LOCUS HSP72_YEAST 639 aa linear PLN 27-NOV-2024
DEFINITION RecName: Full=Heat shock protein SSA2.
ACCESSION P10592
VERSION P10592.3
DBSOURCE UniProtKB: locus HSP72_YEAST, accession P10592;
class: standard.
extra accessions:D6VXY0
created: Jul 1, 1989.
sequence updated: Jan 23, 2007.
annotation updated: Nov 27, 2024.
xrefs: X12927.1, CAA31394.1, Z73129.1, CAA97472.1, X97560.1,
CAA66167.1, BK006945.2, DAA09296.1, S20139, NP_013076.1
xrefs (non-sequence databases): AlphaFoldDB:P10592, SMR:P10592,
BioGRID:31229, ComplexPortal:CPX-1276, ComplexPortal:CPX-1883,
DIP:DIP-2265N, IntAct:P10592, MINT:P10592, STRING:4932.YLL024C,
CarbonylDB:P10592, iPTMnet:P10592, PaxDb:4932-YLL024C,
PeptideAtlas:P10592, EnsemblFungi:YLL024C_mRNA,
EnsemblFungi:YLL024C, EnsemblFungi:YLL024C, GeneID:850636,
KEGG:sce:YLL024C, AGR:SGD:S000003947, SGD:S000003947,
VEuPathDB:FungiDB:YLL024C, eggNOG:KOG0101,
GeneTree:ENSGT00940000176322, HOGENOM:CLU_005965_7_0_1,
InParanoid:P10592, OMA:VNEAESY, OrthoDB:143at2759,
BioCyc:YEAST:G3O-32128-MONOMER, Reactome:R-SCE-3371453,
Reactome:R-SCE-3371497, Reactome:R-SCE-3371571,
Reactome:R-SCE-6798695, Reactome:R-SCE-8876725,
BioGRID-ORCS:850636, PRO:PR:P10592, Proteomes:UP000002311,
RNAct:P10592, GO:0005737, GO:0005829, GO:1903561, GO:0009277,
GO:0000329, GO:0005739, GO:0005634, GO:0005886, GO:0017053,
GO:0005524, GO:0016887, GO:0140662, GO:0031072, GO:0044183,
GO:0000049, GO:0051082, GO:0009267, GO:0051085, GO:0045892,
GO:0043161, GO:0006457, GO:0042026, GO:0070482, GO:0006616,
GO:0035719, CDD:cd10233, FunFam:2.60.34.10:FF:000002,
FunFam:3.90.640.10:FF:000002, FunFam:3.30.30.30:FF:000001,
FunFam:3.30.420.40:FF:000135, FunFam:1.20.1270.10:FF:000016,
FunFam:3.30.420.40:FF:000026, Gene3D:1.20.1270.10,
Gene3D:3.30.30.30, Gene3D:3.30.420.40, InterPro:IPR043129,
InterPro:IPR018181, InterPro:IPR029048, InterPro:IPR029047,
InterPro:IPR013126, PANTHER:PTHR19375:SF395, PANTHER:PTHR19375,
Pfam:PF00012, PRINTS:PR00301, SUPFAM:SSF53067, SUPFAM:SSF100934,
SUPFAM:SSF100920, PROSITE:PS00297, PROSITE:PS00329, PROSITE:PS01036
KEYWORDS Acetylation; ATP-binding; Cell wall; Cytoplasm; Direct protein
sequencing; Isopeptide bond; Nucleotide-binding; Phosphoprotein;
Reference proteome; Secreted; Stress response; Ubl conjugation.
SOURCE Saccharomyces cerevisiae S288C
ORGANISM Saccharomyces cerevisiae S288C
Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina;
Saccharomycetes; Saccharomycetales; Saccharomycetaceae;
Saccharomyces.
REFERENCE 1 (residues 1 to 639)
AUTHORS Slater,M.R. and Craig,E.A.
TITLE The SSA1 and SSA2 genes of the yeast Saccharomyces cerevisiae
JOURNAL Nucleic Acids Res 17 (2), 805-806 (1989)
PUBMED 2644626
REMARK NUCLEOTIDE SEQUENCE [GENOMIC DNA].;
STRAIN=ATCC 204508 / S288c
REFERENCE 2 (residues 1 to 639)
AUTHORS Purnelle,B. and Goffeau,A.
TITLE The sequence of 32b on the left arm of yeast chromosome XII reveals
six known genes, a new member of the seripauperins family and a new
ABS transporter homologous to the human multidrug resistance
protein
JOURNAL Yeast 13 (2), 183-188 (1997)
PUBMED 9046100
REMARK NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].;
STRAIN=ATCC 204508 / S288c
REFERENCE 3 (residues 1 to 639)
AUTHORS 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. and Cherry,J.M.
TITLE The reference genome sequence of Saccharomyces cerevisiae: then and
now
JOURNAL G3 (Bethesda) 4 (3), 389-398 (2014)
PUBMED 24374639
REMARK GENOME REANNOTATION.;
STRAIN=ATCC 204508 / S288c
Publication Status: Online-Only
REFERENCE 4 (residues 1 to 639)
AUTHORS Johnston,M., Hillier,L.W., Riles,L., Albermann,K., Andre,B.,
Ansorge,W., Benes,V., Brueckner,M., Delius,H., Dubois,E.,
Duesterhoeft,A., Entian,K.-D., Floeth,M., Goffeau,A., Hebling,U.,
Heumann,K., Heuss-Neitzel,D., Hilbert,H., Hilger,F., Kleine,K.,
Koetter,P., Louis,E.J., Messenguy,F., Mewes,H.-W., Miosga,T.,
Moestl,D., Mueller-Auer,S., Nentwich,U., Obermaier,B.,
Piravandi,E., Pohl,T.M., Portetelle,D., Purnelle,B., Rechmann,S.,
Rieger,M., Rinke,M., Rose,M., Scharfe,M., Scherens,B., Scholler,P.,
Schwager,C., Schwarz,S., Underwood,A.P., Urrestarazu,L.A.,
Vandenbol,M., Verhasselt,P., Vierendeels,F., Voet,M., Volckaert,G.,
Voss,H., Wambutt,R., Wedler,E., Wedler,H., Zimmermann,F.K.,
Zollner,A., Hani,J. and Hoheisel,J.D.
TITLE The nucleotide sequence of Saccharomyces cerevisiae chromosome XII
JOURNAL Nature 387 (6632 Suppl), 87-90 (1997)
PUBMED 9169871
REMARK NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].;
STRAIN=ATCC 204508 / S288c
REFERENCE 5 (residues 1 to 639)
AUTHORS Garrels,J.I., Futcher,B., Kobayashi,R., Latter,G.I., Schwender,B.,
Volpe,T., Warner,J.R. and McLaughlin,C.S.
TITLE Protein identifications for a Saccharomyces cerevisiae protein
database
JOURNAL Electrophoresis 15 (11), 1466-1486 (1994)
PUBMED 7895733
REMARK PROTEIN SEQUENCE OF 92-98 AND 326-342.;
STRAIN=ATCC 204508 / S288c
REFERENCE 6 (residues 1 to 639)
AUTHORS Norbeck,J. and Blomberg,A.
TITLE Protein expression during exponential growth in 0.7 M NaCl medium
of Saccharomyces cerevisiae
JOURNAL FEMS Microbiol Lett 137 (1), 1-8 (1996)
PUBMED 8935650
REMARK PROTEIN SEQUENCE OF 187-196.;
STRAIN=ATCC 38531 / Y41
REFERENCE 7 (residues 1 to 639)
AUTHORS 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. and Payne,W.E.
TITLE Proteome studies of Saccharomyces cerevisiae: identification and
characterization of abundant proteins
JOURNAL Electrophoresis 18 (8), 1347-1360 (1997)
PUBMED 9298649
REMARK ACETYLATION AT SER-2, AND PHOSPHORYLATION.
REFERENCE 8 (residues 1 to 639)
AUTHORS Li,X.S., Reddy,M.S., Baev,D. and Edgerton,M.
TITLE Candida albicans Ssa1/2p is the cell envelope binding protein for
human salivary histatin 5
JOURNAL J Biol Chem 278 (31), 28553-28561 (2003)
PUBMED 12761219
REMARK FUNCTION, AND INTERACTION WITH HUMAN HTN3.
REFERENCE 9 (residues 1 to 639)
AUTHORS Ghaemmaghami,S., Huh,W.K., Bower,K., Howson,R.W., Belle,A.,
Dephoure,N., O'Shea,E.K. and Weissman,J.S.
TITLE Global analysis of protein expression in yeast
JOURNAL Nature 425 (6959), 737-741 (2003)
PUBMED 14562106
REMARK LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
REFERENCE 10 (residues 1 to 639)
AUTHORS Peng,J., Schwartz,D., Elias,J.E., Thoreen,C.C., Cheng,D.,
Marsischky,G., Roelofs,J., Finley,D. and Gygi,S.P.
TITLE A proteomics approach to understanding protein ubiquitination
JOURNAL Nat Biotechnol 21 (8), 921-926 (2003)
PUBMED 12872131
REMARK UBIQUITINATION [LARGE SCALE ANALYSIS] AT LYS-556, AND
IDENTIFICATION BY MASS SPECTROMETRY.;
STRAIN=SUB592
REFERENCE 11 (residues 1 to 639)
AUTHORS Chi,A., Huttenhower,C., Geer,L.Y., Coon,J.J., Syka,J.E., Bai,D.L.,
Shabanowitz,J., Burke,D.J., Troyanskaya,O.G. and Hunt,D.F.
TITLE Analysis of phosphorylation sites on proteins from Saccharomyces
cerevisiae by electron transfer dissociation (ETD) mass
spectrometry
JOURNAL Proc Natl Acad Sci U S A 104 (7), 2193-2198 (2007)
PUBMED 17287358
REMARK IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
REFERENCE 12 (residues 1 to 639)
AUTHORS Calvert,M.E., Keck,K.M., Ptak,C., Shabanowitz,J., Hunt,D.F. and
Pemberton,L.F.
TITLE Phosphorylation by casein kinase 2 regulates Nap1 localization and
function
JOURNAL Mol Cell Biol 28 (4), 1313-1325 (2008)
PUBMED 18086883
REMARK INTERACTION WITH NAP1, AND IDENTIFICATION BY MASS SPECTROMETRY.
REFERENCE 13 (residues 1 to 639)
AUTHORS Albuquerque,C.P., Smolka,M.B., Payne,S.H., Bafna,V., Eng,J. and
Zhou,H.
TITLE A multidimensional chromatography technology for in-depth
phosphoproteome analysis
JOURNAL Mol Cell Proteomics 7 (7), 1389-1396 (2008)
PUBMED 18407956
REMARK PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-20, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
REFERENCE 14 (residues 1 to 639)
AUTHORS Holt,L.J., Tuch,B.B., Villen,J., Johnson,A.D., Gygi,S.P. and
Morgan,D.O.
TITLE Global analysis of Cdk1 substrate phosphorylation sites provides
insights into evolution
JOURNAL Science 325 (5948), 1682-1686 (2009)
PUBMED 19779198
REMARK IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
REFERENCE 15 (residues 1 to 639)
AUTHORS Van Damme,P., Lasa,M., Polevoda,B., Gazquez,C., Elosegui-Artola,A.,
Kim,D.S., De Juan-Pardo,E., Demeyer,K., Hole,K., Larrea,E.,
Timmerman,E., Prieto,J., Arnesen,T., Sherman,F., Gevaert,K. and
Aldabe,R.
TITLE N-terminal acetylome analyses and functional insights of the
N-terminal acetyltransferase NatB
JOURNAL Proc Natl Acad Sci U S A 109 (31), 12449-12454 (2012)
PUBMED 22814378
REMARK ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, CLEAVAGE OF INITIATOR
METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS
SPECTROMETRY [LARGE SCALE ANALYSIS].
REFERENCE 16 (residues 1 to 639)
AUTHORS Starita,L.M., Lo,R.S., Eng,J.K., von Haller,P.D. and Fields,S.
TITLE Sites of ubiquitin attachment in Saccharomyces cerevisiae
JOURNAL Proteomics 12 (2), 236-240 (2012)
PUBMED 22106047
REMARK UBIQUITINATION [LARGE SCALE ANALYSIS] AT LYS-556, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
COMMENT On Apr 6, 2005 this sequence version replaced gi:101351.
[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. SSA2 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 NAP1.
{ECO:0000269|PubMed:12761219, ECO:0000269|PubMed:18086883}.
[INTERACTION] P10592; P53940: APJ1; NbExp=2; IntAct=EBI-8603,
EBI-2612341; P10592; P18900: COQ1; NbExp=2; IntAct=EBI-8603,
EBI-4912; P10592; P22696: ESS1; NbExp=2; IntAct=EBI-8603, EBI-6679;
P10592; P02829: HSP82; NbExp=3; IntAct=EBI-8603, EBI-8659; P10592;
P25605: ILV6; NbExp=2; IntAct=EBI-8603, EBI-9087; P10592; P17505:
MDH1; NbExp=2; IntAct=EBI-8603, EBI-10594; P10592; P07275: PUT2;
NbExp=2; IntAct=EBI-8603, EBI-14303; P10592; P25294: SIS1; NbExp=3;
IntAct=EBI-8603, EBI-17244; P10592; Q06385: VPS74; NbExp=2;
IntAct=EBI-8603, EBI-35395; P10592; P34761: WHI3; NbExp=2;
IntAct=EBI-8603, EBI-20537; P10592; Q05016: YMR226C; NbExp=2;
IntAct=EBI-8603, EBI-27486.
[SUBCELLULAR LOCATION] Cytoplasm. Secreted, cell wall.
[MISCELLANEOUS] Present with 364000 molecules/cell in log phase SD
medium. {ECO:0000269|PubMed:14562106}.
[SIMILARITY] Belongs to the heat shock protein 70 family.
{ECO:0000305}.
FEATURES Location/Qualifiers
source 1..639
/organism="Saccharomyces cerevisiae S288C"
/db_xref="taxon:559292"
gene 1..639
/gene="SSA2"
/locus_tag="YLL024C"
/gene_synonym="L0931"
Protein 1..639
/product="Heat shock protein SSA2"
/UniProtKB_evidence="Evidence at protein level"
Region 2..639
/region_name="Mature chain"
/note="Heat shock protein SSA2. /id=PRO_0000078386."
Site 2
/site_type="acetylation"
/note="N-acetylserine.
/evidence=ECO:0000269|PubMed:9298649,
ECO:0007744|PubMed:22814378."
Region 4..639
/region_name="PTZ00009"
/note="heat shock 70 kDa protein; Provisional"
/db_xref="CDD:240227"
Site 20
/site_type="phosphorylation"
/note="Phosphoserine.
/evidence=ECO:0007744|PubMed:18407956."
Site 551
/site_type="phosphorylation"
/note="Phosphoserine.
/evidence=ECO:0000250|UniProtKB:P10591."
Bond bond(556)
/bond_type="xlink"
/note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
G-Cter in ubiquitin).
/evidence=ECO:0007744|PubMed:22106047."
Site 603
/site_type="phosphorylation"
/note="Phosphoserine.
/evidence=ECO:0000250|UniProtKB:P10591."
Region 605..639
/region_name="Region of interest in the sequence"
/note="Disordered. /evidence=ECO:0000256|SAM:MobiDB-lite."
ORIGIN
1 mskavgidlg ttyscvahfs ndrvdiiand qgnrttpsfv gftdterlig daaknqaamn
61 pantvfdakr ligrnfndpe vqgdmkhfpf klidvdgkpq iqvefkgetk nftpeqissm
121 vlgkmketae sylgakvnda vvtvpayfnd sqrqatkdag tiaglnvlri ineptaaaia
181 ygldkkgkee hvlifdlggg tfdvsllsie dgifevkata gdthlggedf dnrlvnhfiq
241 efkrknkkdl stnqralrrl rtacerakrt lsssaqtsve idslfegidf ytsitrarfe
301 elcadlfrst ldpvekvlrd akldksqvde ivlvggstri pkvqklvtdy fngkepnrsi
361 npdeavayga avqaailtgd essktqdlll ldvaplslgi etaggvmtkl iprnstiptk
421 ksevfstyad nqpgvliqvf egeraktkdn nllgkfelsg ippaprgvpq ievtfdvdsn
481 gilnvsavek gtgksnkiti tndkgrlske diekmvaeae kfkeedekes qriasknqle
541 siayslknti seagdkleqa dkdavtkkae etiawldsnt tatkeefddq lkelqevanp
601 imsklyqagg apegaapggf pggappapea egptveevd
//