BAG3_MOUSE
ID BAG3_MOUSE Reviewed; 577 AA.
AC Q9JLV1; Q9CQL3; Q9JJC7;
DT 11-JAN-2001, integrated into UniProtKB/Swiss-Prot.
DT 27-JUL-2011, sequence version 2.
DT 03-AUG-2022, entry version 174.
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;
GN Name=Bag3; Synonyms=Bis; ORFNames=MNCb-2243;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Brain;
RA Osada N., Kusuda J., Tanuma R., Ito A., Hirata M., Sugano S., Hashimoto K.;
RT "Isolation of full-length cDNA clones from mouse brain cDNA library made by
RT oligo-capping method.";
RL Submitted (APR-2000) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Bone, Pancreas, and Testis;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-297 AND SER-390, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT "Large-scale phosphorylation analysis of mouse liver.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-138; THR-291; SER-297;
RP SER-380; SER-382 AND SER-390, AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RC TISSUE=Brown adipose tissue, Heart, Liver, Lung, Pancreas, Spleen, and
RC Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [7]
RP METHYLATION [LARGE SCALE ANALYSIS] AT ARG-141 AND ARG-267, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain;
RX PubMed=24129315; DOI=10.1074/mcp.o113.027870;
RA Guo A., Gu H., Zhou J., Mulhern D., Wang Y., Lee K.A., Yang V., Aguiar M.,
RA Kornhauser J., Jia X., Ren J., Beausoleil S.A., Silva J.C., Vemulapalli V.,
RA Bedford M.T., Comb M.J.;
RT "Immunoaffinity enrichment and mass spectrometry analysis of protein
RT methylation.";
RL Mol. Cell. Proteomics 13:372-387(2014).
RN [8]
RP STRUCTURE BY NMR OF 404-503.
RG RIKEN structural genomics initiative (RSGI);
RT "Solution structure of the murine BAG domain of Bcl2-associated athanogene
RT 3.";
RL Submitted (FEB-2004) to the PDB data bank.
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. Has anti-apoptotic activity. Plays a role in the
CC HSF1 nucleocytoplasmic transport. {ECO:0000250|UniProtKB:O95817}.
CC -!- SUBUNIT: Binds to the ATPase domain of HSP70/HSC70 chaperones.
CC Interacts with BCL2. Interacts with phospholipase C-gamma proteins.
CC Interacts with DNAJB6. Interacts (via BAG domain) with HSF1; this
CC interaction occurs in normal and heat-shocked cells. Interacts with
CC HSPA8 (via NBD), HSPA1A (via NBD) and HSPA1B (via NBD). Interacts (via
CC WW domain 1) with SYNPO2 (via PPPY motif).
CC {ECO:0000250|UniProtKB:O95817}.
CC -!- INTERACTION:
CC Q9JLV1; Q8AZK7: EBNA-LP; Xeno; NbExp=2; IntAct=EBI-309231, EBI-1185167;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:O95817}. Cytoplasm
CC {ECO:0000250|UniProtKB:O95817}. Note=Colocalizes with HSF1 to the
CC nucleus upon heat stress. {ECO:0000250|UniProtKB:O95817}.
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DR EMBL; AF130471; AAF26840.1; -; mRNA.
DR EMBL; AB041583; BAA95066.1; -; mRNA.
DR EMBL; AK007414; BAB25024.1; -; mRNA.
DR EMBL; AK016510; BAB30278.1; -; mRNA.
DR EMBL; AK036675; BAC29531.1; -; mRNA.
DR EMBL; CH466531; EDL17651.1; -; Genomic_DNA.
DR CCDS; CCDS21898.1; -.
DR RefSeq; NP_038891.4; NM_013863.5.
DR PDB; 1UK5; NMR; -; A=406-503.
DR PDBsum; 1UK5; -.
DR AlphaFoldDB; Q9JLV1; -.
DR SMR; Q9JLV1; -.
DR BioGRID; 205891; 70.
DR IntAct; Q9JLV1; 5.
DR MINT; Q9JLV1; -.
DR STRING; 10090.ENSMUSP00000033136; -.
DR iPTMnet; Q9JLV1; -.
DR PhosphoSitePlus; Q9JLV1; -.
DR SwissPalm; Q9JLV1; -.
DR jPOST; Q9JLV1; -.
DR MaxQB; Q9JLV1; -.
DR PaxDb; Q9JLV1; -.
DR PRIDE; Q9JLV1; -.
DR ProteomicsDB; 265200; -.
DR Antibodypedia; 18850; 466 antibodies from 40 providers.
DR DNASU; 29810; -.
DR Ensembl; ENSMUST00000033136; ENSMUSP00000033136; ENSMUSG00000030847.
DR GeneID; 29810; -.
DR KEGG; mmu:29810; -.
DR UCSC; uc009jzb.2; mouse.
DR CTD; 9531; -.
DR MGI; MGI:1352493; Bag3.
DR VEuPathDB; HostDB:ENSMUSG00000030847; -.
DR eggNOG; KOG0940; Eukaryota.
DR eggNOG; KOG4361; Eukaryota.
DR GeneTree; ENSGT00940000159204; -.
DR HOGENOM; CLU_034378_0_0_1; -.
DR InParanoid; Q9JLV1; -.
DR OMA; THSPMMQ; -.
DR OrthoDB; 715914at2759; -.
DR TreeFam; TF102013; -.
DR Reactome; R-MMU-3371453; Regulation of HSF1-mediated heat shock response.
DR BioGRID-ORCS; 29810; 2 hits in 74 CRISPR screens.
DR ChiTaRS; Bag3; mouse.
DR EvolutionaryTrace; Q9JLV1; -.
DR PRO; PR:Q9JLV1; -.
DR Proteomes; UP000000589; Chromosome 7.
DR RNAct; Q9JLV1; protein.
DR Bgee; ENSMUSG00000030847; Expressed in cardiac muscle of left ventricle and 209 other tissues.
DR Genevisible; Q9JLV1; MM.
DR GO; GO:0101031; C:chaperone complex; ISO:MGI.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0016020; C:membrane; IBA:GO_Central.
DR GO; GO:0043005; C:neuron projection; ISO:MGI.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0001725; C:stress fiber; ISO:MGI.
DR GO; GO:0030018; C:Z disc; IDA:MGI.
DR GO; GO:0000774; F:adenyl-nucleotide exchange factor activity; ISS:UniProtKB.
DR GO; GO:0051087; F:chaperone binding; ISO:MGI.
DR GO; GO:0044877; F:protein-containing complex binding; IDA:MGI.
DR GO; GO:0000045; P:autophagosome assembly; ISO:MGI.
DR GO; GO:0007420; P:brain development; IEA:Ensembl.
DR GO; GO:0034605; P:cellular response to heat; ISS:UniProtKB.
DR GO; GO:0071260; P:cellular response to mechanical stimulus; IMP:MGI.
DR GO; GO:0034620; P:cellular response to unfolded protein; ISO:MGI.
DR GO; GO:0061684; P:chaperone-mediated autophagy; ISO:MGI.
DR GO; GO:0097192; P:extrinsic apoptotic signaling pathway in absence of ligand; IDA:MGI.
DR GO; GO:0008625; P:extrinsic apoptotic signaling pathway via death domain receptors; ISO:MGI.
DR GO; GO:0046716; P:muscle cell cellular homeostasis; IMP:BHF-UCL.
DR GO; GO:0043066; P:negative regulation of apoptotic process; ISO:MGI.
DR GO; GO:1903215; P:negative regulation of protein targeting to mitochondrion; ISO:MGI.
DR GO; GO:0010664; P:negative regulation of striated muscle cell apoptotic process; IMP:MGI.
DR GO; GO:0097201; P:negative regulation of transcription from RNA polymerase II promoter in response to stress; ISS:UniProtKB.
DR GO; GO:1905337; P:positive regulation of aggrephagy; ISO:MGI.
DR GO; GO:0046827; P:positive regulation of protein export from nucleus; ISS:UniProtKB.
DR GO; GO:0042307; P:positive regulation of protein import into nucleus; ISS:UniProtKB.
DR GO; GO:0050821; P:protein stabilization; IMP:MGI.
DR GO; GO:0021510; P:spinal cord development; IEA:Ensembl.
DR GO; GO:0010658; P:striated muscle cell apoptotic process; IMP:MGI.
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 3D-structure; Acetylation; Apoptosis; Chaperone; Cytoplasm;
KW Isopeptide bond; Methylation; Nucleus; Phosphoprotein; Reference proteome;
KW Repeat; Ubl conjugation.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:O95817"
FT CHAIN 2..577
FT /note="BAG family molecular chaperone regulator 3"
FT /id="PRO_0000088869"
FT DOMAIN 22..56
FT /note="WW 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00224"
FT DOMAIN 126..157
FT /note="WW 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00224"
FT DOMAIN 426..503
FT /note="BAG"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00369"
FT REGION 1..81
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 126..207
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 229..427
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 524..577
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 129..204
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 229..250
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 311..339
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 376..390
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 547..570
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 2
FT /note="N-acetylserine"
FT /evidence="ECO:0000250|UniProtKB:O95817"
FT MOD_RES 138
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 141
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0007744|PubMed:24129315"
FT MOD_RES 179
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O95817"
FT MOD_RES 204
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O95817"
FT MOD_RES 267
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0007744|PubMed:24129315"
FT MOD_RES 280
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O95817"
FT MOD_RES 281
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O95817"
FT MOD_RES 285
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O95817"
FT MOD_RES 291
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 297
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17242355,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 380
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 382
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 390
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17242355,
FT ECO:0007744|PubMed:21183079"
FT CROSSLNK 450
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO1); alternate"
FT /evidence="ECO:0000250|UniProtKB:O95817"
FT CROSSLNK 450
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2); alternate"
FT /evidence="ECO:0000250|UniProtKB:O95817"
FT CONFLICT 74
FT /note="D -> N (in Ref. 1; AAF26840)"
FT /evidence="ECO:0000305"
FT CONFLICT 527
FT /note="Q -> P (in Ref. 1; AAF26840)"
FT /evidence="ECO:0000305"
FT CONFLICT 539
FT /note="K -> E (in Ref. 2; BAA95066)"
FT /evidence="ECO:0000305"
FT STRAND 417..420
FT /evidence="ECO:0007829|PDB:1UK5"
FT HELIX 425..445
FT /evidence="ECO:0007829|PDB:1UK5"
FT STRAND 451..453
FT /evidence="ECO:0007829|PDB:1UK5"
FT HELIX 454..471
FT /evidence="ECO:0007829|PDB:1UK5"
FT HELIX 479..503
FT /evidence="ECO:0007829|PDB:1UK5"
SQ SEQUENCE 577 AA; 61860 MW; 7BBF296A4A2EF7E3 CRC64;
MSAATQSPMM QMASGNGASD RDPLPPGWEI KIDPQTGWPF FVDHNSRTTT WNDPRVPPEG
PKDTASSANG PSRDGSRLLP IREGHPIYPQ LRPGYIPIPV LHEGSENRQP HLFHAYSQPG
VQRFRTEAAA ATPQRSQSPL RGGMTEAAQT DKQCGQMPAT ATTAAAQPPT AHGPERSQSP
AASDCSSSSS SASLPSSGRS SLGSHQLPRG YIPIPVIHEQ NITRPAAQPS FHQAQKTHYP
AQQGEYQPQQ PVYHKIQGDD WEPRPLRAAS PFRSPVRGAS SREGSPARSG TPVHCPSPIR
VHTVVDRPQP MTHREPPPVT QPENKPESKP GPAGPDLPPG HIPIQVIRRE ADSKPVSQKS
PPPAEKVEVK VSSAPIPCPS PSPAPSAVPS PPKNVAAEQK AAPSPAPAEP AAPKSGEAET
PPKHPGVLKV EAILEKVQGL EQAVDSFEGK KTDKKYLMIE EYLTKELLAL DSVDPEGRAD
VRQARRDGVR KVQTILEKLE QKAIDVPGQV QVYELQPSNL EAEQPLQEIM GAVVADKDKK
GPENKDPQTE SQQLEAKAAT PPNPSNPADS AGNLVAP
