WWM1_YEAST
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 03-AUG-2022, entry version 158.
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}.
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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; 224.
DR DIP; DIP-3899N; -.
DR IntAct; P43582; 63.
DR MINT; P43582; -.
DR STRING; 4932.YFL010C; -.
DR iPTMnet; P43582; -.
DR MaxQB; P43582; -.
DR PaxDb; P43582; -.
DR PRIDE; P43582; -.
DR EnsemblFungi; YFL010C_mRNA; YFL010C; YFL010C.
DR GeneID; 850538; -.
DR KEGG; sce:YFL010C; -.
DR SGD; S000001884; WWM1.
DR VEuPathDB; FungiDB:YFL010C; -.
DR eggNOG; ENOG502S4J9; Eukaryota.
DR HOGENOM; CLU_091402_0_0_1; -.
DR InParanoid; P43582; -.
DR OMA; DQYKEWF; -.
DR BioCyc; YEAST:G3O-30446-MON; -.
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 GO; GO:0006915; P:apoptotic process; IEA:UniProtKB-KW.
DR CDD; cd00201; WW; 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; SSF51045; 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 57..112
FT /note="Polar residues"
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
