Full text data of BAG5
BAG5
(KIAA0873)
[Confidence: low (only semi-automatic identification from reviews)]
BAG family molecular chaperone regulator 5; BAG-5 (Bcl-2-associated athanogene 5)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
BAG family molecular chaperone regulator 5; BAG-5 (Bcl-2-associated athanogene 5)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
UniProt
Q9UL15
ID BAG5_HUMAN Reviewed; 447 AA.
AC Q9UL15; O94950; Q86W59;
DT 11-JAN-2001, integrated into UniProtKB/Swiss-Prot.
read moreDT 01-MAY-2000, sequence version 1.
DT 22-JAN-2014, entry version 112.
DE RecName: Full=BAG family molecular chaperone regulator 5;
DE Short=BAG-5;
DE AltName: Full=Bcl-2-associated athanogene 5;
GN Name=BAG5; Synonyms=KIAA0873;
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] (ISOFORM 1).
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] (ISOFORM 1).
RC TISSUE=Brain;
RX PubMed=10048485; DOI=10.1093/dnares/5.6.355;
RA Nagase T., Ishikawa K., Suyama M., Kikuno R., Hirosawa M.,
RA Miyajima N., Tanaka A., Kotani H., Nomura N., Ohara O.;
RT "Prediction of the coding sequences of unidentified human genes. XII.
RT The complete sequences of 100 new cDNA clones from brain which code
RT for large proteins in vitro.";
RL DNA Res. 5:355-364(1998).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=12508121; DOI=10.1038/nature01348;
RA Heilig R., Eckenberg R., Petit J.-L., Fonknechten N., Da Silva C.,
RA Cattolico L., Levy M., Barbe V., De Berardinis V., Ureta-Vidal A.,
RA Pelletier E., Vico V., Anthouard V., Rowen L., Madan A., Qin S.,
RA Sun H., Du H., Pepin K., Artiguenave F., Robert C., Cruaud C.,
RA Bruels T., Jaillon O., Friedlander L., Samson G., Brottier P.,
RA Cure S., Segurens B., Aniere F., Samain S., Crespeau H., Abbasi N.,
RA Aiach N., Boscus D., Dickhoff R., Dors M., Dubois I., Friedman C.,
RA Gouyvenoux M., James R., Madan A., Mairey-Estrada B., Mangenot S.,
RA Martins N., Menard M., Oztas S., Ratcliffe A., Shaffer T., Trask B.,
RA Vacherie B., Bellemere C., Belser C., Besnard-Gonnet M.,
RA Bartol-Mavel D., Boutard M., Briez-Silla S., Combette S.,
RA Dufosse-Laurent V., Ferron C., Lechaplais C., Louesse C., Muselet D.,
RA Magdelenat G., Pateau E., Petit E., Sirvain-Trukniewicz P., Trybou A.,
RA Vega-Czarny N., Bataille E., Bluet E., Bordelais I., Dubois M.,
RA Dumont C., Guerin T., Haffray S., Hammadi R., Muanga J., Pellouin V.,
RA Robert D., Wunderle E., Gauguet G., Roy A., Sainte-Marthe L.,
RA Verdier J., Verdier-Discala C., Hillier L.W., Fulton L., McPherson J.,
RA Matsuda F., Wilson R., Scarpelli C., Gyapay G., Wincker P., Saurin W.,
RA Quetier F., Waterston R., Hood L., Weissenbach J.;
RT "The DNA sequence and analysis of human chromosome 14.";
RL Nature 421:601-607(2003).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2), AND VARIANT
RP TRP-157.
RC TISSUE=Brain;
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 [5]
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 [6]
RP STRUCTURE BY NMR OF 275-350, X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF
RP 341-447 IN COMPLEX WITH HSPA1, DOMAIN BAG, FUNCTION, AND SUBUNIT.
RX PubMed=20223214; DOI=10.1016/j.str.2010.01.004;
RA Arakawa A., Handa N., Ohsawa N., Shida M., Kigawa T., Hayashi F.,
RA Shirouzu M., Yokoyama S.;
RT "The C-terminal BAG domain of BAG5 induces conformational changes of
RT the Hsp70 nucleotide-binding domain for ADP-ATP exchange.";
RL Structure 18:309-319(2010).
CC -!- FUNCTION: Inhibits both auto-ubiquitination of PARK2 and
CC ubiquitination of target proteins by PARK2 (By similarity). May
CC function as a nucleotide exchange factor for HSP/HSP70, promoting
CC ADP release, and activating Hsp70-mediated refolding.
CC -!- SUBUNIT: Binds to the ATPase domain of HSP/HSC70 chaperones. Binds
CC PARK2 (By similarity).
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9UL15-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9UL15-2; Sequence=VSP_037996;
CC Note=No experimental confirmation available;
CC -!- DOMAIN: The fifth BAG domain is responsible for the interaction
CC with HSP70 nucleotide-binding domain.
CC -!- SIMILARITY: Contains 5 BAG domains.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAA74896.1; Type=Erroneous initiation;
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; AF095195; AAD16124.2; -; mRNA.
DR EMBL; AB020680; BAA74896.1; ALT_INIT; mRNA.
DR EMBL; AL139300; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC044216; AAH44216.2; -; mRNA.
DR EMBL; BC050551; AAH50551.1; -; mRNA.
DR RefSeq; NP_001015048.1; NM_001015048.2.
DR RefSeq; NP_001015049.1; NM_001015049.2.
DR RefSeq; NP_004864.1; NM_004873.3.
DR UniGene; Hs.5443; -.
DR PDB; 2D9D; NMR; -; A=275-350.
DR PDB; 3A8Y; X-ray; 2.30 A; C/D=341-447.
DR PDBsum; 2D9D; -.
DR PDBsum; 3A8Y; -.
DR ProteinModelPortal; Q9UL15; -.
DR SMR; Q9UL15; 1-89, 184-258, 276-447.
DR DIP; DIP-53428N; -.
DR IntAct; Q9UL15; 6.
DR MINT; MINT-1147557; -.
DR STRING; 9606.ENSP00000338814; -.
DR PhosphoSite; Q9UL15; -.
DR DMDM; 12643895; -.
DR PaxDb; Q9UL15; -.
DR PRIDE; Q9UL15; -.
DR Ensembl; ENST00000299204; ENSP00000299204; ENSG00000166170.
DR Ensembl; ENST00000337322; ENSP00000338814; ENSG00000166170.
DR Ensembl; ENST00000445922; ENSP00000391713; ENSG00000166170.
DR GeneID; 9529; -.
DR KEGG; hsa:9529; -.
DR UCSC; uc001yni.2; human.
DR CTD; 9529; -.
DR GeneCards; GC14M104022; -.
DR HGNC; HGNC:941; BAG5.
DR HPA; HPA016429; -.
DR MIM; 603885; gene.
DR neXtProt; NX_Q9UL15; -.
DR PharmGKB; PA25241; -.
DR eggNOG; NOG262724; -.
DR HOGENOM; HOG000070447; -.
DR HOVERGEN; HBG004810; -.
DR InParanoid; Q9UL15; -.
DR KO; K09559; -.
DR OMA; DMGNQHP; -.
DR OrthoDB; EOG7WX08F; -.
DR PhylomeDB; Q9UL15; -.
DR EvolutionaryTrace; Q9UL15; -.
DR GeneWiki; BAG5; -.
DR GenomeRNAi; 9529; -.
DR NextBio; 35720; -.
DR PRO; PR:Q9UL15; -.
DR ArrayExpress; Q9UL15; -.
DR Bgee; Q9UL15; -.
DR CleanEx; HS_BAG5; -.
DR Genevestigator; Q9UL15; -.
DR GO; GO:0016234; C:inclusion body; IDA:BHF-UCL.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; IDA:BHF-UCL.
DR GO; GO:0031625; F:ubiquitin protein ligase binding; ISS:BHF-UCL.
DR GO; GO:0061084; P:negative regulation of protein refolding; ISS:BHF-UCL.
DR GO; GO:0051444; P:negative regulation of ubiquitin-protein ligase activity; ISS:BHF-UCL.
DR GO; GO:0070997; P:neuron death; ISS:BHF-UCL.
DR GO; GO:0006457; P:protein folding; TAS:ProtInc.
DR GO; GO:0090083; P:regulation of inclusion body assembly; IMP:BHF-UCL.
DR InterPro; IPR003103; BAG_domain.
DR Pfam; PF02179; BAG; 4.
DR SMART; SM00264; BAG; 4.
DR PROSITE; PS51035; BAG; 4.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Chaperone; Complete proteome;
KW Polymorphism; Reference proteome; Repeat.
FT CHAIN 1 447 BAG family molecular chaperone regulator
FT 5.
FT /FTId=PRO_0000088872.
FT DOMAIN 9 86 BAG 1.
FT DOMAIN 95 167 BAG 2.
FT DOMAIN 182 260 BAG 3.
FT DOMAIN 275 350 BAG 4.
FT DOMAIN 365 442 BAG 5.
FT VAR_SEQ 1 1 M -> MRFHWLPTLSEPFDRNQELETCIRPLWTPSGSACET
FT EHNKSM (in isoform 2).
FT /FTId=VSP_037996.
FT VARIANT 157 157 C -> W (in dbSNP:rs17854644).
FT /FTId=VAR_058712.
FT HELIX 277 295
FT TURN 299 301
FT HELIX 302 317
FT HELIX 318 320
FT HELIX 326 350
FT TURN 356 358
FT HELIX 364 384
FT HELIX 393 410
FT HELIX 418 442
SQ SEQUENCE 447 AA; 51200 MW; 0D3F7EA6B612C1F5 CRC64;
MDMGNQHPSI SRLQEIQKEV KSVEQQVIGF SGLSDDKNYK KLERILTKQL FEIDSVDTEG
KGDIQQARKR AAQETERLLK ELEQNANHPH RIEIQNIFEE AQSLVREKIV PFYNGGNCVT
DEFEEGIQDI ILRLTHVKTG GKISLRKARY HTLTKICAVQ EIIEDCMKKQ PSLPLSEDAH
PSVAKINFVM CEVNKARGVL IALLMGVNNN ETCRHLSCVL SGLIADLDAL DVCGRTEIRN
YRREVVEDIN KLLKYLDLEE EADTTKAFDL RQNHSILKIE KVLKRMREIK NELLQAQNPS
ELYLSSKTEL QGLIGQLDEV SLEKNPCIRE ARRRAVIEVQ TLITYIDLKE ALEKRKLFAC
EEHPSHKAVW NVLGNLSEIQ GEVLSFDGNR TDKNYIRLEE LLTKQLLALD AVDPQGEEKC
KAARKQAVRL AQNILSYLDL KSDEWEY
//
ID BAG5_HUMAN Reviewed; 447 AA.
AC Q9UL15; O94950; Q86W59;
DT 11-JAN-2001, integrated into UniProtKB/Swiss-Prot.
read moreDT 01-MAY-2000, sequence version 1.
DT 22-JAN-2014, entry version 112.
DE RecName: Full=BAG family molecular chaperone regulator 5;
DE Short=BAG-5;
DE AltName: Full=Bcl-2-associated athanogene 5;
GN Name=BAG5; Synonyms=KIAA0873;
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] (ISOFORM 1).
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] (ISOFORM 1).
RC TISSUE=Brain;
RX PubMed=10048485; DOI=10.1093/dnares/5.6.355;
RA Nagase T., Ishikawa K., Suyama M., Kikuno R., Hirosawa M.,
RA Miyajima N., Tanaka A., Kotani H., Nomura N., Ohara O.;
RT "Prediction of the coding sequences of unidentified human genes. XII.
RT The complete sequences of 100 new cDNA clones from brain which code
RT for large proteins in vitro.";
RL DNA Res. 5:355-364(1998).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=12508121; DOI=10.1038/nature01348;
RA Heilig R., Eckenberg R., Petit J.-L., Fonknechten N., Da Silva C.,
RA Cattolico L., Levy M., Barbe V., De Berardinis V., Ureta-Vidal A.,
RA Pelletier E., Vico V., Anthouard V., Rowen L., Madan A., Qin S.,
RA Sun H., Du H., Pepin K., Artiguenave F., Robert C., Cruaud C.,
RA Bruels T., Jaillon O., Friedlander L., Samson G., Brottier P.,
RA Cure S., Segurens B., Aniere F., Samain S., Crespeau H., Abbasi N.,
RA Aiach N., Boscus D., Dickhoff R., Dors M., Dubois I., Friedman C.,
RA Gouyvenoux M., James R., Madan A., Mairey-Estrada B., Mangenot S.,
RA Martins N., Menard M., Oztas S., Ratcliffe A., Shaffer T., Trask B.,
RA Vacherie B., Bellemere C., Belser C., Besnard-Gonnet M.,
RA Bartol-Mavel D., Boutard M., Briez-Silla S., Combette S.,
RA Dufosse-Laurent V., Ferron C., Lechaplais C., Louesse C., Muselet D.,
RA Magdelenat G., Pateau E., Petit E., Sirvain-Trukniewicz P., Trybou A.,
RA Vega-Czarny N., Bataille E., Bluet E., Bordelais I., Dubois M.,
RA Dumont C., Guerin T., Haffray S., Hammadi R., Muanga J., Pellouin V.,
RA Robert D., Wunderle E., Gauguet G., Roy A., Sainte-Marthe L.,
RA Verdier J., Verdier-Discala C., Hillier L.W., Fulton L., McPherson J.,
RA Matsuda F., Wilson R., Scarpelli C., Gyapay G., Wincker P., Saurin W.,
RA Quetier F., Waterston R., Hood L., Weissenbach J.;
RT "The DNA sequence and analysis of human chromosome 14.";
RL Nature 421:601-607(2003).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2), AND VARIANT
RP TRP-157.
RC TISSUE=Brain;
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 [5]
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 [6]
RP STRUCTURE BY NMR OF 275-350, X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF
RP 341-447 IN COMPLEX WITH HSPA1, DOMAIN BAG, FUNCTION, AND SUBUNIT.
RX PubMed=20223214; DOI=10.1016/j.str.2010.01.004;
RA Arakawa A., Handa N., Ohsawa N., Shida M., Kigawa T., Hayashi F.,
RA Shirouzu M., Yokoyama S.;
RT "The C-terminal BAG domain of BAG5 induces conformational changes of
RT the Hsp70 nucleotide-binding domain for ADP-ATP exchange.";
RL Structure 18:309-319(2010).
CC -!- FUNCTION: Inhibits both auto-ubiquitination of PARK2 and
CC ubiquitination of target proteins by PARK2 (By similarity). May
CC function as a nucleotide exchange factor for HSP/HSP70, promoting
CC ADP release, and activating Hsp70-mediated refolding.
CC -!- SUBUNIT: Binds to the ATPase domain of HSP/HSC70 chaperones. Binds
CC PARK2 (By similarity).
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9UL15-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9UL15-2; Sequence=VSP_037996;
CC Note=No experimental confirmation available;
CC -!- DOMAIN: The fifth BAG domain is responsible for the interaction
CC with HSP70 nucleotide-binding domain.
CC -!- SIMILARITY: Contains 5 BAG domains.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAA74896.1; Type=Erroneous initiation;
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; AF095195; AAD16124.2; -; mRNA.
DR EMBL; AB020680; BAA74896.1; ALT_INIT; mRNA.
DR EMBL; AL139300; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC044216; AAH44216.2; -; mRNA.
DR EMBL; BC050551; AAH50551.1; -; mRNA.
DR RefSeq; NP_001015048.1; NM_001015048.2.
DR RefSeq; NP_001015049.1; NM_001015049.2.
DR RefSeq; NP_004864.1; NM_004873.3.
DR UniGene; Hs.5443; -.
DR PDB; 2D9D; NMR; -; A=275-350.
DR PDB; 3A8Y; X-ray; 2.30 A; C/D=341-447.
DR PDBsum; 2D9D; -.
DR PDBsum; 3A8Y; -.
DR ProteinModelPortal; Q9UL15; -.
DR SMR; Q9UL15; 1-89, 184-258, 276-447.
DR DIP; DIP-53428N; -.
DR IntAct; Q9UL15; 6.
DR MINT; MINT-1147557; -.
DR STRING; 9606.ENSP00000338814; -.
DR PhosphoSite; Q9UL15; -.
DR DMDM; 12643895; -.
DR PaxDb; Q9UL15; -.
DR PRIDE; Q9UL15; -.
DR Ensembl; ENST00000299204; ENSP00000299204; ENSG00000166170.
DR Ensembl; ENST00000337322; ENSP00000338814; ENSG00000166170.
DR Ensembl; ENST00000445922; ENSP00000391713; ENSG00000166170.
DR GeneID; 9529; -.
DR KEGG; hsa:9529; -.
DR UCSC; uc001yni.2; human.
DR CTD; 9529; -.
DR GeneCards; GC14M104022; -.
DR HGNC; HGNC:941; BAG5.
DR HPA; HPA016429; -.
DR MIM; 603885; gene.
DR neXtProt; NX_Q9UL15; -.
DR PharmGKB; PA25241; -.
DR eggNOG; NOG262724; -.
DR HOGENOM; HOG000070447; -.
DR HOVERGEN; HBG004810; -.
DR InParanoid; Q9UL15; -.
DR KO; K09559; -.
DR OMA; DMGNQHP; -.
DR OrthoDB; EOG7WX08F; -.
DR PhylomeDB; Q9UL15; -.
DR EvolutionaryTrace; Q9UL15; -.
DR GeneWiki; BAG5; -.
DR GenomeRNAi; 9529; -.
DR NextBio; 35720; -.
DR PRO; PR:Q9UL15; -.
DR ArrayExpress; Q9UL15; -.
DR Bgee; Q9UL15; -.
DR CleanEx; HS_BAG5; -.
DR Genevestigator; Q9UL15; -.
DR GO; GO:0016234; C:inclusion body; IDA:BHF-UCL.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; IDA:BHF-UCL.
DR GO; GO:0031625; F:ubiquitin protein ligase binding; ISS:BHF-UCL.
DR GO; GO:0061084; P:negative regulation of protein refolding; ISS:BHF-UCL.
DR GO; GO:0051444; P:negative regulation of ubiquitin-protein ligase activity; ISS:BHF-UCL.
DR GO; GO:0070997; P:neuron death; ISS:BHF-UCL.
DR GO; GO:0006457; P:protein folding; TAS:ProtInc.
DR GO; GO:0090083; P:regulation of inclusion body assembly; IMP:BHF-UCL.
DR InterPro; IPR003103; BAG_domain.
DR Pfam; PF02179; BAG; 4.
DR SMART; SM00264; BAG; 4.
DR PROSITE; PS51035; BAG; 4.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Chaperone; Complete proteome;
KW Polymorphism; Reference proteome; Repeat.
FT CHAIN 1 447 BAG family molecular chaperone regulator
FT 5.
FT /FTId=PRO_0000088872.
FT DOMAIN 9 86 BAG 1.
FT DOMAIN 95 167 BAG 2.
FT DOMAIN 182 260 BAG 3.
FT DOMAIN 275 350 BAG 4.
FT DOMAIN 365 442 BAG 5.
FT VAR_SEQ 1 1 M -> MRFHWLPTLSEPFDRNQELETCIRPLWTPSGSACET
FT EHNKSM (in isoform 2).
FT /FTId=VSP_037996.
FT VARIANT 157 157 C -> W (in dbSNP:rs17854644).
FT /FTId=VAR_058712.
FT HELIX 277 295
FT TURN 299 301
FT HELIX 302 317
FT HELIX 318 320
FT HELIX 326 350
FT TURN 356 358
FT HELIX 364 384
FT HELIX 393 410
FT HELIX 418 442
SQ SEQUENCE 447 AA; 51200 MW; 0D3F7EA6B612C1F5 CRC64;
MDMGNQHPSI SRLQEIQKEV KSVEQQVIGF SGLSDDKNYK KLERILTKQL FEIDSVDTEG
KGDIQQARKR AAQETERLLK ELEQNANHPH RIEIQNIFEE AQSLVREKIV PFYNGGNCVT
DEFEEGIQDI ILRLTHVKTG GKISLRKARY HTLTKICAVQ EIIEDCMKKQ PSLPLSEDAH
PSVAKINFVM CEVNKARGVL IALLMGVNNN ETCRHLSCVL SGLIADLDAL DVCGRTEIRN
YRREVVEDIN KLLKYLDLEE EADTTKAFDL RQNHSILKIE KVLKRMREIK NELLQAQNPS
ELYLSSKTEL QGLIGQLDEV SLEKNPCIRE ARRRAVIEVQ TLITYIDLKE ALEKRKLFAC
EEHPSHKAVW NVLGNLSEIQ GEVLSFDGNR TDKNYIRLEE LLTKQLLALD AVDPQGEEKC
KAARKQAVRL AQNILSYLDL KSDEWEY
//
MIM
603885
*RECORD*
*FIELD* NO
603885
*FIELD* TI
*603885 BCL2-ASSOCIATED ATHANOGENE 5; BAG5
*FIELD* TX
BAG1 (601497) binds the ATPase domains of Hsp70 (see 140550) and Hsc70
read more(600816), modulating their chaperone activity and functioning as a
competitive antagonist to the co-chaperone Hip, which stabilizes
Hsc70/Hsp70 complexes with substrate polypeptides. See BAG2 (603882).
Takayama et al. (1999) identified cDNAs corresponding to BAG5 and 3
other BAG1-like proteins. These authors concluded that interactions with
various BAG family proteins allow opportunities for specification and
diversification of Hsp70/Hsc70 chaperone functions.
Kalia et al. (2004) demonstrated that rat Bag5 directly interacts with
Hsp70 and parkin (PARK2; 602544), an E3 ubiquitin ligase that is mutated
in a form of early-onset Parkinson disease (600116). Bag5 inhibited both
Hsp70-mediated refolding of misfolded proteins and parkin E3 ubiquitin
ligase activity, and enhanced the sequestration of parkin in protein
aggregates. In rats, overexpression of Bag5 resulted in increased death
of dopaminergic neurons compared to controls, whereas overexpression of
an inhibitory mutant Bag5 resulted in increased dopaminergic survival.
Kalia et al. (2004) concluded that Bag5 is a negative regulator of both
Hsp70 and parkin function that sensitizes dopaminergic neurons to
injury-induced death and thus promotes neurodegeneration.
*FIELD* RF
1. Kalia, S. K.; Lee, S.; Smith, P. D.; Liu, L.; Crocker, S. J.; Thorarinsdottir,
T. E.; Glover, J. R.; Fon, E. A.; Park, D. S.; Lozano, A. M.: BAG5
inhibits parkin and enhances dopaminergic neuron degeneration. Neuron 44:
931-945, 2004.
2. 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* CN
Cassandra L. Kniffin - updated: 4/5/2005
*FIELD* CD
Rebekah S. Rasooly: 6/7/1999
*FIELD* ED
carol: 04/20/2005
wwang: 4/18/2005
ckniffin: 4/5/2005
alopez: 6/7/1999
*RECORD*
*FIELD* NO
603885
*FIELD* TI
*603885 BCL2-ASSOCIATED ATHANOGENE 5; BAG5
*FIELD* TX
BAG1 (601497) binds the ATPase domains of Hsp70 (see 140550) and Hsc70
read more(600816), modulating their chaperone activity and functioning as a
competitive antagonist to the co-chaperone Hip, which stabilizes
Hsc70/Hsp70 complexes with substrate polypeptides. See BAG2 (603882).
Takayama et al. (1999) identified cDNAs corresponding to BAG5 and 3
other BAG1-like proteins. These authors concluded that interactions with
various BAG family proteins allow opportunities for specification and
diversification of Hsp70/Hsc70 chaperone functions.
Kalia et al. (2004) demonstrated that rat Bag5 directly interacts with
Hsp70 and parkin (PARK2; 602544), an E3 ubiquitin ligase that is mutated
in a form of early-onset Parkinson disease (600116). Bag5 inhibited both
Hsp70-mediated refolding of misfolded proteins and parkin E3 ubiquitin
ligase activity, and enhanced the sequestration of parkin in protein
aggregates. In rats, overexpression of Bag5 resulted in increased death
of dopaminergic neurons compared to controls, whereas overexpression of
an inhibitory mutant Bag5 resulted in increased dopaminergic survival.
Kalia et al. (2004) concluded that Bag5 is a negative regulator of both
Hsp70 and parkin function that sensitizes dopaminergic neurons to
injury-induced death and thus promotes neurodegeneration.
*FIELD* RF
1. Kalia, S. K.; Lee, S.; Smith, P. D.; Liu, L.; Crocker, S. J.; Thorarinsdottir,
T. E.; Glover, J. R.; Fon, E. A.; Park, D. S.; Lozano, A. M.: BAG5
inhibits parkin and enhances dopaminergic neuron degeneration. Neuron 44:
931-945, 2004.
2. 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* CN
Cassandra L. Kniffin - updated: 4/5/2005
*FIELD* CD
Rebekah S. Rasooly: 6/7/1999
*FIELD* ED
carol: 04/20/2005
wwang: 4/18/2005
ckniffin: 4/5/2005
alopez: 6/7/1999