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

 BAG3_MOUSE              Reviewed;         577 AA.
Q9JLV1; Q9CQL3; Q9JJC7;
11-JAN-2001, integrated into UniProtKB/Swiss-Prot.
27-JUL-2011, sequence version 2.
05-DEC-2018, entry version 156.
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;
Name=Bag3; Synonyms=Bis; ORFNames=MNCb-2243;
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
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).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=C57BL/6J; TISSUE=Brain;
Osada N., Kusuda J., Tanuma R., Ito A., Hirata M., Sugano S.,
Hashimoto K.;
"Isolation of full-length cDNA clones from mouse brain cDNA library
made by oligo-capping method.";
Submitted (APR-2000) to the EMBL/GenBank/DDBJ databases.
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=C57BL/6J; TISSUE=Bone, Pancreas, and Testis;
PubMed=16141072; DOI=10.1126/science.1112014;
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
Hayashizaki Y.;
"The transcriptional landscape of the mammalian genome.";
Science 309:1559-1563(2005).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
[5]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-297 AND SER-390, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=17242355; DOI=10.1073/pnas.0609836104;
Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
"Large-scale phosphorylation analysis of mouse liver.";
Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
[6]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-138; THR-291; SER-297;
SER-380; SER-382 AND SER-390, AND IDENTIFICATION BY MASS SPECTROMETRY
[LARGE SCALE ANALYSIS].
TISSUE=Brown adipose tissue, Heart, Liver, Lung, Pancreas, Spleen, and
Testis;
PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
"A tissue-specific atlas of mouse protein phosphorylation and
expression.";
Cell 143:1174-1189(2010).
[7]
METHYLATION [LARGE SCALE ANALYSIS] AT ARG-141 AND ARG-267, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Brain;
PubMed=24129315; DOI=10.1074/mcp.O113.027870;
Guo A., Gu H., Zhou J., Mulhern D., Wang Y., Lee K.A., Yang V.,
Aguiar M., Kornhauser J., Jia X., Ren J., Beausoleil S.A., Silva J.C.,
Vemulapalli V., Bedford M.T., Comb M.J.;
"Immunoaffinity enrichment and mass spectrometry analysis of protein
methylation.";
Mol. Cell. Proteomics 13:372-387(2014).
[8]
STRUCTURE BY NMR OF 404-503.
RIKEN structural genomics initiative (RSGI);
"Solution structure of the murine BAG domain of Bcl2-associated
athanogene 3.";
Submitted (FEB-2004) to the PDB data bank.
-!- 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. Has
anti-apoptotic activity. Plays a role in the HSF1
nucleocytoplasmic transport. {ECO:0000250|UniProtKB:O95817}.
-!- SUBUNIT: Binds to the ATPase domain of HSP70/HSC70 chaperones.
Interacts with BCL2. Interacts with phospholipase C-gamma
proteins. Interacts with DNAJB6. Interacts (via BAG domain) with
HSF1; this interaction occurs in normal and heat-shocked cells.
Interacts with HSPA8 (via NBD), HSPA1A (via NBD) and HSPA1B (via
NBD). Interacts (via WW domain 1) with SYNPO2 (via PPPY motif).
{ECO:0000250|UniProtKB:O95817}.
-!- INTERACTION:
Q8AZK7:EBNA-LP (xeno); NbExp=2; IntAct=EBI-309231, EBI-1185167;
-!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:O95817}.
Cytoplasm {ECO:0000250|UniProtKB:O95817}. Note=Colocalizes with
HSF1 to the nucleus upon heat stress.
{ECO:0000250|UniProtKB:O95817}.
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EMBL; AF130471; AAF26840.1; -; mRNA.
EMBL; AB041583; BAA95066.1; -; mRNA.
EMBL; AK007414; BAB25024.1; -; mRNA.
EMBL; AK016510; BAB30278.1; -; mRNA.
EMBL; AK036675; BAC29531.1; -; mRNA.
EMBL; CH466531; EDL17651.1; -; Genomic_DNA.
CCDS; CCDS21898.1; -.
RefSeq; NP_038891.4; NM_013863.5.
UniGene; Mm.84073; -.
PDB; 1UK5; NMR; -; A=406-503.
PDBsum; 1UK5; -.
ProteinModelPortal; Q9JLV1; -.
SMR; Q9JLV1; -.
BioGrid; 205891; 7.
IntAct; Q9JLV1; 6.
MINT; Q9JLV1; -.
STRING; 10090.ENSMUSP00000033136; -.
iPTMnet; Q9JLV1; -.
PhosphoSitePlus; Q9JLV1; -.
SwissPalm; Q9JLV1; -.
MaxQB; Q9JLV1; -.
PaxDb; Q9JLV1; -.
PRIDE; Q9JLV1; -.
Ensembl; ENSMUST00000033136; ENSMUSP00000033136; ENSMUSG00000030847.
GeneID; 29810; -.
KEGG; mmu:29810; -.
UCSC; uc009jzb.2; mouse.
CTD; 9531; -.
MGI; MGI:1352493; Bag3.
eggNOG; KOG0940; Eukaryota.
eggNOG; KOG4361; Eukaryota.
eggNOG; COG5021; LUCA.
GeneTree; ENSGT00940000159204; -.
HOGENOM; HOG000050234; -.
HOVERGEN; HBG003419; -.
InParanoid; Q9JLV1; -.
KO; K09557; -.
OMA; QTGWPFF; -.
OrthoDB; EOG091G08LY; -.
TreeFam; TF102013; -.
Reactome; R-MMU-3371453; Regulation of HSF1-mediated heat shock response.
EvolutionaryTrace; Q9JLV1; -.
PRO; PR:Q9JLV1; -.
Proteomes; UP000000589; Chromosome 7.
Bgee; ENSMUSG00000030847; Expressed in 242 organ(s), highest expression level in cardiac muscle of left ventricle.
CleanEx; MM_BAG3; -.
Genevisible; Q9JLV1; MM.
GO; GO:0101031; C:chaperone complex; IEA:Ensembl.
GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
GO; GO:0005829; C:cytosol; ISO:MGI.
GO; GO:0043005; C:neuron projection; ISO:MGI.
GO; GO:0005634; C:nucleus; ISS:UniProtKB.
GO; GO:0005886; C:plasma membrane; ISO:MGI.
GO; GO:0001725; C:stress fiber; IEA:Ensembl.
GO; GO:0030018; C:Z disc; IDA:MGI.
GO; GO:0000774; F:adenyl-nucleotide exchange factor activity; ISS:UniProtKB.
GO; GO:0051087; F:chaperone binding; IEA:Ensembl.
GO; GO:0044877; F:protein-containing complex binding; IDA:MGI.
GO; GO:0000045; P:autophagosome assembly; IEA:Ensembl.
GO; GO:0007420; P:brain development; IEA:Ensembl.
GO; GO:0034605; P:cellular response to heat; ISS:UniProtKB.
GO; GO:0071260; P:cellular response to mechanical stimulus; IMP:MGI.
GO; GO:0034620; P:cellular response to unfolded protein; IEA:Ensembl.
GO; GO:0061684; P:chaperone-mediated autophagy; IEA:Ensembl.
GO; GO:0097192; P:extrinsic apoptotic signaling pathway in absence of ligand; IDA:MGI.
GO; GO:0008625; P:extrinsic apoptotic signaling pathway via death domain receptors; ISO:MGI.
GO; GO:0046716; P:muscle cell cellular homeostasis; IMP:BHF-UCL.
GO; GO:0043066; P:negative regulation of apoptotic process; ISO:MGI.
GO; GO:1903215; P:negative regulation of protein targeting to mitochondrion; ISO:MGI.
GO; GO:0010664; P:negative regulation of striated muscle cell apoptotic process; IMP:MGI.
GO; GO:0097201; P:negative regulation of transcription from RNA polymerase II promoter in response to stress; ISS:UniProtKB.
GO; GO:1905337; P:positive regulation of aggrephagy; IEA:Ensembl.
GO; GO:0046827; P:positive regulation of protein export from nucleus; ISS:UniProtKB.
GO; GO:0042307; P:positive regulation of protein import into nucleus; ISS:UniProtKB.
GO; GO:0050821; P:protein stabilization; IMP:MGI.
GO; GO:0021510; P:spinal cord development; IEA:Ensembl.
CDD; cd00201; WW; 1.
Gene3D; 1.20.58.120; -; 1.
InterPro; IPR039773; BAG_chaperone_regulator.
InterPro; IPR036533; BAG_dom_sf.
InterPro; IPR003103; BAG_domain.
InterPro; IPR001202; WW_dom.
InterPro; IPR036020; WW_dom_sf.
PANTHER; PTHR12329; PTHR12329; 1.
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;
3D-structure; Acetylation; Apoptosis; Chaperone; Complete proteome;
Cytoplasm; Isopeptide bond; Methylation; Nucleus; Phosphoprotein;
Reference proteome; Repeat; Ubl conjugation.
INIT_MET 1 1 Removed. {ECO:0000250|UniProtKB:O95817}.
CHAIN 2 577 BAG family molecular chaperone regulator
3.
/FTId=PRO_0000088869.
DOMAIN 22 56 WW 1. {ECO:0000255|PROSITE-
ProRule:PRU00224}.
DOMAIN 126 157 WW 2. {ECO:0000255|PROSITE-
ProRule:PRU00224}.
DOMAIN 426 503 BAG. {ECO:0000255|PROSITE-
ProRule:PRU00369}.
COMPBIAS 186 193 Poly-Ser.
MOD_RES 2 2 N-acetylserine.
{ECO:0000250|UniProtKB:O95817}.
MOD_RES 138 138 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 141 141 Omega-N-methylarginine.
{ECO:0000244|PubMed:24129315}.
MOD_RES 179 179 Phosphoserine.
{ECO:0000250|UniProtKB:O95817}.
MOD_RES 204 204 Phosphoserine.
{ECO:0000250|UniProtKB:O95817}.
MOD_RES 267 267 Omega-N-methylarginine.
{ECO:0000244|PubMed:24129315}.
MOD_RES 280 280 Phosphoserine.
{ECO:0000250|UniProtKB:O95817}.
MOD_RES 281 281 Phosphoserine.
{ECO:0000250|UniProtKB:O95817}.
MOD_RES 285 285 Phosphoserine.
{ECO:0000250|UniProtKB:O95817}.
MOD_RES 291 291 Phosphothreonine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 297 297 Phosphoserine.
{ECO:0000244|PubMed:17242355,
ECO:0000244|PubMed:21183079}.
MOD_RES 380 380 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 382 382 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 390 390 Phosphoserine.
{ECO:0000244|PubMed:17242355,
ECO:0000244|PubMed:21183079}.
CROSSLNK 450 450 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO1);
alternate.
{ECO:0000250|UniProtKB:O95817}.
CROSSLNK 450 450 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2);
alternate.
{ECO:0000250|UniProtKB:O95817}.
CONFLICT 74 74 D -> N (in Ref. 1; AAF26840).
{ECO:0000305}.
CONFLICT 527 527 Q -> P (in Ref. 1; AAF26840).
{ECO:0000305}.
CONFLICT 539 539 K -> E (in Ref. 2; BAA95066).
{ECO:0000305}.
STRAND 417 420 {ECO:0000244|PDB:1UK5}.
HELIX 425 445 {ECO:0000244|PDB:1UK5}.
STRAND 451 453 {ECO:0000244|PDB:1UK5}.
HELIX 454 471 {ECO:0000244|PDB:1UK5}.
HELIX 479 503 {ECO:0000244|PDB:1UK5}.
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


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