SSA2/YLL024C Protein Information Help

Standard Name Ssa2p
Systematic Name Yll024cp
Alias Yg102p 1
ORF Classification Verified
Description ATP binding protein involved in protein folding and vacuolar import of proteins; member of heat shock protein 70 (HSP70) family; associated with the chaperonin-containing T-complex; present in the cytoplasm, vacuolar membrane and cell wall; 98% identical with paralog Ssa1p, 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 (2, 3, 4, 5, 6, 7)
Name Description Stress-Seventy subfamily A
Experimental Data
Molecules/cell 364000 8
Predicted Sequence Formatted Sequence or sequence in FASTA format
Length (a.a.) 639
Molecular Weight (Da) 69,469
Isoelectric Point (pI) 4.77

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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 Ssa2p (InterPro)
Physical Interactions There are 415 total physical interactions (BioGRID)
Homologs PDB Homologs | BLASTP | BLASTP v. fungi | Fungal Alignment | Synteny Viewer
External Sequence Databases EBI: UPI000016838F | P10592
MIPS: YLL024C
NCBI: 123624 | 1297007 | 1360202 | 4546 | 6323004 | NP_013076.1
GenBank/EMBL/DDBJ: DAA09296.1 | X12927 | X97560 | Z73129
Amino Acid Sequence (or in FASTA format)
 
       1  MSKAVGIDLG TTYSCVAHFS NDRVDIIAND QGNRTTPSFV GFTDTERLIG
      51  DAAKNQAAMN PANTVFDAKR LIGRNFNDPE VQGDMKHFPF 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 KSEVFSTYAD NQPGVLIQVF EGERAKTKDN
     451  NLLGKFELSG IPPAPRGVPQ IEVTFDVDSN GILNVSAVEK GTGKSNKITI
     501  TNDKGRLSKE DIEKMVAEAE KFKEEDEKES QRIASKNQLE SIAYSLKNTI
     551  SEAGDKLEQA DKDAVTKKAE ETIAWLDSNT TATKEEFDDQ LKELQEVANP
     601  IMSKLYQAGG APEGAAPGGF PGGAPPAPEA EGPTVEEVD*

external links for Ssa2p
Homologs Interaction Resources Protein databases/Other Localization Resources
BLASTP (NCBI) BioGRID SCOP Superfamily Organelle DB
Ashbya (AGD) BOND GPMdb (Mass Spec.) YPL+
YGOB BioPIXIE MIPS YeastGFP
YOGY CYC2008 (complexes) Pfam domains YeastRC Public Image Repository

Complexome YeastRC Structure Prediction (Seattle)

DIP


GeneMANIA

References cited on this page View Complete Literature Guide for Ssa2p
1) Werner-Washburne M, et al.  (1987) Complex interactions among members of an essential subfamily of hsp70 genes in Saccharomyces cerevisiae. Mol Cell Biol 7(7):2568-77
2) 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
3) Satyanarayana C, et al.  (2000) Cytosolic Hsp70s are involved in the transport of aminopeptidase 1 from the cytoplasm into the vacuole. FEBS Lett 470(3):232-8
4) Unno K, et al.  (1997) Role of Hsp70 subfamily, Ssa, in protein folding in yeast cells, seen in luciferase-transformed ssa mutants. Biol Pharm Bull 20(12):1240-4
5) Brown CR, et al.  (2000) The heat shock protein Ssa2p is required for import of fructose-1, 6-bisphosphatase into Vid vesicles. J Cell Biol 150(1):65-76
6) Kabir MA, et al.  (2005) Physiological effects of unassembled chaperonin Cct subunits in the yeast Saccharomyces cerevisiae. Yeast 22(3):219-39
7) 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
8) Ghaemmaghami S, et al.  (2003) Global analysis of protein expression in yeast. Nature 425(6959):737-41