change, caspase
activation, and apoptotic cell death in mouse hematopoietic cells
following IL3 deprivation.
Modregger et al. (2003) found that immobilized mouse endophilin B1 bound
dynamin (see 602378), huntingtin (HTT; 613004), and 2 amphiphysins (see
600418) in mouse brain detergent extracts. It did not bind
synaptojanin-1 (SYNJ1; 604297). Yeast 2-hybrid analysis confirmed that
endophilin B1b interacts with dynamin and huntingtin, and the SH3 domain
of endophilin B1b was sufficient for these interactions. Endophilin B1b
also interacted with itself, and this self-interaction required the
N-terminal LBM domain and the coiled-coil region. Endophilin B1b
expressed in mouse fibroblasts bound palmitoyl-CoA.
Gallop et al. (2005) found that the LPA acyltransferase, or LPAAT,
activity associated with endophilin (e.g., Modregger et al., 2003) is a
contaminant of the purification procedure and could also be found
associated with the pleckstrin homology domain of dynamin.
Karbowski et al. (2004) found that knockdown of endophilin B1 in HeLa
cells by RNA interference led to changes in mitochondrial shape,
formation of vesicular structures continuous with mitochondria, and a
separation of the outer and inner mitochondrial membrane compartments.
Overexpression of endophilin B1 lacking the N-terminal LBM domain caused
similar changes. Endophilin B1 translocated to mitochondria during
synchronous remodeling of the mitochondrial network during apoptosis.
Double knockdown of endophilin B1 and DRP1 (DNM1L; 602462) led to a
mitochondrial phenotype identical to that of DRP1 single knockdown.
Karbowski et al. (2004) concluded that endophilin B1 is required for the
maintenance of mitochondria and that DRP1 acts upstream of endophilin
B1.
GENE STRUCTURE
Modregger et al. (2003) determined that the SH3GLB1 gene contains 11
exons.
MAPPING
By genomic sequence analysis, Modregger et al. (2003) mapped the SH3GLB1
gene to chromosome 1p31.1-p22.2.
MOLECULAR GENETICS
Kim et al. (2008) detected only 1 somatic mutation in the BIF1 gene
among 284 human cancer tissues of various origin. They concluded that
BIF1 mutation is rare in cancers.
*FIELD* RF
1. Cuddeback, S. M.; Yamaguchi, H.; Komatsu, K.; Miyashita, T.; Yamada,
M.; Wu, C.; Singh, S.; Wang, H.-G.: Molecular cloning and characterization
of Bif-1: a novel Src homology 3 domain-containing protein that associates
with Bax. J. Biol. Chem. 276: 20559-20565, 2001.
2. Gallop, J. L.; Butler, P. J. G.; McMahon, H. T.: Endophilin and
CtBP/BARS are not acyl transferases in endocytosis or Golgi fission. Nature 438:
675-678, 2005.
3. Karbowski, M.; Jeong, S.-Y.; Youle, R. J.: Endophilin B1 is required
for the maintenance of mitochondrial morphology. J. Cell Biol. 166:
1027-1039, 2004.
4. Kim, M. S.; Yoo, N. J.; Lee, S. H.: Somatic mutation of pro-cell
death Bif-1 gene is rare in common human cancers. (Letter) APMIS 116:
939-940, 2008.
5. Modregger, J.; Schmidt, A. A.; Ritter, B.; Huttner, W. B.; Plomann,
M.: Characterization of endophilin B1b, a brain-specific membrane-associated
lysophosphatidic acid acyl transferase with properties distinct from
endophilin A1. J. Biol. Chem. 278: 4160-4167, 2003.
6. Pierrat, B.; Simonen, M.; Cueto, M.; Mestan, J.; Ferrigno, P.;
Heim, J.: SH3GLB, a new endophilin-related protein family featuring
an SH3 domain. Genomics 71: 222-234, 2001.
*FIELD* CN
Matthew B. Gross - updated: 06/28/2011
*FIELD* CD
Patricia A. Hartz: 3/31/2005
*FIELD* ED
mgross: 06/28/2011
wwang: 9/15/2009
alopez: 2/1/2006
mgross: 3/31/2005