Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

P38353

- SSH1_YEAST

UniProt

P38353 - SSH1_YEAST

(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Protein

Sec sixty-one protein homolog

Gene

SSH1

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

Functioni

Part of the Ssh1 complex, which probably is the major component of a channel-forming translocon complex that may function exclusively in the cotranslational pathway of protein endoplasmic reticulum (ER) import.1 Publication

GO - Molecular functioni

  1. protein transmembrane transporter activity Source: SGD
  2. signal sequence binding Source: SGD

GO - Biological processi

  1. protein transmembrane transport Source: GOC
  2. SRP-dependent cotranslational protein targeting to membrane Source: SGD
Complete GO annotation...

Keywords - Biological processi

Protein transport, Translocation, Transport

Enzyme and pathway databases

BioCyciYEAST:G3O-29203-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
Sec sixty-one protein homolog
Alternative name(s):
Ssh1 complex subunit SSH1
Ssh1 complex subunit alpha
Gene namesi
Name:SSH1
Ordered Locus Names:YBR283C
ORF Names:YBR2020
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
ProteomesiUP000002311: Chromosome II

Organism-specific databases

CYGDiYBR283c.
SGDiS000000487. SSH1.

Subcellular locationi

GO - Cellular componenti

  1. integral component of membrane Source: UniProtKB-KW
  2. Ssh1 translocon complex Source: SGD
Complete GO annotation...

Keywords - Cellular componenti

Endoplasmic reticulum, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 490490Sec sixty-one protein homologPRO_0000131811Add
BLAST

Proteomic databases

MaxQBiP38353.
PaxDbiP38353.
PeptideAtlasiP38353.

Expressioni

Gene expression databases

GenevestigatoriP38353.

Interactioni

Subunit structurei

Component of the heterotrimeric Ssh1 complex, which is composed of SSH1, SBH2 and SSS1.

Binary interactionsi

WithEntry#Exp.IntActNotes
ERV29P533373EBI-18175,EBI-23662
PHO88P382643EBI-18175,EBI-13350
SSS1P351798EBI-18175,EBI-16406

Protein-protein interaction databases

BioGridi32977. 144 interactions.
DIPiDIP-4962N.
IntActiP38353. 36 interactions.
MINTiMINT-570624.
STRINGi4932.YBR283C.

Structurei

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2WW9electron microscopy8.60A1-490[»]
2WWAelectron microscopy8.90A1-490[»]
ProteinModelPortaliP38353.
SMRiP38353. Positions 1-490.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP38353.

Topological domain

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 3232CytoplasmicSequence AnalysisAdd
BLAST
Topological domaini54 – 12168LumenalSequence AnalysisAdd
BLAST
Topological domaini143 – 1464CytoplasmicSequence Analysis
Topological domaini168 – 1747LumenalSequence Analysis
Topological domaini196 – 24247CytoplasmicSequence AnalysisAdd
BLAST
Topological domaini264 – 29330LumenalSequence AnalysisAdd
BLAST
Topological domaini315 – 33925CytoplasmicSequence AnalysisAdd
BLAST
Topological domaini361 – 3611LumenalSequence Analysis
Topological domaini383 – 42139CytoplasmicSequence AnalysisAdd
BLAST
Topological domaini443 – 4497LumenalSequence Analysis
Topological domaini471 – 49020CytoplasmicSequence AnalysisAdd
BLAST

Transmembrane

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transmembranei33 – 5321HelicalSequence AnalysisAdd
BLAST
Transmembranei122 – 14221HelicalSequence AnalysisAdd
BLAST
Transmembranei147 – 16721HelicalSequence AnalysisAdd
BLAST
Transmembranei175 – 19521HelicalSequence AnalysisAdd
BLAST
Transmembranei243 – 26321HelicalSequence AnalysisAdd
BLAST
Transmembranei294 – 31421HelicalSequence AnalysisAdd
BLAST
Transmembranei340 – 36021HelicalSequence AnalysisAdd
BLAST
Transmembranei362 – 38221HelicalSequence AnalysisAdd
BLAST
Transmembranei422 – 44221HelicalSequence AnalysisAdd
BLAST
Transmembranei450 – 47021HelicalSequence AnalysisAdd
BLAST

Family & Domainsi

Sequence similaritiesi

Belongs to the SecY/SEC61-alpha family.Curated

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiCOG0201.
HOGENOMiHOG000231249.
InParanoidiP38353.
KOiK10956.
OMAiSTKVRGM.
OrthoDBiEOG70CRGV.

Family and domain databases

Gene3Di1.10.3370.10. 1 hit.
InterProiIPR002208. SecY/SEC61-alpha.
IPR023201. SecY_su_dom.
IPR019561. Translocon_Sec61/SecY_plug_dom.
[Graphical view]
PANTHERiPTHR10906. PTHR10906. 1 hit.
PfamiPF10559. Plug_translocon. 1 hit.
PF00344. SecY. 1 hit.
[Graphical view]
PIRSFiPIRSF004557. SecY. 1 hit.
SUPFAMiSSF103491. SSF103491. 2 hits.
PROSITEiPS00755. SECY_1. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P38353-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MSGFRLIDIV KPILPILPEV ELPFEKLPFD DKIVYTIFAG LIYLFAQFPL
60 70 80 90 100
VGLPKATTPN VNDPIYFLRG VFGCEPRTLL EFGLFPNISS GLILQLLAGL
110 120 130 140 150
KVIKVNFKIQ SDRELFQSLT KVFAIVQYVI LTNIFIFAGY FGDDLSVVQI
160 170 180 190 200
GLINFQLVGA GIFTTLLAEV IDKGFGFSSG AMIINTVVIA TNLVADTFGV
210 220 230 240 250
SQIKVGEDDQ TEAQGALINL IQGLRSKHKT FIGGIISAFN RDYLPNLTTT
260 270 280 290 300
IIVLAIAIIV CYLQSVRVEL PIRSTRARGT NNVYPIKLLY TGCLSVLFSY
310 320 330 340 350
TILFYIHIFA FVLIQLVAKN EPTHIICKIM GHYENANNLL AVPTFPLSLL
360 370 380 390 400
APPTSFFKGV TQQPLTFITY SAFILVTGIW FADKWQAISG SSARDVALEF
410 420 430 440 450
KDQGITLMGR REQNVAKELN KVIPIAAVTG ASVLSLITVI GESLGLKGKA
460 470 480 490
AGIVVGIAGG FSLLEVITIE YQQSGGQSAL NQVLGVPGAM
Length:490
Mass (Da):53,312
Last modified:October 1, 1994 - v1
Checksum:i48267EEA3E0191BD
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
U05336 Genomic DNA. Translation: AAB40986.1.
X76053 Genomic DNA. Translation: CAA53646.1.
Z36152 Genomic DNA. Translation: CAA85247.1.
AY692997 Genomic DNA. Translation: AAT93016.1.
S77888 Genomic DNA. Translation: AAB21097.2. Sequence problems.
BK006936 Genomic DNA. Translation: DAA07398.1.
PIRiS44545.
RefSeqiNP_009842.1. NM_001178631.1.

Genome annotation databases

EnsemblFungiiYBR283C; YBR283C; YBR283C.
GeneIDi852586.
KEGGisce:YBR283C.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
U05336 Genomic DNA. Translation: AAB40986.1 .
X76053 Genomic DNA. Translation: CAA53646.1 .
Z36152 Genomic DNA. Translation: CAA85247.1 .
AY692997 Genomic DNA. Translation: AAT93016.1 .
S77888 Genomic DNA. Translation: AAB21097.2 . Sequence problems.
BK006936 Genomic DNA. Translation: DAA07398.1 .
PIRi S44545.
RefSeqi NP_009842.1. NM_001178631.1.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
2WW9 electron microscopy 8.60 A 1-490 [» ]
2WWA electron microscopy 8.90 A 1-490 [» ]
ProteinModelPortali P38353.
SMRi P38353. Positions 1-490.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 32977. 144 interactions.
DIPi DIP-4962N.
IntActi P38353. 36 interactions.
MINTi MINT-570624.
STRINGi 4932.YBR283C.

Proteomic databases

MaxQBi P38353.
PaxDbi P38353.
PeptideAtlasi P38353.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblFungii YBR283C ; YBR283C ; YBR283C .
GeneIDi 852586.
KEGGi sce:YBR283C.

Organism-specific databases

CYGDi YBR283c.
SGDi S000000487. SSH1.

Phylogenomic databases

eggNOGi COG0201.
HOGENOMi HOG000231249.
InParanoidi P38353.
KOi K10956.
OMAi STKVRGM.
OrthoDBi EOG70CRGV.

Enzyme and pathway databases

BioCyci YEAST:G3O-29203-MONOMER.

Miscellaneous databases

EvolutionaryTracei P38353.
NextBioi 971739.

Gene expression databases

Genevestigatori P38353.

Family and domain databases

Gene3Di 1.10.3370.10. 1 hit.
InterProi IPR002208. SecY/SEC61-alpha.
IPR023201. SecY_su_dom.
IPR019561. Translocon_Sec61/SecY_plug_dom.
[Graphical view ]
PANTHERi PTHR10906. PTHR10906. 1 hit.
Pfami PF10559. Plug_translocon. 1 hit.
PF00344. SecY. 1 hit.
[Graphical view ]
PIRSFi PIRSF004557. SecY. 1 hit.
SUPFAMi SSF103491. SSF103491. 2 hits.
PROSITEi PS00755. SECY_1. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "A second trimeric complex containing homologs of the Sec61p complex functions in protein transport across the ER membrane of S. cerevisiae."
    Finke K., Plath K., Panzner S., Prehn S., Rapoport T.A., Hartmann E., Sommer T.
    EMBO J. 15:1482-1494(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  2. "The sequence of a 32,420 bp segment located on the right arm of chromosome II from Saccharomyces cerevisiae."
    Holmstroem K., Brandt T., Kallesoe T.
    Yeast 10:S47-S62(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: ATCC 204508 / S288c.
  3. "Complete DNA sequence of yeast chromosome II."
    Feldmann H., Aigle M., Aljinovic G., Andre B., Baclet M.C., Barthe C., Baur A., Becam A.-M., Biteau N., Boles E., Brandt T., Brendel M., Brueckner M., Bussereau F., Christiansen C., Contreras R., Crouzet M., Cziepluch C.
    , Demolis N., Delaveau T., Doignon F., Domdey H., Duesterhus S., Dubois E., Dujon B., El Bakkoury M., Entian K.-D., Feuermann M., Fiers W., Fobo G.M., Fritz C., Gassenhuber J., Glansdorff N., Goffeau A., Grivell L.A., de Haan M., Hein C., Herbert C.J., Hollenberg C.P., Holmstroem K., Jacq C., Jacquet M., Jauniaux J.-C., Jonniaux J.-L., Kallesoee T., Kiesau P., Kirchrath L., Koetter P., Korol S., Liebl S., Logghe M., Lohan A.J.E., Louis E.J., Li Z.Y., Maat M.J., Mallet L., Mannhaupt G., Messenguy F., Miosga T., Molemans F., Mueller S., Nasr F., Obermaier B., Perea J., Pierard A., Piravandi E., Pohl F.M., Pohl T.M., Potier S., Proft M., Purnelle B., Ramezani Rad M., Rieger M., Rose M., Schaaff-Gerstenschlaeger I., Scherens B., Schwarzlose C., Skala J., Slonimski P.P., Smits P.H.M., Souciet J.-L., Steensma H.Y., Stucka R., Urrestarazu L.A., van der Aart Q.J.M., Van Dyck L., Vassarotti A., Vetter I., Vierendeels F., Vissers S., Wagner G., de Wergifosse P., Wolfe K.H., Zagulski M., Zimmermann F.K., Mewes H.-W., Kleine K.
    EMBO J. 13:5795-5809(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 204508 / S288c.
  4. Cited for: GENOME REANNOTATION.
    Strain: ATCC 204508 / S288c.
  5. Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: ATCC 204508 / S288c.
  6. "The nuclear coded mitoribosomal proteins YmL27 and YmL31 are both essential for mitochondrial function in yeast."
    Graack H.-R., Grohmann L., Kitakawa M.
    Biochimie 73:837-844(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 399-490.
  7. "Ssh1p determines the translocation and dislocation capacities of the yeast endoplasmic reticulum."
    Wilkinson B.M., Tyson J.R., Stirling C.J.
    Dev. Cell 1:401-409(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  8. "Evolutionarily conserved binding of ribosomes to the translocation channel via the large ribosomal RNA."
    Prinz A., Behrens C., Rapoport T.A., Hartmann E., Kalies K.-U.
    EMBO J. 19:1900-1906(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: ASSOCIATION OF THE SSH1 COMPLEX WITH RIBOSOMES.
  9. Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
  10. "A global topology map of the Saccharomyces cerevisiae membrane proteome."
    Kim H., Melen K., Oesterberg M., von Heijne G.
    Proc. Natl. Acad. Sci. U.S.A. 103:11142-11147(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: TOPOLOGY [LARGE SCALE ANALYSIS].
    Strain: ATCC 208353 / W303-1A.

Entry informationi

Entry nameiSSH1_YEAST
AccessioniPrimary (citable) accession number: P38353
Secondary accession number(s): D6VQS8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1994
Last sequence update: October 1, 1994
Last modified: October 29, 2014
This is version 124 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Miscellaneous

Present with 704 molecules/cell in log phase SD medium.1 Publication

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families
  3. Yeast
    Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD
  4. Yeast chromosome II
    Yeast (Saccharomyces cerevisiae) chromosome II: entries and gene names

External Data

Dasty 3