BAG2_HUMAN
ID BAG2_HUMAN Reviewed; 211 AA.
AC O95816; B4DXE2; Q08AS9; Q6FID0;
DT 11-JAN-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1999, sequence version 1.
DT 03-AUG-2022, entry version 189.
DE RecName: Full=BAG family molecular chaperone regulator 2;
DE Short=BAG-2;
DE AltName: Full=Bcl-2-associated athanogene 2;
GN Name=BAG2;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, AND INTERACTION WITH
RP HSP70/HSC70 CHAPERONES.
RX PubMed=9873016; DOI=10.1074/jbc.274.2.781;
RA Takayama S., Xie Z., Reed J.C.;
RT "An evolutionarily conserved family of Hsp70/Hsc70 molecular chaperone
RT regulators.";
RL J. Biol. Chem. 274:781-786(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Uterus;
RX PubMed=11230166; DOI=10.1101/gr.gr1547r;
RA Wiemann S., Weil B., Wellenreuther R., Gassenhuber J., Glassl S.,
RA Ansorge W., Boecher M., Bloecker H., Bauersachs S., Blum H., Lauber J.,
RA Duesterhoeft A., Beyer A., Koehrer K., Strack N., Mewes H.-W.,
RA Ottenwaelder B., Obermaier B., Tampe J., Heubner D., Wambutt R., Korn B.,
RA Klein M., Poustka A.;
RT "Towards a catalog of human genes and proteins: sequencing and analysis of
RT 500 novel complete protein coding human cDNAs.";
RL Genome Res. 11:422-435(2001).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Testis;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RA Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.;
RT "Cloning of human full open reading frames in Gateway(TM) system entry
RT vector (pDONR201).";
RL Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=14574404; DOI=10.1038/nature02055;
RA Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L.,
RA Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., Gilbert J.G.R.,
RA Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D.,
RA Andrews T.D., Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J.,
RA Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H.,
RA Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J.,
RA Brown J.Y., Burford D.C., Burrill W., Burton J., Carder C., Carter N.P.,
RA Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V.,
RA Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J.,
RA Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., Ellington A.E.,
RA Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J.,
RA French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J.,
RA Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C.,
RA Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A.,
RA Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R.,
RA Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M.,
RA Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K.,
RA Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R.,
RA Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M.,
RA Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A.,
RA Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L.,
RA Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I.,
RA Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y.,
RA Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E.,
RA Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A.,
RA Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W.,
RA Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M.,
RA West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J.,
RA Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M.,
RA Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I.,
RA Rogers J., Beck S.;
RT "The DNA sequence and analysis of human chromosome 6.";
RL Nature 425:805-811(2003).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-73, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007;
RA Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,
RA Greff Z., Keri G., Stemmann O., Mann M.;
RT "Kinase-selective enrichment enables quantitative phosphoproteomics of the
RT kinome across the cell cycle.";
RL Mol. Cell 31:438-448(2008).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-20, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [9]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [10]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-terminal
RT acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-31 AND SER-73, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma, and Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [12]
RP FUNCTION, AND INTERACTION WITH HSPA1A; HSPA1B AND HSPA8.
RX PubMed=24318877; DOI=10.1074/jbc.m113.521997;
RA Rauch J.N., Gestwicki J.E.;
RT "Binding of human nucleotide exchange factors to heat shock protein 70
RT (Hsp70) generates functionally distinct complexes in vitro.";
RL J. Biol. Chem. 289:1402-1414(2014).
RN [13]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [14]
RP INTERACTION WITH NWD1.
RX PubMed=24681825; DOI=10.18632/oncotarget.1850;
RA Correa R.G., Krajewska M., Ware C.F., Gerlic M., Reed J.C.;
RT "The NLR-related protein NWD1 is associated with prostate cancer and
RT modulates androgen receptor signaling.";
RL Oncotarget 5:1666-1682(2014).
RN [15]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25944712; DOI=10.1002/pmic.201400617;
RA Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., Ayoub D.,
RA Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
RT "N-terminome analysis of the human mitochondrial proteome.";
RL Proteomics 15:2519-2524(2015).
RN [16]
RP INTERACTION WITH DNJC9.
RX PubMed=33857403; DOI=10.1016/j.molcel.2021.03.041;
RA Hammond C.M., Bao H., Hendriks I.A., Carraro M., Garcia-Nieto A., Liu Y.,
RA Reveron-Gomez N., Spanos C., Chen L., Rappsilber J., Nielsen M.L.,
RA Patel D.J., Huang H., Groth A.;
RT "DNAJC9 integrates heat shock molecular chaperones into the histone
RT chaperone network.";
RL Mol. Cell 0:0-0(2021).
CC -!- FUNCTION: Co-chaperone for HSP70 and HSC70 chaperone proteins. Acts as
CC a nucleotide-exchange factor (NEF) promoting the release of ADP from
CC the HSP70 and HSC70 proteins thereby triggering client/substrate
CC protein release (PubMed:24318877, PubMed:9873016).
CC {ECO:0000269|PubMed:24318877, ECO:0000269|PubMed:9873016}.
CC -!- SUBUNIT: Binds to the ATPase domain of HSP/HSC70 chaperones
CC (PubMed:9873016). May interact with NWD1 (PubMed:24681825). Interacts
CC with HSPA1A (via NBD), HSPA1B (via NBD) and HSPA8 (PubMed:24318877).
CC May interact with DNJC9; the interaction seems to be histone-dependent
CC (PubMed:33857403). {ECO:0000269|PubMed:24318877,
CC ECO:0000269|PubMed:24681825, ECO:0000269|PubMed:33857403,
CC ECO:0000269|PubMed:9873016}.
CC -!- INTERACTION:
CC O95816; P54253: ATXN1; NbExp=4; IntAct=EBI-355275, EBI-930964;
CC O95816; O95816: BAG2; NbExp=3; IntAct=EBI-355275, EBI-355275;
CC O95816; P53355: DAPK1; NbExp=3; IntAct=EBI-355275, EBI-358616;
CC O95816; Q9NRI5-2: DISC1; NbExp=3; IntAct=EBI-355275, EBI-11988027;
CC O95816; Q99615: DNAJC7; NbExp=2; IntAct=EBI-355275, EBI-357552;
CC O95816; P11142: HSPA8; NbExp=8; IntAct=EBI-355275, EBI-351896;
CC O95816; Q5S007: LRRK2; NbExp=3; IntAct=EBI-355275, EBI-5323863;
CC O95816; Q13164: MAPK7; NbExp=3; IntAct=EBI-355275, EBI-1213983;
CC O95816; Q15773: MLF2; NbExp=4; IntAct=EBI-355275, EBI-1051875;
CC O95816; P04049: RAF1; NbExp=3; IntAct=EBI-355275, EBI-365996;
CC O95816; O95072: REC8; NbExp=2; IntAct=EBI-355275, EBI-9361206;
CC O95816; O43765: SGTA; NbExp=2; IntAct=EBI-355275, EBI-347996;
CC O95816; Q9UNE7: STUB1; NbExp=4; IntAct=EBI-355275, EBI-357085;
CC O95816; Q96BE0; NbExp=2; IntAct=EBI-355275, EBI-9356686;
CC O95816; Q8AZK7: EBNA-LP; Xeno; NbExp=3; IntAct=EBI-355275, EBI-1185167;
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=O95816-1; Sequence=Displayed;
CC Name=2;
CC IsoId=O95816-2; Sequence=VSP_056462;
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AF095192; AAD16121.1; -; mRNA.
DR EMBL; AL050287; CAB43388.1; -; mRNA.
DR EMBL; AK301934; BAG63354.1; -; mRNA.
DR EMBL; CR533496; CAG38527.1; -; mRNA.
DR EMBL; AL031321; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL136311; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC125039; AAI25040.1; -; mRNA.
DR CCDS; CCDS4961.1; -. [O95816-1]
DR PIR; T08764; T08764.
DR RefSeq; NP_004273.1; NM_004282.3. [O95816-1]
DR RefSeq; XP_005249547.1; XM_005249490.3. [O95816-2]
DR RefSeq; XP_011513300.1; XM_011514998.2. [O95816-2]
DR RefSeq; XP_011513301.1; XM_011514999.2. [O95816-2]
DR AlphaFoldDB; O95816; -.
DR SMR; O95816; -.
DR BioGRID; 114908; 617.
DR IntAct; O95816; 222.
DR MINT; O95816; -.
DR STRING; 9606.ENSP00000359727; -.
DR GlyGen; O95816; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; O95816; -.
DR MetOSite; O95816; -.
DR PhosphoSitePlus; O95816; -.
DR SwissPalm; O95816; -.
DR BioMuta; BAG2; -.
DR EPD; O95816; -.
DR jPOST; O95816; -.
DR MassIVE; O95816; -.
DR MaxQB; O95816; -.
DR PaxDb; O95816; -.
DR PeptideAtlas; O95816; -.
DR PRIDE; O95816; -.
DR ProteomicsDB; 51064; -. [O95816-1]
DR ProteomicsDB; 5430; -.
DR TopDownProteomics; O95816-1; -. [O95816-1]
DR Antibodypedia; 17541; 317 antibodies from 35 providers.
DR DNASU; 9532; -.
DR Ensembl; ENST00000370693.5; ENSP00000359727.4; ENSG00000112208.11. [O95816-1]
DR GeneID; 9532; -.
DR KEGG; hsa:9532; -.
DR MANE-Select; ENST00000370693.5; ENSP00000359727.4; NM_004282.4; NP_004273.1.
DR UCSC; uc003pdr.4; human. [O95816-1]
DR CTD; 9532; -.
DR DisGeNET; 9532; -.
DR GeneCards; BAG2; -.
DR HGNC; HGNC:938; BAG2.
DR HPA; ENSG00000112208; Low tissue specificity.
DR MIM; 603882; gene.
DR neXtProt; NX_O95816; -.
DR OpenTargets; ENSG00000112208; -.
DR PharmGKB; PA25238; -.
DR VEuPathDB; HostDB:ENSG00000112208; -.
DR eggNOG; KOG3633; Eukaryota.
DR GeneTree; ENSGT00390000017590; -.
DR HOGENOM; CLU_072417_2_0_1; -.
DR InParanoid; O95816; -.
DR OMA; EMIHNIQ; -.
DR OrthoDB; 1268987at2759; -.
DR PhylomeDB; O95816; -.
DR TreeFam; TF102012; -.
DR PathwayCommons; O95816; -.
DR Reactome; R-HSA-3371453; Regulation of HSF1-mediated heat shock response.
DR SignaLink; O95816; -.
DR SIGNOR; O95816; -.
DR BioGRID-ORCS; 9532; 15 hits in 1072 CRISPR screens.
DR ChiTaRS; BAG2; human.
DR GeneWiki; BAG2; -.
DR GenomeRNAi; 9532; -.
DR Pharos; O95816; Tbio.
DR PRO; PR:O95816; -.
DR Proteomes; UP000005640; Chromosome 6.
DR RNAct; O95816; protein.
DR Bgee; ENSG00000112208; Expressed in cauda epididymis and 168 other tissues.
DR Genevisible; O95816; HS.
DR GO; GO:0030424; C:axon; ISS:ARUK-UCL.
DR GO; GO:0101031; C:chaperone complex; IPI:ARUK-UCL.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0030425; C:dendrite; ISS:ARUK-UCL.
DR GO; GO:1901588; C:dendritic microtubule; IEA:Ensembl.
DR GO; GO:0000774; F:adenyl-nucleotide exchange factor activity; IDA:UniProtKB.
DR GO; GO:0051087; F:chaperone binding; IPI:ARUK-UCL.
DR GO; GO:0031072; F:heat shock protein binding; IEA:Ensembl.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0048156; F:tau protein binding; NAS:ARUK-UCL.
DR GO; GO:0044325; F:transmembrane transporter binding; IPI:ARUK-UCL.
DR GO; GO:0031625; F:ubiquitin protein ligase binding; IEA:Ensembl.
DR GO; GO:0032091; P:negative regulation of protein binding; IDA:ARUK-UCL.
DR GO; GO:0031397; P:negative regulation of protein ubiquitination; IDA:ARUK-UCL.
DR GO; GO:1904667; P:negative regulation of ubiquitin protein ligase activity; IDA:ARUK-UCL.
DR GO; GO:1901800; P:positive regulation of proteasomal protein catabolic process; ISS:ARUK-UCL.
DR GO; GO:0010954; P:positive regulation of protein processing; IMP:ARUK-UCL.
DR GO; GO:0006457; P:protein folding; TAS:ProtInc.
DR GO; GO:0019538; P:protein metabolic process; IDA:MGI.
DR GO; GO:0050821; P:protein stabilization; IDA:ARUK-UCL.
DR InterPro; IPR037689; BAG2.
DR InterPro; IPR003103; BAG_domain.
DR PANTHER; PTHR12334; PTHR12334; 1.
DR SMART; SM00264; BAG; 1.
DR PROSITE; PS51035; BAG; 1.
PE 1: Evidence at protein level;
KW Acetylation; Alternative splicing; Chaperone; Coiled coil; Phosphoprotein;
KW Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0007744|PubMed:22814378"
FT CHAIN 2..211
FT /note="BAG family molecular chaperone regulator 2"
FT /id="PRO_0000088866"
FT DOMAIN 109..189
FT /note="BAG"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00369"
FT COILED 20..61
FT /evidence="ECO:0000255"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0007744|PubMed:22814378"
FT MOD_RES 20
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231"
FT MOD_RES 31
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 73
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18691976,
FT ECO:0007744|PubMed:23186163"
FT VAR_SEQ 1..38
FT /note="MAQAKINAKANEGRFCRSSSMADRSSRLLESLDQLELR -> MPHMW (in
FT isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_056462"
FT CONFLICT 180
FT /note="N -> D (in Ref. 4; CAG38527)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 211 AA; 23772 MW; CAF631F4578FCCA3 CRC64;
MAQAKINAKA NEGRFCRSSS MADRSSRLLE SLDQLELRVE ALREAATAVE QEKEILLEMI
HSIQNSQDMR QISDGEREEL NLTANRLMGR TLTVEVSVET IRNPQQQESL KHATRIIDEV
VNKFLDDLGN AKSHLMSLYS ACSSEVPHGP VDQKFQSIVI GCALEDQKKI KRRLETLLRN
IENSDKAIKL LEHSKGAGSK TLQQNAESRF N
