CUE5_YEAST
ID CUE5_YEAST Reviewed; 411 AA.
AC Q08412; D6W2A8;
DT 09-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 149.
DE RecName: Full=Ubiquitin-binding protein CUE5;
DE AltName: Full=Coupling of ubiquitin conjugation to ER degradation protein 5;
GN Name=CUE5 {ECO:0000312|SGD:S000005568}; OrderedLocusNames=YOR042W;
OS Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=559292;
RN [1] {ECO:0000312|EMBL:CAA99232.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169874;
RA Dujon B., Albermann K., Aldea M., Alexandraki D., Ansorge W., Arino J.,
RA Benes V., Bohn C., Bolotin-Fukuhara M., Bordonne R., Boyer J., Camasses A.,
RA Casamayor A., Casas C., Cheret G., Cziepluch C., Daignan-Fornier B.,
RA Dang V.-D., de Haan M., Delius H., Durand P., Fairhead C., Feldmann H.,
RA Gaillon L., Galisson F., Gamo F.-J., Gancedo C., Goffeau A., Goulding S.E.,
RA Grivell L.A., Habbig B., Hand N.J., Hani J., Hattenhorst U., Hebling U.,
RA Hernando Y., Herrero E., Heumann K., Hiesel R., Hilger F., Hofmann B.,
RA Hollenberg C.P., Hughes B., Jauniaux J.-C., Kalogeropoulos A.,
RA Katsoulou C., Kordes E., Lafuente M.J., Landt O., Louis E.J., Maarse A.C.,
RA Madania A., Mannhaupt G., Marck C., Martin R.P., Mewes H.-W., Michaux G.,
RA Paces V., Parle-McDermott A.G., Pearson B.M., Perrin A., Pettersson B.,
RA Poch O., Pohl T.M., Poirey R., Portetelle D., Pujol A., Purnelle B.,
RA Ramezani Rad M., Rechmann S., Schwager C., Schweizer M., Sor F., Sterky F.,
RA Tarassov I.A., Teodoru C., Tettelin H., Thierry A., Tobiasch E.,
RA Tzermia M., Uhlen M., Unseld M., Valens M., Vandenbol M., Vetter I.,
RA Vlcek C., Voet M., Volckaert G., Voss H., Wambutt R., Wedler H.,
RA Wiemann S., Winsor B., Wolfe K.H., Zollner A., Zumstein E., Kleine K.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XV.";
RL Nature 387:98-102(1997).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=24374639; DOI=10.1534/g3.113.008995;
RA Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.;
RT "The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
RL G3 (Bethesda) 4:389-398(2014).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=17322287; DOI=10.1101/gr.6037607;
RA Hu Y., Rolfs A., Bhullar B., Murthy T.V.S., Zhu C., Berger M.F.,
RA Camargo A.A., Kelley F., McCarron S., Jepson D., Richardson A., Raphael J.,
RA Moreira D., Taycher E., Zuo D., Mohr S., Kane M.F., Williamson J.,
RA Simpson A.J.G., Bulyk M.L., Harlow E., Marsischky G., Kolodner R.D.,
RA LaBaer J.;
RT "Approaching a complete repository of sequence-verified protein-encoding
RT clones for Saccharomyces cerevisiae.";
RL Genome Res. 17:536-543(2007).
RN [4] {ECO:0000305}
RP FUNCTION, AND UBIQUITIN-BINDING.
RX PubMed=12628920; DOI=10.1093/emboj/cdg140;
RA Shih S.C., Prag G., Francis S.A., Sutanto M.A., Hurley J.H., Hicke L.;
RT "A ubiquitin-binding motif required for intramolecular monoubiquitylation,
RT the CUE domain.";
RL EMBO J. 22:1273-1281(2003).
RN [5] {ECO:0000305}
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX PubMed=14562095; DOI=10.1038/nature02026;
RA Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W.,
RA Weissman J.S., O'Shea E.K.;
RT "Global analysis of protein localization in budding yeast.";
RL Nature 425:686-691(2003).
RN [6] {ECO:0000305}
RP LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
RX PubMed=14562106; DOI=10.1038/nature02046;
RA Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N.,
RA O'Shea E.K., Weissman J.S.;
RT "Global analysis of protein expression in yeast.";
RL Nature 425:737-741(2003).
RN [7]
RP UBIQUITINATION [LARGE SCALE ANALYSIS] AT LYS-76 AND LYS-396, AND
RP IDENTIFICATION BY MASS SPECTROMETRY.
RC STRAIN=SUB592;
RX PubMed=12872131; DOI=10.1038/nbt849;
RA Peng J., Schwartz D., Elias J.E., Thoreen C.C., Cheng D., Marsischky G.,
RA Roelofs J., Finley D., Gygi S.P.;
RT "A proteomics approach to understanding protein ubiquitination.";
RL Nat. Biotechnol. 21:921-926(2003).
RN [8] {ECO:0000305}
RP IDENTIFICATION BY MASS SPECTROMETRY, AND INTERACTION WITH CLB2.
RX PubMed=15200949; DOI=10.1016/j.molcel.2004.05.025;
RA Archambault V., Chang E.J., Drapkin B.J., Cross F.R., Chait B.T.,
RA Rout M.P.;
RT "Targeted proteomic study of the cyclin-Cdk module.";
RL Mol. Cell 14:699-711(2004).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-21; THR-70; THR-167; SER-220;
RP SER-348; THR-364 AND SER-407, AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RC STRAIN=ADR376;
RX PubMed=17330950; DOI=10.1021/pr060559j;
RA Li X., Gerber S.A., Rudner A.D., Beausoleil S.A., Haas W., Villen J.,
RA Elias J.E., Gygi S.P.;
RT "Large-scale phosphorylation analysis of alpha-factor-arrested
RT Saccharomyces cerevisiae.";
RL J. Proteome Res. 6:1190-1197(2007).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-91, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=17287358; DOI=10.1073/pnas.0607084104;
RA Chi A., Huttenhower C., Geer L.Y., Coon J.J., Syka J.E.P., Bai D.L.,
RA Shabanowitz J., Burke D.J., Troyanskaya O.G., Hunt D.F.;
RT "Analysis of phosphorylation sites on proteins from Saccharomyces
RT cerevisiae by electron transfer dissociation (ETD) mass spectrometry.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:2193-2198(2007).
RN [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-21; SER-36; THR-70; THR-167;
RP SER-220; SER-309; THR-364 AND SER-407, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=18407956; DOI=10.1074/mcp.m700468-mcp200;
RA Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.;
RT "A multidimensional chromatography technology for in-depth phosphoproteome
RT analysis.";
RL Mol. Cell. Proteomics 7:1389-1396(2008).
RN [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-21; THR-70; THR-167; SER-220;
RP SER-309; SER-318; THR-346; THR-352; THR-364; THR-367 AND SER-407, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19779198; DOI=10.1126/science.1172867;
RA Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.;
RT "Global analysis of Cdk1 substrate phosphorylation sites provides insights
RT into evolution.";
RL Science 325:1682-1686(2009).
RN [13]
RP UBIQUITINATION [LARGE SCALE ANALYSIS] AT LYS-15; LYS-59; LYS-76; LYS-156
RP AND LYS-354, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP ANALYSIS].
RX PubMed=22106047; DOI=10.1002/pmic.201100166;
RA Starita L.M., Lo R.S., Eng J.K., von Haller P.D., Fields S.;
RT "Sites of ubiquitin attachment in Saccharomyces cerevisiae.";
RL Proteomics 12:236-240(2012).
RN [14]
RP INTERACTION WITH ATG8 AND UBIQUITIN, DOMAIN, MUTAGENESIS OF PHE-109;
RP PRO-110; LEU-135; LEU-136; TRP-373 AND LEU-376, AND FUNCTION.
RX PubMed=25042851; DOI=10.1016/j.cell.2014.05.048;
RA Lu K., Psakhye I., Jentsch S.;
RT "Autophagic clearance of PolyQ proteins mediated by ubiquitin-Atg8 adaptors
RT of the conserved CUET protein family.";
RL Cell 158:549-563(2014).
CC -!- FUNCTION: Connects the ubiquitin pathway to autophagy by functioning as
CC a ubiquitin-ATG8 adapter and thus mediating autophagic clearance of
CC ubiquitin conjugates under starvation conditions. The CUE5-dependent
CC selective autophagy pathway plays an important role in clearance of
CC cytotoxic protein aggregates. Not required for cytoplasmic to vacuole
CC pathway (cvt), mitophagy, pexophagy, or ribophagy.
CC {ECO:0000269|PubMed:12628920, ECO:0000269|PubMed:25042851}.
CC -!- SUBUNIT: Interacts with ATG8 (via AIM motif), CLB2, and ubiquitin (via
CC CUE domain). {ECO:0000269|PubMed:15200949,
CC ECO:0000269|PubMed:25042851}.
CC -!- INTERACTION:
CC Q08412; P38182: ATG8; NbExp=4; IntAct=EBI-37580, EBI-2684;
CC Q08412; P43603: LSB3; NbExp=8; IntAct=EBI-37580, EBI-22980;
CC Q08412; P39940: RSP5; NbExp=3; IntAct=EBI-37580, EBI-16219;
CC Q08412; P32793: YSC84; NbExp=7; IntAct=EBI-37580, EBI-24460;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:14562095}.
CC Note=Localizes to cytoplasm in a punctate pattern.
CC -!- DOMAIN: The ATG8-interaction motif (AIM) is required for the
CC association with ATG8. {ECO:0000269|PubMed:25042851}.
CC -!- MISCELLANEOUS: Present with 623 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
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DR EMBL; Z74949; CAA99232.1; -; Genomic_DNA.
DR EMBL; AY558044; AAS56370.1; -; Genomic_DNA.
DR EMBL; BK006948; DAA10824.1; -; Genomic_DNA.
DR PIR; S66916; S66916.
DR RefSeq; NP_014685.1; NM_001183461.1.
DR AlphaFoldDB; Q08412; -.
DR SMR; Q08412; -.
DR BioGRID; 34443; 86.
DR IntAct; Q08412; 12.
DR MINT; Q08412; -.
DR STRING; 4932.YOR042W; -.
DR iPTMnet; Q08412; -.
DR MaxQB; Q08412; -.
DR PaxDb; Q08412; -.
DR PRIDE; Q08412; -.
DR EnsemblFungi; YOR042W_mRNA; YOR042W; YOR042W.
DR GeneID; 854206; -.
DR KEGG; sce:YOR042W; -.
DR SGD; S000005568; CUE5.
DR VEuPathDB; FungiDB:YOR042W; -.
DR eggNOG; KOG0504; Eukaryota.
DR GeneTree; ENSGT00390000013104; -.
DR HOGENOM; CLU_052404_0_0_1; -.
DR InParanoid; Q08412; -.
DR OMA; VAETTYI; -.
DR BioCyc; YEAST:G3O-33586-MON; -.
DR Reactome; R-SCE-6798695; Neutrophil degranulation.
DR PRO; PR:Q08412; -.
DR Proteomes; UP000002311; Chromosome XV.
DR RNAct; Q08412; protein.
DR GO; GO:0005737; C:cytoplasm; HDA:SGD.
DR GO; GO:0030674; F:protein-macromolecule adaptor activity; IMP:SGD.
DR GO; GO:0043130; F:ubiquitin binding; IDA:SGD.
DR GO; GO:0031624; F:ubiquitin conjugating enzyme binding; IBA:GO_Central.
DR GO; GO:0006914; P:autophagy; IEA:UniProtKB-KW.
DR GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; IMP:SGD.
DR CDD; cd14372; CUE_Cue5p_like; 1.
DR InterPro; IPR003892; CUE.
DR InterPro; IPR041807; Cue5/Don1_CUE.
DR InterPro; IPR009060; UBA-like_sf.
DR Pfam; PF02845; CUE; 1.
DR SMART; SM00546; CUE; 1.
DR SUPFAM; SSF46934; SSF46934; 1.
DR PROSITE; PS51140; CUE; 1.
PE 1: Evidence at protein level;
KW Autophagy; Cytoplasm; Isopeptide bond; Phosphoprotein; Reference proteome;
KW Ubl conjugation.
FT CHAIN 1..411
FT /note="Ubiquitin-binding protein CUE5"
FT /id="PRO_0000270974"
FT DOMAIN 97..140
FT /note="CUE"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00468"
FT REGION 1..102
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 142..411
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 373..376
FT /note="AIM"
FT COMPBIAS 26..63
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 75..101
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 158..240
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 243..274
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 293..307
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 344..358
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 21
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17330950,
FT ECO:0007744|PubMed:18407956, ECO:0007744|PubMed:19779198"
FT MOD_RES 36
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18407956"
FT MOD_RES 70
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:17330950,
FT ECO:0007744|PubMed:18407956, ECO:0007744|PubMed:19779198"
FT MOD_RES 91
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17287358"
FT MOD_RES 167
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:17330950,
FT ECO:0007744|PubMed:18407956, ECO:0007744|PubMed:19779198"
FT MOD_RES 220
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17330950,
FT ECO:0007744|PubMed:18407956, ECO:0007744|PubMed:19779198"
FT MOD_RES 309
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18407956,
FT ECO:0007744|PubMed:19779198"
FT MOD_RES 318
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 346
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 348
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17330950"
FT MOD_RES 352
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 364
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:17330950,
FT ECO:0007744|PubMed:18407956, ECO:0007744|PubMed:19779198"
FT MOD_RES 367
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 407
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17330950,
FT ECO:0007744|PubMed:18407956, ECO:0007744|PubMed:19779198"
FT CROSSLNK 15
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0007744|PubMed:22106047"
FT CROSSLNK 59
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0007744|PubMed:22106047"
FT CROSSLNK 76
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0007744|PubMed:22106047"
FT CROSSLNK 156
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0007744|PubMed:22106047"
FT CROSSLNK 354
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0007744|PubMed:22106047"
FT CROSSLNK 396
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0000269|PubMed:12872131"
FT MUTAGEN 109
FT /note="F->A: Impairs interaction with ubiquitin; when
FT associated with A-110."
FT /evidence="ECO:0000269|PubMed:25042851"
FT MUTAGEN 110
FT /note="P->A: Impairs interaction with ubiquitin; when
FT associated with A-109."
FT /evidence="ECO:0000269|PubMed:25042851"
FT MUTAGEN 135
FT /note="L->A: Impairs interaction with ubiquitin; when
FT associated with A-136."
FT /evidence="ECO:0000269|PubMed:25042851"
FT MUTAGEN 136
FT /note="L->A: Impairs interaction with ubiquitin; when
FT associated with A-135."
FT /evidence="ECO:0000269|PubMed:25042851"
FT MUTAGEN 373
FT /note="W->A: Impairs interaction with ATG8."
FT /evidence="ECO:0000269|PubMed:25042851"
FT MUTAGEN 376
FT /note="L->A: Impairs interaction with ATG8."
FT /evidence="ECO:0000269|PubMed:25042851"
SQ SEQUENCE 411 AA; 46870 MW; 0D455F9AD637AC8D CRC64;
MEEKEGIKDS SLLEKSNVPE SINEDISKTT DVDLNSDGKK DNDTSAKDGT PKVEEKVNKS
SGIDEDEVVT PAEDAKEEEE EHPPLPARRK SEEEPSKENP ILQELKDAFP NLEEKYIKAV
IIASQGVLSP AFNALLFLSD PESGKDIELP TQPVRKNPEA PARRRQTQLE QDELLARQLD
EQFNSSHSRR RNRDRATRSM HEQRRRRHNP NEREQHHEDS EEEDSWSQFV EKDLPELTDR
AGRSLQDTAN KVSNWISDAY RRNFASGNEQ NDNQHGHQDQ QEWEPEIVDL SQGGKNSRPQ
QPERRRFNSF GVQVGDDSLE SHGITLHNED GFEDDEDVPP QLPTRTKSGE STGKVVAETT
YIDTPDTETK KKWQPLPPEP LDTTPTKVNA VSRNKKNPDE DEFLINSDDE M
