SPC1/YJR010C-A Summary Help

Standard Name SPC1 1
Systematic Name YJR010C-A
Feature Type ORF, Verified
Description Subunit of the signal peptidase complex (SPC); SPC cleaves the signal sequence from proteins targeted to the endoplasmic reticulum (ER); homolog of the SPC12 subunit of mammalian signal peptidase complex; protein abundance increases in response to DNA replication stress (1, 2, 3 and see Summary Paragraph)
Name Description Signal Peptidase Complex 1
Chromosomal Location
ChrX:458361 to 458077 | ORF Map | GBrowse
Note: this feature is encoded on the Crick strand.
Gene Ontology Annotations All SPC1 GO evidence and references
  View Computational GO annotations for SPC1
Molecular Function
Manually curated
Biological Process
Manually curated
Cellular Component
Manually curated
Regulators 5 genes
Large-scale survey
114 total interaction(s) for 88 unique genes/features.
Physical Interactions
  • Affinity Capture-MS: 33
  • Affinity Capture-Western: 2
  • Co-purification: 1
  • PCA: 46
  • Two-hybrid: 1

Genetic Interactions
  • Dosage Rescue: 3
  • Negative Genetic: 15
  • Phenotypic Enhancement: 4
  • Phenotypic Suppression: 2
  • Positive Genetic: 3
  • Synthetic Growth Defect: 3
  • Synthetic Lethality: 1

Expression Summary
Length (a.a.) 94
Molecular Weight (Da) 10,819
Isoelectric Point (pI) 8.79
Phosphorylation PhosphoGRID | PhosphoPep Database
sequence information
ChrX:458361 to 458077 | ORF Map | GBrowse
Note: this feature is encoded on the Crick strand.
Last Update Coordinates: 2011-02-03 | Sequence: 1996-07-31
Subfeature details
Most Recent Updates
Coordinates Sequence
CDS 1..285 458361..458077 2011-02-03 1996-07-31
Retrieve sequences
Analyze Sequence
S288C only
S288C vs. other species
S288C vs. other strains
External Links All Associated Seq | Entrez Gene | Entrez RefSeq Protein | MIPS | Search all NCBI (Entrez) | UniProtKB
Primary SGDIDS000003770

SPC1 encodes a subunit of the signal peptidase complex (SPC), which cleaves the signal sequence from proteins targeted to the endoplasmic reticulum (ER) (1). Signal peptide cleavage occurs concomitantly with translocation through the translocon pore into the ER. In yeast, translocation can occur cotranslationally or posttranslationally, whereas in mammals translocation is always cotranslational. The process of protein translocation into the ER is reviewed in references 4 and 5.

The yeast SPC comprises four proteins, Spc1p, Spc2p, Spc3p, and Sec11p (6, 2). Spc1p is homologous to the mammalian signal peptidase subunit SPC12 (1). Spc1p is not essential for viability or for signal peptidase activity in vivo or in vitro (1, 2), and cells lacking both Spc1p and Spc2p are also viable (7). Deletion of SPC1 is synthetically lethal with a temperature-sensitive mutation in SEC11, which encodes the catalytic SPC subunit (7). Overexpression of SPC1 suppresses the sec11 temperature sensitive phenotype (1).

Last updated: 2000-11-27 Contact SGD

References cited on this page View Complete Literature Guide for SPC1
1) Fang H, et al.  (1996) The homologue of mammalian SPC12 is important for efficient signal peptidase activity in Saccharomyces cerevisiae. J Biol Chem 271(28):16460-5
2) Antonin W, et al.  (2000) Interactions between Spc2p and other components of the endoplasmic reticulum translocation sites of the yeast Saccharomyces cerevisiae. J Biol Chem 275(44):34068-72
3) Tkach JM, et al.  (2012) Dissecting DNA damage response pathways by analysing protein localization and abundance changes during DNA replication stress. Nat Cell Biol 14(9):966-76
4) Rapoport TA, et al.  (1996) Protein transport across the eukaryotic endoplasmic reticulum and bacterial inner membranes. Annu Rev Biochem 65:271-303
5) Johnson AE and van Waes MA  (1999) The translocon: a dynamic gateway at the ER membrane. Annu Rev Cell Dev Biol 15:799-842
6) YaDeau JT, et al.  (1991) Yeast signal peptidase contains a glycoprotein and the Sec11 gene product. Proc Natl Acad Sci U S A 88(2):517-21
7) Mullins C, et al.  (1996) Structurally related Spc1p and Spc2p of yeast signal peptidase complex are functionally distinct. J Biol Chem 271(46):29094-9