ID   BAG1B_SCHPO             Reviewed;         206 AA.
AC   O59739;
DT   06-DEC-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-AUG-1998, sequence version 1.
DT   03-AUG-2022, entry version 113.
DE   RecName: Full=BAG family molecular chaperone regulator 1B;
DE            Short=BAG-1B;
GN   Name=bag102; Synonyms=bag1-b; ORFNames=SPBC530.03c;
OS   Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC   Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae;
OC   Schizosaccharomyces.
OX   NCBI_TaxID=284812;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
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 GENOMIC DNA].
RC   STRAIN=972 / ATCC 24843;
RX   PubMed=11859360; DOI=10.1038/nature724;
RA   Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A.,
RA   Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S.,
RA   Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.,
RA   Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S.,
RA   Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S.,
RA   Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D.,
RA   Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P.,
RA   Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K.,
RA   O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M.,
RA   Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N.,
RA   Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A.,
RA   Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R.,
RA   Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M.,
RA   Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A.,
RA   Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A.,
RA   Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H.,
RA   Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S.,
RA   Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C.,
RA   Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A.,
RA   Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M.,
RA   del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S.,
RA   Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R.,
RA   Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G.,
RA   Nurse P.;
RT   "The genome sequence of Schizosaccharomyces pombe.";
RL   Nature 415:871-880(2002).
RN   [3]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-144, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY.
RX   PubMed=18257517; DOI=10.1021/pr7006335;
RA   Wilson-Grady J.T., Villen J., Gygi S.P.;
RT   "Phosphoproteome analysis of fission yeast.";
RL   J. Proteome Res. 7:1088-1097(2008).
CC   -!- FUNCTION: Inhibits the chaperone activity of HSP70/HSC70 by promoting
CC       substrate release. {ECO:0000250}.
CC   -!- SUBUNIT: Binds to the ATPase domain of HSP70/HSC chaperones.
CC       {ECO:0000250}.
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DR   EMBL; CU329671; CAA19169.1; -; Genomic_DNA.
DR   EMBL; AF095790; AAD16127.1; -; mRNA.
DR   PIR; T40519; T40519.
DR   RefSeq; NP_595316.1; NM_001021223.2.
DR   AlphaFoldDB; O59739; -.
DR   SMR; O59739; -.
DR   BioGRID; 277091; 22.
DR   STRING; 4896.SPBC530.03c.1; -.
DR   iPTMnet; O59739; -.
DR   MaxQB; O59739; -.
DR   PaxDb; O59739; -.
DR   EnsemblFungi; SPBC530.03c.1; SPBC530.03c.1:pep; SPBC530.03c.
DR   GeneID; 2540564; -.
DR   KEGG; spo:SPBC530.03c; -.
DR   PomBase; SPBC530.03c; bag102.
DR   VEuPathDB; FungiDB:SPBC530.03c; -.
DR   eggNOG; KOG4361; Eukaryota.
DR   HOGENOM; CLU_1300318_0_0_1; -.
DR   InParanoid; O59739; -.
DR   OMA; QQYCSSP; -.
DR   PRO; PR:O59739; -.
DR   Proteomes; UP000002485; Chromosome II.
DR   GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR   GO; GO:0016020; C:membrane; IBA:GO_Central.
DR   GO; GO:0031965; C:nuclear membrane; IDA:PomBase.
DR   GO; GO:0000774; F:adenyl-nucleotide exchange factor activity; IBA:GO_Central.
DR   GO; GO:0051087; F:chaperone binding; IBA:GO_Central.
DR   GO; GO:0071630; P:nuclear protein quality control by the ubiquitin-proteasome system; IMP:PomBase.
DR   GO; GO:0006457; P:protein folding; ISO:PomBase.
DR   GO; GO:0050821; P:protein stabilization; IBA:GO_Central.
DR   Gene3D; 1.20.58.120; -; 1.
DR   InterPro; IPR017093; BAG-1.
DR   InterPro; IPR039773; BAG_chaperone_regulator.
DR   InterPro; IPR036533; BAG_dom_sf.
DR   InterPro; IPR003103; BAG_domain.
DR   PANTHER; PTHR12329; PTHR12329; 1.
DR   PANTHER; PTHR12329:SF16; PTHR12329:SF16; 1.
DR   Pfam; PF02179; BAG; 1.
DR   SMART; SM00264; BAG; 1.
DR   SUPFAM; SSF63491; SSF63491; 1.
DR   PROSITE; PS51035; BAG; 1.
PE   1: Evidence at protein level;
KW   Chaperone; Phosphoprotein; Reference proteome.
FT   CHAIN           1..206
FT                   /note="BAG family molecular chaperone regulator 1B"
FT                   /id="PRO_0000088880"
FT   DOMAIN          122..202
FT                   /note="BAG"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00369"
FT   MOD_RES         144
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000269|PubMed:18257517"
SQ   SEQUENCE   206 AA;  23325 MW;  E39F5E6123F0DB60 CRC64;
     MSFFTQLCSM DKKYWISLAV LSVTVLISAL LKKRATETED IVVVHYDGEK LNFVLRQPRL
     NMVSYTSFLR RVCNAFSVMP DKASLKLNGV TLKDGSLSDQ NVQNGSELEL ELPKLSPAMQ
     QIEAYIDELQ QDLVPKIEAF CQSSPASAQD VQDLHTRLSE TLLARMIKLD AVNVEDDPEA
     RLKRKEAIRL SQQYLSKLDS TKNQNK