DMA1_YEAST
ID DMA1_YEAST Reviewed; 416 AA.
AC P38823; D3DL65; Q66GT1;
DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1995, sequence version 1.
DT 03-AUG-2022, entry version 171.
DE RecName: Full=E3 ubiquitin-protein ligase DMA1 {ECO:0000305|PubMed:18202552};
DE EC=2.3.2.27 {ECO:0000269|PubMed:18202552, ECO:0000269|PubMed:23264631};
DE AltName: Full=Checkpoint forkhead associated with RING domains-containing protein 1 {ECO:0000303|PubMed:15319434};
DE AltName: Full=Defective in mitotic arrest protein 1 {ECO:0000303|PubMed:15146058};
DE AltName: Full=RING-type E3 ubiquitin transferase DMA1 {ECO:0000305};
GN Name=DMA1 {ECO:0000303|PubMed:15146058};
GN Synonyms=CHF1 {ECO:0000303|PubMed:15319434};
GN OrderedLocusNames=YHR115C {ECO:0000312|SGD:S000001157};
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], FUNCTION, INTERACTION WITH CDC123, AND
RP MUTAGENESIS OF GLY-192; SER-220; HIS-223; CYS-345 AND HIS-350.
RX PubMed=15319434; DOI=10.1074/jbc.m406151200;
RA Bieganowski P., Shilinski K., Tsichlis P.N., Brenner C.;
RT "Cdc123 and checkpoint forkhead associated with RING proteins control the
RT cell cycle by controlling eIF2gamma abundance.";
RL J. Biol. Chem. 279:44656-44666(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=8091229; DOI=10.1126/science.8091229;
RA Johnston M., Andrews S., Brinkman R., Cooper J., Ding H., Dover J., Du Z.,
RA Favello A., Fulton L., Gattung S., Geisel C., Kirsten J., Kucaba T.,
RA Hillier L.W., Jier M., Johnston L., Langston Y., Latreille P., Louis E.J.,
RA Macri C., Mardis E., Menezes S., Mouser L., Nhan M., Rifkin L., Riles L.,
RA St Peter H., Trevaskis E., Vaughan K., Vignati D., Wilcox L., Wohldman P.,
RA Waterston R., Wilson R., Vaudin M.;
RT "Complete nucleotide sequence of Saccharomyces cerevisiae chromosome
RT VIII.";
RL Science 265:2077-2082(1994).
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 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 [5]
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 [6]
RP FUNCTION.
RX PubMed=15146058; DOI=10.1091/mbc.e04-02-0094;
RA Fraschini R., Bilotta D., Lucchini G., Piatti S.;
RT "Functional characterization of Dma1 and Dma2, the budding yeast homologues
RT of Schizosaccharomyces pombe Dma1 and human Chfr.";
RL Mol. Biol. Cell 15:3796-3810(2004).
RN [7]
RP FUNCTION, CATALYTIC ACTIVITY, IDENTIFICATION BY MASS SPECTROMETRY, AND
RP UBIQUITINATION AT LYS-150; LYS-204; LYS-217; LYS-237; LYS-240; LYS-260;
RP LYS-300; LYS-306; LYS-313 AND LYS-317.
RX PubMed=18202552; DOI=10.4161/cc.7.1.5113;
RA Loring G.L., Christensen K.C., Gerber S.A., Brenner C.;
RT "Yeast Chfr homologs retard cell cycle at G1 and G2/M via Ubc4 and
RT Ubc13/Mms2-dependent ubiquitination.";
RL Cell Cycle 7:96-105(2008).
RN [8]
RP FUNCTION, CATALYTIC ACTIVITY, INDUCTION, AND INTERACTION WITH PCL1.
RX PubMed=23264631; DOI=10.1074/jbc.m112.426593;
RA Hernandez-Ortega S., Bru S., Ricco N., Ramirez S., Casals N., Jimenez J.,
RA Isasa M., Crosas B., Clotet J.;
RT "Defective in mitotic arrest 1 (Dma1) ubiquitin ligase controls G1 cyclin
RT degradation.";
RL J. Biol. Chem. 288:4704-4714(2013).
CC -!- FUNCTION: E3 ubiquitin-protein ligase which functions in cell cycle
CC retarding in conjunction with the UBC4 and UBC13/MMS2 complex, 2 E2
CC ubiquitin conjugating enzymes (PubMed:18202552). Involved in
CC nutritional control of the cell cycle (PubMed:15319434). Targets the G1
CC cyclin PCL1 for destruction (PubMed:23264631). Required for proper
CC spindle positioning, likely regulating septin ring deposition at the
CC bud neck (PubMed:15146058). {ECO:0000269|PubMed:15146058,
CC ECO:0000269|PubMed:15319434, ECO:0000269|PubMed:18202552,
CC ECO:0000269|PubMed:23264631}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine +
CC [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-
CC cysteine + N(6)-ubiquitinyl-[acceptor protein]-L-lysine.;
CC EC=2.3.2.27; Evidence={ECO:0000269|PubMed:18202552,
CC ECO:0000269|PubMed:23264631};
CC -!- SUBUNIT: Interacts with CDC123 (PubMed:15319434). Interacts with PCL1
CC (PubMed:23264631). {ECO:0000269|PubMed:15319434,
CC ECO:0000269|PubMed:23264631}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:14562095}.
CC -!- INDUCTION: Protein levels are regulated by nutrient status, being high
CC under good nutrient conditions. {ECO:0000269|PubMed:23264631}.
CC -!- PTM: UBC4-dependent autoubiquitination occurs at Lys-150, Lys-204, Lys-
CC 217, Lys-237, Lys-240, Lys-260, Lys-300, Lys-306, Lys-313 and Lys-317.
CC UBC4-dependent autoubiquitination is responsible for DMA2 turnover.
CC UBC13/MMS2-dependent autoubiquitination occurs at Lys-237 and Lys-306.
CC Lys-204 and Lys-306 are also ubiquitinated in trans by DMA2 E3 ligase
CC in association with UBC4. {ECO:0000269|PubMed:18202552}.
CC -!- MISCELLANEOUS: Present with 2790 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the DMA1 family. {ECO:0000305}.
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; BK005578; DAA05593.1; -; Genomic_DNA.
DR EMBL; U00059; AAB68865.1; -; Genomic_DNA.
DR EMBL; BK006934; DAA06809.1; -; Genomic_DNA.
DR PIR; S48957; S48957.
DR RefSeq; NP_011983.1; NM_001179245.1.
DR AlphaFoldDB; P38823; -.
DR SMR; P38823; -.
DR BioGRID; 36548; 86.
DR DIP; DIP-1884N; -.
DR IntAct; P38823; 24.
DR MINT; P38823; -.
DR STRING; 4932.YHR115C; -.
DR iPTMnet; P38823; -.
DR MaxQB; P38823; -.
DR PaxDb; P38823; -.
DR PRIDE; P38823; -.
DR EnsemblFungi; YHR115C_mRNA; YHR115C; YHR115C.
DR GeneID; 856515; -.
DR KEGG; sce:YHR115C; -.
DR SGD; S000001157; DMA1.
DR VEuPathDB; FungiDB:YHR115C; -.
DR eggNOG; KOG3872; Eukaryota.
DR GeneTree; ENSGT00940000176812; -.
DR HOGENOM; CLU_017542_2_0_1; -.
DR InParanoid; P38823; -.
DR OMA; SHSWHYQ; -.
DR BioCyc; YEAST:G3O-31157-MON; -.
DR PRO; PR:P38823; -.
DR Proteomes; UP000002311; Chromosome VIII.
DR RNAct; P38823; protein.
DR GO; GO:0032153; C:cell division site; IBA:GO_Central.
DR GO; GO:0005737; C:cytoplasm; HDA:SGD.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0044732; C:mitotic spindle pole body; IBA:GO_Central.
DR GO; GO:0000151; C:ubiquitin ligase complex; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0061630; F:ubiquitin protein ligase activity; IBA:GO_Central.
DR GO; GO:0004842; F:ubiquitin-protein transferase activity; IDA:SGD.
DR GO; GO:0032186; P:cellular bud neck septin ring organization; IGI:SGD.
DR GO; GO:0000132; P:establishment of mitotic spindle orientation; IGI:SGD.
DR GO; GO:0007094; P:mitotic spindle assembly checkpoint signaling; IBA:GO_Central.
DR GO; GO:0031578; P:mitotic spindle orientation checkpoint signaling; IGI:SGD.
DR GO; GO:0031030; P:negative regulation of septation initiation signaling; IBA:GO_Central.
DR GO; GO:0051865; P:protein autoubiquitination; IDA:SGD.
DR GO; GO:0097271; P:protein localization to bud neck; IGI:SGD.
DR GO; GO:0016567; P:protein ubiquitination; IDA:SGD.
DR GO; GO:0090337; P:regulation of formin-nucleated actin cable assembly; IMP:SGD.
DR GO; GO:0000921; P:septin ring assembly; IGI:SGD.
DR GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; IGI:SGD.
DR CDD; cd00060; FHA; 1.
DR CDD; cd16458; RING-H2_Dmap_like; 1.
DR Gene3D; 3.30.40.10; -; 1.
DR InterPro; IPR042823; Dma1/Dma2_RING-H2.
DR InterPro; IPR000253; FHA_dom.
DR InterPro; IPR008984; SMAD_FHA_dom_sf.
DR InterPro; IPR001841; Znf_RING.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR Pfam; PF00498; FHA; 1.
DR Pfam; PF17123; zf-RING_11; 1.
DR SMART; SM00240; FHA; 1.
DR SUPFAM; SSF49879; SSF49879; 1.
DR PROSITE; PS50006; FHA_DOMAIN; 1.
DR PROSITE; PS50089; ZF_RING_2; 1.
PE 1: Evidence at protein level;
KW Cell cycle; Cell division; Cytoplasm; Isopeptide bond; Metal-binding;
KW Mitosis; Reference proteome; Transferase; Ubl conjugation;
KW Ubl conjugation pathway; Zinc; Zinc-finger.
FT CHAIN 1..416
FT /note="E3 ubiquitin-protein ligase DMA1"
FT /id="PRO_0000056338"
FT DOMAIN 189..252
FT /note="FHA"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00086"
FT ZN_FING 327..371
FT /note="RING-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00175"
FT REGION 1..30
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 15..30
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CROSSLNK 150
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0000269|PubMed:18202552"
FT CROSSLNK 204
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0000269|PubMed:18202552"
FT CROSSLNK 217
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0000269|PubMed:18202552"
FT CROSSLNK 237
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0000269|PubMed:18202552"
FT CROSSLNK 240
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0000269|PubMed:18202552"
FT CROSSLNK 260
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0000269|PubMed:18202552"
FT CROSSLNK 300
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0000269|PubMed:18202552"
FT CROSSLNK 306
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0000269|PubMed:18202552"
FT CROSSLNK 313
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0000269|PubMed:18202552"
FT CROSSLNK 317
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0000269|PubMed:18202552"
FT MUTAGEN 192
FT /note="G->E: Decreases the interaction with CDC123."
FT /evidence="ECO:0000269|PubMed:15319434"
FT MUTAGEN 220
FT /note="S->A: Decreases the interaction with CDC123, when
FT associated with L-223."
FT /evidence="ECO:0000269|PubMed:15319434"
FT MUTAGEN 223
FT /note="H->L: Decreases the interaction with CDC123, when
FT associated with A-220."
FT /evidence="ECO:0000269|PubMed:15319434"
FT MUTAGEN 345
FT /note="C->S: Decreases the interaction with CDC123, when
FT associated with A-350."
FT /evidence="ECO:0000269|PubMed:15319434"
FT MUTAGEN 350
FT /note="H->A: Decreases the interaction with CDC123, when
FT associated with S-345."
FT /evidence="ECO:0000269|PubMed:15319434"
SQ SEQUENCE 416 AA; 46098 MW; 4344AB155C83CBF7 CRC64;
MSTNTVPSSP PNQTPPAASG IATSHDHTKF NNPIRLPISI SLTINDTPNN NSNNNSVSNG
LGILPSRTAT SLVVANNGSA NGNVGATAAA AATVETNTAP AVNTTKSIRH FIYPPNQVNQ
TEFSLDIHLP PNTSLPERID QSTLKRRMDK HGLFSIRLTP FIDTSSTSVA NQGLFFDPII
RTAGAGSQII IGRYTERVRE AISKIPDQYH PVVFKSKVIS RTHGCFKVDD QGNWFLKDVK
SSSGTFLNHQ RLSSASTTSK DYLLHDGDII QLGMDFRGGT EEIYRCVKMK IELNKSWKLK
ANAFNKEALS RIKNLQKLTT GLEQEDCSIC LNKIKPCQAI FISPCAHSWH FHCVRRLVIM
NYPQFMCPNC RTNCDLETTL ESESESEFEN EDEDEPDIEM DIDMEINNNL GVRLVD
