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Protein

Ubiquitin-binding protein CUE5

Gene

CUE5

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

Connects the ubiquitin pathway to autophagy by functioning as a ubiquitin-ATG8 adapter and thus mediating autophagic clearance of ubiquitin conjugates under starvation conditions. The CUE5-dependent selective autophagy pathway plays an important role in clearance of cytotoxic protein aggregates. Not required for cytoplasmic to vacuole pathway (cvt), mitophagy, pexophagy, or ribophagy.2 Publications

GO - Molecular functioni

  • protein binding, bridging Source: SGD
  • ubiquitin binding Source: SGD

GO - Biological processi

  • autophagy Source: UniProtKB-KW
  • ubiquitin-dependent protein catabolic process Source: SGD
Complete GO annotation...

Keywords - Biological processi

Autophagy

Enzyme and pathway databases

BioCyciYEAST:G3O-33586-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
Ubiquitin-binding protein CUE5
Alternative name(s):
Coupling of ubiquitin conjugation to ER degradation protein 5
Gene namesi
Name:CUE5Imported
Ordered Locus Names:YOR042W
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
Proteomesi
  • UP000002311 Componenti: Chromosome XV

Organism-specific databases

EuPathDBiFungiDB:YOR042W.
SGDiS000005568. CUE5.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi109 – 1091F → A: Impairs interaction with ubiquitin; when associated with A-110. 1 Publication
Mutagenesisi110 – 1101P → A: Impairs interaction with ubiquitin; when associated with A-109. 1 Publication
Mutagenesisi135 – 1351L → A: Impairs interaction with ubiquitin; when associated with A-136. 1 Publication
Mutagenesisi136 – 1361L → A: Impairs interaction with ubiquitin; when associated with A-135. 1 Publication
Mutagenesisi373 – 3731W → A: Impairs interaction with ATG8. 1 Publication
Mutagenesisi376 – 3761L → A: Impairs interaction with ATG8. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 411411Ubiquitin-binding protein CUE5PRO_0000270974Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei21 – 211PhosphoserineCombined sources
Modified residuei36 – 361PhosphoserineCombined sources
Modified residuei70 – 701PhosphothreonineCombined sources
Cross-linki76 – 76Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)1 Publication
Modified residuei91 – 911PhosphoserineCombined sources
Modified residuei167 – 1671PhosphothreonineCombined sources
Modified residuei220 – 2201PhosphoserineCombined sources
Modified residuei309 – 3091PhosphoserineCombined sources
Modified residuei318 – 3181PhosphoserineCombined sources
Modified residuei346 – 3461PhosphothreonineCombined sources
Modified residuei348 – 3481PhosphoserineCombined sources
Modified residuei352 – 3521PhosphothreonineCombined sources
Modified residuei364 – 3641PhosphothreonineCombined sources
Modified residuei367 – 3671PhosphothreonineCombined sources
Cross-linki396 – 396Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)1 Publication
Modified residuei407 – 4071PhosphoserineCombined sources

Keywords - PTMi

Isopeptide bond, Phosphoprotein, Ubl conjugation

Proteomic databases

MaxQBiQ08412.
PeptideAtlasiQ08412.

PTM databases

iPTMnetiQ08412.

Interactioni

Subunit structurei

Interacts with ATG8 (via AIM motif), CLB2, and ubiquitin (via CUE domain).2 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
ATG8P381824EBI-37580,EBI-2684
LSB3P436037EBI-37580,EBI-22980
RSP5P399403EBI-37580,EBI-16219
YSC84P327937EBI-37580,EBI-24460

GO - Molecular functioni

  • protein binding, bridging Source: SGD
  • ubiquitin binding Source: SGD

Protein-protein interaction databases

BioGridi34443. 46 interactions.
DIPiDIP-6293N.
IntActiQ08412. 11 interactions.
MINTiMINT-601414.

Structurei

3D structure databases

ProteinModelPortaliQ08412.
SMRiQ08412. Positions 105-140.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini97 – 14044CUEPROSITE-ProRule annotationAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi373 – 3764AIM

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi77 – 815Poly-GluSequence analysis
Compositional biasi204 – 2074Poly-ArgSequence analysis

Domaini

The ATG8-interaction motif (AIM) is required for the association with ATG8.1 Publication

Sequence similaritiesi

Contains 1 CUE domain.PROSITE-ProRule annotation

Phylogenomic databases

GeneTreeiENSGT00530000066599.
HOGENOMiHOG000112080.
InParanoidiQ08412.
OMAiELKDAFP.
OrthoDBiEOG7KDFMN.

Family and domain databases

InterProiIPR003892. CUE.
IPR009060. UBA-like.
[Graphical view]
PfamiPF02845. CUE. 1 hit.
[Graphical view]
SMARTiSM00546. CUE. 1 hit.
[Graphical view]
SUPFAMiSSF46934. SSF46934. 1 hit.
PROSITEiPS51140. CUE. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q08412-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MEEKEGIKDS SLLEKSNVPE SINEDISKTT DVDLNSDGKK DNDTSAKDGT
60 70 80 90 100
PKVEEKVNKS SGIDEDEVVT PAEDAKEEEE EHPPLPARRK SEEEPSKENP
110 120 130 140 150
ILQELKDAFP NLEEKYIKAV IIASQGVLSP AFNALLFLSD PESGKDIELP
160 170 180 190 200
TQPVRKNPEA PARRRQTQLE QDELLARQLD EQFNSSHSRR RNRDRATRSM
210 220 230 240 250
HEQRRRRHNP NEREQHHEDS EEEDSWSQFV EKDLPELTDR AGRSLQDTAN
260 270 280 290 300
KVSNWISDAY RRNFASGNEQ NDNQHGHQDQ QEWEPEIVDL SQGGKNSRPQ
310 320 330 340 350
QPERRRFNSF GVQVGDDSLE SHGITLHNED GFEDDEDVPP QLPTRTKSGE
360 370 380 390 400
STGKVVAETT YIDTPDTETK KKWQPLPPEP LDTTPTKVNA VSRNKKNPDE
410
DEFLINSDDE M
Length:411
Mass (Da):46,870
Last modified:November 1, 1996 - v1
Checksum:i0D455F9AD637AC8D
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Z74949 Genomic DNA. Translation: CAA99232.1.
AY558044 Genomic DNA. Translation: AAS56370.1.
BK006948 Genomic DNA. Translation: DAA10824.1.
PIRiS66916.
RefSeqiNP_014685.1. NM_001183461.1.

Genome annotation databases

EnsemblFungiiYOR042W; YOR042W; YOR042W.
GeneIDi854206.
KEGGisce:YOR042W.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Z74949 Genomic DNA. Translation: CAA99232.1.
AY558044 Genomic DNA. Translation: AAS56370.1.
BK006948 Genomic DNA. Translation: DAA10824.1.
PIRiS66916.
RefSeqiNP_014685.1. NM_001183461.1.

3D structure databases

ProteinModelPortaliQ08412.
SMRiQ08412. Positions 105-140.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi34443. 46 interactions.
DIPiDIP-6293N.
IntActiQ08412. 11 interactions.
MINTiMINT-601414.

PTM databases

iPTMnetiQ08412.

Proteomic databases

MaxQBiQ08412.
PeptideAtlasiQ08412.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiYOR042W; YOR042W; YOR042W.
GeneIDi854206.
KEGGisce:YOR042W.

Organism-specific databases

EuPathDBiFungiDB:YOR042W.
SGDiS000005568. CUE5.

Phylogenomic databases

GeneTreeiENSGT00530000066599.
HOGENOMiHOG000112080.
InParanoidiQ08412.
OMAiELKDAFP.
OrthoDBiEOG7KDFMN.

Enzyme and pathway databases

BioCyciYEAST:G3O-33586-MONOMER.

Miscellaneous databases

NextBioi976053.
PROiQ08412.

Family and domain databases

InterProiIPR003892. CUE.
IPR009060. UBA-like.
[Graphical view]
PfamiPF02845. CUE. 1 hit.
[Graphical view]
SMARTiSM00546. CUE. 1 hit.
[Graphical view]
SUPFAMiSSF46934. SSF46934. 1 hit.
PROSITEiPS51140. CUE. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "The nucleotide sequence of Saccharomyces cerevisiae chromosome XV."
    Dujon B., Albermann K., Aldea M., Alexandraki D., Ansorge W., Arino J., Benes V., Bohn C., Bolotin-Fukuhara M., Bordonne R., Boyer J., Camasses A., Casamayor A., Casas C., Cheret G., Cziepluch C., Daignan-Fornier B., Dang V.-D.
    , de Haan M., Delius H., Durand P., Fairhead C., Feldmann H., Gaillon L., Galisson F., Gamo F.-J., Gancedo C., Goffeau A., Goulding S.E., Grivell L.A., Habbig B., Hand N.J., Hani J., Hattenhorst U., Hebling U., Hernando Y., Herrero E., Heumann K., Hiesel R., Hilger F., Hofmann B., Hollenberg C.P., Hughes B., Jauniaux J.-C., Kalogeropoulos A., Katsoulou C., Kordes E., Lafuente M.J., Landt O., Louis E.J., Maarse A.C., Madania A., Mannhaupt G., Marck C., Martin R.P., Mewes H.-W., Michaux G., Paces V., Parle-McDermott A.G., Pearson B.M., Perrin A., Pettersson B., Poch O., Pohl T.M., Poirey R., Portetelle D., Pujol A., Purnelle B., Ramezani Rad M., Rechmann S., Schwager C., Schweizer M., Sor F., Sterky F., Tarassov I.A., Teodoru C., Tettelin H., Thierry A., Tobiasch E., Tzermia M., Uhlen M., Unseld M., Valens M., Vandenbol M., Vetter I., Vlcek C., Voet M., Volckaert G., Voss H., Wambutt R., Wedler H., Wiemann S., Winsor B., Wolfe K.H., Zollner A., Zumstein E., Kleine K.
    Nature 387:98-102(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 204508 / S288c.
  2. Cited for: GENOME REANNOTATION.
    Strain: ATCC 204508 / S288c.
  3. Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: ATCC 204508 / S288c.
  4. "A ubiquitin-binding motif required for intramolecular monoubiquitylation, the CUE domain."
    Shih S.C., Prag G., Francis S.A., Sutanto M.A., Hurley J.H., Hicke L.
    EMBO J. 22:1273-1281(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, UBIQUITIN-BINDING.
  5. Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
  6. Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
  7. Cited for: UBIQUITINATION [LARGE SCALE ANALYSIS] AT LYS-76 AND LYS-396.
    Strain: SUB592.
  8. Cited for: IDENTIFICATION BY MASS SPECTROMETRY, INTERACTION WITH CLB2.
  9. "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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-21; THR-70; THR-167; SER-220; SER-348; THR-364 AND SER-407, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Strain: ADR376.
  10. "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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-91, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  11. "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-21; SER-36; THR-70; THR-167; SER-220; SER-309; THR-364 AND SER-407, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  12. "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-21; THR-70; THR-167; SER-220; SER-309; SER-318; THR-346; THR-352; THR-364; THR-367 AND SER-407, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  13. "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].
  14. "Autophagic clearance of PolyQ proteins mediated by ubiquitin-Atg8 adaptors of the conserved CUET protein family."
    Lu K., Psakhye I., Jentsch S.
    Cell 158:549-563(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH ATG8 AND UBIQUITIN, DOMAIN, MUTAGENESIS OF PHE-109; PRO-110; LEU-135; LEU-136; TRP-373 AND LEU-376, FUNCTION.

Entry informationi

Entry nameiCUE5_YEAST
AccessioniPrimary (citable) accession number: Q08412
Secondary accession number(s): D6W2A8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 9, 2007
Last sequence update: November 1, 1996
Last modified: May 11, 2016
This is version 111 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 623 molecules/cell in log phase SD medium.1 Publication

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

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