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Protein

cAMP-dependent protein kinase regulatory subunit

Gene

BCY1

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

Regulatory subunit of the cyclic AMP-dependent protein kinase (PKA), an effector of the Ras/cAMP pathway. Inhibits PKA activity in the absence of cAMP. cAMP activates PKA and promotes growth and proliferation in response to good nutrient conditions. Together with ZDS1, provides a negative feedback control on the cell wall integrity-signaling pathway by acting as a negative regulator of MAP kinase SLT2/MPK1.4 Publications

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei249 – 2491cAMP 11 Publication
Binding sitei258 – 2581cAMP 11 Publication
Binding sitei368 – 3681cAMP 21 Publication
Binding sitei377 – 3771cAMP 21 Publication

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi184 – 301118cAMP 11 PublicationAdd
BLAST
Nucleotide bindingi302 – 416115cAMP 21 PublicationAdd
BLAST

GO - Molecular functioni

  • cAMP binding Source: UniProtKB-KW
  • cAMP-dependent protein kinase inhibitor activity Source: SGD
  • cAMP-dependent protein kinase regulator activity Source: InterPro
  • identical protein binding Source: IntAct

GO - Biological processi

  • negative regulation of Ras protein signal transduction Source: SGD
  • positive regulation of adenylate cyclase activity Source: SGD
  • protein localization to bud neck Source: SGD
Complete GO annotation...

Keywords - Ligandi

cAMP, cAMP-binding, Nucleotide-binding

Enzyme and pathway databases

BioCyciYEAST:G3O-31305-MONOMER.
ReactomeiR-SCE-163615. PKA activation.
R-SCE-164378. PKA activation in glucagon signalling.
R-SCE-180024. DARPP-32 events.
R-SCE-432040. Vasopressin regulates renal water homeostasis via Aquaporins.
R-SCE-5610787. Hedgehog 'off' state.

Names & Taxonomyi

Protein namesi
Recommended name:
cAMP-dependent protein kinase regulatory subunit
Short name:
cAPK regulatory subunit
Alternative name(s):
Bypass of cyclase mutations protein 1
Protein kinase A regulatory subunit
Short name:
PKA regulatory subunit
Gene namesi
Name:BCY1
Synonyms:REG1, SRA1
Ordered Locus Names:YIL033C
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
Proteomesi
  • UP000002311 Componenti: Chromosome IX

Organism-specific databases

EuPathDBiFungiDB:YIL033C.
SGDiS000001295. BCY1.

Subcellular locationi

  • Cytoplasm
  • Nucleus

  • Note: Cytoplasmic when phosphorylated. Nuclear when not phosphorylated.

GO - Cellular componenti

  • cAMP-dependent protein kinase complex Source: InterPro
  • cytoplasm Source: SGD
  • nuclear chromatin Source: SGD
  • nucleus Source: SGD
  • plasma membrane Source: SGD
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi129 – 1291T → D: Confers increased sensitivity to rapamycin and enhanced accumulation of glycogen upon TORC1 inhibition. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methionineiRemoved3 Publications
Chaini2 – 416415cAMP-dependent protein kinase regulatory subunitPRO_0000205418Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei3 – 31PhosphoserineCurated
Modified residuei4 – 41PhosphoserineCurated
Modified residuei9 – 91PhosphoserineCurated
Modified residuei68 – 681Phosphoserine1 Publication
Modified residuei70 – 701Phosphoserine1 Publication
Modified residuei74 – 741Phosphoserine1 Publication
Modified residuei77 – 771Phosphoserine1 Publication
Modified residuei79 – 791Phosphoserine1 Publication
Modified residuei81 – 811Phosphoserine1 Publication
Modified residuei83 – 831PhosphoserineCombined sources1 Publication
Modified residuei84 – 841Phosphoserine1 Publication
Modified residuei129 – 1291Phosphothreonine1 Publication
Modified residuei130 – 1301Phosphoserine1 Publication
Modified residuei131 – 1311Phosphothreonine1 Publication
Modified residuei144 – 1441Phosphothreonine1 Publication
Modified residuei145 – 1451Phosphoserine; by autocatalysisCombined sources2 Publications
Modified residuei147 – 1471Phosphoserine1 Publication
Modified residuei150 – 1501PhosphothreonineCombined sources1 Publication
Modified residuei160 – 1601Phosphothreonine1 Publication

Post-translational modificationi

Phosphorylated by YAK1 in response to glucose starvation. Phosphorylated by MCK1 at Thr-129 upon TOR complex 1 (TORC1) inhibition. Thr-129 phosphorylation activates BCY1 to inhibit PKA. TORC1 inhibits phosphorylation of RxxS/T sites but has no effect on Ser-145 phosphorylation. The phosphorylation sites can be clustered in several groups, all localized in the N-terminal part. The first cluster termed cluster I (CI) is located close to the N-terminus and includes Ser-3, Ser-4 and Ser-9 (PubMed:11134339, PubMed:12704202). The second includes Ser-68, Ser-70, Ser-74, Ser-77, Ser-79, Ser-81, Ser-83, and Ser-84. This cluster of phosphorylation sites, termed cluster II (CII), is important for BCY1 cytoplasmic localization and function (PubMed:11134339, PubMed:12704202, PubMed:20702584). The third cluster of phosphorylated residues consists of Thr-144, Ser-145, Ser-147, Thr-150, and Thr-160. This cluster falls within or near the so-called autoinhibitory domain where the catalytic subunit of PKA autophosphorylates the highly conserved Ser-145 to inhibit BCY1 (PubMed:20702584). A last cluster of phosphorylated residues included Thr-129, Ser-130, and Thr-131 and is termed cluster III (CIII). Sites in CIII (and to a lesser extend in CII) are hyperphosphorylated in response to rapamycin (PubMed:20702584).3 Publications

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiP07278.
TopDownProteomicsiP07278.

PTM databases

iPTMnetiP07278.

Interactioni

Subunit structurei

The inactive holoenzyme of cAMP-dependent protein kinase is a tetramer, composed of 2 regulatory subunits (R, encoded by BCY1) and two catalytic subunits (C, encoded by the 3 partially redundant TPK1, TPK2, and TPK3 genes). Activation by cAMP causes dissociation of the holoenzyme, producing 2 active catalytic monomers C and a regulatory dimer R2.2 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
itself3EBI-9475,EBI-9475
TPK1P062445EBI-9475,EBI-9458
TPK2P062457EBI-9475,EBI-9465
TPK3P059864EBI-9475,EBI-9470

GO - Molecular functioni

  • identical protein binding Source: IntAct

Protein-protein interaction databases

BioGridi34957. 249 interactions.
DIPiDIP-551N.
IntActiP07278. 17 interactions.
MINTiMINT-411181.

Structurei

Secondary structure

1
416
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi173 – 1808Combined sources
Turni183 – 1875Combined sources
Helixi190 – 1978Combined sources
Beta strandi201 – 2055Combined sources
Beta strandi210 – 2123Combined sources
Beta strandi220 – 2267Combined sources
Beta strandi229 – 2335Combined sources
Beta strandi239 – 2413Combined sources
Helixi249 – 2546Combined sources
Beta strandi259 – 2668Combined sources
Beta strandi268 – 2747Combined sources
Helixi275 – 2806Combined sources
Turni281 – 2866Combined sources
Helixi288 – 2925Combined sources
Helixi294 – 2996Combined sources
Helixi301 – 3033Combined sources
Helixi308 – 3169Combined sources
Beta strandi319 – 3235Combined sources
Beta strandi328 – 3303Combined sources
Beta strandi338 – 3447Combined sources
Beta strandi346 – 3516Combined sources
Turni352 – 3543Combined sources
Beta strandi355 – 3617Combined sources
Helixi368 – 3736Combined sources
Beta strandi378 – 3858Combined sources
Beta strandi387 – 3937Combined sources
Helixi394 – 4007Combined sources
Turni402 – 4043Combined sources
Helixi405 – 4106Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3OF1X-ray2.21A171-416[»]
ProteinModelPortaliP07278.
SMRiP07278. Positions 13-416.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni2 – 183182Dimerization and phosphorylationAdd
BLAST
Regioni8 – 4538Dimerization/docking domain (D/D)Add
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi142 – 1465Inhibitor sequence (IS)

Domaini

The inhibitor sequence (IS) is a substrate recognition motif that docks to the active site cleft of the catalytic subunit rendering the holoenzyme inactive.
Binding of cAMP to the 2 tandem cyclic-nucleotide binding domains (CNB-A and CNB-B) induces a conformational change in BCY1, causing the interaction surface with the catalytic subunit to be destroyed and eventually the dissociation of the R dimer from the C subunits.

Sequence similaritiesi

Contains 2 cyclic nucleotide-binding domains.PROSITE-ProRule annotation

Keywords - Domaini

Repeat

Phylogenomic databases

GeneTreeiENSGT00530000062947.
HOGENOMiHOG000196669.
InParanoidiP07278.
KOiK04739.
OMAiSTRVYND.
OrthoDBiEOG7034TC.

Family and domain databases

Gene3Di2.60.120.10. 2 hits.
InterProiIPR012198. cAMP_dep_PK_reg_su.
IPR003117. cAMP_dep_PK_reg_su_I/II_a/b.
IPR018490. cNMP-bd-like.
IPR018488. cNMP-bd_CS.
IPR000595. cNMP-bd_dom.
IPR014710. RmlC-like_jellyroll.
[Graphical view]
PfamiPF00027. cNMP_binding. 2 hits.
PF02197. RIIa. 1 hit.
[Graphical view]
PIRSFiPIRSF000548. PK_regulatory. 1 hit.
SMARTiSM00100. cNMP. 2 hits.
SM00394. RIIa. 1 hit.
[Graphical view]
SUPFAMiSSF51206. SSF51206. 2 hits.
PROSITEiPS00888. CNMP_BINDING_1. 2 hits.
PS00889. CNMP_BINDING_2. 2 hits.
PS50042. CNMP_BINDING_3. 2 hits.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P07278-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MVSSLPKESQ AELQLFQNEI NAANPSDFLQ FSANYFNKRL EQQRAFLKAR
60 70 80 90 100
EPEFKAKNIV LFPEPEESFS RPQSAQSQSR SRSSVMFKSP FVNEDPHSNV
110 120 130 140 150
FKSGFNLDPH EQDTHQQAQE EQQHTREKTS TPPLPMHFNA QRRTSVSGET
160 170 180 190 200
LQPNNFDDWT PDHYKEKSEQ QLQRLEKSIR NNFLFNKLDS DSKRLVINCL
210 220 230 240 250
EEKSVPKGAT IIKQGDQGDY FYVVEKGTVD FYVNDNKVNS SGPGSSFGEL
260 270 280 290 300
ALMYNSPRAA TVVATSDCLL WALDRLTFRK ILLGSSFKKR LMYDDLLKSM
310 320 330 340 350
PVLKSLTTYD RAKLADALDT KIYQPGETII REGDQGENFY LIEYGAVDVS
360 370 380 390 400
KKGQGVINKL KDHDYFGEVA LLNDLPRQAT VTATKRTKVA TLGKSGFQRL
410
LGPAVDVLKL NDPTRH
Length:416
Mass (Da):47,219
Last modified:January 23, 2007 - v4
Checksum:i6D7D97D8E4340AF3
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti264 – 2641A → P in CAA28726 (PubMed:3547325).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M15756 Genomic DNA. Translation: AAA34468.1.
M17223 Genomic DNA. Translation: AAA66934.1.
X05051 Genomic DNA. Translation: CAA28726.1.
Z46861 Genomic DNA. Translation: CAA86918.1.
AY558087 Genomic DNA. Translation: AAS56413.1.
BK006942 Genomic DNA. Translation: DAA08515.1.
PIRiA25868. OKBYRC.
RefSeqiNP_012231.1. NM_001179383.1.

Genome annotation databases

EnsemblFungiiYIL033C; YIL033C; YIL033C.
GeneIDi854778.
KEGGisce:YIL033C.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M15756 Genomic DNA. Translation: AAA34468.1.
M17223 Genomic DNA. Translation: AAA66934.1.
X05051 Genomic DNA. Translation: CAA28726.1.
Z46861 Genomic DNA. Translation: CAA86918.1.
AY558087 Genomic DNA. Translation: AAS56413.1.
BK006942 Genomic DNA. Translation: DAA08515.1.
PIRiA25868. OKBYRC.
RefSeqiNP_012231.1. NM_001179383.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3OF1X-ray2.21A171-416[»]
ProteinModelPortaliP07278.
SMRiP07278. Positions 13-416.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi34957. 249 interactions.
DIPiDIP-551N.
IntActiP07278. 17 interactions.
MINTiMINT-411181.

PTM databases

iPTMnetiP07278.

Proteomic databases

MaxQBiP07278.
TopDownProteomicsiP07278.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiYIL033C; YIL033C; YIL033C.
GeneIDi854778.
KEGGisce:YIL033C.

Organism-specific databases

EuPathDBiFungiDB:YIL033C.
SGDiS000001295. BCY1.

Phylogenomic databases

GeneTreeiENSGT00530000062947.
HOGENOMiHOG000196669.
InParanoidiP07278.
KOiK04739.
OMAiSTRVYND.
OrthoDBiEOG7034TC.

Enzyme and pathway databases

BioCyciYEAST:G3O-31305-MONOMER.
ReactomeiR-SCE-163615. PKA activation.
R-SCE-164378. PKA activation in glucagon signalling.
R-SCE-180024. DARPP-32 events.
R-SCE-432040. Vasopressin regulates renal water homeostasis via Aquaporins.
R-SCE-5610787. Hedgehog 'off' state.

Miscellaneous databases

PROiP07278.

Family and domain databases

Gene3Di2.60.120.10. 2 hits.
InterProiIPR012198. cAMP_dep_PK_reg_su.
IPR003117. cAMP_dep_PK_reg_su_I/II_a/b.
IPR018490. cNMP-bd-like.
IPR018488. cNMP-bd_CS.
IPR000595. cNMP-bd_dom.
IPR014710. RmlC-like_jellyroll.
[Graphical view]
PfamiPF00027. cNMP_binding. 2 hits.
PF02197. RIIa. 1 hit.
[Graphical view]
PIRSFiPIRSF000548. PK_regulatory. 1 hit.
SMARTiSM00100. cNMP. 2 hits.
SM00394. RIIa. 1 hit.
[Graphical view]
SUPFAMiSSF51206. SSF51206. 2 hits.
PROSITEiPS00888. CNMP_BINDING_1. 2 hits.
PS00889. CNMP_BINDING_2. 2 hits.
PS50042. CNMP_BINDING_3. 2 hits.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Cloning and characterization of BCY1, a locus encoding a regulatory subunit of the cyclic AMP-dependent protein kinase in Saccharomyces cerevisiae."
    Toda T., Cameron S., Sass P., Zoller M., Scott J.D., McMullen B., Hurwitz M., Krebs E.G., Wigler M.
    Mol. Cell. Biol. 7:1371-1377(1987) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 2-80; 83-126; 139-177; 195-203; 227-275; 291-298; 310-340; 345-377 AND 387-399, FUNCTION, SUBUNIT.
  2. "Characterization of Saccharomyces cerevisiae genes encoding subunits of cyclic AMP-dependent protein kinase."
    Cannon J.F., Tatchell K.
    Mol. Cell. Biol. 7:2653-2663(1987) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION.
  3. "Complete nucleotide sequence of the gene encoding the regulatory subunit of 3',5'-cyclic AMP-dependent protein kinase from the yeast Saccharomyces cerevisiae."
    Kunisawa R., Davis T.N., Urdea M.S., Thorner J.
    Nucleic Acids Res. 15:368-369(1987) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 204508 / S288c.
  5. Cited for: GENOME REANNOTATION.
    Strain: ATCC 204508 / S288c.
  6. Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: ATCC 204508 / S288c.
  7. "Characterization of a cyclic AMP-binding protein from bakers' yeast. Identification as a regulatory subunit of cyclic AMP-dependent protein kinase."
    Hixson C.S., Krebs E.G.
    J. Biol. Chem. 255:2137-2145(1980) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 2-21, FUNCTION.
  8. "Translation initiation requires the PAB-dependent poly(A) ribonuclease in yeast."
    Sachs A.B., Deardorff J.A.
    Cell 70:961-973(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 2-19.
  9. "Nucleocytoplasmic distribution of budding yeast protein kinase A regulatory subunit Bcy1 requires Zds1 and is regulated by Yak1-dependent phosphorylation of its targeting domain."
    Griffioen G., Branduardi P., Ballarini A., Anghileri P., Norbeck J., Baroni M.D., Ruis H.
    Mol. Cell. Biol. 21:511-523(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION, SUBCELLULAR LOCATION.
  10. "Feedback inhibition on cell wall integrity signaling by Zds1 involves Gsk3 phosphorylation of a cAMP-dependent protein kinase regulatory subunit."
    Griffioen G., Swinnen S., Thevelein J.M.
    J. Biol. Chem. 278:23460-23471(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION, PHOSPHORYLATION.
  11. Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
  12. Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
  13. "Large-scale phosphorylation analysis of alpha-factor-arrested Saccharomyces cerevisiae."
    Li X., Gerber S.A., Rudner A.D., Beausoleil S.A., Haas W., Villen J., Elias J.E., Gygi S.P.
    J. Proteome Res. 6:1190-1197(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Strain: ADR376.
  14. "Analysis of phosphorylation sites on proteins from Saccharomyces cerevisiae by electron transfer dissociation (ETD) mass spectrometry."
    Chi A., Huttenhower C., Geer L.Y., Coon J.J., Syka J.E.P., Bai D.L., Shabanowitz J., Burke D.J., Troyanskaya O.G., Hunt D.F.
    Proc. Natl. Acad. Sci. U.S.A. 104:2193-2198(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  15. "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-145, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  16. "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 SER-83; SER-145 AND THR-150, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  17. "The rapamycin-sensitive phosphoproteome reveals that TOR controls protein kinase A toward some but not all substrates."
    Soulard A., Cremonesi A., Moes S., Schutz F., Jeno P., Hall M.N.
    Mol. Biol. Cell 21:3475-3486(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION AT SER-68; SER-70; SER-74; SER-77; SER-79; SER-81; SER-83; SER-84; THR-129; SER-130; THR-131; THR-144; SER-145; SER-147; THR-150 AND THR-160, MUTAGENESIS OF THR-129.
  18. "Structure of yeast regulatory subunit: a glimpse into the evolution of PKA signaling."
    Rinaldi J., Wu J., Yang J., Ralston C.Y., Sankaran B., Moreno S., Taylor S.S.
    Structure 18:1471-1482(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.21 ANGSTROMS) OF 171-416 IN COMPLEX WITH CAMP.

Entry informationi

Entry nameiKAPR_YEAST
AccessioniPrimary (citable) accession number: P07278
Secondary accession number(s): D6VVP9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 1, 1988
Last sequence update: January 23, 2007
Last modified: July 6, 2016
This is version 168 of the entry and version 4 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Miscellaneous

Present with 4280 molecules/cell in log phase SD medium.1 Publication

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, 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 IX
    Yeast (Saccharomyces cerevisiae) chromosome IX: 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.