ID BAG6_HUMAN Reviewed; 1132 AA. AC P46379; A2ADJ7; A3KQ42; A3KQ44; A6NGY6; A6PWF7; B0UX84; B4DZ12; B4E3V4; AC E7EMZ4; F8VXY4; O95874; Q5HYL9; Q5SQ35; Q5SQ36; Q5SQ37; Q5SQ41; Q5SRP8; AC Q5SRP9; Q5STC1; Q5STX1; Q5STX3; Q96SA6; Q9BCN4; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 27-SEP-2005, sequence version 2. DT 28-JAN-2026, entry version 222. DE RecName: Full=Large proline-rich protein BAG6 {ECO:0000305}; DE AltName: Full=BAG family molecular chaperone regulator 6; DE AltName: Full=BCL2-associated athanogene 6 {ECO:0000312|HGNC:HGNC:13919}; DE Short=BAG-6; DE AltName: Full=HLA-B-associated transcript 3 {ECO:0000303|PubMed:2156268}; DE AltName: Full=Protein G3; DE AltName: Full=Protein Scythe {ECO:0000303|PubMed:17403783}; GN Name=BAG6 {ECO:0000312|HGNC:HGNC:13919}; GN Synonyms=BAT3 {ECO:0000303|PubMed:2156268}, G3; 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 [GENOMIC DNA / MRNA] (ISOFORM 1), VARIANT PRO-625, AND RP REPEAT. RC TISSUE=T-cell; RX PubMed=2156268; DOI=10.1073/pnas.87.6.2374; RA Banerji J., Sands J., Strominger J.L., Spies T.; RT "A gene pair from the human major histocompatibility complex encodes large RT proline-rich proteins with multiple repeated motifs and a single ubiquitin- RT like domain."; RL Proc. Natl. Acad. Sci. U.S.A. 87:2374-2378(1990). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2). RC TISSUE=Endometrium; RX PubMed=17974005; DOI=10.1186/1471-2164-8-399; RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U., RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D., RA Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A., RA Wiemann S., Schupp I.; RT "The full-ORF clone resource of the German cDNA consortium."; RL BMC Genomics 8:399-399(2007). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 4 AND 5), AND VARIANT RP PRO-625. RC TISSUE=Testis; 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 [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=14656967; DOI=10.1101/gr.1736803; RA Xie T., Rowen L., Aguado B., Ahearn M.E., Madan A., Qin S., Campbell R.D., RA Hood L.; RT "Analysis of the gene-dense major histocompatibility complex class III RT region and its comparison to mouse."; RL Genome Res. 13:2621-2636(2003). RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND VARIANT PRO-625. RA Hirakawa M., Yamaguchi H., Imai K., Shimada J., Shiina S., Tamiya G., RA Oka A., Inoko H.; RT "Homo sapiens 2,229,817bp genomic DNA of 6p21.3 HLA class I region."; RL Submitted (DEC-2004) to the EMBL/GenBank/DDBJ databases. RN [6] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND VARIANT PRO-625. RX PubMed=14574404; DOI=10.1038/nature02055; RA Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L., RA Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., Gilbert J.G.R., RA Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D., RA Andrews T.D., Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J., RA Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H., RA Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J., RA Brown J.Y., Burford D.C., Burrill W., Burton J., Carder C., Carter N.P., RA Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V., RA Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J., RA Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., Ellington A.E., RA Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J., RA French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J., RA Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C., RA Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A., RA Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R., RA Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., RA Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., RA Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., RA Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M., RA Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A., RA Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L., RA Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I., RA Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y., RA Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E., RA Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A., RA Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W., RA Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M., RA West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J., RA Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M., RA Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I., RA Rogers J., Beck S.; RT "The DNA sequence and analysis of human chromosome 6."; RL Nature 425:805-811(2003). RN [7] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND VARIANT PRO-625. RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., RA Hunkapiller M.W., Myers E.W., Venter J.C.; RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases. RN [8] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2). RC TISSUE=Kidney; 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 [9] RP FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH RICIN A CHAIN, MUTAGENESIS RP OF ASP-1001, AND CLEAVAGE BY CASP3. RX PubMed=14960581; DOI=10.1074/jbc.m307049200; RA Wu Y.-H., Shih S.-F., Lin J.-Y.; RT "Ricin triggers apoptotic morphological changes through caspase-3 cleavage RT of BAT3."; RL J. Biol. Chem. 279:19264-19275(2004). RN [10] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=17081983; DOI=10.1016/j.cell.2006.09.026; RA Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.; RT "Global, in vivo, and site-specific phosphorylation dynamics in signaling RT networks."; RL Cell 127:635-648(2006). RN [11] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1117, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=16964243; DOI=10.1038/nbt1240; RA Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.; RT "A probability-based approach for high-throughput protein phosphorylation RT analysis and site localization."; RL Nat. Biotechnol. 24:1285-1292(2006). RN [12] RP FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH EP300. RX PubMed=17403783; DOI=10.1101/gad.1534107; RA Sasaki T., Gan E.C., Wakeham A., Kornbluth S., Mak T.W., Okada H.; RT "HLA-B-associated transcript 3 (Bat3)/Scythe is essential for p300-mediated RT acetylation of p53."; RL Genes Dev. 21:848-861(2007). RN [13] RP FUNCTION IN NK CELL ACTIVATION, AND SUBCELLULAR LOCATION. RX PubMed=18055229; DOI=10.1016/j.immuni.2007.10.010; RA Pogge von Strandmann E., Simhadri V.R., von Tresckow B., Sasse S., RA Reiners K.S., Hansen H.P., Rothe A., Boll B., Simhadri V.L., Borchmann P., RA McKinnon P.J., Hallek M., Engert A.; RT "Human leukocyte antigen-B-associated transcript 3 is released from tumor RT cells and engages the NKp30 receptor on natural killer cells."; RL Immunity 27:965-974(2007). RN [14] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-113, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=17924679; DOI=10.1021/pr070152u; RA Yu L.R., Zhu Z., Chan K.C., Issaq H.J., Dimitrov D.S., Veenstra T.D.; RT "Improved titanium dioxide enrichment of phosphopeptides from HeLa cells RT and high confident phosphopeptide identification by cross-validation of RT MS/MS and MS/MS/MS spectra."; RL J. Proteome Res. 6:4150-4162(2007). RN [15] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-973, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Platelet; RX PubMed=18088087; DOI=10.1021/pr0704130; RA Zahedi R.P., Lewandrowski U., Wiesner J., Wortelkamp S., Moebius J., RA Schuetz C., Walter U., Gambaryan S., Sickmann A.; RT "Phosphoproteome of resting human platelets."; RL J. Proteome Res. 7:526-534(2008). RN [16] RP FUNCTION, AND INTERACTION WITH CTCFL. RX PubMed=18765639; DOI=10.1128/mcb.00568-08; RA Nguyen P., Bar-Sela G., Sun L., Bisht K.S., Cui H., Kohn E., Feinberg A.P., RA Gius D.; RT "BAT3 and SET1A form a complex with CTCFL/BORIS to modulate H3K4 histone RT dimethylation and gene expression."; RL Mol. Cell. Biol. 28:6720-6729(2008). RN [17] RP FUNCTION IN NK CELL ACTIVATION, SUBCELLULAR LOCATION, AND TISSUE RP SPECIFICITY. RX PubMed=18852879; DOI=10.1371/journal.pone.0003377; RA Simhadri V.R., Reiners K.S., Hansen H.P., Topolar D., Simhadri V.L., RA Nohroudi K., Kufer T.A., Engert A., Pogge von Strandmann E.; RT "Dendritic cells release HLA-B-associated transcript-3 positive exosomes to RT regulate natural killer function."; RL PLoS ONE 3:E3377-E3377(2008). RN [18] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-113; SER-973; SER-1081 AND RP SER-1117, PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-832 (ISOFORM 4), RP AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=18669648; DOI=10.1073/pnas.0805139105; RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., RA Elledge S.J., Gygi S.P.; RT "A quantitative atlas of mitotic phosphorylation."; RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008). RN [19] RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND IDENTIFICATION BY MASS RP SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=19413330; DOI=10.1021/ac9004309; RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.; RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a RT refined SCX-based approach."; RL Anal. Chem. 81:4493-4501(2009). RN [20] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-964 AND SER-973, AND RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Leukemic T-cell; RX PubMed=19690332; DOI=10.1126/scisignal.2000007; RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., RA Rodionov V., Han D.K.; RT "Quantitative phosphoproteomic analysis of T cell receptor signaling RT reveals system-wide modulation of protein-protein interactions."; RL Sci. Signal. 2:RA46-RA46(2009). RN [21] RP UBIQUITINATION IN CASE OF INFECTION BY L.PNEUMOPHILA (MICROBIAL INFECTION), RP AND INTERACTION WITH LPG2160 AND LEGU1 (MICROBIAL INFECTION). RX PubMed=20547746; DOI=10.1128/iai.00344-10; RA Ensminger A.W., Isberg R.R.; RT "E3 ubiquitin ligase activity and targeting of BAT3 by multiple Legionella RT pneumophila translocated substrates."; RL Infect. Immun. 78:3905-3919(2010). RN [22] RP FUNCTION. RX PubMed=20516149; DOI=10.1242/jcs.066738; RA Leznicki P., Clancy A., Schwappach B., High S.; RT "Bat3 promotes the membrane integration of tail-anchored proteins."; RL J. Cell Sci. 123:2170-2178(2010). RN [23] RP FUNCTION, SUBCELLULAR LOCATION, RIBOSOME-BINDING, IDENTIFICATION BY MASS RP SPECTROMETRY, AND IDENTIFICATION IN THE BAG6/BAT3 COMPLEX. RX PubMed=20676083; DOI=10.1038/nature09296; RA Mariappan M., Li X., Stefanovic S., Sharma A., Mateja A., Keenan R.J., RA Hegde R.S.; RT "A ribosome-associating factor chaperones tail-anchored membrane RT proteins."; RL Nature 466:1120-1124(2010). RN [24] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-350; SER-964; SER-973 AND RP SER-1117, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=20068231; DOI=10.1126/scisignal.2000475; RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.; RT "Quantitative phosphoproteomics reveals widespread full phosphorylation RT site occupancy during mitosis."; RL Sci. Signal. 3:RA3-RA3(2010). RN [25] 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., Buerckstuemmer T., RA 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 [26] RP FUNCTION, INTERACTION WITH AMFR; GET4; SYVN1 AND VCP, AND SUBCELLULAR RP LOCATION. RX PubMed=21636303; DOI=10.1016/j.molcel.2011.05.010; RA Wang Q., Liu Y., Soetandyo N., Baek K., Hegde R., Ye Y.; RT "A ubiquitin ligase-associated chaperone holdase maintains polypeptides in RT soluble states for proteasome degradation."; RL Mol. Cell 42:758-770(2011). RN [27] RP FUNCTION, AND DOMAIN. RX PubMed=21743475; DOI=10.1038/nature10181; RA Hessa T., Sharma A., Mariappan M., Eshleman H.D., Gutierrez E., Hegde R.S.; RT "Protein targeting and degradation are coupled for elimination of RT mislocalized proteins."; RL Nature 475:394-397(2011). RN [28] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-964 AND SER-973, AND RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=21406692; DOI=10.1126/scisignal.2001570; RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., RA Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.; RT "System-wide temporal characterization of the proteome and phosphoproteome RT of human embryonic stem cell differentiation."; RL Sci. Signal. 4:RS3-RS3(2011). RN [29] RP FUNCTION, AND INTERACTION WITH SGTA. RX PubMed=23129660; DOI=10.1073/pnas.1209997109; RA Leznicki P., High S.; RT "SGTA antagonizes BAG6-mediated protein triage."; RL Proc. Natl. Acad. Sci. U.S.A. 109:19214-19219(2012). RN [30] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-113; SER-964; SER-973; RP THR-1053; SER-1081 AND SER-1117, AND IDENTIFICATION BY MASS SPECTROMETRY RP [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 [31] RP INTERACTION WITH ZFAND2B. RX PubMed=24160817; DOI=10.1042/bj20130710; RA Glinka T., Alter J., Braunstein I., Tzach L., Wei Sheng C., Geifman S., RA Edelmann M.J., Kessler B.M., Stanhill A.; RT "Signal-peptide-mediated translocation is regulated by a p97-AIRAPL RT complex."; RL Biochem. J. 457:253-261(2014). RN [32] RP INTERACTION WITH SGTA AND USP13. RX PubMed=24424410; DOI=10.7554/elife.01369; RA Liu Y., Soetandyo N., Lee J.G., Liu L., Xu Y., Clemons W.M. Jr., Ye Y.; RT "USP13 antagonizes gp78 to maintain functionality of a chaperone in ER- RT associated degradation."; RL Elife 3:E01369-E01369(2014). RN [33] RP FUNCTION, AND INTERACTION WITH SGTA. RX PubMed=25179605; DOI=10.1242/jcs.155648; RA Wunderley L., Leznicki P., Payapilly A., High S.; RT "SGTA regulates the cytosolic quality control of hydrophobic substrates."; RL J. Cell Sci. 127:4728-4739(2014). RN [34] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-96 AND THR-117, AND 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 [35] RP FUNCTION, INTERACTION WITH RNF126, AND DOMAIN. RX PubMed=24981174; DOI=10.1016/j.molcel.2014.05.025; RA Rodrigo-Brenni M.C., Gutierrez E., Hegde R.S.; RT "Cytosolic quality control of mislocalized proteins requires RNF126 RT recruitment to Bag6."; RL Mol. Cell 55:227-237(2014). RN [36] RP FUNCTION. RX PubMed=26565908; DOI=10.1016/j.celrep.2015.09.047; RA Kadowaki H., Nagai A., Maruyama T., Takami Y., Satrimafitrah P., Kato H., RA Honda A., Hatta T., Natsume T., Sato T., Kai H., Ichijo H., Nishitoh H.; RT "Pre-emptive quality control protects the ER from protein overload via the RT proximity of ERAD components and SRP."; RL Cell Rep. 13:944-956(2015). RN [37] RP INTERACTION WITH ZFAND2B. RX PubMed=26337389; DOI=10.1091/mbc.e15-02-0085; RA Braunstein I., Zach L., Allan S., Kalies K.U., Stanhill A.; RT "Proteasomal degradation of preemptive quality control (pQC) substrates is RT mediated by an AIRAPL-p97 complex."; RL Mol. Biol. Cell 26:3719-3727(2015). RN [38] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=25944712; DOI=10.1002/pmic.201400617; RA Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., Ayoub D., RA Lane L., Bairoch A., Van Dorsselaer A., Carapito C.; RT "N-terminome analysis of the human mitochondrial proteome."; RL Proteomics 15:2519-2524(2015). RN [39] RP INTERACTION WITH UBQLN4. RX PubMed=27113755; DOI=10.15252/embr.201541402; RA Suzuki R., Kawahara H.; RT "UBQLN4 recognizes mislocalized transmembrane domain proteins and targets RT these to proteasomal degradation."; RL EMBO Rep. 17:842-857(2016). RN [40] RP FUNCTION. RX PubMed=26692333; DOI=10.1038/nm.4013; RA Osorio F.G., Soria-Valles C., Santiago-Fernandez O., Bernal T., RA Mittelbrunn M., Colado E., Rodriguez F., Bonzon-Kulichenko E., Vazquez J., RA Porta-de-la-Riva M., Ceron J., Fueyo A., Li J., Green A.R., Freije J.M., RA Lopez-Otin C.; RT "Loss of the proteostasis factor AIRAPL causes myeloid transformation by RT deregulating IGF-1 signaling."; RL Nat. Med. 22:91-96(2016). RN [41] RP FUNCTION, DOMAIN, AND REGION. RX PubMed=28104892; DOI=10.1126/science.aah6130; RA Shao S., Rodrigo-Brenni M.C., Kivlen M.H., Hegde R.S.; RT "Mechanistic basis for a molecular triage reaction."; RL Science 355:298-302(2017). RN [42] RP INTERACTION WITH MUL1. RX PubMed=40105103; DOI=10.1242/jcs.263576; RA Oezdemir M., Oeljeklaus S., Schendzielorz A., Morgenstern M., RA Valpadashi A., Yousefi R., Warscheid B., Dennerlein S.; RT "Definition of the human mitochondrial TOM interactome reveals TRABD as a RT new interacting protein."; RL J. Cell Sci. 138:0-0(2025). RN [43] RP STRUCTURE BY NMR OF 17-89. RG RIKEN structural genomics initiative (RSGI); RT "Solution structure of the N-terminal ubiquitin-like domain in the human RT BAT3 protein."; RL Submitted (JUL-2005) to the PDB data bank. RN [44] {ECO:0007744|PDB:4X86} RP X-RAY CRYSTALLOGRAPHY (1.85 ANGSTROMS) OF 1048-1123 IN COMPLEX WITH UBL4A, RP INTERACTION WITH UBL4A, AND MUTAGENESIS OF VAL-1067; PRO-1078; LEU-1085 AND RP ASP-1088. RX PubMed=25713138; DOI=10.1074/jbc.m114.631804; RA Kuwabara N., Minami R., Yokota N., Matsumoto H., Senda T., Kawahara H., RA Kato R.; RT "Structure of a BAG6 (Bcl-2-associated athanogene 6)-Ubl4a (ubiquitin-like RT protein 4a) complex reveals a novel binding interface that functions in RT tail-anchored protein biogenesis."; RL J. Biol. Chem. 290:9387-9398(2015). RN [45] {ECO:0007744|PDB:4WWR} RP X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS) OF 1060-1111 IN COMPLEX WITH UBL4A, RP INTERACTION WITH GET4 AND UBL4A, FUNCTION, AND IDENTIFICATION IN THE RP BAG6/BAT3 COMPLEX. RX PubMed=25535373; DOI=10.1073/pnas.1402745112; RA Mock J.Y., Chartron J.W., Zaslaver M., Xu Y., Ye Y., Clemons W.M. Jr.; RT "Bag6 complex contains a minimal tail-anchor-targeting module and a mock RT BAG domain."; RL Proc. Natl. Acad. Sci. U.S.A. 112:106-111(2015). RN [46] RP STRUCTURE BY NMR OF 17-101 IN COMPLEX WITH RNF126, FUNCTION, INTERACTION RP WITH RNF126 AND SGTA, AND DOMAIN. RX PubMed=27193484; DOI=10.1038/srep26433; RA Krysztofinska E.M., Martinez-Lumbreras S., Thapaliya A., Evans N.J., RA High S., Isaacson R.L.; RT "Structural and functional insights into the E3 ligase, RNF126."; RL Sci. Rep. 6:26433-26433(2016). RN [47] {ECO:0007744|PDB:6AU8} RP X-RAY CRYSTALLOGRAPHY (1.80 ANGSTROMS) OF 1008-1050 IN COMPLEX WITH GET4, RP SUBCELLULAR LOCATION, INTERACTION WITH GET4 AND KPNA2, AND MUTAGENESIS OF RP TRP-1010; TRP-1018; 1030-ARG-LYS-1031; TYR-1042 AND 1049-LYS-ARG-1050. RX PubMed=29042515; DOI=10.1073/pnas.1702940114; RA Mock J.Y., Xu Y., Ye Y., Clemons W.M. Jr.; RT "Structural basis for regulation of the nucleo-cytoplasmic distribution of RT Bag6 by TRC35."; RL Proc. Natl. Acad. Sci. U.S.A. 114:11679-11684(2017). RN [48] {ECO:0007744|PDB:7RU9, ECO:0007744|PDB:7RUA, ECO:0007744|PDB:7RUC} RP STRUCTURE BY ELECTRON MICROSCOPY (3.30 ANGSTROMS) OF 1004-1132 IN COMPLEX RP WITH GET4; UBL4A AND GET3. RX PubMed=34887561; DOI=10.1038/s41594-021-00690-7; RA Keszei A.F.A., Yip M.C.J., Hsieh T.C., Shao S.; RT "Structural insights into metazoan pretargeting GET complexes."; RL Nat. Struct. Mol. Biol. 28:1029-1037(2021). CC -!- FUNCTION: ATP-independent molecular chaperone preventing the CC aggregation of misfolded and hydrophobic patches-containing proteins CC (PubMed:21636303). Functions as part of a cytosolic protein quality CC control complex, the BAG6/BAT3 complex, which maintains these client CC proteins in a soluble state and participates in their proper delivery CC to the endoplasmic reticulum or alternatively can promote their sorting CC to the proteasome where they undergo degradation (PubMed:20516149, CC PubMed:21636303, PubMed:21743475, PubMed:28104892). The BAG6/BAT3 CC complex is involved in the post-translational delivery of tail- CC anchored/type II transmembrane proteins to the endoplasmic reticulum CC membrane. Recruited to ribosomes, it interacts with the transmembrane CC region of newly synthesized tail-anchored proteins and together with CC SGTA and ASNA1 mediates their delivery to the endoplasmic reticulum CC (PubMed:20516149, PubMed:20676083, PubMed:25535373, PubMed:28104892). CC Client proteins that cannot be properly delivered to the endoplasmic CC reticulum are ubiquitinated by RNF126, an E3 ubiquitin-protein ligase CC associated with BAG6 and are sorted to the proteasome (PubMed:24981174, CC PubMed:27193484, PubMed:28104892). SGTA which prevents the recruitment CC of RNF126 to BAG6 may negatively regulate the ubiquitination and the CC proteasomal degradation of client proteins (PubMed:23129660, CC PubMed:25179605, PubMed:27193484). Similarly, the BAG6/BAT3 complex CC also functions as a sorting platform for proteins of the secretory CC pathway that are mislocalized to the cytosol either delivering them to CC the proteasome for degradation or to the endoplasmic reticulum CC (PubMed:21743475). The BAG6/BAT3 complex also plays a role in the CC endoplasmic reticulum-associated degradation (ERAD), a quality control CC mechanism that eliminates unwanted proteins of the endoplasmic CC reticulum through their retrotranslocation to the cytosol and their CC targeting to the proteasome. It maintains these retrotranslocated CC proteins in an unfolded yet soluble state condition in the cytosol to CC ensure their proper delivery to the proteasome (PubMed:21636303). BAG6 CC is also required for selective ubiquitin-mediated degradation of CC defective nascent chain polypeptides by the proteasome. In this CC context, it may participate in the production of antigenic peptides and CC play a role in antigen presentation in immune response (By similarity). CC BAG6 is also involved in endoplasmic reticulum stress-induced pre- CC emptive quality control, a mechanism that selectively attenuates the CC translocation of newly synthesized proteins into the endoplasmic CC reticulum and reroutes them to the cytosol for proteasomal degradation. CC BAG6 may ensure the proper degradation of these proteins and thereby CC protects the endoplasmic reticulum from protein overload upon stress CC (PubMed:26565908). By inhibiting the polyubiquitination and subsequent CC proteasomal degradation of HSPA2 it may also play a role in the CC assembly of the synaptonemal complex during spermatogenesis (By CC similarity). Also positively regulates apoptosis by interacting with CC and stabilizing the proapoptotic factor AIFM1 (By similarity). By CC controlling the steady-state expression of the IGF1R receptor, CC indirectly regulates the insulin-like growth factor receptor signaling CC pathway (PubMed:26692333). {ECO:0000250|UniProtKB:Q9Z1R2, CC ECO:0000269|PubMed:20516149, ECO:0000269|PubMed:20676083, CC ECO:0000269|PubMed:21636303, ECO:0000269|PubMed:21743475, CC ECO:0000269|PubMed:23129660, ECO:0000269|PubMed:24981174, CC ECO:0000269|PubMed:25179605, ECO:0000269|PubMed:26565908, CC ECO:0000269|PubMed:26692333, ECO:0000269|PubMed:27193484, CC ECO:0000269|PubMed:28104892}. CC -!- FUNCTION: Involved in DNA damage-induced apoptosis: following DNA CC damage, accumulates in the nucleus and forms a complex with p300/EP300, CC enhancing p300/EP300-mediated p53/TP53 acetylation leading to increase CC p53/TP53 transcriptional activity (PubMed:17403783). When nuclear, may CC also act as a component of some chromatin regulator complex that CC regulates histone 3 'Lys-4' dimethylation (H3K4me2) (PubMed:18765639). CC {ECO:0000269|PubMed:17403783, ECO:0000269|PubMed:18765639}. CC -!- FUNCTION: Released extracellularly via exosomes, it is a ligand of the CC natural killer/NK cells receptor NCR3 and stimulates NK cells CC cytotoxicity. It may thereby trigger NK cells cytotoxicity against CC neighboring tumor cells and immature myeloid dendritic cells (DC). CC {ECO:0000269|PubMed:18055229, ECO:0000269|PubMed:18852879}. CC -!- FUNCTION: Mediates ricin-induced apoptosis. CC {ECO:0000269|PubMed:14960581}. CC -!- SUBUNIT: Component of the BAG6/BAT3 complex, also named BAT3 complex, CC at least composed of BAG6, UBL4A and GET4/TRC35 (PubMed:20676083, CC PubMed:34887561). Interacts with GET4; the interaction is direct and CC localizes BAG6 in the cytosol (PubMed:21636303, PubMed:29042515). CC Interacts with UBL4A; the interaction is direct and required for UBL4A CC protein stability (PubMed:25713138). Interacts with AIFM1 (By CC similarity). Interacts with HSPA2 (By similarity). Interacts with CTCFL CC (PubMed:18765639). Interacts with p300/EP300 (PubMed:17403783). CC Interacts (via ubiquitin-like domain) with RNF126; required for BAG6- CC dependent ubiquitination of proteins mislocalized to the cytosol CC (PubMed:24981174, PubMed:27193484). Interacts (via ubiquitin-like CC domain) with SGTA; SGTA competes with RNF126 by binding the same region CC of BAG6, thereby promoting deubiquitination of BAG6-target proteins and CC rescuing them from degradation (PubMed:23129660, PubMed:24424410, CC PubMed:25179605, PubMed:27193484). Interacts with ricin A chain CC (PubMed:14960581). Interacts with VCP and AMFR; both form the VCP/p97- CC AMFR/gp78 complex (PubMed:21636303). Interacts with SYVN1 CC (PubMed:21636303). Interacts with USP13; the interaction is direct and CC may mediate UBL4A deubiquitination (PubMed:24424410). Interacts with CC ZFAND2B (PubMed:24160817, PubMed:26337389). Interacts with KPNA2 CC (PubMed:29042515). Interacts with UBQLN4 (PubMed:27113755). Interacts CC with MUL1/MAPL (PubMed:40105103). {ECO:0000250|UniProtKB:Q9Z1R2, CC ECO:0000269|PubMed:14960581, ECO:0000269|PubMed:17403783, CC ECO:0000269|PubMed:18765639, ECO:0000269|PubMed:20676083, CC ECO:0000269|PubMed:21636303, ECO:0000269|PubMed:23129660, CC ECO:0000269|PubMed:24160817, ECO:0000269|PubMed:24424410, CC ECO:0000269|PubMed:24981174, ECO:0000269|PubMed:25179605, CC ECO:0000269|PubMed:25713138, ECO:0000269|PubMed:26337389, CC ECO:0000269|PubMed:27113755, ECO:0000269|PubMed:27193484, CC ECO:0000269|PubMed:29042515, ECO:0000269|PubMed:34887561, CC ECO:0000269|PubMed:40105103}. CC -!- SUBUNIT: (Microbial infection) Interacts with L.pneumophila Lpg2160 and CC LegU1 proteins. {ECO:0000269|PubMed:20547746}. CC -!- INTERACTION: CC P46379; P11802: CDK4; NbExp=2; IntAct=EBI-347552, EBI-295644; CC P46379; Q12805: EFEMP1; NbExp=4; IntAct=EBI-347552, EBI-536772; CC P46379; Q8IZU0: FAM9B; NbExp=3; IntAct=EBI-347552, EBI-10175124; CC P46379; Q53G59: KLHL12; NbExp=4; IntAct=EBI-347552, EBI-740929; CC P46379; Q7Z434: MAVS; NbExp=2; IntAct=EBI-347552, EBI-995373; CC P46379; O14931: NCR3; NbExp=6; IntAct=EBI-347552, EBI-14989262; CC P46379; Q9BV68: RNF126; NbExp=8; IntAct=EBI-347552, EBI-357322; CC P46379; O43765: SGTA; NbExp=6; IntAct=EBI-347552, EBI-347996; CC P46379; Q12800: TFCP2; NbExp=3; IntAct=EBI-347552, EBI-717422; CC P46379; Q19QW2: sars8a; Xeno; NbExp=2; IntAct=EBI-347552, EBI-25489121; CC P46379-1; O14931-1: NCR3; NbExp=5; IntAct=EBI-9640181, EBI-15013584; CC P46379-2; Q99996-3: AKAP9; NbExp=3; IntAct=EBI-10988864, EBI-11022349; CC P46379-2; A0A0S2Z5Q7: ALS2; NbExp=3; IntAct=EBI-10988864, EBI-25928834; CC P46379-2; Q9NP70: AMBN; NbExp=3; IntAct=EBI-10988864, EBI-11893530; CC P46379-2; Q6UX39: AMTN; NbExp=3; IntAct=EBI-10988864, EBI-11892684; CC P46379-2; P13928: ANXA8; NbExp=3; IntAct=EBI-10988864, EBI-2556915; CC P46379-2; O00203: AP3B1; NbExp=3; IntAct=EBI-10988864, EBI-1044383; CC P46379-2; Q7Z5R6-2: APBB1IP; NbExp=3; IntAct=EBI-10988864, EBI-12059807; CC P46379-2; P05067: APP; NbExp=5; IntAct=EBI-10988864, EBI-77613; CC P46379-2; O94778: AQP8; NbExp=3; IntAct=EBI-10988864, EBI-19124986; CC P46379-2; Q52LW3-2: ARHGAP29; NbExp=3; IntAct=EBI-10988864, EBI-22012297; CC P46379-2; Q9Y2Y0: ARL2BP; NbExp=3; IntAct=EBI-10988864, EBI-3449344; CC P46379-2; Q9Y575-3: ASB3; NbExp=3; IntAct=EBI-10988864, EBI-14199987; CC P46379-2; Q96DX5-3: ASB9; NbExp=3; IntAct=EBI-10988864, EBI-25843552; CC P46379-2; Q96FT7-4: ASIC4; NbExp=3; IntAct=EBI-10988864, EBI-9089489; CC P46379-2; P15313: ATP6V1B1; NbExp=3; IntAct=EBI-10988864, EBI-2891281; CC P46379-2; Q99700-5: ATXN2; NbExp=3; IntAct=EBI-10988864, EBI-25891409; CC P46379-2; P46379-2: BAG6; NbExp=4; IntAct=EBI-10988864, EBI-10988864; CC P46379-2; Q8TBE0: BAHD1; NbExp=3; IntAct=EBI-10988864, EBI-742750; CC P46379-2; P06276: BCHE; NbExp=3; IntAct=EBI-10988864, EBI-7936069; CC P46379-2; Q14457: BECN1; NbExp=3; IntAct=EBI-10988864, EBI-949378; CC P46379-2; Q8WUW1: BRK1; NbExp=3; IntAct=EBI-10988864, EBI-2837444; CC P46379-2; A0A1B0GWI1: CCDC196; NbExp=3; IntAct=EBI-10988864, EBI-10181422; CC P46379-2; P50990: CCT8; NbExp=3; IntAct=EBI-10988864, EBI-356507; CC P46379-2; Q9HCU0: CD248; NbExp=3; IntAct=EBI-10988864, EBI-9680942; CC P46379-2; Q9UJX2: CDC23; NbExp=3; IntAct=EBI-10988864, EBI-396137; CC P46379-2; Q7Z7K6: CENPV; NbExp=3; IntAct=EBI-10988864, EBI-1210604; CC P46379-2; Q6PJW8-3: CNST; NbExp=3; IntAct=EBI-10988864, EBI-25836090; CC P46379-2; Q96MW5: COG8; NbExp=3; IntAct=EBI-10988864, EBI-720875; CC P46379-2; Q03060-25: CREM; NbExp=3; IntAct=EBI-10988864, EBI-12884642; CC P46379-2; Q8IUI8: CRLF3; NbExp=3; IntAct=EBI-10988864, EBI-2872414; CC P46379-2; P53672: CRYBA2; NbExp=3; IntAct=EBI-10988864, EBI-750444; CC P46379-2; P78358: CTAG1B; NbExp=3; IntAct=EBI-10988864, EBI-1188472; CC P46379-2; Q9NUQ9: CYRIB; NbExp=3; IntAct=EBI-10988864, EBI-1055930; CC P46379-2; A8MQ03: CYSRT1; NbExp=3; IntAct=EBI-10988864, EBI-3867333; CC P46379-2; Q9UJU6: DBNL; NbExp=3; IntAct=EBI-10988864, EBI-751783; CC P46379-2; Q14203-5: DCTN1; NbExp=3; IntAct=EBI-10988864, EBI-25840379; CC P46379-2; Q9UBP4: DKK3; NbExp=3; IntAct=EBI-10988864, EBI-954409; CC P46379-2; Q6E0U4: DMKN; NbExp=3; IntAct=EBI-10988864, EBI-7943171; CC P46379-2; G5E9A7: DMWD; NbExp=3; IntAct=EBI-10988864, EBI-10976677; CC P46379-2; Q86TI2-2: DPP9; NbExp=3; IntAct=EBI-10988864, EBI-21529239; CC P46379-2; Q14117: DPYS; NbExp=3; IntAct=EBI-10988864, EBI-12275416; CC P46379-2; Q01658: DR1; NbExp=3; IntAct=EBI-10988864, EBI-750300; CC P46379-2; Q9H410: DSN1; NbExp=3; IntAct=EBI-10988864, EBI-1001144; CC P46379-2; O77932: DXO; NbExp=3; IntAct=EBI-10988864, EBI-372173; CC P46379-2; A0AVK6: E2F8; NbExp=3; IntAct=EBI-10988864, EBI-7779316; CC P46379-2; O95967: EFEMP2; NbExp=3; IntAct=EBI-10988864, EBI-743414; CC P46379-2; O00303: EIF3F; NbExp=3; IntAct=EBI-10988864, EBI-711990; CC P46379-2; Q6NXG1: ESRP1; NbExp=3; IntAct=EBI-10988864, EBI-10213520; CC P46379-2; Q6NXG1-3: ESRP1; NbExp=3; IntAct=EBI-10988864, EBI-21567429; CC P46379-2; Q6P1L5: FAM117B; NbExp=3; IntAct=EBI-10988864, EBI-3893327; CC P46379-2; Q49AJ0-4: FAM135B; NbExp=3; IntAct=EBI-10988864, EBI-25835236; CC P46379-2; Q8WVX9: FAR1; NbExp=3; IntAct=EBI-10988864, EBI-1045879; CC P46379-2; Q9NSA1: FGF21; NbExp=3; IntAct=EBI-10988864, EBI-3909329; CC P46379-2; P35637: FUS; NbExp=3; IntAct=EBI-10988864, EBI-400434; CC P46379-2; P06241-3: FYN; NbExp=3; IntAct=EBI-10988864, EBI-10691738; CC P46379-2; P15976-2: GATA1; NbExp=3; IntAct=EBI-10988864, EBI-9090198; CC P46379-2; Q7L5D6: GET4; NbExp=4; IntAct=EBI-10988864, EBI-711823; CC P46379-2; Q9BRX5: GINS3; NbExp=3; IntAct=EBI-10988864, EBI-2857315; CC P46379-2; Q96IJ6: GMPPA; NbExp=3; IntAct=EBI-10988864, EBI-750953; CC P46379-2; A6NEM1: GOLGA6L9; NbExp=3; IntAct=EBI-10988864, EBI-5916454; CC P46379-2; P28799: GRN; NbExp=3; IntAct=EBI-10988864, EBI-747754; CC P46379-2; Q9Y5Q9: GTF3C3; NbExp=3; IntAct=EBI-10988864, EBI-1054873; CC P46379-2; Q93077: H2AC6; NbExp=3; IntAct=EBI-10988864, EBI-725259; CC P46379-2; Q6NXT2: H3-5; NbExp=3; IntAct=EBI-10988864, EBI-2868501; CC P46379-2; Q96CS2: HAUS1; NbExp=3; IntAct=EBI-10988864, EBI-2514791; CC P46379-2; P04792: HSPB1; NbExp=3; IntAct=EBI-10988864, EBI-352682; CC P46379-2; P80217-2: IFI35; NbExp=3; IntAct=EBI-10988864, EBI-12823003; CC P46379-2; P08833: IGFBP1; NbExp=3; IntAct=EBI-10988864, EBI-13646303; CC P46379-2; P22692: IGFBP4; NbExp=3; IntAct=EBI-10988864, EBI-2831948; CC P46379-2; Q14005-2: IL16; NbExp=3; IntAct=EBI-10988864, EBI-17178971; CC P46379-2; Q13352: ITGB3BP; NbExp=3; IntAct=EBI-10988864, EBI-712105; CC P46379-2; Q96I82: KAZALD1; NbExp=3; IntAct=EBI-10988864, EBI-25904181; CC P46379-2; A1A512: KIAA0355; NbExp=3; IntAct=EBI-10988864, EBI-25844799; CC P46379-2; O60333-2: KIF1B; NbExp=3; IntAct=EBI-10988864, EBI-10975473; CC P46379-2; Q9UIH9: KLF15; NbExp=3; IntAct=EBI-10988864, EBI-2796400; CC P46379-2; P57682: KLF3; NbExp=3; IntAct=EBI-10988864, EBI-8472267; CC P46379-2; Q13887: KLF5; NbExp=3; IntAct=EBI-10988864, EBI-2696013; CC P46379-2; Q53G59: KLHL12; NbExp=3; IntAct=EBI-10988864, EBI-740929; CC P46379-2; Q9Y2M5: KLHL20; NbExp=3; IntAct=EBI-10988864, EBI-714379; CC P46379-2; Q8N1A0: KRT222; NbExp=3; IntAct=EBI-10988864, EBI-8473062; CC P46379-2; Q15012: LAPTM4A; NbExp=3; IntAct=EBI-10988864, EBI-723416; CC P46379-2; Q92615: LARP4B; NbExp=3; IntAct=EBI-10988864, EBI-1052558; CC P46379-2; Q6DKI2: LGALS9C; NbExp=3; IntAct=EBI-10988864, EBI-9088829; CC P46379-2; P02545: LMNA; NbExp=3; IntAct=EBI-10988864, EBI-351935; CC P46379-2; Q9BV99: LRRC61; NbExp=3; IntAct=EBI-10988864, EBI-2350424; CC P46379-2; Q9UDY8-2: MALT1; NbExp=3; IntAct=EBI-10988864, EBI-12056869; CC P46379-2; Q14696: MESD; NbExp=3; IntAct=EBI-10988864, EBI-6165891; CC P46379-2; Q8N6F8: METTL27; NbExp=3; IntAct=EBI-10988864, EBI-8487781; CC P46379-2; Q9HBH9-2: MKNK2; NbExp=3; IntAct=EBI-10988864, EBI-14141314; CC P46379-2; Q9BV20: MRI1; NbExp=3; IntAct=EBI-10988864, EBI-747381; CC P46379-2; O14931-1: NCR3; NbExp=4; IntAct=EBI-10988864, EBI-15013584; CC P46379-2; Q96FW1: OTUB1; NbExp=3; IntAct=EBI-10988864, EBI-1058491; CC P46379-2; Q6GQQ9-2: OTUD7B; NbExp=3; IntAct=EBI-10988864, EBI-25830200; CC P46379-2; Q9BR81: PCDHGC3; NbExp=3; IntAct=EBI-10988864, EBI-22012354; CC P46379-2; O15534: PER1; NbExp=3; IntAct=EBI-10988864, EBI-2557276; CC P46379-2; Q6P1K2: PMF1; NbExp=3; IntAct=EBI-10988864, EBI-713832; CC P46379-2; Q6ZMI0-5: PPP1R21; NbExp=3; IntAct=EBI-10988864, EBI-25835994; CC P46379-2; P31321: PRKAR1B; NbExp=3; IntAct=EBI-10988864, EBI-2805516; CC P46379-2; O60260-5: PRKN; NbExp=3; IntAct=EBI-10988864, EBI-21251460; CC P46379-2; Q8WUY3: PRUNE2; NbExp=3; IntAct=EBI-10988864, EBI-743880; CC P46379-2; Q96QF0-7: RAB3IP; NbExp=3; IntAct=EBI-10988864, EBI-11984839; CC P46379-2; Q15293: RCN1; NbExp=3; IntAct=EBI-10988864, EBI-948278; CC P46379-2; P47804-3: RGR; NbExp=3; IntAct=EBI-10988864, EBI-25834767; CC P46379-2; Q9Y3C5: RNF11; NbExp=3; IntAct=EBI-10988864, EBI-396669; CC P46379-2; Q9BV68: RNF126; NbExp=4; IntAct=EBI-10988864, EBI-357322; CC P46379-2; P51812: RPS6KA3; NbExp=3; IntAct=EBI-10988864, EBI-1046616; CC P46379-2; Q9BY12-3: SCAPER; NbExp=3; IntAct=EBI-10988864, EBI-25837959; CC P46379-2; O43765: SGTA; NbExp=3; IntAct=EBI-10988864, EBI-347996; CC P46379-2; Q96GM5: SMARCD1; NbExp=3; IntAct=EBI-10988864, EBI-358489; CC P46379-2; P37840: SNCA; NbExp=3; IntAct=EBI-10988864, EBI-985879; CC P46379-2; Q7Z6I5: SPATA12; NbExp=3; IntAct=EBI-10988864, EBI-10696971; CC P46379-2; P10451: SPP1; NbExp=3; IntAct=EBI-10988864, EBI-723648; CC P46379-2; Q7Z699: SPRED1; NbExp=3; IntAct=EBI-10988864, EBI-5235340; CC P46379-2; Q13148: TARDBP; NbExp=6; IntAct=EBI-10988864, EBI-372899; CC P46379-2; Q8N4U5: TCP11L2; NbExp=3; IntAct=EBI-10988864, EBI-11897462; CC P46379-2; Q6NUS6: TCTN3; NbExp=3; IntAct=EBI-10988864, EBI-11278332; CC P46379-2; Q9NUW8: TDP1; NbExp=3; IntAct=EBI-10988864, EBI-2902553; CC P46379-2; Q86WV5: TEN1; NbExp=3; IntAct=EBI-10988864, EBI-2562799; CC P46379-2; Q8WTV1: THAP3; NbExp=3; IntAct=EBI-10988864, EBI-17438286; CC P46379-2; Q8IUR5-4: TMTC1; NbExp=3; IntAct=EBI-10988864, EBI-9089156; CC P46379-2; Q12888: TP53BP1; NbExp=3; IntAct=EBI-10988864, EBI-396540; CC P46379-2; Q86WT6-2: TRIM69; NbExp=3; IntAct=EBI-10988864, EBI-11525489; CC P46379-2; Q86WV8: TSC1; NbExp=5; IntAct=EBI-10988864, EBI-12806590; CC P46379-2; Q99598: TSNAX; NbExp=3; IntAct=EBI-10988864, EBI-21353855; CC P46379-2; Q8N7F7: UBL4B; NbExp=3; IntAct=EBI-10988864, EBI-10267507; CC P46379-2; Q9UMX0: UBQLN1; NbExp=3; IntAct=EBI-10988864, EBI-741480; CC P46379-2; Q9UHD9: UBQLN2; NbExp=3; IntAct=EBI-10988864, EBI-947187; CC P46379-2; P45880: VDAC2; NbExp=3; IntAct=EBI-10988864, EBI-354022; CC P46379-2; Q9NZR4: VSX1; NbExp=3; IntAct=EBI-10988864, EBI-21789837; CC P46379-2; P58304: VSX2; NbExp=3; IntAct=EBI-10988864, EBI-6427899; CC P46379-2; O76024: WFS1; NbExp=3; IntAct=EBI-10988864, EBI-720609; CC P46379-2; Q86U90: YRDC; NbExp=3; IntAct=EBI-10988864, EBI-21659356; CC P46379-2; Q8IWT0-2: ZBTB8OS; NbExp=3; IntAct=EBI-10988864, EBI-12956041; CC P46379-2; Q9H4I2-2: ZHX3; NbExp=3; IntAct=EBI-10988864, EBI-10693326; CC P46379-2; Q9UL40: ZNF346; NbExp=3; IntAct=EBI-10988864, EBI-2462313; CC P46379-2; Q96MN9-2: ZNF488; NbExp=3; IntAct=EBI-10988864, EBI-25831733; CC P46379-2; Q2QGD7: ZXDC; NbExp=3; IntAct=EBI-10988864, EBI-1538838; CC P46379-2; A0A1U9X8X8; NbExp=3; IntAct=EBI-10988864, EBI-17234977; CC P46379-2; B7Z3E8; NbExp=3; IntAct=EBI-10988864, EBI-25831617; CC P46379-2; Q9P1N4; NbExp=3; IntAct=EBI-10988864, EBI-25878161; CC P46379-2; P23285: CPR2; Xeno; NbExp=3; IntAct=EBI-10988864, EBI-5448; CC P46379-2; P35176: CPR5; Xeno; NbExp=3; IntAct=EBI-10988864, EBI-5458; CC P46379-2; P43552: YFL051C; Xeno; NbExp=3; IntAct=EBI-10988864, EBI-22855; CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000269|PubMed:17403783, CC ECO:0000269|PubMed:20676083, ECO:0000269|PubMed:21636303, CC ECO:0000269|PubMed:29042515}. Nucleus {ECO:0000269|PubMed:14960581, CC ECO:0000269|PubMed:17403783, ECO:0000269|PubMed:21636303, CC ECO:0000269|PubMed:29042515}. Secreted, extracellular exosome CC {ECO:0000269|PubMed:18055229, ECO:0000269|PubMed:18852879}. CC Note=Normally localized in cytosol and nucleus, it can also be released CC extracellularly, in exosomes, by tumor and myeloid dendritic cells CC (PubMed:18055229, PubMed:18852879). Cytoplasmic retention is due to CC interaction with GET4 (PubMed:29042515). {ECO:0000269|PubMed:18055229, CC ECO:0000269|PubMed:18852879, ECO:0000269|PubMed:29042515}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=5; CC Name=1; CC IsoId=P46379-1; Sequence=Displayed; CC Name=2; CC IsoId=P46379-2; Sequence=VSP_015695; CC Name=3; CC IsoId=P46379-3; Sequence=VSP_015695, VSP_030519; CC Name=4; CC IsoId=P46379-4; Sequence=VSP_015695, VSP_045910, VSP_045911, CC VSP_045912, VSP_045913; CC Name=5; CC IsoId=P46379-5; Sequence=VSP_015695, VSP_045913; CC -!- TISSUE SPECIFICITY: Expressed by immature dendritic cells (at protein CC level). {ECO:0000269|PubMed:18852879}. CC -!- DOMAIN: The ubiquitin-like domain mediates interaction with the E3 CC ubiquitin-protein ligase RNF126 which is responsible for the BAG6- CC dependent ubiquitination of client proteins (PubMed:21743475, CC PubMed:24981174, PubMed:27193484, PubMed:28104892). SGTA also binds CC this domain and competes with RNF126 to antagonize client protein CC ubiquitination and degradation (PubMed:28104892). The ubiquitin-like CC domain also mediates the interaction with USP13 (PubMed:24424410). CC {ECO:0000269|PubMed:21743475, ECO:0000269|PubMed:24424410, CC ECO:0000269|PubMed:24981174, ECO:0000269|PubMed:27193484, CC ECO:0000269|PubMed:28104892}. CC -!- PTM: Ricin can induce a cleavage by the caspase CASP3. The released C- CC terminal peptide induces apoptosis. {ECO:0000269|PubMed:14960581}. CC -!- PTM: (Microbial infection) In case of infection by L.pneumophila, CC ubiquitinated by the SCF(LegU1) complex. {ECO:0000269|PubMed:20547746}. CC -!- SEQUENCE CAUTION: CC Sequence=AAD18085.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305}; CC Sequence=BAB63390.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305}; CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; M33519; AAA35587.1; -; mRNA. DR EMBL; M33521; AAA35588.1; -; Genomic_DNA. DR EMBL; M33520; AAA35588.1; JOINED; Genomic_DNA. DR EMBL; BX647244; CAI46045.1; -; mRNA. DR EMBL; AK302695; BAG63924.1; -; mRNA. DR EMBL; AK304879; BAG65616.1; -; mRNA. DR EMBL; AF129756; AAD18085.1; ALT_INIT; Genomic_DNA. DR EMBL; BA000025; BAB63390.1; ALT_INIT; Genomic_DNA. DR EMBL; AL662801; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AL662847; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AL670886; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AL805934; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; BX511262; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; CR354443; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; CR753842; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; CR753892; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; CR759761; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; CH471081; EAX03455.1; -; Genomic_DNA. DR EMBL; BC003133; AAH03133.1; -; mRNA. DR CCDS; CCDS4709.1; -. [P46379-2] DR CCDS; CCDS56414.1; -. [P46379-4] DR CCDS; CCDS56415.1; -. [P46379-5] DR CCDS; CCDS93882.1; -. [P46379-3] DR PIR; A35098; A35098. DR RefSeq; NP_001092004.1; NM_001098534.2. [P46379-2] DR RefSeq; NP_001186626.1; NM_001199697.2. [P46379-4] DR RefSeq; NP_001186627.1; NM_001199698.2. [P46379-5] DR RefSeq; NP_001374869.1; NM_001387940.1. [P46379-5] DR RefSeq; NP_001374885.1; NM_001387956.1. [P46379-5] DR RefSeq; NP_001374890.1; NM_001387961.1. [P46379-2] DR RefSeq; NP_001374915.1; NM_001387986.1. [P46379-2] DR RefSeq; NP_001374918.1; NM_001387989.1. [P46379-3] DR RefSeq; NP_001374923.1; NM_001387994.1. [P46379-3] DR RefSeq; NP_001374925.1; NM_001387996.1. [P46379-3] DR RefSeq; NP_001374928.1; NM_001387999.1. [P46379-5] DR RefSeq; NP_001374930.1; NM_001388001.1. [P46379-5] DR RefSeq; NP_001374940.1; NM_001388011.1. [P46379-3] DR RefSeq; NP_001374943.1; NM_001388014.1. [P46379-5] DR RefSeq; NP_001374944.1; NM_001388015.1. [P46379-2] DR RefSeq; NP_001374946.1; NM_001388017.1. [P46379-2] DR RefSeq; NP_001374947.1; NM_001388018.1. [P46379-2] DR RefSeq; NP_001374949.1; NM_001388020.1. [P46379-3] DR RefSeq; NP_542433.1; NM_080702.3. [P46379-2] DR RefSeq; NP_542434.1; NM_080703.3. [P46379-2] DR PDB; 1WX9; NMR; -; A=17-89. DR PDB; 2N9P; NMR; -; C=17-101. DR PDB; 4DWF; X-ray; 1.80 A; A/B=13-101. DR PDB; 4EEW; X-ray; 1.30 A; A/B=1-87. DR PDB; 4WWR; X-ray; 2.00 A; A/C/E/G=1060-1111. DR PDB; 4X86; X-ray; 1.85 A; B=1048-1123. DR PDB; 6AU8; X-ray; 1.80 A; C=1008-1050. DR PDB; 7RU9; EM; 3.30 A; D/G=1004-1132. DR PDB; 7RUA; EM; 3.40 A; D/G=1004-1132. DR PDB; 7RUC; EM; 3.60 A; D/G=1004-1132. DR PDBsum; 1WX9; -. DR PDBsum; 2N9P; -. DR PDBsum; 4DWF; -. DR PDBsum; 4EEW; -. DR PDBsum; 4WWR; -. DR PDBsum; 4X86; -. DR PDBsum; 6AU8; -. DR PDBsum; 7RU9; -. DR PDBsum; 7RUA; -. DR PDBsum; 7RUC; -. DR AlphaFoldDB; P46379; -. DR EMDB; EMD-24700; -. DR EMDB; EMD-24701; -. DR EMDB; EMD-24702; -. DR SMR; P46379; -. DR BioGRID; 113647; 512. DR ComplexPortal; CPX-132; BAT3 complex. DR CORUM; P46379; -. DR DIP; DIP-31191N; -. DR FunCoup; P46379; 3901. DR IntAct; P46379; 473. DR MINT; P46379; -. DR STRING; 9606.ENSP00000365131; -. DR GlyCosmos; P46379; 1 site, 1 glycan. DR GlyGen; P46379; 5 sites, 2 O-linked glycans (2 sites). DR iPTMnet; P46379; -. DR MetOSite; P46379; -. DR PhosphoSitePlus; P46379; -. DR SwissPalm; P46379; -. DR BioMuta; BAG6; -. DR DMDM; 76800648; -. DR jPOST; P46379; -. DR MassIVE; P46379; -. DR PaxDb; 9606-ENSP00000365131; -. DR PeptideAtlas; P46379; -. DR ProteomicsDB; 17045; -. DR ProteomicsDB; 29168; -. DR ProteomicsDB; 55736; -. [P46379-1] DR ProteomicsDB; 55737; -. [P46379-2] DR ProteomicsDB; 55738; -. [P46379-3] DR Pumba; P46379; -. DR Antibodypedia; 27346; 305 antibodies from 37 providers. DR DNASU; 7917; -. DR Ensembl; ENST00000211379.9; ENSP00000211379.5; ENSG00000204463.15. [P46379-2] DR Ensembl; ENST00000361076.9; ENSP00000354368.5; ENSG00000096155.15. [P46379-1] DR Ensembl; ENST00000362049.10; ENSP00000354875.6; ENSG00000204463.15. [P46379-5] DR Ensembl; ENST00000375976.8; ENSP00000365143.4; ENSG00000204463.15. [P46379-2] DR Ensembl; ENST00000383446.8; ENSP00000372938.4; ENSG00000096155.15. [P46379-2] DR Ensembl; ENST00000383448.6; ENSP00000372940.2; ENSG00000096155.15. [P46379-2] DR Ensembl; ENST00000417144.5; ENSP00000412110.1; ENSG00000229524.10. [P46379-2] DR Ensembl; ENST00000419847.5; ENSP00000389121.1; ENSG00000233348.10. [P46379-2] DR Ensembl; ENST00000439687.6; ENSP00000402856.2; ENSG00000204463.15. [P46379-4] DR Ensembl; ENST00000442479.6; ENSP00000413698.2; ENSG00000229524.10. [P46379-2] DR Ensembl; ENST00000443182.6; ENSP00000410156.2; ENSG00000233348.10. [P46379-2] DR Ensembl; ENST00000449450.6; ENSP00000397894.2; ENSG00000229524.10. [P46379-1] DR Ensembl; ENST00000451932.6; ENSP00000390966.2; ENSG00000233348.10. [P46379-1] DR Ensembl; ENST00000551350.5; ENSP00000447546.2; ENSG00000229524.10. [P46379-5] DR Ensembl; ENST00000552116.2; ENSP00000447946.2; ENSG00000233348.10. [P46379-5] DR Ensembl; ENST00000552605.4; ENSP00000446525.2; ENSG00000096155.15. [P46379-5] DR Ensembl; ENST00000613474.4; ENSP00000478966.1; ENSG00000227761.10. [P46379-4] DR Ensembl; ENST00000615143.1; ENSP00000482413.1; ENSG00000229524.10. [P46379-4] DR Ensembl; ENST00000615224.2; ENSP00000477951.1; ENSG00000228760.10. [P46379-4] DR Ensembl; ENST00000615725.4; ENSP00000479238.1; ENSG00000233348.10. [P46379-4] DR Ensembl; ENST00000617635.2; ENSP00000484238.1; ENSG00000096155.15. [P46379-4] DR Ensembl; ENST00000621056.2; ENSP00000477867.1; ENSG00000234651.10. [P46379-4] DR Ensembl; ENST00000676615.2; ENSP00000502941.1; ENSG00000204463.15. [P46379-3] DR GeneID; 7917; -. DR KEGG; hsa:7917; -. DR MANE-Select; ENST00000676615.2; ENSP00000502941.1; NM_001387994.1; NP_001374923.1. [P46379-3] DR UCSC; uc003nvf.4; human. [P46379-1] DR AGR; HGNC:13919; -. DR ClinPGx; PA25264; -. DR CTD; 7917; -. DR DisGeNET; 7917; -. DR GeneCards; BAG6; -. DR HGNC; HGNC:13919; BAG6. DR HPA; ENSG00000204463; Low tissue specificity. DR MIM; 142590; gene. DR OpenTargets; ENSG00000204463; -. DR VEuPathDB; HostDB:ENSG00000204463; -. DR eggNOG; KOG4248; Eukaryota. DR GeneTree; ENSGT00390000016199; -. DR HOGENOM; CLU_012159_0_0_1; -. DR InParanoid; P46379; -. DR OrthoDB; 1885901at2759; -. DR PAN-GO; P46379; 4 GO annotations based on evolutionary models. DR PhylomeDB; P46379; -. DR PathwayCommons; P46379; -. DR Reactome; R-HSA-9609523; Insertion of tail-anchored proteins into the endoplasmic reticulum membrane. DR SignaLink; P46379; -. DR SIGNOR; P46379; -. DR Agora; ENSG00000204463; -. DR BioGRID-ORCS; 7917; 50 hits in 1161 CRISPR screens. DR ChiTaRS; BAG6; human. DR EvolutionaryTrace; P46379; -. DR GeneWiki; HLA-B_associated_transcript_3; -. DR GenomeRNAi; 7917; -. DR Pharos; P46379; Tbio. DR PRO; PR:P46379; -. DR Proteomes; UP000005640; Chromosome 6. DR RNAct; P46379; protein. DR Bgee; ENSG00000204463; Expressed in right testis and 95 other cell types or tissues. DR ExpressionAtlas; P46379; baseline and differential. DR GO; GO:0071818; C:BAT3 complex; IDA:UniProtKB. DR GO; GO:0005737; C:cytoplasm; IDA:ParkinsonsUK-UCL. DR GO; GO:0005829; C:cytosol; IDA:HPA. DR GO; GO:0070062; C:extracellular exosome; IDA:UniProtKB. DR GO; GO:0016020; C:membrane; IDA:ParkinsonsUK-UCL. DR GO; GO:0005654; C:nucleoplasm; IDA:HPA. DR GO; GO:0005634; C:nucleus; IDA:UniProtKB. DR GO; GO:0030544; F:Hsp70 protein binding; IEA:Ensembl. DR GO; GO:0042802; F:identical protein binding; IPI:IntAct. DR GO; GO:0051787; F:misfolded protein binding; IDA:ParkinsonsUK-UCL. DR GO; GO:0060090; F:molecular adaptor activity; EXP:DisProt. DR GO; GO:0140677; F:molecular function activator activity; IEP:DisProt. DR GO; GO:0031593; F:polyubiquitin modification-dependent protein binding; ISS:UniProtKB. DR GO; GO:0070628; F:proteasome binding; ISS:UniProtKB. DR GO; GO:0140597; F:protein carrier chaperone; IDA:ParkinsonsUK-UCL. DR GO; GO:0048018; F:receptor ligand activity; IDA:UniProt. DR GO; GO:0043022; F:ribosome binding; IDA:UniProtKB. DR GO; GO:0005102; F:signaling receptor binding; IPI:UniProtKB. DR GO; GO:0031625; F:ubiquitin protein ligase binding; IPI:UniProtKB. DR GO; GO:1990381; F:ubiquitin-specific protease binding; IPI:ParkinsonsUK-UCL. DR GO; GO:0006915; P:apoptotic process; IDA:UniProtKB. DR GO; GO:0007420; P:brain development; ISS:UniProtKB. DR GO; GO:0030154; P:cell differentiation; IEA:UniProtKB-KW. DR GO; GO:0006325; P:chromatin organization; IEA:UniProtKB-KW. DR GO; GO:0061857; P:endoplasmic reticulum stress-induced pre-emptive quality control; IMP:UniProtKB. DR GO; GO:0036503; P:ERAD pathway; IDA:UniProtKB. DR GO; GO:0002429; P:immune response-activating cell surface receptor signaling pathway; IDA:UniProtKB. DR GO; GO:0018393; P:internal peptidyl-lysine acetylation; IDA:UniProtKB. DR GO; GO:0042771; P:intrinsic apoptotic signaling pathway in response to DNA damage by p53 class mediator; IMP:UniProtKB. DR GO; GO:0070059; P:intrinsic apoptotic signaling pathway in response to endoplasmic reticulum stress; ISS:UniProtKB. DR GO; GO:0001822; P:kidney development; ISS:UniProtKB. DR GO; GO:0030324; P:lung development; ISS:UniProtKB. DR GO; GO:0036506; P:maintenance of unfolded protein; IMP:ParkinsonsUK-UCL. DR GO; GO:0030101; P:natural killer cell activation; IDA:UniProtKB. DR GO; GO:0043066; P:negative regulation of apoptotic process; IEA:Ensembl. DR GO; GO:0032435; P:negative regulation of proteasomal ubiquitin-dependent protein catabolic process; ISS:UniProtKB. DR GO; GO:0045861; P:negative regulation of proteolysis; ISS:UniProtKB. DR GO; GO:0051132; P:NK T cell activation; IDA:UniProt. DR GO; GO:1904294; P:positive regulation of ERAD pathway; IMP:ParkinsonsUK-UCL. DR GO; GO:0006620; P:post-translational protein targeting to endoplasmic reticulum membrane; IDA:ComplexPortal. DR GO; GO:0010498; P:proteasomal protein catabolic process; IMP:UniProtKB. DR GO; GO:0043161; P:proteasome-mediated ubiquitin-dependent protein catabolic process; IEA:Ensembl. DR GO; GO:0050821; P:protein stabilization; ISS:UniProtKB. DR GO; GO:0045995; P:regulation of embryonic development; ISS:UniProtKB. DR GO; GO:0031647; P:regulation of protein stability; IDA:ComplexPortal. DR GO; GO:0007283; P:spermatogenesis; ISS:UniProtKB. DR GO; GO:0007130; P:synaptonemal complex assembly; ISS:UniProtKB. DR GO; GO:0071816; P:tail-anchored membrane protein insertion into ER membrane; IDA:UniProtKB. DR GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; IDA:ComplexPortal. DR CDD; cd01809; Ubl_BAG6; 1. DR DisProt; DP02829; -. DR FunFam; 3.10.20.90:FF:000041; large proline-rich protein BAG6 isoform X1; 1. DR Gene3D; 3.10.20.90; Phosphatidylinositol 3-kinase Catalytic Subunit, Chain A, domain 1; 1. DR InterPro; IPR021925; BAG6. DR InterPro; IPR048926; Bag6_BAGS. DR InterPro; IPR000626; Ubiquitin-like_dom. DR InterPro; IPR029071; Ubiquitin-like_domsf. DR InterPro; IPR019954; Ubiquitin_CS. DR PANTHER; PTHR15204; LARGE PROLINE-RICH PROTEIN BAG6; 1. DR PANTHER; PTHR15204:SF0; LARGE PROLINE-RICH PROTEIN BAG6; 1. DR Pfam; PF12057; BAG6; 1. DR Pfam; PF20960; Bag6_BAGS; 1. DR Pfam; PF00240; ubiquitin; 1. DR SMART; SM00213; UBQ; 1. DR SUPFAM; SSF101447; Formin homology 2 domain (FH2 domain); 1. DR SUPFAM; SSF54236; Ubiquitin-like; 1. DR PROSITE; PS00299; UBIQUITIN_1; 1. DR PROSITE; PS50053; UBIQUITIN_2; 1. PE 1: Evidence at protein level; KW 3D-structure; Acetylation; Alternative splicing; Apoptosis; Chaperone; KW Chromatin regulator; Cytoplasm; Differentiation; Immunity; Nucleus; KW Phosphoprotein; Proteomics identification; Reference proteome; Repeat; KW Secreted; Spermatogenesis; Transport; Ubl conjugation. FT CHAIN 1..1132 FT /note="Large proline-rich protein BAG6" FT /id="PRO_0000114897" FT DOMAIN 17..92 FT /note="Ubiquitin-like" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00214" FT REPEAT 242..270 FT /note="1" FT /evidence="ECO:0000303|PubMed:2156268" FT REPEAT 415..443 FT /note="2" FT /evidence="ECO:0000303|PubMed:2156268" FT REPEAT 574..602 FT /note="3" FT /evidence="ECO:0000303|PubMed:2156268" FT REPEAT 608..636 FT /note="4" FT /evidence="ECO:0000303|PubMed:2156268" FT REGION 87..126 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 189..272 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 242..636 FT /note="4 X 29 AA approximate repeats" FT /evidence="ECO:0000303|PubMed:2156268" FT REGION 385..441 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 461..528 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 560..603 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 651..692 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 947..1132 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 1010..1040 FT /note="Required for interaction with GET4" FT /evidence="ECO:0000269|PubMed:25535373, FT ECO:0000269|PubMed:29042515" FT REGION 1022..1132 FT /note="Sufficient for the delivery of client proteins to FT the endoplasmic reticulum" FT /evidence="ECO:0000269|PubMed:28104892" FT REGION 1058..1115 FT /note="BAG-similar domain, required and sufficient for FT interaction with UBL4A" FT /evidence="ECO:0000269|PubMed:25535373, FT ECO:0000269|PubMed:25713138" FT MOTIF 1012..1054 FT /note="Nuclear localization site" FT /evidence="ECO:0000305|PubMed:25535373, FT ECO:0000305|PubMed:29042515" FT COMPBIAS 95..108 FT /note="Low complexity" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 200..210 FT /note="Pro residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 251..262 FT /note="Pro residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 393..407 FT /note="Pro residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 408..426 FT /note="Low complexity" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 427..438 FT /note="Pro residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 507..520 FT /note="Pro residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 569..586 FT /note="Low complexity" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 588..599 FT /note="Pro residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 656..680 FT /note="Pro residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 681..692 FT /note="Gly residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 1005..1020 FT /note="Low complexity" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 1066..1076 FT /note="Low complexity" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT SITE 1001..1002 FT /note="Cleavage; by CASP3" FT /evidence="ECO:0000269|PubMed:14960581" FT MOD_RES 1 FT /note="N-acetylmethionine" FT /evidence="ECO:0007744|PubMed:19413330" FT MOD_RES 96 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:24275569" FT MOD_RES 113 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:17924679, FT ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:23186163" FT MOD_RES 117 FT /note="Phosphothreonine" FT /evidence="ECO:0007744|PubMed:24275569" FT MOD_RES 350 FT /note="Phosphothreonine" FT /evidence="ECO:0007744|PubMed:20068231" FT MOD_RES 964 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:19690332, FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692, FT ECO:0007744|PubMed:23186163" FT MOD_RES 973 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18088087, FT ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:19690332, FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692, FT ECO:0007744|PubMed:23186163" FT MOD_RES 1053 FT /note="Phosphothreonine" FT /evidence="ECO:0007744|PubMed:23186163" FT MOD_RES 1081 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18669648, FT ECO:0007744|PubMed:23186163" FT MOD_RES 1117 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:16964243, FT ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:20068231, FT ECO:0007744|PubMed:23186163" FT VAR_SEQ 185..190 FT /note="Missing (in isoform 2, isoform 3, isoform 4 and FT isoform 5)" FT /evidence="ECO:0000303|PubMed:14702039, FT ECO:0000303|PubMed:15489334, ECO:0000303|PubMed:17974005" FT /id="VSP_015695" FT VAR_SEQ 489 FT /note="G -> GSTLIQLPSLPPEFMHAVAHQITHQAMVAAVASAAAG (in FT isoform 3)" FT /evidence="ECO:0000305" FT /id="VSP_030519" FT VAR_SEQ 527 FT /note="Missing (in isoform 4)" FT /evidence="ECO:0000303|PubMed:14702039" FT /id="VSP_045910" FT VAR_SEQ 561..685 FT /note="Missing (in isoform 4)" FT /evidence="ECO:0000303|PubMed:14702039" FT /id="VSP_045911" FT VAR_SEQ 969..1016 FT /note="Missing (in isoform 4)" FT /evidence="ECO:0000303|PubMed:14702039" FT /id="VSP_045912" FT VAR_SEQ 1053..1101 FT /note="Missing (in isoform 4 and isoform 5)" FT /evidence="ECO:0000303|PubMed:14702039" FT /id="VSP_045913" FT VARIANT 625 FT /note="S -> P (in dbSNP:rs1052486)" FT /evidence="ECO:0000269|PubMed:14574404, FT ECO:0000269|PubMed:14702039, ECO:0000269|PubMed:2156268, FT ECO:0000269|Ref.5, ECO:0000269|Ref.7" FT /id="VAR_023531" FT VARIANT 728 FT /note="A -> V (in dbSNP:rs11548856)" FT /id="VAR_037150" FT MUTAGEN 1001 FT /note="D->A: Abolishes cleavage by the caspase CASP3." FT /evidence="ECO:0000269|PubMed:14960581" FT MUTAGEN 1010 FT /note="W->A: Decreases interaction with GET4. Localizes in FT the nucleus and cytoplasm. Decreases interaction with GET4, FT localizes in the nucleus and increases GET4 ubiquitination; FT when associated with A-1042." FT /evidence="ECO:0000269|PubMed:29042515" FT MUTAGEN 1018 FT /note="W->A: Decreases interaction with GET4. Localizes in FT the nucleus. Decreases interaction with GET4, localizes in FT the nucleus and increases GET4 ubiquitination; when FT associated with A-1042." FT /evidence="ECO:0000269|PubMed:29042515" FT MUTAGEN 1030..1031 FT /note="RK->SL: No effect on interaction with GET4 and FT KPNA2." FT /evidence="ECO:0000269|PubMed:29042515" FT MUTAGEN 1042 FT /note="Y->A: Decreases interaction with GET4. Localizes in FT the nucleus. Decreases interaction with GET4, localizes in FT the nucleus and increases GET4 ubiquitination; when FT associated with A-1010 or A-1018." FT /evidence="ECO:0000269|PubMed:29042515" FT MUTAGEN 1049..1050 FT /note="KR->SL: No effect on interaction with GET4. Inhibits FT interaction with KPNA2." FT /evidence="ECO:0000269|PubMed:29042515" FT MUTAGEN 1067 FT /note="V->R: No effect on interaction with UBL4A. No effect FT on interaction with UBL4A; when associated with A-1078. FT Abolishes on interaction with UBL4A; when associated with FT R-1085." FT /evidence="ECO:0000269|PubMed:25713138" FT MUTAGEN 1078 FT /note="P->A: No effect on interaction with UBL4A. No effect FT on interaction with UBL4A; when associated with R-1067 or FT R-1085." FT /evidence="ECO:0000269|PubMed:25713138" FT MUTAGEN 1085 FT /note="L->R: No effect on interaction with UBL4A. No effect FT on interaction with UBL4A; when associated with R-1078. FT Abolishes on interaction with UBL4A; when associated with FT R-1067." FT /evidence="ECO:0000269|PubMed:25713138" FT MUTAGEN 1088 FT /note="D->H: No effect on interaction with UBL4A." FT /evidence="ECO:0000269|PubMed:25713138" FT CONFLICT 43 FT /note="K -> R (in Ref. 3; BAG65616)" FT /evidence="ECO:0000305" FT CONFLICT 47 FT /note="A -> R (in Ref. 1; AAA35587)" FT /evidence="ECO:0000305" FT CONFLICT 150 FT /note="H -> D (in Ref. 3; BAG65616)" FT /evidence="ECO:0000305" FT CONFLICT 511 FT /note="Q -> R (in Ref. 3; BAG65616)" FT /evidence="ECO:0000305" FT CONFLICT 561 FT /note="G -> D (in Ref. 3; BAG65616)" FT /evidence="ECO:0000305" FT CONFLICT 617 FT /note="P -> L (in Ref. 3; BAG65616)" FT /evidence="ECO:0000305" FT CONFLICT 679 FT /note="G -> R (in Ref. 3; BAG65616)" FT /evidence="ECO:0000305" FT CONFLICT 839 FT /note="L -> R (in Ref. 3; BAG63924)" FT /evidence="ECO:0000305" FT CONFLICT 842 FT /note="L -> P (in Ref. 3; BAG63924)" FT /evidence="ECO:0000305" FT CONFLICT 853 FT /note="V -> M (in Ref. 2; CAI46045)" FT /evidence="ECO:0000305" FT CONFLICT 854 FT /note="L -> Q (in Ref. 3; BAG65616)" FT /evidence="ECO:0000305" FT CONFLICT 927 FT /note="E -> D (in Ref. 3; BAG65616)" FT /evidence="ECO:0000305" FT STRAND 16..23 FT /evidence="ECO:0007829|PDB:4EEW" FT STRAND 28..34 FT /evidence="ECO:0007829|PDB:4EEW" FT STRAND 35..37 FT /evidence="ECO:0007829|PDB:2N9P" FT HELIX 39..50 FT /evidence="ECO:0007829|PDB:4EEW" FT HELIX 54..56 FT /evidence="ECO:0007829|PDB:4EEW" FT STRAND 57..61 FT /evidence="ECO:0007829|PDB:4EEW" FT STRAND 64..66 FT /evidence="ECO:0007829|PDB:2N9P" FT STRAND 68..71 FT /evidence="ECO:0007829|PDB:1WX9" FT HELIX 72..75 FT /evidence="ECO:0007829|PDB:4EEW" FT STRAND 80..86 FT /evidence="ECO:0007829|PDB:4EEW" FT TURN 91..93 FT /evidence="ECO:0007829|PDB:2N9P" FT HELIX 1009..1013 FT /evidence="ECO:0007829|PDB:6AU8" FT HELIX 1016..1018 FT /evidence="ECO:0007829|PDB:6AU8" FT HELIX 1019..1028 FT /evidence="ECO:0007829|PDB:6AU8" FT HELIX 1040..1043 FT /evidence="ECO:0007829|PDB:6AU8" FT HELIX 1063..1074 FT /evidence="ECO:0007829|PDB:4X86" FT HELIX 1082..1089 FT /evidence="ECO:0007829|PDB:4X86" FT HELIX 1092..1110 FT /evidence="ECO:0007829|PDB:4X86" FT MOD_RES P46379-4:832 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18669648" SQ SEQUENCE 1132 AA; 119409 MW; 625B5F86321367ED CRC64; MEPNDSTSTA VEEPDSLEVL VKTLDSQTRT FIVGAQMNVK EFKEHIAASV SIPSEKQRLI YQGRVLQDDK KLQEYNVGGK VIHLVERAPP QTHLPSGASS GTGSASATHG GGSPPGTRGP GASVHDRNAN SYVMVGTFNL PSDGSAVDVH INMEQAPIQS EPRVRLVMAQ HMIRDIQTLL SRMETLPYLQ CRGGPQPQHS QPPPQPPAVT PEPVALSSQT SEPVESEAPP REPMEAEEVE ERAPAQNPEL TPGPAPAGPT PAPETNAPNH PSPAEYVEVL QELQRLESRL QPFLQRYYEV LGAAATTDYN NNHEGREEDQ RLINLVGESL RLLGNTFVAL SDLRCNLACT PPRHLHVVRP MSHYTTPMVL QQAAIPIQIN VGTTVTMTGN GTRPPPTPNA EAPPPGPGQA SSVAPSSTNV ESSAEGAPPP GPAPPPATSH PRVIRISHQS VEPVVMMHMN IQDSGTQPGG VPSAPTGPLG PPGHGQTLGQ QVPGFPTAPT RVVIARPTPP QARPSHPGGP PVSGTLQGAG LGTNASLAQM VSGLVGQLLM QPVLVAQGTP GMAPPPAPAT ASASAGTTNT ATTAGPAPGG PAQPPPTPQP SMADLQFSQL LGNLLGPAGP GAGGSGVASP TITVAMPGVP AFLQGMTDFL QATQTAPPPP PPPPPPPPAP EQQTMPPPGS PSGGAGSPGG LGLESLSPEF FTSVVQGVLS SLLGSLGARA GSSESIAAFI QRLSGSSNIF EPGADGALGF FGALLSLLCQ NFSMVDVVML LHGHFQPLQR LQPQLRSFFH QHYLGGQEPT PSNIRMATHT LITGLEEYVR ESFSLVQVQP GVDIIRTNLE FLQEQFNSIA AHVLHCTDSG FGARLLELCN QGLFECLALN LHCLGGQQME LAAVINGRIR RMSRGVNPSL VSWLTTMMGL RLQVVLEHMP VGPDAILRYV RRVGDPPQPL PEEPMEVQGA ERASPEPQRE NASPAPGTTA EEAMSRGPPP APEGGSRDEQ DGASAETEPW AAAVPPEWVP IIQQDIQSQR KVKPQPPLSD AYLSGMPAKR RKTMQGEGPQ LLLSEAVSRA AKAAGARPLT SPESLSRDLE APEVQESYRQ QLRSDIQKRL QEDPNYSPQR FPNAQRAFAD DP //