SSA1/YAL005C Protein Information Help

Standard Name Ssa1p 1
Systematic Name Yal005cp
Alias Yg100p 2
ORF Classification Verified
Description ATPase involved in protein folding and NLS-directed nuclear transport; member of HSP70 family; forms chaperone complex with Ydj1p; localized to nucleus, cytoplasm, and cell wall; 98% identical with paralog Ssa2p, but subtle differences between the two proteins provide functional specificity with respect to propagation of yeast [URE3] prions and vacuolar-mediated degradations of gluconeogenesis enzymes; general targeting factor of Hsp104p to prion fibrils (3, 4, 5, 6, 7, 8, 9)
Name Description Stress-Seventy subfamily A
Experimental Data
Molecules/cell 269000 10
Predicted Sequence Formatted Sequence or sequence in FASTA format
Length (a.a.) 642
Molecular Weight (Da) 69,657
Isoelectric Point (pI) 4.82

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Post-translational Modifications PhosphoGRID | PhosphoPep Database
Domains/motifs See the graphical view and list of proteins that share domains/motifs in common with Ssa1p (InterPro)
Physical Interactions There are 752 total physical interactions (BioGRID)
Homologs PDB Homologs | BLASTP | BLASTP v. fungi | Fungal Alignment | Synteny Viewer
External Sequence Databases EBI: UPI0000168E53 | P10591
MIPS: YAL005C
NCBI: 144228166 | 315364443 | 349747 | 417149 | NP_009396.2
GenBank/EMBL/DDBJ: DAA06982.1 | L22015 | X12926
Amino Acid Sequence (or in FASTA format)
       1  MSKAVGIDLG TTYSCVAHFA NDRVDIIAND QGNRTTPSFV AFTDTERLIG
      51  DAAKNQAAMN PSNTVFDAKR LIGRNFNDPE VQADMKHFPF KLIDVDGKPQ
     101  IQVEFKGETK NFTPEQISSM VLGKMKETAE SYLGAKVNDA VVTVPAYFND
     151  SQRQATKDAG TIAGLNVLRI INEPTAAAIA YGLDKKGKEE HVLIFDLGGG
     201  TFDVSLLSIE DGIFEVKATA GDTHLGGEDF DNRLVNHFIQ EFKRKNKKDL
     251  STNQRALRRL RTACERAKRT LSSSAQTSVE IDSLFEGIDF YTSITRARFE
     301  ELCADLFRST LDPVEKVLRD AKLDKSQVDE IVLVGGSTRI PKVQKLVTDY
     351  FNGKEPNRSI NPDEAVAYGA AVQAAILTGD ESSKTQDLLL LDVAPLSLGI
     401  ETAGGVMTKL IPRNSTIPTK KSEIFSTYAD NQPGVLIQVF EGERAKTKDN
     451  NLLGKFELSG IPPAPRGVPQ IEVTFDVDSN GILNVSAVEK GTGKSNKITI
     501  TNDKGRLSKE DIEKMVAEAE KFKEEDEKES QRIASKNQLE SIAYSLKNTI
     551  SEAGDKLEQA DKDTVTKKAE ETISWLDSNT TASKEEFDDK LKELQDIANP
     601  IMSKLYQAGG APGGAAGGAP GGFPGGAPPA PEAEGPTVEE VD*       

external links for Ssa1p
Homologs Interaction Resources Protein databases/Other Localization Resources
BLASTP (NCBI) BioGRID SCOP Superfamily Organelle DB
Ashbya (AGD) BOND GPMdb (Mass Spec.) YPL+
Aspergillus (AspGD) BioPIXIE MIPS YeastGFP
YGOB CYC2008 (complexes) Pfam domains
YOGY Complexome YeastRC Structure Prediction (Seattle)

DIP


GeneMANIA

References cited on this page View Complete Literature Guide for Ssa1p
1) Slater, M.  (1989) Personal Communication, Mortimer Map Edition 10
2) Ingolia TD, et al.  (1982) Saccharomyces cerevisiae contains a complex multigene family related to the major heat shock-inducible gene of Drosophila. Mol Cell Biol 2(11):1388-98
3) Lopez-Ribot JL and Chaffin WL  (1996) Members of the Hsp70 family of proteins in the cell wall of Saccharomyces cerevisiae. J Bacteriol 178(15):4724-6
4) Kim S, et al.  (1998) Folding in vivo of a newly translated yeast cytosolic enzyme is mediated by the SSA class of cytosolic yeast Hsp70 proteins. Proc Natl Acad Sci U S A 95(22):12860-5
5) Shulga N, et al.  (1999) A nuclear export signal prevents Saccharomyces cerevisiae Hsp70 Ssb1p from stimulating nuclear localization signal-directed nuclear transport. J Biol Chem 274(23):16501-7
6) Ziegelhoffer T, et al.  (1995) The dissociation of ATP from hsp70 of Saccharomyces cerevisiae is stimulated by both Ydj1p and peptide substrates. J Biol Chem 270(18):10412-9
7) Bush GL and Meyer DI  (1996) The refolding activity of the yeast heat shock proteins Ssa1 and Ssa2 defines their role in protein translocation. J Cell Biol 135(5):1229-37
8) Sharma D and Masison DC  (2011) Single methyl group determines prion propagation and protein degradation activities of yeast heat shock protein (Hsp)-70 chaperones Ssa1p and Ssa2p. Proc Natl Acad Sci U S A 108(33):13665-70
9) Winkler J, et al.  (2012) Hsp70 targets Hsp100 chaperones to substrates for protein disaggregation and prion fragmentation. J Cell Biol 198(3):387-404
10) Ghaemmaghami S, et al.  (2003) Global analysis of protein expression in yeast. Nature 425(6959):737-41