CUE4_YEAST
ID CUE4_YEAST Reviewed; 117 AA.
AC Q04201; D6W0I3;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 1.
DT 03-AUG-2022, entry version 135.
DE RecName: Full=CUE domain-containing protein CUE4;
DE AltName: Full=Coupling of ubiquitin conjugation to ER degradation protein 4;
GN Name=CUE4; OrderedLocusNames=YML101C;
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]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169872;
RA Bowman S., Churcher C.M., Badcock K., Brown D., Chillingworth T.,
RA Connor R., Dedman K., Devlin K., Gentles S., Hamlin N., Hunt S., Jagels K.,
RA Lye G., Moule S., Odell C., Pearson D., Rajandream M.A., Rice P.,
RA Skelton J., Walsh S.V., Whitehead S., Barrell B.G.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XIII.";
RL Nature 387:90-93(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 SUBCELLULAR LOCATION.
RX PubMed=11914276; DOI=10.1101/gad.970902;
RA Kumar A., Agarwal S., Heyman J.A., Matson S., Heidtman M., Piccirillo S.,
RA Umansky L., Drawid A., Jansen R., Liu Y., Cheung K.-H., Miller P.,
RA Gerstein M., Roeder G.S., Snyder M.;
RT "Subcellular localization of the yeast proteome.";
RL Genes Dev. 16:707-719(2002).
RN [4]
RP GENE NAME, CUE DOMAIN, AND UBIQUITINATION.
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]
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]
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 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-48, AND IDENTIFICATION BY
RP MASS 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 [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-48, AND IDENTIFICATION BY
RP 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 [9]
RP UBIQUITINATION [LARGE SCALE ANALYSIS] AT LYS-37, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE 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).
CC -!- INTERACTION:
CC Q04201; P47155: ILM1; NbExp=3; IntAct=EBI-27928, EBI-2051644;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:11914276}.
CC Endoplasmic reticulum {ECO:0000269|PubMed:14562095}.
CC -!- DOMAIN: The CUE domain binds ubiquitin, which may facilitate
CC intramolecular monoubiquitination.
CC -!- PTM: Ubiquitinated. {ECO:0000269|PubMed:12628920}.
CC -!- MISCELLANEOUS: Present with 1850 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
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DR EMBL; X80835; CAA56796.1; -; Genomic_DNA.
DR EMBL; BK006946; DAA09797.1; -; Genomic_DNA.
DR PIR; S47448; S47448.
DR RefSeq; NP_013607.1; NM_001182462.1.
DR AlphaFoldDB; Q04201; -.
DR SMR; Q04201; -.
DR BioGRID; 35042; 69.
DR DIP; DIP-4525N; -.
DR IntAct; Q04201; 5.
DR MINT; Q04201; -.
DR STRING; 4932.YML101C; -.
DR iPTMnet; Q04201; -.
DR MaxQB; Q04201; -.
DR PaxDb; Q04201; -.
DR PRIDE; Q04201; -.
DR EnsemblFungi; YML101C_mRNA; YML101C; YML101C.
DR GeneID; 854871; -.
DR KEGG; sce:YML101C; -.
DR SGD; S000004568; CUE4.
DR VEuPathDB; FungiDB:YML101C; -.
DR HOGENOM; CLU_2225278_0_0_1; -.
DR InParanoid; Q04201; -.
DR OMA; XSVATND; -.
DR BioCyc; YEAST:G3O-32685-MON; -.
DR PRO; PR:Q04201; -.
DR Proteomes; UP000002311; Chromosome XIII.
DR RNAct; Q04201; protein.
DR GO; GO:0005737; C:cytoplasm; HDA:SGD.
DR GO; GO:0005783; C:endoplasmic reticulum; HDA:SGD.
DR GO; GO:0043130; F:ubiquitin binding; IEA:InterPro.
DR InterPro; IPR003892; CUE.
DR Pfam; PF02845; CUE; 1.
DR SMART; SM00546; CUE; 1.
DR PROSITE; PS51140; CUE; 1.
PE 1: Evidence at protein level;
KW Cytoplasm; Endoplasmic reticulum; Isopeptide bond; Phosphoprotein;
KW Reference proteome; Ubl conjugation.
FT CHAIN 1..117
FT /note="CUE domain-containing protein CUE4"
FT /id="PRO_0000203244"
FT DOMAIN 74..116
FT /note="CUE"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00468"
FT REGION 27..74
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 59..74
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 48
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18407956,
FT ECO:0007744|PubMed:19779198"
FT CROSSLNK 37
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0007744|PubMed:22106047"
SQ SEQUENCE 117 AA; 12893 MW; EC50D817C4B66947 CRC64;
MDGSTIVFIL TMVCLFVYTV KHRGAKQVPS RTVQDAKPAP SVATNDPSPE PVPSAPEERV
ARLNRHGSDR KRAVNSDMVE IVMTMAPHVP QEKVVQDLRN TGSIEHTMEN IFAGKLD
