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Large proline-rich protein BAG6 (BAG family molecular chaperone regulator 6) (BCL2-associated athanogene 6) (BAG-6) (HLA-B-associated transcript 3) (Protein G3) (Protein Scythe)

 BAG6_HUMAN              Reviewed;        1132 AA.
P46379; A2ADJ7; A3KQ42; A3KQ44; A6NGY6; A6PWF7; B0UX84; B4DZ12;
B4E3V4; E7EMZ4; F8VXY4; O95874; Q5HYL9; Q5SQ35; Q5SQ36; Q5SQ37;
Q5SQ41; Q5SRP8; Q5SRP9; Q5STC1; Q5STX1; Q5STX3; Q96SA6; Q9BCN4;
01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
27-SEP-2005, sequence version 2.
18-JUL-2018, entry version 177.
RecName: Full=Large proline-rich protein BAG6 {ECO:0000305};
AltName: Full=BAG family molecular chaperone regulator 6;
AltName: Full=BCL2-associated athanogene 6 {ECO:0000312|HGNC:HGNC:13919};
Short=BAG-6;
AltName: Full=HLA-B-associated transcript 3 {ECO:0000303|PubMed:2156268};
AltName: Full=Protein G3;
AltName: Full=Protein Scythe {ECO:0000303|PubMed:17403783};
Name=BAG6 {ECO:0000312|HGNC:HGNC:13919};
Synonyms=BAT3 {ECO:0000303|PubMed:2156268}, G3;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORM 1), VARIANT PRO-625,
AND REPEAT.
TISSUE=T-cell;
PubMed=2156268; DOI=10.1073/pnas.87.6.2374;
Banerji J., Sands J., Strominger J.L., Spies T.;
"A gene pair from the human major histocompatibility complex encodes
large proline-rich proteins with multiple repeated motifs and a single
ubiquitin-like domain.";
Proc. Natl. Acad. Sci. U.S.A. 87:2374-2378(1990).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
TISSUE=Endometrium;
PubMed=17974005; DOI=10.1186/1471-2164-8-399;
Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H.,
Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K.,
Ottenwaelder B., Poustka A., Wiemann S., Schupp I.;
"The full-ORF clone resource of the German cDNA consortium.";
BMC Genomics 8:399-399(2007).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 4 AND 5), AND VARIANT
PRO-625.
TISSUE=Testis;
PubMed=14702039; DOI=10.1038/ng1285;
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=14656967; DOI=10.1101/gr.1736803;
Xie T., Rowen L., Aguado B., Ahearn M.E., Madan A., Qin S.,
Campbell R.D., Hood L.;
"Analysis of the gene-dense major histocompatibility complex class III
region and its comparison to mouse.";
Genome Res. 13:2621-2636(2003).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND VARIANT PRO-625.
Hirakawa M., Yamaguchi H., Imai K., Shimada J., Shiina S., Tamiya G.,
Oka A., Inoko H.;
"Homo sapiens 2,229,817bp genomic DNA of 6p21.3 HLA class I region.";
Submitted (DEC-2004) to the EMBL/GenBank/DDBJ databases.
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND VARIANT PRO-625.
PubMed=14574404; DOI=10.1038/nature02055;
Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L.,
Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E.,
Gilbert J.G.R., Clamp M.E., Bethel G., Milne S., Ainscough R.,
Almeida J.P., Ambrose K.D., Andrews T.D., Ashwell R.I.S.,
Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Barker D.J.,
Barlow K.F., Bates K., Beare D.M., Beasley H., Beasley O., Bird C.P.,
Blakey S.E., Bray-Allen S., Brook J., Brown A.J., Brown J.Y.,
Burford D.C., Burrill W., Burton J., Carder C., Carter N.P.,
Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V.,
Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J.,
Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E.,
Ellington A.E., Evans K.A., Faulkner L., Francis M.D., Frankish A.,
Frankland J., French L., Garner P., Garnett J., Ghori M.J.,
Gilby L.M., Gillson C.J., Glithero R.J., Grafham D.V., Grant M.,
Gribble S., Griffiths C., Griffiths M.N.D., Hall R., Halls K.S.,
Hammond S., Harley J.L., Hart E.A., Heath P.D., Heathcott R.,
Holmes S.J., Howden P.J., Howe K.L., Howell G.R., Huckle E.,
Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., Joy A.A.,
Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., Langford C.,
Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., Lloyd D.M.,
Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M.,
Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K.,
McMurray A., Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T.,
Novik K.L., Oliver K., Overton-Larty E.K., Parker A., Patel R.,
Pearce A.V., Peck A.I., Phillimore B.J.C.T., Phillips S., Plumb R.W.,
Porter K.M., Ramsey Y., Ranby S.A., Rice C.M., Ross M.T., Searle S.M.,
Sehra H.K., Sheridan E., Skuce C.D., Smith S., Smith M., Spraggon L.,
Squares S.L., Steward C.A., Sycamore N., Tamlyn-Hall G., Tester J.,
Theaker A.J., Thomas D.W., Thorpe A., Tracey A., Tromans A., Tubby B.,
Wall M., Wallis J.M., West A.P., White S.S., Whitehead S.L.,
Whittaker H., Wild A., Willey D.J., Wilmer T.E., Wood J.M., Wray P.W.,
Wyatt J.C., Young L., Younger R.M., Bentley D.R., Coulson A.,
Durbin R.M., Hubbard T., Sulston J.E., Dunham I., Rogers J., Beck S.;
"The DNA sequence and analysis of human chromosome 6.";
Nature 425:805-811(2003).
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND VARIANT PRO-625.
Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
[8]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
TISSUE=Kidney;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[9]
FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH RICIN A CHAIN,
MUTAGENESIS OF ASP-1001, AND CLEAVAGE BY CASP3.
PubMed=14960581; DOI=10.1074/jbc.M307049200;
Wu Y.-H., Shih S.-F., Lin J.-Y.;
"Ricin triggers apoptotic morphological changes through caspase-3
cleavage of BAT3.";
J. Biol. Chem. 279:19264-19275(2004).
[10]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,
Mann M.;
"Global, in vivo, and site-specific phosphorylation dynamics in
signaling networks.";
Cell 127:635-648(2006).
[11]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1117, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=16964243; DOI=10.1038/nbt1240;
Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.;
"A probability-based approach for high-throughput protein
phosphorylation analysis and site localization.";
Nat. Biotechnol. 24:1285-1292(2006).
[12]
FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH EP300.
PubMed=17403783; DOI=10.1101/gad.1534107;
Sasaki T., Gan E.C., Wakeham A., Kornbluth S., Mak T.W., Okada H.;
"HLA-B-associated transcript 3 (Bat3)/Scythe is essential for p300-
mediated acetylation of p53.";
Genes Dev. 21:848-861(2007).
[13]
FUNCTION IN NK CELL ACTIVATION, AND SUBCELLULAR LOCATION.
PubMed=18055229; DOI=10.1016/j.immuni.2007.10.010;
Pogge von Strandmann E., Simhadri V.R., von Tresckow B., Sasse S.,
Reiners K.S., Hansen H.P., Rothe A., Boll B., Simhadri V.L.,
Borchmann P., McKinnon P.J., Hallek M., Engert A.;
"Human leukocyte antigen-B-associated transcript 3 is released from
tumor cells and engages the NKp30 receptor on natural killer cells.";
Immunity 27:965-974(2007).
[14]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-113, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=17924679; DOI=10.1021/pr070152u;
Yu L.R., Zhu Z., Chan K.C., Issaq H.J., Dimitrov D.S., Veenstra T.D.;
"Improved titanium dioxide enrichment of phosphopeptides from HeLa
cells and high confident phosphopeptide identification by cross-
validation of MS/MS and MS/MS/MS spectra.";
J. Proteome Res. 6:4150-4162(2007).
[15]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-973, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Platelet;
PubMed=18088087; DOI=10.1021/pr0704130;
Zahedi R.P., Lewandrowski U., Wiesner J., Wortelkamp S., Moebius J.,
Schuetz C., Walter U., Gambaryan S., Sickmann A.;
"Phosphoproteome of resting human platelets.";
J. Proteome Res. 7:526-534(2008).
[16]
FUNCTION, AND INTERACTION WITH CTCFL.
PubMed=18765639; DOI=10.1128/MCB.00568-08;
Nguyen P., Bar-Sela G., Sun L., Bisht K.S., Cui H., Kohn E.,
Feinberg A.P., Gius D.;
"BAT3 and SET1A form a complex with CTCFL/BORIS to modulate H3K4
histone dimethylation and gene expression.";
Mol. Cell. Biol. 28:6720-6729(2008).
[17]
FUNCTION IN NK CELL ACTIVATION, SUBCELLULAR LOCATION, AND TISSUE
SPECIFICITY.
PubMed=18852879; DOI=10.1371/journal.pone.0003377;
Simhadri V.R., Reiners K.S., Hansen H.P., Topolar D., Simhadri V.L.,
Nohroudi K., Kufer T.A., Engert A., Pogge von Strandmann E.;
"Dendritic cells release HLA-B-associated transcript-3 positive
exosomes to regulate natural killer function.";
PLoS ONE 3:E3377-E3377(2008).
[18]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-113; SER-973; SER-1081
AND SER-1117, PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-832
(ISOFORM 4), AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18669648; DOI=10.1073/pnas.0805139105;
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
Elledge S.J., Gygi S.P.;
"A quantitative atlas of mitotic phosphorylation.";
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
[19]
ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19413330; DOI=10.1021/ac9004309;
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,
Mohammed S.;
"Lys-N and trypsin cover complementary parts of the phosphoproteome in
a refined SCX-based approach.";
Anal. Chem. 81:4493-4501(2009).
[20]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-964 AND SER-973, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Leukemic T-cell;
PubMed=19690332; DOI=10.1126/scisignal.2000007;
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
Rodionov V., Han D.K.;
"Quantitative phosphoproteomic analysis of T cell receptor signaling
reveals system-wide modulation of protein-protein interactions.";
Sci. Signal. 2:RA46-RA46(2009).
[21]
UBIQUITINATION IN CASE OF INFECTION BY L.PNEUMOPHILA (MICROBIAL
INFECTION), AND INTERACTION WITH LPG2160 AND LEGU1 (MICROBIAL
INFECTION).
PubMed=20547746; DOI=10.1128/IAI.00344-10;
Ensminger A.W., Isberg R.R.;
"E3 ubiquitin ligase activity and targeting of BAT3 by multiple
Legionella pneumophila translocated substrates.";
Infect. Immun. 78:3905-3919(2010).
[22]
FUNCTION.
PubMed=20516149; DOI=10.1242/jcs.066738;
Leznicki P., Clancy A., Schwappach B., High S.;
"Bat3 promotes the membrane integration of tail-anchored proteins.";
J. Cell Sci. 123:2170-2178(2010).
[23]
FUNCTION, SUBCELLULAR LOCATION, RIBOSOME-BINDING, IDENTIFICATION BY
MASS SPECTROMETRY, AND IDENTIFICATION IN THE BAG6/BAT3 COMPLEX.
PubMed=20676083; DOI=10.1038/nature09296;
Mariappan M., Li X., Stefanovic S., Sharma A., Mateja A., Keenan R.J.,
Hegde R.S.;
"A ribosome-associating factor chaperones tail-anchored membrane
proteins.";
Nature 466:1120-1124(2010).
[24]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-350; SER-964; SER-973
AND SER-1117, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=20068231; DOI=10.1126/scisignal.2000475;
Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S.,
Mann M.;
"Quantitative phosphoproteomics reveals widespread full
phosphorylation site occupancy during mitosis.";
Sci. Signal. 3:RA3-RA3(2010).
[25]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21269460; DOI=10.1186/1752-0509-5-17;
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
"Initial characterization of the human central proteome.";
BMC Syst. Biol. 5:17-17(2011).
[26]
FUNCTION, INTERACTION WITH AMFR; GET4; SYVN1 AND VCP, AND SUBCELLULAR
LOCATION.
PubMed=21636303; DOI=10.1016/j.molcel.2011.05.010;
Wang Q., Liu Y., Soetandyo N., Baek K., Hegde R., Ye Y.;
"A ubiquitin ligase-associated chaperone holdase maintains
polypeptides in soluble states for proteasome degradation.";
Mol. Cell 42:758-770(2011).
[27]
FUNCTION, AND DOMAIN.
PubMed=21743475; DOI=10.1038/nature10181;
Hessa T., Sharma A., Mariappan M., Eshleman H.D., Gutierrez E.,
Hegde R.S.;
"Protein targeting and degradation are coupled for elimination of
mislocalized proteins.";
Nature 475:394-397(2011).
[28]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-964 AND SER-973, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21406692; DOI=10.1126/scisignal.2001570;
Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J.,
Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V.,
Blagoev B.;
"System-wide temporal characterization of the proteome and
phosphoproteome of human embryonic stem cell differentiation.";
Sci. Signal. 4:RS3-RS3(2011).
[29]
FUNCTION, AND INTERACTION WITH SGTA.
PubMed=23129660; DOI=10.1073/pnas.1209997109;
Leznicki P., High S.;
"SGTA antagonizes BAG6-mediated protein triage.";
Proc. Natl. Acad. Sci. U.S.A. 109:19214-19219(2012).
[30]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-113; SER-964; SER-973;
THR-1053; SER-1081 AND SER-1117, AND IDENTIFICATION BY MASS
SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma, and Erythroleukemia;
PubMed=23186163; DOI=10.1021/pr300630k;
Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
Mohammed S.;
"Toward a comprehensive characterization of a human cancer cell
phosphoproteome.";
J. Proteome Res. 12:260-271(2013).
[31]
INTERACTION WITH ZFAND2B.
PubMed=24160817; DOI=10.1042/BJ20130710;
Glinka T., Alter J., Braunstein I., Tzach L., Wei Sheng C.,
Geifman S., Edelmann M.J., Kessler B.M., Stanhill A.;
"Signal-peptide-mediated translocation is regulated by a p97-AIRAPL
complex.";
Biochem. J. 457:253-261(2014).
[32]
INTERACTION WITH SGTA AND USP13.
PubMed=24424410; DOI=10.7554/eLife.01369;
Liu Y., Soetandyo N., Lee J.G., Liu L., Xu Y., Clemons W.M. Jr.,
Ye Y.;
"USP13 antagonizes gp78 to maintain functionality of a chaperone in
ER-associated degradation.";
Elife 3:E01369-E01369(2014).
[33]
FUNCTION, AND INTERACTION WITH SGTA.
PubMed=25179605; DOI=10.1242/jcs.155648;
Wunderley L., Leznicki P., Payapilly A., High S.;
"SGTA regulates the cytosolic quality control of hydrophobic
substrates.";
J. Cell Sci. 127:4728-4739(2014).
[34]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-96 AND THR-117, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D.,
Wang L., Ye M., Zou H.;
"An enzyme assisted RP-RPLC approach for in-depth analysis of human
liver phosphoproteome.";
J. Proteomics 96:253-262(2014).
[35]
FUNCTION, INTERACTION WITH RNF126, AND DOMAIN.
PubMed=24981174; DOI=10.1016/j.molcel.2014.05.025;
Rodrigo-Brenni M.C., Gutierrez E., Hegde R.S.;
"Cytosolic quality control of mislocalized proteins requires RNF126
recruitment to Bag6.";
Mol. Cell 55:227-237(2014).
[36]
FUNCTION.
PubMed=26565908; DOI=10.1016/j.celrep.2015.09.047;
Kadowaki H., Nagai A., Maruyama T., Takami Y., Satrimafitrah P.,
Kato H., Honda A., Hatta T., Natsume T., Sato T., Kai H., Ichijo H.,
Nishitoh H.;
"Pre-emptive quality control protects the ER from protein overload via
the proximity of ERAD components and SRP.";
Cell Rep. 13:944-956(2015).
[37]
INTERACTION WITH ZFAND2B.
PubMed=26337389; DOI=10.1091/mbc.E15-02-0085;
Braunstein I., Zach L., Allan S., Kalies K.U., Stanhill A.;
"Proteasomal degradation of preemptive quality control (pQC)
substrates is mediated by an AIRAPL-p97 complex.";
Mol. Biol. Cell 26:3719-3727(2015).
[38]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=25944712; DOI=10.1002/pmic.201400617;
Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M.,
Ayoub D., Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
"N-terminome analysis of the human mitochondrial proteome.";
Proteomics 15:2519-2524(2015).
[39]
FUNCTION.
PubMed=26692333; DOI=10.1038/nm.4013;
Osorio F.G., Soria-Valles C., Santiago-Fernandez O., Bernal T.,
Mittelbrunn M., Colado E., Rodriguez F., Bonzon-Kulichenko E.,
Vazquez J., Porta-de-la-Riva M., Ceron J., Fueyo A., Li J.,
Green A.R., Freije J.M., Lopez-Otin C.;
"Loss of the proteostasis factor AIRAPL causes myeloid transformation
by deregulating IGF-1 signaling.";
Nat. Med. 22:91-96(2016).
[40]
FUNCTION, DOMAIN, AND REGION.
PubMed=28104892; DOI=10.1126/science.aah6130;
Shao S., Rodrigo-Brenni M.C., Kivlen M.H., Hegde R.S.;
"Mechanistic basis for a molecular triage reaction.";
Science 355:298-302(2017).
[41]
STRUCTURE BY NMR OF 17-89.
RIKEN structural genomics initiative (RSGI);
"Solution structure of the N-terminal ubiquitin-like domain in the
human BAT3 protein.";
Submitted (JUL-2005) to the PDB data bank.
[42] {ECO:0000244|PDB:4X86}
X-RAY CRYSTALLOGRAPHY (1.85 ANGSTROMS) OF 1048-1123 IN COMPLEX WITH
UBL4A, INTERACTION WITH UBL4A, AND MUTAGENESIS OF VAL-1067; PRO-1078;
LEU-1085 AND ASP-1088.
PubMed=25713138; DOI=10.1074/jbc.M114.631804;
Kuwabara N., Minami R., Yokota N., Matsumoto H., Senda T.,
Kawahara H., Kato R.;
"Structure of a BAG6 (Bcl-2-associated athanogene 6)-Ubl4a (ubiquitin-
like protein 4a) complex reveals a novel binding interface that
functions in tail-anchored protein biogenesis.";
J. Biol. Chem. 290:9387-9398(2015).
[43] {ECO:0000244|PDB:4WWR}
X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS) OF 1060-1111 IN COMPLEX WITH
UBL4A, INTERACTION WITH GET4 AND UBL4A, FUNCTION, AND IDENTIFICATION
IN THE BAG6/BAT3 COMPLEX.
PubMed=25535373; DOI=10.1073/pnas.1402745112;
Mock J.Y., Chartron J.W., Zaslaver M., Xu Y., Ye Y., Clemons W.M. Jr.;
"Bag6 complex contains a minimal tail-anchor-targeting module and a
mock BAG domain.";
Proc. Natl. Acad. Sci. U.S.A. 112:106-111(2015).
[44]
STRUCTURE BY NMR OF 17-101 IN COMPLEX WITH RNF126, FUNCTION,
INTERACTION WITH RNF126 AND SGTA, AND DOMAIN.
PubMed=27193484; DOI=10.1038/srep26433;
Krysztofinska E.M., Martinez-Lumbreras S., Thapaliya A., Evans N.J.,
High S., Isaacson R.L.;
"Structural and functional insights into the E3 ligase, RNF126.";
Sci. Rep. 6:26433-26433(2016).
[45] {ECO:0000244|PDB:6AU8}
X-RAY CRYSTALLOGRAPHY (1.80 ANGSTROMS) OF 1008-1050 IN COMPLEX WITH
GET4, SUBCELLULAR LOCATION, INTERACTION WITH GET4 AND KPNA2, AND
MUTAGENESIS OF TRP-1010; TRP-1018; 1030-ARG-LYS-1031; TYR-1042 AND
1049-LYS-ARG-1050.
PubMed=29042515; DOI=10.1073/pnas.1702940114;
Mock J.Y., Xu Y., Ye Y., Clemons W.M. Jr.;
"Structural basis for regulation of the nucleo-cytoplasmic
distribution of Bag6 by TRC35.";
Proc. Natl. Acad. Sci. U.S.A. 114:11679-11684(2017).
-!- FUNCTION: ATP-independent molecular chaperone preventing the
aggregation of misfolded and hydrophobic patches-containing
proteins (PubMed:21636303). Functions as part of a cytosolic
protein quality control complex, the BAG6/BAT3 complex, which
maintains these client proteins in a soluble state and
participates to their proper delivery to the endoplasmic reticulum
or alternatively can promote their sorting to the proteasome where
they undergo degradation (PubMed:20516149, PubMed:21636303,
PubMed:21743475, PubMed:28104892). The BAG6/BAT3 complex is
involved in the post-translational delivery of tail-anchored/type
II transmembrane proteins to the endoplasmic reticulum membrane.
Recruited to ribosomes, it interacts with the transmembrane region
of newly synthesized tail-anchored proteins and together with SGTA
and ASNA1 mediates their delivery to the endoplasmic reticulum
(PubMed:20516149, PubMed:20676083, PubMed:28104892,
PubMed:25535373). Client proteins that cannot be properly
delivered to the endoplasmic reticulum are ubiquitinated by
RNF126, an E3 ubiquitin-protein ligase associated with BAG6 and
are sorted to the proteasome (PubMed:24981174, PubMed:28104892,
PubMed:27193484). SGTA which prevents the recruitment of RNF126 to
BAG6 may negatively regulate the ubiquitination and the
proteasomal degradation of client proteins (PubMed:23129660,
PubMed:25179605, PubMed:27193484). Similarly, the BAG6/BAT3
complex also functions as a sorting platform for proteins of the
secretory pathway that are mislocalized to the cytosol either
delivering them to the proteasome for degradation or to the
endoplasmic reticulum (PubMed:21743475). The BAG6/BAT3 complex
also plays a role in the endoplasmic reticulum-associated
degradation (ERAD), a quality control mechanism that eliminates
unwanted proteins of the endoplasmic reticulum through their
retrotranslocation to the cytosol and their targeting to the
proteasome. It maintains these retrotranslocated proteins in an
unfolded yet soluble state condition in the cytosol to ensure
their proper delivery to the proteasome (PubMed:21636303). BAG6 is
also required for selective ubiquitin-mediated degradation of
defective nascent chain polypeptides by the proteasome. In this
context, it may participate to the production of antigenic
peptides and play a role in antigen presentation in immune
response (By similarity). BAG6 is also involved in endoplasmic
reticulum stress-induced pre-emptive quality control, a mechanism
that selectively attenuates the translocation of newly synthesized
proteins into the endoplasmic reticulum and reroutes them to the
cytosol for proteasomal degradation. BAG6 may ensure the proper
degradation of these proteins and thereby protects the endoplasmic
reticulum from protein overload upon stress (PubMed:26565908). By
inhibiting the polyubiquitination and subsequent proteasomal
degradation of HSPA2 it may also play a role in the assembly of
the synaptonemal complex during spermatogenesis (By similarity).
Also positively regulates apoptosis by interacting with and
stabilizing the proapoptotic factor AIFM1 (By similarity). By
controlling the steady-state expression of the IGF1R receptor,
indirectly regulates the insulin-like growth factor receptor
signaling pathway (PubMed:26692333).
{ECO:0000250|UniProtKB:Q9Z1R2, ECO:0000269|PubMed:20516149,
ECO:0000269|PubMed:20676083, ECO:0000269|PubMed:21636303,
ECO:0000269|PubMed:21743475, ECO:0000269|PubMed:23129660,
ECO:0000269|PubMed:24981174, ECO:0000269|PubMed:25179605,
ECO:0000269|PubMed:26565908, ECO:0000269|PubMed:26692333,
ECO:0000269|PubMed:27193484, ECO:0000269|PubMed:28104892}.
-!- FUNCTION: Involved in DNA damage-induced apoptosis: following DNA
damage, accumulates in the nucleus and forms a complex with
p300/EP300, enhancing p300/EP300-mediated p53/TP53 acetylation
leading to increase p53/TP53 transcriptional activity
(PubMed:17403783). When nuclear, may also act as a component of
some chromatin regulator complex that regulates histone 3 'Lys-4'
dimethylation (H3K4me2) (PubMed:18765639).
{ECO:0000269|PubMed:17403783, ECO:0000269|PubMed:18765639}.
-!- FUNCTION: Released extracellularly via exosomes, it is a ligand of
the natural killer/NK cells receptor NCR3 and stimulates NK cells
cytotoxicity. It may thereby trigger NK cells cytotoxicity against
neighboring tumor cells and immature myeloid dendritic cells (DC).
{ECO:0000269|PubMed:18055229, ECO:0000269|PubMed:18852879}.
-!- FUNCTION: Mediates ricin-induced apoptosis.
{ECO:0000269|PubMed:14960581}.
-!- SUBUNIT: Component of the BAG6/BAT3 complex, also named BAT3
complex, at least composed of BAG6, UBL4A and GET4/TRC35
(PubMed:20676083). Interacts with GET4; the interaction is direct
and localizes BAG6 in the cytosol (PubMed:21636303,
PubMed:29042515). Interacts with UBL4A; the interaction is direct
and required for UBL4A protein stability (PubMed:25713138).
Interacts with AIFM1 (By similarity). Interacts with HSPA2 (By
similarity). Interacts with CTCFL (PubMed:18765639). Interacts
with p300/EP300 (PubMed:17403783). Interacts (via ubiquitin-like
domain) with RNF126; required for BAG6-dependent ubiquitination of
proteins mislocalized to the cytosol (PubMed:24981174,
PubMed:27193484). Interacts (via ubiquitin-like domain) with SGTA;
SGTA competes with RNF126 by binding the same region of BAG6,
thereby promoting deubiquitination of BAG6-target proteins and
rescuing them from degradation (PubMed:23129660, PubMed:24424410,
PubMed:25179605, PubMed:27193484). Interacts with ricin A chain
(PubMed:14960581). Interacts with VCP and AMFR; both form the
VCP/p97-AMFR/gp78 complex (PubMed:21636303). Interacts with SYVN1
(PubMed:21636303). Interacts with USP13; the interaction is direct
and may mediate UBL4A deubiquitination (PubMed:24424410).
Interacts with ZFAND2B (PubMed:24160817, PubMed:26337389,
PubMed:14960581, PubMed:17403783, PubMed:18765639,
PubMed:20676083, PubMed:21636303, PubMed:23129660,
PubMed:24424410, PubMed:24981174, PubMed:25179605,
PubMed:27193484, PubMed:25713138, PubMed:29042515) (By
similarity). Interacts with KPNA2 (PubMed:29042515).
{ECO:0000250|UniProtKB:Q9Z1R2, ECO:0000269|PubMed:14960581,
ECO:0000269|PubMed:17403783, ECO:0000269|PubMed:18765639,
ECO:0000269|PubMed:20676083, ECO:0000269|PubMed:21636303,
ECO:0000269|PubMed:23129660, ECO:0000269|PubMed:24160817,
ECO:0000269|PubMed:24424410, ECO:0000269|PubMed:24981174,
ECO:0000269|PubMed:25179605, ECO:0000269|PubMed:25713138,
ECO:0000269|PubMed:26337389, ECO:0000269|PubMed:27193484,
ECO:0000269|PubMed:29042515}.
-!- SUBUNIT: (Microbial infection) Interacts with L. pneumophila
Lpg2160 and LegU1 proteins. {ECO:0000269|PubMed:20547746}.
-!- INTERACTION:
P11802:CDK4; NbExp=2; IntAct=EBI-347552, EBI-295644;
P23285:CPR2 (xeno); NbExp=3; IntAct=EBI-10988864, EBI-5448;
P35176:CPR5 (xeno); NbExp=3; IntAct=EBI-10988864, EBI-5458;
Q12805:EFEMP1; NbExp=3; IntAct=EBI-347552, EBI-536772;
Q8IZU0:FAM9B; NbExp=3; IntAct=EBI-347552, EBI-10175124;
Q53G59:KLHL12; NbExp=4; IntAct=EBI-347552, EBI-740929;
Q7Z434:MAVS; NbExp=2; IntAct=EBI-347552, EBI-995373;
O14931:NCR3; NbExp=6; IntAct=EBI-347552, EBI-14989262;
O14931-1:NCR3; NbExp=5; IntAct=EBI-9640181, EBI-15013584;
Q9BV68:RNF126; NbExp=4; IntAct=EBI-347552, EBI-357322;
O43765:SGTA; NbExp=5; IntAct=EBI-347552, EBI-347996;
Q12800:TFCP2; NbExp=3; IntAct=EBI-347552, EBI-717422;
P43552:YFL051C (xeno); NbExp=3; IntAct=EBI-10988864, EBI-22855;
-!- SUBCELLULAR LOCATION: Cytoplasm, cytosol
{ECO:0000269|PubMed:17403783, ECO:0000269|PubMed:20676083,
ECO:0000269|PubMed:21636303, ECO:0000269|PubMed:29042515}. Nucleus
{ECO:0000269|PubMed:14960581, ECO:0000269|PubMed:17403783,
ECO:0000269|PubMed:21636303, ECO:0000269|PubMed:29042515}.
Secreted, exosome {ECO:0000269|PubMed:18055229,
ECO:0000269|PubMed:18852879}. Note=Normally localized in cytosol
and nucleus, it can also be released extracellularly, in exosomes,
by tumor and myeloid dendritic cells (PubMed:18055229,
PubMed:18852879). Cytoplasmic retention is due to interaction with
GET4 (PubMed:29042515). {ECO:0000269|PubMed:18055229,
ECO:0000269|PubMed:18852879, ECO:0000269|PubMed:29042515}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=5;
Name=1;
IsoId=P46379-1; Sequence=Displayed;
Name=2;
IsoId=P46379-2; Sequence=VSP_015695;
Name=3;
IsoId=P46379-3; Sequence=VSP_015695, VSP_030519;
Note=No experimental confirmation available.;
Name=4;
IsoId=P46379-4; Sequence=VSP_015695, VSP_045910, VSP_045911,
VSP_045912, VSP_045913;
Note=No experimental confirmation available. Contains a
phosphoserine at position 832. {ECO:0000244|PubMed:18669648};
Name=5;
IsoId=P46379-5; Sequence=VSP_015695, VSP_045913;
Note=No experimental confirmation available.;
-!- TISSUE SPECIFICITY: Expressed by immature dendritic cells (at
protein level). {ECO:0000269|PubMed:18852879}.
-!- DOMAIN: The ubiquitin-like domain mediates interaction with the E3
ubiquitin-protein ligase RNF126 which is responsible for the BAG6-
dependent ubiquitination of client proteins (PubMed:21743475,
PubMed:24981174, PubMed:28104892, PubMed:27193484). SGTA also
binds this domain and competes with RNF126 to antagonize client
protein ubiquitination and degradation (PubMed:28104892). The
ubiquitin-like domain also mediates the interaction with USP13
(PubMed:24424410). {ECO:0000269|PubMed:21743475,
ECO:0000269|PubMed:24424410, ECO:0000269|PubMed:24981174,
ECO:0000269|PubMed:27193484, ECO:0000269|PubMed:28104892}.
-!- PTM: Ricin can induce a cleavage by the caspase CASP3. The
released C-terminal peptide induces apoptosis.
{ECO:0000269|PubMed:14960581}.
-!- PTM: (Microbial infection) In case of infection by L.pneumophila,
ubiquitinated by the SCF(LegU1) complex.
{ECO:0000269|PubMed:20547746}.
-!- SEQUENCE CAUTION:
Sequence=AAD18085.1; Type=Erroneous initiation; Note=Translation N-terminally shortened.; Evidence={ECO:0000305};
Sequence=BAB63390.1; Type=Erroneous initiation; Note=Translation N-terminally shortened.; Evidence={ECO:0000305};
Sequence=CAI18318.2; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
-----------------------------------------------------------------------
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EMBL; M33519; AAA35587.1; -; mRNA.
EMBL; M33521; AAA35588.1; -; Genomic_DNA.
EMBL; M33520; AAA35588.1; JOINED; Genomic_DNA.
EMBL; BX647244; CAI46045.1; -; mRNA.
EMBL; AK302695; BAG63924.1; -; mRNA.
EMBL; AK304879; BAG65616.1; -; mRNA.
EMBL; AF129756; AAD18085.1; ALT_INIT; Genomic_DNA.
EMBL; BA000025; BAB63390.1; ALT_INIT; Genomic_DNA.
EMBL; AL662801; CAI18314.1; -; Genomic_DNA.
EMBL; AL662801; CAI18315.1; -; Genomic_DNA.
EMBL; AL662801; CAI18316.2; -; Genomic_DNA.
EMBL; AL662801; CAI18318.2; ALT_SEQ; Genomic_DNA.
EMBL; AL662847; CAI17658.1; -; Genomic_DNA.
EMBL; AL670886; CAI17658.1; JOINED; Genomic_DNA.
EMBL; AL662847; CAI17659.1; -; Genomic_DNA.
EMBL; AL670886; CAI17659.1; JOINED; Genomic_DNA.
EMBL; AL670886; CAI17784.1; -; Genomic_DNA.
EMBL; AL662847; CAI17784.1; JOINED; Genomic_DNA.
EMBL; AL670886; CAI17785.1; -; Genomic_DNA.
EMBL; AL662847; CAI17785.1; JOINED; Genomic_DNA.
EMBL; AL670886; CAI17786.1; -; Genomic_DNA.
EMBL; AL662847; CAI17786.1; JOINED; Genomic_DNA.
EMBL; AL805934; CAI18501.1; -; Genomic_DNA.
EMBL; AL805934; CAI18504.1; -; Genomic_DNA.
EMBL; AL805934; CAI18508.2; -; Genomic_DNA.
EMBL; AL805934; CAI18509.1; -; Genomic_DNA.
EMBL; AL670886; CAM25014.1; -; Genomic_DNA.
EMBL; AL662847; CAM25014.1; JOINED; Genomic_DNA.
EMBL; BX511262; CAM45799.1; -; Genomic_DNA.
EMBL; BX511262; CAM45800.1; -; Genomic_DNA.
EMBL; BX511262; CAM45801.1; -; Genomic_DNA.
EMBL; AL662847; CAO72072.1; -; Genomic_DNA.
EMBL; AL670886; CAO72072.1; JOINED; Genomic_DNA.
EMBL; CR753842; CAQ06558.1; -; Genomic_DNA.
EMBL; CR753892; CAQ06558.1; JOINED; Genomic_DNA.
EMBL; CR753892; CAQ06931.1; -; Genomic_DNA.
EMBL; CR753842; CAQ06931.1; JOINED; Genomic_DNA.
EMBL; CR354443; CAQ06977.1; -; Genomic_DNA.
EMBL; CR759761; CAQ10854.1; -; Genomic_DNA.
EMBL; CH471081; EAX03455.1; -; Genomic_DNA.
EMBL; BC003133; AAH03133.1; -; mRNA.
CCDS; CCDS4709.1; -. [P46379-2]
CCDS; CCDS47403.1; -. [P46379-1]
CCDS; CCDS56414.1; -. [P46379-4]
CCDS; CCDS56415.1; -. [P46379-5]
PIR; A35098; A35098.
RefSeq; NP_001092004.1; NM_001098534.1. [P46379-2]
RefSeq; NP_001186626.1; NM_001199697.1. [P46379-4]
RefSeq; NP_001186627.1; NM_001199698.1. [P46379-5]
RefSeq; NP_004630.3; NM_004639.3. [P46379-1]
RefSeq; NP_542433.1; NM_080702.2. [P46379-2]
RefSeq; NP_542434.1; NM_080703.2. [P46379-2]
RefSeq; XP_016866776.1; XM_017011287.1. [P46379-3]
UniGene; Hs.440900; -.
PDB; 1WX9; NMR; -; A=17-89.
PDB; 2N9P; NMR; -; C=17-101.
PDB; 4DWF; X-ray; 1.80 A; A/B=13-101.
PDB; 4EEW; X-ray; 1.30 A; A/B=1-87.
PDB; 4WWR; X-ray; 2.00 A; A/C/E/G=1060-1111.
PDB; 4X86; X-ray; 1.85 A; B=1048-1123.
PDB; 6AU8; X-ray; 1.80 A; C=1008-1050.
PDBsum; 1WX9; -.
PDBsum; 2N9P; -.
PDBsum; 4DWF; -.
PDBsum; 4EEW; -.
PDBsum; 4WWR; -.
PDBsum; 4X86; -.
PDBsum; 6AU8; -.
ProteinModelPortal; P46379; -.
SMR; P46379; -.
BioGrid; 113647; 297.
ComplexPortal; CPX-132; BAT3 complex.
CORUM; P46379; -.
DIP; DIP-31191N; -.
IntAct; P46379; 268.
MINT; P46379; -.
STRING; 9606.ENSP00000365131; -.
iPTMnet; P46379; -.
PhosphoSitePlus; P46379; -.
SwissPalm; P46379; -.
BioMuta; BAG6; -.
DMDM; 76800648; -.
EPD; P46379; -.
MaxQB; P46379; -.
PaxDb; P46379; -.
PeptideAtlas; P46379; -.
PRIDE; P46379; -.
ProteomicsDB; 55736; -.
ProteomicsDB; 55737; -. [P46379-2]
ProteomicsDB; 55738; -. [P46379-3]
Ensembl; ENST00000211379; ENSP00000211379; ENSG00000204463. [P46379-2]
Ensembl; ENST00000361076; ENSP00000354368; ENSG00000096155. [P46379-1]
Ensembl; ENST00000362049; ENSP00000354875; ENSG00000204463. [P46379-5]
Ensembl; ENST00000375964; ENSP00000365131; ENSG00000204463. [P46379-1]
Ensembl; ENST00000375976; ENSP00000365143; ENSG00000204463. [P46379-2]
Ensembl; ENST00000383446; ENSP00000372938; ENSG00000096155. [P46379-2]
Ensembl; ENST00000383448; ENSP00000372940; ENSG00000096155. [P46379-2]
Ensembl; ENST00000417144; ENSP00000412110; ENSG00000229524. [P46379-2]
Ensembl; ENST00000419847; ENSP00000389121; ENSG00000233348. [P46379-2]
Ensembl; ENST00000439687; ENSP00000402856; ENSG00000204463. [P46379-4]
Ensembl; ENST00000442479; ENSP00000413698; ENSG00000229524. [P46379-2]
Ensembl; ENST00000443182; ENSP00000410156; ENSG00000233348. [P46379-2]
Ensembl; ENST00000449450; ENSP00000397894; ENSG00000229524. [P46379-1]
Ensembl; ENST00000451932; ENSP00000390966; ENSG00000233348. [P46379-1]
Ensembl; ENST00000551350; ENSP00000447546; ENSG00000229524. [P46379-5]
Ensembl; ENST00000552116; ENSP00000447946; ENSG00000233348. [P46379-5]
Ensembl; ENST00000552605; ENSP00000446525; ENSG00000096155. [P46379-5]
Ensembl; ENST00000613474; ENSP00000478966; ENSG00000227761. [P46379-4]
Ensembl; ENST00000615143; ENSP00000482413; ENSG00000229524. [P46379-4]
Ensembl; ENST00000615224; ENSP00000477951; ENSG00000228760. [P46379-4]
Ensembl; ENST00000615725; ENSP00000479238; ENSG00000233348. [P46379-4]
Ensembl; ENST00000617635; ENSP00000484238; ENSG00000096155. [P46379-4]
Ensembl; ENST00000621056; ENSP00000477867; ENSG00000234651. [P46379-4]
GeneID; 7917; -.
KEGG; hsa:7917; -.
UCSC; uc003nvf.4; human. [P46379-1]
CTD; 7917; -.
DisGeNET; 7917; -.
EuPathDB; HostDB:ENSG00000204463.12; -.
GeneCards; BAG6; -.
H-InvDB; HIX0165051; -.
H-InvDB; HIX0166179; -.
H-InvDB; HIX0166289; -.
H-InvDB; HIX0166578; -.
H-InvDB; HIX0166832; -.
H-InvDB; HIX0167081; -.
H-InvDB; HIX0167222; -.
H-InvDB; HIX0167321; -.
H-InvDB; HIX0167461; -.
H-InvDB; HIX0167568; -.
HGNC; HGNC:13919; BAG6.
HPA; CAB020704; -.
HPA; HPA045116; -.
HPA; HPA053291; -.
MIM; 142590; gene.
neXtProt; NX_P46379; -.
OpenTargets; ENSG00000204463; -.
PharmGKB; PA25264; -.
eggNOG; KOG4248; Eukaryota.
eggNOG; ENOG410XS9P; LUCA.
GeneTree; ENSGT00390000016199; -.
HOVERGEN; HBG002193; -.
InParanoid; P46379; -.
OMA; PMVAPNA; -.
OrthoDB; EOG091G0XSR; -.
PhylomeDB; P46379; -.
TreeFam; TF328437; -.
ChiTaRS; BAG6; human.
EvolutionaryTrace; P46379; -.
GeneWiki; HLA-B_associated_transcript_3; -.
GenomeRNAi; 7917; -.
PMAP-CutDB; B0UX84; -.
PRO; PR:P46379; -.
Proteomes; UP000005640; Chromosome 6.
Bgee; ENSG00000204463; -.
ExpressionAtlas; P46379; baseline and differential.
Genevisible; P46379; HS.
GO; GO:0071818; C:BAT3 complex; IDA:UniProtKB.
GO; GO:0005737; C:cytoplasm; IDA:ParkinsonsUK-UCL.
GO; GO:0005829; C:cytosol; IDA:UniProtKB.
GO; GO:0070062; C:extracellular exosome; IDA:UniProtKB.
GO; GO:0043231; C:intracellular membrane-bounded organelle; IDA:HPA.
GO; GO:0016020; C:membrane; IDA:ParkinsonsUK-UCL.
GO; GO:0005654; C:nucleoplasm; IDA:HPA.
GO; GO:0005634; C:nucleus; IDA:UniProtKB.
GO; GO:0030544; F:Hsp70 protein binding; IEA:Ensembl.
GO; GO:0042802; F:identical protein binding; IPI:IntAct.
GO; GO:0051787; F:misfolded protein binding; IDA:ParkinsonsUK-UCL.
GO; GO:0031593; F:polyubiquitin modification-dependent protein binding; ISS:UniProtKB.
GO; GO:0070628; F:proteasome binding; ISS:UniProtKB.
GO; GO:0043022; F:ribosome binding; IDA:UniProtKB.
GO; GO:0005102; F:signaling receptor binding; IPI:UniProtKB.
GO; GO:0031625; F:ubiquitin protein ligase binding; IPI:UniProtKB.
GO; GO:1990381; F:ubiquitin-specific protease binding; IPI:ParkinsonsUK-UCL.
GO; GO:0006915; P:apoptotic process; IDA:UniProtKB.
GO; GO:0007420; P:brain development; ISS:UniProtKB.
GO; GO:0030154; P:cell differentiation; IEA:UniProtKB-KW.
GO; GO:0006325; P:chromatin organization; IEA:UniProtKB-KW.
GO; GO:0061857; P:endoplasmic reticulum stress-induced pre-emptive quality control; IMP:UniProtKB.
GO; GO:0071712; P:ER-associated misfolded protein catabolic process; IDA:UniProtKB.
GO; GO:0002429; P:immune response-activating cell surface receptor signaling pathway; IDA:UniProtKB.
GO; GO:0018393; P:internal peptidyl-lysine acetylation; IDA:UniProtKB.
GO; GO:0042771; P:intrinsic apoptotic signaling pathway in response to DNA damage by p53 class mediator; IMP:UniProtKB.
GO; GO:0070059; P:intrinsic apoptotic signaling pathway in response to endoplasmic reticulum stress; ISS:UniProtKB.
GO; GO:0001822; P:kidney development; ISS:UniProtKB.
GO; GO:0030324; P:lung development; ISS:UniProtKB.
GO; GO:1904378; P:maintenance of unfolded protein involved in ERAD pathway; IMP:ParkinsonsUK-UCL.
GO; GO:0030101; P:natural killer cell activation; IDA:UniProtKB.
GO; GO:0043066; P:negative regulation of apoptotic process; IEA:Ensembl.
GO; GO:0032435; P:negative regulation of proteasomal ubiquitin-dependent protein catabolic process; ISS:UniProtKB.
GO; GO:0045861; P:negative regulation of proteolysis; ISS:UniProtKB.
GO; GO:1904294; P:positive regulation of ERAD pathway; IMP:ParkinsonsUK-UCL.
GO; GO:0010498; P:proteasomal protein catabolic process; IMP:UniProtKB.
GO; GO:1904379; P:protein localization to cytosolic proteasome complex involved in ERAD pathway; NAS:ParkinsonsUK-UCL.
GO; GO:0050821; P:protein stabilization; ISS:UniProtKB.
GO; GO:0042127; P:regulation of cell proliferation; IEA:Ensembl.
GO; GO:0045995; P:regulation of embryonic development; ISS:UniProtKB.
GO; GO:0007283; P:spermatogenesis; ISS:UniProtKB.
GO; GO:0007130; P:synaptonemal complex assembly; ISS:UniProtKB.
GO; GO:0071816; P:tail-anchored membrane protein insertion into ER membrane; IDA:UniProtKB.
GO; GO:0030433; P:ubiquitin-dependent ERAD pathway; IDA:UniProtKB.
GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; ISS:UniProtKB.
InterPro; IPR021925; BAG6.
InterPro; IPR029071; Ubiquitin-like_domsf.
InterPro; IPR019954; Ubiquitin_CS.
InterPro; IPR000626; Ubiquitin_dom.
Pfam; PF12057; DUF3538; 1.
Pfam; PF00240; ubiquitin; 1.
SMART; SM00213; UBQ; 1.
SUPFAM; SSF54236; SSF54236; 1.
PROSITE; PS00299; UBIQUITIN_1; 1.
PROSITE; PS50053; UBIQUITIN_2; 1.
1: Evidence at protein level;
3D-structure; Acetylation; Alternative splicing; Apoptosis; Chaperone;
Chromatin regulator; Complete proteome; Cytoplasm; Differentiation;
Immunity; Nucleus; Phosphoprotein; Polymorphism; Reference proteome;
Repeat; Secreted; Spermatogenesis; Transport; Ubl conjugation.
CHAIN 1 1132 Large proline-rich protein BAG6.
/FTId=PRO_0000114897.
DOMAIN 17 92 Ubiquitin-like. {ECO:0000255|PROSITE-
ProRule:PRU00214}.
REPEAT 242 270 1. {ECO:0000303|PubMed:2156268}.
REPEAT 415 443 2. {ECO:0000303|PubMed:2156268}.
REPEAT 574 602 3. {ECO:0000303|PubMed:2156268}.
REPEAT 608 636 4. {ECO:0000303|PubMed:2156268}.
REGION 242 636 4 X 29 AA approximate repeats.
{ECO:0000303|PubMed:2156268}.
REGION 1010 1040 Required for interaction with GET4.
{ECO:0000269|PubMed:25535373,
ECO:0000269|PubMed:29042515}.
REGION 1022 1132 Sufficient for the delivery of client
proteins to the endoplasmic reticulum.
{ECO:0000269|PubMed:28104892}.
REGION 1058 1115 BAG-similar domain, required and
sufficient for interaction with UBL4A.
{ECO:0000269|PubMed:25535373,
ECO:0000269|PubMed:25713138}.
MOTIF 1012 1054 Nuclear localization site.
{ECO:0000305|PubMed:25535373,
ECO:0000305|PubMed:29042515}.
COMPBIAS 195 273 Pro-rich. {ECO:0000255|PROSITE-
ProRule:PRU00015}.
COMPBIAS 394 681 Pro-rich. {ECO:0000255|PROSITE-
ProRule:PRU00015}.
SITE 1001 1002 Cleavage; by CASP3.
{ECO:0000269|PubMed:14960581}.
MOD_RES 1 1 N-acetylmethionine.
{ECO:0000244|PubMed:19413330}.
MOD_RES 96 96 Phosphoserine.
{ECO:0000244|PubMed:24275569}.
MOD_RES 113 113 Phosphoserine.
{ECO:0000244|PubMed:17924679,
ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:23186163}.
MOD_RES 117 117 Phosphothreonine.
{ECO:0000244|PubMed:24275569}.
MOD_RES 350 350 Phosphothreonine.
{ECO:0000244|PubMed:20068231}.
MOD_RES 964 964 Phosphoserine.
{ECO:0000244|PubMed:19690332,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:21406692,
ECO:0000244|PubMed:23186163}.
MOD_RES 973 973 Phosphoserine.
{ECO:0000244|PubMed:18088087,
ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:19690332,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:21406692,
ECO:0000244|PubMed:23186163}.
MOD_RES 1053 1053 Phosphothreonine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 1081 1081 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:23186163}.
MOD_RES 1117 1117 Phosphoserine.
{ECO:0000244|PubMed:16964243,
ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:23186163}.
VAR_SEQ 185 190 Missing (in isoform 2, isoform 3, isoform
4 and isoform 5).
{ECO:0000303|PubMed:14702039,
ECO:0000303|PubMed:15489334,
ECO:0000303|PubMed:17974005}.
/FTId=VSP_015695.
VAR_SEQ 489 489 G -> GSTLIQLPSLPPEFMHAVAHQITHQAMVAAVASAAA
G (in isoform 3). {ECO:0000305}.
/FTId=VSP_030519.
VAR_SEQ 527 527 Missing (in isoform 4).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_045910.
VAR_SEQ 561 685 Missing (in isoform 4).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_045911.
VAR_SEQ 969 1016 Missing (in isoform 4).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_045912.
VAR_SEQ 1053 1101 Missing (in isoform 4 and isoform 5).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_045913.
VARIANT 625 625 S -> P (in dbSNP:rs1052486).
{ECO:0000269|PubMed:14574404,
ECO:0000269|PubMed:14702039,
ECO:0000269|PubMed:2156268,
ECO:0000269|Ref.5, ECO:0000269|Ref.7}.
/FTId=VAR_023531.
VARIANT 728 728 A -> V (in dbSNP:rs11548856).
/FTId=VAR_037150.
MUTAGEN 1001 1001 D->A: Abolishes cleavage by the caspase
CASP3. {ECO:0000269|PubMed:14960581}.
MUTAGEN 1010 1010 W->A: Decreases interaction with GET4.
Localizes in the nucleus and cytoplasm.
Decreases interaction with GET4,
localizes in the nucleus and increases
GET4 ubiquitination; when associated with
A-1042. {ECO:0000269|PubMed:29042515}.
MUTAGEN 1018 1018 W->A: Decreases interaction with GET4.
Localizes in the nucleus. Decreases
interaction with GET4, localizes in the
nucleus and increases GET4
ubiquitination; when associated with A-
1042. {ECO:0000269|PubMed:29042515}.
MUTAGEN 1030 1031 RK->SL: No effect on interaction with
GET4 and KPNA2.
{ECO:0000269|PubMed:29042515}.
MUTAGEN 1042 1042 Y->A: Decreases interaction with GET4.
Localizes in the nucleus. Decreases
interaction with GET4, localizes in the
nucleus and increases GET4
ubiquitination; when associated with A-
1010 or A-1018.
{ECO:0000269|PubMed:29042515}.
MUTAGEN 1049 1050 KR->SL: No effect on interaction with
GET4. Inhibits interaction with KPNA2.
{ECO:0000269|PubMed:29042515}.
MUTAGEN 1067 1067 V->R: No effect on interaction with
UBL4A. No effect on interaction with
UBL4A; when associated with A-1078.
Abolishes on interaction with UBL4A; when
associated with R-1085.
{ECO:0000269|PubMed:25713138}.
MUTAGEN 1078 1078 P->A: No effect on interaction with
UBL4A. No effect on interaction with
UBL4A; when associated with R-1067 or R-
1085. {ECO:0000269|PubMed:25713138}.
MUTAGEN 1085 1085 L->R: No effect on interaction with
UBL4A. No effect on interaction with
UBL4A; when associated with R-1078.
Abolishes on interaction with UBL4A; when
associated with R-1067.
{ECO:0000269|PubMed:25713138}.
MUTAGEN 1088 1088 D->H: No effect on interaction with
UBL4A. {ECO:0000269|PubMed:25713138}.
CONFLICT 43 43 K -> R (in Ref. 3; BAG65616).
{ECO:0000305}.
CONFLICT 47 47 A -> R (in Ref. 1; AAA35587).
{ECO:0000305}.
CONFLICT 150 150 H -> D (in Ref. 3; BAG65616).
{ECO:0000305}.
CONFLICT 511 511 Q -> R (in Ref. 3; BAG65616).
{ECO:0000305}.
CONFLICT 561 561 G -> D (in Ref. 3; BAG65616).
{ECO:0000305}.
CONFLICT 617 617 P -> L (in Ref. 3; BAG65616).
{ECO:0000305}.
CONFLICT 679 679 G -> R (in Ref. 3; BAG65616).
{ECO:0000305}.
CONFLICT 839 839 L -> R (in Ref. 3; BAG63924).
{ECO:0000305}.
CONFLICT 842 842 L -> P (in Ref. 3; BAG63924).
{ECO:0000305}.
CONFLICT 853 853 V -> M (in Ref. 2; CAI46045).
{ECO:0000305}.
CONFLICT 854 854 L -> Q (in Ref. 3; BAG65616).
{ECO:0000305}.
CONFLICT 927 927 E -> D (in Ref. 3; BAG65616).
{ECO:0000305}.
STRAND 16 23 {ECO:0000244|PDB:4EEW}.
STRAND 28 34 {ECO:0000244|PDB:4EEW}.
STRAND 35 37 {ECO:0000244|PDB:2N9P}.
HELIX 39 50 {ECO:0000244|PDB:4EEW}.
HELIX 54 56 {ECO:0000244|PDB:4EEW}.
STRAND 57 61 {ECO:0000244|PDB:4EEW}.
STRAND 64 66 {ECO:0000244|PDB:2N9P}.
STRAND 68 71 {ECO:0000244|PDB:1WX9}.
HELIX 72 75 {ECO:0000244|PDB:4EEW}.
STRAND 80 86 {ECO:0000244|PDB:4EEW}.
TURN 91 93 {ECO:0000244|PDB:2N9P}.
HELIX 1009 1013 {ECO:0000244|PDB:6AU8}.
HELIX 1016 1018 {ECO:0000244|PDB:6AU8}.
HELIX 1019 1028 {ECO:0000244|PDB:6AU8}.
HELIX 1040 1043 {ECO:0000244|PDB:6AU8}.
HELIX 1063 1074 {ECO:0000244|PDB:4X86}.
HELIX 1082 1089 {ECO:0000244|PDB:4X86}.
HELIX 1092 1110 {ECO:0000244|PDB:4X86}.
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


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