ID   BAG2_HUMAN              Reviewed;         211 AA.
AC   O95816; Q08AS9; Q6FID0;
DT   11-JAN-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1999, sequence version 1.
DT   03-NOV-2009, entry version 75.
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;
OC   Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC   Catarrhini; Hominidae; Homo.
OX   NCBI_TaxID=9606;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   MEDLINE=99091615; 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].
RC   TISSUE=Uterus;
RX   MEDLINE=21154917; 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.,
RA   Lauber J., Duesterhoeft A., Beyer A., Koehrer K., Strack N.,
RA   Mewes H.-W., Ottenwaelder B., Obermaier B., Tampe J., Heubner D.,
RA   Wambutt R., Korn B., Klein M., Poustka A.;
RT   "Towards a catalog of human genes and proteins: sequencing and
RT   analysis of 500 novel complete protein coding human cDNAs.";
RL   Genome Res. 11:422-435(2001).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   MEDLINE=22935763; 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   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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   [6]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-73, AND MASS
RP   SPECTROMETRY.
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
RT   the kinome across the cell cycle.";
RL   Mol. Cell 31:438-448(2008).
RN   [7]
RP   IDENTIFICATION [LARGE SCALE ANALYSIS], AND MASS SPECTROMETRY.
RA   Colinge J., Superti-Furga G., Bennett K.L.;
RL   Submitted (OCT-2008) to UniProtKB.
RN   [8]
RP   ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-111, AND MASS SPECTROMETRY.
RX   PubMed=19608861; DOI=10.1126/science.1175371;
RA   Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.,
RA   Olsen J.V., Mann M.;
RT   "Lysine acetylation targets protein complexes and co-regulates major
RT   cellular functions.";
RL   Science 325:834-840(2009).
CC   -!- FUNCTION: Inhibits the chaperone activity of HSP70/HSC70 by
CC       promoting substrate release.
CC   -!- SUBUNIT: Binds to the ATPase domain of HSP70/HSC chaperones.
CC   -!- INTERACTION:
CC       Q15773:MLF2; NbExp=1; IntAct=EBI-355275, EBI-1051875;
CC       P43686:PSMC4; NbExp=1; IntAct=EBI-355275, EBI-743997;
CC   -!- SIMILARITY: Contains 1 BAG domain.
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DR   EMBL; AF095192; AAD16121.1; -; mRNA.
DR   EMBL; AL050287; CAB43388.1; -; mRNA.
DR   EMBL; CR533496; CAG38527.1; -; mRNA.
DR   EMBL; AL031321; CAI21565.1; -; Genomic_DNA.
DR   EMBL; AL136311; CAI21565.1; JOINED; Genomic_DNA.
DR   EMBL; AL136311; CAI20515.1; -; Genomic_DNA.
DR   EMBL; AL031321; CAI20515.1; JOINED; Genomic_DNA.
DR   EMBL; BC125039; AAI25040.1; -; mRNA.
DR   IPI; IPI00000643; -.
DR   PIR; T08764; T08764.
DR   RefSeq; NP_004273.1; -.
DR   UniGene; Hs.55220; -.
DR   IntAct; O95816; 22.
DR   STRING; O95816; -.
DR   PhosphoSite; O95816; -.
DR   PeptideAtlas; O95816; -.
DR   PRIDE; O95816; -.
DR   Ensembl; ENST00000370693; ENSP00000359727; ENSG00000112208; Homo sapiens.
DR   Ensembl; ENST00000438730; ENSP00000401851; ENSG00000112208; Homo sapiens.
DR   Ensembl; ENST00000447026; ENSP00000403477; ENSG00000112208; Homo sapiens.
DR   GeneID; 9532; -.
DR   KEGG; hsa:9532; -.
DR   UCSC; uc003pdr.1; human.
DR   CTD; 9532; -.
DR   GeneCards; GC06P057145; -.
DR   H-InvDB; HIX0022299; -.
DR   HGNC; HGNC:938; BAG2.
DR   MIM; 603882; gene.
DR   PharmGKB; PA25238; -.
DR   HOGENOM; O95816; -.
DR   HOVERGEN; O95816; -.
DR   OMA; VVSKFLD; -.
DR   NextBio; 35736; -.
DR   ArrayExpress; O95816; -.
DR   Bgee; O95816; -.
DR   CleanEx; HS_BAG2; -.
DR   Genevestigator; O95816; -.
DR   GermOnline; ENSG00000112208; Homo sapiens.
DR   GO; GO:0005515; F:protein binding; IPI:IntAct.
DR   GO; GO:0006915; P:apoptosis; IEA:InterPro.
DR   GO; GO:0006457; P:protein folding; TAS:ProtInc.
DR   InterPro; IPR003103; Apoptosis_reg_Bcl-2_prot_BAG.
DR   Pfam; PF02179; BAG; 1.
DR   SMART; SM00264; BAG; 1.
DR   PROSITE; PS51035; BAG; 1.
PE   1: Evidence at protein level;
KW   Acetylation; Chaperone; Coiled coil; Complete proteome;
KW   Phosphoprotein.
FT   CHAIN         1    211       BAG family molecular chaperone regulator
FT                                2.
FT                                /FTId=PRO_0000088866.
FT   DOMAIN      109    189       BAG.
FT   COILED       20     61       Potential.
FT   MOD_RES      73     73       Phosphoserine.
FT   MOD_RES     111    111       N6-acetyllysine.
FT   CONFLICT    180    180       N -> D (in Ref. 3; CAG38527).
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
//