SSB1/YDL229W Protein Information Help

Standard Name Ssb1p
Systematic Name Ydl229wp
Alias Yg101p 1
ORF Classification Verified
Description Cytoplasmic ATPase that is a ribosome-associated molecular chaperone; functions with J-protein partner Zuo1p; may be involved in folding of newly-made polypeptide chains; member of the HSP70 family; interacts with phosphatase subunit Reg1p; SSB1 has a paralog, SSB2, that arose from the whole genome duplication (2, 3, 4, 5, 6, 7, 8, 9)
Name Description Stress-Seventy subfamily B
Experimental Data
Molecules/cell 170000 10
Predicted Sequence Formatted Sequence or sequence in FASTA format
Length (a.a.) 613
Molecular Weight (Da) 66,601
Isoelectric Point (pI) 5.18

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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 Ssb1p (InterPro)
Physical Interactions There are 959 total physical interactions (BioGRID)
Homologs PDB Homologs | BLASTP | BLASTP v. fungi | Fungal Alignment | Synteny Viewer
External Sequence Databases EBI: UPI00001682D1 | P11484
MIPS: YDL229W
NCBI: 123635 | 1431385 | 172722 | 225734321 | 225734322 | 454437 | 4548 | 6319972 | NP_010052.1
GenBank/EMBL/DDBJ: DAA11637.1 | M17585 | M25395 | X13713 | Z74277
Amino Acid Sequence (or in FASTA format)
       1  MAEGVFQGAI GIDLGTTYSC VATYESSVEI IANEQGNRVT PSFVAFTPEE
      51  RLIGDAAKNQ AALNPRNTVF DAKRLIGRRF DDESVQKDMK TWPFKVIDVD
     101  GNPVIEVQYL EETKTFSPQE ISAMVLTKMK EIAEAKIGKK VEKAVITVPA
     151  YFNDAQRQAT KDAGAISGLN VLRIINEPTA AAIAYGLGAG KSEKERHVLI
     201  FDLGGGTFDV SLLHIAGGVY TVKSTSGNTH LGGQDFDTNL LEHFKAEFKK
     251  KTGLDISDDA RALRRLRTAA ERAKRTLSSV TQTTVEVDSL FDGEDFESSL
     301  TRARFEDLNA ALFKSTLEPV EQVLKDAKIS KSQIDEVVLV GGSTRIPKVQ
     351  KLLSDFFDGK QLEKSINPDE AVAYGAAVQG AILTGQSTSD ETKDLLLLDV
     401  APLSLGVGMQ GDMFGIVVPR NTTVPTIKRR TFTTCADNQT TVQFPVYQGE
     451  RVNCKENTLL GEFDLKNIPM MPAGEPVLEA IFEVDANGIL KVTAVEKSTG
     501  KSSNITISNA VGRLSSEEIE KMVNQAEEFK AADEAFAKKH EARQRLESYV
     551  ASIEQTVTDP VLSSKLKRGS KSKIEAALSD ALAALQIEDP SADELRKAEV
     601  GLKRVVTKAM SSR*                                       

external links for Ssb1p
Homologs Interaction Resources Protein databases/Other Localization Resources
BLASTP (NCBI) BioGRID SCOP Superfamily Organelle DB
Ashbya (AGD) BOND GPMdb (Mass Spec.) YPL+
Candida (CGD) BioPIXIE MIPS YeastGFP
Candida (CandidaDB) CYC2008 (complexes) Pfam domains YeastRC Public Image Repository
YGOB Complexome YeastRC Structure Prediction (Seattle)
YOGY DIP


GeneMANIA

References cited on this page View Complete Literature Guide for Ssb1p
1) 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
2) Nelson RJ, et al.  (1992) The translation machinery and 70 kd heat shock protein cooperate in protein synthesis. Cell 71(1):97-105
3) 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
4) Craig EA, et al.  (1993) Heat shock proteins: molecular chaperones of protein biogenesis. Microbiol Rev 57(2):402-14
5) Lopez-Buesa P, et al.  (1998) The biochemical properties of the ATPase activity of a 70-kDa heat shock protein (Hsp70) are governed by the C-terminal domains. Proc Natl Acad Sci U S A 95(26):15253-8
6) de Nobel H, et al.  (2001) Parallel and comparative analysis of the proteome and transcriptome of sorbic acid-stressed Saccharomyces cerevisiae. Yeast 18(15):1413-28
7) Kim SY and Craig EA  (2005) Broad sensitivity of Saccharomyces cerevisiae lacking ribosome-associated chaperone ssb or zuo1 to cations, including aminoglycosides. Eukaryot Cell 4(1):82-9
8) Huang P, et al.  (2005) The Hsp70 Ssz1 modulates the function of the ribosome-associated J-protein Zuo1. Nat Struct Mol Biol 12(6):497-504
9) Byrne KP and Wolfe KH  (2005) The Yeast Gene Order Browser: combining curated homology and syntenic context reveals gene fate in polyploid species. Genome Res 15(10):1456-61
10) Ghaemmaghami S, et al.  (2003) Global analysis of protein expression in yeast. Nature 425(6959):737-41