ID   BAG5_HUMAN              Reviewed;         447 AA.
AC   Q9UL15; O94950; Q86W59;
DT   11-JAN-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2000, sequence version 1.
DT   25-JAN-2012, entry version 95.
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   MEDLINE=99091615; 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   MEDLINE=99156230; 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   MEDLINE=22459283; 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   ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-278, AND MASS SPECTROMETRY.
RX   PubMed=19608861; DOI=10.1126/science.1175371;
RA   Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.,
RA   Olsen J.V., Mann M.;
RT   "Lysine acetylation targets protein complexes and co-regulates major
RT   cellular functions.";
RL   Science 325:834-840(2009).
RN   [6]
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   [7]
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;
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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   IPI; IPI00007731; -.
DR   IPI; IPI00556027; -.
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, 178-259, 276-447.
DR   DIP; DIP-53428N; -.
DR   IntAct; Q9UL15; 5.
DR   MINT; MINT-1147557; -.
DR   STRING; Q9UL15; -.
DR   PhosphoSite; Q9UL15; -.
DR   DMDM; 12643895; -.
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; uc001ynh.1; human.
DR   CTD; 9529; -.
DR   GeneCards; GC14M104022; -.
DR   H-InvDB; HIX0012003; -.
DR   HGNC; HGNC:941; BAG5.
DR   HPA; HPA016429; -.
DR   MIM; 603885; gene.
DR   neXtProt; NX_Q9UL15; -.
DR   PharmGKB; PA25241; -.
DR   eggNOG; prNOG13028; -.
DR   GeneTree; ENSGT00530000063256; -.
DR   HOGENOM; HBG713028; -.
DR   HOVERGEN; HBG004810; -.
DR   InParanoid; Q9UL15; -.
DR   OMA; YIRLEEL; -.
DR   OrthoDB; EOG46T31D; -.
DR   PhylomeDB; Q9UL15; -.
DR   NextBio; 35720; -.
DR   ArrayExpress; Q9UL15; -.
DR   Bgee; Q9UL15; -.
DR   CleanEx; HS_BAG5; -.
DR   Genevestigator; Q9UL15; -.
DR   GermOnline; ENSG00000166170; Homo sapiens.
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:0051087; F:chaperone binding; IPI: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   KO; K09559; -.
DR   Pfam; PF02179; BAG; 4.
DR   SMART; SM00264; BAG; 4.
DR   PROSITE; PS51035; BAG; 4.
PE   1: Evidence at protein level;
KW   3D-structure; Acetylation; Alternative splicing; Chaperone;
KW   Complete proteome; 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   MOD_RES     278    278       N6-acetyllysine.
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    310
FT   HELIX       317    320
FT   HELIX       326    350
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
//