ID WWM1_YEAST Reviewed; 211 AA. AC P43582; D6VTM0; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 02-SEP-2026, entry version 175. DE RecName: Full=WW domain-containing protein WWM1; DE AltName: Full=WW domain-containing protein interacting with metacaspase; GN Name=WWM1; OrderedLocusNames=YFL010C; 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=7670463; DOI=10.1038/ng0795-261; RA Murakami Y., Naitou M., Hagiwara H., Shibata T., Ozawa M., Sasanuma S., RA Sasanuma M., Tsuchiya Y., Soeda E., Yokoyama K., Yamazaki M., Tashiro H., RA Eki T.; RT "Analysis of the nucleotide sequence of chromosome VI from Saccharomyces RT cerevisiae."; RL Nat. Genet. 10:261-268(1995). 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 204511 / S288c / AB972; RA Barrell B.G., Churcher C., Rajandream M.A.; RL Submitted (SEP-1994) to the EMBL/GenBank/DDBJ databases. RN [4] RP INTERACTION WITH MCA1. RX PubMed=10688190; DOI=10.1038/35001009; RA Uetz P., Giot L., Cagney G., Mansfield T.A., Judson R.S., Knight J.R., RA Lockshon D., Narayan V., Srinivasan M., Pochart P., Qureshi-Emili A., RA Li Y., Godwin B., Conover D., Kalbfleisch T., Vijayadamodar G., Yang M., RA Johnston M., Fields S., Rothberg J.M.; RT "A comprehensive analysis of protein-protein interactions in Saccharomyces RT cerevisiae."; RL Nature 403:623-627(2000). RN [5] RP FUNCTION. RX PubMed=11274415; DOI=10.1073/pnas.051013498; RA Stevenson L.F., Kennedy B.K., Harlow E.; RT "A large-scale overexpression screen in Saccharomyces cerevisiae identifies RT previously uncharacterized cell cycle genes."; RL Proc. Natl. Acad. Sci. U.S.A. 98:3946-3951(2001). RN [6] RP SUBCELLULAR LOCATION, AND FUNCTION. RX PubMed=12062425; DOI=10.1016/s0014-5793(02)02608-x; RA Szallies A., Kubata B.K., Duszenko M.; RT "A metacaspase of Trypanosoma brucei causes loss of respiration competence RT and clonal death in the yeast Saccharomyces cerevisiae."; RL FEBS Lett. 517:144-150(2002). RN [7] 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 [8] 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 [9] RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS]. RC STRAIN=ATCC 76625 / YPH499; RX PubMed=14576278; DOI=10.1073/pnas.2135385100; RA Sickmann A., Reinders J., Wagner Y., Joppich C., Zahedi R.P., Meyer H.E., RA Schoenfisch B., Perschil I., Chacinska A., Guiard B., Rehling P., RA Pfanner N., Meisinger C.; RT "The proteome of Saccharomyces cerevisiae mitochondria."; RL Proc. Natl. Acad. Sci. U.S.A. 100:13207-13212(2003). RN [10] RP DOMAIN. RX PubMed=16606443; DOI=10.1186/gb-2006-7-4-r30; RA Hesselberth J.R., Miller J.P., Golob A., Stajich J.E., Michaud G.A., RA Fields S.; RT "Comparative analysis of Saccharomyces cerevisiae WW domains and their RT interacting proteins."; RL Genome Biol. 7:R30.1-R30.15(2006). RN [11] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-75 AND THR-78, 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 [12] RP UBIQUITINATION [LARGE SCALE ANALYSIS] AT LYS-50 AND LYS-60, AND RP IDENTIFICATION BY MASS 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 -!- FUNCTION: Involved in apoptosis. May play a role in nuclear function CC controlling cellular proliferation coupled to mitochondrial biogenesis. CC Causes impaired growth when overexpressed. CC {ECO:0000269|PubMed:11274415, ECO:0000269|PubMed:12062425}. CC -!- SUBUNIT: Interacts with metacaspase MCA1. CC {ECO:0000269|PubMed:10688190}. CC -!- SUBCELLULAR LOCATION: Cytoplasm. Nucleus. Mitochondrion. CC -!- MISCELLANEOUS: Present with 6020 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; D50617; BAA09228.1; -; Genomic_DNA. DR EMBL; Z46255; CAA86342.1; -; Genomic_DNA. DR EMBL; BK006940; DAA12430.1; -; Genomic_DNA. DR PIR; S48311; S48311. DR RefSeq; NP_570898.1; NM_001179956.1. DR AlphaFoldDB; P43582; -. DR SMR; P43582; -. DR BioGRID; 31137; 236. DR DIP; DIP-3899N; -. DR FunCoup; P43582; 102. DR IntAct; P43582; 63. DR MINT; P43582; -. DR STRING; 4932.YFL010C; -. DR GlyGen; P43582; 6 sites, 1 O-linked glycan (6 sites). DR iPTMnet; P43582; -. DR PaxDb; 4932-YFL010C; -. DR PeptideAtlas; P43582; -. DR EnsemblFungi; YFL010C_mRNA; YFL010C; YFL010C. DR GeneID; 850538; -. DR KEGG; sce:YFL010C; -. DR AGR; SGD:S000001884; -. DR SGD; S000001884; WWM1. DR VEuPathDB; FungiDB:YFL010C; -. DR eggNOG; ENOG502S4J9; Eukaryota. DR HOGENOM; CLU_091402_0_0_1; -. DR InParanoid; P43582; -. DR OMA; RWNDQYK; -. DR OrthoDB; 2444812at2759; -. DR BioCyc; YEAST:G3O-30446-MONOMER; -. DR BioGRID-ORCS; 850538; 8 hits in 10 CRISPR screens. DR PRO; PR:P43582; -. DR Proteomes; UP000002311; Chromosome VI. DR RNAct; P43582; protein. DR GO; GO:0005737; C:cytoplasm; HDA:SGD. DR GO; GO:0005739; C:mitochondrion; HDA:SGD. DR GO; GO:0005634; C:nucleus; IDA:SGD. DR CDD; cd00201; WW; 1. DR Gene3D; 2.20.70.10; -; 1. DR InterPro; IPR001202; WW_dom. DR InterPro; IPR036020; WW_dom_sf. DR Pfam; PF00397; WW; 1. DR SMART; SM00456; WW; 1. DR SUPFAM; SSF51045; WW domain; 1. DR PROSITE; PS01159; WW_DOMAIN_1; 1. DR PROSITE; PS50020; WW_DOMAIN_2; 1. PE 1: Evidence at protein level; KW Apoptosis; Cytoplasm; Isopeptide bond; Mitochondrion; Nucleus; KW Phosphoprotein; Reference proteome; Ubl conjugation. FT CHAIN 1..211 FT /note="WW domain-containing protein WWM1" FT /id="PRO_0000076096" FT DOMAIN 9..43 FT /note="WW" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00224" FT REGION 32..116 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 80..116 FT /note="Low complexity" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT MOD_RES 75 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:19779198" FT MOD_RES 78 FT /note="Phosphothreonine" FT /evidence="ECO:0007744|PubMed:19779198" FT CROSSLNK 50 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in ubiquitin)" FT /evidence="ECO:0007744|PubMed:22106047" FT CROSSLNK 60 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in ubiquitin)" FT /evidence="ECO:0007744|PubMed:22106047" SQ SEQUENCE 211 AA; 22655 MW; 2731E7C69817B82F CRC64; MAQSKSNPPQ VPSGWKAVFD DEYQTWYYVD LSTNSSQWEP PRGTTWPRPK GPPPGVNNEK SSRQQADQAP PPYSSQSTPQ VQAGAQAQQP RYYQPQQPQY PQYPQQQRYY PQQAPMPAAA PQQAYYGTAP STSKGSGHGG AMMGGLLGVG AGLLGGAMLE HAFDDHNYDG PDTVVVENNY YGDDAGGSDG GFDDAGGFDG GFDDGFDGSD F //