BAG1_HUMAN
ID BAG1_HUMAN Reviewed; 345 AA.
AC Q99933; O75315; Q14414; Q53H32; Q5VZE8; Q5VZE9; Q5VZF0; Q96TG2; Q9Y2V4;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 18-MAY-2010, sequence version 4.
DT 03-AUG-2022, entry version 213.
DE RecName: Full=BAG family molecular chaperone regulator 1;
DE Short=BAG-1;
DE AltName: Full=Bcl-2-associated athanogene 1;
GN Name=BAG1; Synonyms=HAP;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC TISSUE=Liver;
RX PubMed=8524784; DOI=10.1073/pnas.92.25.11465;
RA Zeiner M., Gehring U.;
RT "A protein that interacts with members of the nuclear hormone receptor
RT family: identification and cDNA cloning.";
RL Proc. Natl. Acad. Sci. U.S.A. 92:11465-11469(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC TISSUE=Mammary gland;
RX PubMed=8812483; DOI=10.1006/geno.1996.0389;
RA Takayama S., Kochel K., Irie S., Inazawa J., Abe T., Sato T., Druck T.,
RA Huebner K., Reed J.C.;
RT "Cloning of cDNAs encoding the human BAG1 protein and localization of the
RT human BAG1 gene to chromosome 9p12.";
RL Genomics 35:494-498(1996).
RN [3]
RP SEQUENCE REVISION TO N-TERMINUS; 79; 84; 90; 245 AND 293.
RA Takayama S.;
RL Submitted (SEP-1997) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), ANTI-APOPTOTIC ACTIVITY,
RP SUBCELLULAR LOCATION, AND INTERACTION WITH STK19.
RC TISSUE=T-cell;
RX PubMed=15986447; DOI=10.1002/ijc.21259;
RA Wadle A., Mischo A., Henrich P.P., Stenner-Lieven F., Scherer C., Imig J.,
RA Petersen G., Pfreundschuh M., Renner C.;
RT "Characterization of Hap/BAG-1 variants as RP1 binding proteins with
RT antiapoptotic activity.";
RL Int. J. Cancer 117:896-904(2005).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Dermoid cancer;
RA Suzuki Y., Sugano S., Totoki Y., Toyoda A., Takeda T., Sakaki Y.,
RA Tanaka A., Yokoyama S.;
RL Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15164053; DOI=10.1038/nature02465;
RA Humphray S.J., Oliver K., Hunt A.R., Plumb R.W., Loveland J.E., Howe K.L.,
RA Andrews T.D., Searle S., Hunt S.E., Scott C.E., Jones M.C., Ainscough R.,
RA Almeida J.P., Ambrose K.D., Ashwell R.I.S., Babbage A.K., Babbage S.,
RA Bagguley C.L., Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K.,
RA Beasley H., Beasley O., Bird C.P., Bray-Allen S., Brown A.J., Brown J.Y.,
RA Burford D., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C.,
RA Chen Y., Clarke G., Clark S.Y., Clee C.M., Clegg S., Collier R.E.,
RA Corby N., Crosier M., Cummings A.T., Davies J., Dhami P., Dunn M.,
RA Dutta I., Dyer L.W., Earthrowl M.E., Faulkner L., Fleming C.J.,
RA Frankish A., Frankland J.A., French L., Fricker D.G., Garner P.,
RA Garnett J., Ghori J., Gilbert J.G.R., Glison C., Grafham D.V., Gribble S.,
RA Griffiths C., Griffiths-Jones S., Grocock R., Guy J., Hall R.E.,
RA Hammond S., Harley J.L., Harrison E.S.I., Hart E.A., Heath P.D.,
RA Henderson C.D., Hopkins B.L., Howard P.J., Howden P.J., Huckle E.,
RA Johnson C., Johnson D., Joy A.A., Kay M., Keenan S., Kershaw J.K.,
RA Kimberley A.M., King A., Knights A., Laird G.K., Langford C., Lawlor S.,
RA Leongamornlert D.A., Leversha M., Lloyd C., Lloyd D.M., Lovell J.,
RA Martin S., Mashreghi-Mohammadi M., Matthews L., McLaren S., McLay K.E.,
RA McMurray A., Milne S., Nickerson T., Nisbett J., Nordsiek G., Pearce A.V.,
RA Peck A.I., Porter K.M., Pandian R., Pelan S., Phillimore B., Povey S.,
RA Ramsey Y., Rand V., Scharfe M., Sehra H.K., Shownkeen R., Sims S.K.,
RA Skuce C.D., Smith M., Steward C.A., Swarbreck D., Sycamore N., Tester J.,
RA Thorpe A., Tracey A., Tromans A., Thomas D.W., Wall M., Wallis J.M.,
RA West A.P., Whitehead S.L., Willey D.L., Williams S.A., Wilming L.,
RA Wray P.W., Young L., Ashurst J.L., Coulson A., Blocker H., Durbin R.M.,
RA Sulston J.E., Hubbard T., Jackson M.J., Bentley D.R., Beck S., Rogers J.,
RA Dunham I.;
RT "DNA sequence and analysis of human chromosome 9.";
RL Nature 429:369-374(2004).
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Cervix, and Lung;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [9]
RP IDENTIFICATION OF ISOFORMS 1 AND 4, AND ALTERNATIVE INITIATION.
RX PubMed=9396724; DOI=10.1042/bj3280807;
RA Packham G., Brimmell M., Cleveland J.L.;
RT "Mammalian cells express two differently localized Bag-1 isoforms generated
RT by alternative translation initiation.";
RL Biochem. J. 328:807-813(1997).
RN [10]
RP FUNCTION, SUBUNIT, AND INTERACTION WITH BCL2; HSP70 AND HSPA8.
RX PubMed=9305631; DOI=10.1093/emboj/16.16.4887;
RA Takayama S., Bimston D.N., Matsuzawa S.-I., Freeman B.C., Aime-Sempe C.,
RA Xie Z., Morimoto R.I., Reed J.C.;
RT "BAG-1 modulates the chaperone activity of Hsp70/Hsc70.";
RL EMBO J. 16:4887-4896(1997).
RN [11]
RP IDENTIFICATION OF ISOFORMS 1; 3 AND 4, ALTERNATIVE INITIATION, SUBCELLULAR
RP LOCATION, INTERACTION WITH HSPA8, INDUCTION, AND TISSUE SPECIFICITY.
RX PubMed=9679980;
RA Takayama S., Krajewski S., Krajewska M., Kitada S., Zapata J.M., Kochel K.,
RA Knee D., Scudiero D., Tudor G., Miller G.J., Miyashita T., Yamada M.,
RA Reed J.C.;
RT "Expression and location of Hsp70/Hsc-binding anti-apoptotic protein BAG-1
RT and its variants in normal tissues and tumor cell lines.";
RL Cancer Res. 58:3116-3131(1998).
RN [12]
RP INTERACTION WITH SIAH1.
RX PubMed=9582267; DOI=10.1093/emboj/17.10.2736;
RA Matsuzawa S., Takayama S., Froesch B.A., Zapata J.M., Reed J.C.;
RT "p53-inducible human homologue of Drosophila seven in absentia (Siah)
RT inhibits cell growth: suppression by BAG-1.";
RL EMBO J. 17:2736-2747(1998).
RN [13]
RP FUNCTION.
RX PubMed=9873016; DOI=10.1074/jbc.274.2.781;
RA Takayama S., Xie Z., Reed J.C.;
RT "An evolutionarily conserved family of Hsp70/Hsc70 molecular chaperone
RT regulators.";
RL J. Biol. Chem. 274:781-786(1999).
RN [14]
RP INTERACTION WITH NR3C1.
RX PubMed=10477749; DOI=10.1083/jcb.146.5.929;
RA Schneikert J., Huebner S., Martin E., Cato A.B.C.;
RT "A nuclear action of the eukaryotic cochaperone RAP46 in downregulation of
RT glucocorticoid receptor activity.";
RL J. Cell Biol. 146:929-940(1999).
RN [15]
RP INTERACTION WITH PPP1R15A, AND FUNCTION.
RX PubMed=12724406; DOI=10.1128/mcb.23.10.3477-3486.2003;
RA Hung W.J., Roberson R.S., Taft J., Wu D.Y.;
RT "Human BAG-1 proteins bind to the cellular stress response protein GADD34
RT and interfere with GADD34 functions.";
RL Mol. Cell. Biol. 23:3477-3486(2003).
RN [16]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-223, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [17]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-terminal
RT acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN [18]
RP FUNCTION, AND INTERACTION WITH HSPA1A; HSPA1B AND HSPA8.
RX PubMed=24318877; DOI=10.1074/jbc.m113.521997;
RA Rauch J.N., Gestwicki J.E.;
RT "Binding of human nucleotide exchange factors to heat shock protein 70
RT (Hsp70) generates functionally distinct complexes in vitro.";
RL J. Biol. Chem. 289:1402-1414(2014).
RN [19]
RP FUNCTION, INTERACTION WITH HSPA8, AND MUTAGENESIS OF 308-ARG-LYS-309.
RX PubMed=27474739; DOI=10.1074/jbc.m116.742502;
RA Rauch J.N., Zuiderweg E.R., Gestwicki J.E.;
RT "Non-canonical interactions between heat shock cognate protein 70 (Hsc70)
RT and Bcl2-associated anthanogene (BAG) co-chaperones are important for
RT client release.";
RL J. Biol. Chem. 291:19848-19857(2016).
RN [20]
RP X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 222-334 IN COMPLEX WITH HSC70.
RX PubMed=11222862; DOI=10.1126/science.291.5508.1553;
RA Sondermann H., Scheufler C., Schneider C., Hohfeld J., Hartl F.U.,
RA Moarefi I.;
RT "Structure of a Bag/Hsc70 complex: convergent functional evolution of Hsp70
RT nucleotide exchange factors.";
RL Science 291:1553-1557(2001).
RN [21]
RP STRUCTURE BY NMR OF 143-223.
RG RIKEN structural genomics initiative (RSGI);
RT "Solution structure of the ubiquitin domain of Bcl-2 binding athanogene-
RT 1.";
RL Submitted (AUG-2005) 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 (PubMed:27474739, PubMed:9873016,
CC PubMed:24318877). Inhibits the pro-apoptotic function of PPP1R15A, and
CC has anti-apoptotic activity (PubMed:12724406). Markedly increases the
CC anti-cell death function of BCL2 induced by various stimuli
CC (PubMed:9305631). {ECO:0000269|PubMed:12724406,
CC ECO:0000269|PubMed:24318877, ECO:0000269|PubMed:27474739,
CC ECO:0000269|PubMed:9305631, ECO:0000269|PubMed:9873016}.
CC -!- SUBUNIT: Homodimer. Forms a heteromeric complex with HSP70/HSC70
CC (PubMed:9305631). Binds to the ATPase domain of HSP/HSC70 chaperones.
CC Isoform 1, isoform 3 and isoform 4 but not isoform 2 interact with
CC HSPA8/HSC70 (PubMed:27474739, PubMed:24318877, PubMed:9305631,
CC PubMed:9679980). Interacts with NR3C1 (PubMed:10477749). Interacts with
CC the N-terminal region of STK19 (PubMed:15986447). Interacts with
CC PPP1R15A (PubMed:12724406). Interacts with BCL2 in an ATP-dependent
CC manner. Isoform 2 does not interact with BCL2 (PubMed:9305631).
CC Interacts with SIAH1 (PubMed:9582267). Interacts with HSPA8 (via NBD)
CC (PubMed:27474739, PubMed:24318877). Interacts with HSPA1A (via NBD) and
CC HSPA1B (via NBD) (PubMed:24318877). Interacts with SIAH2 (By
CC similarity). {ECO:0000250|UniProtKB:Q60739,
CC ECO:0000269|PubMed:10477749, ECO:0000269|PubMed:11222862,
CC ECO:0000269|PubMed:12724406, ECO:0000269|PubMed:15986447,
CC ECO:0000269|PubMed:24318877, ECO:0000269|PubMed:27474739,
CC ECO:0000269|PubMed:9305631, ECO:0000269|PubMed:9582267,
CC ECO:0000269|PubMed:9679980}.
CC -!- INTERACTION:
CC Q99933; P11142: HSPA8; NbExp=13; IntAct=EBI-1030678, EBI-351896;
CC Q99933; Q96IS6: HSPA8; NbExp=5; IntAct=EBI-1030678, EBI-10289199;
CC Q99933; Q15773: MLF2; NbExp=2; IntAct=EBI-1030678, EBI-1051875;
CC Q99933; Q13200: PSMD2; NbExp=8; IntAct=EBI-1030678, EBI-357648;
CC Q99933; Q9UNE7: STUB1; NbExp=2; IntAct=EBI-1030678, EBI-357085;
CC Q99933; P36406: TRIM23; NbExp=5; IntAct=EBI-1030678, EBI-740098;
CC Q99933; P14373: TRIM27; NbExp=7; IntAct=EBI-1030678, EBI-719493;
CC Q99933; Q53FC7; NbExp=2; IntAct=EBI-1030678, EBI-9356749;
CC Q99933; Q96BE0; NbExp=2; IntAct=EBI-1030678, EBI-9356686;
CC -!- SUBCELLULAR LOCATION: [Isoform 1]: Nucleus. Cytoplasm. Note=Isoform 1
CC localizes predominantly to the nucleus.
CC -!- SUBCELLULAR LOCATION: [Isoform 2]: Cytoplasm. Nucleus. Note=Isoform 2
CC localizes to the cytoplasm and shuttles into the nucleus in response to
CC heat shock.
CC -!- SUBCELLULAR LOCATION: [Isoform 4]: Cytoplasm. Nucleus. Note=Isoform 4
CC localizes predominantly to the cytoplasm. The cellular background in
CC which it is expressed can influence whether it resides primarily in the
CC cytoplasm or is also found in the nucleus. In the presence of BCL2,
CC localizes to intracellular membranes (what appears to be the nuclear
CC envelope and perinuclear membranes) as well as punctate cytosolic
CC structures suggestive of mitochondria.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing, Alternative initiation; Named isoforms=4;
CC Name=1; Synonyms=BAG-1L, p50;
CC IsoId=Q99933-1; Sequence=Displayed;
CC Name=2; Synonyms=BAG1V, HAPV;
CC IsoId=Q99933-2; Sequence=VSP_000453;
CC Name=3; Synonyms=BAG-1M, RAP46;
CC IsoId=Q99933-3; Sequence=VSP_038395;
CC Name=4; Synonyms=BAG-1, p32;
CC IsoId=Q99933-4; Sequence=VSP_038394;
CC -!- TISSUE SPECIFICITY: Isoform 4 is the most abundantly expressed isoform.
CC It is ubiquitously expressed throughout most tissues, except the liver,
CC colon, breast and uterine myometrium. Isoform 1 is expressed in the
CC ovary and testis. Isoform 4 is expressed in several types of tumor cell
CC lines, and at consistently high levels in leukemia and lymphoma cell
CC lines. Isoform 1 is expressed in the prostate, breast and leukemia cell
CC lines. Isoform 3 is the least abundant isoform in tumor cell lines (at
CC protein level). {ECO:0000269|PubMed:9679980}.
CC -!- INDUCTION: Up-regulated during differentiation of bladder epithelial
CC cells and down-regulated during differentiation of prostate epithelium.
CC {ECO:0000269|PubMed:9679980}.
CC -!- PTM: Ubiquitinated; mediated by SIAH1 or SIAH2 and leading to its
CC subsequent proteasomal degradation. {ECO:0000305}.
CC -!- MISCELLANEOUS: [Isoform 2]: Produced by alternative splicing.
CC {ECO:0000305}.
CC -!- MISCELLANEOUS: [Isoform 3]: Produced by alternative initiation at Met-
CC 72 of isoform 1. {ECO:0000305}.
CC -!- MISCELLANEOUS: [Isoform 4]: Produced by alternative initiation at Met-
CC 116 of isoform 1. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAD11467.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=AAD25045.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=BAD96469.1; Type=Miscellaneous discrepancy; Note=Unusual initiator. The initiator methionine is coded by a non-canonical CTG leucine codon.; Evidence={ECO:0000305};
CC Sequence=CAA84624.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=EAW58515.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC -!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology and
CC Haematology;
CC URL="http://atlasgeneticsoncology.org/Genes/BAG1ID742ch9p13.html";
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DR EMBL; Z35491; CAA84624.1; ALT_INIT; mRNA.
DR EMBL; U46917; AAD11467.1; ALT_INIT; mRNA.
DR EMBL; AF022224; AAC34258.1; -; mRNA.
DR EMBL; AF116273; AAD25045.1; ALT_INIT; mRNA.
DR EMBL; AK222749; BAD96469.1; ALT_INIT; mRNA.
DR EMBL; AL161445; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL356472; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471071; EAW58514.1; -; Genomic_DNA.
DR EMBL; CH471071; EAW58515.1; ALT_SEQ; Genomic_DNA.
DR EMBL; BC001936; AAH01936.2; -; mRNA.
DR EMBL; BC014774; AAH14774.2; -; mRNA.
DR CCDS; CCDS35004.1; -. [Q99933-1]
DR CCDS; CCDS55301.1; -. [Q99933-4]
DR RefSeq; NP_001165886.1; NM_001172415.1. [Q99933-4]
DR RefSeq; NP_004314.5; NM_004323.5. [Q99933-1]
DR PDB; 1HX1; X-ray; 1.90 A; B=222-334.
DR PDB; 1WXV; NMR; -; A=144-222.
DR PDB; 3FZF; X-ray; 2.20 A; B=222-334.
DR PDB; 3FZH; X-ray; 2.00 A; B=222-334.
DR PDB; 3FZK; X-ray; 2.10 A; B=222-334.
DR PDB; 3FZL; X-ray; 2.20 A; B=222-334.
DR PDB; 3FZM; X-ray; 2.30 A; B=222-334.
DR PDB; 3LDQ; X-ray; 1.90 A; B=222-334.
DR PDB; 3M3Z; X-ray; 2.10 A; B=222-334.
DR PDB; 5AQF; X-ray; 1.88 A; B/D=222-334.
DR PDB; 5AQG; X-ray; 2.24 A; B/D/F=222-334.
DR PDB; 5AQH; X-ray; 2.00 A; B=222-334.
DR PDB; 5AQI; X-ray; 1.98 A; B/D=222-334.
DR PDB; 5AQJ; X-ray; 1.96 A; B/D/F=222-334.
DR PDB; 5AQK; X-ray; 2.09 A; B=222-334.
DR PDB; 5AQL; X-ray; 1.69 A; B/D=222-334.
DR PDB; 5AQM; X-ray; 1.63 A; B/D=222-334.
DR PDB; 5AQN; X-ray; 2.45 A; B/D/F=222-334.
DR PDB; 5AQO; X-ray; 2.12 A; B/D/F=222-334.
DR PDB; 5AQP; X-ray; 2.08 A; B/D/F=222-334.
DR PDB; 5AQQ; X-ray; 2.72 A; B/D/F=222-334.
DR PDB; 5AQR; X-ray; 1.91 A; B/D/F=222-334.
DR PDB; 5AQS; X-ray; 2.00 A; B/D=222-334.
DR PDB; 5AQT; X-ray; 1.90 A; B=222-334.
DR PDB; 5AQU; X-ray; 1.92 A; B=222-334.
DR PDB; 5AQV; X-ray; 1.75 A; B=222-334.
DR PDBsum; 1HX1; -.
DR PDBsum; 1WXV; -.
DR PDBsum; 3FZF; -.
DR PDBsum; 3FZH; -.
DR PDBsum; 3FZK; -.
DR PDBsum; 3FZL; -.
DR PDBsum; 3FZM; -.
DR PDBsum; 3LDQ; -.
DR PDBsum; 3M3Z; -.
DR PDBsum; 5AQF; -.
DR PDBsum; 5AQG; -.
DR PDBsum; 5AQH; -.
DR PDBsum; 5AQI; -.
DR PDBsum; 5AQJ; -.
DR PDBsum; 5AQK; -.
DR PDBsum; 5AQL; -.
DR PDBsum; 5AQM; -.
DR PDBsum; 5AQN; -.
DR PDBsum; 5AQO; -.
DR PDBsum; 5AQP; -.
DR PDBsum; 5AQQ; -.
DR PDBsum; 5AQR; -.
DR PDBsum; 5AQS; -.
DR PDBsum; 5AQT; -.
DR PDBsum; 5AQU; -.
DR PDBsum; 5AQV; -.
DR AlphaFoldDB; Q99933; -.
DR SMR; Q99933; -.
DR BioGRID; 107049; 166.
DR CORUM; Q99933; -.
DR DIP; DIP-3341N; -.
DR IntAct; Q99933; 57.
DR MINT; Q99933; -.
DR STRING; 9606.ENSP00000420514; -.
DR DrugBank; DB07045; (2R,3R,4S,5R)-2-[6-amino-8-[(3,4-dichlorophenyl)methylamino]purin-9-yl]-5-(hydroxymethyl)oxolane-3,4-diol.
DR GlyGen; Q99933; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q99933; -.
DR PhosphoSitePlus; Q99933; -.
DR BioMuta; BAG1; -.
DR DMDM; 296439462; -.
DR EPD; Q99933; -.
DR jPOST; Q99933; -.
DR MassIVE; Q99933; -.
DR MaxQB; Q99933; -.
DR PaxDb; Q99933; -.
DR PeptideAtlas; Q99933; -.
DR PRIDE; Q99933; -.
DR ProteomicsDB; 78526; -. [Q99933-1]
DR ProteomicsDB; 78527; -. [Q99933-2]
DR ProteomicsDB; 78528; -. [Q99933-3]
DR ProteomicsDB; 78529; -. [Q99933-4]
DR Antibodypedia; 2968; 543 antibodies from 41 providers.
DR DNASU; 573; -.
DR Ensembl; ENST00000379704.7; ENSP00000369026.2; ENSG00000107262.26. [Q99933-4]
DR Ensembl; ENST00000634734.3; ENSP00000489189.2; ENSG00000107262.26. [Q99933-1]
DR GeneID; 573; -.
DR KEGG; hsa:573; -.
DR MANE-Select; ENST00000634734.3; ENSP00000489189.2; NM_004323.6; NP_004314.6.
DR UCSC; uc064sos.1; human. [Q99933-1]
DR CTD; 573; -.
DR DisGeNET; 573; -.
DR GeneCards; BAG1; -.
DR HGNC; HGNC:937; BAG1.
DR HPA; ENSG00000107262; Low tissue specificity.
DR MIM; 601497; gene.
DR neXtProt; NX_Q99933; -.
DR OpenTargets; ENSG00000107262; -.
DR PharmGKB; PA25237; -.
DR VEuPathDB; HostDB:ENSG00000107262; -.
DR eggNOG; ENOG502RN5W; Eukaryota.
DR GeneTree; ENSGT00450000040296; -.
DR HOGENOM; CLU_055378_0_1_1; -.
DR InParanoid; Q99933; -.
DR OMA; VKTVQGF; -.
DR OrthoDB; 1450573at2759; -.
DR PhylomeDB; Q99933; -.
DR PathwayCommons; Q99933; -.
DR Reactome; R-HSA-3371453; Regulation of HSF1-mediated heat shock response.
DR SignaLink; Q99933; -.
DR SIGNOR; Q99933; -.
DR BioGRID-ORCS; 573; 14 hits in 1091 CRISPR screens.
DR ChiTaRS; BAG1; human.
DR EvolutionaryTrace; Q99933; -.
DR GeneWiki; BAG1; -.
DR GenomeRNAi; 573; -.
DR Pharos; Q99933; Tbio.
DR PRO; PR:Q99933; -.
DR Proteomes; UP000005640; Chromosome 9.
DR RNAct; Q99933; protein.
DR Bgee; ENSG00000107262; Expressed in palpebral conjunctiva and 211 other tissues.
DR ExpressionAtlas; Q99933; baseline and differential.
DR Genevisible; Q99933; HS.
DR GO; GO:0005737; C:cytoplasm; TAS:ProtInc.
DR GO; GO:0005829; C:cytosol; IDA:HPA.
DR GO; GO:0016020; C:membrane; IBA:GO_Central.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0000774; F:adenyl-nucleotide exchange factor activity; IDA:UniProtKB.
DR GO; GO:0051087; F:chaperone binding; IBA:GO_Central.
DR GO; GO:0031625; F:ubiquitin protein ligase binding; IPI:ARUK-UCL.
DR GO; GO:0006915; P:apoptotic process; IEA:UniProtKB-KW.
DR GO; GO:0007166; P:cell surface receptor signaling pathway; TAS:ProtInc.
DR GO; GO:0051085; P:chaperone cofactor-dependent protein refolding; IDA:UniProtKB.
DR GO; GO:0043066; P:negative regulation of apoptotic process; TAS:ProtInc.
DR GO; GO:0050821; P:protein stabilization; IBA:GO_Central.
DR Gene3D; 1.20.58.120; -; 1.
DR IDEAL; IID00495; -.
DR InterPro; IPR017093; BAG-1.
DR InterPro; IPR039773; BAG_chaperone_regulator.
DR InterPro; IPR036533; BAG_dom_sf.
DR InterPro; IPR003103; BAG_domain.
DR InterPro; IPR000626; Ubiquitin-like_dom.
DR InterPro; IPR029071; Ubiquitin-like_domsf.
DR PANTHER; PTHR12329; PTHR12329; 1.
DR PANTHER; PTHR12329:SF16; PTHR12329:SF16; 1.
DR Pfam; PF02179; BAG; 1.
DR Pfam; PF00240; ubiquitin; 1.
DR SMART; SM00264; BAG; 1.
DR SMART; SM00213; UBQ; 1.
DR SUPFAM; SSF54236; SSF54236; 1.
DR SUPFAM; SSF63491; SSF63491; 1.
DR PROSITE; PS51035; BAG; 1.
DR PROSITE; PS50053; UBIQUITIN_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative initiation; Alternative splicing; Apoptosis;
KW Chaperone; Cytoplasm; Nucleus; Phosphoprotein; Reference proteome; Repeat;
KW Ubl conjugation.
FT CHAIN 1..345
FT /note="BAG family molecular chaperone regulator 1"
FT /id="PRO_0000088865"
FT REPEAT 96..101
FT /note="1"
FT REPEAT 102..107
FT /note="2"
FT REPEAT 108..113
FT /note="3"
FT REPEAT 114..119
FT /note="4"
FT REPEAT 120..125
FT /note="5"
FT REPEAT 126..131
FT /note="6"
FT REPEAT 132..137
FT /note="7"
FT DOMAIN 144..224
FT /note="Ubiquitin-like"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00214"
FT DOMAIN 246..326
FT /note="BAG"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00369"
FT REGION 1..137
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 96..137
FT /note="7 X 6 AA tandem repeat of E-E-X(4)"
FT REGION 172..219
FT /note="Interaction with HSPA8"
FT REGION 216..345
FT /note="Interaction with PPP1R15A"
FT /evidence="ECO:0000269|PubMed:12724406"
FT COMPBIAS 7..29
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 98..113
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 114..137
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 223
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231"
FT VAR_SEQ 1..115
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000305"
FT /id="VSP_038394"
FT VAR_SEQ 1..71
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000305"
FT /id="VSP_038395"
FT VAR_SEQ 302..345
FT /note="KDSRLKRKGLVKKVQAFLAECDTVEQNICQETERLQSTNFALAE -> PTLT
FT LVLNEK (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15986447"
FT /id="VSP_000453"
FT MUTAGEN 308..309
FT /note="RK->AA: Significant loss of interaction with HSPA8."
FT /evidence="ECO:0000269|PubMed:27474739"
FT CONFLICT 45
FT /note="G -> R (in Ref. 2; AAC34258, 5; BAD96469 and 8;
FT AAH01936/AAH14774)"
FT /evidence="ECO:0000305"
FT CONFLICT 79
FT /note="R -> F (in Ref. 2; AAD11467)"
FT /evidence="ECO:0000305"
FT CONFLICT 84
FT /note="E -> K (in Ref. 2; AAD11467)"
FT /evidence="ECO:0000305"
FT CONFLICT 90
FT /note="E -> K (in Ref. 2; AAD11467)"
FT /evidence="ECO:0000305"
FT CONFLICT 245
FT /note="D -> N (in Ref. 2; AAD11467)"
FT /evidence="ECO:0000305"
FT CONFLICT 293
FT /note="D -> H (in Ref. 2; AAD11467)"
FT /evidence="ECO:0000305"
FT STRAND 144..149
FT /evidence="ECO:0007829|PDB:1WXV"
FT STRAND 151..159
FT /evidence="ECO:0007829|PDB:1WXV"
FT STRAND 163..167
FT /evidence="ECO:0007829|PDB:1WXV"
FT HELIX 170..180
FT /evidence="ECO:0007829|PDB:1WXV"
FT TURN 185..187
FT /evidence="ECO:0007829|PDB:1WXV"
FT STRAND 189..192
FT /evidence="ECO:0007829|PDB:1WXV"
FT STRAND 195..197
FT /evidence="ECO:0007829|PDB:1WXV"
FT STRAND 200..203
FT /evidence="ECO:0007829|PDB:1WXV"
FT HELIX 204..207
FT /evidence="ECO:0007829|PDB:1WXV"
FT STRAND 211..219
FT /evidence="ECO:0007829|PDB:1WXV"
FT HELIX 224..259
FT /evidence="ECO:0007829|PDB:5AQM"
FT STRAND 260..262
FT /evidence="ECO:0007829|PDB:5AQR"
FT HELIX 264..272
FT /evidence="ECO:0007829|PDB:5AQM"
FT HELIX 275..292
FT /evidence="ECO:0007829|PDB:5AQM"
FT HELIX 302..327
FT /evidence="ECO:0007829|PDB:5AQM"
SQ 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
