---

• Site Map |
• Search Options |
• Help |
• Home |
•   |
•  

•  
• Community Info
• Submit Data
• BLAST
• Primers
• PatMatch
• Gene/Seq Resources
• Advanced Search
• Community Wiki

---

SSS1/YDR086C Single Page Format

This page provides an alternative format to the SGD Locus Summary Page. Note that additional information may be available on or linked from the standard format SGD Locus Summary page.

Contents

Names and Identifiers GO Annotations Pathways Summary Paragraph Mutant Phenotypes Interactions Homologs Protein Info (physical properties, transcript info) PDB Homologs (protein structure info) Motifs Genome-wide Expression (and other large-scale analyses) Locus History (misc. notes) Sequence Retrieval and Analysis Map and Displays Localization Community Annotation Literature Guide

Sequence Coordinates   ChrIV: 617168 to 616926 CDS: 617168 - 616926 Click on map for expanded view SGD ORF map GBrowse

SGD Locus Page

Names and Identifiers [TOP] [NEXT]
Standard Name	Systematic Name	Alias	Feature Type	SGDID
SSS1	YDR086C		ORF, Verified	S000002493
Description
Subunit of the Sec61p translocation complex (Sec61p-Sss1p-Sbh1p) that forms a channel for passage of secretory proteins through the endoplasmic reticulum membrane, and of the Ssh1p complex (Ssh1p-Sbh2p-Sss1p); interacts with Ost4p and Wbp1p

GO Annotations [TOP] [NEXT]
Molecular Function Annotation(s) Reference(s) Evidence Assigned By P-P-bond-hydrolysis-driven protein transmembrane transporter activity DDB, et al. (2001) Gene Ontology annotation through association of InterPro records with GO terms.      IEA : Inferred from Electronic Annotation with EBI:IPR008158 Assigned on 2007-05-23 UniProtKB contributes_to P-P-bond-hydrolysis-driven protein transmembrane transporter activity Panzner S, et al. (1995) Posttranslational protein transport in yeast reconstituted with a purified complex of Sec proteins and Kar2p. Cell 81(4):561-70        IDA : Inferred from Direct Assay Assigned on 2009-12-11 SGD structural molecule activity Esnault Y, et al. (1994) SSS1 encodes a stabilizing component of the Sec61 subcomplex of the yeast protein translocation apparatus. J Biol Chem 269(44):27478-85      IMP : Inferred from Mutant Phenotype IGI : Inferred from Genetic Interaction with SGD:SEC61 Assigned on 2009-12-11 SGD
Biological Process Annotation(s) Reference(s) Evidence Assigned By SRP-dependent cotranslational protein targeting to membrane, translocation Scheper W, et al. (2003) Coordination of N-glycosylation and protein translocation across the endoplasmic reticulum membrane by Sss1 protein. J Biol Chem 278(39):37998-8003        IMP : Inferred from Mutant Phenotype Assigned on 2009-12-11 SGD intracellular protein transport DDB, et al. (2001) Gene Ontology annotation through association of InterPro records with GO terms.      IEA : Inferred from Electronic Annotation with EBI:IPR001901 Assigned on 2007-05-23 UniProtKB posttranslational protein targeting to membrane, translocation Panzner S, et al. (1995) Posttranslational protein transport in yeast reconstituted with a purified complex of Sec proteins and Kar2p. Cell 81(4):561-70        IDA : Inferred from Direct Assay Assigned on 2007-11-05 SGD protein targeting DDB, et al. (2001) Gene Ontology annotation through association of InterPro records with GO terms.      IEA : Inferred from Electronic Annotation with EBI:IPR001901 Assigned on 2008-02-13 UniProtKB protein transport DDB, et al. (2001) Gene Ontology annotation through association of InterPro records with GO terms.      IEA : Inferred from Electronic Annotation with EBI:IPR008158 Assigned on 2007-05-23 UniProtKB GOA curators (2000) Gene Ontology annotation based on Swiss-Prot keyword mapping.      IEA : Inferred from Electronic Annotation with EBI:KW-0653 Assigned on 2007-05-23 UniProtKB transmembrane transport GOA curators (2000) Gene Ontology annotation based on Swiss-Prot keyword mapping.      IEA : Inferred from Electronic Annotation with EBI:KW-0811 Assigned on 2009-10-01 UniProtKB transport GOA curators (2000) Gene Ontology annotation based on Swiss-Prot keyword mapping.      IEA : Inferred from Electronic Annotation with EBI:KW-0813 Assigned on 2007-05-23 UniProtKB
Cellular Component Annotation(s) Reference(s) Evidence Assigned By Sec61 translocon complex Finke K, et al. (1996) A second trimeric complex containing homologs of the Sec61p complex functions in protein transport across the ER membrane of S. cerevisiae. EMBO J 15(7):1482-94      IDA : Inferred from Direct Assay Assigned on 2009-12-11 SGD Panzner S, et al. (1995) Posttranslational protein transport in yeast reconstituted with a purified complex of Sec proteins and Kar2p. Cell 81(4):561-70        IDA : Inferred from Direct Assay Assigned on 2009-12-11 SGD Ssh1 translocon complex Finke K, et al. (1996) A second trimeric complex containing homologs of the Sec61p complex functions in protein transport across the ER membrane of S. cerevisiae. EMBO J 15(7):1482-94      IDA : Inferred from Direct Assay Assigned on 2009-12-11 SGD endoplasmic reticulum GOA curators (2000) Gene Ontology annotation based on Swiss-Prot keyword mapping.      IEA : Inferred from Electronic Annotation with EBI:KW-0256 Assigned on 2007-05-23 UniProtKB integral to membrane GOA curators (2000) Gene Ontology annotation based on Swiss-Prot keyword mapping.      IEA : Inferred from Electronic Annotation with EBI:KW-0812 Assigned on 2007-05-23 UniProtKB GOA curators and UniProt curators (2007) Gene Ontology annotation based on Swiss-Prot Subcellular Location vocabulary mapping.      IEA : Inferred from Electronic Annotation with EBI:SL-9904 Assigned on 2009-10-01 UniProtKB membrane DDB, et al. (2001) Gene Ontology annotation through association of InterPro records with GO terms.      IEA : Inferred from Electronic Annotation with EBI:IPR001901 , EBI:IPR008158 Assigned on 2007-05-23 UniProtKB GOA curators (2000) Gene Ontology annotation based on Swiss-Prot keyword mapping.      IEA : Inferred from Electronic Annotation with EBI:KW-0472 Assigned on 2007-05-23 UniProtKB

Pathways [TOP] [NEXT]
No pathways available

Summary Paragraph [TOP] [NEXT]

SUMMARY PARAGRAPH for SSS1/YDR086C for SSS1 Sss1p, a small essential protein, is a subunit of the heterotrimeric Sec61 complex, also referred to as the translocon (1, reviewed in 2). The Sec61 complex forms a channel in the endoplasmic reticulum (ER) membrane and mediates translocation of secretory and membrane proteins into the ER and also retrograde transport of misfolded proteins to the cytoplasm for degradation (reviewed in 3 and 4). The other subunits of the Sec61 complex include Sec61p, the major subunit that contains ten transmembrane domains and forms the protein-conducting channel, and Sbh1p (5, 6, reviewed in 2). Sss1p is also a subunit of the structurally related trimeric Ssh1p complex, consisting of Ssh1p, Sbh2p, and Sss1p, that is thought to function exclusively in cotranslational translocation (7). Proteins that are transported into or across the ER membrane are directed there by signal sequences or by transmembrane segments that interact with the translocation apparatus. In S. cerevisiae the Sec61 complex mediates both co- and posttranslational translocation (while the mammalian Sec61 complex functions primarily with the cotranslational pathway; 8). During cotranslational translocation, ribosomes synthesizing signal sequence-containing proteins are targeted to the translocon via the signal recognition particle (SRP), and the ribosomes bind directly to Sec61p such that protein biosynthesis and translocation are synchronous (9). Posttranslational translocation requires Sec62p, Sec63p, Sec66p, and Sec72p (comprising the Sec63 complex), as well as Kar2p, in place of SRP to facilitate interaction of the full-length polypeptide with the translocon via the signal sequence (10, 11). Retrograde transport of misfolded proteins into the cytoplasm (also called dislocation) employs the Sec61 channel via interaction with the 19S proteasome regulatory particle (12). This interaction, which competes with the ribosome-Sec61p interaction, defines the Sec61 complex as the principal proteasome receptor in the ER membrane (12). SSS1 (for Sec Sixty-one Suppressor) overexpression restores translocation in the sec61-3 temperature sensitive mutant (13, 14). Sss1p interacts physically with Sec61p in a region including the transmembrane segments TM6, TM7, and TM8 (amino acids L232-R406), and functions to stabilize the translocation channel (1, 14). In addition, Sss1p exhibits physical interactions with some of the oligosaccharyltransferase (OST) subunits and thus may facilitate binding of OST to the channel to promote efficient N-linked glycosylation of glycoproteins (15, 16). Sss1p is an integral membrane protein and its amino terminal half is exposed to the cytosol (1). Sss1p is conserved among organisms and the human homolog, Sec61 gamma, functionally complements an sss1 null mutation in S. cerevisiae (17). Bacterial and archaeal Sss1p orthologs are referred to as SecE (17, reviewed in 2). Last Updated: 2007-11-09

Basic References [TOP]

BASIC INFORMATION REFERENCES forSSS1/YDR086C for SSS1 1) Esnault Y, et al. (1994) SSS1 encodes a stabilizing component of the Sec61 subcomplex of the yeast protein translocation apparatus. J Biol Chem 269(44):27478-85      2) Osborne AR, et al. (2005) Protein translocation by the Sec61/SecY channel. Annu Rev Cell Dev Biol 21():529-50            3) Sommer T and Wolf DH (1997) Endoplasmic reticulum degradation: reverse protein flow of no return. FASEB J 11(14):1227-33      4) Romisch K (1999) Surfing the Sec61 channel: bidirectional protein translocation across the ER membrane. J Cell Sci 112 ( Pt 23)():4185-91        5) Wilkinson BM, et al. (1996) Determination of the transmembrane topology of yeast Sec61p, an essential component of the endoplasmic reticulum translocation complex. J Biol Chem 271(41):25590-7        6) Toikkanen J, et al. (1996) Yeast protein translocation complex: isolation of two genes SEB1 and SEB2 encoding proteins homologous to the Sec61 beta subunit. Yeast 12(5):425-38      7) Finke K, et al. (1996) A second trimeric complex containing homologs of the Sec61p complex functions in protein transport across the ER membrane of S. cerevisiae. EMBO J 15(7):1482-94      8) Ng DT, et al. (1996) Signal sequences specify the targeting route to the endoplasmic reticulum membrane. J Cell Biol 134(2):269-78      9) Prinz A, et al. (2000) Sec61p is the main ribosome receptor in the endoplasmic reticulum of Saccharomyces cerevisiae. Biol Chem 381(9-10):1025-9        10) Plath K, et al. (1998) Signal sequence recognition in posttranslational protein transport across the yeast ER membrane. Cell 94(6):795-807        11) Panzner S, et al. (1995) Posttranslational protein transport in yeast reconstituted with a purified complex of Sec proteins and Kar2p. Cell 81(4):561-70        12) Kalies KU, et al. (2005) The protein translocation channel binds proteasomes to the endoplasmic reticulum membrane. EMBO J 24(13):2284-93          13) Esnault Y, et al. (1993) The yeast SSS1 gene is essential for secretory protein translocation and encodes a conserved protein of the endoplasmic reticulum. EMBO J 12(11):4083-93      14) Wilkinson BM, et al. (1997) Molecular architecture of the ER translocase probed by chemical crosslinking of Sss1p to complementary fragments of Sec61p. EMBO J 16(15):4549-59        15) Scheper W, et al. (2003) Coordination of N-glycosylation and protein translocation across the endoplasmic reticulum membrane by Sss1 protein. J Biol Chem 278(39):37998-8003        16) Chavan M, et al. (2005) Subunits of the translocon interact with components of the oligosaccharyl transferase complex. J Biol Chem 280(24):22917-24        17) Hartmann E, et al. (1994) Evolutionary conservation of components of the protein translocation complex. Nature 367(6464):654-7

Mutant Phenotypes [TOP] [NEXT]
Phenotype page for SSS1/YDR086C

Interactions: genetic, physical, and other gene-gene links. [TOP] [NEXT]
Interaction page for SSS1/YDR086C

Homologs [TOP] [NEXT]
Comparison Resources PSI-BLAST Results Ashbya Homologs (AGD) BLASTN vs. fungi BLASTP at NCBI BLASTP vs. fungi Candida Homologs (CGD) Candida Homologs (CandidaDB) Fungal Alignment Fungal Orthogroups Repository Ortholog Search (P-POD) PhylomeDB Synteny Viewer Yeast Gene Order Browser (YGOB) eukarYotic OrtholoGY (YOGY)

Physical Properties and Transcript Information: predicted from sequence [TOP] [NEXT]
Protein Sequence Calculations from Predicted Full length Translation N-term MARASEK C-term PIRYVIV Length(aa) 80 MW(Da) 8,944 pI 10.26 Amino Acid Composition (full length) GCG tools: PepPlot, Helical Wheel, PepStruct Transcript Translation Calculations Codon Bias 0.551   Codon Adaptation Index 0.441   Frequency of Optimal Codons 0.747   Hydropathicity of Protein 0.009   Aromaticity Score 0.075	10 20 30 40 50 | | | | | MARASEKGEEKKQSNNQVEKLVEAPVEFVREGTQFLAKCKKPDLKEYTKI VKAVGIGFIAVGIIGYAIKLIHIPIRYVIV*

Protein Structures from PDB: proteins of known structure with sequence similarity to SSS1/YDR086C, based on Smith-Waterman analysis. [TOP] [NEXT]

PDB protein structure(s) homologous to SSS1 Homolog Source (per PDB) Protein Alignment: SSS1 vs. Homolog External Links P-Value %Identical %Similar Alignment 2yxr ( Chain: B) The plug domain of the secy protein stablizes the closed state of the translocation channel and maintains a membrane seal PDB_Info PDB_Structure Methanocaldococcus jannaschii 0.000770 34 28 View alignment SCOP MMDB CATH 1rhz ( Chain: B) The structure of a protein conducting channel PDB_Info PDB_Structure Methanocaldococcus jannaschii 0.000770 34 28 View alignment SCOP MMDB CATH 2yxq ( Chain: B) The plug domain of the secy protein stablizes the closed state of the translocation channel and maintains a membrane seal PDB_Info PDB_Structure Methanocaldococcus jannaschii 0.000770 34 28 View alignment SCOP MMDB CATH 1rh5 ( Chain: B) The structure of a protein conducting channel PDB_Info PDB_Structure Methanocaldococcus jannaschii 0.000770 34 28 View alignment SCOP MMDB CATH 3dkn ( Chain: B) Sec61 in the canine ribosome-channel complex from the endoplasmic reticulum PDB_Info PDB_Structure Canis lupus familiaris 0.000999 34 29 View alignment SCOP MMDB CATH 3bo0 ( Chain: B) Ribosome-secy complex PDB_Info PDB_Structure Escherichia coli 0.004897 35 27 View alignment SCOP MMDB CATH 3bo1 ( Chain: B) Ribosome-secy complex PDB_Info PDB_Structure Escherichia coli 0.004897 35 27 View alignment SCOP MMDB CATH

Genome-wide Expression and Other Large-Scale Analyses [TOP] [NEXT]
Functional Analysis Expression Connection Summary Cell cycle and metabolic oscillation Cell cycle transcript profile Cyclebase Genevestigator GermOnline SPELL Microarray Search YGAC Triples Yeast Microarray Global Viewer YeastFunc	You can also search multiple datasets simultaneously using Expression Connection for expression studies or Function Junction for other large scale analyses.

Locus History (misc. notes) [TOP] [NEXT]

Nomenclature History

Standard Name	Reference
SSS1	SGD (2007) Information without a citation in SGD

Sequence Retrieval [TOP] [NEXT]
Sequence Type	Output Format
Genomic DNA	GCG | FASTA | NoHeader
Genomic DNA with 1 kb up and downstream	GCG | FASTA | NoHeader
DNA coding sequence (without introns, without flanking regions)	GCG | FASTA | NoHeader
Protein Translation of ORF	GCG | FASTA | NoHeader
6-Frame Translation(with Restriction Map)	GCG
Restriction Fragment Sizes	GCG
Sequence Analysis Tools BLASTP BLASTN Design Primers FASTA aa FASTA nt Restriction Fragment Map Restriction Fragment Sizes Six-Frame Translation

Sequence from other databases
Sequence ID	Source
YDR086C	SGD Systematic Sequence
851659	NCBI: Gene ID
NP_010371.1	NCBI: RefSeq protein version ID
NP_010371.1	NCBI: RefSeq protein version ID
6320291	NCBI: NCBI protein GI

Map and Displays [TOP] [NEXT]
Physical, Genetic Maps:	Chromosomal Feature Map	GBrowse	Combined Physical and Genetic Map	Genetic Distance vs. Physical Distance Ratios
Similarity Viewers:	Synteny Viewer	Genomic Stripe View	SAGE Results Map

Localization [TOP] [NEXT]
Localization Resources YeastRC Localization (Seattle) YGAC Triples YeastGFP DB (UCSF) at SGD

Community Annotation [TOP] [NEXT]
No community annotation available.

Literature Guide: papers categorized by topic. [TOP]
Topics	Reference	Other Genes Addressed
39 curated references; 0 references not yet curated
Non-Fungal Related Genes/Proteins Protein-protein Interactions Protein/Nucleic Acid Structure	Becker T, et al. (2009) Structure of monomeric yeast and mammalian Sec61 complexes interacting with the translating ribosome. Science 326(5958):1369-73	|SBH1 |SBH2 |SEC61 |SSH1
Function/Process Protein-protein Interactions	Harada Y, et al. (2009) Oligosaccharyltransferase directly binds to ribosome at a location near the translocon-binding site. Proc Natl Acad Sci U S A 106(17):6945-9	|NIP7 |NMD3 |OST1 |OST2 |OST3 |OST4 |OST5 |OST6 |RDN25-1 |RDN25-2 |RDN5-1 |RDN5-2 |RDN5-3 |RDN5-4 |MORE
Regulation of Transcription	Ohtsuki K, et al. (2009) Genome-wide localization analysis of a complete set of Tafs reveals a specific effect of the taf1 mutation on Taf2 occupancy and provides indirect evidence for different TFIID conformations at different promoters. Nucleic Acids Res	|ARF1 |BAP3 |BUR6 |CDC48 |CDC53 |CDC9 |COP1 |CYK3 |DLD3 |DOS2 |GCN5 |HEM12 |HNT1 |HTB1 |MORE
Protein-protein Interactions	Zhao X and Jantti J (2009) Functional characterization of the trans-membrane domain interactions of the Sec61 protein translocation complex beta-subunit. BMC Cell Biol 10():76	|RTN1 |RTN2 |SBH1 |SBH2 |SEC61 |YOP1
Genetic Interactions Mutants/Phenotypes Strains/Constructs	Jiang Y, et al. (2008) An interaction between the SRP receptor and the translocon is critical during cotranslational protein translocation. J Cell Biol 180(6):1149-61	|SBH1 |SBH2 |SEC61 |SRP101 |SRP102 |SSH1
Protein-protein Interactions	Feng D, et al. (2007) The transmembrane domain is sufficient for Sbh1p function, its association with the Sec61 complex, and interaction with Rtn1p. J Biol Chem 282(42):30618-28	|RTN1 |SBH1 |SBH2 |SEC15 |SEC61 |SEC62 |SEC63
Protein-protein Interactions	Ng W, et al. (2007) Characterization of the proteasome interaction with the Sec61 channel in the endoplasmic reticulum. J Cell Sci 120(Pt 4):682-91	|CDC48 |CUE1 |HRD1 |KAR2 |RPT1 |RPT3 |RPT5 |RPT6 |SBH1 |SEC61 |SEC62 |SEC63 |SEC72 |SSH1 |MORE
Evolution Fungal Related Genes/Proteins	De Hertogh B, et al. (2006) Emergence of species-specific transporters during evolution of the hemiascomycete phylum. Genetics 172(2):771-81	|AAC1 |AAC3 |ACS2 |ADP1 |ADY2 |AGC1 |AGP1 |AGP2 |AGP3 |ALP1 |ALR1 |ALR2 |ANT1 |AQR1 |MORE
Protein Processing/Modification/Regulation Techniques and Reagents	Tagwerker C, et al. (2006) A tandem affinity tag for two-step purification under fully denaturing conditions: application in ubiquitin profiling and protein complex identification combined with in vivocross-linking. Mol Cell Proteomics 5(4):737-48	|AAC1 |AAC3 |ACB1 |ACC1 |ACS2 |ADE3 |ADE5,7 |ADE6 |ADH4 |ADO1 |AGP1 |AHA1 |AHP1 |ALA1 |MORE
Function/Process Protein-protein Interactions Strains/Constructs Techniques and Reagents	Chavan M, et al. (2005) Subunits of the translocon interact with components of the oligosaccharyl transferase complex. J Biol Chem 280(24):22917-24	|OST1 |OST2 |OST3 |OST4 |OST5 |OST6 |SBH1 |SEC61 |STT3 |SWP1 |WBP1
Protein-protein Interactions	Cheng Z, et al. (2005) Identification of cytoplasmic residues of Sec61p involved in ribosome binding and cotranslational translocation. J Cell Biol 168(1):67-77	|SBH1 |SEC61 |SSH1
Function/Process Protein-protein Interactions	Kalies KU, et al. (2005) The protein translocation channel binds proteasomes to the endoplasmic reticulum membrane. EMBO J 24(13):2284-93	|PRE1 |RPN1 |RPN10 |RPN11 |RPN12 |RPN13 |RPN2 |RPN3 |RPN5 |RPN6 |RPN7 |RPN8 |RPN9 |RPT1 |MORE
Reviews	Osborne AR, et al. (2005) Protein translocation by the Sec61/SecY channel. Annu Rev Cell Dev Biol 21():529-50	|KAR2 |SBH1 |SBH2 |SEC61 |SSH1
Cellular Location Function/Process Mutants/Phenotypes Protein-protein Interactions Strains/Constructs Techniques and Reagents	Scheper W, et al. (2003) Coordination of N-glycosylation and protein translocation across the endoplasmic reticulum membrane by Sss1 protein. J Biol Chem 278(39):37998-8003	|SBH1 |SEC61 |WBP1
Cellular Location Function/Process Genetic Interactions Mutants/Phenotypes Protein-protein Interactions Strains/Constructs	Toikkanen JH, et al. (2003) The beta subunit of the Sec61p endoplasmic reticulum translocon interacts with the exocyst complex in Saccharomyces cerevisiae. J Biol Chem 278(23):20946-53	|SBH1 |SEC15 |SEC4 |SEC61 |SEC8
Function/Process Genetic Interactions Mutants/Phenotypes Protein Physical Properties Protein-protein Interactions Protein/Nucleic Acid Structure Strains/Constructs Techniques and Reagents	Morrow MW and Brodsky JL (2001) Yeast ribosomes bind to highly purified reconstituted Sec61p complex and to mammalian p180. Traffic 2(10):705-16	|KAR2 |SBH1 |SEC61 |SEC62 |SEC63 |SEC66 |SEC72 |TEF2
Cellular Location Function/Process Mutants/Phenotypes Strains/Constructs	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	|SBH1 |SBH2 |SEC11 |SEC61 |SPC1 |SPC2 |SPC3 |SSH1
Techniques and Reagents	Meisinger C, et al. (2000) Purification of Saccharomcyes cerevisiae mitochondria devoid of microsomal and cytosolic contaminations. Anal Biochem 287(2):339-42	|SEC61 |TIM23 |TOM70
Cellular Location Function/Process Genetic Interactions Mutants/Phenotypes Protein Sequence Features Protein-protein Interactions Strains/Constructs	Prinz A, et al. (2000) Sec61p is the main ribosome receptor in the endoplasmic reticulum of Saccharomyces cerevisiae. Biol Chem 381(9-10):1025-9	|SBH1 |SEC61 |SSH1
Cellular Location Function/Process Protein-protein Interactions	Jensen RE and Johnson AE (1999) Protein translocation: is Hsp70 pulling my chain? Curr Biol 9(20):R779-82	|KAR2 |SBH1 |SEC61 |SSC1
Cellular Location Function/Process Non-Fungal Related Genes/Proteins Protein Sequence Features Protein-protein Interactions Protein/Nucleic Acid Structure	Rapoport TA, et al. (1999) Posttranslational protein translocation across the membrane of the endoplasmic reticulum. Biol Chem 380(10):1143-50	|SBH1 |SEC61
Cellular Location Function/Process Mutants/Phenotypes Protein Sequence Features Strains/Constructs Techniques and Reagents	Beswick V, et al. (1998) Expression, purification, and characterization of Sss1p, an essential component of the yeast Sec61p protein translocation complex. Protein Expr Purif 13(3):423-32
Cellular Location Function/Process Genetic Interactions Mutants/Phenotypes Non-Fungal Related Genes/Proteins Protein-protein Interactions	Plath K, et al. (1998) Signal sequence recognition in posttranslational protein transport across the yeast ER membrane. Cell 94(6):795-807	|KAR2 |SBH1 |SEC61 |SEC62 |SEC66
Cellular Location Function/Process Genetic Interactions Mutants/Phenotypes Protein-protein Interactions Strains/Constructs	van Dyck L, et al. (1998) The ATP-dependent PIM1 protease is required for the expression of intron-containing genes in mitochondria. Genes Dev 12(10):1515-24	|COB |COX1 |PIM1
Cellular Location Function/Process Non-Fungal Related Genes/Proteins Protein-protein Interactions Techniques and Reagents	Beckmann R, et al. (1997) Alignment of conduits for the nascent polypeptide chain in the ribosome-Sec61 complex. Science 278(5346):2123-6	|SBH1 |SEC61
Cellular Location Function/Process Protein-protein Interactions Techniques and Reagents	Matlack KE, et al. (1997) Protein transport by purified yeast Sec complex and Kar2p without membranes. Science 277(5328):938-41	|KAR2 |SBH1 |SEC61 |SEC62 |SEC63 |SEC66 |SEC72
Cellular Location Function/Process Mutants/Phenotypes Protein-protein Interactions Strains/Constructs	Plemper RK, et al. (1997) Mutant analysis links the translocon and BiP to retrograde protein transport for ER degradation. Nature 388(6645):891-5	|KAR2 |SBH1 |SEC61 |SEC63 |UBC6
Cellular Location Function/Process Genetic Interactions Mutants/Phenotypes Protein Sequence Features Protein-protein Interactions Strains/Constructs	Wilkinson BM, et al. (1997) Molecular architecture of the ER translocase probed by chemical crosslinking of Sss1p to complementary fragments of Sec61p. EMBO J 16(15):4549-59	|SEC61
Protein Physical Properties Protein Processing/Modification/Regulation Regulation of	Biederer T, et al. (1996) Degradation of subunits of the Sec61p complex, an integral component of the ER membrane, by the ubiquitin-proteasome pathway. EMBO J 15(9):2069-76	|SBH1 |UBC6 |UBC7
Function/Process Genetic Interactions Protein-protein Interactions	Corsi AK and Schekman R (1996) Mechanism of polypeptide translocation into the endoplasmic reticulum. J Biol Chem 271(48):30299-302	|SBH2
Protein Physical Properties Protein-protein Interactions	Finke K, et al. (1996) A second trimeric complex containing homologs of the Sec61p complex functions in protein transport across the ER membrane of S. cerevisiae. EMBO J 15(7):1482-94	|SBH1 |SBH2 |SEC61 |SEC62 |SEC63 |SEC66 |SEC72 |SSH1
Protein-protein Interactions Protein/Nucleic Acid Structure	Hanein D, et al. (1996) Oligomeric rings of the Sec61p complex induced by ligands required for protein translocation. Cell 87(4):721-32	|SBH1 |SEC61 |SEC62 |SEC63 |SEC72
Genetic Interactions Mutants/Phenotypes Non-Fungal Related Genes/Proteins Protein Sequence Features Protein-protein Interactions Strains/Constructs	Iwasaki K, et al. (1996) emo-1, a Caenorhabditis elegans Sec61p gamma homologue, is required for oocyte development and ovulation. J Cell Biol 134(3):699-714
Cellular Location Non-Fungal Related Genes/Proteins Protein-protein Interactions	Rapoport TA, et al. (1996) Approaching the mechanism of protein transport across the ER membrane. Curr Opin Cell Biol 8(4):499-504	|SBH2
DNA/RNA Sequence Features Mapping	Coster F, et al. (1995) Analysis of a 32.8 kb segment of yeast chromosome IV reveals 21 open reading frames, including TPS2, PPH3, RAD55, SED1, PDC2, AFR1, SSS1, SLU7 and a tRNA for arginine. Yeast 11(7):673-9	|AFR1 |IPT1 |PDC2 |PPH3 |RAD55 |SED1 |SLU7 |STN1 |TPS2 |VPS41
Protein Physical Properties Protein-protein Interactions Techniques and Reagents	Panzner S, et al. (1995) Posttranslational protein transport in yeast reconstituted with a purified complex of Sec proteins and Kar2p. Cell 81(4):561-70	|KAR2 |SBH1 |SEC61 |SEC72
Cellular Location Function/Process Genetic Interactions Mutants/Phenotypes Protein Physical Properties Protein-protein Interactions Regulatory Role Strains/Constructs	Esnault Y, et al. (1994) SSS1 encodes a stabilizing component of the Sec61 subcomplex of the yeast protein translocation apparatus. J Biol Chem 269(44):27478-85	|SEC61
Function/Process Fungal Related Genes/Proteins Genetic Interactions	Hartmann E, et al. (1994) Evolutionary conservation of components of the protein translocation complex. Nature 367(6464):654-7	|SEC61
Cellular Location Function/Process Genetic Interactions Mutants/Phenotypes Non-Fungal Related Genes/Proteins Regulatory Role Strains/Constructs	Esnault Y, et al. (1993) The yeast SSS1 gene is essential for secretory protein translocation and encodes a conserved protein of the endoplasmic reticulum. EMBO J 12(11):4083-93	|SEC61 |TDH3

Return to SGD

Send a Message to the SGD Curators