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Heat shock protein SSA1 (Heat shock protein YG100)

 HSP71_YEAST             Reviewed;         642 AA.
P10591; D6VPL2;
01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
23-JAN-2007, sequence version 4.
22-NOV-2017, entry version 196.
RecName: Full=Heat shock protein SSA1;
AltName: Full=Heat shock protein YG100;
Name=SSA1; OrderedLocusNames=YAL005C;
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina;
Saccharomycetes; Saccharomycetales; Saccharomycetaceae; Saccharomyces.
NCBI_TaxID=559292;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=ATCC 204508 / S288c;
PubMed=2644626; DOI=10.1093/nar/17.2.805;
Slater M.R., Craig E.A.;
"The SSA1 and SSA2 genes of the yeast Saccharomyces cerevisiae.";
Nucleic Acids Res. 17:805-806(1989).
[2]
SEQUENCE REVISION TO 208; 418 AND 422.
Slater M.R.;
Submitted (JUN-1993) to the EMBL/GenBank/DDBJ databases.
[3]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=ATCC 204511 / S288c / AB972;
PubMed=7941740; DOI=10.1002/yea.320100413;
Clark M.W., Keng T., Storms R.K., Zhong W.-W., Fortin N., Zeng B.,
Delaney S., Ouellette B.F.F., Barton A.B., Kaback D.B., Bussey H.;
"Sequencing of chromosome I of Saccharomyces cerevisiae: analysis of
the 42 kbp SPO7-CENI-CDC15 region.";
Yeast 10:535-541(1994).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ATCC 204508 / S288c;
PubMed=7731988; DOI=10.1073/pnas.92.9.3809;
Bussey H., Kaback D.B., Zhong W.-W., Vo D.H., Clark M.W., Fortin N.,
Hall J., Ouellette B.F.F., Keng T., Barton A.B., Su Y., Davies C.J.,
Storms R.K.;
"The nucleotide sequence of chromosome I from Saccharomyces
cerevisiae.";
Proc. Natl. Acad. Sci. U.S.A. 92:3809-3813(1995).
[5]
GENOME REANNOTATION.
STRAIN=ATCC 204508 / S288c;
PubMed=24374639; DOI=10.1534/g3.113.008995;
Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M.,
Cherry J.M.;
"The reference genome sequence of Saccharomyces cerevisiae: Then and
now.";
G3 (Bethesda) 4:389-398(2014).
[6]
PROTEIN SEQUENCE OF 92-98 AND 326-342.
STRAIN=ATCC 204508 / S288c;
PubMed=7895733; DOI=10.1002/elps.11501501210;
Garrels J.I., Futcher B., Kobayashi R., Latter G.I., Schwender B.,
Volpe T., Warner J.R., McLaughlin C.S.;
"Protein identifications for a Saccharomyces cerevisiae protein
database.";
Electrophoresis 15:1466-1486(1994).
[7]
PROTEIN SEQUENCE OF 187-196.
STRAIN=ATCC 38531 / Y41;
PubMed=8935650; DOI=10.1111/j.1574-6968.1996.tb08073.x;
Norbeck J., Blomberg A.;
"Protein expression during exponential growth in 0.7 M NaCl medium of
Saccharomyces cerevisiae.";
FEMS Microbiol. Lett. 137:1-8(1996).
[8]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 591-642.
PubMed=6096826; DOI=10.1093/nar/12.24.9367;
Ogden R.C., Lee M.-C., Knapp G.;
"Transfer RNA splicing in Saccharomyces cerevisiae: defining the
substrates.";
Nucleic Acids Res. 12:9367-9382(1984).
[9]
ACETYLATION AT SER-2.
PubMed=9298649; DOI=10.1002/elps.1150180810;
Garrels J.I., McLaughlin C.S., Warner J.R., Futcher B., Latter G.I.,
Kobayashi R., Schwender B., Volpe T., Anderson D.S.,
Mesquita-Fuentes R., Payne W.E.;
"Proteome studies of Saccharomyces cerevisiae: identification and
characterization of abundant proteins.";
Electrophoresis 18:1347-1360(1997).
[10]
INTERACTION WITH PAB1 AND SIS1.
PubMed=11279042; DOI=10.1074/jbc.M100266200;
Horton L.E., James P., Craig E.A., Hensold J.O.;
"The yeast hsp70 homologue Ssa is required for translation and
interacts with Sis1 and Pab1 on translating ribosomes.";
J. Biol. Chem. 276:14426-14433(2001).
[11]
FUNCTION, AND INTERACTION WITH HUMAN HTN3.
PubMed=12761219; DOI=10.1074/jbc.M300680200;
Li X.S., Reddy M.S., Baev D., Edgerton M.;
"Candida albicans Ssa1/2p is the cell envelope binding protein for
human salivary histatin 5.";
J. Biol. Chem. 278:28553-28561(2003).
[12]
SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
PubMed=14562095; DOI=10.1038/nature02026;
Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W.,
Weissman J.S., O'Shea E.K.;
"Global analysis of protein localization in budding yeast.";
Nature 425:686-691(2003).
[13]
LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
PubMed=14562106; DOI=10.1038/nature02046;
Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A.,
Dephoure N., O'Shea E.K., Weissman J.S.;
"Global analysis of protein expression in yeast.";
Nature 425:737-741(2003).
[14]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=17287358; DOI=10.1073/pnas.0607084104;
Chi A., Huttenhower C., Geer L.Y., Coon J.J., Syka J.E.P., Bai D.L.,
Shabanowitz J., Burke D.J., Troyanskaya O.G., Hunt D.F.;
"Analysis of phosphorylation sites on proteins from Saccharomyces
cerevisiae by electron transfer dissociation (ETD) mass
spectrometry.";
Proc. Natl. Acad. Sci. U.S.A. 104:2193-2198(2007).
[15]
INTERACTION WITH NAP1, AND IDENTIFICATION BY MASS SPECTROMETRY.
PubMed=18086883; DOI=10.1128/MCB.01035-07;
Calvert M.E.K., Keck K.M., Ptak C., Shabanowitz J., Hunt D.F.,
Pemberton L.F.;
"Phosphorylation by casein kinase 2 regulates Nap1 localization and
function.";
Mol. Cell. Biol. 28:1313-1325(2008).
[16]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-62 AND SER-603, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=18407956; DOI=10.1074/mcp.M700468-MCP200;
Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.;
"A multidimensional chromatography technology for in-depth
phosphoproteome analysis.";
Mol. Cell. Proteomics 7:1389-1396(2008).
[17]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-551, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19779198; DOI=10.1126/science.1172867;
Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.;
"Global analysis of Cdk1 substrate phosphorylation sites provides
insights into evolution.";
Science 325:1682-1686(2009).
[18]
UBIQUITINATION [LARGE SCALE ANALYSIS] AT LYS-556, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=22106047; DOI=10.1002/pmic.201100166;
Starita L.M., Lo R.S., Eng J.K., von Haller P.D., Fields S.;
"Sites of ubiquitin attachment in Saccharomyces cerevisiae.";
Proteomics 12:236-240(2012).
-!- FUNCTION: May play a role in the transport of polypeptides both
across the mitochondrial membranes and into the endoplasmic
reticulum. A functional difference between SSA1 and SSA2 proteins
is expected. SSA1 can participate in the ATP-dependent disassembly
of clathrin-coated vesicles. {ECO:0000269|PubMed:12761219}.
-!- SUBUNIT: Binds human HTN3/histatin-5, a peptide from saliva, and
mediates its fungicidal activity. Interacts with polyadenylate-
binding protein PAB1 and Hsp70 chaperone SSA1 on translating
ribosomes. Interacts with NAP1. {ECO:0000269|PubMed:11279042,
ECO:0000269|PubMed:12761219, ECO:0000269|PubMed:18086883}.
-!- INTERACTION:
P53940:APJ1; NbExp=2; IntAct=EBI-8591, EBI-2612341;
P35190:CLG1; NbExp=3; IntAct=EBI-8591, EBI-4762;
P38260:FES1; NbExp=3; IntAct=EBI-8591, EBI-21563;
P15108:HSC82; NbExp=2; IntAct=EBI-8591, EBI-8666;
P33416:HSP78; NbExp=2; IntAct=EBI-8591, EBI-8680;
P02829:HSP82; NbExp=3; IntAct=EBI-8591, EBI-8659;
P25693:PCL2; NbExp=3; IntAct=EBI-8591, EBI-4499;
P17157:PHO85; NbExp=2; IntAct=EBI-8591, EBI-13327;
Q01939:RPT6; NbExp=2; IntAct=EBI-8591, EBI-13914;
P25294:SIS1; NbExp=4; IntAct=EBI-8591, EBI-17244;
P32589:SSE1; NbExp=8; IntAct=EBI-8591, EBI-8648;
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:14562095}.
Secreted, cell wall {ECO:0000269|PubMed:14562095}.
-!- MISCELLANEOUS: Present with 269000 molecules/cell in log phase SD
medium. {ECO:0000269|PubMed:14562106}.
-!- SIMILARITY: Belongs to the heat shock protein 70 family.
{ECO:0000305}.
-----------------------------------------------------------------------
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Distributed under the Creative Commons Attribution-NoDerivs License
-----------------------------------------------------------------------
EMBL; X12926; CAA31393.1; -; Genomic_DNA.
EMBL; L22015; AAC04952.1; -; Genomic_DNA.
EMBL; BK006935; DAA06982.1; -; Genomic_DNA.
PIR; S43449; HHBYA1.
RefSeq; NP_009396.2; NM_001178151.1.
PDB; 3LCA; X-ray; 2.19 A; Q=631-642.
PDBsum; 3LCA; -.
ProteinModelPortal; P10591; -.
SMR; P10591; -.
BioGrid; 31786; 777.
DIP; DIP-2253N; -.
IntAct; P10591; 582.
MINT; MINT-8285515; -.
STRING; 4932.YAL005C; -.
ChEMBL; CHEMBL5186; -.
iPTMnet; P10591; -.
COMPLUYEAST-2DPAGE; P10591; -.
SWISS-2DPAGE; P10591; -.
MaxQB; P10591; -.
PRIDE; P10591; -.
EnsemblFungi; YAL005C; YAL005C; YAL005C.
GeneID; 851259; -.
KEGG; sce:YAL005C; -.
EuPathDB; FungiDB:YAL005C; -.
SGD; S000000004; SSA1.
GeneTree; ENSGT00900000141036; -.
HOGENOM; HOG000228135; -.
InParanoid; P10591; -.
KO; K03283; -.
OMA; AYTKNQD; -.
OrthoDB; EOG092C1VPN; -.
BioCyc; YEAST:G3O-28819-MONOMER; -.
EvolutionaryTrace; P10591; -.
PRO; PR:P10591; -.
Proteomes; UP000002311; Chromosome I.
GO; GO:0005737; C:cytoplasm; IDA:SGD.
GO; GO:0005576; C:extracellular region; IEA:UniProtKB-KW.
GO; GO:0009277; C:fungal-type cell wall; IDA:SGD.
GO; GO:0000329; C:fungal-type vacuole membrane; IDA:SGD.
GO; GO:0005634; C:nucleus; IDA:SGD.
GO; GO:0005844; C:polysome; IDA:SGD.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0016887; F:ATPase activity; IDA:SGD.
GO; GO:0000049; F:tRNA binding; IDA:SGD.
GO; GO:0051082; F:unfolded protein binding; IDA:SGD.
GO; GO:0072318; P:clathrin coat disassembly; IDA:SGD.
GO; GO:0002181; P:cytoplasmic translation; IMP:SGD.
GO; GO:0090344; P:negative regulation of cell aging; IMP:SGD.
GO; GO:0043161; P:proteasome-mediated ubiquitin-dependent protein catabolic process; IMP:SGD.
GO; GO:0006457; P:protein folding; IDA:SGD.
GO; GO:0000060; P:protein import into nucleus, translocation; IDA:SGD.
GO; GO:0000209; P:protein polyubiquitination; IDA:SGD.
GO; GO:0042026; P:protein refolding; IDA:SGD.
GO; GO:0006626; P:protein targeting to mitochondrion; IMP:SGD.
GO; GO:0006616; P:SRP-dependent cotranslational protein targeting to membrane, translocation; IDA:SGD.
GO; GO:0035617; P:stress granule disassembly; IDA:SGD.
Gene3D; 1.20.1270.10; -; 1.
Gene3D; 2.60.34.10; -; 1.
InterPro; IPR018181; Heat_shock_70_CS.
InterPro; IPR029048; HSP70_C_sf.
InterPro; IPR029047; HSP70_peptide-bd_sf.
InterPro; IPR013126; Hsp_70_fam.
Pfam; PF00012; HSP70; 1.
PRINTS; PR00301; HEATSHOCK70.
SUPFAM; SSF100920; SSF100920; 1.
SUPFAM; SSF100934; SSF100934; 1.
PROSITE; PS00297; HSP70_1; 1.
PROSITE; PS00329; HSP70_2; 1.
PROSITE; PS01036; HSP70_3; 1.
1: Evidence at protein level;
3D-structure; Acetylation; ATP-binding; Cell wall; Complete proteome;
Cytoplasm; Direct protein sequencing; Isopeptide bond;
Nucleotide-binding; Phosphoprotein; Reference proteome; Secreted;
Stress response; Ubl conjugation.
INIT_MET 1 1 Removed. {ECO:0000269|PubMed:9298649}.
CHAIN 2 642 Heat shock protein SSA1.
/FTId=PRO_0000078385.
MOD_RES 2 2 N-acetylserine.
{ECO:0000269|PubMed:9298649}.
MOD_RES 62 62 Phosphoserine.
{ECO:0000244|PubMed:18407956}.
MOD_RES 551 551 Phosphoserine.
{ECO:0000244|PubMed:19779198}.
MOD_RES 603 603 Phosphoserine.
{ECO:0000244|PubMed:18407956}.
CROSSLNK 556 556 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in ubiquitin).
{ECO:0000244|PubMed:22106047}.
CONFLICT 208 208 S -> F (in Ref. 3; AAC04952).
{ECO:0000305}.
CONFLICT 418 418 P -> S (in Ref. 3; AAC04952).
{ECO:0000305}.
CONFLICT 422 422 S -> F (in Ref. 3; AAC04952).
{ECO:0000305}.
SEQUENCE 642 AA; 69657 MW; 249D8A3BC42527CA CRC64;
MSKAVGIDLG TTYSCVAHFA NDRVDIIAND QGNRTTPSFV AFTDTERLIG DAAKNQAAMN
PSNTVFDAKR LIGRNFNDPE VQADMKHFPF KLIDVDGKPQ IQVEFKGETK NFTPEQISSM
VLGKMKETAE SYLGAKVNDA VVTVPAYFND SQRQATKDAG TIAGLNVLRI INEPTAAAIA
YGLDKKGKEE HVLIFDLGGG TFDVSLLSIE DGIFEVKATA GDTHLGGEDF DNRLVNHFIQ
EFKRKNKKDL STNQRALRRL RTACERAKRT LSSSAQTSVE IDSLFEGIDF YTSITRARFE
ELCADLFRST LDPVEKVLRD AKLDKSQVDE IVLVGGSTRI PKVQKLVTDY FNGKEPNRSI
NPDEAVAYGA AVQAAILTGD ESSKTQDLLL LDVAPLSLGI ETAGGVMTKL IPRNSTIPTK
KSEIFSTYAD NQPGVLIQVF EGERAKTKDN NLLGKFELSG IPPAPRGVPQ IEVTFDVDSN
GILNVSAVEK GTGKSNKITI TNDKGRLSKE DIEKMVAEAE KFKEEDEKES QRIASKNQLE
SIAYSLKNTI SEAGDKLEQA DKDTVTKKAE ETISWLDSNT TASKEEFDDK LKELQDIANP
IMSKLYQAGG APGGAAGGAP GGFPGGAPPA PEAEGPTVEE VD


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