Did you know ? If you order before Friday 14h we deliver 90PCT of the the time next Tuesday, GENTAUR another in time delivery

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

 BAG1_HUMAN              Reviewed;         345 AA.
Q99933; O75315; Q14414; Q53H32; Q5VZE8; Q5VZE9; Q5VZF0; Q96TG2;
Q9Y2V4;
01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
18-MAY-2010, sequence version 4.
27-SEP-2017, entry version 181.
RecName: Full=BAG family molecular chaperone regulator 1;
Short=BAG-1;
AltName: Full=Bcl-2-associated athanogene 1;
Name=BAG1; Synonyms=HAP;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
TISSUE=Liver;
PubMed=8524784; DOI=10.1073/pnas.92.25.11465;
Zeiner M., Gehring U.;
"A protein that interacts with members of the nuclear hormone receptor
family: identification and cDNA cloning.";
Proc. Natl. Acad. Sci. U.S.A. 92:11465-11469(1995).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
TISSUE=Mammary gland;
PubMed=8812483; DOI=10.1006/geno.1996.0389;
Takayama S., Kochel K., Irie S., Inazawa J., Abe T., Sato T.,
Druck T., Huebner K., Reed J.C.;
"Cloning of cDNAs encoding the human BAG1 protein and localization of
the human BAG1 gene to chromosome 9p12.";
Genomics 35:494-498(1996).
[3]
SEQUENCE REVISION TO N-TERMINUS; 79; 84; 90; 245 AND 293.
Takayama S.;
Submitted (SEP-1997) to the EMBL/GenBank/DDBJ databases.
[4]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), ANTI-APOPTOTIC ACTIVITY,
SUBCELLULAR LOCATION, AND INTERACTION WITH STK19.
TISSUE=T-cell;
PubMed=15986447; DOI=10.1002/ijc.21259;
Wadle A., Mischo A., Henrich P.P., Stenner-Lieven F., Scherer C.,
Imig J., Petersen G., Pfreundschuh M., Renner C.;
"Characterization of Hap/BAG-1 variants as RP1 binding proteins with
antiapoptotic activity.";
Int. J. Cancer 117:896-904(2005).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Dermoid cancer;
Suzuki Y., Sugano S., Totoki Y., Toyoda A., Takeda T., Sakaki Y.,
Tanaka A., Yokoyama S.;
Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases.
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=15164053; DOI=10.1038/nature02465;
Humphray S.J., Oliver K., Hunt A.R., Plumb R.W., Loveland J.E.,
Howe K.L., Andrews T.D., Searle S., Hunt S.E., Scott C.E., Jones M.C.,
Ainscough R., Almeida J.P., Ambrose K.D., Ashwell R.I.S.,
Babbage A.K., Babbage S., Bagguley C.L., Bailey J., Banerjee R.,
Barker D.J., Barlow K.F., Bates K., Beasley H., Beasley O., Bird C.P.,
Bray-Allen S., Brown A.J., Brown J.Y., Burford D., Burrill W.,
Burton J., Carder C., Carter N.P., Chapman J.C., Chen Y., Clarke G.,
Clark S.Y., Clee C.M., Clegg S., Collier R.E., Corby N., Crosier M.,
Cummings A.T., Davies J., Dhami P., Dunn M., Dutta I., Dyer L.W.,
Earthrowl M.E., Faulkner L., Fleming C.J., Frankish A.,
Frankland J.A., French L., Fricker D.G., Garner P., Garnett J.,
Ghori J., Gilbert J.G.R., Glison C., Grafham D.V., Gribble S.,
Griffiths C., Griffiths-Jones S., Grocock R., Guy J., Hall R.E.,
Hammond S., Harley J.L., Harrison E.S.I., Hart E.A., Heath P.D.,
Henderson C.D., Hopkins B.L., Howard P.J., Howden P.J., Huckle E.,
Johnson C., Johnson D., Joy A.A., Kay M., Keenan S., Kershaw J.K.,
Kimberley A.M., King A., Knights A., Laird G.K., Langford C.,
Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C., Lloyd D.M.,
Lovell J., Martin S., Mashreghi-Mohammadi M., Matthews L., McLaren S.,
McLay K.E., McMurray A., Milne S., Nickerson T., Nisbett J.,
Nordsiek G., Pearce A.V., Peck A.I., Porter K.M., Pandian R.,
Pelan S., Phillimore B., Povey S., Ramsey Y., Rand V., Scharfe M.,
Sehra H.K., Shownkeen R., Sims S.K., Skuce C.D., Smith M.,
Steward C.A., Swarbreck D., Sycamore N., Tester J., Thorpe A.,
Tracey A., Tromans A., Thomas D.W., Wall M., Wallis J.M., West A.P.,
Whitehead S.L., Willey D.L., Williams S.A., Wilming L., Wray P.W.,
Young L., Ashurst J.L., Coulson A., Blocker H., Durbin R.M.,
Sulston J.E., Hubbard T., Jackson M.J., Bentley D.R., Beck S.,
Rogers J., Dunham I.;
"DNA sequence and analysis of human chromosome 9.";
Nature 429:369-374(2004).
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
[8]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Cervix, and Lung;
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).
[9]
IDENTIFICATION OF ISOFORMS 1 AND 4, AND ALTERNATIVE INITIATION.
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).
[10]
FUNCTION, SUBUNIT, AND INTERACTION WITH BCL2; HSP70 AND HSPA8.
PubMed=9305631; DOI=10.1093/emboj/16.16.4887;
Takayama S., Bimston D.N., Matsuzawa S.-I., Freeman B.C.,
Aime-Sempe C., Xie Z., Morimoto R.I., Reed J.C.;
"BAG-1 modulates the chaperone activity of Hsp70/Hsc70.";
EMBO J. 16:4887-4896(1997).
[11]
IDENTIFICATION OF ISOFORMS 1; 3 AND 4, ALTERNATIVE INITIATION,
SUBCELLULAR LOCATION, INTERACTION WITH HSPA8, INDUCTION, 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).
[12]
INTERACTION WITH SIAH1.
PubMed=9582267; DOI=10.1093/emboj/17.10.2736;
Matsuzawa S., Takayama S., Froesch B.A., Zapata J.M., Reed J.C.;
"p53-inducible human homologue of Drosophila seven in absentia (Siah)
inhibits cell growth: suppression by BAG-1.";
EMBO J. 17:2736-2747(1998).
[13]
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).
[14]
INTERACTION WITH NR3C1.
PubMed=10477749; DOI=10.1083/jcb.146.5.929;
Schneikert J., Huebner S., Martin E., Cato A.B.C.;
"A nuclear action of the eukaryotic cochaperone RAP46 in
downregulation of glucocorticoid receptor activity.";
J. Cell Biol. 146:929-940(1999).
[15]
INTERACTION WITH PPP1R15A, AND FUNCTION.
PubMed=12724406; DOI=10.1128/MCB.23.10.3477-3486.2003;
Hung W.J., Roberson R.S., Taft J., Wu D.Y.;
"Human BAG-1 proteins bind to the cellular stress response protein
GADD34 and interfere with GADD34 functions.";
Mol. Cell. Biol. 23:3477-3486(2003).
[16]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-223, 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).
[17]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=22814378; DOI=10.1073/pnas.1210303109;
Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E.,
Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K.,
Aldabe R.;
"N-terminal acetylome analyses and functional insights of the N-
terminal acetyltransferase NatB.";
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
[18]
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).
[19]
FUNCTION, INTERACTION WITH HSPA8, AND MUTAGENESIS OF 308-ARG-LYS-309.
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).
[20]
X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 222-334 IN COMPLEX WITH
HSC70.
PubMed=11222862; DOI=10.1126/science.1057268;
Sondermann H., Scheufler C., Schneider C., Hohfeld J., Hartl F.U.,
Moarefi I.;
"Structure of a Bag/Hsc70 complex: convergent functional evolution of
Hsp70 nucleotide exchange factors.";
Science 291:1553-1557(2001).
[21]
STRUCTURE BY NMR OF 143-223.
RIKEN structural genomics initiative (RSGI);
"Solution structure of the ubiquitin domain of Bcl-2 binding
athanogene-1.";
Submitted (AUG-2005) 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
(PubMed:27474739, PubMed:9873016, PubMed:24318877). Inhibits the
pro-apoptotic function of PPP1R15A, and has anti-apoptotic
activity (PubMed:12724406). Markedly increases the anti-cell death
function of BCL2 induced by various stimuli (PubMed:9305631).
{ECO:0000269|PubMed:12724406, ECO:0000269|PubMed:24318877,
ECO:0000269|PubMed:27474739, ECO:0000269|PubMed:9305631,
ECO:0000269|PubMed:9873016}.
-!- SUBUNIT: Homodimer. Forms a heteromeric complex with HSP70/HSC70
(PubMed:9305631). Binds to the ATPase domain of HSP/HSC70
chaperones. Isoform 1, isoform 3 and isoform 4 but not isoform 2
interact with HSPA8/HSC70 (PubMed:27474739, PubMed:24318877,
PubMed:9305631, PubMed:9679980). Interacts with NR3C1
(PubMed:10477749). Interacts with the N-terminal region of STK19
(PubMed:15986447). Interacts with PPP1R15A (PubMed:12724406).
Interacts with BCL2 in an ATP-dependent manner. Isoform 2 does not
interact with BCL2 (PubMed:9305631). Interacts with SIAH1
(PubMed:9582267). Interacts with HSPA8 (via NBD) (PubMed:27474739,
PubMed:24318877). Interacts with HSPA1A (via NBD) and HSPA1B (via
NBD) (PubMed:24318877). Interacts with SIAH2 (By similarity).
{ECO:0000250|UniProtKB:Q60739, ECO:0000269|PubMed:10477749,
ECO:0000269|PubMed:11222862, ECO:0000269|PubMed:12724406,
ECO:0000269|PubMed:15986447, ECO:0000269|PubMed:24318877,
ECO:0000269|PubMed:27474739, ECO:0000269|PubMed:9305631,
ECO:0000269|PubMed:9582267, ECO:0000269|PubMed:9679980}.
-!- INTERACTION:
Q53FC7:-; NbExp=2; IntAct=EBI-1030678, EBI-9356749;
Q96BE0:-; NbExp=2; IntAct=EBI-1030678, EBI-9356686;
P08107:HSPA1B; NbExp=3; IntAct=EBI-1030678, EBI-629985;
P11142:HSPA8; NbExp=10; IntAct=EBI-1030678, EBI-351896;
Q96IS6:HSPA8; NbExp=5; IntAct=EBI-1030678, EBI-10289199;
Q13200:PSMD2; NbExp=7; IntAct=EBI-1030678, EBI-357648;
P04049:RAF1; NbExp=2; IntAct=EBI-1030678, EBI-365996;
P50502:ST13; NbExp=2; IntAct=EBI-1030678, EBI-357285;
Q9UNE7:STUB1; NbExp=2; IntAct=EBI-1030678, EBI-357085;
P36406:TRIM23; NbExp=5; IntAct=EBI-1030678, EBI-740098;
P14373:TRIM27; NbExp=3; IntAct=EBI-1030678, EBI-719493;
-!- SUBCELLULAR LOCATION: Isoform 1: Nucleus. Cytoplasm. Note=Isoform
1 localizes predominantly to the nucleus.
-!- SUBCELLULAR LOCATION: Isoform 2: Cytoplasm. Nucleus. Note=Isoform
2 localizes to the cytoplasm and shuttles into the nucleus in
response to heat shock.
-!- SUBCELLULAR LOCATION: Isoform 4: Cytoplasm. Nucleus. Note=Isoform
4 localizes predominantly to the cytoplasm. The cellular
background in which it is expressed can influence whether it
resides primarily in the cytoplasm or is also found in the
nucleus. In the presence of BCL2, localizes to intracellular
membranes (what appears to be the nuclear envelope and perinuclear
membranes) as well as punctate cytosolic structures suggestive of
mitochondria.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing, Alternative initiation; Named isoforms=4;
Name=1; Synonyms=BAG-1L, p50;
IsoId=Q99933-1; Sequence=Displayed;
Name=2; Synonyms=BAG1V, HAPV;
IsoId=Q99933-2; Sequence=VSP_000453;
Note=Produced by alternative splicing.;
Name=3; Synonyms=BAG-1M, RAP46;
IsoId=Q99933-3; Sequence=VSP_038395;
Note=Produced by alternative initiation at Met-72 of isoform 1.;
Name=4; Synonyms=BAG-1, p32;
IsoId=Q99933-4; Sequence=VSP_038394;
Note=Produced by alternative initiation at Met-116 of isoform
1.;
-!- TISSUE SPECIFICITY: Isoform 4 is the most abundantly expressed
isoform. It is ubiquitously expressed throughout most tissues,
except the liver, colon, breast and uterine myometrium. Isoform 1
is expressed in the ovary and testis. Isoform 4 is expressed in
several types of tumor cell lines, and at consistently high levels
in leukemia and lymphoma cell lines. Isoform 1 is expressed in the
prostate, breast and leukemia cell lines. Isoform 3 is the least
abundant isoform in tumor cell lines (at protein level).
{ECO:0000269|PubMed:9679980}.
-!- INDUCTION: Up-regulated during differentiation of bladder
epithelial cells and down-regulated during differentiation of
prostate epithelium. {ECO:0000269|PubMed:9679980}.
-!- PTM: Ubiquitinated; mediated by SIAH1 or SIAH2 and leading to its
subsequent proteasomal degradation. {ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=AAD11467.1; Type=Erroneous initiation; Note=Translation N-terminally extended.; Evidence={ECO:0000305};
Sequence=AAD25045.1; Type=Erroneous initiation; Note=Translation N-terminally extended.; Evidence={ECO:0000305};
Sequence=BAD96469.1; Type=Miscellaneous discrepancy; Note=Unusual initiator. The initiator methionine is coded by a non-canonical CTG leucine codon.; Evidence={ECO:0000305};
Sequence=CAA84624.1; Type=Erroneous initiation; Note=Translation N-terminally extended.; Evidence={ECO:0000305};
Sequence=CAH72516.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
Sequence=CAH72518.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
Sequence=CAH72741.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
Sequence=CAH72742.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
Sequence=EAW58515.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
-!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology
and Haematology;
URL="http://atlasgeneticsoncology.org/Genes/BAG1ID742ch9p13.html";
-----------------------------------------------------------------------
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
Distributed under the Creative Commons Attribution-NoDerivs License
-----------------------------------------------------------------------
EMBL; Z35491; CAA84624.1; ALT_INIT; mRNA.
EMBL; U46917; AAD11467.1; ALT_INIT; mRNA.
EMBL; AF022224; AAC34258.1; -; mRNA.
EMBL; AF116273; AAD25045.1; ALT_INIT; mRNA.
EMBL; AK222749; BAD96469.1; ALT_INIT; mRNA.
EMBL; AL161445; CAH72516.1; ALT_SEQ; Genomic_DNA.
EMBL; AL356472; CAH72516.1; JOINED; Genomic_DNA.
EMBL; AL161445; CAH72517.1; -; Genomic_DNA.
EMBL; AL356472; CAH72517.1; JOINED; Genomic_DNA.
EMBL; AL161445; CAH72518.1; ALT_SEQ; Genomic_DNA.
EMBL; AL356472; CAH72518.1; JOINED; Genomic_DNA.
EMBL; AL356472; CAH72741.1; ALT_SEQ; Genomic_DNA.
EMBL; AL161445; CAH72741.1; JOINED; Genomic_DNA.
EMBL; AL356472; CAH72742.1; ALT_SEQ; Genomic_DNA.
EMBL; AL161445; CAH72742.1; JOINED; Genomic_DNA.
EMBL; AL356472; CAH72743.1; -; Genomic_DNA.
EMBL; AL161445; CAH72743.1; JOINED; Genomic_DNA.
EMBL; CH471071; EAW58514.1; -; Genomic_DNA.
EMBL; CH471071; EAW58515.1; ALT_SEQ; Genomic_DNA.
EMBL; BC001936; AAH01936.2; -; mRNA.
EMBL; BC014774; AAH14774.2; -; mRNA.
CCDS; CCDS35004.1; -. [Q99933-1]
CCDS; CCDS55301.1; -. [Q99933-4]
RefSeq; NP_001165886.1; NM_001172415.1. [Q99933-4]
RefSeq; NP_004314.5; NM_004323.5.
UniGene; Hs.377484; -.
PDB; 1HX1; X-ray; 1.90 A; B=222-334.
PDB; 1WXV; NMR; -; A=144-222.
PDB; 3FZF; X-ray; 2.20 A; B=222-334.
PDB; 3FZH; X-ray; 2.00 A; B=222-334.
PDB; 3FZK; X-ray; 2.10 A; B=222-334.
PDB; 3FZL; X-ray; 2.20 A; B=222-334.
PDB; 3FZM; X-ray; 2.30 A; B=222-334.
PDB; 3LDQ; X-ray; 1.90 A; B=222-334.
PDB; 3M3Z; X-ray; 2.10 A; B=222-334.
PDB; 5AQF; X-ray; 1.88 A; B/D=222-334.
PDB; 5AQG; X-ray; 2.24 A; B/D/F=222-334.
PDB; 5AQH; X-ray; 2.00 A; B=222-334.
PDB; 5AQI; X-ray; 1.98 A; B/D=222-334.
PDB; 5AQJ; X-ray; 1.96 A; B/D/F=222-334.
PDB; 5AQK; X-ray; 2.09 A; B=222-334.
PDB; 5AQL; X-ray; 1.69 A; B/D=222-334.
PDB; 5AQM; X-ray; 1.63 A; B/D=222-334.
PDB; 5AQN; X-ray; 2.45 A; B/D/F=222-334.
PDB; 5AQO; X-ray; 2.12 A; B/D/F=222-334.
PDB; 5AQP; X-ray; 2.08 A; B/D/F=222-334.
PDB; 5AQQ; X-ray; 2.72 A; B/D/F=222-334.
PDB; 5AQR; X-ray; 1.91 A; B/D/F=222-334.
PDB; 5AQS; X-ray; 2.00 A; B/D=222-334.
PDB; 5AQT; X-ray; 1.90 A; B=222-334.
PDB; 5AQU; X-ray; 1.92 A; B=222-334.
PDB; 5AQV; X-ray; 1.75 A; B=222-334.
PDBsum; 1HX1; -.
PDBsum; 1WXV; -.
PDBsum; 3FZF; -.
PDBsum; 3FZH; -.
PDBsum; 3FZK; -.
PDBsum; 3FZL; -.
PDBsum; 3FZM; -.
PDBsum; 3LDQ; -.
PDBsum; 3M3Z; -.
PDBsum; 5AQF; -.
PDBsum; 5AQG; -.
PDBsum; 5AQH; -.
PDBsum; 5AQI; -.
PDBsum; 5AQJ; -.
PDBsum; 5AQK; -.
PDBsum; 5AQL; -.
PDBsum; 5AQM; -.
PDBsum; 5AQN; -.
PDBsum; 5AQO; -.
PDBsum; 5AQP; -.
PDBsum; 5AQQ; -.
PDBsum; 5AQR; -.
PDBsum; 5AQS; -.
PDBsum; 5AQT; -.
PDBsum; 5AQU; -.
PDBsum; 5AQV; -.
ProteinModelPortal; Q99933; -.
SMR; Q99933; -.
BioGrid; 107049; 143.
CORUM; Q99933; -.
DIP; DIP-3341N; -.
IntAct; Q99933; 41.
MINT; MINT-189058; -.
STRING; 9606.ENSP00000420514; -.
iPTMnet; Q99933; -.
PhosphoSitePlus; Q99933; -.
BioMuta; BAG1; -.
DMDM; 296439462; -.
EPD; Q99933; -.
MaxQB; Q99933; -.
PaxDb; Q99933; -.
PeptideAtlas; Q99933; -.
PRIDE; Q99933; -.
DNASU; 573; -.
Ensembl; ENST00000379704; ENSP00000369026; ENSG00000107262. [Q99933-4]
GeneID; 573; -.
KEGG; hsa:573; -.
UCSC; uc064sos.1; human. [Q99933-1]
CTD; 573; -.
DisGeNET; 573; -.
EuPathDB; HostDB:ENSG00000107262.17; -.
GeneCards; BAG1; -.
HGNC; HGNC:937; BAG1.
HPA; CAB002486; -.
HPA; HPA018121; -.
MIM; 601497; gene.
neXtProt; NX_Q99933; -.
OpenTargets; ENSG00000107262; -.
PharmGKB; PA25237; -.
eggNOG; ENOG410IHYI; Eukaryota.
eggNOG; ENOG4111SUG; LUCA.
GeneTree; ENSGT00450000040296; -.
HOVERGEN; HBG000236; -.
InParanoid; Q99933; -.
KO; K09555; -.
PhylomeDB; Q99933; -.
Reactome; R-HSA-3371453; Regulation of HSF1-mediated heat shock response.
ChiTaRS; BAG1; human.
EvolutionaryTrace; Q99933; -.
GeneWiki; BAG1; -.
GenomeRNAi; 573; -.
PRO; PR:Q99933; -.
Proteomes; UP000005640; Chromosome 9.
Bgee; ENSG00000107262; -.
CleanEx; HS_BAG1; -.
ExpressionAtlas; Q99933; baseline and differential.
Genevisible; Q99933; HS.
GO; GO:0005737; C:cytoplasm; TAS:ProtInc.
GO; GO:0005829; C:cytosol; TAS:Reactome.
GO; GO:0005634; C:nucleus; IDA:UniProtKB.
GO; GO:0000774; F:adenyl-nucleotide exchange factor activity; IDA:UniProtKB.
GO; GO:0051087; F:chaperone binding; IEA:InterPro.
GO; GO:0005057; F:signal transducer activity, downstream of receptor; TAS:ProtInc.
GO; GO:0006915; P:apoptotic process; IEA:UniProtKB-KW.
GO; GO:0007166; P:cell surface receptor signaling pathway; TAS:ProtInc.
GO; GO:0070389; P:chaperone cofactor-dependent protein refolding; IDA:UniProtKB.
GO; GO:0043066; P:negative regulation of apoptotic process; TAS:ProtInc.
GO; GO:1900034; P:regulation of cellular response to heat; TAS:Reactome.
Gene3D; 1.20.58.120; -; 1.
InterPro; IPR003103; BAG_domain.
InterPro; IPR029071; Ubiquitin-rel_dom.
InterPro; IPR000626; Ubiquitin_dom.
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; Alternative splicing; Apoptosis;
Chaperone; Complete proteome; Cytoplasm; Nucleus; Phosphoprotein;
Reference proteome; Repeat; Ubl conjugation.
CHAIN 1 345 BAG family molecular chaperone regulator
1.
/FTId=PRO_0000088865.
REPEAT 96 101 1.
REPEAT 102 107 2.
REPEAT 108 113 3.
REPEAT 114 119 4.
REPEAT 120 125 5.
REPEAT 126 131 6.
REPEAT 132 137 7.
DOMAIN 144 224 Ubiquitin-like. {ECO:0000255|PROSITE-
ProRule:PRU00214}.
DOMAIN 246 326 BAG. {ECO:0000255|PROSITE-
ProRule:PRU00369}.
REGION 96 137 7 X 6 AA tandem repeat of E-E-X(4).
REGION 172 219 Interaction with HSPA8.
REGION 216 345 Interaction with PPP1R15A.
{ECO:0000269|PubMed:12724406}.
COMPBIAS 4 82 Arg-rich.
MOD_RES 223 223 Phosphoserine.
{ECO:0000244|PubMed:20068231}.
VAR_SEQ 1 115 Missing (in isoform 4). {ECO:0000305}.
/FTId=VSP_038394.
VAR_SEQ 1 71 Missing (in isoform 3). {ECO:0000305}.
/FTId=VSP_038395.
VAR_SEQ 302 345 KDSRLKRKGLVKKVQAFLAECDTVEQNICQETERLQSTNFA
LAE -> PTLTLVLNEK (in isoform 2).
{ECO:0000303|PubMed:15986447}.
/FTId=VSP_000453.
MUTAGEN 308 309 RK->AA: Significant loss of interaction
with HSPA8.
{ECO:0000269|PubMed:27474739}.
CONFLICT 45 45 G -> R (in Ref. 2; AAC34258, 5; BAD96469
and 8; AAH01936/AAH14774). {ECO:0000305}.
CONFLICT 79 79 R -> F (in Ref. 2; AAD11467).
{ECO:0000305}.
CONFLICT 84 84 E -> K (in Ref. 2; AAD11467).
{ECO:0000305}.
CONFLICT 90 90 E -> K (in Ref. 2; AAD11467).
{ECO:0000305}.
CONFLICT 245 245 D -> N (in Ref. 2; AAD11467).
{ECO:0000305}.
CONFLICT 293 293 D -> H (in Ref. 2; AAD11467).
{ECO:0000305}.
STRAND 144 149 {ECO:0000244|PDB:1WXV}.
STRAND 151 159 {ECO:0000244|PDB:1WXV}.
STRAND 163 167 {ECO:0000244|PDB:1WXV}.
HELIX 170 180 {ECO:0000244|PDB:1WXV}.
TURN 185 187 {ECO:0000244|PDB:1WXV}.
STRAND 189 192 {ECO:0000244|PDB:1WXV}.
STRAND 195 197 {ECO:0000244|PDB:1WXV}.
STRAND 200 203 {ECO:0000244|PDB:1WXV}.
HELIX 204 207 {ECO:0000244|PDB:1WXV}.
STRAND 211 219 {ECO:0000244|PDB:1WXV}.
HELIX 224 259 {ECO:0000244|PDB:5AQM}.
STRAND 260 262 {ECO:0000244|PDB:5AQR}.
HELIX 264 272 {ECO:0000244|PDB:5AQM}.
HELIX 275 292 {ECO:0000244|PDB:5AQM}.
HELIX 302 327 {ECO:0000244|PDB:5AQM}.
SEQUENCE 345 AA; 38779 MW; 8B40EF078C66335F CRC64;
MAQRGGARRP RGDRERLGSR LRALRPGREP RQSEPPAQRG PPPSGRPPAR STASGHDRPT
RGAAAGARRP RMKKKTRRRS TRSEELTRSE ELTLSEEATW SEEATQSEEA TQGEEMNRSQ
EVTRDEESTR SEEVTREEMA AAGLTVTVTH SNEKHDLHVT SQQGSSEPVV QDLAQVVEEV
IGVPQSFQKL IFKGKSLKEM ETPLSALGIQ DGCRVMLIGK KNSPQEEVEL KKLKHLEKSV
EKIADQLEEL NKELTGIQQG FLPKDLQAEA LCKLDRRVKA TIEQFMKILE EIDTLILPEN
FKDSRLKRKG LVKKVQAFLA ECDTVEQNIC QETERLQSTN FALAE


Related products :

Catalog number Product name Quantity
18-003-43726 BAG family molecular chaperone regulator 2 - Bcl-2-associated athanogene 2; BAG-2 Polyclonal 0.1 mg Protein A
18-661-15066 BAG family molecular chaperone regulator 4 - BCL2-associated athanogene 4; BAG-4; Silencer of death domains Polyclonal 0.1 mg
CE40 BAG Family Molecular Chaperone Regulator 2 BAG2 500
CE40 BAG Family Molecular Chaperone Regulator 2 BAG2 lmg
CE40 Human BAG Family Molecular Chaperone Regulator 2 BAG2 l0
E14188c Bovine ELISA Kit FOR BAG family molecular chaperone regulator 5 96T
BAG3_HUMAN Human ELISA Kit FOR BAG family molecular chaperone regulator 3 96T
C103 Human BAG Family Molecular Chaperone Regulator 2 BAG2 50
CSB-EL002533RA Rat BAG family molecular chaperone regulator 5(BAG5) ELISA kit 96T
CSB-EL002529RA Rat BAG family molecular chaperone regulator 1(BAG1) ELISA kit 96T
abx109564 Polyclonal Rabbit BAG family molecular chaperone regulator 5 Antibody 100 μg
CSB-EL002529RA Rat BAG family molecular chaperone regulator 1(BAG1) ELISA kit SpeciesRat 96T
CSB-EL002533CH Chicken BAG family molecular chaperone regulator 5(BAG5) ELISA kit 96T
abx108010 Polyclonal Rabbit BAG family molecular chaperone regulator 5 Antibody (HRP) 100 μg
abx109563 Polyclonal Rabbit BAG family molecular chaperone regulator 3 Antibody 100 μg
CE40 Recombinant Human BAG family molecular chaperone regulator 2_BAG2 1mg
CSB-EL002533RA Rat BAG family molecular chaperone regulator 5(BAG5) ELISA kit SpeciesRat 96T
CSB-EL002533MO Mouse BAG family molecular chaperone regulator 5(BAG5) ELISA kit 96T
abx108009 Polyclonal Rabbit BAG family molecular chaperone regulator 3 Antibody (HRP) 100 μg
CSB-EL002530MO Mouse BAG family molecular chaperone regulator 2(BAG2) ELISA kit 96T
CSB-EL002529MO Mouse BAG family molecular chaperone regulator 1(BAG1) ELISA kit 96T
CSB-EL002531MO Mouse BAG family molecular chaperone regulator 3(BAG3) ELISA kit 96T
CE40 Recombinant Human BAG family molecular chaperone regulator 2_BAG2 50ug
CSB-EL002532MO Mouse BAG family molecular chaperone regulator 4(BAG4) ELISA kit 96T
CSB-EL002533BO Bovine BAG family molecular chaperone regulator 5(BAG5) ELISA kit 96T


 

GENTAUR Belgium BVBA BE0473327336
Voortstraat 49, 1910 Kampenhout BELGIUM
Tel 0032 16 58 90 45

Fax 0032 16 50 90 45
info@gentaur.com | Gentaur





GENTAUR Ltd.
Howard Frank Turnberry House
1404-1410 High Road
Whetstone London N20 9BH
Tel 020 3393 8531 Fax 020 8445 9411
uk@gentaur.com | Gentaur

 

 




GENTAUR France SARL
9, rue Lagrange, 75005 Paris
Tel 01 43 25 01 50

Fax 01 43 25 01 60
RCS Paris B 484 237 888

SIRET 48423788800017

BNP PARIBAS PARIS PL MAUBERT BIC BNPAFRPPPRG

france@gentaur.com | Gentaur

GENTAUR GmbH
Marienbongard 20
52062 Aachen Deutschland
Support Karolina Elandt
Tel: 0035929830070
Fax: (+49) 241 56 00 47 88

Logistic :0241 40 08 90 86
Bankleitzahl 39050000
IBAN lautet DE8839050000107569353
Handelsregister Aachen HR B 16058
Umsatzsteuer-Identifikationsnummer *** DE 815175831
Steuernummer 201/5961/3925
de@gentaur.com | Gentaur

GENTAUR U.S.A
Genprice Inc, Logistics
547, Yurok Circle
San Jose, CA 95123
CA 95123
Tel (408) 780-0908,
Fax (408) 780-0908,
sales@genprice.com

Genprice Inc, Invoices and accounting
6017 Snell Ave, Ste 357
San Jose, CA 95123




GENTAUR Nederland BV
NL850396268B01 KVK nummer 52327027
Kuiper 1
5521 DG Eersel Nederland
Tel:  0208-080893  Fax: 0497-517897
nl@gentaur.com | Gentaur
IBAN: NL04 RABO 0156 9854 62   SWIFT RABONL2U






GENTAUR Spain
tel:0911876558
spain@gentaur.com | Gentaur






ГЕНТАУЪР БЪЛГАРИЯ
ID # 201 358 931 /BULSTAT
София 1000, ул. "Граф Игнатиев" 53 вх. В, ет. 2
Tel 0035924682280 Fax 0035924808322
e-mail: Sofia@gentaur.com | Gentaur
IBAN: BG11FINV91501014771636
BIC: FINVBGSF

GENTAUR Poland Sp. z o.o.


ul. Grunwaldzka 88/A m.2
81-771 Sopot, Poland
TEL Gdansk 058 710 33 44 FAX  058 710 33 48              

poland@gentaur.com | Gentaur

Other countries

Österreich +43720880899

Canada Montreal +15149077481

Ceská republika Praha +420246019719

Danmark +4569918806

Finland Helsset +358942419041

Magyarország Budapest +3619980547

Ireland Dublin+35316526556

Luxembourg+35220880274

Norge Oslo+4721031366

Sverige Stockholm+46852503438

Schweiz Züri+41435006251

US New York+17185132983

GENTAUR Italy
SRL IVA IT03841300167
Piazza Giacomo Matteotti, 6
24122 Bergamo Tel 02 36 00 65 93
Fax 02 36 00 65 94
italia@gentaur.com | Gentaur