BAG2_MOUSE
ID BAG2_MOUSE Reviewed; 210 AA.
AC Q91YN9; Q3UMR7;
DT 26-APR-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 03-AUG-2022, entry version 141.
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 Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Embryo, and Lung;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=FVB/N, and FVB/N-3; TISSUE=Mammary tumor;
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 [3]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Heart, Kidney, Lung, Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
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. {ECO:0000250|UniProtKB:O95816}.
CC -!- SUBUNIT: Binds to the ATPase domain of HSP/HSC70 chaperones. May
CC interact with NWD1. Interacts with HSPA1A (via NBD), HSPA1B (via NBD)
CC and HSPA8. May interact with DNJC9; the interaction seems to be
CC histone-dependent (By similarity). {ECO:0000250|UniProtKB:O95816}.
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DR EMBL; AK083600; BAC38967.1; -; mRNA.
DR EMBL; AK144720; BAE26031.1; -; mRNA.
DR EMBL; BC016230; AAH16230.1; -; mRNA.
DR EMBL; BC028944; AAH28944.1; -; mRNA.
DR CCDS; CCDS14864.1; -.
DR RefSeq; NP_663367.1; NM_145392.2.
DR PDB; 3CQX; X-ray; 2.30 A; C/D=107-188.
DR PDB; 3D0T; X-ray; 2.55 A; A/B/C/D=107-189.
DR PDBsum; 3CQX; -.
DR PDBsum; 3D0T; -.
DR AlphaFoldDB; Q91YN9; -.
DR SMR; Q91YN9; -.
DR BioGRID; 229449; 72.
DR IntAct; Q91YN9; 74.
DR MINT; Q91YN9; -.
DR STRING; 10090.ENSMUSP00000042009; -.
DR iPTMnet; Q91YN9; -.
DR PhosphoSitePlus; Q91YN9; -.
DR EPD; Q91YN9; -.
DR MaxQB; Q91YN9; -.
DR PaxDb; Q91YN9; -.
DR PeptideAtlas; Q91YN9; -.
DR PRIDE; Q91YN9; -.
DR ProteomicsDB; 265199; -.
DR TopDownProteomics; Q91YN9; -.
DR Antibodypedia; 17541; 317 antibodies from 35 providers.
DR DNASU; 213539; -.
DR Ensembl; ENSMUST00000044691; ENSMUSP00000042009; ENSMUSG00000042215.
DR GeneID; 213539; -.
DR KEGG; mmu:213539; -.
DR UCSC; uc007any.1; mouse.
DR CTD; 9532; -.
DR MGI; MGI:1891254; Bag2.
DR VEuPathDB; HostDB:ENSMUSG00000042215; -.
DR eggNOG; KOG3633; Eukaryota.
DR GeneTree; ENSGT00390000017590; -.
DR HOGENOM; CLU_072417_2_0_1; -.
DR InParanoid; Q91YN9; -.
DR OMA; EMIHNIQ; -.
DR OrthoDB; 1268987at2759; -.
DR PhylomeDB; Q91YN9; -.
DR TreeFam; TF102012; -.
DR Reactome; R-MMU-3371453; Regulation of HSF1-mediated heat shock response.
DR BioGRID-ORCS; 213539; 2 hits in 72 CRISPR screens.
DR ChiTaRS; Bag2; mouse.
DR EvolutionaryTrace; Q91YN9; -.
DR PRO; PR:Q91YN9; -.
DR Proteomes; UP000000589; Chromosome 1.
DR RNAct; Q91YN9; protein.
DR Bgee; ENSMUSG00000042215; Expressed in ectoplacental cone and 225 other tissues.
DR ExpressionAtlas; Q91YN9; baseline and differential.
DR Genevisible; Q91YN9; MM.
DR GO; GO:0030424; C:axon; IDA:ARUK-UCL.
DR GO; GO:0101031; C:chaperone complex; ISO:MGI.
DR GO; GO:0030425; C:dendrite; IDA:ARUK-UCL.
DR GO; GO:0000774; F:adenyl-nucleotide exchange factor activity; ISS:UniProtKB.
DR GO; GO:0051087; F:chaperone binding; ISO:MGI.
DR GO; GO:0031072; F:heat shock protein binding; IPI:ARUK-UCL.
DR GO; GO:0042802; F:identical protein binding; ISO:MGI.
DR GO; GO:0048156; F:tau protein binding; IPI:ARUK-UCL.
DR GO; GO:0044325; F:transmembrane transporter binding; ISO:MGI.
DR GO; GO:0031625; F:ubiquitin protein ligase binding; IPI:ARUK-UCL.
DR GO; GO:0032091; P:negative regulation of protein binding; ISO:MGI.
DR GO; GO:0031397; P:negative regulation of protein ubiquitination; IGI:ARUK-UCL.
DR GO; GO:1904667; P:negative regulation of ubiquitin protein ligase activity; ISO:MGI.
DR GO; GO:1901800; P:positive regulation of proteasomal protein catabolic process; IGI:ARUK-UCL.
DR GO; GO:0010954; P:positive regulation of protein processing; ISO:MGI.
DR GO; GO:0019538; P:protein metabolic process; ISO:MGI.
DR GO; GO:0050821; P:protein stabilization; ISO:MGI.
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 3D-structure; Acetylation; Chaperone; Coiled coil; Phosphoprotein;
KW Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:O95816"
FT CHAIN 2..210
FT /note="BAG family molecular chaperone regulator 2"
FT /id="PRO_0000088867"
FT DOMAIN 109..189
FT /note="BAG"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00369"
FT COILED 20..60
FT /evidence="ECO:0000255"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000250|UniProtKB:O95816"
FT MOD_RES 20
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O95816"
FT MOD_RES 31
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O95816"
FT MOD_RES 73
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O95816"
FT HELIX 109..142
FT /evidence="ECO:0007829|PDB:3CQX"
FT HELIX 153..160
FT /evidence="ECO:0007829|PDB:3CQX"
FT HELIX 164..186
FT /evidence="ECO:0007829|PDB:3CQX"
SQ SEQUENCE 210 AA; 23474 MW; 96D693F88A1D35D3 CRC64;
MAQAKISAKA HEGRFCRSSS MADRSSRLLE SLDQLELRVE ALRDAATAVE QEKEILLEMI
HSIQNSQDMR QISDGEREEL NLTANRLMGR TLTVEVSVET IRNPQQEESL KHATRIIDEV
VSKFLDDLGN AKSHLMSLYS ACSSEVPPGP VDQKFQSIVI GCALEDQKKI KRRLETLLRN
IDNSDKAIKL LEHAKGAGSK SLQNTDGKFN
