BAG4_HUMAN
ID BAG4_HUMAN Reviewed; 457 AA.
AC O95429; B4E217; O95818;
DT 11-JAN-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1999, sequence version 1.
DT 03-AUG-2022, entry version 185.
DE RecName: Full=BAG family molecular chaperone regulator 4;
DE Short=BAG-4;
DE AltName: Full=Bcl-2-associated athanogene 4;
DE AltName: Full=Silencer of death domains;
GN Name=BAG4; Synonyms=SODD;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC TISSUE=Leukemic T-cell;
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 [MRNA] (ISOFORM 1), AND INTERACTION WITH TNFRSF1A AND
RP TNFRSF12.
RC TISSUE=Leukemic T-cell;
RX PubMed=9915703; DOI=10.1126/science.283.5401.543;
RA Jiang Y., Woronicz J.D., Liu W., Goeddel D.V.;
RT "Prevention of constitutive TNF receptor 1 signaling by silencer of death
RT domains.";
RL Science 283:543-546(1999).
RN [3]
RP ERRATUM OF PUBMED:9915703.
RA Jiang Y., Woronicz J.D., Liu W., Goeddel D.V.;
RL Science 283:1852-1852(1999).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Trachea;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16421571; DOI=10.1038/nature04406;
RA Nusbaum C., Mikkelsen T.S., Zody M.C., Asakawa S., Taudien S., Garber M.,
RA Kodira C.D., Schueler M.G., Shimizu A., Whittaker C.A., Chang J.L.,
RA Cuomo C.A., Dewar K., FitzGerald M.G., Yang X., Allen N.R., Anderson S.,
RA Asakawa T., Blechschmidt K., Bloom T., Borowsky M.L., Butler J., Cook A.,
RA Corum B., DeArellano K., DeCaprio D., Dooley K.T., Dorris L. III,
RA Engels R., Gloeckner G., Hafez N., Hagopian D.S., Hall J.L., Ishikawa S.K.,
RA Jaffe D.B., Kamat A., Kudoh J., Lehmann R., Lokitsang T., Macdonald P.,
RA Major J.E., Matthews C.D., Mauceli E., Menzel U., Mihalev A.H.,
RA Minoshima S., Murayama Y., Naylor J.W., Nicol R., Nguyen C., O'Leary S.B.,
RA O'Neill K., Parker S.C.J., Polley A., Raymond C.K., Reichwald K.,
RA Rodriguez J., Sasaki T., Schilhabel M., Siddiqui R., Smith C.L.,
RA Sneddon T.P., Talamas J.A., Tenzin P., Topham K., Venkataraman V., Wen G.,
RA Yamazaki S., Young S.K., Zeng Q., Zimmer A.R., Rosenthal A., Birren B.W.,
RA Platzer M., Shimizu N., Lander E.S.;
RT "DNA sequence and analysis of human chromosome 8.";
RL Nature 439:331-335(2006).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
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 project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-7, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma, and Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [8]
RP FUNCTION, AND INTERACTION WITH PRKN.
RX PubMed=24270810; DOI=10.1038/nature12748;
RA Hasson S.A., Kane L.A., Yamano K., Huang C.H., Sliter D.A., Buehler E.,
RA Wang C., Heman-Ackah S.M., Hessa T., Guha R., Martin S.E., Youle R.J.;
RT "High-content genome-wide RNAi screens identify regulators of parkin
RT upstream of mitophagy.";
RL Nature 504:291-295(2013).
RN [9]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [10]
RP METHYLATION [LARGE SCALE ANALYSIS] AT ARG-40; ARG-53; ARG-108 AND ARG-185,
RP AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Colon carcinoma;
RX PubMed=24129315; DOI=10.1074/mcp.o113.027870;
RA Guo A., Gu H., Zhou J., Mulhern D., Wang Y., Lee K.A., Yang V., Aguiar M.,
RA Kornhauser J., Jia X., Ren J., Beausoleil S.A., Silva J.C., Vemulapalli V.,
RA Bedford M.T., Comb M.J.;
RT "Immunoaffinity enrichment and mass spectrometry analysis of protein
RT methylation.";
RL Mol. Cell. Proteomics 13:372-387(2014).
RN [11]
RP STRUCTURE BY NMR OF 376-457, INTERACTION WITH HSP70, AND MUTAGENESIS OF
RP GLU-414; ASP-424; 438-ARG-LYS-439 AND GLN-446.
RX PubMed=12058034; DOI=10.1074/jbc.m202792200;
RA Briknarova K., Takayama S., Homma S., Baker K., Cabezas E., Hoyt D.W.,
RA Li Z., Satterthwait A.C., Ely K.R.;
RT "BAG4/SODD protein contains a short BAG domain.";
RL J. Biol. Chem. 277:31172-31178(2002).
CC -!- FUNCTION: Inhibits the chaperone activity of HSP70/HSC70 by promoting
CC substrate release (By similarity). Prevents constitutive TNFRSF1A
CC signaling. Negative regulator of PRKN translocation to damaged
CC mitochondria. {ECO:0000250, ECO:0000269|PubMed:24270810}.
CC -!- SUBUNIT: Binds to the ATPase domain of HSP/HSC70 chaperones. Binds to
CC the death domain of TNFRSF1A in the absence of TNF and thereby prevents
CC binding of adapter molecules such as TRADD or TRAF2. Binds to the death
CC domain of TNFRSF12. Interacts with PRKN. {ECO:0000269|PubMed:12058034,
CC ECO:0000269|PubMed:24270810, ECO:0000269|PubMed:9915703}.
CC -!- INTERACTION:
CC O95429; Q9NYB9-2: ABI2; NbExp=5; IntAct=EBI-2949658, EBI-11096309;
CC O95429; O00154-4: ACOT7; NbExp=3; IntAct=EBI-2949658, EBI-12007918;
CC O95429; Q6UY14-3: ADAMTSL4; NbExp=3; IntAct=EBI-2949658, EBI-10173507;
CC O95429; Q9NP73-4: ALG13; NbExp=3; IntAct=EBI-2949658, EBI-10186621;
CC O95429; Q03989: ARID5A; NbExp=3; IntAct=EBI-2949658, EBI-948603;
CC O95429; Q9Y6H3: ATP23; NbExp=3; IntAct=EBI-2949658, EBI-12811889;
CC O95429; A8KA13: BCL6B; NbExp=3; IntAct=EBI-2949658, EBI-10174813;
CC O95429; Q9H2G9: BLZF1; NbExp=3; IntAct=EBI-2949658, EBI-2548012;
CC O95429; Q5JPI3-2: C3orf38; NbExp=4; IntAct=EBI-2949658, EBI-12009184;
CC O95429; P42575: CASP2; NbExp=3; IntAct=EBI-2949658, EBI-520342;
CC O95429; O43439-4: CBFA2T2; NbExp=3; IntAct=EBI-2949658, EBI-11954144;
CC O95429; Q9NPI6: DCP1A; NbExp=5; IntAct=EBI-2949658, EBI-374238;
CC O95429; Q8IZD4: DCP1B; NbExp=2; IntAct=EBI-2949658, EBI-521595;
CC O95429; Q96D03: DDIT4L; NbExp=3; IntAct=EBI-2949658, EBI-742054;
CC O95429; Q99615: DNAJC7; NbExp=2; IntAct=EBI-2949658, EBI-357552;
CC O95429; Q86Y13: DZIP3; NbExp=3; IntAct=EBI-2949658, EBI-948630;
CC O95429; Q12805: EFEMP1; NbExp=3; IntAct=EBI-2949658, EBI-536772;
CC O95429; Q96A10: ERVK3-1; NbExp=3; IntAct=EBI-2949658, EBI-10486892;
CC O95429; Q7L5A3: FAM214B; NbExp=5; IntAct=EBI-2949658, EBI-745689;
CC O95429; Q8WU58: FAM222B; NbExp=3; IntAct=EBI-2949658, EBI-2807642;
CC O95429; O95363: FARS2; NbExp=3; IntAct=EBI-2949658, EBI-2513774;
CC O95429; P02794: FTH1; NbExp=4; IntAct=EBI-2949658, EBI-713259;
CC O95429; P06241-3: FYN; NbExp=3; IntAct=EBI-2949658, EBI-10691738;
CC O95429; O95872: GPANK1; NbExp=3; IntAct=EBI-2949658, EBI-751540;
CC O95429; Q13227: GPS2; NbExp=3; IntAct=EBI-2949658, EBI-713355;
CC O95429; P49639: HOXA1; NbExp=3; IntAct=EBI-2949658, EBI-740785;
CC O95429; P34931: HSPA1L; NbExp=4; IntAct=EBI-2949658, EBI-354912;
CC O95429; P54652: HSPA2; NbExp=5; IntAct=EBI-2949658, EBI-356991;
CC O95429; P17066: HSPA6; NbExp=3; IntAct=EBI-2949658, EBI-355106;
CC O95429; P11142: HSPA8; NbExp=6; IntAct=EBI-2949658, EBI-351896;
CC O95429; P53990-3: IST1; NbExp=3; IntAct=EBI-2949658, EBI-12188567;
CC O95429; Q8NC69: KCTD6; NbExp=3; IntAct=EBI-2949658, EBI-2511344;
CC O95429; Q96MP8-2: KCTD7; NbExp=3; IntAct=EBI-2949658, EBI-11954971;
CC O95429; P33176: KIF5B; NbExp=3; IntAct=EBI-2949658, EBI-355878;
CC O95429; Q3LI77: KRTAP13-4; NbExp=3; IntAct=EBI-2949658, EBI-11953996;
CC O95429; Q9BQ66: KRTAP4-12; NbExp=3; IntAct=EBI-2949658, EBI-739863;
CC O95429; Q9BYR5: KRTAP4-2; NbExp=3; IntAct=EBI-2949658, EBI-10172511;
CC O95429; Q9BYR3: KRTAP4-4; NbExp=3; IntAct=EBI-2949658, EBI-11958132;
CC O95429; Q9BYR2: KRTAP4-5; NbExp=3; IntAct=EBI-2949658, EBI-11993254;
CC O95429; Q14847-2: LASP1; NbExp=3; IntAct=EBI-2949658, EBI-9088686;
CC O95429; Q9Y5V3: MAGED1; NbExp=3; IntAct=EBI-2949658, EBI-716006;
CC O95429; A8MW99: MEI4; NbExp=3; IntAct=EBI-2949658, EBI-19944212;
CC O95429; Q9NP98: MYOZ1; NbExp=3; IntAct=EBI-2949658, EBI-744402;
CC O95429; Q8TDC0: MYOZ3; NbExp=3; IntAct=EBI-2949658, EBI-5662487;
CC O95429; Q86VE0: MYPOP; NbExp=3; IntAct=EBI-2949658, EBI-2858213;
CC O95429; Q14990: ODF1; NbExp=3; IntAct=EBI-2949658, EBI-10234557;
CC O95429; Q8IXM7: ODF3L1; NbExp=3; IntAct=EBI-2949658, EBI-13331299;
CC O95429; Q7Z4N8: P4HA3; NbExp=3; IntAct=EBI-2949658, EBI-10181968;
CC O95429; O75340: PDCD6; NbExp=3; IntAct=EBI-2949658, EBI-352915;
CC O95429; Q9UBV8: PEF1; NbExp=5; IntAct=EBI-2949658, EBI-724639;
CC O95429; O15173: PGRMC2; NbExp=5; IntAct=EBI-2949658, EBI-1050125;
CC O95429; Q5T6S3: PHF19; NbExp=3; IntAct=EBI-2949658, EBI-2339674;
CC O95429; Q8IXY8: PPIL6; NbExp=3; IntAct=EBI-2949658, EBI-12226639;
CC O95429; Q7Z5V6-2: PPP1R32; NbExp=6; IntAct=EBI-2949658, EBI-12000762;
CC O95429; P28074: PSMB5; NbExp=5; IntAct=EBI-2949658, EBI-357828;
CC O95429; Q53H96: PYCR3; NbExp=3; IntAct=EBI-2949658, EBI-2959680;
CC O95429; Q9BTL3: RAMAC; NbExp=6; IntAct=EBI-2949658, EBI-744023;
CC O95429; Q01196-8: RUNX1; NbExp=3; IntAct=EBI-2949658, EBI-12001422;
CC O95429; Q9UPU9-3: SAMD4A; NbExp=3; IntAct=EBI-2949658, EBI-11986417;
CC O95429; Q8IYX7: SAXO1; NbExp=3; IntAct=EBI-2949658, EBI-3957636;
CC O95429; Q8TEC5: SH3RF2; NbExp=3; IntAct=EBI-2949658, EBI-2130111;
CC O95429; Q8IUQ4-2: SIAH1; NbExp=3; IntAct=EBI-2949658, EBI-11522811;
CC O95429; P14678-2: SNRPB; NbExp=5; IntAct=EBI-2949658, EBI-372475;
CC O95429; P09234: SNRPC; NbExp=3; IntAct=EBI-2949658, EBI-766589;
CC O95429; O75177-5: SS18L1; NbExp=3; IntAct=EBI-2949658, EBI-12035119;
CC O95429; P51687: SUOX; NbExp=3; IntAct=EBI-2949658, EBI-3921347;
CC O95429; Q6DHY5: TBC1D3G; NbExp=3; IntAct=EBI-2949658, EBI-13092532;
CC O95429; Q9P0N9: TBC1D7; NbExp=5; IntAct=EBI-2949658, EBI-3258000;
CC O95429; O95988: TCL1B; NbExp=3; IntAct=EBI-2949658, EBI-727338;
CC O95429; Q96M29: TEKT5; NbExp=3; IntAct=EBI-2949658, EBI-10239812;
CC O95429; Q7Z6R9: TFAP2D; NbExp=5; IntAct=EBI-2949658, EBI-11952651;
CC O95429; Q9GZM7: TINAGL1; NbExp=3; IntAct=EBI-2949658, EBI-715869;
CC O95429; Q08117-2: TLE5; NbExp=3; IntAct=EBI-2949658, EBI-11741437;
CC O95429; O75865-2: TRAPPC6A; NbExp=3; IntAct=EBI-2949658, EBI-8451480;
CC O95429; Q99816: TSG101; NbExp=3; IntAct=EBI-2949658, EBI-346882;
CC O95429; Q7KZS0: UBE2I; NbExp=3; IntAct=EBI-2949658, EBI-10180829;
CC O95429; Q9H9P5-5: UNKL; NbExp=3; IntAct=EBI-2949658, EBI-12817837;
CC O95429; Q9UPT9-2: USP22; NbExp=3; IntAct=EBI-2949658, EBI-12074414;
CC O95429; A5D8V6: VPS37C; NbExp=3; IntAct=EBI-2949658, EBI-2559305;
CC O95429; Q96K62: ZBTB45; NbExp=3; IntAct=EBI-2949658, EBI-714373;
CC O95429; O15062: ZBTB5; NbExp=3; IntAct=EBI-2949658, EBI-722671;
CC O95429; Q9NZV7: ZIM2; NbExp=3; IntAct=EBI-2949658, EBI-11962760;
CC O95429; Q53FC7; NbExp=2; IntAct=EBI-2949658, EBI-9356749;
CC O95429; Q96EJ4; NbExp=3; IntAct=EBI-2949658, EBI-750454;
CC O95429; P0DTC4: E; Xeno; NbExp=3; IntAct=EBI-2949658, EBI-25475850;
CC O95429; PRO_0000449622 [P0DTD1]: rep; Xeno; NbExp=3; IntAct=EBI-2949658, EBI-25475862;
CC -!- SUBCELLULAR LOCATION: Cytoplasm.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=O95429-1; Sequence=Displayed;
CC Name=2;
CC IsoId=O95429-2; Sequence=VSP_042741;
CC -!- TISSUE SPECIFICITY: Ubiquitous.
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DR EMBL; AF095194; AAD16123.2; -; mRNA.
DR EMBL; AF111116; AAD05226.1; -; mRNA.
DR EMBL; AK304072; BAG64979.1; -; mRNA.
DR EMBL; AC084024; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC038505; AAH38505.2; -; mRNA.
DR CCDS; CCDS56533.1; -. [O95429-2]
DR CCDS; CCDS6104.1; -. [O95429-1]
DR RefSeq; NP_001191807.1; NM_001204878.1. [O95429-2]
DR RefSeq; NP_004865.1; NM_004874.3. [O95429-1]
DR PDB; 1M62; NMR; -; A=376-457.
DR PDB; 1M7K; NMR; -; A=358-456.
DR PDBsum; 1M62; -.
DR PDBsum; 1M7K; -.
DR AlphaFoldDB; O95429; -.
DR SMR; O95429; -.
DR BioGRID; 114906; 226.
DR IntAct; O95429; 169.
DR MINT; O95429; -.
DR STRING; 9606.ENSP00000287322; -.
DR GlyGen; O95429; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; O95429; -.
DR PhosphoSitePlus; O95429; -.
DR BioMuta; BAG4; -.
DR EPD; O95429; -.
DR jPOST; O95429; -.
DR MassIVE; O95429; -.
DR MaxQB; O95429; -.
DR PaxDb; O95429; -.
DR PeptideAtlas; O95429; -.
DR PRIDE; O95429; -.
DR ProteomicsDB; 50875; -. [O95429-1]
DR ProteomicsDB; 50876; -. [O95429-2]
DR Antibodypedia; 4434; 416 antibodies from 43 providers.
DR DNASU; 9530; -.
DR Ensembl; ENST00000287322.5; ENSP00000287322.4; ENSG00000156735.11. [O95429-1]
DR Ensembl; ENST00000432471.6; ENSP00000393298.2; ENSG00000156735.11. [O95429-2]
DR GeneID; 9530; -.
DR KEGG; hsa:9530; -.
DR MANE-Select; ENST00000287322.5; ENSP00000287322.4; NM_004874.4; NP_004865.1.
DR UCSC; uc003xky.3; human. [O95429-1]
DR CTD; 9530; -.
DR DisGeNET; 9530; -.
DR GeneCards; BAG4; -.
DR HGNC; HGNC:940; BAG4.
DR HPA; ENSG00000156735; Low tissue specificity.
DR MIM; 603884; gene.
DR neXtProt; NX_O95429; -.
DR OpenTargets; ENSG00000156735; -.
DR PharmGKB; PA25240; -.
DR VEuPathDB; HostDB:ENSG00000156735; -.
DR eggNOG; KOG4361; Eukaryota.
DR GeneTree; ENSGT00940000158936; -.
DR HOGENOM; CLU_051025_0_0_1; -.
DR InParanoid; O95429; -.
DR OMA; YQPKDQQ; -.
DR OrthoDB; 1392346at2759; -.
DR PhylomeDB; O95429; -.
DR TreeFam; TF102013; -.
DR PathwayCommons; O95429; -.
DR Reactome; R-HSA-3371453; Regulation of HSF1-mediated heat shock response.
DR Reactome; R-HSA-5655302; Signaling by FGFR1 in disease.
DR Reactome; R-HSA-75893; TNF signaling.
DR Reactome; R-HSA-8853336; Signaling by plasma membrane FGFR1 fusions.
DR SignaLink; O95429; -.
DR SIGNOR; O95429; -.
DR BioGRID-ORCS; 9530; 26 hits in 1081 CRISPR screens.
DR ChiTaRS; BAG4; human.
DR EvolutionaryTrace; O95429; -.
DR GeneWiki; BAG4; -.
DR GenomeRNAi; 9530; -.
DR Pharos; O95429; Tbio.
DR PRO; PR:O95429; -.
DR Proteomes; UP000005640; Chromosome 8.
DR RNAct; O95429; protein.
DR Bgee; ENSG00000156735; Expressed in Brodmann (1909) area 23 and 186 other tissues.
DR ExpressionAtlas; O95429; baseline and differential.
DR Genevisible; O95429; HS.
DR GO; GO:0005829; C:cytosol; IDA:UniProtKB.
DR GO; GO:0016020; C:membrane; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
DR GO; GO:0000774; F:adenyl-nucleotide exchange factor activity; IBA:GO_Central.
DR GO; GO:0051087; F:chaperone binding; IBA:GO_Central.
DR GO; GO:0003723; F:RNA binding; HDA:UniProtKB.
DR GO; GO:0031625; F:ubiquitin protein ligase binding; IPI:ParkinsonsUK-UCL.
DR GO; GO:0071364; P:cellular response to epidermal growth factor stimulus; IEA:Ensembl.
DR GO; GO:0071356; P:cellular response to tumor necrosis factor; IDA:UniProtKB.
DR GO; GO:0043066; P:negative regulation of apoptotic process; TAS:ProtInc.
DR GO; GO:2001145; P:negative regulation of phosphatidylinositol-3,4,5-trisphosphate 5-phosphatase activity; IEA:Ensembl.
DR GO; GO:1903215; P:negative regulation of protein targeting to mitochondrion; IMP:ParkinsonsUK-UCL.
DR GO; GO:0030838; P:positive regulation of actin filament polymerization; IEA:Ensembl.
DR GO; GO:0045785; P:positive regulation of cell adhesion; IEA:Ensembl.
DR GO; GO:0010763; P:positive regulation of fibroblast migration; IEA:Ensembl.
DR GO; GO:0033138; P:positive regulation of peptidyl-serine phosphorylation; IEA:Ensembl.
DR GO; GO:0051897; P:positive regulation of protein kinase B signaling; IEA:Ensembl.
DR GO; GO:0051496; P:positive regulation of stress fiber assembly; IEA:Ensembl.
DR GO; GO:0006457; P:protein folding; TAS:ProtInc.
DR GO; GO:0072659; P:protein localization to plasma membrane; IEA:Ensembl.
DR GO; GO:0050821; P:protein stabilization; IBA:GO_Central.
DR GO; GO:0097178; P:ruffle assembly; IEA:Ensembl.
DR Gene3D; 1.20.58.120; -; 1.
DR InterPro; IPR039773; BAG_chaperone_regulator.
DR InterPro; IPR036533; BAG_dom_sf.
DR InterPro; IPR003103; BAG_domain.
DR PANTHER; PTHR12329; PTHR12329; 1.
DR Pfam; PF02179; BAG; 1.
DR SMART; SM00264; BAG; 1.
DR SUPFAM; SSF63491; SSF63491; 1.
DR PROSITE; PS51035; BAG; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Chaperone; Cytoplasm; Methylation;
KW Phosphoprotein; Reference proteome.
FT CHAIN 1..457
FT /note="BAG family molecular chaperone regulator 4"
FT /id="PRO_0000088870"
FT DOMAIN 379..456
FT /note="BAG"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00369"
FT REGION 1..101
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 113..136
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 166..333
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 347..378
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 27..50
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 120..136
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 166..191
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 265..280
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 281..295
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 296..333
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 347..370
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 7
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 40
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0007744|PubMed:24129315"
FT MOD_RES 53
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0007744|PubMed:24129315"
FT MOD_RES 108
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0007744|PubMed:24129315"
FT MOD_RES 185
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0007744|PubMed:24129315"
FT VAR_SEQ 90..125
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_042741"
FT MUTAGEN 414
FT /note="E->A: Reduces interaction with HSP70."
FT /evidence="ECO:0000269|PubMed:12058034"
FT MUTAGEN 424
FT /note="D->A: Abolishes interaction with HSP70."
FT /evidence="ECO:0000269|PubMed:12058034"
FT MUTAGEN 438..439
FT /note="RK->AA: Reduces interaction with HSP70."
FT /evidence="ECO:0000269|PubMed:12058034"
FT MUTAGEN 446
FT /note="Q->A: Abolishes interaction with HSP70."
FT /evidence="ECO:0000269|PubMed:12058034"
FT HELIX 380..399
FT /evidence="ECO:0007829|PDB:1M62"
FT HELIX 407..423
FT /evidence="ECO:0007829|PDB:1M62"
FT HELIX 432..456
FT /evidence="ECO:0007829|PDB:1M62"
SQ 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
