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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.
30-AUG-2017, entry version 166.
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; 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 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).
[32]
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).
[33]
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).
[34]
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).
[35]
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).
[36]
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).
[37]
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).
[38]
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.
[39]
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).
-!- 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). 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).
{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: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). 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).
{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:24424410,
ECO:0000269|PubMed:24981174, ECO:0000269|PubMed:25179605,
ECO:0000269|PubMed:27193484}.
-!- SUBUNIT: (Microbial infection) Interacts with L. pneumophila
Lpg2160 and LegU1 proteins. {ECO:0000269|PubMed:20547746}.
-!- INTERACTION:
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;
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;
Q9UHD9:UBQLN2; NbExp=4; IntAct=EBI-10988864, EBI-947187;
-!- SUBCELLULAR LOCATION: Cytoplasm, cytosol
{ECO:0000269|PubMed:17403783, ECO:0000269|PubMed:20676083,
ECO:0000269|PubMed:21636303}. Nucleus
{ECO:0000269|PubMed:14960581, ECO:0000269|PubMed:17403783,
ECO:0000269|PubMed:21636303}. 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. {ECO:0000269|PubMed:18055229,
ECO:0000269|PubMed:18852879}.
-!- 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.
PDBsum; 1WX9; -.
PDBsum; 2N9P; -.
PDBsum; 4DWF; -.
PDBsum; 4EEW; -.
PDBsum; 4WWR; -.
PDBsum; 4X86; -.
ProteinModelPortal; P46379; -.
SMR; P46379; -.
BioGrid; 113647; 290.
DIP; DIP-31191N; -.
IntAct; P46379; 256.
MINT; MINT-1032268; -.
STRING; 9606.ENSP00000365131; -.
iPTMnet; P46379; -.
PhosphoSitePlus; P46379; -.
SwissPalm; P46379; -.
BioMuta; BAG6; -.
DMDM; 76800648; -.
EPD; P46379; -.
MaxQB; P46379; -.
PaxDb; P46379; -.
PeptideAtlas; P46379; -.
PRIDE; P46379; -.
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; -.
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; LPVHVMT; -.
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:UniProtKB.
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:0051787; F:misfolded protein binding; IDA:ParkinsonsUK-UCL.
GO; GO:0031593; F:polyubiquitin binding; ISS:UniProtKB.
GO; GO:0070628; F:proteasome binding; ISS:UniProtKB.
GO; GO:0005102; F:receptor binding; IPI:UniProtKB.
GO; GO:0043022; F:ribosome binding; IDA:UniProtKB.
GO; GO:0015643; F:toxic substance 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:0016569; P:covalent chromatin modification; IEA:UniProtKB-KW.
GO; GO:0009790; P:embryo development; ISS:UniProtKB.
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: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:0006810; P:transport; IEA:UniProtKB-KW.
GO; GO:0030433; P:ubiquitin-dependent ERAD pathway; IDA:UniProtKB.
GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; ISS:UniProtKB.
InterPro; IPR021925; DUF3538.
InterPro; IPR029071; Ubiquitin-rel_dom.
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 1022 1132 Mediates interaction with UBL4A and GET4
and is sufficient for the delivery of
client proteins to the endoplasmic
reticulum. {ECO:0000269|PubMed:28104892}.
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}.
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 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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