HSP72_SCHPO
ID HSP72_SCHPO Reviewed; 647 AA.
AC O59855;
DT 06-DEC-2002, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 151.
DE RecName: Full=Probable heat shock protein ssa2;
GN Name=ssa2; ORFNames=SPCC1739.13;
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].
RA Kawamukai M.;
RT "S.pombe heat shock protein of HSP70 family.";
RL Submitted (MAR-1998) to the EMBL/GenBank/DDBJ databases.
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 THR-36; THR-339; THR-417 AND
RP SER-546, AND IDENTIFICATION BY 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 -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the heat shock protein 70 family. {ECO:0000305}.
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DR EMBL; AB012387; BAA25322.1; -; mRNA.
DR EMBL; CU329672; CAA20787.1; -; Genomic_DNA.
DR PIR; T41121; T41121.
DR RefSeq; NP_588421.1; NM_001023412.2.
DR AlphaFoldDB; O59855; -.
DR SMR; O59855; -.
DR BioGRID; 275795; 25.
DR IntAct; O59855; 3.
DR MINT; O59855; -.
DR STRING; 4896.SPCC1739.13.1; -.
DR iPTMnet; O59855; -.
DR MaxQB; O59855; -.
DR PaxDb; O59855; -.
DR PRIDE; O59855; -.
DR EnsemblFungi; SPCC1739.13.1; SPCC1739.13.1:pep; SPCC1739.13.
DR GeneID; 2539225; -.
DR KEGG; spo:SPCC1739.13; -.
DR PomBase; SPCC1739.13; ssa2.
DR VEuPathDB; FungiDB:SPCC1739.13; -.
DR eggNOG; KOG0101; Eukaryota.
DR HOGENOM; CLU_005965_7_0_1; -.
DR InParanoid; O59855; -.
DR OMA; VVVQFKG; -.
DR PhylomeDB; O59855; -.
DR Reactome; R-SPO-3371453; Regulation of HSF1-mediated heat shock response.
DR Reactome; R-SPO-3371497; HSP90 chaperone cycle for steroid hormone receptors (SHR) in the presence of ligand.
DR Reactome; R-SPO-3371568; Attenuation phase.
DR PRO; PR:O59855; -.
DR Proteomes; UP000002485; Chromosome III.
DR GO; GO:0005737; C:cytoplasm; IDA:PomBase.
DR GO; GO:0005829; C:cytosol; HDA:PomBase.
DR GO; GO:0140602; C:nucleolar ring; IDA:PomBase.
DR GO; GO:0005634; C:nucleus; IDA:PomBase.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0071014; C:post-mRNA release spliceosomal complex; IDA:PomBase.
DR GO; GO:0140453; C:protein aggregate center; IDA:PomBase.
DR GO; GO:0005524; F:ATP binding; IBA:GO_Central.
DR GO; GO:0016887; F:ATP hydrolysis activity; ISO:PomBase.
DR GO; GO:0140662; F:ATP-dependent protein folding chaperone; IEA:InterPro.
DR GO; GO:0031072; F:heat shock protein binding; IBA:GO_Central.
DR GO; GO:0051787; F:misfolded protein binding; IBA:GO_Central.
DR GO; GO:0044183; F:protein folding chaperone; IBA:GO_Central.
DR GO; GO:0051082; F:unfolded protein binding; ISO:PomBase.
DR GO; GO:0034605; P:cellular response to heat; IMP:PomBase.
DR GO; GO:0034620; P:cellular response to unfolded protein; IBA:GO_Central.
DR GO; GO:0051085; P:chaperone cofactor-dependent protein refolding; IBA:GO_Central.
DR GO; GO:0042026; P:protein refolding; ISO:PomBase.
DR GO; GO:0016192; P:vesicle-mediated transport; IBA:GO_Central.
DR Gene3D; 1.20.1270.10; -; 1.
DR Gene3D; 2.60.34.10; -; 1.
DR InterPro; IPR043129; ATPase_NBD.
DR InterPro; IPR018181; Heat_shock_70_CS.
DR InterPro; IPR029048; HSP70_C_sf.
DR InterPro; IPR029047; HSP70_peptide-bd_sf.
DR InterPro; IPR013126; Hsp_70_fam.
DR PANTHER; PTHR19375; PTHR19375; 1.
DR Pfam; PF00012; HSP70; 1.
DR SUPFAM; SSF100920; SSF100920; 1.
DR SUPFAM; SSF100934; SSF100934; 1.
DR SUPFAM; SSF53067; SSF53067; 2.
DR PROSITE; PS00297; HSP70_1; 1.
DR PROSITE; PS00329; HSP70_2; 1.
DR PROSITE; PS01036; HSP70_3; 1.
PE 1: Evidence at protein level;
KW Acetylation; ATP-binding; Cytoplasm; Nucleotide-binding; Phosphoprotein;
KW Reference proteome; Stress response.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250"
FT CHAIN 2..647
FT /note="Probable heat shock protein ssa2"
FT /id="PRO_0000078380"
FT REGION 611..647
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 2
FT /note="N-acetylserine"
FT /evidence="ECO:0000250"
FT MOD_RES 36
FT /note="Phosphothreonine"
FT /evidence="ECO:0000269|PubMed:18257517"
FT MOD_RES 339
FT /note="Phosphothreonine"
FT /evidence="ECO:0000269|PubMed:18257517"
FT MOD_RES 417
FT /note="Phosphothreonine"
FT /evidence="ECO:0000269|PubMed:18257517"
FT MOD_RES 546
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18257517"
SQ SEQUENCE 647 AA; 70233 MW; 02CAFB9E80516362 CRC64;
MSKSIGIDLG TTYSCVGHFS NNRVEIIAND QGNRTTPSYV AFTDTERLIG DAAKNQVAMN
PHNTIFDAKR LIGRKFDDPE VQSDMKHWPF KVISKDGKPV LQVEYKGETK TFTPEEISSM
VLMKMRETAE AYLGGKVTDA VVTVPAYFND SQRQATKDAG LIAGLNVLRI INEPTAAAIA
YGLDRSNQGE SNVLIFDLGG GTFDVSLLTI EEGIFEVKAT AGDTHLGGED FDSRLVNHFI
QEFKRKNKKD ITGNARAVRR LRTACERAKR TLSSSAQASI EIDSLFEGID FYTSITRARF
EELCADLFRK TMEPVERVLR DSKVDKASVN EIVLVGGSTR IPRVQKLVSD FFNGKEPCKS
INPDEAVAYG AAVQAAVLTG DTSEKTQDLL LLDVAPLSMG IETAGGVMTP LIKRNTTIPT
KKSEIFSTYS DNQPGVLIQV FEGERARTKD CNLLGKFELS GIPPAPRGVP QIEVTFDVDA
NGILNVSALE KGTGKTQKIT ITNDKGRLSK EEIDRMVAEA EKYKAEDEAE SGRIQAKNHL
ESYAYSLRNS LDDPNLKDKV DASDKETVDK AVKETIEWLD SNTTAAKDEF EAKQKELESV
ANPIMAKIYQ AGGAPGGMPG AAPGAAPGAA PGAAPGGDNG PEVEEVD
