SEC63/YOR254C Summary Help

SEC63 BASIC INFORMATION

Standard Name SEC63 1
Systematic Name YOR254C
Alias PTL1 2
Feature Type ORF, Verified
Description Essential subunit of Sec63 complex (Sec63p, Sec62p, Sec66p and Sec72p); with Sec61 complex, Kar2p/BiP and Lhs1p forms a channel competent for SRP-dependent and post-translational SRP-independent protein targeting and import into the ER (3, 4, 5 and see Summary Paragraph)
Name Description SECretory 6
GO Annotations All SEC63 GO evidence and references
    View Computational GO annotations for SEC63
Molecular Function
Manually curated
Biological Process
Manually curated
Cellular Component
Manually curated
High-throughput
Mutant Phenotype All SEC63 Phenotype details and references
Classical genetics
conditional
null
reduction of function
Large-scale survey
null
repressible
Interactions SEC63 All interactions details and references
143 total interaction(s) for 64 unique genes/features.
Physical Interactions
  • Affinity Capture-MS: 16
  • Affinity Capture-RNA: 1
  • Affinity Capture-Western: 5
  • Biochemical Activity: 5
  • Co-purification: 14
  • Reconstituted Complex: 2
  • Two-hybrid: 26

Genetic Interactions
  • Dosage Rescue: 4
  • Phenotypic Enhancement: 60
  • Phenotypic Suppression: 4
  • Synthetic Lethality: 2
  • Synthetic Rescue: 4

Sequence Information
ChrXV:807024 to 805033 | ORF Map | GBrowse
Note: this feature is encoded on the Crick strand.
Gbrowse
Last Update Coordinates: 2006-01-05 | Sequence: 1996-07-31
Subfeature details
Relative
Coordinates
Chromosomal
Coordinates
Most Recent Updates
Coordinates Sequence
CDS 1..1992 807024..805033 2006-01-05 1996-07-31
External Links All Associated Seq | Entrez Gene | Entrez RefSeq Protein | MIPS | UniProtKB
Primary SGDIDS000005780

SEC63 RESOURCES

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SGD ORF mapGBrowse
SGD ORF map
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  • Functional Analysis

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Expression Summary histogram

SUMMARY PARAGRAPH for SEC63

Hsp40/DnaJ is a family of proteins, established by bacterial DnaJ, that regulates Hsp70 chaperone activity. Hsp40s stimulate the intrinsically weak ATPase activity of Hsp70 proteins and facilitate Hsp70 interaction with polypeptide substrates. Hsp70 family members often have multiple Hsp40 partners, and these specific pairings govern Hsp70 chaperone involvement in particular processes (reviewed in 7, 8, and 9). All Hsp40s contain a highly conserved 75-amino acid J domain, which interacts with the ATPase domain of Hsp70 to stimulate ATP hydrolysis. However, there are also other conserved structural domains, and based on the presence or absence of these regions, the Hsp40 family can be divided into three subtypes: type I, type II and type III (a comprehensive overview of the structural features of the different HSP40 subtypes can be found in 9). Sequence analysis of the S. cerevisiae genome has revealed 22 proteins in the Hsp40/DnaJ family: YDJ1, XDJ1, APJ1, SIS1, DJP1, ZUO1, SWA2, JJJ1, JJJ2, JJJ3, CAJ1, CWC23, MDJ1, MDJ2, PAM18, JAC1, JID1, SCJ1, HLJ1, JEM1, SEC63, and ERJ5 (9).

Last updated: 2006-12-19

REFERENCES CITED ON THIS PAGE [View Complete Literature Guide for SEC63]

1) Rothblatt JA, et al.  (1989) Multiple genes are required for proper insertion of secretory proteins into the endoplasmic reticulum in yeast. J Cell Biol 109(6 Pt 1):2641-52
2) Toyn J, et al.  (1988) In vivo and in vitro analysis of ptl1, a yeast ts mutant with a membrane-associated defect in protein translocation. EMBO J 7(13):4347-53
3) Young BP, et al.  (2001) Sec63p and Kar2p are required for the translocation of SRP-dependent precursors into the yeast endoplasmic reticulum in vivo. EMBO J 20(1-2):262-71
4) Willer M, et al.  (2003) Identification of novel protein-protein interactions at the cytosolic surface of the Sec63 complex in the yeast ER membrane. Yeast 20(2):133-48
5) Misselwitz B, et al.  (1999) Interaction of BiP with the J-domain of the Sec63p component of the endoplasmic reticulum protein translocation complex. J Biol Chem 274(29):20110-5
6) Novick P, et al.  (1980) Identification of 23 complementation groups required for post-translational events in the yeast secretory pathway. Cell 21(1):205-15
7) Qiu XB, et al.  (2006) The diversity of the DnaJ/Hsp40 family, the crucial partners for Hsp70 chaperones. Cell Mol Life Sci 63(22):2560-2570
8) Cyr DM, et al.  (1994) DnaJ-like proteins: molecular chaperones and specific regulators of Hsp70. Trends Biochem Sci 19(4):176-81
9) Walsh P, et al.  (2004) The J-protein family: modulating protein assembly, disassembly and translocation. EMBO Rep 5(6):567-71