BAG6_HUMAN
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 03-AUG-2022, entry version 205.
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 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 [43] {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 [44] {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 [45]
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 [46] {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).
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:28104892, PubMed:25535373).
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:28104892, PubMed:27193484). 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 Interacts with GET4; the interaction is direct and localizes BAG6 in
CC the cytosol (PubMed:21636303, PubMed:29042515). Interacts with UBL4A;
CC the interaction is direct and required for UBL4A protein stability
CC (PubMed:25713138). Interacts with AIFM1 (By similarity). Interacts with
CC HSPA2 (By similarity). Interacts with CTCFL (PubMed:18765639).
CC Interacts with p300/EP300 (PubMed:17403783). Interacts (via ubiquitin-
CC like domain) with RNF126; required for BAG6-dependent ubiquitination of
CC proteins mislocalized to the cytosol (PubMed:24981174,
CC PubMed:27193484). Interacts (via ubiquitin-like domain) with SGTA; SGTA
CC competes with RNF126 by binding the same region of BAG6, thereby
CC promoting deubiquitination of BAG6-target proteins and rescuing them
CC from degradation (PubMed:23129660, PubMed:24424410, PubMed:25179605,
CC PubMed:27193484). Interacts with ricin A chain (PubMed:14960581).
CC Interacts with VCP and AMFR; both form the VCP/p97-AMFR/gp78 complex
CC (PubMed:21636303). Interacts with SYVN1 (PubMed:21636303). Interacts
CC with USP13; the interaction is direct and may mediate UBL4A
CC deubiquitination (PubMed:24424410). Interacts with ZFAND2B
CC (PubMed:24160817, PubMed:26337389). Interacts with KPNA2
CC (PubMed:29042515). Interacts with UBQLN4 (PubMed:27113755).
CC {ECO:0000250|UniProtKB:Q9Z1R2, ECO:0000269|PubMed:14960581,
CC ECO:0000269|PubMed:17403783, ECO:0000269|PubMed:18765639,
CC ECO:0000269|PubMed:20676083, ECO:0000269|PubMed:21636303,
CC ECO:0000269|PubMed:23129660, ECO:0000269|PubMed:24160817,
CC ECO:0000269|PubMed:24424410, ECO:0000269|PubMed:24981174,
CC ECO:0000269|PubMed:25179605, ECO:0000269|PubMed:25713138,
CC ECO:0000269|PubMed:26337389, ECO:0000269|PubMed:27113755,
CC ECO:0000269|PubMed:27193484, ECO:0000269|PubMed:29042515}.
CC -!- SUBUNIT: (Microbial infection) Interacts with L. pneumophila Lpg2160
CC and LegU1 proteins. {ECO:0000269|PubMed:20547746}.
CC -!- INTERACTION:
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=6; 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: orf8a; 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; A0A024RCP2: DOM3Z; NbExp=3; IntAct=EBI-10988864, EBI-25847826;
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; 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; A0A0C4DFM3: PRUNE2; NbExp=3; IntAct=EBI-10988864, EBI-25830870;
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-742638;
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 -!- 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:28104892, PubMed:27193484). 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};
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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 PIR; A35098; A35098.
DR RefSeq; NP_001092004.1; NM_001098534.1. [P46379-2]
DR RefSeq; NP_001186626.1; NM_001199697.1. [P46379-4]
DR RefSeq; NP_001186627.1; NM_001199698.1. [P46379-5]
DR RefSeq; NP_004630.3; NM_004639.3.
DR RefSeq; NP_542433.1; NM_080702.2. [P46379-2]
DR RefSeq; NP_542434.1; NM_080703.2. [P46379-2]
DR RefSeq; XP_016866776.1; XM_017011287.1. [P46379-3]
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 SMR; P46379; -.
DR BioGRID; 113647; 425.
DR ComplexPortal; CPX-132; BAT3 complex.
DR CORUM; P46379; -.
DR DIP; DIP-31191N; -.
DR IntAct; P46379; 418.
DR MINT; P46379; -.
DR STRING; 9606.ENSP00000365131; -.
DR GlyGen; P46379; 2 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 EPD; P46379; -.
DR jPOST; P46379; -.
DR MassIVE; P46379; -.
DR MaxQB; P46379; -.
DR PaxDb; P46379; -.
DR PeptideAtlas; P46379; -.
DR PRIDE; P46379; -.
DR ProteomicsDB; 17045; -.
DR ProteomicsDB; 29168; -.
DR ProteomicsDB; 55736; -. [P46379-1]
DR ProteomicsDB; 55737; -. [P46379-2]
DR ProteomicsDB; 55738; -. [P46379-3]
DR Antibodypedia; 27346; 307 antibodies from 37 providers.
DR DNASU; 7917; -.
DR Ensembl; ENST00000211379.9; ENSP00000211379.5; ENSG00000204463.14. [P46379-2]
DR Ensembl; ENST00000361076.9; ENSP00000354368.5; ENSG00000096155.15. [P46379-1]
DR Ensembl; ENST00000362049.10; ENSP00000354875.6; ENSG00000204463.14. [P46379-5]
DR Ensembl; ENST00000375976.8; ENSP00000365143.4; ENSG00000204463.14. [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; ENSG00000204463.14. [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; ENSG00000204463.14. [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 CTD; 7917; -.
DR DisGeNET; 7917; -.
DR GeneCards; BAG6; -.
DR HGNC; HGNC:13919; BAG6.
DR HPA; ENSG00000204463; Low tissue specificity.
DR MIM; 142590; gene.
DR neXtProt; NX_P46379; -.
DR OpenTargets; ENSG00000204463; -.
DR PharmGKB; PA25264; -.
DR VEuPathDB; HostDB:ENSG00000204463; -.
DR eggNOG; KOG4248; Eukaryota.
DR GeneTree; ENSGT00390000016199; -.
DR HOGENOM; CLU_012159_0_0_1; -.
DR InParanoid; P46379; -.
DR OrthoDB; 1233552at2759; -.
DR PhylomeDB; P46379; -.
DR TreeFam; TF328437; -.
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 BioGRID-ORCS; 7917; 43 hits in 1084 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 93 other tissues.
DR ExpressionAtlas; P46379; baseline and differential.
DR Genevisible; P46379; HS.
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:UniProtKB.
DR GO; GO:0070062; C:extracellular exosome; IDA:UniProtKB.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; IDA:HPA.
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:0031593; F:polyubiquitin modification-dependent protein binding; ISS:UniProtKB.
DR GO; GO:0070628; F:proteasome binding; ISS:UniProtKB.
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:0071712; P:ER-associated misfolded protein catabolic process; 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:1904378; P:maintenance of unfolded protein involved in ERAD pathway; 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: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:1904379; P:protein localization to cytosolic proteasome complex involved in ERAD pathway; NAS:ParkinsonsUK-UCL.
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:0030433; P:ubiquitin-dependent ERAD pathway; IDA:UniProtKB.
DR GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; IDA:ComplexPortal.
DR InterPro; IPR021925; BAG6.
DR InterPro; IPR000626; Ubiquitin-like_dom.
DR InterPro; IPR029071; Ubiquitin-like_domsf.
DR InterPro; IPR019954; Ubiquitin_CS.
DR Pfam; PF12057; BAG6; 1.
DR Pfam; PF00240; ubiquitin; 1.
DR SMART; SM00213; UBQ; 1.
DR SUPFAM; SSF54236; SSF54236; 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; Reference proteome; Repeat; Secreted; Spermatogenesis;
KW 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 93..111
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 197..211
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 228..244
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 249..268
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 396..410
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 571..586
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 654..683
FT /note="Pro residues"
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
