Skip Header

 
Contribute Send feedback
Read comments (0) or add your own

Reviewed, UniProtKB/Swiss-Prot P10592 (HSP72_YEAST)

Last modified June 16, 2009. Version 107. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Binary interactions · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Hide | Top

Names and origin

Protein namesRecommended name:
    Heat shock protein SSA2
Gene names
Name: SSA2
Ordered Locus Names: YLL024C
ORF Names: L0931
OrganismSaccharomyces cerevisiae (Baker's yeast) [Complete proteome]
Taxonomic identifier4932 [NCBI]
Taxonomic lineageEukaryota › Fungi › Dikarya › Ascomycota › Saccharomycotina › Saccharomycetes › Saccharomycetales › Saccharomycetaceae › Saccharomyces

Hide | Top

Protein attributes

Sequence length639 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level.

Hide | Top

General annotation (Comments)

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. Ref.7

Subunit structure

Binds human HTN3/histatin-5, a peptide from saliva, and mediates its fungicidal activity. Interacts with NAP1.

Subcellular location

Cytoplasm. Secreted › cell wall.

Post-translational modification

Phosphorylated. Ref.6 Ref.10 Ref.11 Ref.12 Ref.14

Miscellaneous

Present with 364000 molecules/cell in log phase SD medium. Ref.8

Sequence similarities

Belongs to the heat shock protein 70 family.

Hide | Top

Binary interactions

With

Entry

#Exp.

IntAct

Notes

P381391EBI-8603,EBI-20951
P386941EBI-8603,EBI-24511
P400531EBI-8603,EBI-22593
P405061EBI-8603,EBI-25089
P405641EBI-8603,EBI-25380
P405791EBI-8603,EBI-1804
Q050161EBI-8603,EBI-27486
Q065231EBI-8603,EBI-33312
Q089711EBI-8603,EBI-33531
ARO4P324491EBI-8603,EBI-2915
BLM10P435831EBI-8603,EBI-22761
BNA4P381691EBI-8603,EBI-21350
BRO1P485821EBI-8603,EBI-3768
BUL1P485241EBI-8603,EBI-3881
CLN2P204381EBI-8603,EBI-4483
COQ1P189001EBI-8603,EBI-4912
CTC1P071431EBI-8603,EBI-5357
EMI2Q044091EBI-8603,EBI-38225
ENT2Q057851EBI-8603,EBI-35928
ERG10P413381EBI-8603,EBI-19240
ERG19P323771EBI-8603,EBI-6498
ESS1P226962EBI-8603,EBI-6679
FAT1P382251EBI-8603,EBI-6819
GCR2Q017221EBI-8603,EBI-7469
GDA1P326211EBI-8603,EBI-7511
GLR1P419211EBI-8603,EBI-7920
GPI8P490181EBI-8603,EBI-7822
GPP1P412771EBI-8603,EBI-7829
GSH2Q082201EBI-8603,EBI-7915
HNT1Q043441EBI-8603,EBI-8416
ILV6P256051EBI-8603,EBI-9087
MDH1P175051EBI-8603,EBI-10594
MET4P323891EBI-8603,EBI-10757
MLP1Q024551EBI-8603,EBI-11009
MOB1P404841EBI-8603,EBI-11119
NDE1P402151EBI-8603,EBI-27294
NEO1P405271EBI-8603,EBI-3137
NPY1P531641EBI-8603,EBI-11856
NUM1Q004021EBI-8603,EBI-12386
OSH6Q022011EBI-8603,EBI-12636
PRP40P332031EBI-8603,EBI-701
PRS5Q122651EBI-8603,EBI-9886
PUT2P072751EBI-8603,EBI-14303
RKI1Q121891EBI-8603,EBI-15898
SKG3Q063151EBI-8603,EBI-34508
SSM4P403181EBI-8603,EBI-18208
STE24P471541EBI-8603,EBI-18298
TAT2P389671EBI-8603,EBI-18970
UBP10P538741EBI-8603,EBI-19873
URN1Q065251EBI-8603,EBI-35138
USO1P253861EBI-8603,EBI-20157
VPS74Q063851EBI-8603,EBI-35395
WHI3P347611EBI-8603,EBI-20537
YDR531WQ044301EBI-8603,EBI-35891
YLR301WQ059051EBI-8603,EBI-37584
YRB30P531071EBI-8603,EBI-24056

Hide | Top

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed
Chain2 – 639638Heat shock protein SSA2
PRO_0000078386

Amino acid modifications

Modified residue21N-acetylserine Ref.6
Modified residue201Phosphoserine Ref.14
Modified residue351Phosphothreonine Ref.14
Modified residue361Phosphothreonine Ref.14
Modified residue4261Phosphoserine Ref.11
Modified residue5511Phosphoserine Ref.10 Ref.12 Ref.14
Cross-link556Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) Ref.9

Hide | Top

Sequences

Sequence LengthMass (Da)Tools
P10592-1 [UniParc].

Last modified January 23, 2007. Version 3.
Checksum: 129049E21C9DD1F3

FASTA63969,470
        10         20         30         40         50         60 
MSKAVGIDLG TTYSCVAHFS NDRVDIIAND QGNRTTPSFV GFTDTERLIG DAAKNQAAMN 

        70         80         90        100        110        120 
PANTVFDAKR LIGRNFNDPE VQGDMKHFPF KLIDVDGKPQ IQVEFKGETK NFTPEQISSM 

       130        140        150        160        170        180 
VLGKMKETAE SYLGAKVNDA VVTVPAYFND SQRQATKDAG TIAGLNVLRI INEPTAAAIA 

       190        200        210        220        230        240 
YGLDKKGKEE HVLIFDLGGG TFDVSLLSIE DGIFEVKATA GDTHLGGEDF DNRLVNHFIQ 

       250        260        270        280        290        300 
EFKRKNKKDL STNQRALRRL RTACERAKRT LSSSAQTSVE IDSLFEGIDF YTSITRARFE 

       310        320        330        340        350        360 
ELCADLFRST LDPVEKVLRD AKLDKSQVDE IVLVGGSTRI PKVQKLVTDY FNGKEPNRSI 

       370        380        390        400        410        420 
NPDEAVAYGA AVQAAILTGD ESSKTQDLLL LDVAPLSLGI ETAGGVMTKL IPRNSTIPTK 

       430        440        450        460        470        480 
KSEVFSTYAD NQPGVLIQVF EGERAKTKDN NLLGKFELSG IPPAPRGVPQ IEVTFDVDSN 

       490        500        510        520        530        540 
GILNVSAVEK GTGKSNKITI TNDKGRLSKE DIEKMVAEAE KFKEEDEKES QRIASKNQLE 

       550        560        570        580        590        600 
SIAYSLKNTI SEAGDKLEQA DKDAVTKKAE ETIAWLDSNT TATKEEFDDQ LKELQEVANP 

       610        620        630 
IMSKLYQAGG APEGAAPGGF PGGAPPAPEA EGPTVEEVD

« Hide

Hide | Top

References

« Hide 'large scale' references
[1]"The SSA1 and SSA2 genes of the yeast Saccharomyces cerevisiae."
Slater M.R., Craig E.A.
Nucleic Acids Res. 17:805-806(1989) [PubMed: 2644626] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: ATCC 204508 / S288c.
[2]"The sequence of 32kb on the left arm of yeast chromosome XII reveals six known genes, a new member of the seripauperins family and a new ABC transporter homologous to the human multidrug resistance protein."
Purnelle B., Goffeau A.
Yeast 13:183-188(1997) [PubMed: 9046100] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 204508 / S288c.
[3]"The nucleotide sequence of Saccharomyces cerevisiae chromosome XII."
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. expand/collapse author list , 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., Hoheisel J.D.
Nature 387:87-90(1997) [PubMed: 9169871] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 204511 / S288c / AB972.
[4]"Protein identifications for a Saccharomyces cerevisiae protein database."
Garrels J.I., Futcher B., Kobayashi R., Latter G.I., Schwender B., Volpe T., Warner J.R., McLaughlin C.S.
Electrophoresis 15:1466-1486(1994) [PubMed: 7895733] [Abstract]
Cited for: PROTEIN SEQUENCE OF 92-98 AND 326-342.
Strain: ATCC 204508 / S288c.
[5]"Protein expression during exponential growth in 0.7 M NaCl medium of Saccharomyces cerevisiae."
Norbeck J., Blomberg A.
FEMS Microbiol. Lett. 137:1-8(1996) [PubMed: 8935650] [Abstract]
Cited for: PROTEIN SEQUENCE OF 187-196.
Strain: ATCC 38531 / Y41.
[6]"Proteome studies of Saccharomyces cerevisiae: identification and characterization of abundant proteins."
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.
Electrophoresis 18:1347-1360(1997) [PubMed: 9298649] [Abstract]
Cited for: ACETYLATION AT SER-2, PHOSPHORYLATION.
[7]"Candida albicans Ssa1/2p is the cell envelope binding protein for human salivary histatin 5."
Li X.S., Reddy M.S., Baev D., Edgerton M.
J. Biol. Chem. 278:28553-28561(2003) [PubMed: 12761219] [Abstract]
Cited for: FUNCTION, INTERACTION WITH HUMAN HTN3.
[8]"Global analysis of protein expression in yeast."
Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N., O'Shea E.K., Weissman J.S.
Nature 425:737-741(2003) [PubMed: 14562106] [Abstract]
Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
[9]"A proteomics approach to understanding protein ubiquitination."
Peng J., Schwartz D., Elias J.E., Thoreen C.C., Cheng D., Marsischky G., Roelofs J., Finley D., Gygi S.P.
Nat. Biotechnol. 21:921-926(2003) [PubMed: 12872131] [Abstract]
Cited for: UBIQUITINATION [LARGE SCALE ANALYSIS] AT LYS-556, MASS SPECTROMETRY.
[10]"Quantitative phosphoproteomics applied to the yeast pheromone signaling pathway."
Gruhler A., Olsen J.V., Mohammed S., Mortensen P., Faergeman N.J., Mann M., Jensen O.N.
Mol. Cell. Proteomics 4:310-327(2005) [PubMed: 15665377] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-551, MASS SPECTROMETRY.
[11]"Analysis of phosphorylation sites on proteins from Saccharomyces cerevisiae by electron transfer dissociation (ETD) mass spectrometry."
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.
Proc. Natl. Acad. Sci. U.S.A. 104:2193-2198(2007) [PubMed: 17287358] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-426, MASS SPECTROMETRY.
[12]"Proteome-wide identification of in vivo targets of DNA damage checkpoint kinases."
Smolka M.B., Albuquerque C.P., Chen S.H., Zhou H.
Proc. Natl. Acad. Sci. U.S.A. 104:10364-10369(2007) [PubMed: 17563356] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-551, MASS SPECTROMETRY.
[13]"Phosphorylation by casein kinase 2 regulates Nap1 localization and function."
Calvert M.E.K., Keck K.M., Ptak C., Shabanowitz J., Hunt D.F., Pemberton L.F.
Mol. Cell. Biol. 28:1313-1325(2008) [PubMed: 18086883] [Abstract]
Cited for: INTERACTION WITH NAP1, MASS SPECTROMETRY.
[14]"A multidimensional chromatography technology for in-depth phosphoproteome analysis."
Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.
Mol. Cell. Proteomics 7:1389-1396(2008) [PubMed: 18407956] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-20; THR-35; THR-36 AND SER-551, MASS SPECTROMETRY.
+Additional computationally mapped references.

Hide | Top

Cross-references

Sequence databases

X12927 Genomic DNA. Translation: CAA31394.1.
Z73129 Genomic DNA. Translation: CAA97472.1.
X97560 Genomic DNA. Translation: CAA66167.1.
PIRS20139.
RefSeqNP_013076.1.

3D structure databases

HSSPHSSP built from PDB template 3HSC based on UniProtKB P19120.
SMRP10592. Positions 1-550.
ModBaseSearch...

Protein-protein interaction databases

DIPDIP:2265N.
IntActP10592. 968 interactions.

2-D gel databases

SWISS-2DPAGEP10592.
COMPLUYEAST-2DPAGEP10592.

Proteomic databases

PeptideAtlasP10592.
PRIDEP10592.

Genome annotation databases

EnsemblYLL024C. Saccharomyces cerevisiae. [Contig view]
GeneID850636.
GenomeReviewsGene locus YLL024C in contig Y13138_GR.
KEGGsce:YLL024C.
NMPDRfig|4932.3.peg.4067.

Organism-specific databases

CYGDYLL024c.
SGDS000003947. SSA2.
Yeast-GFPSearch...

Phylogenomic databases

HOGENOMP10592.
OMAP10592. SASTWAP.

Gene expression databases

ArrayExpressP10592.
GermOnlineYLL024C. Saccharomyces cerevisiae.

Family and domain databases

InterProIPR018181. Heat_shock_70_CS.
IPR001023. Hsp70.
IPR013126. Hsp_70.
[Graphical view]
PANTHERPTHR19375. Hsp70. 1 hit.
PfamPF00012. HSP70. 1 hit.
[Graphical view]
PRINTSPR00301. HEATSHOCK70.
ProDomPD000089. Hsp70. 1 hit.
[Graphical view] [Entries sharing at least one domain]
PROSITEPS00297. HSP70_1. 1 hit.
PS00329. HSP70_2. 1 hit.
PS01036. HSP70_3. 1 hit.
[Graphical view]
ProtoNetSearch...

Other Resources

NextBio966561.

Hide | Top

Entry information

Entry nameHSP72_YEAST
AccessionPrimary (citable) accession number: P10592
Entry history
Integrated into UniProtKB/Swiss-Prot: July 1, 1989
Last sequence update: January 23, 2007
Last modified: June 16, 2009
This is version 107 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectFPAP (Fungal Proteome Annotation Project)

Hide | Top

Relevant documents

SIMILARITY comments

Index of protein domains and families

Yeast

Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Binary interactions · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents