CUZ1_YEAST
ID CUZ1_YEAST Reviewed; 274 AA.
AC P53899; D6W128;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 03-AUG-2022, entry version 150.
DE RecName: Full=CDC48-associated ubiquitin-like/zinc finger protein 1 {ECO:0000303|PubMed:24121501};
DE Short=CDC48-associated UBL/Zn-finger protein 1 {ECO:0000303|PubMed:24121501};
GN Name=CUZ1 {ECO:0000303|PubMed:24121501};
GN OrderedLocusNames=YNL155W {ECO:0000312|SGD:S000005099}; ORFNames=N1751;
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 [GENOMIC DNA].
RC STRAIN=ATCC 96604 / S288c / FY1679;
RX PubMed=8686380;
RX DOI=10.1002/(sici)1097-0061(199602)12:2<169::aid-yea894>3.0.co;2-b;
RA Nasr F., Becam A.-M., Herbert C.J.;
RT "The sequence of 36.8 kb from the left arm of chromosome XIV reveals 24
RT complete open reading frames: 18 correspond to new genes, one of which
RT encodes a protein similar to the human myotonic dystrophy kinase.";
RL Yeast 12:169-175(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169873;
RA Philippsen P., Kleine K., Poehlmann R., Duesterhoeft A., Hamberg K.,
RA Hegemann J.H., Obermaier B., Urrestarazu L.A., Aert R., Albermann K.,
RA Altmann R., Andre B., Baladron V., Ballesta J.P.G., Becam A.-M.,
RA Beinhauer J.D., Boskovic J., Buitrago M.J., Bussereau F., Coster F.,
RA Crouzet M., D'Angelo M., Dal Pero F., De Antoni A., del Rey F., Doignon F.,
RA Domdey H., Dubois E., Fiedler T.A., Fleig U., Floeth M., Fritz C.,
RA Gaillardin C., Garcia-Cantalejo J.M., Glansdorff N., Goffeau A.,
RA Gueldener U., Herbert C.J., Heumann K., Heuss-Neitzel D., Hilbert H.,
RA Hinni K., Iraqui Houssaini I., Jacquet M., Jimenez A., Jonniaux J.-L.,
RA Karpfinger-Hartl L., Lanfranchi G., Lepingle A., Levesque H., Lyck R.,
RA Maftahi M., Mallet L., Maurer C.T.C., Messenguy F., Mewes H.-W., Moestl D.,
RA Nasr F., Nicaud J.-M., Niedenthal R.K., Pandolfo D., Pierard A.,
RA Piravandi E., Planta R.J., Pohl T.M., Purnelle B., Rebischung C.,
RA Remacha M.A., Revuelta J.L., Rinke M., Saiz J.E., Sartorello F.,
RA Scherens B., Sen-Gupta M., Soler-Mira A., Urbanus J.H.M., Valle G.,
RA Van Dyck L., Verhasselt P., Vierendeels F., Vissers S., Voet M.,
RA Volckaert G., Wach A., Wambutt R., Wedler H., Zollner A., Hani J.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XIV and its
RT evolutionary implications.";
RL Nature 387:93-98(1997).
RN [3]
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 [4]
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 [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-273, 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-273, 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 FUNCTION, AND INTERACTION WITH CDC48 AND THE PROTEASOME.
RX PubMed=24121501; DOI=10.1074/jbc.m113.521088;
RA Sa-Moura B., Funakoshi M., Tomko R.J. Jr., Dohmen R.J., Wu Z., Peng J.,
RA Hochstrasser M.;
RT "A conserved protein with AN1 zinc finger and ubiquitin-like domains
RT modulates Cdc48 (p97) function in the ubiquitin-proteasome pathway.";
RL J. Biol. Chem. 288:33682-33696(2013).
RN [10]
RP FUNCTION, INTERACTION WITH CDC48; RPN2; THE PROTEASOME AND UBIQUITINATED
RP PROTEINS, AND INDUCTION BY RPN4.
RX PubMed=24297164; DOI=10.1074/jbc.m113.534032;
RA Hanna J., Waterman D., Isasa M., Elsasser S., Shi Y., Gygi S., Finley D.;
RT "Cuz1/Ynl155w, a zinc-dependent ubiquitin-binding protein, protects cells
RT from metalloid-induced proteotoxicity.";
RL J. Biol. Chem. 289:1876-1885(2014).
RN [11]
RP FUNCTION.
RX PubMed=29804830; DOI=10.1016/j.molcel.2018.04.021;
RA Turakhiya A., Meyer S.R., Marincola G., Boehm S., Vanselow J.T.,
RA Schlosser A., Hofmann K., Buchberger A.;
RT "ZFAND1 recruits p97 and the 26S proteasome to promote the clearance of
RT arsenite-induced stress granules.";
RL Mol. Cell 70:906-919(2018).
CC -!- FUNCTION: Promotes efficient arsenite-induced clearance of stress
CC granules (SGs) (PubMed:29804830). May have a role in the ubiquitin-
CC proteasome system (UPS) protecting cells from metalloid-induced
CC proteotoxicity (PubMed:24121501, PubMed:24297164).
CC {ECO:0000269|PubMed:24121501, ECO:0000269|PubMed:24297164,
CC ECO:0000269|PubMed:29804830}.
CC -!- SUBUNIT: Interacts (via its ubiquitin-like domain) with CDC48 (via N-
CC terminus). Associates with the 26S proteasome. Specifically interacts
CC with the regulatory particle (RP) subunit RPN2. Exposure to arsenite, a
CC known inducer of protein misfolding resulting in accumulation of
CC polyubiquitinated conjugates, enhances the association with the
CC proteoasome. Binds to ubiquitinated proteins conjugated to a 4 or more
CC molecule ubiquitin chain. Binding to ubiquitinated proteins is zinc-
CC dependent. {ECO:0000269|PubMed:24121501, ECO:0000269|PubMed:24297164}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:14562095}. Nucleus
CC {ECO:0000269|PubMed:14562095}.
CC -!- INDUCTION: By transcriptional activator RPN4.
CC {ECO:0000269|PubMed:24297164}.
CC -!- MISCELLANEOUS: Present with 4280 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
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DR EMBL; X92517; CAA63284.1; -; Genomic_DNA.
DR EMBL; Z71431; CAA96042.1; -; Genomic_DNA.
DR EMBL; AY692693; AAT92712.1; -; Genomic_DNA.
DR EMBL; BK006947; DAA10394.1; -; Genomic_DNA.
DR PIR; S60972; S60972.
DR RefSeq; NP_014244.1; NM_001182993.1.
DR PDB; 5IJ4; NMR; -; A=11-59.
DR PDBsum; 5IJ4; -.
DR AlphaFoldDB; P53899; -.
DR SMR; P53899; -.
DR BioGRID; 35674; 99.
DR DIP; DIP-1796N; -.
DR IntAct; P53899; 6.
DR MINT; P53899; -.
DR STRING; 4932.YNL155W; -.
DR iPTMnet; P53899; -.
DR MaxQB; P53899; -.
DR PaxDb; P53899; -.
DR PRIDE; P53899; -.
DR EnsemblFungi; YNL155W_mRNA; YNL155W; YNL155W.
DR GeneID; 855567; -.
DR KEGG; sce:YNL155W; -.
DR SGD; S000005099; CUZ1.
DR VEuPathDB; FungiDB:YNL155W; -.
DR eggNOG; KOG3183; Eukaryota.
DR HOGENOM; CLU_052358_2_1_1; -.
DR InParanoid; P53899; -.
DR OMA; EAIGAHC; -.
DR BioCyc; YEAST:G3O-33171-MON; -.
DR PRO; PR:P53899; -.
DR Proteomes; UP000002311; Chromosome XIV.
DR RNAct; P53899; protein.
DR GO; GO:0005737; C:cytoplasm; HDA:SGD.
DR GO; GO:0005634; C:nucleus; HDA:SGD.
DR GO; GO:0070628; F:proteasome binding; IDA:SGD.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0071243; P:cellular response to arsenic-containing substance; IMP:SGD.
DR GO; GO:1903843; P:cellular response to arsenite ion; IMP:UniProtKB.
DR GO; GO:0043161; P:proteasome-mediated ubiquitin-dependent protein catabolic process; IMP:SGD.
DR GO; GO:0035617; P:stress granule disassembly; IMP:UniProtKB.
DR Gene3D; 4.10.1110.10; -; 1.
DR InterPro; IPR035896; AN1-like_Znf.
DR InterPro; IPR000058; Znf_AN1.
DR Pfam; PF01428; zf-AN1; 1.
DR SMART; SM00154; ZnF_AN1; 1.
DR SUPFAM; SSF118310; SSF118310; 1.
DR PROSITE; PS51039; ZF_AN1; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cytoplasm; Metal-binding; Nucleus; Phosphoprotein;
KW Reference proteome; Stress response; Zinc; Zinc-finger.
FT CHAIN 1..274
FT /note="CDC48-associated ubiquitin-like/zinc finger protein
FT 1"
FT /id="PRO_0000203418"
FT ZN_FING 12..58
FT /note="AN1-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00449"
FT REGION 170..266
FT /note="Ubiquitin-like"
FT /evidence="ECO:0000303|PubMed:24121501"
FT BINDING 18
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00449"
FT BINDING 21
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00449"
FT BINDING 31
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00449"
FT BINDING 34
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00449"
FT BINDING 39
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00449"
FT BINDING 42
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00449"
FT BINDING 48
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00449"
FT BINDING 50
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00449"
FT MOD_RES 273
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18407956,
FT ECO:0007744|PubMed:19779198"
FT STRAND 19..21
FT /evidence="ECO:0007829|PDB:5IJ4"
FT STRAND 24..27
FT /evidence="ECO:0007829|PDB:5IJ4"
FT TURN 32..34
FT /evidence="ECO:0007829|PDB:5IJ4"
FT HELIX 40..42
FT /evidence="ECO:0007829|PDB:5IJ4"
FT HELIX 46..48
FT /evidence="ECO:0007829|PDB:5IJ4"
FT HELIX 51..55
FT /evidence="ECO:0007829|PDB:5IJ4"
SQ SEQUENCE 274 AA; 31517 MW; 1BC3E0D932AC1365 CRC64;
MSAAIEKETG MLDVGKHCAY CRQLDFLPFH CSFCNEDFCS NHRLKEDHHC RWLLEHEEVH
KTEKSPSKSR DGSSSNDEAY FKSLLPERAS VRIQRVSETR EPLRGSNTAK VSSTLNSKTL
DKIFKFFQRN EKRKSNNKSK KNFGSSSNKI IQLANLKKIA KGDPKIPMQN RIYIWCYLVD
GDETDIAKED TRMPLYINKM WPVGRAMDYL SIQLNVKSST LTNSSSNDKF QLCKLKEGKQ
VSFYNIGASL RVTNEIKDLD TLYLVHNNAD EKSN
