Full text data of BAG2
BAG2
[Confidence: medium (present in either hRBCD or BSc_CH or PM22954596)]
BAG family molecular chaperone regulator 2; BAG-2 (Bcl-2-associated athanogene 2)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
BAG family molecular chaperone regulator 2; BAG-2 (Bcl-2-associated athanogene 2)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
hRBCD
IPI00000643
IPI00000643 BAG-family molecular chaperone regulator-2 BAG-family molecular chaperone regulator-2 membrane n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a 1 n/a n/a cytoplamic n/a found at its expected molecular weight found at molecular weight
IPI00000643 BAG-family molecular chaperone regulator-2 BAG-family molecular chaperone regulator-2 membrane n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a 1 n/a n/a cytoplamic n/a found at its expected molecular weight found at molecular weight
UniProt
O95816
ID BAG2_HUMAN Reviewed; 211 AA.
AC O95816; Q08AS9; Q6FID0;
DT 11-JAN-2001, integrated into UniProtKB/Swiss-Prot.
read moreDT 01-MAY-1999, sequence version 1.
DT 22-JAN-2014, entry version 117.
DE RecName: Full=BAG family molecular chaperone regulator 2;
DE Short=BAG-2;
DE AltName: Full=Bcl-2-associated athanogene 2;
GN Name=BAG2;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Uterus;
RX PubMed=11230166; DOI=10.1101/gr.GR1547R;
RA Wiemann S., Weil B., Wellenreuther R., Gassenhuber J., Glassl S.,
RA Ansorge W., Boecher M., Bloecker H., Bauersachs S., Blum H.,
RA Lauber J., Duesterhoeft A., Beyer A., Koehrer K., Strack N.,
RA Mewes H.-W., Ottenwaelder B., Obermaier B., Tampe J., Heubner D.,
RA Wambutt R., Korn B., Klein M., Poustka A.;
RT "Towards a catalog of human genes and proteins: sequencing and
RT analysis of 500 novel complete protein coding human cDNAs.";
RL Genome Res. 11:422-435(2001).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.;
RT "Cloning of human full open reading frames in Gateway(TM) system entry
RT vector (pDONR201).";
RL Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=14574404; DOI=10.1038/nature02055;
RA Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L.,
RA Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E.,
RA Gilbert J.G.R., Clamp M.E., Bethel G., Milne S., Ainscough R.,
RA Almeida J.P., Ambrose K.D., Andrews T.D., Ashwell R.I.S.,
RA Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Barker D.J.,
RA Barlow K.F., Bates K., Beare D.M., Beasley H., Beasley O., Bird C.P.,
RA Blakey S.E., Bray-Allen S., Brook J., Brown A.J., Brown J.Y.,
RA Burford D.C., Burrill W., Burton J., Carder C., Carter N.P.,
RA Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V.,
RA Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J.,
RA Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E.,
RA Ellington A.E., Evans K.A., Faulkner L., Francis M.D., Frankish A.,
RA Frankland J., French L., Garner P., Garnett J., Ghori M.J.,
RA Gilby L.M., Gillson C.J., Glithero R.J., Grafham D.V., Grant M.,
RA Gribble S., Griffiths C., Griffiths M.N.D., Hall R., Halls K.S.,
RA Hammond S., Harley J.L., Hart E.A., Heath P.D., Heathcott R.,
RA Holmes S.J., Howden P.J., Howe K.L., Howell G.R., Huckle E.,
RA Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., Joy A.A.,
RA Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., Langford C.,
RA Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., Lloyd D.M.,
RA Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M.,
RA Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K.,
RA McMurray A., Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T.,
RA Novik K.L., Oliver K., Overton-Larty E.K., Parker A., Patel R.,
RA Pearce A.V., Peck A.I., Phillimore B.J.C.T., Phillips S., Plumb R.W.,
RA Porter K.M., Ramsey Y., Ranby S.A., Rice C.M., Ross M.T., Searle S.M.,
RA Sehra H.K., Sheridan E., Skuce C.D., Smith S., Smith M., Spraggon L.,
RA Squares S.L., Steward C.A., Sycamore N., Tamlyn-Hall G., Tester J.,
RA Theaker A.J., Thomas D.W., Thorpe A., Tracey A., Tromans A., Tubby B.,
RA Wall M., Wallis J.M., West A.P., White S.S., Whitehead S.L.,
RA Whittaker H., Wild A., Willey D.J., Wilmer T.E., Wood J.M., Wray P.W.,
RA Wyatt J.C., Young L., Younger R.M., Bentley D.R., Coulson A.,
RA Durbin R.M., Hubbard T., Sulston J.E., Dunham I., Rogers J., Beck S.;
RT "The DNA sequence and analysis of human chromosome 6.";
RL Nature 425:805-811(2003).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-73, AND MASS
RP SPECTROMETRY.
RC TISSUE=Cervix carcinoma;
RX PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007;
RA Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,
RA Greff Z., Keri G., Stemmann O., Mann M.;
RT "Kinase-selective enrichment enables quantitative phosphoproteomics of
RT the kinome across the cell cycle.";
RL Mol. Cell 31:438-448(2008).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-20, AND MASS
RP SPECTROMETRY.
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.,
RA Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full
RT phosphorylation site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [8]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
RA Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [9]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, MASS SPECTROMETRY, AND
RP CLEAVAGE OF INITIATOR METHIONINE.
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.,
RA Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K.,
RA Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-
RT terminal acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
CC -!- FUNCTION: Inhibits the chaperone activity of HSP70/HSC70 by
CC promoting substrate release.
CC -!- SUBUNIT: Binds to the ATPase domain of HSP/HSC70 chaperones.
CC -!- INTERACTION:
CC Q8AZK7:EBNA-LP (xeno); NbExp=2; IntAct=EBI-355275, EBI-1185167;
CC -!- SIMILARITY: Contains 1 BAG domain.
CC -----------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution-NoDerivs License
CC -----------------------------------------------------------------------
DR EMBL; AF095192; AAD16121.1; -; mRNA.
DR EMBL; AL050287; CAB43388.1; -; mRNA.
DR EMBL; CR533496; CAG38527.1; -; mRNA.
DR EMBL; AL031321; CAI21565.1; -; Genomic_DNA.
DR EMBL; AL136311; CAI21565.1; JOINED; Genomic_DNA.
DR EMBL; AL136311; CAI20515.1; -; Genomic_DNA.
DR EMBL; AL031321; CAI20515.1; JOINED; Genomic_DNA.
DR EMBL; BC125039; AAI25040.1; -; mRNA.
DR PIR; T08764; T08764.
DR RefSeq; NP_004273.1; NM_004282.3.
DR UniGene; Hs.745046; -.
DR ProteinModelPortal; O95816; -.
DR SMR; O95816; 108-188.
DR IntAct; O95816; 28.
DR MINT; MINT-5002329; -.
DR STRING; 9606.ENSP00000359727; -.
DR PhosphoSite; O95816; -.
DR PaxDb; O95816; -.
DR PeptideAtlas; O95816; -.
DR PRIDE; O95816; -.
DR DNASU; 9532; -.
DR Ensembl; ENST00000370693; ENSP00000359727; ENSG00000112208.
DR GeneID; 9532; -.
DR KEGG; hsa:9532; -.
DR UCSC; uc003pdr.3; human.
DR CTD; 9532; -.
DR GeneCards; GC06P057084; -.
DR HGNC; HGNC:938; BAG2.
DR MIM; 603882; gene.
DR neXtProt; NX_O95816; -.
DR PharmGKB; PA25238; -.
DR eggNOG; NOG251652; -.
DR HOGENOM; HOG000073529; -.
DR HOVERGEN; HBG004808; -.
DR InParanoid; O95816; -.
DR KO; K09556; -.
DR OMA; IQAKMNE; -.
DR PhylomeDB; O95816; -.
DR GeneWiki; BAG2; -.
DR GenomeRNAi; 9532; -.
DR NextBio; 35736; -.
DR PRO; PR:O95816; -.
DR ArrayExpress; O95816; -.
DR Bgee; O95816; -.
DR CleanEx; HS_BAG2; -.
DR Genevestigator; O95816; -.
DR GO; GO:0006457; P:protein folding; TAS:ProtInc.
DR InterPro; IPR003103; BAG_domain.
DR Pfam; PF02179; BAG; 1.
DR SMART; SM00264; BAG; 1.
DR PROSITE; PS51035; BAG; 1.
PE 1: Evidence at protein level;
KW Acetylation; Chaperone; Coiled coil; Complete proteome;
KW Phosphoprotein; Reference proteome.
FT INIT_MET 1 1 Removed.
FT CHAIN 2 211 BAG family molecular chaperone regulator
FT 2.
FT /FTId=PRO_0000088866.
FT DOMAIN 109 189 BAG.
FT COILED 20 61 Potential.
FT MOD_RES 2 2 N-acetylalanine.
FT MOD_RES 20 20 Phosphoserine.
FT MOD_RES 73 73 Phosphoserine.
FT CONFLICT 180 180 N -> D (in Ref. 3; CAG38527).
SQ SEQUENCE 211 AA; 23772 MW; CAF631F4578FCCA3 CRC64;
MAQAKINAKA NEGRFCRSSS MADRSSRLLE SLDQLELRVE ALREAATAVE QEKEILLEMI
HSIQNSQDMR QISDGEREEL NLTANRLMGR TLTVEVSVET IRNPQQQESL KHATRIIDEV
VNKFLDDLGN AKSHLMSLYS ACSSEVPHGP VDQKFQSIVI GCALEDQKKI KRRLETLLRN
IENSDKAIKL LEHSKGAGSK TLQQNAESRF N
//
ID BAG2_HUMAN Reviewed; 211 AA.
AC O95816; Q08AS9; Q6FID0;
DT 11-JAN-2001, integrated into UniProtKB/Swiss-Prot.
read moreDT 01-MAY-1999, sequence version 1.
DT 22-JAN-2014, entry version 117.
DE RecName: Full=BAG family molecular chaperone regulator 2;
DE Short=BAG-2;
DE AltName: Full=Bcl-2-associated athanogene 2;
GN Name=BAG2;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Uterus;
RX PubMed=11230166; DOI=10.1101/gr.GR1547R;
RA Wiemann S., Weil B., Wellenreuther R., Gassenhuber J., Glassl S.,
RA Ansorge W., Boecher M., Bloecker H., Bauersachs S., Blum H.,
RA Lauber J., Duesterhoeft A., Beyer A., Koehrer K., Strack N.,
RA Mewes H.-W., Ottenwaelder B., Obermaier B., Tampe J., Heubner D.,
RA Wambutt R., Korn B., Klein M., Poustka A.;
RT "Towards a catalog of human genes and proteins: sequencing and
RT analysis of 500 novel complete protein coding human cDNAs.";
RL Genome Res. 11:422-435(2001).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.;
RT "Cloning of human full open reading frames in Gateway(TM) system entry
RT vector (pDONR201).";
RL Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=14574404; DOI=10.1038/nature02055;
RA Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L.,
RA Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E.,
RA Gilbert J.G.R., Clamp M.E., Bethel G., Milne S., Ainscough R.,
RA Almeida J.P., Ambrose K.D., Andrews T.D., Ashwell R.I.S.,
RA Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Barker D.J.,
RA Barlow K.F., Bates K., Beare D.M., Beasley H., Beasley O., Bird C.P.,
RA Blakey S.E., Bray-Allen S., Brook J., Brown A.J., Brown J.Y.,
RA Burford D.C., Burrill W., Burton J., Carder C., Carter N.P.,
RA Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V.,
RA Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J.,
RA Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E.,
RA Ellington A.E., Evans K.A., Faulkner L., Francis M.D., Frankish A.,
RA Frankland J., French L., Garner P., Garnett J., Ghori M.J.,
RA Gilby L.M., Gillson C.J., Glithero R.J., Grafham D.V., Grant M.,
RA Gribble S., Griffiths C., Griffiths M.N.D., Hall R., Halls K.S.,
RA Hammond S., Harley J.L., Hart E.A., Heath P.D., Heathcott R.,
RA Holmes S.J., Howden P.J., Howe K.L., Howell G.R., Huckle E.,
RA Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., Joy A.A.,
RA Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., Langford C.,
RA Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., Lloyd D.M.,
RA Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M.,
RA Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K.,
RA McMurray A., Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T.,
RA Novik K.L., Oliver K., Overton-Larty E.K., Parker A., Patel R.,
RA Pearce A.V., Peck A.I., Phillimore B.J.C.T., Phillips S., Plumb R.W.,
RA Porter K.M., Ramsey Y., Ranby S.A., Rice C.M., Ross M.T., Searle S.M.,
RA Sehra H.K., Sheridan E., Skuce C.D., Smith S., Smith M., Spraggon L.,
RA Squares S.L., Steward C.A., Sycamore N., Tamlyn-Hall G., Tester J.,
RA Theaker A.J., Thomas D.W., Thorpe A., Tracey A., Tromans A., Tubby B.,
RA Wall M., Wallis J.M., West A.P., White S.S., Whitehead S.L.,
RA Whittaker H., Wild A., Willey D.J., Wilmer T.E., Wood J.M., Wray P.W.,
RA Wyatt J.C., Young L., Younger R.M., Bentley D.R., Coulson A.,
RA Durbin R.M., Hubbard T., Sulston J.E., Dunham I., Rogers J., Beck S.;
RT "The DNA sequence and analysis of human chromosome 6.";
RL Nature 425:805-811(2003).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-73, AND MASS
RP SPECTROMETRY.
RC TISSUE=Cervix carcinoma;
RX PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007;
RA Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,
RA Greff Z., Keri G., Stemmann O., Mann M.;
RT "Kinase-selective enrichment enables quantitative phosphoproteomics of
RT the kinome across the cell cycle.";
RL Mol. Cell 31:438-448(2008).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-20, AND MASS
RP SPECTROMETRY.
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.,
RA Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full
RT phosphorylation site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [8]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
RA Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [9]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, MASS SPECTROMETRY, AND
RP CLEAVAGE OF INITIATOR METHIONINE.
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.,
RA Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K.,
RA Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-
RT terminal acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
CC -!- FUNCTION: Inhibits the chaperone activity of HSP70/HSC70 by
CC promoting substrate release.
CC -!- SUBUNIT: Binds to the ATPase domain of HSP/HSC70 chaperones.
CC -!- INTERACTION:
CC Q8AZK7:EBNA-LP (xeno); NbExp=2; IntAct=EBI-355275, EBI-1185167;
CC -!- SIMILARITY: Contains 1 BAG domain.
CC -----------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution-NoDerivs License
CC -----------------------------------------------------------------------
DR EMBL; AF095192; AAD16121.1; -; mRNA.
DR EMBL; AL050287; CAB43388.1; -; mRNA.
DR EMBL; CR533496; CAG38527.1; -; mRNA.
DR EMBL; AL031321; CAI21565.1; -; Genomic_DNA.
DR EMBL; AL136311; CAI21565.1; JOINED; Genomic_DNA.
DR EMBL; AL136311; CAI20515.1; -; Genomic_DNA.
DR EMBL; AL031321; CAI20515.1; JOINED; Genomic_DNA.
DR EMBL; BC125039; AAI25040.1; -; mRNA.
DR PIR; T08764; T08764.
DR RefSeq; NP_004273.1; NM_004282.3.
DR UniGene; Hs.745046; -.
DR ProteinModelPortal; O95816; -.
DR SMR; O95816; 108-188.
DR IntAct; O95816; 28.
DR MINT; MINT-5002329; -.
DR STRING; 9606.ENSP00000359727; -.
DR PhosphoSite; O95816; -.
DR PaxDb; O95816; -.
DR PeptideAtlas; O95816; -.
DR PRIDE; O95816; -.
DR DNASU; 9532; -.
DR Ensembl; ENST00000370693; ENSP00000359727; ENSG00000112208.
DR GeneID; 9532; -.
DR KEGG; hsa:9532; -.
DR UCSC; uc003pdr.3; human.
DR CTD; 9532; -.
DR GeneCards; GC06P057084; -.
DR HGNC; HGNC:938; BAG2.
DR MIM; 603882; gene.
DR neXtProt; NX_O95816; -.
DR PharmGKB; PA25238; -.
DR eggNOG; NOG251652; -.
DR HOGENOM; HOG000073529; -.
DR HOVERGEN; HBG004808; -.
DR InParanoid; O95816; -.
DR KO; K09556; -.
DR OMA; IQAKMNE; -.
DR PhylomeDB; O95816; -.
DR GeneWiki; BAG2; -.
DR GenomeRNAi; 9532; -.
DR NextBio; 35736; -.
DR PRO; PR:O95816; -.
DR ArrayExpress; O95816; -.
DR Bgee; O95816; -.
DR CleanEx; HS_BAG2; -.
DR Genevestigator; O95816; -.
DR GO; GO:0006457; P:protein folding; TAS:ProtInc.
DR InterPro; IPR003103; BAG_domain.
DR Pfam; PF02179; BAG; 1.
DR SMART; SM00264; BAG; 1.
DR PROSITE; PS51035; BAG; 1.
PE 1: Evidence at protein level;
KW Acetylation; Chaperone; Coiled coil; Complete proteome;
KW Phosphoprotein; Reference proteome.
FT INIT_MET 1 1 Removed.
FT CHAIN 2 211 BAG family molecular chaperone regulator
FT 2.
FT /FTId=PRO_0000088866.
FT DOMAIN 109 189 BAG.
FT COILED 20 61 Potential.
FT MOD_RES 2 2 N-acetylalanine.
FT MOD_RES 20 20 Phosphoserine.
FT MOD_RES 73 73 Phosphoserine.
FT CONFLICT 180 180 N -> D (in Ref. 3; CAG38527).
SQ SEQUENCE 211 AA; 23772 MW; CAF631F4578FCCA3 CRC64;
MAQAKINAKA NEGRFCRSSS MADRSSRLLE SLDQLELRVE ALREAATAVE QEKEILLEMI
HSIQNSQDMR QISDGEREEL NLTANRLMGR TLTVEVSVET IRNPQQQESL KHATRIIDEV
VNKFLDDLGN AKSHLMSLYS ACSSEVPHGP VDQKFQSIVI GCALEDQKKI KRRLETLLRN
IENSDKAIKL LEHSKGAGSK TLQQNAESRF N
//
MIM
603882
*RECORD*
*FIELD* NO
603882
*FIELD* TI
*603882 BCL2-ASSOCIATED ATHANOGENE 2; BAG2
*FIELD* TX
The chaperone activity of Hsp70 (see 140550) family members such as
read moreHsc70 (600816) is regulated by partner proteins that either modulate the
peptide-binding cycle or target the actions of these chaperones to
specific proteins and subcellular compartments. The Hip protein
collaborates with Hsc70/Hsp70 and DNAJ (see 602837) family proteins to
stimulate ATP hydrolysis and thus stabilize Hsc70/Hsp70 complexes with
substrate polypeptides. BAG1 (601497) competes with Hip for binding to
the Hsc70/Hsp70 ATPase domain and promotes substrate release. Using a
yeast 2-hybrid screen with the ATPase domain of Hsc70 as bait, Takayama
et al. (1999) isolated cDNAs encoding 2 BAG1-like proteins that they
named BAG2 and BAG3 (603883). By searching an EST database, they
identified partial cDNAs corresponding to 2 additional BAG1 family
members, BAG4 (603884) and BAG5 (603885). All the BAG proteins have an
approximately 45-amino acid BAG domain near the C terminus but differ
markedly in their N-terminal regions. The predicted BAG2 protein
contains 211 amino acids. Takayama et al. (1999) demonstrated that the
BAG domains of BAG1, BAG2, and BAG3 interact specifically with the Hsc70
ATPase domain in vitro and in mammalian cells. Surface plasmon resonance
and in vitro protein refolding assays revealed that all 3 proteins bind
with high affinity to the ATPase domain of Hsc70 and inhibit its
chaperone activity in a Hip-repressible manner. These authors stated
that the functional antagonisms displayed between BAG family proteins
and Hip suggest that a proper balance of these 2 types of protein is
required for achieving optimal cycles of substrate binding and release
required for inducting conformational changes in proteins, with Hip
promoting peptide substrate binding by Hsc70/Hsp70 and BAG family
proteins promoting dissociation.
*FIELD* RF
1. Takayama, S.; Xie, Z.; Reed, J. C.: An evolutionarily conserved
family of Hsp70/Hsc70 molecular chaperone regulators. J. Biol. Chem. 274:
781-786, 1999.
*FIELD* CD
Rebekah S. Rasooly: 6/7/1999
*FIELD* ED
alopez: 06/07/1999
*RECORD*
*FIELD* NO
603882
*FIELD* TI
*603882 BCL2-ASSOCIATED ATHANOGENE 2; BAG2
*FIELD* TX
The chaperone activity of Hsp70 (see 140550) family members such as
read moreHsc70 (600816) is regulated by partner proteins that either modulate the
peptide-binding cycle or target the actions of these chaperones to
specific proteins and subcellular compartments. The Hip protein
collaborates with Hsc70/Hsp70 and DNAJ (see 602837) family proteins to
stimulate ATP hydrolysis and thus stabilize Hsc70/Hsp70 complexes with
substrate polypeptides. BAG1 (601497) competes with Hip for binding to
the Hsc70/Hsp70 ATPase domain and promotes substrate release. Using a
yeast 2-hybrid screen with the ATPase domain of Hsc70 as bait, Takayama
et al. (1999) isolated cDNAs encoding 2 BAG1-like proteins that they
named BAG2 and BAG3 (603883). By searching an EST database, they
identified partial cDNAs corresponding to 2 additional BAG1 family
members, BAG4 (603884) and BAG5 (603885). All the BAG proteins have an
approximately 45-amino acid BAG domain near the C terminus but differ
markedly in their N-terminal regions. The predicted BAG2 protein
contains 211 amino acids. Takayama et al. (1999) demonstrated that the
BAG domains of BAG1, BAG2, and BAG3 interact specifically with the Hsc70
ATPase domain in vitro and in mammalian cells. Surface plasmon resonance
and in vitro protein refolding assays revealed that all 3 proteins bind
with high affinity to the ATPase domain of Hsc70 and inhibit its
chaperone activity in a Hip-repressible manner. These authors stated
that the functional antagonisms displayed between BAG family proteins
and Hip suggest that a proper balance of these 2 types of protein is
required for achieving optimal cycles of substrate binding and release
required for inducting conformational changes in proteins, with Hip
promoting peptide substrate binding by Hsc70/Hsp70 and BAG family
proteins promoting dissociation.
*FIELD* RF
1. Takayama, S.; Xie, Z.; Reed, J. C.: An evolutionarily conserved
family of Hsp70/Hsc70 molecular chaperone regulators. J. Biol. Chem. 274:
781-786, 1999.
*FIELD* CD
Rebekah S. Rasooly: 6/7/1999
*FIELD* ED
alopez: 06/07/1999