SHLB1_HUMAN
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 03-AUG-2022, entry version 190.
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 -!- INTERACTION:
CC Q9Y371; P45844-6: ABCG1; NbExp=3; IntAct=EBI-2623095, EBI-25873349;
CC Q9Y371; Q7Z5M8-2: ABHD12B; NbExp=3; IntAct=EBI-2623095, EBI-21854797;
CC Q9Y371; Q8WTS1: ABHD5; NbExp=3; IntAct=EBI-2623095, EBI-2813554;
CC Q9Y371; Q96CM8: ACSF2; NbExp=3; IntAct=EBI-2623095, EBI-2876502;
CC Q9Y371; O95994: AGR2; NbExp=3; IntAct=EBI-2623095, EBI-712648;
CC Q9Y371; Q6RW13-2: AGTRAP; NbExp=3; IntAct=EBI-2623095, EBI-11522760;
CC Q9Y371; Q96MA6: AK8; NbExp=3; IntAct=EBI-2623095, EBI-8466265;
CC Q9Y371; Q5T2L2: AKR1C8P; NbExp=3; IntAct=EBI-2623095, EBI-22006248;
CC Q9Y371; Q96Q83-2: ALKBH3; NbExp=3; IntAct=EBI-2623095, EBI-9089544;
CC Q9Y371; Q9NU02: ANKEF1; NbExp=3; IntAct=EBI-2623095, EBI-8464238;
CC Q9Y371; P02647: APOA1; NbExp=3; IntAct=EBI-2623095, EBI-701692;
CC Q9Y371; P06727: APOA4; NbExp=3; IntAct=EBI-2623095, EBI-1222447;
CC Q9Y371; P02749: APOH; NbExp=3; IntAct=EBI-2623095, EBI-2114682;
CC Q9Y371; P53365: ARFIP2; NbExp=6; IntAct=EBI-2623095, EBI-638194;
CC Q9Y371; P18848: ATF4; NbExp=3; IntAct=EBI-2623095, EBI-492498;
CC Q9Y371; C1IDX9: ATG12; NbExp=3; IntAct=EBI-2623095, EBI-25836940;
CC Q9Y371; O75964: ATP5MG; NbExp=3; IntAct=EBI-2623095, EBI-1044001;
CC Q9Y371; Q14032: BAAT; NbExp=3; IntAct=EBI-2623095, EBI-8994378;
CC Q9Y371; Q8WZ55: BSND; NbExp=3; IntAct=EBI-2623095, EBI-7996695;
CC Q9Y371; Q9NQ89: C12orf4; NbExp=3; IntAct=EBI-2623095, EBI-11090973;
CC Q9Y371; Q13901: C1D; NbExp=6; IntAct=EBI-2623095, EBI-3844053;
CC Q9Y371; Q8N1A6: C4orf33; NbExp=3; IntAct=EBI-2623095, EBI-10264911;
CC Q9Y371; Q9UGQ2: CACFD1; NbExp=3; IntAct=EBI-2623095, EBI-8652492;
CC Q9Y371; P20807-4: CAPN3; NbExp=3; IntAct=EBI-2623095, EBI-11532021;
CC Q9Y371; P24863: CCNC; NbExp=3; IntAct=EBI-2623095, EBI-395261;
CC Q9Y371; Q9UK58-5: CCNL1; NbExp=3; IntAct=EBI-2623095, EBI-25873837;
CC Q9Y371; P01730: CD4; NbExp=3; IntAct=EBI-2623095, EBI-353826;
CC Q9Y371; O15182: CETN3; NbExp=3; IntAct=EBI-2623095, EBI-712959;
CC Q9Y371; Q9UHD4: CIDEB; NbExp=3; IntAct=EBI-2623095, EBI-7062247;
CC Q9Y371; P09496-2: CLTA; NbExp=3; IntAct=EBI-2623095, EBI-4401010;
CC Q9Y371; Q96DZ9: CMTM5; NbExp=3; IntAct=EBI-2623095, EBI-2548702;
CC Q9Y371; Q96DZ9-2: CMTM5; NbExp=3; IntAct=EBI-2623095, EBI-11522780;
CC Q9Y371; Q8NI60: COQ8A; NbExp=11; IntAct=EBI-2623095, EBI-745535;
CC Q9Y371; Q9UGL9: CRCT1; NbExp=3; IntAct=EBI-2623095, EBI-713677;
CC Q9Y371; Q53TN4: CYBRD1; NbExp=3; IntAct=EBI-2623095, EBI-8637742;
CC Q9Y371; P10632: CYP2C8; NbExp=3; IntAct=EBI-2623095, EBI-2951522;
CC Q9Y371; Q9BSY9: DESI2; NbExp=3; IntAct=EBI-2623095, EBI-12878374;
CC Q9Y371; Q96LJ7: DHRS1; NbExp=3; IntAct=EBI-2623095, EBI-746300;
CC Q9Y371; Q96KC8: DNAJC1; NbExp=3; IntAct=EBI-2623095, EBI-296550;
CC Q9Y371; Q96BY6: DOCK10; NbExp=3; IntAct=EBI-2623095, EBI-748520;
CC Q9Y371; O00303: EIF3F; NbExp=3; IntAct=EBI-2623095, EBI-711990;
CC Q9Y371; O00472: ELL2; NbExp=3; IntAct=EBI-2623095, EBI-395274;
CC Q9Y371; O95278-6: EPM2A; NbExp=3; IntAct=EBI-2623095, EBI-25836908;
CC Q9Y371; Q9NRY5: FAM114A2; NbExp=3; IntAct=EBI-2623095, EBI-10973142;
CC Q9Y371; Q8N128-2: FAM177A1; NbExp=3; IntAct=EBI-2623095, EBI-12201693;
CC Q9Y371; Q8IZU1: FAM9A; NbExp=3; IntAct=EBI-2623095, EBI-8468186;
CC Q9Y371; Q9NYY8: FASTKD2; NbExp=3; IntAct=EBI-2623095, EBI-1055752;
CC Q9Y371; P02671-2: FGA; NbExp=3; IntAct=EBI-2623095, EBI-9640259;
CC Q9Y371; P49771-3: FLT3LG; NbExp=3; IntAct=EBI-2623095, EBI-25872794;
CC Q9Y371; Q8IVP5: FUNDC1; NbExp=3; IntAct=EBI-2623095, EBI-3059266;
CC Q9Y371; Q6P7E6: FUT6; NbExp=3; IntAct=EBI-2623095, EBI-25872807;
CC Q9Y371; P24522: GADD45A; NbExp=2; IntAct=EBI-2623095, EBI-448167;
CC Q9Y371; Q9H3K2: GHITM; NbExp=3; IntAct=EBI-2623095, EBI-2868909;
CC Q9Y371; Q8WWP7: GIMAP1; NbExp=3; IntAct=EBI-2623095, EBI-11991950;
CC Q9Y371; Q9HAV0: GNB4; NbExp=3; IntAct=EBI-2623095, EBI-358539;
CC Q9Y371; P32780: GTF2H1; NbExp=3; IntAct=EBI-2623095, EBI-715539;
CC Q9Y371; O75409: H2AP; NbExp=3; IntAct=EBI-2623095, EBI-6447217;
CC Q9Y371; Q6NXT2: H3-5; NbExp=3; IntAct=EBI-2623095, EBI-2868501;
CC Q9Y371; P68431: H3C12; NbExp=3; IntAct=EBI-2623095, EBI-79722;
CC Q9Y371; P53701: HCCS; NbExp=3; IntAct=EBI-2623095, EBI-10763431;
CC Q9Y371; Q9BUP3-3: HTATIP2; NbExp=3; IntAct=EBI-2623095, EBI-12937691;
CC Q9Y371; P0C870: JMJD7; NbExp=3; IntAct=EBI-2623095, EBI-9090173;
CC Q9Y371; Q9UK76: JPT1; NbExp=3; IntAct=EBI-2623095, EBI-720411;
CC Q9Y371; Q8N5Z5: KCTD17; NbExp=3; IntAct=EBI-2623095, EBI-743960;
CC Q9Y371; Q6DKI2: LGALS9C; NbExp=3; IntAct=EBI-2623095, EBI-9088829;
CC Q9Y371; Q5VYH9: LY9; NbExp=3; IntAct=EBI-2623095, EBI-25872860;
CC Q9Y371; P43361: MAGEA8; NbExp=3; IntAct=EBI-2623095, EBI-10182930;
CC Q9Y371; Q96M61: MAGEB18; NbExp=3; IntAct=EBI-2623095, EBI-741835;
CC Q9Y371; Q969L2: MAL2; NbExp=6; IntAct=EBI-2623095, EBI-944295;
CC Q9Y371; P27338: MAOB; NbExp=3; IntAct=EBI-2623095, EBI-3911344;
CC Q9Y371; Q8NI22: MCFD2; NbExp=3; IntAct=EBI-2623095, EBI-2689785;
CC Q9Y371; Q96C03-3: MIEF2; NbExp=3; IntAct=EBI-2623095, EBI-11988931;
CC Q9Y371; Q9BV20: MRI1; NbExp=3; IntAct=EBI-2623095, EBI-747381;
CC Q9Y371; Q8N387: MUC15; NbExp=3; IntAct=EBI-2623095, EBI-17937277;
CC Q9Y371; P01106: MYC; NbExp=3; IntAct=EBI-2623095, EBI-447544;
CC Q9Y371; Q9H7X0: NAA60; NbExp=3; IntAct=EBI-2623095, EBI-12260336;
CC Q9Y371; Q9UJ70-2: NAGK; NbExp=3; IntAct=EBI-2623095, EBI-11526455;
CC Q9Y371; Q69YL0: NCBP2AS2; NbExp=3; IntAct=EBI-2623095, EBI-10986258;
CC Q9Y371; P25208: NFYB; NbExp=3; IntAct=EBI-2623095, EBI-389728;
CC Q9Y371; O15130-2: NPFF; NbExp=3; IntAct=EBI-2623095, EBI-25840002;
CC Q9Y371; P27815-4: PDE4A; NbExp=3; IntAct=EBI-2623095, EBI-12080840;
CC Q9Y371; A5PLL7: PEDS1; NbExp=3; IntAct=EBI-2623095, EBI-11337896;
CC Q9Y371; Q00169: PITPNA; NbExp=3; IntAct=EBI-2623095, EBI-1042490;
CC Q9Y371; P48739: PITPNB; NbExp=3; IntAct=EBI-2623095, EBI-1047143;
CC Q9Y371; O60664: PLIN3; NbExp=3; IntAct=EBI-2623095, EBI-725795;
CC Q9Y371; Q14181: POLA2; NbExp=3; IntAct=EBI-2623095, EBI-712752;
CC Q9Y371; P02775: PPBP; NbExp=3; IntAct=EBI-2623095, EBI-718973;
CC Q9Y371; Q6ZMI0-5: PPP1R21; NbExp=3; IntAct=EBI-2623095, EBI-25835994;
CC Q9Y371; P23942: PRPH2; NbExp=3; IntAct=EBI-2623095, EBI-25836834;
CC Q9Y371; P25786: PSMA1; NbExp=3; IntAct=EBI-2623095, EBI-359352;
CC Q9Y371; P41222: PTGDS; NbExp=3; IntAct=EBI-2623095, EBI-948821;
CC Q9Y371; Q9UI14: RABAC1; NbExp=3; IntAct=EBI-2623095, EBI-712367;
CC Q9Y371; Q09028: RBBP4; NbExp=3; IntAct=EBI-2623095, EBI-620823;
CC Q9Y371; Q96HR9-2: REEP6; NbExp=3; IntAct=EBI-2623095, EBI-14065960;
CC Q9Y371; Q6ZWK4: RHEX; NbExp=3; IntAct=EBI-2623095, EBI-18304046;
CC Q9Y371; Q9NPQ8-4: RIC8A; NbExp=8; IntAct=EBI-2623095, EBI-9091816;
CC Q9Y371; P62701: RPS4X; NbExp=3; IntAct=EBI-2623095, EBI-354303;
CC Q9Y371; O15126: SCAMP1; NbExp=3; IntAct=EBI-2623095, EBI-954338;
CC Q9Y371; Q9BRK5: SDF4; NbExp=3; IntAct=EBI-2623095, EBI-1389808;
CC Q9Y371; P01011: SERPINA3; NbExp=3; IntAct=EBI-2623095, EBI-296557;
CC Q9Y371; A0A1P0AYU5: SFXN3; NbExp=3; IntAct=EBI-2623095, EBI-14193895;
CC Q9Y371; Q7L8J4: SH3BP5L; NbExp=3; IntAct=EBI-2623095, EBI-747389;
CC Q9Y371; Q9Y371: SH3GLB1; NbExp=8; IntAct=EBI-2623095, EBI-2623095;
CC Q9Y371; Q9NR46: SH3GLB2; NbExp=20; IntAct=EBI-2623095, EBI-749607;
CC Q9Y371; Q9BZQ2: SHCBP1L; NbExp=3; IntAct=EBI-2623095, EBI-10818532;
CC Q9Y371; H3BQL7: SIN3A; NbExp=3; IntAct=EBI-2623095, EBI-13384308;
CC Q9Y371; Q96EX1: SMIM12; NbExp=3; IntAct=EBI-2623095, EBI-2874543;
CC Q9Y371; Q71RC9: SMIM5; NbExp=3; IntAct=EBI-2623095, EBI-12334905;
CC Q9Y371; O60906: SMPD2; NbExp=3; IntAct=EBI-2623095, EBI-12828299;
CC Q9Y371; Q13573: SNW1; NbExp=3; IntAct=EBI-2623095, EBI-632715;
CC Q9Y371; Q13596: SNX1; NbExp=3; IntAct=EBI-2623095, EBI-2822329;
CC Q9Y371; O95219: SNX4; NbExp=3; IntAct=EBI-2623095, EBI-724909;
CC Q9Y371; Q8N0X7: SPART; NbExp=3; IntAct=EBI-2623095, EBI-2643803;
CC Q9Y371; Q9NYA1-2: SPHK1; NbExp=3; IntAct=EBI-2623095, EBI-12512419;
CC Q9Y371; Q9BPZ2: SPIN2B; NbExp=3; IntAct=EBI-2623095, EBI-21726245;
CC Q9Y371; Q9BXA5: SUCNR1; NbExp=3; IntAct=EBI-2623095, EBI-17962797;
CC Q9Y371; O60506-4: SYNCRIP; NbExp=3; IntAct=EBI-2623095, EBI-11123832;
CC Q9Y371; O43761: SYNGR3; NbExp=6; IntAct=EBI-2623095, EBI-11321949;
CC Q9Y371; P08247: SYP; NbExp=6; IntAct=EBI-2623095, EBI-9071725;
CC Q9Y371; Q17RD7: SYT16; NbExp=3; IntAct=EBI-2623095, EBI-10238936;
CC Q9Y371; P54274-2: TERF1; NbExp=3; IntAct=EBI-2623095, EBI-711018;
CC Q9Y371; Q9UBB9: TFIP11; NbExp=7; IntAct=EBI-2623095, EBI-1105213;
CC Q9Y371; P22735: TGM1; NbExp=3; IntAct=EBI-2623095, EBI-2562368;
CC Q9Y371; Q9NQ88: TIGAR; NbExp=3; IntAct=EBI-2623095, EBI-3920747;
CC Q9Y371; O14925: TIMM23; NbExp=3; IntAct=EBI-2623095, EBI-1047996;
CC Q9Y371; Q12893: TMEM115; NbExp=3; IntAct=EBI-2623095, EBI-8633987;
CC Q9Y371; Q8WVE6-2: TMEM171; NbExp=3; IntAct=EBI-2623095, EBI-25874374;
CC Q9Y371; Q53NU3: tmp_locus_54; NbExp=3; IntAct=EBI-2623095, EBI-10242677;
CC Q9Y371; Q9NS69: TOMM22; NbExp=3; IntAct=EBI-2623095, EBI-1047508;
CC Q9Y371; P55327-2: TPD52; NbExp=3; IntAct=EBI-2623095, EBI-12124194;
CC Q9Y371; O43399: TPD52L2; NbExp=3; IntAct=EBI-2623095, EBI-782604;
CC Q9Y371; Q6FGS1: TPD52L2; NbExp=3; IntAct=EBI-2623095, EBI-10327230;
CC Q9Y371; Q9C035-3: TRIM5; NbExp=3; IntAct=EBI-2623095, EBI-12840050;
CC Q9Y371; Q86WT6-2: TRIM69; NbExp=3; IntAct=EBI-2623095, EBI-11525489;
CC Q9Y371; P49638: TTPA; NbExp=3; IntAct=EBI-2623095, EBI-10210710;
CC Q9Y371; Q9H313-4: TTYH1; NbExp=3; IntAct=EBI-2623095, EBI-17671298;
CC Q9Y371; Q9BQE3: TUBA1C; NbExp=3; IntAct=EBI-2623095, EBI-1103245;
CC Q9Y371; P62253: UBE2G1; NbExp=3; IntAct=EBI-2623095, EBI-2340619;
CC Q9Y371; Q9P2Y5: UVRAG; NbExp=11; IntAct=EBI-2623095, EBI-2952704;
CC Q9Y371; O95070: YIF1A; NbExp=3; IntAct=EBI-2623095, EBI-2799703;
CC Q9Y371; O43829: ZBTB14; NbExp=3; IntAct=EBI-2623095, EBI-10176632;
CC Q9Y371; Q53FD0-2: ZC2HC1C; NbExp=3; IntAct=EBI-2623095, EBI-14104088;
CC Q9Y371; Q9H609: ZNF576; NbExp=6; IntAct=EBI-2623095, EBI-3921014;
CC Q9Y371; Q3KNS6-3: ZNF829; NbExp=3; IntAct=EBI-2623095, EBI-18036029;
CC Q9Y371-1; Q07812: BAX; NbExp=2; IntAct=EBI-5291808, EBI-516580;
CC Q9Y371-2; Q9Y371-2: SH3GLB1; NbExp=3; IntAct=EBI-5282812, EBI-5282812;
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_001206652.1. [Q9Y371-2]
DR RefSeq; NP_001193582.1; NM_001206653.1. [Q9Y371-3]
DR RefSeq; NP_057093.1; NM_016009.4. [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 PDBsum; 6UP6; -.
DR PDBsum; 6UPN; -.
DR AlphaFoldDB; Q9Y371; -.
DR SMR; Q9Y371; -.
DR BioGRID; 119289; 115.
DR DIP; DIP-41970N; -.
DR IntAct; Q9Y371; 189.
DR MINT; Q9Y371; -.
DR STRING; 9606.ENSP00000479919; -.
DR TCDB; 8.A.34.1.4; the endophilin (endophilin) family.
DR GlyGen; Q9Y371; 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 EPD; Q9Y371; -.
DR jPOST; Q9Y371; -.
DR MassIVE; Q9Y371; -.
DR MaxQB; Q9Y371; -.
DR PeptideAtlas; Q9Y371; -.
DR PRIDE; Q9Y371; -.
DR ProteomicsDB; 5734; -.
DR ProteomicsDB; 85978; -. [Q9Y371-1]
DR ProteomicsDB; 85979; -. [Q9Y371-2]
DR Antibodypedia; 2824; 559 antibodies from 37 providers.
DR DNASU; 51100; -.
DR Ensembl; ENST00000370558.8; ENSP00000473267.1; ENSG00000097033.14. [Q9Y371-1]
DR Ensembl; ENST00000482504.1; ENSP00000418744.1; ENSG00000097033.14. [Q9Y371-2]
DR Ensembl; ENST00000535010.5; ENSP00000441355.1; ENSG00000097033.14. [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 CTD; 51100; -.
DR DisGeNET; 51100; -.
DR GeneCards; SH3GLB1; -.
DR HGNC; HGNC:10833; SH3GLB1.
DR HPA; ENSG00000097033; Low tissue specificity.
DR MIM; 609287; gene.
DR neXtProt; NX_Q9Y371; -.
DR OpenTargets; ENSG00000097033; -.
DR PharmGKB; PA35739; -.
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; 803053at2759; -.
DR PhylomeDB; Q9Y371; -.
DR TreeFam; TF313281; -.
DR PathwayCommons; Q9Y371; -.
DR SignaLink; Q9Y371; -.
DR SIGNOR; Q9Y371; -.
DR BioGRID-ORCS; 51100; 14 hits in 1081 CRISPR screens.
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 207 other tissues.
DR ExpressionAtlas; Q9Y371; baseline and differential.
DR Genevisible; Q9Y371; HS.
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:0032991; C:protein-containing complex; IDA:UniProtKB.
DR GO; GO:0045296; F:cadherin binding; HDA:BHF-UCL.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0008289; F:lipid binding; IEA:UniProtKB-KW.
DR GO; GO:0042803; F:protein homodimerization activity; IPI:HGNC-UCL.
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: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 Gene3D; 1.20.1270.60; -; 1.
DR InterPro; IPR027267; AH/BAR_dom_sf.
DR InterPro; IPR004148; BAR_dom.
DR InterPro; IPR036028; SH3-like_dom_sf.
DR InterPro; IPR001452; SH3_domain.
DR InterPro; IPR028503; SH3GLB1.
DR InterPro; IPR035695; SH3GLB1_BAR.
DR PANTHER; PTHR14167:SF52; PTHR14167:SF52; 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; SSF103657; 1.
DR SUPFAM; SSF50044; SSF50044; 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; 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"
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
