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BAG family molecular chaperone regulator 5 (BAG-5) (Bcl-2-associated athanogene 5)

 BAG5_HUMAN              Reviewed;         447 AA.
Q9UL15; O94950; Q86W59;
11-JAN-2001, integrated into UniProtKB/Swiss-Prot.
01-MAY-2000, sequence version 1.
28-MAR-2018, entry version 151.
RecName: Full=BAG family molecular chaperone regulator 5;
Short=BAG-5;
AltName: Full=Bcl-2-associated athanogene 5;
Name=BAG5; Synonyms=KIAA0873;
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).
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).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Brain;
PubMed=10048485; DOI=10.1093/dnares/5.6.355;
Nagase T., Ishikawa K., Suyama M., Kikuno R., Hirosawa M.,
Miyajima N., Tanaka A., Kotani H., Nomura N., Ohara O.;
"Prediction of the coding sequences of unidentified human genes. XII.
The complete sequences of 100 new cDNA clones from brain which code
for large proteins in vitro.";
DNA Res. 5:355-364(1998).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=12508121; DOI=10.1038/nature01348;
Heilig R., Eckenberg R., Petit J.-L., Fonknechten N., Da Silva C.,
Cattolico L., Levy M., Barbe V., De Berardinis V., Ureta-Vidal A.,
Pelletier E., Vico V., Anthouard V., Rowen L., Madan A., Qin S.,
Sun H., Du H., Pepin K., Artiguenave F., Robert C., Cruaud C.,
Bruels T., Jaillon O., Friedlander L., Samson G., Brottier P.,
Cure S., Segurens B., Aniere F., Samain S., Crespeau H., Abbasi N.,
Aiach N., Boscus D., Dickhoff R., Dors M., Dubois I., Friedman C.,
Gouyvenoux M., James R., Madan A., Mairey-Estrada B., Mangenot S.,
Martins N., Menard M., Oztas S., Ratcliffe A., Shaffer T., Trask B.,
Vacherie B., Bellemere C., Belser C., Besnard-Gonnet M.,
Bartol-Mavel D., Boutard M., Briez-Silla S., Combette S.,
Dufosse-Laurent V., Ferron C., Lechaplais C., Louesse C., Muselet D.,
Magdelenat G., Pateau E., Petit E., Sirvain-Trukniewicz P., Trybou A.,
Vega-Czarny N., Bataille E., Bluet E., Bordelais I., Dubois M.,
Dumont C., Guerin T., Haffray S., Hammadi R., Muanga J., Pellouin V.,
Robert D., Wunderle E., Gauguet G., Roy A., Sainte-Marthe L.,
Verdier J., Verdier-Discala C., Hillier L.W., Fulton L., McPherson J.,
Matsuda F., Wilson R., Scarpelli C., Gyapay G., Wincker P., Saurin W.,
Quetier F., Waterston R., Hood L., Weissenbach J.;
"The DNA sequence and analysis of human chromosome 14.";
Nature 421:601-607(2003).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2), AND VARIANT
TRP-157.
TISSUE=Brain;
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).
[5]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21269460; DOI=10.1186/1752-0509-5-17;
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
"Initial characterization of the human central proteome.";
BMC Syst. Biol. 5:17-17(2011).
[6]
INTERACTION WITH PRKN.
PubMed=24270810; DOI=10.1038/nature12748;
Hasson S.A., Kane L.A., Yamano K., Huang C.H., Sliter D.A.,
Buehler E., Wang C., Heman-Ackah S.M., Hessa T., Guha R., Martin S.E.,
Youle R.J.;
"High-content genome-wide RNAi screens identify regulators of parkin
upstream of mitophagy.";
Nature 504:291-295(2013).
[7]
STRUCTURE BY NMR OF 275-350, X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF
341-447 IN COMPLEX WITH HSPA1, DOMAIN BAG, FUNCTION, AND SUBUNIT.
PubMed=20223214; DOI=10.1016/j.str.2010.01.004;
Arakawa A., Handa N., Ohsawa N., Shida M., Kigawa T., Hayashi F.,
Shirouzu M., Yokoyama S.;
"The C-terminal BAG domain of BAG5 induces conformational changes of
the Hsp70 nucleotide-binding domain for ADP-ATP exchange.";
Structure 18:309-319(2010).
-!- FUNCTION: Inhibits both auto-ubiquitination of PRKN and
ubiquitination of target proteins by PRKN (By similarity). May
function as a nucleotide exchange factor for HSP/HSP70, promoting
ADP release, and activating Hsp70-mediated refolding.
{ECO:0000250, ECO:0000269|PubMed:20223214}.
-!- SUBUNIT: Binds to the ATPase domain of HSP/HSC70 chaperones. Binds
PRKN. {ECO:0000269|PubMed:20223214}.
-!- INTERACTION:
Q53FC7:-; NbExp=2; IntAct=EBI-356517, EBI-9356749;
Q8N9N5:BANP; NbExp=3; IntAct=EBI-356517, EBI-744695;
Q8N6L0:CCDC155; NbExp=5; IntAct=EBI-356517, EBI-749265;
Q9BPY3:FAM118B; NbExp=3; IntAct=EBI-356517, EBI-726822;
Q9NYA3:GOLGA6A; NbExp=4; IntAct=EBI-356517, EBI-11163335;
P0DMV8:HSPA1A; NbExp=3; IntAct=EBI-16247256, EBI-11820565;
P08107:HSPA1B; NbExp=6; IntAct=EBI-356517, EBI-629985;
Q38SD2:LRRK1; NbExp=3; IntAct=EBI-356517, EBI-1050422;
Q5S007:LRRK2; NbExp=12; IntAct=EBI-356517, EBI-5323863;
Q9Y6D9:MAD1L1; NbExp=6; IntAct=EBI-356517, EBI-742610;
Q9NVV9:THAP1; NbExp=7; IntAct=EBI-356517, EBI-741515;
P14373:TRIM27; NbExp=5; IntAct=EBI-356517, EBI-719493;
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1;
IsoId=Q9UL15-1; Sequence=Displayed;
Name=2;
IsoId=Q9UL15-2; Sequence=VSP_037996;
Note=No experimental confirmation available.;
-!- DOMAIN: The fifth BAG domain is responsible for the interaction
with HSP70 nucleotide-binding domain.
{ECO:0000269|PubMed:20223214}.
-!- SEQUENCE CAUTION:
Sequence=BAA74896.1; Type=Erroneous initiation; Evidence={ECO:0000305};
-----------------------------------------------------------------------
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EMBL; AF095195; AAD16124.2; -; mRNA.
EMBL; AB020680; BAA74896.1; ALT_INIT; mRNA.
EMBL; AL139300; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; BC044216; AAH44216.2; -; mRNA.
EMBL; BC050551; AAH50551.1; -; mRNA.
CCDS; CCDS41995.1; -. [Q9UL15-2]
CCDS; CCDS9982.1; -. [Q9UL15-1]
RefSeq; NP_001015048.1; NM_001015048.2. [Q9UL15-1]
RefSeq; NP_001015049.1; NM_001015049.2. [Q9UL15-2]
RefSeq; NP_004864.1; NM_004873.3. [Q9UL15-1]
UniGene; Hs.5443; -.
PDB; 2D9D; NMR; -; A=275-350.
PDB; 3A8Y; X-ray; 2.30 A; C/D=341-447.
PDBsum; 2D9D; -.
PDBsum; 3A8Y; -.
ProteinModelPortal; Q9UL15; -.
SMR; Q9UL15; -.
BioGrid; 114905; 46.
CORUM; Q9UL15; -.
DIP; DIP-53428N; -.
IntAct; Q9UL15; 54.
MINT; Q9UL15; -.
STRING; 9606.ENSP00000338814; -.
iPTMnet; Q9UL15; -.
PhosphoSitePlus; Q9UL15; -.
BioMuta; BAG5; -.
DMDM; 12643895; -.
EPD; Q9UL15; -.
PaxDb; Q9UL15; -.
PeptideAtlas; Q9UL15; -.
PRIDE; Q9UL15; -.
Ensembl; ENST00000299204; ENSP00000299204; ENSG00000166170. [Q9UL15-1]
Ensembl; ENST00000337322; ENSP00000338814; ENSG00000166170. [Q9UL15-2]
Ensembl; ENST00000445922; ENSP00000391713; ENSG00000166170. [Q9UL15-1]
GeneID; 9529; -.
KEGG; hsa:9529; -.
UCSC; uc001ynh.3; human. [Q9UL15-1]
CTD; 9529; -.
DisGeNET; 9529; -.
EuPathDB; HostDB:ENSG00000166170.9; -.
GeneCards; BAG5; -.
HGNC; HGNC:941; BAG5.
HPA; HPA016429; -.
MIM; 603885; gene.
neXtProt; NX_Q9UL15; -.
OpenTargets; ENSG00000166170; -.
PharmGKB; PA25241; -.
eggNOG; KOG4361; Eukaryota.
eggNOG; ENOG4111WNH; LUCA.
GeneTree; ENSGT00530000063256; -.
HOGENOM; HOG000070447; -.
HOVERGEN; HBG004810; -.
InParanoid; Q9UL15; -.
KO; K09559; -.
OMA; RTEIRNY; -.
OrthoDB; EOG091G08LY; -.
PhylomeDB; Q9UL15; -.
TreeFam; TF102014; -.
Reactome; R-HSA-3371453; Regulation of HSF1-mediated heat shock response.
EvolutionaryTrace; Q9UL15; -.
GeneWiki; BAG5; -.
GenomeRNAi; 9529; -.
PRO; PR:Q9UL15; -.
Proteomes; UP000005640; Chromosome 14.
Bgee; ENSG00000166170; -.
CleanEx; HS_BAG5; -.
ExpressionAtlas; Q9UL15; baseline and differential.
Genevisible; Q9UL15; HS.
GO; GO:0005829; C:cytosol; IDA:ParkinsonsUK-UCL.
GO; GO:0016234; C:inclusion body; IDA:BHF-UCL.
GO; GO:0016020; C:membrane; HDA:UniProtKB.
GO; GO:0005739; C:mitochondrion; IDA:ParkinsonsUK-UCL.
GO; GO:0005634; C:nucleus; IDA:ParkinsonsUK-UCL.
GO; GO:0048471; C:perinuclear region of cytoplasm; IDA:BHF-UCL.
GO; GO:0000774; F:adenyl-nucleotide exchange factor activity; TAS:Reactome.
GO; GO:0051087; F:chaperone binding; IPI:BHF-UCL.
GO; GO:0019901; F:protein kinase binding; IPI:ParkinsonsUK-UCL.
GO; GO:0031625; F:ubiquitin protein ligase binding; IPI:ParkinsonsUK-UCL.
GO; GO:0007030; P:Golgi organization; IMP:ParkinsonsUK-UCL.
GO; GO:0010977; P:negative regulation of neuron projection development; IDA:ParkinsonsUK-UCL.
GO; GO:1902176; P:negative regulation of oxidative stress-induced intrinsic apoptotic signaling pathway; IDA:ParkinsonsUK-UCL.
GO; GO:0032435; P:negative regulation of proteasomal ubiquitin-dependent protein catabolic process; IDA:ParkinsonsUK-UCL.
GO; GO:0061084; P:negative regulation of protein refolding; ISS:BHF-UCL.
GO; GO:0031397; P:negative regulation of protein ubiquitination; IMP:ParkinsonsUK-UCL.
GO; GO:0051444; P:negative regulation of ubiquitin-protein transferase activity; ISS:BHF-UCL.
GO; GO:0070997; P:neuron death; ISS:BHF-UCL.
GO; GO:0006457; P:protein folding; TAS:ProtInc.
GO; GO:1900034; P:regulation of cellular response to heat; TAS:Reactome.
GO; GO:0090083; P:regulation of inclusion body assembly; IMP:BHF-UCL.
GO; GO:0051438; P:regulation of ubiquitin-protein transferase activity; TAS:ParkinsonsUK-UCL.
Gene3D; 1.20.58.120; -; 5.
InterPro; IPR036533; BAG_dom_sf.
InterPro; IPR003103; BAG_domain.
Pfam; PF02179; BAG; 4.
SMART; SM00264; BAG; 4.
SUPFAM; SSF63491; SSF63491; 4.
PROSITE; PS51035; BAG; 4.
1: Evidence at protein level;
3D-structure; Alternative splicing; Chaperone; Complete proteome;
Polymorphism; Reference proteome; Repeat.
CHAIN 1 447 BAG family molecular chaperone regulator
5.
/FTId=PRO_0000088872.
DOMAIN 9 86 BAG 1. {ECO:0000255|PROSITE-
ProRule:PRU00369}.
DOMAIN 95 167 BAG 2. {ECO:0000255|PROSITE-
ProRule:PRU00369}.
DOMAIN 182 260 BAG 3. {ECO:0000255|PROSITE-
ProRule:PRU00369}.
DOMAIN 275 350 BAG 4. {ECO:0000255|PROSITE-
ProRule:PRU00369}.
DOMAIN 365 442 BAG 5. {ECO:0000255|PROSITE-
ProRule:PRU00369}.
VAR_SEQ 1 1 M -> MRFHWLPTLSEPFDRNQELETCIRPLWTPSGSACET
EHNKSM (in isoform 2).
{ECO:0000303|PubMed:15489334}.
/FTId=VSP_037996.
VARIANT 157 157 C -> W (in dbSNP:rs17854644).
{ECO:0000269|PubMed:15489334}.
/FTId=VAR_058712.
HELIX 277 295 {ECO:0000244|PDB:2D9D}.
TURN 299 301 {ECO:0000244|PDB:2D9D}.
HELIX 302 317 {ECO:0000244|PDB:2D9D}.
HELIX 318 320 {ECO:0000244|PDB:2D9D}.
HELIX 326 350 {ECO:0000244|PDB:2D9D}.
TURN 356 358 {ECO:0000244|PDB:3A8Y}.
HELIX 364 384 {ECO:0000244|PDB:3A8Y}.
HELIX 393 410 {ECO:0000244|PDB:3A8Y}.
HELIX 418 442 {ECO:0000244|PDB:3A8Y}.
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


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