CUE2_YEAST
ID CUE2_YEAST Reviewed; 443 AA.
AC P36075; D6VXJ8;
DT 01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-1994, sequence version 1.
DT 03-AUG-2022, entry version 160.
DE RecName: Full=Ubiquitin-binding protein CUE2;
DE AltName: Full=Coupling of ubiquitin conjugation to ER degradation protein 2;
GN Name=CUE2; OrderedLocusNames=YKL090W;
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=8196765; DOI=10.1038/369371a0;
RA Dujon B., Alexandraki D., Andre B., Ansorge W., Baladron V.,
RA Ballesta J.P.G., Banrevi A., Bolle P.-A., Bolotin-Fukuhara M., Bossier P.,
RA Bou G., Boyer J., Buitrago M.J., Cheret G., Colleaux L.,
RA Daignan-Fornier B., del Rey F., Dion C., Domdey H., Duesterhoeft A.,
RA Duesterhus S., Entian K.-D., Erfle H., Esteban P.F., Feldmann H.,
RA Fernandes L., Fobo G.M., Fritz C., Fukuhara H., Gabel C., Gaillon L.,
RA Garcia-Cantalejo J.M., Garcia-Ramirez J.J., Gent M.E., Ghazvini M.,
RA Goffeau A., Gonzalez A., Grothues D., Guerreiro P., Hegemann J.H.,
RA Hewitt N., Hilger F., Hollenberg C.P., Horaitis O., Indge K.J.,
RA Jacquier A., James C.M., Jauniaux J.-C., Jimenez A., Keuchel H.,
RA Kirchrath L., Kleine K., Koetter P., Legrain P., Liebl S., Louis E.J.,
RA Maia e Silva A., Marck C., Monnier A.-L., Moestl D., Mueller S.,
RA Obermaier B., Oliver S.G., Pallier C., Pascolo S., Pfeiffer F.,
RA Philippsen P., Planta R.J., Pohl F.M., Pohl T.M., Poehlmann R.,
RA Portetelle D., Purnelle B., Puzos V., Ramezani Rad M., Rasmussen S.W.,
RA Remacha M.A., Revuelta J.L., Richard G.-F., Rieger M.,
RA Rodrigues-Pousada C., Rose M., Rupp T., Santos M.A., Schwager C.,
RA Sensen C., Skala J., Soares H., Sor F., Stegemann J., Tettelin H.,
RA Thierry A., Tzermia M., Urrestarazu L.A., van Dyck L.,
RA van Vliet-Reedijk J.C., Valens M., Vandenbol M., Vilela C., Vissers S.,
RA von Wettstein D., Voss H., Wiemann S., Xu G., Zimmermann J., Haasemann M.,
RA Becker I., Mewes H.-W.;
RT "Complete DNA sequence of yeast chromosome XI.";
RL Nature 369:371-378(1994).
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 STRUCTURE BY NMR OF 1-54 IN COMPLEX WITH UBIQUITIN.
RX PubMed=12787503; DOI=10.1016/s0092-8674(03)00362-3;
RA Kang R.S., Daniels C.M., Francis S.A., Shih S.C., Salerno W.J., Hicke L.,
RA Radhakrishnan I.;
RT "Solution structure of a CUE-ubiquitin complex reveals a conserved mode of
RT ubiquitin binding.";
RL Cell 113:621-630(2003).
CC -!- SUBUNIT: Binds to ubiquitin. {ECO:0000269|PubMed:12787503}.
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DR EMBL; Z28090; CAA81928.1; -; Genomic_DNA.
DR EMBL; BK006944; DAA09068.1; -; Genomic_DNA.
DR PIR; S37915; S37915.
DR RefSeq; NP_012833.1; NM_001179656.1.
DR PDB; 1OTR; NMR; -; A=6-54.
DR PDBsum; 1OTR; -.
DR AlphaFoldDB; P36075; -.
DR SMR; P36075; -.
DR BioGRID; 34043; 28.
DR DIP; DIP-1917N; -.
DR IntAct; P36075; 4.
DR MINT; P36075; -.
DR STRING; 4932.YKL090W; -.
DR iPTMnet; P36075; -.
DR MaxQB; P36075; -.
DR PaxDb; P36075; -.
DR PRIDE; P36075; -.
DR EnsemblFungi; YKL090W_mRNA; YKL090W; YKL090W.
DR GeneID; 853772; -.
DR KEGG; sce:YKL090W; -.
DR SGD; S000001573; CUE2.
DR VEuPathDB; FungiDB:YKL090W; -.
DR eggNOG; KOG2401; Eukaryota.
DR HOGENOM; CLU_590497_0_0_1; -.
DR InParanoid; P36075; -.
DR OMA; NDDHESK; -.
DR BioCyc; YEAST:G3O-31881-MON; -.
DR EvolutionaryTrace; P36075; -.
DR PRO; PR:P36075; -.
DR Proteomes; UP000002311; Chromosome XI.
DR RNAct; P36075; protein.
DR GO; GO:0004519; F:endonuclease activity; IDA:SGD.
DR GO; GO:0043130; F:ubiquitin binding; IDA:SGD.
DR GO; GO:0006379; P:mRNA cleavage; IDA:SGD.
DR GO; GO:0070966; P:nuclear-transcribed mRNA catabolic process, no-go decay; IDA:SGD.
DR CDD; cd14374; CUE1_Cue2p_like; 1.
DR CDD; cd14375; CUE2_Cue2p_like; 1.
DR Gene3D; 3.30.1370.110; -; 1.
DR InterPro; IPR003892; CUE.
DR InterPro; IPR041809; Cue2_CUE1.
DR InterPro; IPR041810; Cue2_CUE2.
DR InterPro; IPR002625; Smr_dom.
DR InterPro; IPR036063; Smr_dom_sf.
DR InterPro; IPR009060; UBA-like_sf.
DR Pfam; PF02845; CUE; 2.
DR SMART; SM00546; CUE; 2.
DR SMART; SM00463; SMR; 1.
DR SUPFAM; SSF160443; SSF160443; 1.
DR SUPFAM; SSF46934; SSF46934; 2.
DR PROSITE; PS51140; CUE; 2.
DR PROSITE; PS50828; SMR; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Reference proteome; Repeat; Ubl conjugation pathway.
FT CHAIN 1..443
FT /note="Ubiquitin-binding protein CUE2"
FT /id="PRO_0000079558"
FT DOMAIN 8..51
FT /note="CUE 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00468"
FT DOMAIN 55..98
FT /note="CUE 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00468"
FT DOMAIN 347..443
FT /note="Smr"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00321"
FT HELIX 9..19
FT /evidence="ECO:0007829|PDB:1OTR"
FT STRAND 21..23
FT /evidence="ECO:0007829|PDB:1OTR"
FT HELIX 25..34
FT /evidence="ECO:0007829|PDB:1OTR"
FT TURN 35..37
FT /evidence="ECO:0007829|PDB:1OTR"
FT HELIX 40..49
FT /evidence="ECO:0007829|PDB:1OTR"
SQ SEQUENCE 443 AA; 50874 MW; 8B7BB872C2BDC734 CRC64;
MSMDNNDDHE SKLSILMDMF PAISKSKLQV HLLENNNDLD LTIGLLLKEN DDKSTVDNEL
HQLYDMFPQL DCSVIKDQFV INEKSVESTI SDLLNYETLQ KLKDNQANSP DSVKRNEKKN
NWESTNDHIE SIIKFTDAPK NIAQEYLAEN GFDTVKAIIK IILDYYDKRD FKKDVDTFKV
KRSPNTTVRG GRVQSSTGLA HVLKKGKESA NVAQESLKRP RSYKHSLDSP QMVELNELVA
DNRDLKAINH EFLQKCLQFY DGDVVKVLNI SSLLIEDDKN ITKTWNFDEG FTLTSRDNCK
QHLPKFSTPQ ISRRNEVGNT YKLPLHDKET PEGAVPVINN LFQTYRLDFH GFLPSEAVST
LKLALNKWWS KEVAERELNS HNINSYGSKV QFVSPLIVVT GRGIHSIGGI SKVRLQVKSF
LEKNHYIFWE ESSYFRIEGK KKK
