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BAG family molecular chaperone regulator 3 (BAG-3) (Bcl-2-associated athanogene 3) (Bcl-2-binding protein Bis) (Docking protein CAIR-1)

 BAG3_HUMAN              Reviewed;         575 AA.
O95817; A8K5L8; Q3B763; Q9NT20; Q9P120;
11-JAN-2001, integrated into UniProtKB/Swiss-Prot.
11-JAN-2001, sequence version 3.
27-SEP-2017, entry version 178.
RecName: Full=BAG family molecular chaperone regulator 3;
Short=BAG-3;
AltName: Full=Bcl-2-associated athanogene 3;
AltName: Full=Bcl-2-binding protein Bis;
AltName: Full=Docking protein CAIR-1;
Name=BAG3; Synonyms=BIS;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND INTERACTION WITH HSP70/HSC70
CHAPERONES.
PubMed=9873016; DOI=10.1074/jbc.274.2.781;
Takayama S., Xie Z., Reed J.C.;
"An evolutionarily conserved family of Hsp70/Hsc70 molecular chaperone
regulators.";
J. Biol. Chem. 274:781-786(1999).
[2]
NUCLEOTIDE SEQUENCE [MRNA], VARIANT ARG-151, FUNCTION, AND INTERACTION
WITH BCL2.
PubMed=10597216; DOI=10.1038/sj.onc.1203043;
Lee J.H., Takahashi T., Yasuhara N., Inazawa J., Kamada S.,
Tsujimoto Y.;
"Bis, a Bcl-2-binding protein that synergizes with Bcl-2 in preventing
cell death.";
Oncogene 18:6183-6190(1999).
[3]
NUCLEOTIDE SEQUENCE [MRNA], AND INTERACTION WITH PHOSPHOLIPASE C-GAMMA
PROTEINS.
PubMed=10980614; DOI=10.1038/sj.onc.1203797;
Doong H., Price J., Kim Y.S., Gasbarre C., Probst J., Liotta L.A.,
Blanchette J., Rizzo K., Kohn E.;
"CAIR-1/BAG-3 forms an EGF-regulated ternary complex with
phospholipase C-gamma and Hsp70/Hsc70.";
Oncogene 19:4385-4395(2000).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Tongue;
PubMed=14702039; DOI=10.1038/ng1285;
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Testis;
PubMed=17974005; DOI=10.1186/1471-2164-8-399;
Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H.,
Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K.,
Ottenwaelder B., Poustka A., Wiemann S., Schupp I.;
"The full-ORF clone resource of the German cDNA consortium.";
BMC Genomics 8:399-399(2007).
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Brain, Lung, and Placenta;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[7]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,
Mann M.;
"Global, in vivo, and site-specific phosphorylation dynamics in
signaling networks.";
Cell 127:635-648(2006).
[8]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18220336; DOI=10.1021/pr0705441;
Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D.,
Yates J.R. III;
"Combining protein-based IMAC, peptide-based IMAC, and MudPIT for
efficient phosphoproteomic analysis.";
J. Proteome Res. 7:1346-1351(2008).
[9]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-377, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007;
Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,
Greff Z., Keri G., Stemmann O., Mann M.;
"Kinase-selective enrichment enables quantitative phosphoproteomics of
the kinome across the cell cycle.";
Mol. Cell 31:438-448(2008).
[10]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-274; SER-275; SER-279;
THR-285; SER-289; SER-291; SER-377; SER-386 AND THR-406, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18669648; DOI=10.1073/pnas.0805139105;
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
Elledge S.J., Gygi S.P.;
"A quantitative atlas of mitotic phosphorylation.";
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
[11]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19413330; DOI=10.1021/ac9004309;
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,
Mohammed S.;
"Lys-N and trypsin cover complementary parts of the phosphoproteome in
a refined SCX-based approach.";
Anal. Chem. 81:4493-4501(2009).
[12]
ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, PHOSPHORYLATION [LARGE
SCALE ANALYSIS] AT SER-198; SER-289; SER-377; SER-386 AND THR-406,
CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS], AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=20068231; DOI=10.1126/scisignal.2000475;
Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S.,
Mann M.;
"Quantitative phosphoproteomics reveals widespread full
phosphorylation site occupancy during mitosis.";
Sci. Signal. 3:RA3-RA3(2010).
[13]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21269460; DOI=10.1186/1752-0509-5-17;
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
"Initial characterization of the human central proteome.";
BMC Syst. Biol. 5:17-17(2011).
[14]
INTERACTION WITH DNAJB6.
PubMed=22366786; DOI=10.1038/ng.1103;
Sarparanta J., Jonson P.H., Golzio C., Sandell S., Luque H.,
Screen M., McDonald K., Stajich J.M., Mahjneh I., Vihola A.,
Raheem O., Penttila S., Lehtinen S., Huovinen S., Palmio J., Tasca G.,
Ricci E., Hackman P., Hauser M., Katsanis N., Udd B.;
"Mutations affecting the cytoplasmic functions of the co-chaperone
DNAJB6 cause limb-girdle muscular dystrophy.";
Nat. Genet. 44:450-455(2012).
[15]
INTERACTION WITH SYNPO2.
PubMed=23434281; DOI=10.1016/j.cub.2013.01.064;
Ulbricht A., Eppler F.J., Tapia V.E., van der Ven P.F., Hampe N.,
Hersch N., Vakeel P., Stadel D., Haas A., Saftig P., Behrends C.,
Fuerst D.O., Volkmer R., Hoffmann B., Kolanus W., Hoehfeld J.;
"Cellular mechanotransduction relies on tension-induced and chaperone-
assisted autophagy.";
Curr. Biol. 23:430-435(2013).
[16]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-173; SER-269; SER-275;
SER-279; THR-285; SER-289; SER-291; SER-377 AND THR-406, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma, and Erythroleukemia;
PubMed=23186163; DOI=10.1021/pr300630k;
Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
Mohammed S.;
"Toward a comprehensive characterization of a human cancer cell
phosphoproteome.";
J. Proteome Res. 12:260-271(2013).
[17]
FUNCTION, AND INTERACTION WITH HSPA1A; HSPA1B AND HSPA8.
PubMed=24318877; DOI=10.1074/jbc.M113.521997;
Rauch J.N., Gestwicki J.E.;
"Binding of human nucleotide exchange factors to heat shock protein 70
(Hsp70) generates functionally distinct complexes in vitro.";
J. Biol. Chem. 289:1402-1414(2014).
[18]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-377 AND SER-385, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D.,
Wang L., Ye M., Zou H.;
"An enzyme assisted RP-RPLC approach for in-depth analysis of human
liver phosphoproteome.";
J. Proteomics 96:253-262(2014).
[19]
SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-445, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=25114211; DOI=10.1073/pnas.1413825111;
Impens F., Radoshevich L., Cossart P., Ribet D.;
"Mapping of SUMO sites and analysis of SUMOylation changes induced by
external stimuli.";
Proc. Natl. Acad. Sci. U.S.A. 111:12432-12437(2014).
[20]
FUNCTION, INTERACTION WITH HSF1, AND SUBCELLULAR LOCATION.
PubMed=26159920; DOI=10.1016/j.bbrc.2015.07.006;
Jin Y.H., Ahn S.G., Kim S.A.;
"BAG3 affects the nucleocytoplasmic shuttling of HSF1 upon heat
stress.";
Biochem. Biophys. Res. Commun. 464:561-567(2015).
[21]
FUNCTION, INTERACTION WITH HSPA8, AND MUTAGENESIS OF 480-ARG-LYS-481.
PubMed=27474739; DOI=10.1074/jbc.M116.742502;
Rauch J.N., Zuiderweg E.R., Gestwicki J.E.;
"Non-canonical interactions between heat shock cognate protein 70
(Hsc70) and Bcl2-associated anthanogene (BAG) co-chaperones are
important for client release.";
J. Biol. Chem. 291:19848-19857(2016).
[22]
INTERACTION WITH HSPB8.
PubMed=28144995; DOI=10.1002/humu.23189;
Echaniz-Laguna A., Geuens T., Petiot P., Pereon Y., Adriaenssens E.,
Haidar M., Capponi S., Maisonobe T., Fournier E., Dubourg O.,
Degos B., Salachas F., Lenglet T., Eymard B., Delmont E., Pouget J.,
Juntas Morales R., Goizet C., Latour P., Timmerman V., Stojkovic T.;
"Axonal Neuropathies due to Mutations in Small Heat Shock Proteins:
Clinical, Genetic, and Functional Insights into Novel Mutations.";
Hum. Mutat. 38:556-568(2017).
[23]
SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-445, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=28112733; DOI=10.1038/nsmb.3366;
Hendriks I.A., Lyon D., Young C., Jensen L.J., Vertegaal A.C.,
Nielsen M.L.;
"Site-specific mapping of the human SUMO proteome reveals co-
modification with phosphorylation.";
Nat. Struct. Mol. Biol. 24:325-336(2017).
[24]
VARIANT MFM6 LEU-209.
PubMed=19085932; DOI=10.1002/ana.21553;
Selcen D., Muntoni F., Burton B.K., Pegoraro E., Sewry C., Bite A.V.,
Engel A.G.;
"Mutation in BAG3 causes severe dominant childhood muscular
dystrophy.";
Ann. Neurol. 65:83-89(2009).
[25]
VARIANTS CMD1HH TRP-71 AND HIS-477.
PubMed=21353195; DOI=10.1016/j.ajhg.2011.01.016;
Norton N., Li D., Rieder M.J., Siegfried J.D., Rampersaud E.,
Zuchner S., Mangos S., Gonzalez-Quintana J., Wang L., McGee S.,
Reiser J., Martin E., Nickerson D.A., Hershberger R.E.;
"Genome-wide studies of copy number variation and exome sequencing
identify rare variants in BAG3 as a cause of dilated cardiomyopathy.";
Am. J. Hum. Genet. 88:273-282(2011).
[26]
VARIANT MFM6 LEU-209, AND VARIANT TRP-258.
PubMed=21361913; DOI=10.1111/j.1399-0004.2011.01659.x;
Lee H., Cherk S., Chan S., Wong S., Tong T., Ho W., Chan A., Lee K.,
Mak C.;
"BAG3-related myofibrillar myopathy in a Chinese family.";
Clin. Genet. 81:394-398(2012).
[27]
VARIANTS GLN-71; LEU-77; PHE-94; SER-115; ARG-151; THR-155; SER-380
AND LEU-407, AND VARIANTS CMD1HH LYS-455 AND MET-468.
PubMed=21459883; DOI=10.1093/eurheartj/ehr105;
Villard E., Perret C., Gary F., Proust C., Dilanian G.,
Hengstenberg C., Ruppert V., Arbustini E., Wichter T., Germain M.,
Dubourg O., Tavazzi L., Aumont M.C., DeGroote P., Fauchier L.,
Trochu J.N., Gibelin P., Aupetit J.F., Stark K., Erdmann J.,
Hetzer R., Roberts A.M., Barton P.J., Regitz-Zagrosek V., Aslam U.,
Duboscq-Bidot L., Meyborg M., Maisch B., Madeira H., Waldenstrom A.,
Galve E., Cleland J.G., Dorent R., Roizes G., Zeller T.,
Blankenberg S., Goodall A.H., Cook S., Tregouet D.A., Tiret L.,
Isnard R., Komajda M., Charron P., Cambien F.;
"A genome-wide association study identifies two loci associated with
heart failure due to dilated cardiomyopathy.";
Eur. Heart J. 32:1065-1076(2011).
[28]
VARIANTS CMD1HH TRP-218 AND PRO-462, VARIANTS TRP-258; ASN-300;
LEU-407 AND ASP-553, CHARACTERIZATION OF VARIANTS CMD1HH TRP-218 AND
PRO-462, CHARACTERIZATION OF VARIANT MFM6 LEU-209, AND
CHARACTERIZATION OF VARIANT TRP-258.
PubMed=21898660; DOI=10.1002/humu.21603;
Arimura T., Ishikawa T., Nunoda S., Kawai S., Kimura A.;
"Dilated cardiomyopathy-associated BAG3 mutations impair Z-disc
assembly and enhance sensitivity to apoptosis in cardiomyocytes.";
Hum. Mutat. 32:1481-1491(2011).
-!- FUNCTION: Co-chaperone for HSP70 and HSC70 chaperone proteins.
Acts as a nucleotide-exchange factor (NEF) promoting the release
of ADP from the HSP70 and HSC70 proteins thereby triggering
client/substrate protein release. Nucleotide release is mediated
via its binding to the nucleotide-binding domain (NBD) of
HSPA8/HSC70 where as the substrate release is mediated via its
binding to the substrate-binding domain (SBD) of HSPA8/HSC70
(PubMed:9873016, PubMed:27474739). Has anti-apoptotic activity
(PubMed:10597216). Plays a role in the HSF1 nucleocytoplasmic
transport (PubMed:26159920). {ECO:0000269|PubMed:10597216,
ECO:0000269|PubMed:24318877, ECO:0000269|PubMed:26159920,
ECO:0000269|PubMed:27474739, ECO:0000269|PubMed:9873016}.
-!- SUBUNIT: Binds to the ATPase domain of HSP70/HSC70 chaperones
(PubMed:9873016). Interacts with BCL2 (PubMed:10597216). Interacts
with phospholipase C-gamma proteins (PubMed:10980614). Interacts
with DNAJB6 (PubMed:22366786). Interacts (via BAG domain) with
HSF1; this interaction occurs in normal and heat-shocked cells
promoting HSF1 nucleocytoplasmic shuttling (PubMed:26159920).
Interacts with HSPA8 (via NBD) (PubMed:27474739, PubMed:24318877).
Interacts with HSPA1A (via NBD) and HSPA1B (via NBD)
(PubMed:24318877). Interacts (via WW domain 1) with SYNPO2 (via
PPPY motif) (PubMed:23434281). Interacts with HSPB8
(PubMed:28144995). {ECO:0000269|PubMed:10597216,
ECO:0000269|PubMed:10980614, ECO:0000269|PubMed:22366786,
ECO:0000269|PubMed:23434281, ECO:0000269|PubMed:24318877,
ECO:0000269|PubMed:26159920, ECO:0000269|PubMed:27474739,
ECO:0000269|PubMed:28144995, ECO:0000269|PubMed:9873016}.
-!- INTERACTION:
Q96BE0:-; NbExp=2; IntAct=EBI-747185, EBI-9356686;
Q96B67:ARRDC3; NbExp=7; IntAct=EBI-747185, EBI-2875665;
Q15038:DAZAP2; NbExp=8; IntAct=EBI-747185, EBI-724310;
Q00613:HSF1; NbExp=3; IntAct=EBI-747185, EBI-719620;
Q96IS6:HSPA8; NbExp=3; IntAct=EBI-747185, EBI-10289199;
P04792:HSPB1; NbExp=6; IntAct=EBI-747185, EBI-352682;
Q9UJY1:HSPB8; NbExp=8; IntAct=EBI-747185, EBI-739074;
Q99732:LITAF; NbExp=7; IntAct=EBI-747185, EBI-725647;
Q5S007:LRRK2; NbExp=2; IntAct=EBI-747185, EBI-5323863;
Q9Y5V3:MAGED1; NbExp=5; IntAct=EBI-747185, EBI-716006;
O76083:PDE9A; NbExp=3; IntAct=EBI-747185, EBI-742764;
Q15427:SF3B4; NbExp=7; IntAct=EBI-747185, EBI-348469;
Q13501:SQSTM1; NbExp=3; IntAct=EBI-747185, EBI-307104;
Q9UNE7:STUB1; NbExp=3; IntAct=EBI-747185, EBI-357085;
Q9BSI4:TINF2; NbExp=2; IntAct=EBI-747185, EBI-717399;
Q05BL1:TP53BP2; NbExp=4; IntAct=EBI-747185, EBI-11952721;
-!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:26159920}.
Cytoplasm {ECO:0000269|PubMed:26159920}. Note=Colocalizes with
HSF1 to the nucleus upon heat stress (PubMed:26159920).
{ECO:0000269|PubMed:26159920}.
-!- DISEASE: Myopathy, myofibrillar, 6 (MFM6) [MIM:612954]: A form of
myofibrillar myopathy, a group of chronic neuromuscular disorders
characterized at ultrastructural level by disintegration of the
sarcomeric Z disc and myofibrils, and replacement of the normal
myofibrillar markings by small dense granules, or larger hyaline
masses, or amorphous material. MFM6 is characterized by early-
onset of severe, progressive, diffuse muscle weakness associated
with cardiomyopathy, severe respiratory insufficiency during
adolescence, and a rigid spine in some patients.
{ECO:0000269|PubMed:19085932, ECO:0000269|PubMed:21361913,
ECO:0000269|PubMed:21898660}. Note=The disease is caused by
mutations affecting the gene represented in this entry.
-!- DISEASE: Cardiomyopathy, dilated 1HH (CMD1HH) [MIM:613881]: A
disorder characterized by ventricular dilation and impaired
systolic function, resulting in congestive heart failure and
arrhythmia. Patients are at risk of premature death.
{ECO:0000269|PubMed:21353195, ECO:0000269|PubMed:21459883,
ECO:0000269|PubMed:21898660}. Note=The disease is caused by
mutations affecting the gene represented in this entry.
-!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology
and Haematology;
URL="http://atlasgeneticsoncology.org/Genes/BAG3ID43160ch10q26.html";
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EMBL; AF095193; AAD16122.2; -; mRNA.
EMBL; AF127139; AAF26839.1; -; mRNA.
EMBL; AF071218; AAF69592.2; -; mRNA.
EMBL; AK291333; BAF84022.1; -; mRNA.
EMBL; AL137582; CAB70824.1; -; mRNA.
EMBL; BC006418; AAH06418.1; -; mRNA.
EMBL; BC014656; AAH14656.1; -; mRNA.
EMBL; BC107786; AAI07787.1; -; mRNA.
CCDS; CCDS7615.1; -.
RefSeq; NP_004272.2; NM_004281.3.
UniGene; Hs.523309; -.
ProteinModelPortal; O95817; -.
SMR; O95817; -.
BioGrid; 114907; 484.
CORUM; O95817; -.
DIP; DIP-41273N; -.
IntAct; O95817; 129.
MINT; MINT-208995; -.
STRING; 9606.ENSP00000358081; -.
iPTMnet; O95817; -.
PhosphoSitePlus; O95817; -.
BioMuta; BAG3; -.
EPD; O95817; -.
MaxQB; O95817; -.
PaxDb; O95817; -.
PeptideAtlas; O95817; -.
PRIDE; O95817; -.
DNASU; 9531; -.
Ensembl; ENST00000369085; ENSP00000358081; ENSG00000151929.
GeneID; 9531; -.
KEGG; hsa:9531; -.
UCSC; uc001lem.4; human.
CTD; 9531; -.
DisGeNET; 9531; -.
EuPathDB; HostDB:ENSG00000151929.9; -.
GeneCards; BAG3; -.
GeneReviews; BAG3; -.
HGNC; HGNC:939; BAG3.
HPA; HPA018493; -.
HPA; HPA020586; -.
MalaCards; BAG3; -.
MIM; 603883; gene.
MIM; 612954; phenotype.
MIM; 613881; phenotype.
neXtProt; NX_O95817; -.
OpenTargets; ENSG00000151929; -.
Orphanet; 154; Familial isolated dilated cardiomyopathy.
Orphanet; 199340; Muscular dystrophy, Selcen type.
PharmGKB; PA25239; -.
eggNOG; KOG0940; Eukaryota.
eggNOG; KOG4361; Eukaryota.
eggNOG; COG5021; LUCA.
GeneTree; ENSGT00530000063256; -.
HOGENOM; HOG000050234; -.
HOVERGEN; HBG003419; -.
InParanoid; O95817; -.
KO; K09557; -.
OMA; QTGWPFF; -.
OrthoDB; EOG091G08LY; -.
PhylomeDB; O95817; -.
TreeFam; TF102013; -.
Reactome; R-HSA-3371453; Regulation of HSF1-mediated heat shock response.
SignaLink; O95817; -.
SIGNOR; O95817; -.
ChiTaRS; BAG3; human.
GeneWiki; BAG3; -.
GenomeRNAi; 9531; -.
PMAP-CutDB; O95817; -.
PRO; PR:O95817; -.
Proteomes; UP000005640; Chromosome 10.
Bgee; ENSG00000151929; -.
CleanEx; HS_BAG3; -.
ExpressionAtlas; O95817; baseline and differential.
Genevisible; O95817; HS.
GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
GO; GO:0005829; C:cytosol; IDA:HPA.
GO; GO:0043005; C:neuron projection; IEA:Ensembl.
GO; GO:0005634; C:nucleus; IDA:UniProtKB.
GO; GO:0005886; C:plasma membrane; IDA:HPA.
GO; GO:0030018; C:Z disc; IEA:Ensembl.
GO; GO:0000774; F:adenyl-nucleotide exchange factor activity; IDA:UniProtKB.
GO; GO:0045296; F:cadherin binding; IDA:BHF-UCL.
GO; GO:0051087; F:chaperone binding; IEA:InterPro.
GO; GO:0032403; F:protein complex binding; IEA:Ensembl.
GO; GO:0007420; P:brain development; IEA:Ensembl.
GO; GO:0034605; P:cellular response to heat; IDA:UniProtKB.
GO; GO:0071260; P:cellular response to mechanical stimulus; IEA:Ensembl.
GO; GO:0097192; P:extrinsic apoptotic signaling pathway in absence of ligand; IEA:Ensembl.
GO; GO:0008625; P:extrinsic apoptotic signaling pathway via death domain receptors; IDA:MGI.
GO; GO:0043066; P:negative regulation of apoptotic process; NAS:UniProtKB.
GO; GO:0010664; P:negative regulation of striated muscle cell apoptotic process; IEA:Ensembl.
GO; GO:0097201; P:negative regulation of transcription from RNA polymerase II promoter in response to stress; IMP:UniProtKB.
GO; GO:0046827; P:positive regulation of protein export from nucleus; IMP:UniProtKB.
GO; GO:0042993; P:positive regulation of transcription factor import into nucleus; IMP:UniProtKB.
GO; GO:0006457; P:protein folding; NAS:UniProtKB.
GO; GO:0050821; P:protein stabilization; IEA:Ensembl.
GO; GO:1900034; P:regulation of cellular response to heat; TAS:Reactome.
GO; GO:0021510; P:spinal cord development; IEA:Ensembl.
CDD; cd00201; WW; 1.
Gene3D; 1.20.58.120; -; 1.
InterPro; IPR003103; BAG_domain.
InterPro; IPR001202; WW_dom.
Pfam; PF02179; BAG; 1.
Pfam; PF00397; WW; 1.
SMART; SM00264; BAG; 1.
SMART; SM00456; WW; 1.
SUPFAM; SSF51045; SSF51045; 1.
SUPFAM; SSF63491; SSF63491; 1.
PROSITE; PS51035; BAG; 1.
PROSITE; PS01159; WW_DOMAIN_1; 1.
PROSITE; PS50020; WW_DOMAIN_2; 1.
1: Evidence at protein level;
Acetylation; Apoptosis; Cardiomyopathy; Chaperone; Complete proteome;
Cytoplasm; Disease mutation; Isopeptide bond; Methylation;
Myofibrillar myopathy; Nucleus; Phosphoprotein; Polymorphism;
Reference proteome; Repeat; Ubl conjugation.
INIT_MET 1 1 Removed. {ECO:0000244|PubMed:20068231}.
CHAIN 2 575 BAG family molecular chaperone regulator
3.
/FTId=PRO_0000088868.
DOMAIN 20 54 WW 1. {ECO:0000255|PROSITE-
ProRule:PRU00224}.
DOMAIN 124 154 WW 2. {ECO:0000255|PROSITE-
ProRule:PRU00224}.
DOMAIN 421 498 BAG. {ECO:0000255|PROSITE-
ProRule:PRU00369}.
COMPBIAS 180 187 Poly-Ser.
MOD_RES 2 2 N-acetylserine.
{ECO:0000244|PubMed:20068231}.
MOD_RES 136 136 Phosphoserine.
{ECO:0000250|UniProtKB:Q9JLV1}.
MOD_RES 139 139 Omega-N-methylarginine.
{ECO:0000250|UniProtKB:Q9JLV1}.
MOD_RES 173 173 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 198 198 Phosphoserine.
{ECO:0000244|PubMed:20068231}.
MOD_RES 261 261 Omega-N-methylarginine.
{ECO:0000250|UniProtKB:Q9JLV1}.
MOD_RES 269 269 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 274 274 Phosphoserine.
{ECO:0000244|PubMed:18669648}.
MOD_RES 275 275 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:23186163}.
MOD_RES 279 279 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:23186163}.
MOD_RES 285 285 Phosphothreonine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:23186163}.
MOD_RES 289 289 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:23186163}.
MOD_RES 291 291 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:23186163}.
MOD_RES 377 377 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:18691976,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:23186163,
ECO:0000244|PubMed:24275569}.
MOD_RES 385 385 Phosphoserine.
{ECO:0000244|PubMed:24275569}.
MOD_RES 386 386 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:20068231}.
MOD_RES 406 406 Phosphothreonine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:23186163}.
CROSSLNK 445 445 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO1).
{ECO:0000244|PubMed:25114211}.
CROSSLNK 445 445 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:28112733}.
VARIANT 71 71 R -> Q (in dbSNP:rs35434411).
{ECO:0000269|PubMed:21459883}.
/FTId=VAR_048344.
VARIANT 71 71 R -> W (in CMD1HH; dbSNP:rs387906874).
{ECO:0000269|PubMed:21353195}.
/FTId=VAR_065479.
VARIANT 77 77 P -> L (in dbSNP:rs141355480).
{ECO:0000269|PubMed:21459883}.
/FTId=VAR_066777.
VARIANT 94 94 I -> F (in dbSNP:rs145393807).
{ECO:0000269|PubMed:21459883}.
/FTId=VAR_066778.
VARIANT 115 115 P -> S (in dbSNP:rs774241343).
{ECO:0000269|PubMed:21459883}.
/FTId=VAR_066779.
VARIANT 151 151 C -> R (in dbSNP:rs2234962).
{ECO:0000269|PubMed:10597216,
ECO:0000269|PubMed:21459883}.
/FTId=VAR_048345.
VARIANT 155 155 A -> T (in dbSNP:rs61756328).
{ECO:0000269|PubMed:21459883}.
/FTId=VAR_066780.
VARIANT 209 209 P -> L (in MFM6; interferes with the
differentiation of skeletal muscle cells;
does not cause functional alterations in
cardiomyocyte cells; dbSNP:rs121918312).
{ECO:0000269|PubMed:19085932,
ECO:0000269|PubMed:21361913,
ECO:0000269|PubMed:21898660}.
/FTId=VAR_063089.
VARIANT 218 218 R -> W (in CMD1HH; interferes with the
assembly of Z-disks; increases stress-
induced apoptosis; dbSNP:rs397514506).
{ECO:0000269|PubMed:21898660}.
/FTId=VAR_066781.
VARIANT 258 258 R -> W (polymorphism; no functional
consequences; dbSNP:rs117671123).
{ECO:0000269|PubMed:21361913,
ECO:0000269|PubMed:21898660}.
/FTId=VAR_066782.
VARIANT 300 300 D -> N (in dbSNP:rs78439745).
{ECO:0000269|PubMed:21898660}.
/FTId=VAR_066783.
VARIANT 380 380 P -> S (in dbSNP:rs144692954).
{ECO:0000269|PubMed:21459883}.
/FTId=VAR_066784.
VARIANT 405 405 A -> V (in dbSNP:rs11199064).
/FTId=VAR_048346.
VARIANT 407 407 P -> L (in dbSNP:rs3858340).
{ECO:0000269|PubMed:21459883,
ECO:0000269|PubMed:21898660}.
/FTId=VAR_048347.
VARIANT 455 455 E -> K (in CMD1HH; dbSNP:rs397516881).
{ECO:0000269|PubMed:21459883}.
/FTId=VAR_066785.
VARIANT 462 462 L -> P (in CMD1HH; interferes with the
assembly of Z-disks; increases stress-
induced apoptosis; dbSNP:rs397514507).
{ECO:0000269|PubMed:21898660}.
/FTId=VAR_066786.
VARIANT 468 468 V -> M (in CMD1HH).
{ECO:0000269|PubMed:21459883}.
/FTId=VAR_066787.
VARIANT 477 477 R -> H (in CMD1HH; dbSNP:rs387906876).
{ECO:0000269|PubMed:21353195}.
/FTId=VAR_065480.
VARIANT 553 553 E -> D (in dbSNP:rs763530097).
{ECO:0000269|PubMed:21898660}.
/FTId=VAR_066788.
MUTAGEN 480 481 RR->AA: Significant loss of interaction
with HSPA8.
{ECO:0000269|PubMed:27474739}.
CONFLICT 227 227 Q -> K (in Ref. 1; AAD16122).
{ECO:0000305}.
CONFLICT 237 237 Q -> R (in Ref. 1; AAD16122).
{ECO:0000305}.
CONFLICT 304 304 Missing (in Ref. 5; CAB70824).
{ECO:0000305}.
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


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