DMA2_YEAST
ID DMA2_YEAST Reviewed; 522 AA.
AC P53924; B0KZS8; B0KZU6; B0KZW4; B0L009; D6W166; Q66GT0;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 03-AUG-2022, entry version 180.
DE RecName: Full=E3 ubiquitin-protein ligase DMA2;
DE EC=2.3.2.27 {ECO:0000269|PubMed:18202552};
DE AltName: Full=Checkpoint forkhead associated with RING domains-containing protein 1;
DE AltName: Full=Defective in mitotic arrest protein 2;
DE AltName: Full=RING-type E3 ubiquitin transferase DMA2 {ECO:0000305};
GN Name=DMA2; Synonyms=CHF2; OrderedLocusNames=YNL116W; ORFNames=N1925;
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], AND VARIANTS ALA-13; HIS-111; LEU-149;
RP THR-165; THR-202; GLN-239; VAL-428 AND 511-LEU--PRO-522 DEL.
RC STRAIN=ATCC 200060 / W303, S103, SK1, V1-09, YJM 1129, YJM 230, YJM 269,
RC YJM 270, YJM 320, YJM 326, YJM 339, and YJM 627;
RX PubMed=18780730; DOI=10.1534/genetics.108.092932;
RA Sinha H., David L., Pascon R.C., Clauder-Muenster S., Krishnakumar S.,
RA Nguyen M., Shi G., Dean J., Davis R.W., Oefner P.J., McCusker J.H.,
RA Steinmetz L.M.;
RT "Sequential elimination of major-effect contributors identifies additional
RT quantitative trait loci conditioning high-temperature growth in yeast.";
RL Genetics 180:1661-1670(2008).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=9090055;
RX DOI=10.1002/(sici)1097-0061(19970315)13:3<261::aid-yea64>3.0.co;2-l;
RA de Antoni A., D'Angelo M., Dal Pero F., Sartorello F., Pandolfo D.,
RA Pallavicini A., Lanfranchi G., Valle G.;
RT "The DNA sequence of cosmid 14-13b from chromosome XIV of Saccharomyces
RT cerevisiae reveals an unusually high number of overlapping open reading
RT frames.";
RL Yeast 13:261-266(1997).
RN [3]
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 [4]
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 [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 FUNCTION, AND INTERACTION WITH CDC123.
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 [8]
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 [9]
RP FUNCTION, CATALYTIC ACTIVITY, IDENTIFICATION BY MASS SPECTROMETRY, AND
RP UBIQUITINATION AT LYS-211; LYS-256; LYS-258; LYS-288; LYS-310; LYS-333;
RP LYS-343; LYS-346; LYS-366; LYS-406; LYS-412 AND LYS-423.
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 [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-206, 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).
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. Involved in nutritional control of the
CC cell cycle. Required for proper spindle positioning, likely regulating
CC septin ring deposition at the bud neck. {ECO:0000269|PubMed:15146058,
CC ECO:0000269|PubMed:15319434, ECO:0000269|PubMed:18202552}.
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 -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:14562095}.
CC -!- PTM: UBC4-dependent autoubiquitination occurs at Lys-211, Lys-258, Lys-
CC 288, Lys-310, Lys-333, Lys-343, Lys-346, Lys-366, Lys-406, Lys-412 and
CC Lys-423. UBC4-dependent autoubiquitination is responsible for DMA2
CC turnover. UBC13/MMS2-dependent autoubiquitination occurs at Lys-258,
CC Lys-310, Lys-346 and Lys-366. Lys-211, Lys-256, Lys-288, Lys-310, Lys-
CC 343, Lys-258, Lys-366 and Lys-412 are also ubiquitinated in trans by
CC DMA1 E3 ligase in association with UBC4. {ECO:0000269|PubMed:18202552}.
CC -!- MISCELLANEOUS: Present with 1750 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the DMA1 family. {ECO:0000305}.
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DR EMBL; EF125216; ABN58541.1; -; Genomic_DNA.
DR EMBL; EF125217; ABN58550.1; -; Genomic_DNA.
DR EMBL; EF125218; ABN58559.1; -; Genomic_DNA.
DR EMBL; EF125219; ABN58568.1; -; Genomic_DNA.
DR EMBL; EF125220; ABN58576.1; -; Genomic_DNA.
DR EMBL; EF125221; ABN58586.1; -; Genomic_DNA.
DR EMBL; EF125222; ABN58595.1; -; Genomic_DNA.
DR EMBL; EF125223; ABN58604.1; -; Genomic_DNA.
DR EMBL; EF125224; ABN58613.1; -; Genomic_DNA.
DR EMBL; EF125225; ABN58622.1; -; Genomic_DNA.
DR EMBL; EF125226; ABN58631.1; -; Genomic_DNA.
DR EMBL; EF125228; ABN58649.1; -; Genomic_DNA.
DR EMBL; Z69382; CAA93391.1; -; Genomic_DNA.
DR EMBL; Z71392; CAA95996.1; -; Genomic_DNA.
DR EMBL; BK005579; DAA05594.1; -; Genomic_DNA.
DR EMBL; BK006947; DAA10432.1; -; Genomic_DNA.
DR PIR; S63057; S63057.
DR RefSeq; NP_014283.3; NM_001182954.3.
DR AlphaFoldDB; P53924; -.
DR SMR; P53924; -.
DR BioGRID; 35710; 175.
DR DIP; DIP-1774N; -.
DR IntAct; P53924; 17.
DR MINT; P53924; -.
DR STRING; 4932.YNL116W; -.
DR iPTMnet; P53924; -.
DR MaxQB; P53924; -.
DR PaxDb; P53924; -.
DR PRIDE; P53924; -.
DR EnsemblFungi; YNL116W_mRNA; YNL116W; YNL116W.
DR GeneID; 855607; -.
DR KEGG; sce:YNL116W; -.
DR SGD; S000005060; DMA2.
DR VEuPathDB; FungiDB:YNL116W; -.
DR eggNOG; KOG3872; Eukaryota.
DR GeneTree; ENSGT00940000176812; -.
DR HOGENOM; CLU_017542_2_0_1; -.
DR InParanoid; P53924; -.
DR BioCyc; YEAST:G3O-33139-MON; -.
DR Reactome; R-SCE-5693565; Recruitment and ATM-mediated phosphorylation of repair and signaling proteins at DNA double strand breaks.
DR PRO; PR:P53924; -.
DR Proteomes; UP000002311; Chromosome XIV.
DR RNAct; P53924; protein.
DR GO; GO:0032153; C:cell division site; IBA:GO_Central.
DR GO; GO:0032177; C:cellular bud neck split septin rings; IMP:SGD.
DR GO; GO:0005934; C:cellular bud tip; IMP:SGD.
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; IBA:GO_Central.
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; Phosphoprotein; Reference proteome; Transferase; Ubl conjugation;
KW Ubl conjugation pathway; Zinc; Zinc-finger.
FT CHAIN 1..522
FT /note="E3 ubiquitin-protein ligase DMA2"
FT /id="PRO_0000056342"
FT DOMAIN 295..358
FT /note="FHA"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00086"
FT ZN_FING 433..477
FT /note="RING-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00175"
FT REGION 1..56
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 69..92
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 12..56
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 206
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18407956"
FT CROSSLNK 211
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0000269|PubMed:18202552"
FT CROSSLNK 256
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0000269|PubMed:18202552"
FT CROSSLNK 258
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0000269|PubMed:18202552"
FT CROSSLNK 288
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0000269|PubMed:18202552"
FT CROSSLNK 310
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0000269|PubMed:18202552"
FT CROSSLNK 333
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0000269|PubMed:18202552"
FT CROSSLNK 343
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0000269|PubMed:18202552"
FT CROSSLNK 346
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0000269|PubMed:18202552"
FT CROSSLNK 366
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0000269|PubMed:18202552"
FT CROSSLNK 406
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0000269|PubMed:18202552"
FT CROSSLNK 412
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0000269|PubMed:18202552"
FT CROSSLNK 423
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0000269|PubMed:18202552"
FT VARIANT 13
FT /note="T -> A (in strain: YJM 269, YJM 270, YJM 326 and YJM
FT 1129)"
FT /evidence="ECO:0000269|PubMed:18780730"
FT VARIANT 111
FT /note="R -> H (in strain: YJM 269, YJM 270, YJM 326 and YJM
FT 1129)"
FT /evidence="ECO:0000269|PubMed:18780730"
FT VARIANT 149
FT /note="S -> L (in strain: YJM 269, YJM 270, YJM 326 and YJM
FT 1129)"
FT /evidence="ECO:0000269|PubMed:18780730"
FT VARIANT 165
FT /note="S -> T (in strain: YJM 267)"
FT /evidence="ECO:0000269|PubMed:18780730"
FT VARIANT 202
FT /note="I -> T (in strain: YJM 269, YJM 270, YJM 326 and YJM
FT 1129)"
FT /evidence="ECO:0000269|PubMed:18780730"
FT VARIANT 239
FT /note="E -> Q (in strain: YJM 267)"
FT /evidence="ECO:0000269|PubMed:18780730"
FT VARIANT 428
FT /note="I -> V (in strain: SK1, V1-09, YJM 267, YJM 269, YJM
FT 270, YJM 280, YJM 320,YJM 326, YJM 339 and YJM 1129)"
FT /evidence="ECO:0000269|PubMed:18780730"
FT VARIANT 511..522
FT /note="Missing (in strain: SK1)"
FT /evidence="ECO:0000269|PubMed:18780730"
SQ SEQUENCE 522 AA; 57584 MW; AE1BD2D617221607 CRC64;
MYTPIPANTP APTAPTSSMT SNSSSASNAN TTSSSGINPR NRASGTPSNE RARPASGISS
FLNTFGIRQN SQTASSSAAP DQRLFGTTPS NSHMSVAMES IDTAPQQQEP RLHHPIQMPL
SAQFHVHRNY QLPISISLTA PTTTDHQQSS AHNFEGNNVG NVQESLNQRQ PNGTNNTTTS
IISMAPAATT RNIVGGADGS TIVNNSQEMY KNLRHLIYAA NQPNGTEILH LDLPATSAEE
SNNMFNVDEV TLKQRKDKHG LFSIRLTPFI DSSSTTNQGL FFEPIIRKAG PGSQLVIGRY
TERVRDAISK IPEQYHPVVF KSKVVSRTHG CFKVDSQGNW YIKDVKSSSG TFLNHQRLSP
ASSLSKDTPL RDGDILQLGM DFRGGTEEIY RCVRMRIELN RSWKLKANSF NKEALQRLQN
LQKLTTGIEE EDCSICLCKI KPCQAIFISP CAHSWHFRCV RRLVMLSYPQ FVCPNCRSSC
DLEASFESSD EEDESDVESE GDQLVDQLSV LMETSKDVDS HP
