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BAG family molecular chaperone regulator 1 (BAG-1) (Bcl-2-associated athanogene 1)

 BAG1_MOUSE              Reviewed;         355 AA.
Q60739; Q561N1; Q6IS45; Q9D7K6;
01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
15-JUL-1999, sequence version 3.
12-SEP-2018, entry version 159.
RecName: Full=BAG family molecular chaperone regulator 1;
Short=BAG-1;
AltName: Full=Bcl-2-associated athanogene 1;
Name=Bag1;
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] (ISOFORM 1).
TISSUE=Embryo;
PubMed=7834747; DOI=10.1016/0092-8674(95)90410-7;
Takayama S., Sato T., Krajewski S., Kochel K., Irie S., Millan J.A.,
Reed J.C.;
"Cloning and functional analysis of BAG-1: a novel Bcl-2-binding
protein with anti-cell death activity.";
Cell 80:279-284(1995).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
STRAIN=C57BL/6J; TISSUE=Tongue;
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).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=C57BL/6J;
PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
Lindblad-Toh K., Eichler E.E., Ponting C.P.;
"Lineage-specific biology revealed by a finished genome assembly of
the mouse.";
PLoS Biol. 7:E1000112-E1000112(2009).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
STRAIN=Czech II, and NMRI; TISSUE=Mammary tumor;
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).
[6]
IDENTIFICATION OF ISOFORMS 1 AND 2, ALTERNATIVE INITIATION,
SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
PubMed=9396724; DOI=10.1042/bj3280807;
Packham G., Brimmell M., Cleveland J.L.;
"Mammalian cells express two differently localized Bag-1 isoforms
generated by alternative translation initiation.";
Biochem. J. 328:807-813(1997).
[7]
IDENTIFICATION OF ISOFORMS 1 AND 2, ALTERNATIVE INITIATION,
SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
PubMed=9679980;
Takayama S., Krajewski S., Krajewska M., Kitada S., Zapata J.M.,
Kochel K., Knee D., Scudiero D., Tudor G., Miller G.J., Miyashita T.,
Yamada M., Reed J.C.;
"Expression and location of Hsp70/Hsc-binding anti-apoptotic protein
BAG-1 and its variants in normal tissues and tumor cell lines.";
Cancer Res. 58:3116-3131(1998).
[8]
FUNCTION.
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).
[9]
INTERACTION WITH SIAH2, AND UBIQUITINATION.
PubMed=11257006;
Sourisseau T., Desbois C., Debure L., Bowtell D.D.L., Cato A.C.B.,
Schneikert J., Moyse E., Michel D.;
"Alteration of the stability of Bag-1 protein in the control of
olfactory neuronal apoptosis.";
J. Cell Sci. 114:1409-1416(2001).
[10]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Brain, Heart, Kidney, Lung, 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).
-!- FUNCTION: Co-chaperone for HSP70 and HSC70 chaperone proteins
(PubMed:9873016). 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. Inhibits the pro-apoptotic function of PPP1R15A, and
has anti-apoptotic activity. Markedly increases the anti-cell
death function of BCL2 induced by various stimuli (By similarity).
{ECO:0000250|UniProtKB:Q99933, ECO:0000269|PubMed:9873016}.
-!- SUBUNIT: Homodimer. Forms a heteromeric complex with HSP70/HSC70.
Binds to the ATPase domain of HSP/HSC70 chaperones. Interacts with
NR3C1. Interacts with the N-terminal region of STK19. Interacts
with PPP1R15A. Interacts with BCL2 in an ATP-dependent manner.
Interacts with SIAH1, HSPA8 (via NBD), HSPA1A (via NBD) and HSPA1B
(via NBD) (By similarity). Interacts with SIAH2 (PubMed:11257006).
{ECO:0000250|UniProtKB:Q99933, ECO:0000269|PubMed:11257006}.
-!- SUBCELLULAR LOCATION: Isoform 1: Nucleus.
-!- SUBCELLULAR LOCATION: Isoform 2: Cytoplasm.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative initiation; Named isoforms=2;
Name=1; Synonyms=BAG-1L, p50;
IsoId=Q60739-1; Sequence=Displayed;
Name=2; Synonyms=BAG-1S, p32;
IsoId=Q60739-2; Sequence=VSP_018667;
-!- TISSUE SPECIFICITY: Isoform 2 is expressed in the heart, lung,
kidney and spinal cord. Isoform 1 and isoform 2 are expressed in
hematopoietic cell lines. The levels of isoform 2 are relatively
constant in all the cell lines examined while the levels of
isoform 1 are more variable (at protein level). Isoform 1 is
expressed in the lung and kidney. Isoform 2 is expressed in
various tissues, with highest levels in testis and stomach.
{ECO:0000269|PubMed:9396724, ECO:0000269|PubMed:9679980}.
-!- PTM: Ubiquitinated; mediated by SIAH1 or SIAH2 and leading to its
subsequent proteasomal degradation. {ECO:0000305|PubMed:11257006}.
-----------------------------------------------------------------------
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EMBL; AF022223; AAC34259.1; -; mRNA.
EMBL; AK009149; BAB26106.1; -; mRNA.
EMBL; AL837521; CAM19843.1; -; Genomic_DNA.
EMBL; CH466538; EDL05422.1; -; Genomic_DNA.
EMBL; BC003722; AAH03722.2; -; mRNA.
EMBL; BC069918; AAH69918.2; -; mRNA.
EMBL; BC093509; AAH93509.2; -; mRNA.
CCDS; CCDS38713.1; -. [Q60739-1]
CCDS; CCDS51139.1; -. [Q60739-2]
RefSeq; NP_001165210.1; NM_001171739.1. [Q60739-2]
RefSeq; NP_033866.4; NM_009736.3.
UniGene; Mm.688; -.
PDB; 1I6Z; NMR; -; A=226-355.
PDB; 2LWP; NMR; -; A=137-233.
PDB; 2M8S; NMR; -; A=137-233.
PDBsum; 1I6Z; -.
PDBsum; 2LWP; -.
PDBsum; 2M8S; -.
ProteinModelPortal; Q60739; -.
SMR; Q60739; -.
BioGrid; 198298; 6.
DIP; DIP-272N; -.
STRING; 10090.ENSMUSP00000030125; -.
iPTMnet; Q60739; -.
PhosphoSitePlus; Q60739; -.
PaxDb; Q60739; -.
PRIDE; Q60739; -.
Ensembl; ENSMUST00000108089; ENSMUSP00000103724; ENSMUSG00000028416. [Q60739-2]
Ensembl; ENSMUST00000191273; ENSMUSP00000139864; ENSMUSG00000028416. [Q60739-2]
GeneID; 12017; -.
KEGG; mmu:12017; -.
CTD; 573; -.
MGI; MGI:108047; Bag1.
eggNOG; ENOG410IHYI; Eukaryota.
eggNOG; ENOG4111SUG; LUCA.
GeneTree; ENSGT00450000040296; -.
HOGENOM; HOG000286009; -.
HOVERGEN; HBG000236; -.
InParanoid; Q60739; -.
KO; K09555; -.
PhylomeDB; Q60739; -.
Reactome; R-MMU-3371453; Regulation of HSF1-mediated heat shock response.
EvolutionaryTrace; Q60739; -.
PRO; PR:Q60739; -.
Proteomes; UP000000589; Chromosome 4.
Bgee; ENSMUSG00000028416; Expressed in 294 organ(s), highest expression level in blood.
CleanEx; MM_BAG1; -.
ExpressionAtlas; Q60739; baseline and differential.
Genevisible; Q60739; MM.
GO; GO:0005737; C:cytoplasm; IDA:MGI.
GO; GO:0005829; C:cytosol; IDA:MGI.
GO; GO:0005739; C:mitochondrion; ISO:MGI.
GO; GO:0005634; C:nucleus; IDA:UniProtKB.
GO; GO:0048471; C:perinuclear region of cytoplasm; ISO:MGI.
GO; GO:0000774; F:adenyl-nucleotide exchange factor activity; ISS:UniProtKB.
GO; GO:0051087; F:chaperone binding; IEA:InterPro.
GO; GO:0051219; F:phosphoprotein binding; IPI:MGI.
GO; GO:0031625; F:ubiquitin protein ligase binding; ISO:MGI.
GO; GO:0006915; P:apoptotic process; IEA:UniProtKB-KW.
GO; GO:0051085; P:chaperone cofactor-dependent protein refolding; ISO:MGI.
GO; GO:0043066; P:negative regulation of apoptotic process; IMP:MGI.
GO; GO:2000672; P:negative regulation of motor neuron apoptotic process; IMP:MGI.
GO; GO:0001933; P:negative regulation of protein phosphorylation; IMP:MGI.
GO; GO:0030182; P:neuron differentiation; IDA:MGI.
GO; GO:0043525; P:positive regulation of neuron apoptotic process; IDA:MGI.
GO; GO:0014040; P:positive regulation of Schwann cell differentiation; ISO:MGI.
GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IDA:MGI.
GO; GO:0070585; P:protein localization to mitochondrion; IMP:MGI.
Gene3D; 1.20.58.120; -; 1.
InterPro; IPR017093; BAG-1.
InterPro; IPR036533; BAG_dom_sf.
InterPro; IPR003103; BAG_domain.
InterPro; IPR029071; Ubiquitin-like_domsf.
InterPro; IPR000626; Ubiquitin_dom.
PANTHER; PTHR12329:SF16; PTHR12329:SF16; 1.
Pfam; PF02179; BAG; 1.
Pfam; PF00240; ubiquitin; 1.
SMART; SM00264; BAG; 1.
SMART; SM00213; UBQ; 1.
SUPFAM; SSF54236; SSF54236; 1.
SUPFAM; SSF63491; SSF63491; 1.
PROSITE; PS51035; BAG; 1.
PROSITE; PS50053; UBIQUITIN_2; 1.
1: Evidence at protein level;
3D-structure; Alternative initiation; Apoptosis; Chaperone;
Complete proteome; Cytoplasm; Nucleus; Reference proteome; Repeat;
Ubl conjugation.
CHAIN 1 355 BAG family molecular chaperone regulator
1.
/FTId=PRO_0000002782.
REPEAT 103 108 1.
REPEAT 111 116 2.
REPEAT 117 122 3.
REPEAT 123 128 4.
REPEAT 129 134 5.
REPEAT 141 146 6.
REPEAT 147 152 7.
DOMAIN 154 234 Ubiquitin-like. {ECO:0000255|PROSITE-
ProRule:PRU00214}.
DOMAIN 256 336 BAG. {ECO:0000255|PROSITE-
ProRule:PRU00369}.
REGION 111 209 7 X 6 AA tandem repeat of E-E-X(4).
REGION 182 229 Interaction with HSPA8. {ECO:0000250}.
REGION 226 355 Interaction with PPP1R15A. {ECO:0000250}.
VAR_SEQ 1 136 Missing (in isoform 2).
{ECO:0000303|PubMed:16141072}.
/FTId=VSP_018667.
CONFLICT 64 64 P -> A (in Ref. 5; AAH93509/AAH69918/
AAH03722). {ECO:0000305}.
STRAND 149 153 {ECO:0000244|PDB:2LWP}.
STRAND 155 160 {ECO:0000244|PDB:2LWP}.
STRAND 163 168 {ECO:0000244|PDB:2LWP}.
STRAND 171 173 {ECO:0000244|PDB:2LWP}.
STRAND 175 177 {ECO:0000244|PDB:2LWP}.
HELIX 180 191 {ECO:0000244|PDB:2LWP}.
HELIX 195 197 {ECO:0000244|PDB:2LWP}.
STRAND 200 202 {ECO:0000244|PDB:2LWP}.
STRAND 205 210 {ECO:0000244|PDB:2M8S}.
TURN 215 218 {ECO:0000244|PDB:2LWP}.
STRAND 220 222 {ECO:0000244|PDB:2LWP}.
STRAND 226 228 {ECO:0000244|PDB:1I6Z}.
HELIX 234 268 {ECO:0000244|PDB:1I6Z}.
STRAND 270 272 {ECO:0000244|PDB:1I6Z}.
HELIX 274 303 {ECO:0000244|PDB:1I6Z}.
HELIX 312 346 {ECO:0000244|PDB:1I6Z}.
SEQUENCE 355 AA; 39740 MW; 077A765CA869D3A7 CRC64;
MAGRSAARRP RGDREPLGPR LRAPRPAREP RQSESRAERG LPPSQRSSVR SAASGHDRST
RGAPAGACKP RVKKKVRPRS SQSEKVGSSS RELTRSKKVT RSKNVTGTQV EEVTKIEEAT
QTEEVTVAEE VTQTDNMAKT EEMVQTEEME TPRLSVIVTH SNERYDLLVT PQQGNSEPVV
QDLAQLVEEA TGVPLPFQKL IFKGKSLKEM ETPLSALGMQ NGCRVMLIGE KSNPEEEVEL
KKLKDLEVSA EKIANHLQEL NKELSGIQQG FLAKELQAEA LCKLDRKVKA TIEQFMKILE
EIDTMVLPEQ FKDSRLKRKN LVKKVQVFLA ECDTVEQYIC QETERLQSTN LALAE


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