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 27-MAR-2024, entry version 156. 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}; GN 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}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- 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; 117. DR DIP; DIP-1796N; -. DR IntAct; P53899; 6. DR MINT; P53899; -. DR STRING; 4932.YNL155W; -. DR iPTMnet; P53899; -. DR MaxQB; P53899; -. DR PaxDb; 4932-YNL155W; -. DR PeptideAtlas; P53899; -. DR EnsemblFungi; YNL155W_mRNA; YNL155W; YNL155W. DR GeneID; 855567; -. DR KEGG; sce:YNL155W; -. DR AGR; SGD:S000005099; -. DR SGD; S000005099; CUZ1. DR VEuPathDB; FungiDB:YNL155W; -. DR eggNOG; KOG3183; Eukaryota. DR HOGENOM; CLU_052358_2_1_1; -. DR InParanoid; P53899; -. DR OMA; KETQFRV; -. DR OrthoDB; 103213at2759; -. DR BioCyc; YEAST:G3O-33171-MONOMER; -. DR BioGRID-ORCS; 855567; 0 hits in 10 CRISPR screens. 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; AN1-like Zinc finger; 1. DR InterPro; IPR035896; AN1-like_Znf. DR InterPro; IPR000058; Znf_AN1. DR PANTHER; PTHR14677:SF20; AN1-TYPE ZINC FINGER PROTEIN 1; 1. DR PANTHER; PTHR14677; ARSENITE INDUCUBLE RNA ASSOCIATED PROTEIN AIP-1-RELATED; 1. DR Pfam; PF01428; zf-AN1; 1. DR SMART; SM00154; ZnF_AN1; 1. DR SUPFAM; SSF118310; AN1-like Zinc finger; 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 //