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Protein

Small COPII coat GTPase SAR1

Gene

SAR1

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

Functioni

Small GTPase component of the coat protein complex II (COPII) which promotes the formation of transport vesicles from the endoplasmic reticulum (ER). The coat has two main functions, the physical deformation of the endoplasmic reticulum membrane into vesicles and the selection of cargo molecules. SAR1 controls the coat assembly in a stepwise manner. Activated SAR1-GTP by SEC12 binds to membranes first and recruits the SEC23/24 complex. These SEC23/24-SAR1 prebudding intermediates are then collected by the SEC13/31 complex as subunits polymerize to form coated transport vesicles. Conversion to SAR1-GDP triggers coat release and recycles COPII subunits.14 Publications

Catalytic activityi

GTP + H2O = GDP + phosphate.

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi30 – 378GTP
Nucleotide bindingi73 – 764GTP
Nucleotide bindingi132 – 1354GTP

GO - Molecular functioni

  • GTPase activity Source: SGD
  • GTP binding Source: UniProtKB-KW

GO - Biological processi

  • intracellular protein transport Source: InterPro
  • regulation of COPII vesicle coating Source: SGD
  • vesicle-mediated transport Source: UniProtKB-KW
  • vesicle organization Source: SGD
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase

Keywords - Biological processi

ER-Golgi transport, Protein transport, Transport

Keywords - Ligandi

GTP-binding, Nucleotide-binding

Enzyme and pathway databases

BioCyciYEAST:G3O-34107-MONOMER.
ReactomeiR-SCE-204005. COPII (Coat Protein 2) Mediated Vesicle Transport.
R-SCE-5694530. Cargo concentration in the ER.
R-SCE-983170. Antigen Presentation: Folding, assembly and peptide loading of class I MHC.

Names & Taxonomyi

Protein namesi
Recommended name:
Small COPII coat GTPase SAR1 (EC:3.6.5.-)
Alternative name(s):
GTP-binding protein SAR1
Secretion-associated RAS-related protein 1
Gene namesi
Name:SAR1
Ordered Locus Names:YPL218W
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
Proteomesi
  • UP000002311 Componenti: Chromosome XVI

Organism-specific databases

EuPathDBiFungiDB:YPL218W.
SGDiS000006139. SAR1.

Subcellular locationi

GO - Cellular componenti

  • COPII vesicle coat Source: SGD
  • endoplasmic reticulum exit site Source: SGD
  • endoplasmic reticulum membrane Source: UniProtKB-SubCell
  • Golgi membrane Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasmic vesicle, Endoplasmic reticulum, Golgi apparatus, Membrane

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi32 – 321D → G: No cell growth at 37 degrees Celsius. Decreases GTP binding and ER-to-Golgi vesicle transport. 3 Publications
Mutagenesisi36 – 361K → M: No cell growth at 23 or 37 degrees Celsius. 1 Publication
Mutagenesisi54 – 541T → A: No cell growth at 23 or 37 degrees Celsius. Decreases GTP binding and impairs ER-to-Golgi vesicle transport. 2 Publications
Mutagenesisi73 – 731D → V: No cell growth at 23 or 37 degrees Celsius. 1 Publication
Mutagenesisi77 – 771H → L: No cell growth at 23 or 37 degrees Celsius. Impairs ER-to-Golgi vesicle transport. 2 Publications
Mutagenesisi112 – 1121E → K: Decreases guanine nucleotide binding. 2 Publications
Mutagenesisi132 – 1321N → I: No cell growth at 37 degrees Celsius. 2 Publications
Mutagenesisi171 – 1711C → S: Normal cell growth. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 190190Small COPII coat GTPase SAR1PRO_0000206275Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei155 – 1551PhosphothreonineCombined sources
Modified residuei157 – 1571PhosphoserineCombined sources

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiP20606.
PeptideAtlasiP20606.

PTM databases

iPTMnetiP20606.

Interactioni

Subunit structurei

COPII is composed of at least 5 proteins: the SEC23/24 complex, the SEC13/31 complex and SAR1. Interacts with EMP24.6 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
CRN1Q064402EBI-16472,EBI-4950

Protein-protein interaction databases

BioGridi35967. 53 interactions.
DIPiDIP-2231N.
IntActiP20606. 8 interactions.
MINTiMINT-479143.

Structurei

Secondary structure

1
190
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi25 – 317Combined sources
Helixi36 – 4510Combined sources
Beta strandi58 – 647Combined sources
Beta strandi67 – 737Combined sources
Helixi78 – 803Combined sources
Helixi84 – 874Combined sources
Beta strandi93 – 997Combined sources
Helixi103 – 1053Combined sources
Helixi106 – 11712Combined sources
Helixi120 – 1223Combined sources
Beta strandi127 – 1326Combined sources
Beta strandi136 – 1383Combined sources
Helixi142 – 1487Combined sources
Beta strandi166 – 1705Combined sources
Turni173 – 1764Combined sources
Helixi179 – 1879Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1M2OX-ray2.50B/D1-190[»]
2QTVX-ray2.50B23-189[»]
4BZIelectron microscopy23.00B/J/K1-190[»]
ProteinModelPortaliP20606.
SMRiP20606. Positions 23-189.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP20606.

Family & Domainsi

Sequence similaritiesi

Belongs to the small GTPase superfamily. SAR1 family.Curated

Phylogenomic databases

GeneTreeiENSGT00550000074696.
HOGENOMiHOG000163690.
InParanoidiP20606.
KOiK07953.
OMAiFDESKME.
OrthoDBiEOG7FNCKB.

Family and domain databases

Gene3Di3.40.50.300. 1 hit.
InterProiIPR027417. P-loop_NTPase.
IPR005225. Small_GTP-bd_dom.
IPR006689. Small_GTPase_ARF/SAR.
IPR006687. Small_GTPase_SAR1.
[Graphical view]
PfamiPF00025. Arf. 1 hit.
[Graphical view]
PRINTSiPR00328. SAR1GTPBP.
SUPFAMiSSF52540. SSF52540. 1 hit.
TIGRFAMsiTIGR00231. small_GTP. 1 hit.
PROSITEiPS51422. SAR1. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P20606-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAGWDIFGWF RDVLASLGLW NKHGKLLFLG LDNAGKTTLL HMLKNDRLAT
60 70 80 90 100
LQPTWHPTSE ELAIGNIKFT TFDLGGHIQA RRLWKDYFPE VNGIVFLVDA
110 120 130 140 150
ADPERFDEAR VELDALFNIA ELKDVPFVIL GNKIDAPNAV SEAELRSALG
160 170 180 190
LLNTTGSQRI EGQRPVEVFM CSVVMRNGYL EAFQWLSQYI
Length:190
Mass (Da):21,451
Last modified:February 1, 1991 - v1
Checksum:iE2348B57896B5A13
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X51667 Genomic DNA. Translation: CAA35978.1.
Z73574 Genomic DNA. Translation: CAA97933.1.
BK006949 Genomic DNA. Translation: DAA11218.1.
PIRiA33619.
RefSeqiNP_015106.1. NM_001184032.1.

Genome annotation databases

EnsemblFungiiYPL218W; YPL218W; YPL218W.
GeneIDi855883.
KEGGisce:YPL218W.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X51667 Genomic DNA. Translation: CAA35978.1.
Z73574 Genomic DNA. Translation: CAA97933.1.
BK006949 Genomic DNA. Translation: DAA11218.1.
PIRiA33619.
RefSeqiNP_015106.1. NM_001184032.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1M2OX-ray2.50B/D1-190[»]
2QTVX-ray2.50B23-189[»]
4BZIelectron microscopy23.00B/J/K1-190[»]
ProteinModelPortaliP20606.
SMRiP20606. Positions 23-189.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi35967. 53 interactions.
DIPiDIP-2231N.
IntActiP20606. 8 interactions.
MINTiMINT-479143.

PTM databases

iPTMnetiP20606.

Proteomic databases

MaxQBiP20606.
PeptideAtlasiP20606.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiYPL218W; YPL218W; YPL218W.
GeneIDi855883.
KEGGisce:YPL218W.

Organism-specific databases

EuPathDBiFungiDB:YPL218W.
SGDiS000006139. SAR1.

Phylogenomic databases

GeneTreeiENSGT00550000074696.
HOGENOMiHOG000163690.
InParanoidiP20606.
KOiK07953.
OMAiFDESKME.
OrthoDBiEOG7FNCKB.

Enzyme and pathway databases

BioCyciYEAST:G3O-34107-MONOMER.
ReactomeiR-SCE-204005. COPII (Coat Protein 2) Mediated Vesicle Transport.
R-SCE-5694530. Cargo concentration in the ER.
R-SCE-983170. Antigen Presentation: Folding, assembly and peptide loading of class I MHC.

Miscellaneous databases

EvolutionaryTraceiP20606.
NextBioi980541.
PROiP20606.

Family and domain databases

Gene3Di3.40.50.300. 1 hit.
InterProiIPR027417. P-loop_NTPase.
IPR005225. Small_GTP-bd_dom.
IPR006689. Small_GTPase_ARF/SAR.
IPR006687. Small_GTPase_SAR1.
[Graphical view]
PfamiPF00025. Arf. 1 hit.
[Graphical view]
PRINTSiPR00328. SAR1GTPBP.
SUPFAMiSSF52540. SSF52540. 1 hit.
TIGRFAMsiTIGR00231. small_GTP. 1 hit.
PROSITEiPS51422. SAR1. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "A novel GTP-binding protein, Sar1p, is involved in transport from the endoplasmic reticulum to the Golgi apparatus."
    Nakano A., Muramatsu M.-A.
    J. Cell Biol. 109:2677-2691(1989) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION.
  2. "The nucleotide sequence of Saccharomyces cerevisiae chromosome XVI."
    Bussey H., Storms R.K., Ahmed A., Albermann K., Allen E., Ansorge W., Araujo R., Aparicio A., Barrell B.G., Badcock K., Benes V., Botstein D., Bowman S., Brueckner M., Carpenter J., Cherry J.M., Chung E., Churcher C.M.
    , Coster F., Davis K., Davis R.W., Dietrich F.S., Delius H., DiPaolo T., Dubois E., Duesterhoeft A., Duncan M., Floeth M., Fortin N., Friesen J.D., Fritz C., Goffeau A., Hall J., Hebling U., Heumann K., Hilbert H., Hillier L.W., Hunicke-Smith S., Hyman R.W., Johnston M., Kalman S., Kleine K., Komp C., Kurdi O., Lashkari D., Lew H., Lin A., Lin D., Louis E.J., Marathe R., Messenguy F., Mewes H.-W., Mirtipati S., Moestl D., Mueller-Auer S., Namath A., Nentwich U., Oefner P., Pearson D., Petel F.X., Pohl T.M., Purnelle B., Rajandream M.A., Rechmann S., Rieger M., Riles L., Roberts D., Schaefer M., Scharfe M., Scherens B., Schramm S., Schroeder M., Sdicu A.-M., Tettelin H., Urrestarazu L.A., Ushinsky S., Vierendeels F., Vissers S., Voss H., Walsh S.V., Wambutt R., Wang Y., Wedler E., Wedler H., Winnett E., Zhong W.-W., Zollner A., Vo D.H., Hani J.
    Nature 387:103-105(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 204508 / S288c.
  3. Cited for: GENOME REANNOTATION.
    Strain: ATCC 204508 / S288c.
  4. "The GTP-binding Sar1 protein is localized to the early compartment of the yeast secretory pathway."
    Nishikawa S., Nakano A.
    Biochim. Biophys. Acta 1093:135-143(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION.
  5. "Sec12p-dependent membrane binding of the small GTP-binding protein Sar1p promotes formation of transport vesicles from the ER."
    d'Enfert C., Wuestehube L.J., Lila T., Schekman R.W.
    J. Cell Biol. 114:663-670(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION.
  6. "Reconstitution of GTP-binding Sar1 protein function in ER to Golgi transport."
    Oka T., Nishikawa S., Nakano A.
    J. Cell Biol. 114:671-679(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  7. "Structural and functional dissection of a membrane glycoprotein required for vesicle budding from the endoplasmic reticulum."
    d'Enfert C., Barlowe C., Nishikawa S., Nakano A., Schekman R.W.
    Mol. Cell. Biol. 11:5727-5734(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION.
  8. "Purification and characterization of SAR1p, a small GTP-binding protein required for transport vesicle formation from the endoplasmic reticulum."
    Barlowe C., d'Enfert C., Schekman R.W.
    J. Biol. Chem. 268:873-879(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: CHARACTERIZATION.
  9. "Requirement for a GTPase-activating protein in vesicle budding from the endoplasmic reticulum."
    Yoshihisa T., Barlowe C., Schekman R.W.
    Science 259:1466-1468(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: CHARACTERIZATION, ENZYME REGULATION, INTERACTION WITH SEC23.
  10. "Mutational analysis of the Sar1 protein, a small GTPase which is essential for vesicular transport from the endoplasmic reticulum."
    Nakano A., Otsuka H., Yamagishi M., Yamamoto E., Kimura K., Nishikawa S., Oka T.
    J. Biochem. 116:243-247(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: MUTAGENESIS OF ASP-32; LYS-36; THR-54; ASP-73; HIS-77; ASN-132 AND CYS-171.
  11. "Inhibition of GTP hydrolysis by Sar1p causes accumulation of vesicles that are a functional intermediate of the ER-to-Golgi transport in yeast."
    Oka T., Nakano A.
    J. Cell Biol. 124:425-434(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION.
  12. "COPI- and COPII-coated vesicles bud directly from the endoplasmic reticulum in yeast."
    Bednarek S.Y., Ravazzola M., Hosobuchi M., Amherdt M., Perrelet A., Schekman R.W., Orci L.
    Cell 83:1183-1196(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION.
  13. "Uncoupled packaging of targeting and cargo molecules during transport vesicle budding from the endoplasmic reticulum."
    Yeung T., Barlowe C., Schekman R.W.
    J. Biol. Chem. 270:30567-30570(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  14. "Characterization of yeast sar1 temperature-sensitive mutants, which are defective in protein transport from the endoplasmic reticulum."
    Yamanushi T., Hirata A., Oka T., Nakano A.
    J. Biochem. 120:452-458(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: MUTAGENESIS OF ASP-32; GLU-112 AND ASN-132.
  15. "Selective packaging of cargo molecules into endoplasmic reticulum-derived COPII vesicles."
    Campbell J.L., Schekman R.W.
    Proc. Natl. Acad. Sci. U.S.A. 94:837-842(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  16. "COPII-coated vesicle formation reconstituted with purified coat proteins and chemically defined liposomes."
    Matsuoka K., Orci L., Amherdt M., Bednarek S.Y., Hamamoto S., Schekman R.W., Yeung T.
    Cell 93:263-275(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBUNIT, SUBCELLULAR LOCATION.
  17. "Activities of mutant Sar1 proteins in guanine nucleotide binding, GTP hydrolysis, and cell-free transport from the endoplasmic reticulum to the Golgi apparatus."
    Saito Y., Kimura K., Oka T., Nakano A.
    J. Biochem. 124:816-823(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, MUTAGENESIS OF ASP-32; THR-54; HIS-77 AND GLU-112.
  18. "COPII-cargo interactions direct protein sorting into ER-derived transport vesicles."
    Kuehn M.J., Herrmann J.M., Schekman R.W.
    Nature 391:187-190(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  19. "Nucleation of COPII vesicular coat complex by endoplasmic reticulum to Golgi vesicle SNAREs."
    Springer S., Schekman R.W.
    Science 281:698-700(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH BET1; BOS1; SEC23 AND SEC24.
  20. "The use of liposomes to study COPII- and COPI-coated vesicle formation and membrane protein sorting."
    Matsuoka K., Schekman R.W.
    Methods 20:417-428(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION.
  21. "Distinct roles for the cytoplasmic tail sequences of Emp24p and Erv25p in transport between the endoplasmic reticulum and Golgi complex."
    Belden W.J., Barlowe C.
    J. Biol. Chem. 276:43040-43048(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH EMP24 AND ERV25.
  22. "Dynamics of the COPII coat with GTP and stable analogues."
    Antonny B., Madden D.T., Hamamoto S., Orci L., Schekman R.W.
    Nat. Cell Biol. 3:531-537(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, IDENTIFICATION IN THE COPII COAT.
  23. "Sec16p potentiates the action of COPII proteins to bud transport vesicles."
    Supek F., Madden D.T., Hamamoto S., Orci L., Schekman R.W.
    J. Cell Biol. 158:1029-1038(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION.
  24. "Activation of phospholipase D by the small GTPase Sar1p is required to support COPII assembly and ER export."
    Pathre P., Shome K., Blumental-Perry A., Bielli A., Haney C.J., Alber S., Watkins S.C., Romero G., Aridor M.
    EMBO J. 22:4059-4069(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION.
  25. Cited for: STRUCTURE OF THE COPII COMPLEX.
  26. "Reconstitution of coat protein complex II (COPII) vesicle formation from cargo-reconstituted proteoliposomes reveals the potential role of GTP hydrolysis by Sar1p in protein sorting."
    Sato K., Nakano A.
    J. Biol. Chem. 279:1330-1335(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN COPII COMPLEX ASSEMBLY.
  27. "Immunoisolaton of the yeast Golgi subcompartments and characterization of a novel membrane protein, Svp26, discovered in the Sed5-containing compartments."
    Inadome H., Noda Y., Adachi H., Yoda K.
    Mol. Cell. Biol. 25:7696-7710(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION, IDENTIFICATION BY MASS SPECTROMETRY.
  28. "Dissection of COPII subunit-cargo assembly and disassembly kinetics during Sar1p-GTP hydrolysis."
    Sato K., Nakano A.
    Nat. Struct. Mol. Biol. 12:167-174(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN COPII COMPLEX ASSEMBLY AND DISASSEMBLY.
  29. "A multidimensional chromatography technology for in-depth phosphoproteome analysis."
    Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.
    Mol. Cell. Proteomics 7:1389-1396(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-157, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  30. "Global analysis of Cdk1 substrate phosphorylation sites provides insights into evolution."
    Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.
    Science 325:1682-1686(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-155 AND SER-157, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  31. "Sites of ubiquitin attachment in Saccharomyces cerevisiae."
    Starita L.M., Lo R.S., Eng J.K., von Haller P.D., Fields S.
    Proteomics 12:236-240(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  32. "Structure of the Sec23/24-Sar1 pre-budding complex of the COPII vesicle coat."
    Bi X., Corpina R.A., Goldberg J.
    Nature 419:271-277(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) IN COMPLEX WITH SEC23 AND A GTP ANALOG.

Entry informationi

Entry nameiSAR1_YEAST
AccessioniPrimary (citable) accession number: P20606
Secondary accession number(s): D6W3F2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 1991
Last sequence update: February 1, 1991
Last modified: May 11, 2016
This is version 162 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

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 XVI
    Yeast (Saccharomyces cerevisiae) chromosome XVI: entries and gene names

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.