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BAG family molecular chaperone regulator 4 (BAG-4) (Bcl-2-associated athanogene 4) (Silencer of death domains)

 BAG4_HUMAN              Reviewed;         457 AA.
O95429; B4E217; O95818;
11-JAN-2001, integrated into UniProtKB/Swiss-Prot.
01-MAY-1999, sequence version 1.
18-JUL-2018, entry version 161.
RecName: Full=BAG family molecular chaperone regulator 4;
Short=BAG-4;
AltName: Full=Bcl-2-associated athanogene 4;
AltName: Full=Silencer of death domains;
Name=BAG4; Synonyms=SODD;
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).
TISSUE=Leukemic T-cell;
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 [MRNA] (ISOFORM 1), AND INTERACTION WITH TNFRSF1A
AND TNFRSF12.
TISSUE=Leukemic T-cell;
PubMed=9915703; DOI=10.1126/science.283.5401.543;
Jiang Y., Woronicz J.D., Liu W., Goeddel D.V.;
"Prevention of constitutive TNF receptor 1 signaling by silencer of
death domains.";
Science 283:543-546(1999).
[3]
ERRATUM.
Jiang Y., Woronicz J.D., Liu W., Goeddel D.V.;
Science 283:1852-1852(1999).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
TISSUE=Trachea;
PubMed=14702039; DOI=10.1038/ng1285;
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=16421571; DOI=10.1038/nature04406;
Nusbaum C., Mikkelsen T.S., Zody M.C., Asakawa S., Taudien S.,
Garber M., Kodira C.D., Schueler M.G., Shimizu A., Whittaker C.A.,
Chang J.L., Cuomo C.A., Dewar K., FitzGerald M.G., Yang X.,
Allen N.R., Anderson S., Asakawa T., Blechschmidt K., Bloom T.,
Borowsky M.L., Butler J., Cook A., Corum B., DeArellano K.,
DeCaprio D., Dooley K.T., Dorris L. III, Engels R., Gloeckner G.,
Hafez N., Hagopian D.S., Hall J.L., Ishikawa S.K., Jaffe D.B.,
Kamat A., Kudoh J., Lehmann R., Lokitsang T., Macdonald P.,
Major J.E., Matthews C.D., Mauceli E., Menzel U., Mihalev A.H.,
Minoshima S., Murayama Y., Naylor J.W., Nicol R., Nguyen C.,
O'Leary S.B., O'Neill K., Parker S.C.J., Polley A., Raymond C.K.,
Reichwald K., Rodriguez J., Sasaki T., Schilhabel M., Siddiqui R.,
Smith C.L., Sneddon T.P., Talamas J.A., Tenzin P., Topham K.,
Venkataraman V., Wen G., Yamazaki S., Young S.K., Zeng Q.,
Zimmer A.R., Rosenthal A., Birren B.W., Platzer M., Shimizu N.,
Lander E.S.;
"DNA sequence and analysis of human chromosome 8.";
Nature 439:331-335(2006).
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
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).
[7]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-7, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma, and Erythroleukemia;
PubMed=23186163; DOI=10.1021/pr300630k;
Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
Mohammed S.;
"Toward a comprehensive characterization of a human cancer cell
phosphoproteome.";
J. Proteome Res. 12:260-271(2013).
[8]
FUNCTION, AND 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).
[9]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D.,
Wang L., Ye M., Zou H.;
"An enzyme assisted RP-RPLC approach for in-depth analysis of human
liver phosphoproteome.";
J. Proteomics 96:253-262(2014).
[10]
METHYLATION [LARGE SCALE ANALYSIS] AT ARG-40; ARG-53; ARG-108 AND
ARG-185, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
ANALYSIS].
TISSUE=Colon carcinoma;
PubMed=24129315; DOI=10.1074/mcp.O113.027870;
Guo A., Gu H., Zhou J., Mulhern D., Wang Y., Lee K.A., Yang V.,
Aguiar M., Kornhauser J., Jia X., Ren J., Beausoleil S.A., Silva J.C.,
Vemulapalli V., Bedford M.T., Comb M.J.;
"Immunoaffinity enrichment and mass spectrometry analysis of protein
methylation.";
Mol. Cell. Proteomics 13:372-387(2014).
[11]
STRUCTURE BY NMR OF 376-457, INTERACTION WITH HSP70, AND MUTAGENESIS
OF GLU-414; ASP-424; 438-ARG-LYS-439 AND GLN-446.
PubMed=12058034; DOI=10.1074/jbc.M202792200;
Briknarova K., Takayama S., Homma S., Baker K., Cabezas E., Hoyt D.W.,
Li Z., Satterthwait A.C., Ely K.R.;
"BAG4/SODD protein contains a short BAG domain.";
J. Biol. Chem. 277:31172-31178(2002).
-!- FUNCTION: Inhibits the chaperone activity of HSP70/HSC70 by
promoting substrate release (By similarity). Prevents constitutive
TNFRSF1A signaling. Negative regulator of PRKN translocation to
damaged mitochondria. {ECO:0000250, ECO:0000269|PubMed:24270810}.
-!- SUBUNIT: Binds to the ATPase domain of HSP/HSC70 chaperones. Binds
to the death domain of TNFRSF1A in the absence of TNF and thereby
prevents binding of adapter molecules such as TRADD or TRAF2.
Binds to the death domain of TNFRSF12. Interacts with PRKN.
{ECO:0000269|PubMed:12058034, ECO:0000269|PubMed:24270810,
ECO:0000269|PubMed:9915703}.
-!- INTERACTION:
Q53FC7:-; NbExp=2; IntAct=EBI-2949658, EBI-9356749;
Q9NPI6:DCP1A; NbExp=4; IntAct=EBI-2949658, EBI-374238;
Q99615:DNAJC7; NbExp=2; IntAct=EBI-2949658, EBI-357552;
P34931:HSPA1L; NbExp=3; IntAct=EBI-2949658, EBI-354912;
P54652:HSPA2; NbExp=4; IntAct=EBI-2949658, EBI-356991;
P11142:HSPA8; NbExp=3; IntAct=EBI-2949658, EBI-351896;
Q7Z5V6-2:PPP1R32; NbExp=4; IntAct=EBI-2949658, EBI-12000762;
Q9P0N9:TBC1D7; NbExp=4; IntAct=EBI-2949658, EBI-3258000;
Q99816:TSG101; NbExp=4; IntAct=EBI-2949658, EBI-346882;
-!- SUBCELLULAR LOCATION: Cytoplasm.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1;
IsoId=O95429-1; Sequence=Displayed;
Name=2;
IsoId=O95429-2; Sequence=VSP_042741;
Note=No experimental confirmation available.;
-!- TISSUE SPECIFICITY: Ubiquitous.
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EMBL; AF095194; AAD16123.2; -; mRNA.
EMBL; AF111116; AAD05226.1; -; mRNA.
EMBL; AK304072; BAG64979.1; -; mRNA.
EMBL; AC084024; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; BC038505; AAH38505.2; -; mRNA.
CCDS; CCDS56533.1; -. [O95429-2]
CCDS; CCDS6104.1; -. [O95429-1]
RefSeq; NP_001191807.1; NM_001204878.1. [O95429-2]
RefSeq; NP_004865.1; NM_004874.3. [O95429-1]
UniGene; Hs.194726; -.
PDB; 1M62; NMR; -; A=376-457.
PDB; 1M7K; NMR; -; A=358-456.
PDBsum; 1M62; -.
PDBsum; 1M7K; -.
ProteinModelPortal; O95429; -.
SMR; O95429; -.
BioGrid; 114906; 89.
IntAct; O95429; 137.
MINT; O95429; -.
STRING; 9606.ENSP00000287322; -.
iPTMnet; O95429; -.
PhosphoSitePlus; O95429; -.
BioMuta; BAG4; -.
EPD; O95429; -.
MaxQB; O95429; -.
PaxDb; O95429; -.
PeptideAtlas; O95429; -.
PRIDE; O95429; -.
ProteomicsDB; 50875; -.
ProteomicsDB; 50876; -. [O95429-2]
DNASU; 9530; -.
Ensembl; ENST00000287322; ENSP00000287322; ENSG00000156735. [O95429-1]
Ensembl; ENST00000432471; ENSP00000393298; ENSG00000156735. [O95429-2]
GeneID; 9530; -.
KEGG; hsa:9530; -.
UCSC; uc003xky.3; human. [O95429-1]
CTD; 9530; -.
DisGeNET; 9530; -.
EuPathDB; HostDB:ENSG00000156735.10; -.
GeneCards; BAG4; -.
HGNC; HGNC:940; BAG4.
HPA; CAB013716; -.
HPA; HPA018951; -.
MIM; 603884; gene.
neXtProt; NX_O95429; -.
OpenTargets; ENSG00000156735; -.
PharmGKB; PA25240; -.
eggNOG; KOG4361; Eukaryota.
eggNOG; ENOG4111WNH; LUCA.
GeneTree; ENSGT00530000063256; -.
HOGENOM; HOG000290673; -.
HOVERGEN; HBG004809; -.
InParanoid; O95429; -.
KO; K09558; -.
OMA; PAETTWP; -.
OrthoDB; EOG091G08LY; -.
PhylomeDB; O95429; -.
TreeFam; TF102013; -.
Reactome; R-HSA-3371453; Regulation of HSF1-mediated heat shock response.
Reactome; R-HSA-5655302; Signaling by FGFR1 in disease.
Reactome; R-HSA-75893; TNF signaling.
Reactome; R-HSA-8853336; Signaling by plasma membrane FGFR1 fusions.
SIGNOR; O95429; -.
ChiTaRS; BAG4; human.
EvolutionaryTrace; O95429; -.
GeneWiki; BAG4; -.
GenomeRNAi; 9530; -.
PRO; PR:O95429; -.
Proteomes; UP000005640; Chromosome 8.
Bgee; ENSG00000156735; -.
CleanEx; HS_BAG4; -.
ExpressionAtlas; O95429; baseline and differential.
Genevisible; O95429; HS.
GO; GO:0005829; C:cytosol; IDA:UniProtKB.
GO; GO:0005634; C:nucleus; IDA:UniProtKB.
GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
GO; GO:0000774; F:adenyl-nucleotide exchange factor activity; TAS:Reactome.
GO; GO:0051087; F:chaperone binding; IEA:InterPro.
GO; GO:0003723; F:RNA binding; HDA:UniProtKB.
GO; GO:0031625; F:ubiquitin protein ligase binding; IPI:ParkinsonsUK-UCL.
GO; GO:0071364; P:cellular response to epidermal growth factor stimulus; IEA:Ensembl.
GO; GO:0071356; P:cellular response to tumor necrosis factor; IDA:UniProtKB.
GO; GO:0043066; P:negative regulation of apoptotic process; TAS:ProtInc.
GO; GO:2001145; P:negative regulation of phosphatidylinositol-3,4,5-trisphosphate 5-phosphatase activity; IEA:Ensembl.
GO; GO:1903215; P:negative regulation of protein targeting to mitochondrion; IMP:ParkinsonsUK-UCL.
GO; GO:0030838; P:positive regulation of actin filament polymerization; IEA:Ensembl.
GO; GO:0045785; P:positive regulation of cell adhesion; IEA:Ensembl.
GO; GO:0010763; P:positive regulation of fibroblast migration; IEA:Ensembl.
GO; GO:0033138; P:positive regulation of peptidyl-serine phosphorylation; IEA:Ensembl.
GO; GO:0051897; P:positive regulation of protein kinase B signaling; IEA:Ensembl.
GO; GO:0051496; P:positive regulation of stress fiber assembly; IEA:Ensembl.
GO; GO:0006457; P:protein folding; TAS:ProtInc.
GO; GO:0072659; P:protein localization to plasma membrane; IEA:Ensembl.
GO; GO:1900034; P:regulation of cellular response to heat; TAS:Reactome.
GO; GO:0097178; P:ruffle assembly; IEA:Ensembl.
GO; GO:0033209; P:tumor necrosis factor-mediated signaling pathway; TAS:Reactome.
Gene3D; 1.20.58.120; -; 1.
InterPro; IPR036533; BAG_dom_sf.
InterPro; IPR003103; BAG_domain.
Pfam; PF02179; BAG; 1.
SMART; SM00264; BAG; 1.
SUPFAM; SSF63491; SSF63491; 1.
PROSITE; PS51035; BAG; 1.
1: Evidence at protein level;
3D-structure; Alternative splicing; Chaperone; Complete proteome;
Cytoplasm; Methylation; Phosphoprotein; Reference proteome.
CHAIN 1 457 BAG family molecular chaperone regulator
4.
/FTId=PRO_0000088870.
DOMAIN 379 456 BAG. {ECO:0000255|PROSITE-
ProRule:PRU00369}.
MOD_RES 7 7 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 40 40 Omega-N-methylarginine.
{ECO:0000244|PubMed:24129315}.
MOD_RES 53 53 Omega-N-methylarginine.
{ECO:0000244|PubMed:24129315}.
MOD_RES 108 108 Omega-N-methylarginine.
{ECO:0000244|PubMed:24129315}.
MOD_RES 185 185 Omega-N-methylarginine.
{ECO:0000244|PubMed:24129315}.
VAR_SEQ 90 125 Missing (in isoform 2).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_042741.
MUTAGEN 414 414 E->A: Reduces interaction with HSP70.
{ECO:0000269|PubMed:12058034}.
MUTAGEN 424 424 D->A: Abolishes interaction with HSP70.
{ECO:0000269|PubMed:12058034}.
MUTAGEN 438 439 RK->AA: Reduces interaction with HSP70.
{ECO:0000269|PubMed:12058034}.
MUTAGEN 446 446 Q->A: Abolishes interaction with HSP70.
{ECO:0000269|PubMed:12058034}.
HELIX 380 399 {ECO:0000244|PDB:1M62}.
HELIX 407 423 {ECO:0000244|PDB:1M62}.
HELIX 432 456 {ECO:0000244|PDB:1M62}.
SEQUENCE 457 AA; 49594 MW; B89D59E8118684A3 CRC64;
MSALRRSGYG PSDGPSYGRY YGPGGGDVPV HPPPPLYPLR PEPPQPPISW RVRGGGPAET
TWLGEGGGGD GYYPSGGAWP EPGRAGGSHQ EQPPYPSYNS NYWNSTARSR APYPSTYPVR
PELQGQSLNS YTNGAYGPTY PPGPGANTAS YSGAYYAPGY TQTSYSTEVP STYRSSGNSP
TPVSRWIYPQ QDCQTEAPPL RGQVPGYPPS QNPGMTLPHY PYGDGNRSVP QSGPTVRPQE
DAWASPGAYG MGGRYPWPSS APSAPPGNLY MTESTSPWPS SGSPQSPPSP PVQQPKDSSY
PYSQSDQSMN RHNFPCSVHQ YESSGTVNND DSDLLDSQVQ YSAEPQLYGN ATSDHPNNQD
QSSSLPEECV PSDESTPPSI KKIIHVLEKV QYLEQEVEEF VGKKTDKAYW LLEEMLTKEL
LELDSVETGG QDSVRQARKE AVCKIQAILE KLEKKGL


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