Full text data of BAG6
BAG6
(BAT3, G3)
[Confidence: medium (present in either hRBCD or BSc_CH or PM22954596)]
Large proline-rich protein BAG6 (BAG family molecular chaperone regulator 6; BCL2-associated athanogene 6; BAG-6; BAG6; HLA-B-associated transcript 3; Protein G3; Protein Scythe)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
Large proline-rich protein BAG6 (BAG family molecular chaperone regulator 6; BCL2-associated athanogene 6; BAG-6; BAG6; HLA-B-associated transcript 3; Protein G3; Protein Scythe)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
UniProt
P46379
ID BAG6_HUMAN Reviewed; 1132 AA.
AC P46379; A2ADJ7; A3KQ42; A3KQ44; A6NGY6; A6PWF7; B0UX84; B4DZ12;
read moreAC B4E3V4; E7EMZ4; F8VXY4; O95874; Q5HYL9; Q5SQ35; Q5SQ36; Q5SQ37;
AC Q5SQ41; Q5SRP8; Q5SRP9; Q5STC1; Q5STX1; Q5STX3; Q96SA6; Q9BCN4;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 27-SEP-2005, sequence version 2.
DT 22-JAN-2014, entry version 128.
DE RecName: Full=Large proline-rich protein BAG6;
DE AltName: Full=BAG family molecular chaperone regulator 6;
DE AltName: Full=BCL2-associated athanogene 6;
DE Short=BAG-6;
DE Short=BAG6;
DE AltName: Full=HLA-B-associated transcript 3;
DE AltName: Full=Protein G3;
DE AltName: Full=Protein Scythe;
GN Name=BAG6; Synonyms=BAT3, G3;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORM 1), AND VARIANT
RP PRO-625.
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
RT large proline-rich proteins with multiple repeated motifs and a single
RT ubiquitin-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.,
RA Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K.,
RA Ottenwaelder B., Poustka A., 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.,
RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA 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.,
RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA Nakai K., Yada T., Nakamura Y., Ohara O., 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.,
RA Campbell R.D., 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.,
RA Gilbert J.G.R., Clamp M.E., Bethel G., Milne S., Ainscough R.,
RA Almeida J.P., Ambrose K.D., Andrews T.D., Ashwell R.I.S.,
RA Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Barker D.J.,
RA Barlow K.F., Bates K., Beare D.M., Beasley H., Beasley O., Bird C.P.,
RA Blakey S.E., Bray-Allen S., Brook J., Brown A.J., Brown J.Y.,
RA 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.,
RA Ellington A.E., Evans K.A., Faulkner L., Francis M.D., Frankish A.,
RA Frankland J., French L., Garner P., Garnett J., Ghori M.J.,
RA Gilby L.M., Gillson C.J., Glithero R.J., Grafham D.V., Grant M.,
RA Gribble S., Griffiths C., Griffiths M.N.D., Hall R., Halls K.S.,
RA Hammond S., Harley J.L., Hart E.A., Heath P.D., Heathcott R.,
RA Holmes S.J., Howden P.J., Howe K.L., Howell G.R., Huckle E.,
RA Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., Joy A.A.,
RA Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., Langford C.,
RA Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., Lloyd D.M.,
RA Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M.,
RA Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K.,
RA McMurray A., Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T.,
RA Novik K.L., Oliver K., Overton-Larty E.K., Parker A., Patel R.,
RA Pearce A.V., Peck A.I., Phillimore B.J.C.T., Phillips S., Plumb R.W.,
RA Porter K.M., Ramsey Y., Ranby S.A., Rice C.M., Ross M.T., Searle S.M.,
RA Sehra H.K., Sheridan E., Skuce C.D., Smith S., Smith M., Spraggon L.,
RA Squares S.L., Steward C.A., Sycamore N., Tamlyn-Hall G., Tester J.,
RA Theaker A.J., Thomas D.W., Thorpe A., Tracey A., Tromans A., Tubby B.,
RA Wall M., Wallis J.M., West A.P., White S.S., Whitehead S.L.,
RA Whittaker H., Wild A., Willey D.J., Wilmer T.E., Wood J.M., Wray P.W.,
RA Wyatt J.C., Young L., Younger R.M., Bentley D.R., Coulson A.,
RA Durbin R.M., Hubbard T., Sulston J.E., Dunham I., 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.,
RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA 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
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [9]
RP FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH RICIN A CHAIN,
RP MUTAGENESIS OF ASP-1001, AND CLEAVAGE BY CASPASE-3.
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
RT cleavage 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.,
RA Mann M.;
RT "Global, in vivo, and site-specific phosphorylation dynamics in
RT signaling networks.";
RL Cell 127:635-648(2006).
RN [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1117, AND MASS
RP SPECTROMETRY.
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
RT phosphorylation 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-
RT mediated acetylation of p53.";
RL Genes Dev. 21:848-861(2007).
RN [13]
RP FUNCTION IN NK CELL ACTIVATION, AND INTERACTION WITH NCR3.
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.,
RA Borchmann P., McKinnon P.J., Hallek M., Engert A.;
RT "Human leukocyte antigen-B-associated transcript 3 is released from
RT tumor 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 MASS
RP SPECTROMETRY.
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
RT cells and high confident phosphopeptide identification by cross-
RT validation of 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 MASS
RP SPECTROMETRY.
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.,
RA Feinberg A.P., Gius D.;
RT "BAT3 and SET1A form a complex with CTCFL/BORIS to modulate H3K4
RT histone dimethylation and gene expression.";
RL Mol. Cell. Biol. 28:6720-6729(2008).
RN [17]
RP FUNCTION IN NK CELL ACTIVATION, AND INTERACTION WITH NCR3.
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
RT exosomes to 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
RP AND SER-1117, PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-832
RP (ISOFORM 4), AND MASS SPECTROMETRY.
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 MASS SPECTROMETRY.
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,
RA Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in
RT a 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 MASS SPECTROMETRY.
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.
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
RT Legionella 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
RP MASS 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
RP AND SER-1117, AND MASS SPECTROMETRY.
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.,
RA Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full
RT phosphorylation 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.,
RA Buerckstuemmer T., 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 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-964 AND SER-973, AND
RP MASS SPECTROMETRY.
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J.,
RA Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V.,
RA Blagoev B.;
RT "System-wide temporal characterization of the proteome and
RT phosphoproteome of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [27]
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
RT human BAT3 protein.";
RL Submitted (JUL-2005) to the PDB data bank.
CC -!- FUNCTION: Chaperone that plays a key role in various processes
CC such as apoptosis, insertion of tail-anchored (TA) membrane
CC proteins to the endoplasmic reticulum membrane and regulation of
CC chromatin. Acts in part by regulating stability of proteins and
CC their degradation by the proteasome. Participates in endoplasmic
CC reticulum stress-induced apoptosis via its interaction with
CC AIFM1/AIF by regulating AIFM1/AIF stability and preventing its
CC degradation. Also required during spermatogenesis for synaptonemal
CC complex assembly via its interaction with HSPA2, by inhibiting
CC polyubiquitination and subsequent proteasomal degradation of
CC HSPA2. Required for selective ubiquitin-mediated degradation of
CC defective nascent chain polypeptides by the proteasome. In this
CC context, may play a role in immuno-proteasomes to generate
CC antigenic peptides via targeted degradation, thereby playing a
CC role in antigen presentation in immune response. Key component of
CC the BAG6/BAT3 complex, a cytosolic multiprotein complex involved
CC in the post-translational delivery of tail-anchored (TA) membrane
CC proteins to the endoplasmic reticulum membrane. TA membrane
CC proteins, also named type II transmembrane proteins, contain a
CC single C-terminal transmembrane region. BAG6/BAT3 acts by
CC facilitating TA membrane proteins capture by ASNA1/TRC40: it is
CC recruited to ribosomes synthesizing membrane proteins, interacts
CC with the transmembrane region of newly released TA proteins and
CC transfers them to ASNA1/TRC40 for targeting to the endoplasmic
CC reticulum membrane.
CC -!- FUNCTION: Involved in DNA damage-induced apoptosis: following DNA
CC damage, accumulates in the nucleus and forms a complex with
CC p300/EP300, enhancing p300/EP300-mediated p53/TP53 acetylation
CC leading to increase p53/TP53 transcriptional activity. When
CC nuclear, may also act as a component of some chromatin regulator
CC complex that regulates histone 3 'Lys-4' dimethylation (H3K4me2).
CC -!- FUNCTION: Can be released from tumor and dendritic cells in
CC membrane vesicles or exosomes, and engage NCR3 thereby promoting
CC natural killer cell (NK) activation and cytotoxicity.
CC -!- SUBUNIT: Component of the BAT3 complex, at least composed of
CC BAG6/BAT3, UBL4A and GET3/TRC35. Interacts with AIFM1, CTCFL,
CC HSPA2 and p300/EP300. Interacts with ricin A chain. Interacts with
CC L.pneumophila proteins Lpg2160 and LegU1. Interacts with NCR3.
CC -!- INTERACTION:
CC Q7Z434:MAVS; NbExp=2; IntAct=EBI-347552, EBI-995373;
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol. Nucleus. Note=The C-
CC terminal fragment generated by caspase-3 is cytoplasmic. Also
CC found in extracellular vesicular exosomes in some tumor cells.
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 Note=No experimental confirmation available;
CC Name=4;
CC IsoId=P46379-4; Sequence=VSP_015695, VSP_045910, VSP_045911,
CC VSP_045912, VSP_045913;
CC Note=No experimental confirmation available. Contains a
CC phosphoserine at position 832;
CC Name=5;
CC IsoId=P46379-5; Sequence=VSP_015695, VSP_045913;
CC Note=No experimental confirmation available;
CC -!- PTM: Cleavage by caspase-3 releases a C-terminal peptide that
CC plays a role in ricin-induced apoptosis.
CC -!- PTM: In case of infection by L.pneumophila, ubiquitinated by the
CC SCF(LegU1) complex.
CC -!- SIMILARITY: Contains 1 ubiquitin-like domain.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAD18085.1; Type=Erroneous initiation; Note=Translation N-terminally shortened;
CC Sequence=BAB63390.1; Type=Erroneous initiation; Note=Translation N-terminally shortened;
CC Sequence=CAI18318.2; Type=Erroneous gene model prediction;
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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; CAI18314.1; -; Genomic_DNA.
DR EMBL; AL662801; CAI18315.1; -; Genomic_DNA.
DR EMBL; AL662801; CAI18316.2; -; Genomic_DNA.
DR EMBL; AL662801; CAI18318.2; ALT_SEQ; Genomic_DNA.
DR EMBL; AL662847; CAI17658.1; -; Genomic_DNA.
DR EMBL; AL670886; CAI17658.1; JOINED; Genomic_DNA.
DR EMBL; AL662847; CAI17659.1; -; Genomic_DNA.
DR EMBL; AL670886; CAI17659.1; JOINED; Genomic_DNA.
DR EMBL; AL670886; CAI17784.1; -; Genomic_DNA.
DR EMBL; AL662847; CAI17784.1; JOINED; Genomic_DNA.
DR EMBL; AL670886; CAI17785.1; -; Genomic_DNA.
DR EMBL; AL662847; CAI17785.1; JOINED; Genomic_DNA.
DR EMBL; AL670886; CAI17786.1; -; Genomic_DNA.
DR EMBL; AL662847; CAI17786.1; JOINED; Genomic_DNA.
DR EMBL; AL805934; CAI18501.1; -; Genomic_DNA.
DR EMBL; AL805934; CAI18504.1; -; Genomic_DNA.
DR EMBL; AL805934; CAI18508.2; -; Genomic_DNA.
DR EMBL; AL805934; CAI18509.1; -; Genomic_DNA.
DR EMBL; AL670886; CAM25014.1; -; Genomic_DNA.
DR EMBL; AL662847; CAM25014.1; JOINED; Genomic_DNA.
DR EMBL; BX511262; CAM45799.1; -; Genomic_DNA.
DR EMBL; BX511262; CAM45800.1; -; Genomic_DNA.
DR EMBL; BX511262; CAM45801.1; -; Genomic_DNA.
DR EMBL; AL662847; CAO72072.1; -; Genomic_DNA.
DR EMBL; AL670886; CAO72072.1; JOINED; Genomic_DNA.
DR EMBL; CR753842; CAQ06558.1; -; Genomic_DNA.
DR EMBL; CR753892; CAQ06558.1; JOINED; Genomic_DNA.
DR EMBL; CR753892; CAQ06931.1; -; Genomic_DNA.
DR EMBL; CR753842; CAQ06931.1; JOINED; Genomic_DNA.
DR EMBL; CR354443; CAQ06977.1; -; Genomic_DNA.
DR EMBL; CR759761; CAQ10854.1; -; Genomic_DNA.
DR EMBL; CH471081; EAX03455.1; -; Genomic_DNA.
DR EMBL; BC003133; AAH03133.1; -; mRNA.
DR PIR; A35098; A35098.
DR RefSeq; NP_001092004.1; NM_001098534.1.
DR RefSeq; NP_001186626.1; NM_001199697.1.
DR RefSeq; NP_001186627.1; NM_001199698.1.
DR RefSeq; NP_004630.3; NM_004639.3.
DR RefSeq; NP_542433.1; NM_080702.2.
DR RefSeq; NP_542434.1; NM_080703.2.
DR RefSeq; XP_005249450.1; XM_005249393.1.
DR RefSeq; XP_005249451.1; XM_005249394.1.
DR RefSeq; XP_005272937.1; XM_005272880.1.
DR RefSeq; XP_005272938.1; XM_005272881.1.
DR RefSeq; XP_005275521.1; XM_005275464.1.
DR RefSeq; XP_005275522.1; XM_005275465.1.
DR RefSeq; XP_005275523.1; XM_005275466.1.
DR RefSeq; XP_005275654.1; XM_005275597.1.
DR RefSeq; XP_005275655.1; XM_005275598.1.
DR RefSeq; XP_005275656.1; XM_005275599.1.
DR UniGene; Hs.440900; -.
DR PDB; 1WX9; NMR; -; A=17-89.
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 PDBsum; 1WX9; -.
DR PDBsum; 4DWF; -.
DR PDBsum; 4EEW; -.
DR ProteinModelPortal; P46379; -.
DR SMR; P46379; 13-87.
DR DIP; DIP-31191N; -.
DR IntAct; P46379; 119.
DR MINT; MINT-1032268; -.
DR PhosphoSite; P46379; -.
DR DMDM; 76800648; -.
DR PaxDb; P46379; -.
DR PRIDE; P46379; -.
DR Ensembl; ENST00000211379; ENSP00000211379; ENSG00000204463.
DR Ensembl; ENST00000361076; ENSP00000354368; ENSG00000096155.
DR Ensembl; ENST00000362049; ENSP00000354875; ENSG00000204463.
DR Ensembl; ENST00000375964; ENSP00000365131; ENSG00000204463.
DR Ensembl; ENST00000375976; ENSP00000365143; ENSG00000204463.
DR Ensembl; ENST00000383446; ENSP00000372938; ENSG00000096155.
DR Ensembl; ENST00000383448; ENSP00000372940; ENSG00000096155.
DR Ensembl; ENST00000404765; ENSP00000384494; ENSG00000204463.
DR Ensembl; ENST00000417144; ENSP00000412110; ENSG00000229524.
DR Ensembl; ENST00000419847; ENSP00000389121; ENSG00000233348.
DR Ensembl; ENST00000425649; ENSP00000413341; ENSG00000227761.
DR Ensembl; ENST00000439687; ENSP00000402856; ENSG00000204463.
DR Ensembl; ENST00000442479; ENSP00000413698; ENSG00000229524.
DR Ensembl; ENST00000443182; ENSP00000410156; ENSG00000233348.
DR Ensembl; ENST00000444402; ENSP00000413327; ENSG00000228760.
DR Ensembl; ENST00000449450; ENSP00000397894; ENSG00000229524.
DR Ensembl; ENST00000451932; ENSP00000390966; ENSG00000233348.
DR Ensembl; ENST00000454478; ENSP00000415427; ENSG00000234651.
DR Ensembl; ENST00000551350; ENSP00000447546; ENSG00000229524.
DR Ensembl; ENST00000552116; ENSP00000447946; ENSG00000233348.
DR Ensembl; ENST00000552605; ENSP00000446525; ENSG00000096155.
DR GeneID; 7917; -.
DR KEGG; hsa:7917; -.
DR UCSC; uc011dnx.2; human.
DR CTD; 7917; -.
DR GeneCards; GC06M031666; -.
DR GeneCards; GC06Mj31594; -.
DR GeneCards; GC06Mk31588; -.
DR GeneCards; GC06Ml31646; -.
DR GeneCards; GC06Mm31683; -.
DR GeneCards; GC06Mn31597; -.
DR GeneCards; GC06Mo31596; -.
DR H-InvDB; HIX0165051; -.
DR H-InvDB; HIX0166179; -.
DR H-InvDB; HIX0166289; -.
DR H-InvDB; HIX0166578; -.
DR H-InvDB; HIX0166832; -.
DR H-InvDB; HIX0167081; -.
DR H-InvDB; HIX0167222; -.
DR H-InvDB; HIX0167321; -.
DR H-InvDB; HIX0167461; -.
DR H-InvDB; HIX0167568; -.
DR HGNC; HGNC:13919; BAG6.
DR HPA; CAB020704; -.
DR MIM; 142590; gene.
DR neXtProt; NX_P46379; -.
DR PharmGKB; PA25264; -.
DR eggNOG; NOG297129; -.
DR HOVERGEN; HBG002193; -.
DR InParanoid; P46379; -.
DR OMA; ERTHSIL; -.
DR ChiTaRS; BAG6; human.
DR EvolutionaryTrace; P46379; -.
DR GeneWiki; HLA-B_associated_transcript_3; -.
DR GenomeRNAi; 7917; -.
DR NextBio; 30391; -.
DR PMAP-CutDB; B0UX84; -.
DR PRO; PR:P46379; -.
DR ArrayExpress; P46379; -.
DR Bgee; P46379; -.
DR Genevestigator; P46379; -.
DR GO; GO:0071818; C:BAT3 complex; IDA:UniProtKB.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0031593; F:polyubiquitin binding; ISS:UniProtKB.
DR GO; GO:0070628; F:proteasome binding; ISS:UniProtKB.
DR GO; GO:0043022; F:ribosome binding; IDA:UniProtKB.
DR GO; GO:0007420; P:brain development; ISS:UniProtKB.
DR GO; GO:0030154; P:cell differentiation; IEA:UniProtKB-KW.
DR GO; GO:0016568; P:chromatin modification; IEA:UniProtKB-KW.
DR GO; GO:0009790; P:embryo development; ISS: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:0032435; P:negative regulation of proteasomal ubiquitin-dependent protein catabolic process; ISS:UniProtKB.
DR GO; GO:0050821; P:protein stabilization; ISS:UniProtKB.
DR GO; GO:0042127; P:regulation of cell proliferation; IEA:Ensembl.
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:0006810; P:transport; IEA:UniProtKB-KW.
DR GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; ISS:UniProtKB.
DR InterPro; IPR021925; DUF3538.
DR InterPro; IPR019954; Ubiquitin_CS.
DR InterPro; IPR000626; Ubiquitin_dom.
DR Pfam; PF12057; DUF3538; 1.
DR Pfam; PF00240; ubiquitin; 1.
DR SMART; SM00213; UBQ; 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; Complete proteome; Cytoplasm; Differentiation;
KW Immunity; Nucleus; Phosphoprotein; Polymorphism; Reference proteome;
KW Repeat; Spermatogenesis; Transport; Ubl conjugation.
FT CHAIN 1 1132 Large proline-rich protein BAG6.
FT /FTId=PRO_0000114897.
FT DOMAIN 17 92 Ubiquitin-like.
FT REPEAT 242 270 1.
FT REPEAT 415 443 2.
FT REPEAT 574 602 3.
FT REPEAT 608 636 4.
FT REGION 242 636 4 X 29 AA approximate repeats.
FT COMPBIAS 195 273 Pro-rich.
FT COMPBIAS 394 681 Pro-rich.
FT SITE 1001 1002 Cleavage; by caspase-3.
FT MOD_RES 1 1 N-acetylmethionine.
FT MOD_RES 113 113 Phosphoserine.
FT MOD_RES 350 350 Phosphothreonine.
FT MOD_RES 964 964 Phosphoserine.
FT MOD_RES 973 973 Phosphoserine.
FT MOD_RES 1081 1081 Phosphoserine.
FT MOD_RES 1117 1117 Phosphoserine.
FT VAR_SEQ 185 190 Missing (in isoform 2, isoform 3, isoform
FT 4 and isoform 5).
FT /FTId=VSP_015695.
FT VAR_SEQ 489 489 G -> GSTLIQLPSLPPEFMHAVAHQITHQAMVAAVASAAA
FT G (in isoform 3).
FT /FTId=VSP_030519.
FT VAR_SEQ 527 527 Missing (in isoform 4).
FT /FTId=VSP_045910.
FT VAR_SEQ 561 685 Missing (in isoform 4).
FT /FTId=VSP_045911.
FT VAR_SEQ 969 1016 Missing (in isoform 4).
FT /FTId=VSP_045912.
FT VAR_SEQ 1053 1101 Missing (in isoform 4 and isoform 5).
FT /FTId=VSP_045913.
FT VARIANT 625 625 S -> P (in dbSNP:rs1052486).
FT /FTId=VAR_023531.
FT VARIANT 728 728 A -> V (in dbSNP:rs11548856).
FT /FTId=VAR_037150.
FT MUTAGEN 1001 1001 D->A: Abolishes cleavage by caspase-3.
FT CONFLICT 43 43 K -> R (in Ref. 3; BAG65616).
FT CONFLICT 47 47 A -> R (in Ref. 1; AAA35587).
FT CONFLICT 150 150 H -> D (in Ref. 3; BAG65616).
FT CONFLICT 511 511 Q -> R (in Ref. 3; BAG65616).
FT CONFLICT 561 561 G -> D (in Ref. 3; BAG65616).
FT CONFLICT 617 617 P -> L (in Ref. 3; BAG65616).
FT CONFLICT 679 679 G -> R (in Ref. 3; BAG65616).
FT CONFLICT 839 839 L -> R (in Ref. 3; BAG63924).
FT CONFLICT 842 842 L -> P (in Ref. 3; BAG63924).
FT CONFLICT 853 853 V -> M (in Ref. 2; CAI46045).
FT CONFLICT 854 854 L -> Q (in Ref. 3; BAG65616).
FT CONFLICT 927 927 E -> D (in Ref. 3; BAG65616).
FT STRAND 16 23
FT STRAND 28 34
FT HELIX 39 50
FT HELIX 54 56
FT STRAND 57 61
FT STRAND 68 71
FT HELIX 72 75
FT STRAND 80 86
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
//
ID BAG6_HUMAN Reviewed; 1132 AA.
AC P46379; A2ADJ7; A3KQ42; A3KQ44; A6NGY6; A6PWF7; B0UX84; B4DZ12;
read moreAC B4E3V4; E7EMZ4; F8VXY4; O95874; Q5HYL9; Q5SQ35; Q5SQ36; Q5SQ37;
AC Q5SQ41; Q5SRP8; Q5SRP9; Q5STC1; Q5STX1; Q5STX3; Q96SA6; Q9BCN4;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 27-SEP-2005, sequence version 2.
DT 22-JAN-2014, entry version 128.
DE RecName: Full=Large proline-rich protein BAG6;
DE AltName: Full=BAG family molecular chaperone regulator 6;
DE AltName: Full=BCL2-associated athanogene 6;
DE Short=BAG-6;
DE Short=BAG6;
DE AltName: Full=HLA-B-associated transcript 3;
DE AltName: Full=Protein G3;
DE AltName: Full=Protein Scythe;
GN Name=BAG6; Synonyms=BAT3, G3;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORM 1), AND VARIANT
RP PRO-625.
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
RT large proline-rich proteins with multiple repeated motifs and a single
RT ubiquitin-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.,
RA Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K.,
RA Ottenwaelder B., Poustka A., 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.,
RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA 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.,
RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA Nakai K., Yada T., Nakamura Y., Ohara O., 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.,
RA Campbell R.D., 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.,
RA Gilbert J.G.R., Clamp M.E., Bethel G., Milne S., Ainscough R.,
RA Almeida J.P., Ambrose K.D., Andrews T.D., Ashwell R.I.S.,
RA Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Barker D.J.,
RA Barlow K.F., Bates K., Beare D.M., Beasley H., Beasley O., Bird C.P.,
RA Blakey S.E., Bray-Allen S., Brook J., Brown A.J., Brown J.Y.,
RA 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.,
RA Ellington A.E., Evans K.A., Faulkner L., Francis M.D., Frankish A.,
RA Frankland J., French L., Garner P., Garnett J., Ghori M.J.,
RA Gilby L.M., Gillson C.J., Glithero R.J., Grafham D.V., Grant M.,
RA Gribble S., Griffiths C., Griffiths M.N.D., Hall R., Halls K.S.,
RA Hammond S., Harley J.L., Hart E.A., Heath P.D., Heathcott R.,
RA Holmes S.J., Howden P.J., Howe K.L., Howell G.R., Huckle E.,
RA Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., Joy A.A.,
RA Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., Langford C.,
RA Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., Lloyd D.M.,
RA Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M.,
RA Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K.,
RA McMurray A., Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T.,
RA Novik K.L., Oliver K., Overton-Larty E.K., Parker A., Patel R.,
RA Pearce A.V., Peck A.I., Phillimore B.J.C.T., Phillips S., Plumb R.W.,
RA Porter K.M., Ramsey Y., Ranby S.A., Rice C.M., Ross M.T., Searle S.M.,
RA Sehra H.K., Sheridan E., Skuce C.D., Smith S., Smith M., Spraggon L.,
RA Squares S.L., Steward C.A., Sycamore N., Tamlyn-Hall G., Tester J.,
RA Theaker A.J., Thomas D.W., Thorpe A., Tracey A., Tromans A., Tubby B.,
RA Wall M., Wallis J.M., West A.P., White S.S., Whitehead S.L.,
RA Whittaker H., Wild A., Willey D.J., Wilmer T.E., Wood J.M., Wray P.W.,
RA Wyatt J.C., Young L., Younger R.M., Bentley D.R., Coulson A.,
RA Durbin R.M., Hubbard T., Sulston J.E., Dunham I., 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.,
RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA 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
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [9]
RP FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH RICIN A CHAIN,
RP MUTAGENESIS OF ASP-1001, AND CLEAVAGE BY CASPASE-3.
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
RT cleavage 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.,
RA Mann M.;
RT "Global, in vivo, and site-specific phosphorylation dynamics in
RT signaling networks.";
RL Cell 127:635-648(2006).
RN [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1117, AND MASS
RP SPECTROMETRY.
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
RT phosphorylation 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-
RT mediated acetylation of p53.";
RL Genes Dev. 21:848-861(2007).
RN [13]
RP FUNCTION IN NK CELL ACTIVATION, AND INTERACTION WITH NCR3.
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.,
RA Borchmann P., McKinnon P.J., Hallek M., Engert A.;
RT "Human leukocyte antigen-B-associated transcript 3 is released from
RT tumor 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 MASS
RP SPECTROMETRY.
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
RT cells and high confident phosphopeptide identification by cross-
RT validation of 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 MASS
RP SPECTROMETRY.
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.,
RA Feinberg A.P., Gius D.;
RT "BAT3 and SET1A form a complex with CTCFL/BORIS to modulate H3K4
RT histone dimethylation and gene expression.";
RL Mol. Cell. Biol. 28:6720-6729(2008).
RN [17]
RP FUNCTION IN NK CELL ACTIVATION, AND INTERACTION WITH NCR3.
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
RT exosomes to 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
RP AND SER-1117, PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-832
RP (ISOFORM 4), AND MASS SPECTROMETRY.
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 MASS SPECTROMETRY.
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,
RA Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in
RT a 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 MASS SPECTROMETRY.
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.
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
RT Legionella 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
RP MASS 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
RP AND SER-1117, AND MASS SPECTROMETRY.
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.,
RA Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full
RT phosphorylation 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.,
RA Buerckstuemmer T., 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 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-964 AND SER-973, AND
RP MASS SPECTROMETRY.
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J.,
RA Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V.,
RA Blagoev B.;
RT "System-wide temporal characterization of the proteome and
RT phosphoproteome of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [27]
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
RT human BAT3 protein.";
RL Submitted (JUL-2005) to the PDB data bank.
CC -!- FUNCTION: Chaperone that plays a key role in various processes
CC such as apoptosis, insertion of tail-anchored (TA) membrane
CC proteins to the endoplasmic reticulum membrane and regulation of
CC chromatin. Acts in part by regulating stability of proteins and
CC their degradation by the proteasome. Participates in endoplasmic
CC reticulum stress-induced apoptosis via its interaction with
CC AIFM1/AIF by regulating AIFM1/AIF stability and preventing its
CC degradation. Also required during spermatogenesis for synaptonemal
CC complex assembly via its interaction with HSPA2, by inhibiting
CC polyubiquitination and subsequent proteasomal degradation of
CC HSPA2. Required for selective ubiquitin-mediated degradation of
CC defective nascent chain polypeptides by the proteasome. In this
CC context, may play a role in immuno-proteasomes to generate
CC antigenic peptides via targeted degradation, thereby playing a
CC role in antigen presentation in immune response. Key component of
CC the BAG6/BAT3 complex, a cytosolic multiprotein complex involved
CC in the post-translational delivery of tail-anchored (TA) membrane
CC proteins to the endoplasmic reticulum membrane. TA membrane
CC proteins, also named type II transmembrane proteins, contain a
CC single C-terminal transmembrane region. BAG6/BAT3 acts by
CC facilitating TA membrane proteins capture by ASNA1/TRC40: it is
CC recruited to ribosomes synthesizing membrane proteins, interacts
CC with the transmembrane region of newly released TA proteins and
CC transfers them to ASNA1/TRC40 for targeting to the endoplasmic
CC reticulum membrane.
CC -!- FUNCTION: Involved in DNA damage-induced apoptosis: following DNA
CC damage, accumulates in the nucleus and forms a complex with
CC p300/EP300, enhancing p300/EP300-mediated p53/TP53 acetylation
CC leading to increase p53/TP53 transcriptional activity. When
CC nuclear, may also act as a component of some chromatin regulator
CC complex that regulates histone 3 'Lys-4' dimethylation (H3K4me2).
CC -!- FUNCTION: Can be released from tumor and dendritic cells in
CC membrane vesicles or exosomes, and engage NCR3 thereby promoting
CC natural killer cell (NK) activation and cytotoxicity.
CC -!- SUBUNIT: Component of the BAT3 complex, at least composed of
CC BAG6/BAT3, UBL4A and GET3/TRC35. Interacts with AIFM1, CTCFL,
CC HSPA2 and p300/EP300. Interacts with ricin A chain. Interacts with
CC L.pneumophila proteins Lpg2160 and LegU1. Interacts with NCR3.
CC -!- INTERACTION:
CC Q7Z434:MAVS; NbExp=2; IntAct=EBI-347552, EBI-995373;
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol. Nucleus. Note=The C-
CC terminal fragment generated by caspase-3 is cytoplasmic. Also
CC found in extracellular vesicular exosomes in some tumor cells.
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 Note=No experimental confirmation available;
CC Name=4;
CC IsoId=P46379-4; Sequence=VSP_015695, VSP_045910, VSP_045911,
CC VSP_045912, VSP_045913;
CC Note=No experimental confirmation available. Contains a
CC phosphoserine at position 832;
CC Name=5;
CC IsoId=P46379-5; Sequence=VSP_015695, VSP_045913;
CC Note=No experimental confirmation available;
CC -!- PTM: Cleavage by caspase-3 releases a C-terminal peptide that
CC plays a role in ricin-induced apoptosis.
CC -!- PTM: In case of infection by L.pneumophila, ubiquitinated by the
CC SCF(LegU1) complex.
CC -!- SIMILARITY: Contains 1 ubiquitin-like domain.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAD18085.1; Type=Erroneous initiation; Note=Translation N-terminally shortened;
CC Sequence=BAB63390.1; Type=Erroneous initiation; Note=Translation N-terminally shortened;
CC Sequence=CAI18318.2; Type=Erroneous gene model prediction;
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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; CAI18314.1; -; Genomic_DNA.
DR EMBL; AL662801; CAI18315.1; -; Genomic_DNA.
DR EMBL; AL662801; CAI18316.2; -; Genomic_DNA.
DR EMBL; AL662801; CAI18318.2; ALT_SEQ; Genomic_DNA.
DR EMBL; AL662847; CAI17658.1; -; Genomic_DNA.
DR EMBL; AL670886; CAI17658.1; JOINED; Genomic_DNA.
DR EMBL; AL662847; CAI17659.1; -; Genomic_DNA.
DR EMBL; AL670886; CAI17659.1; JOINED; Genomic_DNA.
DR EMBL; AL670886; CAI17784.1; -; Genomic_DNA.
DR EMBL; AL662847; CAI17784.1; JOINED; Genomic_DNA.
DR EMBL; AL670886; CAI17785.1; -; Genomic_DNA.
DR EMBL; AL662847; CAI17785.1; JOINED; Genomic_DNA.
DR EMBL; AL670886; CAI17786.1; -; Genomic_DNA.
DR EMBL; AL662847; CAI17786.1; JOINED; Genomic_DNA.
DR EMBL; AL805934; CAI18501.1; -; Genomic_DNA.
DR EMBL; AL805934; CAI18504.1; -; Genomic_DNA.
DR EMBL; AL805934; CAI18508.2; -; Genomic_DNA.
DR EMBL; AL805934; CAI18509.1; -; Genomic_DNA.
DR EMBL; AL670886; CAM25014.1; -; Genomic_DNA.
DR EMBL; AL662847; CAM25014.1; JOINED; Genomic_DNA.
DR EMBL; BX511262; CAM45799.1; -; Genomic_DNA.
DR EMBL; BX511262; CAM45800.1; -; Genomic_DNA.
DR EMBL; BX511262; CAM45801.1; -; Genomic_DNA.
DR EMBL; AL662847; CAO72072.1; -; Genomic_DNA.
DR EMBL; AL670886; CAO72072.1; JOINED; Genomic_DNA.
DR EMBL; CR753842; CAQ06558.1; -; Genomic_DNA.
DR EMBL; CR753892; CAQ06558.1; JOINED; Genomic_DNA.
DR EMBL; CR753892; CAQ06931.1; -; Genomic_DNA.
DR EMBL; CR753842; CAQ06931.1; JOINED; Genomic_DNA.
DR EMBL; CR354443; CAQ06977.1; -; Genomic_DNA.
DR EMBL; CR759761; CAQ10854.1; -; Genomic_DNA.
DR EMBL; CH471081; EAX03455.1; -; Genomic_DNA.
DR EMBL; BC003133; AAH03133.1; -; mRNA.
DR PIR; A35098; A35098.
DR RefSeq; NP_001092004.1; NM_001098534.1.
DR RefSeq; NP_001186626.1; NM_001199697.1.
DR RefSeq; NP_001186627.1; NM_001199698.1.
DR RefSeq; NP_004630.3; NM_004639.3.
DR RefSeq; NP_542433.1; NM_080702.2.
DR RefSeq; NP_542434.1; NM_080703.2.
DR RefSeq; XP_005249450.1; XM_005249393.1.
DR RefSeq; XP_005249451.1; XM_005249394.1.
DR RefSeq; XP_005272937.1; XM_005272880.1.
DR RefSeq; XP_005272938.1; XM_005272881.1.
DR RefSeq; XP_005275521.1; XM_005275464.1.
DR RefSeq; XP_005275522.1; XM_005275465.1.
DR RefSeq; XP_005275523.1; XM_005275466.1.
DR RefSeq; XP_005275654.1; XM_005275597.1.
DR RefSeq; XP_005275655.1; XM_005275598.1.
DR RefSeq; XP_005275656.1; XM_005275599.1.
DR UniGene; Hs.440900; -.
DR PDB; 1WX9; NMR; -; A=17-89.
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 PDBsum; 1WX9; -.
DR PDBsum; 4DWF; -.
DR PDBsum; 4EEW; -.
DR ProteinModelPortal; P46379; -.
DR SMR; P46379; 13-87.
DR DIP; DIP-31191N; -.
DR IntAct; P46379; 119.
DR MINT; MINT-1032268; -.
DR PhosphoSite; P46379; -.
DR DMDM; 76800648; -.
DR PaxDb; P46379; -.
DR PRIDE; P46379; -.
DR Ensembl; ENST00000211379; ENSP00000211379; ENSG00000204463.
DR Ensembl; ENST00000361076; ENSP00000354368; ENSG00000096155.
DR Ensembl; ENST00000362049; ENSP00000354875; ENSG00000204463.
DR Ensembl; ENST00000375964; ENSP00000365131; ENSG00000204463.
DR Ensembl; ENST00000375976; ENSP00000365143; ENSG00000204463.
DR Ensembl; ENST00000383446; ENSP00000372938; ENSG00000096155.
DR Ensembl; ENST00000383448; ENSP00000372940; ENSG00000096155.
DR Ensembl; ENST00000404765; ENSP00000384494; ENSG00000204463.
DR Ensembl; ENST00000417144; ENSP00000412110; ENSG00000229524.
DR Ensembl; ENST00000419847; ENSP00000389121; ENSG00000233348.
DR Ensembl; ENST00000425649; ENSP00000413341; ENSG00000227761.
DR Ensembl; ENST00000439687; ENSP00000402856; ENSG00000204463.
DR Ensembl; ENST00000442479; ENSP00000413698; ENSG00000229524.
DR Ensembl; ENST00000443182; ENSP00000410156; ENSG00000233348.
DR Ensembl; ENST00000444402; ENSP00000413327; ENSG00000228760.
DR Ensembl; ENST00000449450; ENSP00000397894; ENSG00000229524.
DR Ensembl; ENST00000451932; ENSP00000390966; ENSG00000233348.
DR Ensembl; ENST00000454478; ENSP00000415427; ENSG00000234651.
DR Ensembl; ENST00000551350; ENSP00000447546; ENSG00000229524.
DR Ensembl; ENST00000552116; ENSP00000447946; ENSG00000233348.
DR Ensembl; ENST00000552605; ENSP00000446525; ENSG00000096155.
DR GeneID; 7917; -.
DR KEGG; hsa:7917; -.
DR UCSC; uc011dnx.2; human.
DR CTD; 7917; -.
DR GeneCards; GC06M031666; -.
DR GeneCards; GC06Mj31594; -.
DR GeneCards; GC06Mk31588; -.
DR GeneCards; GC06Ml31646; -.
DR GeneCards; GC06Mm31683; -.
DR GeneCards; GC06Mn31597; -.
DR GeneCards; GC06Mo31596; -.
DR H-InvDB; HIX0165051; -.
DR H-InvDB; HIX0166179; -.
DR H-InvDB; HIX0166289; -.
DR H-InvDB; HIX0166578; -.
DR H-InvDB; HIX0166832; -.
DR H-InvDB; HIX0167081; -.
DR H-InvDB; HIX0167222; -.
DR H-InvDB; HIX0167321; -.
DR H-InvDB; HIX0167461; -.
DR H-InvDB; HIX0167568; -.
DR HGNC; HGNC:13919; BAG6.
DR HPA; CAB020704; -.
DR MIM; 142590; gene.
DR neXtProt; NX_P46379; -.
DR PharmGKB; PA25264; -.
DR eggNOG; NOG297129; -.
DR HOVERGEN; HBG002193; -.
DR InParanoid; P46379; -.
DR OMA; ERTHSIL; -.
DR ChiTaRS; BAG6; human.
DR EvolutionaryTrace; P46379; -.
DR GeneWiki; HLA-B_associated_transcript_3; -.
DR GenomeRNAi; 7917; -.
DR NextBio; 30391; -.
DR PMAP-CutDB; B0UX84; -.
DR PRO; PR:P46379; -.
DR ArrayExpress; P46379; -.
DR Bgee; P46379; -.
DR Genevestigator; P46379; -.
DR GO; GO:0071818; C:BAT3 complex; IDA:UniProtKB.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0031593; F:polyubiquitin binding; ISS:UniProtKB.
DR GO; GO:0070628; F:proteasome binding; ISS:UniProtKB.
DR GO; GO:0043022; F:ribosome binding; IDA:UniProtKB.
DR GO; GO:0007420; P:brain development; ISS:UniProtKB.
DR GO; GO:0030154; P:cell differentiation; IEA:UniProtKB-KW.
DR GO; GO:0016568; P:chromatin modification; IEA:UniProtKB-KW.
DR GO; GO:0009790; P:embryo development; ISS: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:0032435; P:negative regulation of proteasomal ubiquitin-dependent protein catabolic process; ISS:UniProtKB.
DR GO; GO:0050821; P:protein stabilization; ISS:UniProtKB.
DR GO; GO:0042127; P:regulation of cell proliferation; IEA:Ensembl.
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:0006810; P:transport; IEA:UniProtKB-KW.
DR GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; ISS:UniProtKB.
DR InterPro; IPR021925; DUF3538.
DR InterPro; IPR019954; Ubiquitin_CS.
DR InterPro; IPR000626; Ubiquitin_dom.
DR Pfam; PF12057; DUF3538; 1.
DR Pfam; PF00240; ubiquitin; 1.
DR SMART; SM00213; UBQ; 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; Complete proteome; Cytoplasm; Differentiation;
KW Immunity; Nucleus; Phosphoprotein; Polymorphism; Reference proteome;
KW Repeat; Spermatogenesis; Transport; Ubl conjugation.
FT CHAIN 1 1132 Large proline-rich protein BAG6.
FT /FTId=PRO_0000114897.
FT DOMAIN 17 92 Ubiquitin-like.
FT REPEAT 242 270 1.
FT REPEAT 415 443 2.
FT REPEAT 574 602 3.
FT REPEAT 608 636 4.
FT REGION 242 636 4 X 29 AA approximate repeats.
FT COMPBIAS 195 273 Pro-rich.
FT COMPBIAS 394 681 Pro-rich.
FT SITE 1001 1002 Cleavage; by caspase-3.
FT MOD_RES 1 1 N-acetylmethionine.
FT MOD_RES 113 113 Phosphoserine.
FT MOD_RES 350 350 Phosphothreonine.
FT MOD_RES 964 964 Phosphoserine.
FT MOD_RES 973 973 Phosphoserine.
FT MOD_RES 1081 1081 Phosphoserine.
FT MOD_RES 1117 1117 Phosphoserine.
FT VAR_SEQ 185 190 Missing (in isoform 2, isoform 3, isoform
FT 4 and isoform 5).
FT /FTId=VSP_015695.
FT VAR_SEQ 489 489 G -> GSTLIQLPSLPPEFMHAVAHQITHQAMVAAVASAAA
FT G (in isoform 3).
FT /FTId=VSP_030519.
FT VAR_SEQ 527 527 Missing (in isoform 4).
FT /FTId=VSP_045910.
FT VAR_SEQ 561 685 Missing (in isoform 4).
FT /FTId=VSP_045911.
FT VAR_SEQ 969 1016 Missing (in isoform 4).
FT /FTId=VSP_045912.
FT VAR_SEQ 1053 1101 Missing (in isoform 4 and isoform 5).
FT /FTId=VSP_045913.
FT VARIANT 625 625 S -> P (in dbSNP:rs1052486).
FT /FTId=VAR_023531.
FT VARIANT 728 728 A -> V (in dbSNP:rs11548856).
FT /FTId=VAR_037150.
FT MUTAGEN 1001 1001 D->A: Abolishes cleavage by caspase-3.
FT CONFLICT 43 43 K -> R (in Ref. 3; BAG65616).
FT CONFLICT 47 47 A -> R (in Ref. 1; AAA35587).
FT CONFLICT 150 150 H -> D (in Ref. 3; BAG65616).
FT CONFLICT 511 511 Q -> R (in Ref. 3; BAG65616).
FT CONFLICT 561 561 G -> D (in Ref. 3; BAG65616).
FT CONFLICT 617 617 P -> L (in Ref. 3; BAG65616).
FT CONFLICT 679 679 G -> R (in Ref. 3; BAG65616).
FT CONFLICT 839 839 L -> R (in Ref. 3; BAG63924).
FT CONFLICT 842 842 L -> P (in Ref. 3; BAG63924).
FT CONFLICT 853 853 V -> M (in Ref. 2; CAI46045).
FT CONFLICT 854 854 L -> Q (in Ref. 3; BAG65616).
FT CONFLICT 927 927 E -> D (in Ref. 3; BAG65616).
FT STRAND 16 23
FT STRAND 28 34
FT HELIX 39 50
FT HELIX 54 56
FT STRAND 57 61
FT STRAND 68 71
FT HELIX 72 75
FT STRAND 80 86
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
//
MIM
142590
*RECORD*
*FIELD* NO
142590
*FIELD* TI
*142590 BCL2-ASSOCIATED ATHANOGENE 6; BAG6
;;SCYTHE, XENOPUS, HOMOLOG OF;;
HLA-B-ASSOCIATED TRANSCRIPT 3; BAT3;;
read moreD6S52E
*FIELD* TX
CLONING
By chromosome walking with overlapping cosmids, Spies et al. (1989)
isolated a 435-kb DNA segment that was centromeric to HLA-B (142830) in
the human major histocompatibility complex. The presence of additional
genes was suggested by a large cluster of CpG islands. With cosmid
probes, 5 distinct transcripts, including BAT3, were detected in RNA
samples from a variety of cell lines, and the corresponding cDNA clones
were isolated.
From cDNA clones, Banerji et al. (1990) determined the complete
sequences of the closely linked BAT2 (142580) and BAT3 genes. The
putative proteins are 228 and 110 kD, respectively. BAT3 contains an
N-terminal ubiquitin-like domain, and both BAT2 and BAT3 are rich in
proline and include short tracts of polyproline, polyglycine, and
charged amino acids.
GENE FUNCTION
Sasaki et al. (2007) showed that depletion of BAT3 from human and mouse
cells impaired p53 (TP53; 191170)-mediated transactivation of its target
genes Puma (BBC3; 605854) and p21 (CDKN1A; 116899). Although DNA
damage-induced phosphorylation, stabilization, and nuclear accumulation
of p53 were not significantly affected by BAT3 depletion, p53
acetylation was almost completely abolished. BAT3 formed a complex with
p300 (EP300; 602700), and an increased amount of BAT3 enhanced
recruitment of p53 to p300 and facilitated subsequent p53 acetylation.
In contrast, Bat3-depleted cells showed reduced p53-p300 complex
formation and decreased p53 acetylation. Thymocytes from Bat3-deficient
mice exhibited reduced p53-mediated induction of Puma and p21 and were
resistant to DNA damage-induced apoptosis in vivo. Sasaki et al. (2007)
concluded that BAT3 is an essential regulator of p53-mediated responses
to genotoxic stress, and that BAT3 controls DNA damage-induced
acetylation of p53.
Mariappan et al. (2010) identified a conserved 3-protein complex
composed of BAT3, TRC35 (612056), and UBL4A (312070) that facilitates
tail-anchored protein capture by TRC40 (601913). This BAT3 complex is
recruited to ribosomes synthesizing membrane proteins, interacts with
the transmembrane domains of newly released tail-anchored proteins, and
transfers them to TRC40 for targeting. Depletion of the BAT3 complex
allows non-TRC40 factors to compete for tail-anchored proteins,
explaining their mislocalization in the analogous yeast deletion
strains. Thus, the BAT3 complex acts as a TMD-selective chaperone that
effectively channels tail-anchored proteins to the TRC40 insertion
pathway.
Hessa et al. (2011) reconstituted mislocalized protein degradation in
vitro to identify factors involved in the pathway and found that nascent
membrane proteins tethered to ribosomes are not substrates for
ubiquitination unless they are released into the cytosol. Their
inappropriate release results in capture by the BAG6 complex, a
ribosome-associating chaperone. BAG6 complex-mediated capture depends on
the presence of unprocessed or noninserted hydrophobic domains that
distinguish mislocalized proteins from potential cytosolic proteins. A
subset of these BAG6 complex 'clients' are transferred to TRC40 for
insertion into the membrane, whereas the remainder are rapidly
ubiquitinated. Depletion of the BAG6 complex selectively impairs the
efficient ubiquitination of mislocalized proteins. Thus, Hessa et al.
(2011) concluded that by its presence on ribosomes that are synthesizing
nascent membrane proteins, the BAG6 complex links targeting and
ubiquitination pathways. The authors proposed that such coupling allows
the fast tracking of mislocalized proteins for degradation without
futile engagement of the cytosolic folding machinery.
MAPPING
Spies et al. (1989) mapped the BAG6 (BAT3) gene to chromosome 6p21.
ANIMAL MODEL
Sasaki et al. (2007) found that embryonic lethality of Bat3 deletion in
mice was dependent on genetic background.
*FIELD* RF
1. 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. Nat. Acad. Sci. 87: 2374-2378, 1990.
2. 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.
3. 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.
4. 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.
5. Spies, T.; Blanck, G.; Bresnahan, M.; Sands, J.; Strominger, J.
L.: A new cluster of genes within the human major histocompatibility
complex. Science 243: 214-217, 1989.
*FIELD* CN
Ada Hamosh - updated: 8/4/2011
Ada Hamosh - updated: 9/14/2010
Patricia A. Hartz - updated: 5/15/2007
*FIELD* CD
Victor A. McKusick: 2/2/1989
*FIELD* ED
alopez: 08/15/2011
terry: 8/4/2011
alopez: 9/15/2010
terry: 9/14/2010
mgross: 5/30/2007
terry: 5/15/2007
carol: 7/18/2001
terry: 2/28/2000
carol: 2/22/1999
alopez: 9/5/1997
terry: 10/7/1994
supermim: 3/16/1992
supermim: 3/20/1990
carol: 3/9/1990
ddp: 10/27/1989
root: 2/2/1989
*RECORD*
*FIELD* NO
142590
*FIELD* TI
*142590 BCL2-ASSOCIATED ATHANOGENE 6; BAG6
;;SCYTHE, XENOPUS, HOMOLOG OF;;
HLA-B-ASSOCIATED TRANSCRIPT 3; BAT3;;
read moreD6S52E
*FIELD* TX
CLONING
By chromosome walking with overlapping cosmids, Spies et al. (1989)
isolated a 435-kb DNA segment that was centromeric to HLA-B (142830) in
the human major histocompatibility complex. The presence of additional
genes was suggested by a large cluster of CpG islands. With cosmid
probes, 5 distinct transcripts, including BAT3, were detected in RNA
samples from a variety of cell lines, and the corresponding cDNA clones
were isolated.
From cDNA clones, Banerji et al. (1990) determined the complete
sequences of the closely linked BAT2 (142580) and BAT3 genes. The
putative proteins are 228 and 110 kD, respectively. BAT3 contains an
N-terminal ubiquitin-like domain, and both BAT2 and BAT3 are rich in
proline and include short tracts of polyproline, polyglycine, and
charged amino acids.
GENE FUNCTION
Sasaki et al. (2007) showed that depletion of BAT3 from human and mouse
cells impaired p53 (TP53; 191170)-mediated transactivation of its target
genes Puma (BBC3; 605854) and p21 (CDKN1A; 116899). Although DNA
damage-induced phosphorylation, stabilization, and nuclear accumulation
of p53 were not significantly affected by BAT3 depletion, p53
acetylation was almost completely abolished. BAT3 formed a complex with
p300 (EP300; 602700), and an increased amount of BAT3 enhanced
recruitment of p53 to p300 and facilitated subsequent p53 acetylation.
In contrast, Bat3-depleted cells showed reduced p53-p300 complex
formation and decreased p53 acetylation. Thymocytes from Bat3-deficient
mice exhibited reduced p53-mediated induction of Puma and p21 and were
resistant to DNA damage-induced apoptosis in vivo. Sasaki et al. (2007)
concluded that BAT3 is an essential regulator of p53-mediated responses
to genotoxic stress, and that BAT3 controls DNA damage-induced
acetylation of p53.
Mariappan et al. (2010) identified a conserved 3-protein complex
composed of BAT3, TRC35 (612056), and UBL4A (312070) that facilitates
tail-anchored protein capture by TRC40 (601913). This BAT3 complex is
recruited to ribosomes synthesizing membrane proteins, interacts with
the transmembrane domains of newly released tail-anchored proteins, and
transfers them to TRC40 for targeting. Depletion of the BAT3 complex
allows non-TRC40 factors to compete for tail-anchored proteins,
explaining their mislocalization in the analogous yeast deletion
strains. Thus, the BAT3 complex acts as a TMD-selective chaperone that
effectively channels tail-anchored proteins to the TRC40 insertion
pathway.
Hessa et al. (2011) reconstituted mislocalized protein degradation in
vitro to identify factors involved in the pathway and found that nascent
membrane proteins tethered to ribosomes are not substrates for
ubiquitination unless they are released into the cytosol. Their
inappropriate release results in capture by the BAG6 complex, a
ribosome-associating chaperone. BAG6 complex-mediated capture depends on
the presence of unprocessed or noninserted hydrophobic domains that
distinguish mislocalized proteins from potential cytosolic proteins. A
subset of these BAG6 complex 'clients' are transferred to TRC40 for
insertion into the membrane, whereas the remainder are rapidly
ubiquitinated. Depletion of the BAG6 complex selectively impairs the
efficient ubiquitination of mislocalized proteins. Thus, Hessa et al.
(2011) concluded that by its presence on ribosomes that are synthesizing
nascent membrane proteins, the BAG6 complex links targeting and
ubiquitination pathways. The authors proposed that such coupling allows
the fast tracking of mislocalized proteins for degradation without
futile engagement of the cytosolic folding machinery.
MAPPING
Spies et al. (1989) mapped the BAG6 (BAT3) gene to chromosome 6p21.
ANIMAL MODEL
Sasaki et al. (2007) found that embryonic lethality of Bat3 deletion in
mice was dependent on genetic background.
*FIELD* RF
1. 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. Nat. Acad. Sci. 87: 2374-2378, 1990.
2. 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.
3. 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.
4. 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.
5. Spies, T.; Blanck, G.; Bresnahan, M.; Sands, J.; Strominger, J.
L.: A new cluster of genes within the human major histocompatibility
complex. Science 243: 214-217, 1989.
*FIELD* CN
Ada Hamosh - updated: 8/4/2011
Ada Hamosh - updated: 9/14/2010
Patricia A. Hartz - updated: 5/15/2007
*FIELD* CD
Victor A. McKusick: 2/2/1989
*FIELD* ED
alopez: 08/15/2011
terry: 8/4/2011
alopez: 9/15/2010
terry: 9/14/2010
mgross: 5/30/2007
terry: 5/15/2007
carol: 7/18/2001
terry: 2/28/2000
carol: 2/22/1999
alopez: 9/5/1997
terry: 10/7/1994
supermim: 3/16/1992
supermim: 3/20/1990
carol: 3/9/1990
ddp: 10/27/1989
root: 2/2/1989