BAG3_HUMAN
ID BAG3_HUMAN Reviewed; 575 AA.
AC O95817; A8K5L8; Q3B763; Q9NT20; Q9P120;
DT 11-JAN-2001, integrated into UniProtKB/Swiss-Prot.
DT 11-JAN-2001, sequence version 3.
DT 03-AUG-2022, entry version 211.
DE RecName: Full=BAG family molecular chaperone regulator 3;
DE Short=BAG-3;
DE AltName: Full=Bcl-2-associated athanogene 3;
DE AltName: Full=Bcl-2-binding protein Bis;
DE AltName: Full=Docking protein CAIR-1;
GN Name=BAG3; Synonyms=BIS;
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], FUNCTION, AND INTERACTION WITH HSP70/HSC70
RP CHAPERONES.
RX PubMed=9873016; DOI=10.1074/jbc.274.2.781;
RA Takayama S., Xie Z., Reed J.C.;
RT "An evolutionarily conserved family of Hsp70/Hsc70 molecular chaperone
RT regulators.";
RL J. Biol. Chem. 274:781-786(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], VARIANT ARG-151, FUNCTION, AND INTERACTION WITH
RP BCL2.
RX PubMed=10597216; DOI=10.1038/sj.onc.1203043;
RA Lee J.H., Takahashi T., Yasuhara N., Inazawa J., Kamada S., Tsujimoto Y.;
RT "Bis, a Bcl-2-binding protein that synergizes with Bcl-2 in preventing cell
RT death.";
RL Oncogene 18:6183-6190(1999).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA], AND INTERACTION WITH PHOSPHOLIPASE C-GAMMA
RP PROTEINS.
RX PubMed=10980614; DOI=10.1038/sj.onc.1203797;
RA Doong H., Price J., Kim Y.S., Gasbarre C., Probst J., Liotta L.A.,
RA Blanchette J., Rizzo K., Kohn E.;
RT "CAIR-1/BAG-3 forms an EGF-regulated ternary complex with phospholipase C-
RT gamma and Hsp70/Hsc70.";
RL Oncogene 19:4385-4395(2000).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Tongue;
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Testis;
RX PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D.,
RA Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A.,
RA Wiemann S., Schupp I.;
RT "The full-ORF clone resource of the German cDNA consortium.";
RL BMC Genomics 8:399-399(2007).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain, Lung, and Placenta;
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 [7]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
RA Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.;
RT "Global, in vivo, and site-specific phosphorylation dynamics in signaling
RT networks.";
RL Cell 127:635-648(2006).
RN [8]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18220336; DOI=10.1021/pr0705441;
RA Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D., Yates J.R. III;
RT "Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient
RT phosphoproteomic analysis.";
RL J. Proteome Res. 7:1346-1351(2008).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-377, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007;
RA Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,
RA Greff Z., Keri G., Stemmann O., Mann M.;
RT "Kinase-selective enrichment enables quantitative phosphoproteomics of the
RT kinome across the cell cycle.";
RL Mol. Cell 31:438-448(2008).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-274; SER-275; SER-279;
RP THR-285; SER-289; SER-291; SER-377; SER-386 AND THR-406, AND IDENTIFICATION
RP BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [11]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a
RT refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [12]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, PHOSPHORYLATION [LARGE SCALE
RP ANALYSIS] AT SER-198; SER-289; SER-377; SER-386 AND THR-406, CLEAVAGE OF
RP INITIATOR METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [13]
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 [14]
RP INTERACTION WITH DNAJB6.
RX PubMed=22366786; DOI=10.1038/ng.1103;
RA Sarparanta J., Jonson P.H., Golzio C., Sandell S., Luque H., Screen M.,
RA McDonald K., Stajich J.M., Mahjneh I., Vihola A., Raheem O., Penttila S.,
RA Lehtinen S., Huovinen S., Palmio J., Tasca G., Ricci E., Hackman P.,
RA Hauser M., Katsanis N., Udd B.;
RT "Mutations affecting the cytoplasmic functions of the co-chaperone DNAJB6
RT cause limb-girdle muscular dystrophy.";
RL Nat. Genet. 44:450-455(2012).
RN [15]
RP INTERACTION WITH SYNPO2.
RX PubMed=23434281; DOI=10.1016/j.cub.2013.01.064;
RA Ulbricht A., Eppler F.J., Tapia V.E., van der Ven P.F., Hampe N.,
RA Hersch N., Vakeel P., Stadel D., Haas A., Saftig P., Behrends C.,
RA Fuerst D.O., Volkmer R., Hoffmann B., Kolanus W., Hoehfeld J.;
RT "Cellular mechanotransduction relies on tension-induced and chaperone-
RT assisted autophagy.";
RL Curr. Biol. 23:430-435(2013).
RN [16]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-173; SER-269; SER-275;
RP SER-279; THR-285; SER-289; SER-291; SER-377 AND THR-406, AND IDENTIFICATION
RP BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma, and Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [17]
RP FUNCTION, AND INTERACTION WITH HSPA1A; HSPA1B AND HSPA8.
RX PubMed=24318877; DOI=10.1074/jbc.m113.521997;
RA Rauch J.N., Gestwicki J.E.;
RT "Binding of human nucleotide exchange factors to heat shock protein 70
RT (Hsp70) generates functionally distinct complexes in vitro.";
RL J. Biol. Chem. 289:1402-1414(2014).
RN [18]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-377 AND SER-385, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [19]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-445, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25114211; DOI=10.1073/pnas.1413825111;
RA Impens F., Radoshevich L., Cossart P., Ribet D.;
RT "Mapping of SUMO sites and analysis of SUMOylation changes induced by
RT external stimuli.";
RL Proc. Natl. Acad. Sci. U.S.A. 111:12432-12437(2014).
RN [20]
RP FUNCTION, INTERACTION WITH HSF1, AND SUBCELLULAR LOCATION.
RX PubMed=26159920; DOI=10.1016/j.bbrc.2015.07.006;
RA Jin Y.H., Ahn S.G., Kim S.A.;
RT "BAG3 affects the nucleocytoplasmic shuttling of HSF1 upon heat stress.";
RL Biochem. Biophys. Res. Commun. 464:561-567(2015).
RN [21]
RP FUNCTION, INTERACTION WITH HSPA8, AND MUTAGENESIS OF 480-ARG-LYS-481.
RX PubMed=27474739; DOI=10.1074/jbc.m116.742502;
RA Rauch J.N., Zuiderweg E.R., Gestwicki J.E.;
RT "Non-canonical interactions between heat shock cognate protein 70 (Hsc70)
RT and Bcl2-associated anthanogene (BAG) co-chaperones are important for
RT client release.";
RL J. Biol. Chem. 291:19848-19857(2016).
RN [22]
RP INTERACTION WITH HSPB8.
RX PubMed=28144995; DOI=10.1002/humu.23189;
RA Echaniz-Laguna A., Geuens T., Petiot P., Pereon Y., Adriaenssens E.,
RA Haidar M., Capponi S., Maisonobe T., Fournier E., Dubourg O., Degos B.,
RA Salachas F., Lenglet T., Eymard B., Delmont E., Pouget J.,
RA Juntas Morales R., Goizet C., Latour P., Timmerman V., Stojkovic T.;
RT "Axonal Neuropathies due to Mutations in Small Heat Shock Proteins:
RT Clinical, Genetic, and Functional Insights into Novel Mutations.";
RL Hum. Mutat. 38:556-568(2017).
RN [23]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-445, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=28112733; DOI=10.1038/nsmb.3366;
RA Hendriks I.A., Lyon D., Young C., Jensen L.J., Vertegaal A.C.,
RA Nielsen M.L.;
RT "Site-specific mapping of the human SUMO proteome reveals co-modification
RT with phosphorylation.";
RL Nat. Struct. Mol. Biol. 24:325-336(2017).
RN [24]
RP VARIANT MFM6 LEU-209.
RX PubMed=19085932; DOI=10.1002/ana.21553;
RA Selcen D., Muntoni F., Burton B.K., Pegoraro E., Sewry C., Bite A.V.,
RA Engel A.G.;
RT "Mutation in BAG3 causes severe dominant childhood muscular dystrophy.";
RL Ann. Neurol. 65:83-89(2009).
RN [25]
RP VARIANTS CMD1HH TRP-71 AND HIS-477.
RX PubMed=21353195; DOI=10.1016/j.ajhg.2011.01.016;
RA Norton N., Li D., Rieder M.J., Siegfried J.D., Rampersaud E., Zuchner S.,
RA Mangos S., Gonzalez-Quintana J., Wang L., McGee S., Reiser J., Martin E.,
RA Nickerson D.A., Hershberger R.E.;
RT "Genome-wide studies of copy number variation and exome sequencing identify
RT rare variants in BAG3 as a cause of dilated cardiomyopathy.";
RL Am. J. Hum. Genet. 88:273-282(2011).
RN [26]
RP VARIANT MFM6 LEU-209, AND VARIANT TRP-258.
RX PubMed=21361913; DOI=10.1111/j.1399-0004.2011.01659.x;
RA Lee H., Cherk S., Chan S., Wong S., Tong T., Ho W., Chan A., Lee K.,
RA Mak C.;
RT "BAG3-related myofibrillar myopathy in a Chinese family.";
RL Clin. Genet. 81:394-398(2012).
RN [27]
RP VARIANTS GLN-71; LEU-77; PHE-94; SER-115; ARG-151; THR-155; SER-380 AND
RP LEU-407, AND VARIANTS CMD1HH LYS-455 AND MET-468.
RX PubMed=21459883; DOI=10.1093/eurheartj/ehr105;
RA Villard E., Perret C., Gary F., Proust C., Dilanian G., Hengstenberg C.,
RA Ruppert V., Arbustini E., Wichter T., Germain M., Dubourg O., Tavazzi L.,
RA Aumont M.C., DeGroote P., Fauchier L., Trochu J.N., Gibelin P.,
RA Aupetit J.F., Stark K., Erdmann J., Hetzer R., Roberts A.M., Barton P.J.,
RA Regitz-Zagrosek V., Aslam U., Duboscq-Bidot L., Meyborg M., Maisch B.,
RA Madeira H., Waldenstrom A., Galve E., Cleland J.G., Dorent R., Roizes G.,
RA Zeller T., Blankenberg S., Goodall A.H., Cook S., Tregouet D.A., Tiret L.,
RA Isnard R., Komajda M., Charron P., Cambien F.;
RT "A genome-wide association study identifies two loci associated with heart
RT failure due to dilated cardiomyopathy.";
RL Eur. Heart J. 32:1065-1076(2011).
RN [28]
RP VARIANTS CMD1HH TRP-218 AND PRO-462, VARIANTS TRP-258; ASN-300; LEU-407 AND
RP ASP-553, CHARACTERIZATION OF VARIANTS CMD1HH TRP-218 AND PRO-462,
RP CHARACTERIZATION OF VARIANT MFM6 LEU-209, AND CHARACTERIZATION OF VARIANT
RP TRP-258.
RX PubMed=21898660; DOI=10.1002/humu.21603;
RA Arimura T., Ishikawa T., Nunoda S., Kawai S., Kimura A.;
RT "Dilated cardiomyopathy-associated BAG3 mutations impair Z-disc assembly
RT and enhance sensitivity to apoptosis in cardiomyocytes.";
RL Hum. Mutat. 32:1481-1491(2011).
CC -!- FUNCTION: Co-chaperone for HSP70 and HSC70 chaperone proteins. Acts as
CC a nucleotide-exchange factor (NEF) promoting the release of ADP from
CC the HSP70 and HSC70 proteins thereby triggering client/substrate
CC protein release. Nucleotide release is mediated via its binding to the
CC nucleotide-binding domain (NBD) of HSPA8/HSC70 where as the substrate
CC release is mediated via its binding to the substrate-binding domain
CC (SBD) of HSPA8/HSC70 (PubMed:9873016, PubMed:27474739). Has anti-
CC apoptotic activity (PubMed:10597216). Plays a role in the HSF1
CC nucleocytoplasmic transport (PubMed:26159920).
CC {ECO:0000269|PubMed:10597216, ECO:0000269|PubMed:24318877,
CC ECO:0000269|PubMed:26159920, ECO:0000269|PubMed:27474739,
CC ECO:0000269|PubMed:9873016}.
CC -!- SUBUNIT: Binds to the ATPase domain of HSP70/HSC70 chaperones
CC (PubMed:9873016). Interacts with BCL2 (PubMed:10597216). Interacts with
CC phospholipase C-gamma proteins (PubMed:10980614). Interacts with DNAJB6
CC (PubMed:22366786). Interacts (via BAG domain) with HSF1; this
CC interaction occurs in normal and heat-shocked cells promoting HSF1
CC nucleocytoplasmic shuttling (PubMed:26159920). Interacts with HSPA8
CC (via NBD) (PubMed:27474739, PubMed:24318877). Interacts with HSPA1A
CC (via NBD) and HSPA1B (via NBD) (PubMed:24318877). Interacts (via WW
CC domain 1) with SYNPO2 (via PPPY motif) (PubMed:23434281). Interacts
CC with HSPB8 (PubMed:28144995). {ECO:0000269|PubMed:10597216,
CC ECO:0000269|PubMed:10980614, ECO:0000269|PubMed:22366786,
CC ECO:0000269|PubMed:23434281, ECO:0000269|PubMed:24318877,
CC ECO:0000269|PubMed:26159920, ECO:0000269|PubMed:27474739,
CC ECO:0000269|PubMed:28144995, ECO:0000269|PubMed:9873016}.
CC -!- INTERACTION:
CC O95817; Q96B67: ARRDC3; NbExp=10; IntAct=EBI-747185, EBI-2875665;
CC O95817; Q86V38: ATN1; NbExp=6; IntAct=EBI-747185, EBI-11954292;
CC O95817; Q9UHR4: BAIAP2L1; NbExp=3; IntAct=EBI-747185, EBI-2483278;
CC O95817; Q9H2G9: BLZF1; NbExp=3; IntAct=EBI-747185, EBI-2548012;
CC O95817; Q96IK1-2: BOD1; NbExp=3; IntAct=EBI-747185, EBI-18924329;
CC O95817; P48643: CCT5; NbExp=3; IntAct=EBI-747185, EBI-355710;
CC O95817; Q16630-2: CPSF6; NbExp=3; IntAct=EBI-747185, EBI-11088043;
CC O95817; P02489: CRYAA; NbExp=3; IntAct=EBI-747185, EBI-6875961;
CC O95817; Q9GZU7: CTDSP1; NbExp=3; IntAct=EBI-747185, EBI-751587;
CC O95817; A8MQ03: CYSRT1; NbExp=3; IntAct=EBI-747185, EBI-3867333;
CC O95817; Q9H1C7: CYSTM1; NbExp=3; IntAct=EBI-747185, EBI-12867082;
CC O95817; Q15038: DAZAP2; NbExp=9; IntAct=EBI-747185, EBI-724310;
CC O95817; P50570: DNM2; NbExp=3; IntAct=EBI-747185, EBI-346547;
CC O95817; Q8N9I9: DTX3; NbExp=3; IntAct=EBI-747185, EBI-2340258;
CC O95817; Q86TH3: DVL1; NbExp=7; IntAct=EBI-747185, EBI-10185025;
CC O95817; Q14204: DYNC1H1; NbExp=3; IntAct=EBI-747185, EBI-356015;
CC O95817; Q05215: EGR4; NbExp=3; IntAct=EBI-747185, EBI-19949420;
CC O95817; O00167-2: EYA2; NbExp=4; IntAct=EBI-747185, EBI-12807776;
CC O95817; A1KXE4-2: FAM168B; NbExp=3; IntAct=EBI-747185, EBI-12193763;
CC O95817; Q9NU39: FOXD4L1; NbExp=3; IntAct=EBI-747185, EBI-11320806;
CC O95817; Q86UU5: GGN; NbExp=3; IntAct=EBI-747185, EBI-10259069;
CC O95817; Q8NEA6-2: GLIS3; NbExp=3; IntAct=EBI-747185, EBI-12232117;
CC O95817; A0A087WSW0: HELT; NbExp=3; IntAct=EBI-747185, EBI-12057631;
CC O95817; Q96IS6: HSPA8; NbExp=3; IntAct=EBI-747185, EBI-10289199;
CC O95817; P04792: HSPB1; NbExp=7; IntAct=EBI-747185, EBI-352682;
CC O95817; Q16082: HSPB2; NbExp=3; IntAct=EBI-747185, EBI-739395;
CC O95817; Q9UBY9: HSPB7; NbExp=3; IntAct=EBI-747185, EBI-739361;
CC O95817; Q9UJY1: HSPB8; NbExp=11; IntAct=EBI-747185, EBI-739074;
CC O95817; Q0VD86: INCA1; NbExp=3; IntAct=EBI-747185, EBI-6509505;
CC O95817; Q8WZ19: KCTD13; NbExp=3; IntAct=EBI-747185, EBI-742916;
CC O95817; Q92876: KLK6; NbExp=3; IntAct=EBI-747185, EBI-2432309;
CC O95817; Q96PV6: LENG8; NbExp=3; IntAct=EBI-747185, EBI-739546;
CC O95817; Q99732: LITAF; NbExp=7; IntAct=EBI-747185, EBI-725647;
CC O95817; Q5S007: LRRK2; NbExp=2; IntAct=EBI-747185, EBI-5323863;
CC O95817; Q9Y5V3: MAGED1; NbExp=6; IntAct=EBI-747185, EBI-716006;
CC O95817; Q99750: MDFI; NbExp=3; IntAct=EBI-747185, EBI-724076;
CC O95817; Q15773: MLF2; NbExp=4; IntAct=EBI-747185, EBI-1051875;
CC O95817; Q96DV4: MRPL38; NbExp=3; IntAct=EBI-747185, EBI-720441;
CC O95817; P07196: NEFL; NbExp=3; IntAct=EBI-747185, EBI-475646;
CC O95817; Q86XR2: NIBAN3; NbExp=3; IntAct=EBI-747185, EBI-2796690;
CC O95817; A8MTQ0: NOTO; NbExp=3; IntAct=EBI-747185, EBI-17490746;
CC O95817; Q13133-3: NR1H3; NbExp=3; IntAct=EBI-747185, EBI-11952806;
CC O95817; Q9NPF4: OSGEP; NbExp=3; IntAct=EBI-747185, EBI-1056510;
CC O95817; O76083: PDE9A; NbExp=3; IntAct=EBI-747185, EBI-742764;
CC O95817; O76083-2: PDE9A; NbExp=3; IntAct=EBI-747185, EBI-11524542;
CC O95817; Q9NR12: PDLIM7; NbExp=5; IntAct=EBI-747185, EBI-350517;
CC O95817; Q9BRX2: PELO; NbExp=3; IntAct=EBI-747185, EBI-1043580;
CC O95817; Q8WWB5: PIH1D2; NbExp=3; IntAct=EBI-747185, EBI-10232538;
CC O95817; O15496: PLA2G10; NbExp=3; IntAct=EBI-747185, EBI-726466;
CC O95817; Q9UF11-2: PLEKHB1; NbExp=3; IntAct=EBI-747185, EBI-12832742;
CC O95817; Q9NQX0: PRDM6; NbExp=3; IntAct=EBI-747185, EBI-11320284;
CC O95817; P31321: PRKAR1B; NbExp=3; IntAct=EBI-747185, EBI-2805516;
CC O95817; Q9NV39: PRR34; NbExp=3; IntAct=EBI-747185, EBI-11959565;
CC O95817; Q16825: PTPN21; NbExp=3; IntAct=EBI-747185, EBI-2860264;
CC O95817; Q09028: RBBP4; NbExp=3; IntAct=EBI-747185, EBI-620823;
CC O95817; Q9H6L5-2: RETREG1; NbExp=3; IntAct=EBI-747185, EBI-13382642;
CC O95817; Q01196-8: RUNX1; NbExp=3; IntAct=EBI-747185, EBI-12001422;
CC O95817; O75446: SAP30; NbExp=3; IntAct=EBI-747185, EBI-632609;
CC O95817; Q15427: SF3B4; NbExp=6; IntAct=EBI-747185, EBI-348469;
CC O95817; Q6ZSJ9: SHISA6; NbExp=5; IntAct=EBI-747185, EBI-12037847;
CC O95817; Q8IUQ4-2: SIAH1; NbExp=3; IntAct=EBI-747185, EBI-11522811;
CC O95817; Q13501: SQSTM1; NbExp=3; IntAct=EBI-747185, EBI-307104;
CC O95817; Q9UNE7: STUB1; NbExp=3; IntAct=EBI-747185, EBI-357085;
CC O95817; Q6DHY5: TBC1D3G; NbExp=3; IntAct=EBI-747185, EBI-13092532;
CC O95817; Q9BSI4: TINF2; NbExp=2; IntAct=EBI-747185, EBI-717399;
CC O95817; Q8WUU8: TMEM174; NbExp=3; IntAct=EBI-747185, EBI-10276729;
CC O95817; Q05BL1: TP53BP2; NbExp=3; IntAct=EBI-747185, EBI-11952721;
CC O95817; Q96RU7: TRIB3; NbExp=3; IntAct=EBI-747185, EBI-492476;
CC O95817; P14373: TRIM27; NbExp=3; IntAct=EBI-747185, EBI-719493;
CC O95817; Q15654: TRIP6; NbExp=3; IntAct=EBI-747185, EBI-742327;
CC O95817; Q86WV8: TSC1; NbExp=3; IntAct=EBI-747185, EBI-12806590;
CC O95817; Q9H9P5-5: UNKL; NbExp=3; IntAct=EBI-747185, EBI-12817837;
CC O95817; Q9H9H4: VPS37B; NbExp=3; IntAct=EBI-747185, EBI-4400866;
CC O95817; Q969T9: WBP2; NbExp=4; IntAct=EBI-747185, EBI-727055;
CC O95817; O76024: WFS1; NbExp=3; IntAct=EBI-747185, EBI-720609;
CC O95817; Q7Z783; NbExp=3; IntAct=EBI-747185, EBI-9088990;
CC O95817; Q96BE0; NbExp=2; IntAct=EBI-747185, EBI-9356686;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:26159920}. Cytoplasm
CC {ECO:0000269|PubMed:26159920}. Note=Colocalizes with HSF1 to the
CC nucleus upon heat stress (PubMed:26159920).
CC {ECO:0000269|PubMed:26159920}.
CC -!- DISEASE: Myopathy, myofibrillar, 6 (MFM6) [MIM:612954]: A form of
CC myofibrillar myopathy, a group of chronic neuromuscular disorders
CC characterized at ultrastructural level by disintegration of the
CC sarcomeric Z disk and myofibrils, and replacement of the normal
CC myofibrillar markings by small dense granules, or larger hyaline
CC masses, or amorphous material. MFM6 is characterized by early-onset of
CC severe, progressive, diffuse muscle weakness associated with
CC cardiomyopathy, severe respiratory insufficiency during adolescence,
CC and a rigid spine in some patients. {ECO:0000269|PubMed:19085932,
CC ECO:0000269|PubMed:21361913, ECO:0000269|PubMed:21898660}. Note=The
CC disease is caused by variants affecting the gene represented in this
CC entry.
CC -!- DISEASE: Cardiomyopathy, dilated 1HH (CMD1HH) [MIM:613881]: A disorder
CC characterized by ventricular dilation and impaired systolic function,
CC resulting in congestive heart failure and arrhythmia. Patients are at
CC risk of premature death. {ECO:0000269|PubMed:21353195,
CC ECO:0000269|PubMed:21459883, ECO:0000269|PubMed:21898660}. Note=The
CC disease is caused by variants affecting the gene represented in this
CC entry.
CC -!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology and
CC Haematology;
CC URL="https://atlasgeneticsoncology.org/gene/43160/bag3-(bcl-2-associated-athanogene-3)";
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DR EMBL; AF095193; AAD16122.2; -; mRNA.
DR EMBL; AF127139; AAF26839.1; -; mRNA.
DR EMBL; AF071218; AAF69592.2; -; mRNA.
DR EMBL; AK291333; BAF84022.1; -; mRNA.
DR EMBL; AL137582; CAB70824.1; -; mRNA.
DR EMBL; BC006418; AAH06418.1; -; mRNA.
DR EMBL; BC014656; AAH14656.1; -; mRNA.
DR EMBL; BC107786; AAI07787.1; -; mRNA.
DR CCDS; CCDS7615.1; -.
DR RefSeq; NP_004272.2; NM_004281.3.
DR AlphaFoldDB; O95817; -.
DR SMR; O95817; -.
DR BioGRID; 114907; 610.
DR CORUM; O95817; -.
DR DIP; DIP-41273N; -.
DR IntAct; O95817; 172.
DR MINT; O95817; -.
DR STRING; 9606.ENSP00000358081; -.
DR GlyGen; O95817; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; O95817; -.
DR MetOSite; O95817; -.
DR PhosphoSitePlus; O95817; -.
DR BioMuta; BAG3; -.
DR CPTAC; CPTAC-317; -.
DR CPTAC; CPTAC-318; -.
DR EPD; O95817; -.
DR jPOST; O95817; -.
DR MassIVE; O95817; -.
DR MaxQB; O95817; -.
DR PaxDb; O95817; -.
DR PeptideAtlas; O95817; -.
DR PRIDE; O95817; -.
DR ProteomicsDB; 51065; -.
DR Antibodypedia; 18850; 466 antibodies from 40 providers.
DR DNASU; 9531; -.
DR Ensembl; ENST00000369085.8; ENSP00000358081.4; ENSG00000151929.10.
DR GeneID; 9531; -.
DR KEGG; hsa:9531; -.
DR MANE-Select; ENST00000369085.8; ENSP00000358081.4; NM_004281.4; NP_004272.2.
DR UCSC; uc001lem.4; human.
DR CTD; 9531; -.
DR DisGeNET; 9531; -.
DR GeneCards; BAG3; -.
DR GeneReviews; BAG3; -.
DR HGNC; HGNC:939; BAG3.
DR HPA; ENSG00000151929; Tissue enhanced (brain, skeletal muscle).
DR MalaCards; BAG3; -.
DR MIM; 603883; gene.
DR MIM; 612954; phenotype.
DR MIM; 613881; phenotype.
DR neXtProt; NX_O95817; -.
DR OpenTargets; ENSG00000151929; -.
DR Orphanet; 154; Familial isolated dilated cardiomyopathy.
DR Orphanet; 199340; Muscular dystrophy, Selcen type.
DR PharmGKB; PA25239; -.
DR VEuPathDB; HostDB:ENSG00000151929; -.
DR eggNOG; KOG0940; Eukaryota.
DR eggNOG; KOG4361; Eukaryota.
DR GeneTree; ENSGT00940000159204; -.
DR HOGENOM; CLU_034378_0_0_1; -.
DR InParanoid; O95817; -.
DR OMA; THSPMMQ; -.
DR OrthoDB; 715914at2759; -.
DR PhylomeDB; O95817; -.
DR TreeFam; TF102013; -.
DR PathwayCommons; O95817; -.
DR Reactome; R-HSA-3371453; Regulation of HSF1-mediated heat shock response.
DR SignaLink; O95817; -.
DR SIGNOR; O95817; -.
DR BioGRID-ORCS; 9531; 14 hits in 1072 CRISPR screens.
DR ChiTaRS; BAG3; human.
DR GeneWiki; BAG3; -.
DR GenomeRNAi; 9531; -.
DR Pharos; O95817; Tbio.
DR PRO; PR:O95817; -.
DR Proteomes; UP000005640; Chromosome 10.
DR RNAct; O95817; protein.
DR Bgee; ENSG00000151929; Expressed in gastrocnemius and 204 other tissues.
DR ExpressionAtlas; O95817; baseline and differential.
DR Genevisible; O95817; HS.
DR GO; GO:0016235; C:aggresome; TAS:ARUK-UCL.
DR GO; GO:0101031; C:chaperone complex; IDA:ARUK-UCL.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005829; C:cytosol; IDA:HPA.
DR GO; GO:0016020; C:membrane; IBA:GO_Central.
DR GO; GO:0043005; C:neuron projection; IEA:Ensembl.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0001725; C:stress fiber; IEA:Ensembl.
DR GO; GO:0030018; C:Z disc; IEA:Ensembl.
DR GO; GO:0000774; F:adenyl-nucleotide exchange factor activity; IDA:UniProtKB.
DR GO; GO:0045296; F:cadherin binding; HDA:BHF-UCL.
DR GO; GO:0051087; F:chaperone binding; IPI:ARUK-UCL.
DR GO; GO:0045505; F:dynein intermediate chain binding; NAS:ARUK-UCL.
DR GO; GO:0140597; F:protein carrier chaperone; TAS:ARUK-UCL.
DR GO; GO:0044877; F:protein-containing complex binding; IEA:Ensembl.
DR GO; GO:0070842; P:aggresome assembly; TAS:ARUK-UCL.
DR GO; GO:0000045; P:autophagosome assembly; IEA:Ensembl.
DR GO; GO:0007420; P:brain development; IEA:Ensembl.
DR GO; GO:0034605; P:cellular response to heat; IDA:UniProtKB.
DR GO; GO:0071260; P:cellular response to mechanical stimulus; IEA:Ensembl.
DR GO; GO:0034620; P:cellular response to unfolded protein; IMP:ARUK-UCL.
DR GO; GO:0061684; P:chaperone-mediated autophagy; IEA:Ensembl.
DR GO; GO:0097192; P:extrinsic apoptotic signaling pathway in absence of ligand; IEA:Ensembl.
DR GO; GO:0008625; P:extrinsic apoptotic signaling pathway via death domain receptors; IDA:MGI.
DR GO; GO:0046716; P:muscle cell cellular homeostasis; IMP:ARUK-UCL.
DR GO; GO:0043066; P:negative regulation of apoptotic process; NAS:UniProtKB.
DR GO; GO:1903215; P:negative regulation of protein targeting to mitochondrion; IEA:Ensembl.
DR GO; GO:0010664; P:negative regulation of striated muscle cell apoptotic process; IMP:ARUK-UCL.
DR GO; GO:0097201; P:negative regulation of transcription from RNA polymerase II promoter in response to stress; IMP:UniProtKB.
DR GO; GO:1905337; P:positive regulation of aggrephagy; IMP:ARUK-UCL.
DR GO; GO:0046827; P:positive regulation of protein export from nucleus; IMP:UniProtKB.
DR GO; GO:0042307; P:positive regulation of protein import into nucleus; IMP:UniProtKB.
DR GO; GO:0006457; P:protein folding; NAS:UniProtKB.
DR GO; GO:0050821; P:protein stabilization; IDA:ARUK-UCL.
DR GO; GO:0098840; P:protein transport along microtubule; TAS:ARUK-UCL.
DR GO; GO:0021510; P:spinal cord development; IEA:Ensembl.
DR GO; GO:0010658; P:striated muscle cell apoptotic process; IEA:Ensembl.
DR CDD; cd00201; WW; 1.
DR Gene3D; 1.20.58.120; -; 1.
DR InterPro; IPR039773; BAG_chaperone_regulator.
DR InterPro; IPR036533; BAG_dom_sf.
DR InterPro; IPR003103; BAG_domain.
DR InterPro; IPR001202; WW_dom.
DR InterPro; IPR036020; WW_dom_sf.
DR PANTHER; PTHR12329; PTHR12329; 1.
DR Pfam; PF02179; BAG; 1.
DR Pfam; PF00397; WW; 1.
DR SMART; SM00264; BAG; 1.
DR SMART; SM00456; WW; 1.
DR SUPFAM; SSF51045; SSF51045; 1.
DR SUPFAM; SSF63491; SSF63491; 1.
DR PROSITE; PS51035; BAG; 1.
DR PROSITE; PS01159; WW_DOMAIN_1; 1.
DR PROSITE; PS50020; WW_DOMAIN_2; 1.
PE 1: Evidence at protein level;
KW Acetylation; Apoptosis; Cardiomyopathy; Chaperone; Cytoplasm;
KW Disease variant; Isopeptide bond; Methylation; Myofibrillar myopathy;
KW Nucleus; Phosphoprotein; Reference proteome; Repeat; Ubl conjugation.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0007744|PubMed:20068231"
FT CHAIN 2..575
FT /note="BAG family molecular chaperone regulator 3"
FT /id="PRO_0000088868"
FT DOMAIN 20..54
FT /note="WW 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00224"
FT DOMAIN 124..154
FT /note="WW 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00224"
FT DOMAIN 421..498
FT /note="BAG"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00369"
FT REGION 1..92
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 123..200
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 240..421
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 532..575
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 39..53
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 137..151
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 166..200
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 267..291
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 351..383
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 544..575
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 2
FT /note="N-acetylserine"
FT /evidence="ECO:0007744|PubMed:20068231"
FT MOD_RES 136
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9JLV1"
FT MOD_RES 139
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0000250|UniProtKB:Q9JLV1"
FT MOD_RES 173
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 198
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231"
FT MOD_RES 261
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0000250|UniProtKB:Q9JLV1"
FT MOD_RES 269
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 274
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 275
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 279
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 285
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 289
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163"
FT MOD_RES 291
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 377
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:18691976, ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569"
FT MOD_RES 385
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 386
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:20068231"
FT MOD_RES 406
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163"
FT CROSSLNK 445
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO1); alternate"
FT /evidence="ECO:0007744|PubMed:25114211"
FT CROSSLNK 445
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2); alternate"
FT /evidence="ECO:0007744|PubMed:28112733"
FT VARIANT 71
FT /note="R -> Q (in dbSNP:rs35434411)"
FT /evidence="ECO:0000269|PubMed:21459883"
FT /id="VAR_048344"
FT VARIANT 71
FT /note="R -> W (in CMD1HH; dbSNP:rs387906874)"
FT /evidence="ECO:0000269|PubMed:21353195"
FT /id="VAR_065479"
FT VARIANT 77
FT /note="P -> L (in dbSNP:rs141355480)"
FT /evidence="ECO:0000269|PubMed:21459883"
FT /id="VAR_066777"
FT VARIANT 94
FT /note="I -> F (in dbSNP:rs145393807)"
FT /evidence="ECO:0000269|PubMed:21459883"
FT /id="VAR_066778"
FT VARIANT 115
FT /note="P -> S (in dbSNP:rs774241343)"
FT /evidence="ECO:0000269|PubMed:21459883"
FT /id="VAR_066779"
FT VARIANT 151
FT /note="C -> R (in dbSNP:rs2234962)"
FT /evidence="ECO:0000269|PubMed:10597216,
FT ECO:0000269|PubMed:21459883"
FT /id="VAR_048345"
FT VARIANT 155
FT /note="A -> T (in dbSNP:rs61756328)"
FT /evidence="ECO:0000269|PubMed:21459883"
FT /id="VAR_066780"
FT VARIANT 209
FT /note="P -> L (in MFM6; interferes with the differentiation
FT of skeletal muscle cells; does not cause functional
FT alterations in cardiomyocyte cells; dbSNP:rs121918312)"
FT /evidence="ECO:0000269|PubMed:19085932,
FT ECO:0000269|PubMed:21361913, ECO:0000269|PubMed:21898660"
FT /id="VAR_063089"
FT VARIANT 218
FT /note="R -> W (in CMD1HH; interferes with the assembly of
FT Z-disks; increases stress-induced apoptosis;
FT dbSNP:rs397514506)"
FT /evidence="ECO:0000269|PubMed:21898660"
FT /id="VAR_066781"
FT VARIANT 258
FT /note="R -> W (no functional consequences;
FT dbSNP:rs117671123)"
FT /evidence="ECO:0000269|PubMed:21361913,
FT ECO:0000269|PubMed:21898660"
FT /id="VAR_066782"
FT VARIANT 300
FT /note="D -> N (in dbSNP:rs78439745)"
FT /evidence="ECO:0000269|PubMed:21898660"
FT /id="VAR_066783"
FT VARIANT 380
FT /note="P -> S (in dbSNP:rs144692954)"
FT /evidence="ECO:0000269|PubMed:21459883"
FT /id="VAR_066784"
FT VARIANT 405
FT /note="A -> V (in dbSNP:rs11199064)"
FT /id="VAR_048346"
FT VARIANT 407
FT /note="P -> L (in dbSNP:rs3858340)"
FT /evidence="ECO:0000269|PubMed:21459883,
FT ECO:0000269|PubMed:21898660"
FT /id="VAR_048347"
FT VARIANT 455
FT /note="E -> K (in CMD1HH; dbSNP:rs397516881)"
FT /evidence="ECO:0000269|PubMed:21459883"
FT /id="VAR_066785"
FT VARIANT 462
FT /note="L -> P (in CMD1HH; interferes with the assembly of
FT Z-disks; increases stress-induced apoptosis;
FT dbSNP:rs397514507)"
FT /evidence="ECO:0000269|PubMed:21898660"
FT /id="VAR_066786"
FT VARIANT 468
FT /note="V -> M (in CMD1HH)"
FT /evidence="ECO:0000269|PubMed:21459883"
FT /id="VAR_066787"
FT VARIANT 477
FT /note="R -> H (in CMD1HH; dbSNP:rs387906876)"
FT /evidence="ECO:0000269|PubMed:21353195"
FT /id="VAR_065480"
FT VARIANT 553
FT /note="E -> D (in dbSNP:rs763530097)"
FT /evidence="ECO:0000269|PubMed:21898660"
FT /id="VAR_066788"
FT MUTAGEN 480..481
FT /note="RR->AA: Significant loss of interaction with HSPA8."
FT /evidence="ECO:0000269|PubMed:27474739"
FT CONFLICT 227
FT /note="Q -> K (in Ref. 1; AAD16122)"
FT /evidence="ECO:0000305"
FT CONFLICT 237
FT /note="Q -> R (in Ref. 1; AAD16122)"
FT /evidence="ECO:0000305"
FT CONFLICT 304
FT /note="Missing (in Ref. 5; CAB70824)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 575 AA; 61595 MW; A6328A44F37A406A CRC64;
MSAATHSPMM QVASGNGDRD PLPPGWEIKI DPQTGWPFFV DHNSRTTTWN DPRVPSEGPK
ETPSSANGPS REGSRLPPAR EGHPVYPQLR PGYIPIPVLH EGAENRQVHP FHVYPQPGMQ
RFRTEAAAAA PQRSQSPLRG MPETTQPDKQ CGQVAAAAAA QPPASHGPER SQSPAASDCS
SSSSSASLPS SGRSSLGSHQ LPRGYISIPV IHEQNVTRPA AQPSFHQAQK THYPAQQGEY
QTHQPVYHKI QGDDWEPRPL RAASPFRSSV QGASSREGSP ARSSTPLHSP SPIRVHTVVD
RPQQPMTHRE TAPVSQPENK PESKPGPVGP ELPPGHIPIQ VIRKEVDSKP VSQKPPPPSE
KVEVKVPPAP VPCPPPSPGP SAVPSSPKSV ATEERAAPST APAEATPPKP GEAEAPPKHP
GVLKVEAILE KVQGLEQAVD NFEGKKTDKK YLMIEEYLTK ELLALDSVDP EGRADVRQAR
RDGVRKVQTI LEKLEQKAID VPGQVQVYEL QPSNLEADQP LQAIMEMGAV AADKGKKNAG
NAEDPHTETQ QPEATAAATS NPSSMTDTPG NPAAP
