NSE2_YEAST
ID NSE2_YEAST Reviewed; 267 AA.
AC P38632; D3DLN0;
DT 01-OCT-1994, integrated into UniProtKB/Swiss-Prot.
DT 27-SEP-2004, sequence version 2.
DT 03-AUG-2022, entry version 178.
DE RecName: Full=E3 SUMO-protein ligase MMS21;
DE EC=2.3.2.-;
DE AltName: Full=E3 SUMO-protein transferase MMS21 {ECO:0000305};
DE AltName: Full=Methyl methanesulfonate-sensitivity protein 21;
DE AltName: Full=Non-structural maintenance of chromosome element 2;
DE Short=Non-SMC element 2;
GN Name=MMS21; Synonyms=NSE2; OrderedLocusNames=YEL019C;
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=D7;
RA Williams T.L., Montelone B.A.;
RT "Cloning and sequence analysis of the MMS21 gene of yeast.";
RL Submitted (JUL-1994) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169868;
RA Dietrich F.S., Mulligan J.T., Hennessy K.M., Yelton M.A., Allen E.,
RA Araujo R., Aviles E., Berno A., Brennan T., Carpenter J., Chen E.,
RA Cherry J.M., Chung E., Duncan M., Guzman E., Hartzell G., Hunicke-Smith S.,
RA Hyman R.W., Kayser A., Komp C., Lashkari D., Lew H., Lin D., Mosedale D.,
RA Nakahara K., Namath A., Norgren R., Oefner P., Oh C., Petel F.X.,
RA Roberts D., Sehl P., Schramm S., Shogren T., Smith V., Taylor P., Wei Y.,
RA Botstein D., Davis R.W.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome V.";
RL Nature 387:78-81(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 IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=14690591; DOI=10.1016/s1097-2765(03)00476-3;
RA Hazbun T.R., Malmstroem L., Anderson S., Graczyk B.J., Fox B., Riffle M.,
RA Sundin B.A., Aranda J.D., McDonald W.H., Chiu C.-H., Snydsman B.E.,
RA Bradley P., Muller E.G.D., Fields S., Baker D., Yates J.R. III, Davis T.N.;
RT "Assigning function to yeast proteins by integration of technologies.";
RL Mol. Cell 12:1353-1365(2003).
RN [6]
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 [7]
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 [8]
RP FUNCTION, SUBUNIT, AND SUBCELLULAR LOCATION.
RX PubMed=15738391; DOI=10.1073/pnas.0500537102;
RA Zhao X., Blobel G.;
RT "A SUMO ligase is part of a nuclear multiprotein complex that affects DNA
RT repair and chromosomal organization.";
RL Proc. Natl. Acad. Sci. U.S.A. 102:4777-4782(2005).
CC -!- FUNCTION: Acts as an E3 ligase mediating SUMO/Smt3 attachment to SMC5
CC and YKU70. Acts in a DNA repair pathway for removal of UV-induced DNA
CC damage that is distinct from classical nucleotide excision repair and
CC in repair of ionizing radiation damage. Functions in homologous
CC recombination repair of DNA double strand breaks and in recovery of
CC stalled replication forks. {ECO:0000269|PubMed:15738391}.
CC -!- PATHWAY: Protein modification; protein sumoylation.
CC -!- SUBUNIT: Component of the Smc5-Smc6 complex which consists of KRE29,
CC NSE1, NSE2/MMS21, NSE3, NSE4, NSE5, SMC5 and SMC6.
CC {ECO:0000269|PubMed:15738391}.
CC -!- INTERACTION:
CC P38632; P53067: KAP114; NbExp=2; IntAct=EBI-11017, EBI-9174;
CC P38632; Q08204: SMC5; NbExp=5; IntAct=EBI-11017, EBI-34125;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:15738391}. Cytoplasm
CC {ECO:0000269|PubMed:14562095}.
CC -!- MISCELLANEOUS: Present with 2800 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the NSE2 family. {ECO:0000305}.
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DR EMBL; U12311; AAA20471.1; -; Genomic_DNA.
DR EMBL; U18530; AAB64496.1; -; Genomic_DNA.
DR EMBL; AY558441; AAS56767.1; -; Genomic_DNA.
DR EMBL; BK006939; DAA07634.1; -; Genomic_DNA.
DR PIR; S50440; S50440.
DR RefSeq; NP_010896.3; NM_001178834.3.
DR PDB; 3HTK; X-ray; 2.31 A; C=1-267.
DR PDB; 7P47; X-ray; 3.31 A; A=27-267.
DR PDBsum; 3HTK; -.
DR PDBsum; 7P47; -.
DR AlphaFoldDB; P38632; -.
DR SMR; P38632; -.
DR BioGRID; 36711; 386.
DR ComplexPortal; CPX-1364; SMC5-SMC6 SUMO ligase complex.
DR DIP; DIP-4100N; -.
DR IntAct; P38632; 4.
DR MINT; P38632; -.
DR STRING; 4932.YEL019C; -.
DR iPTMnet; P38632; -.
DR MaxQB; P38632; -.
DR PaxDb; P38632; -.
DR PRIDE; P38632; -.
DR EnsemblFungi; YEL019C_mRNA; YEL019C; YEL019C.
DR GeneID; 856695; -.
DR KEGG; sce:YEL019C; -.
DR SGD; S000000745; MMS21.
DR VEuPathDB; FungiDB:YEL019C; -.
DR eggNOG; KOG2979; Eukaryota.
DR HOGENOM; CLU_088986_0_0_1; -.
DR InParanoid; P38632; -.
DR OMA; IELICPI; -.
DR BioCyc; YEAST:G3O-30144-MON; -.
DR Reactome; R-SCE-3108214; SUMOylation of DNA damage response and repair proteins.
DR UniPathway; UPA00886; -.
DR EvolutionaryTrace; P38632; -.
DR PRO; PR:P38632; -.
DR Proteomes; UP000002311; Chromosome V.
DR RNAct; P38632; protein.
DR GO; GO:0000781; C:chromosome, telomeric region; IC:ComplexPortal.
DR GO; GO:0005737; C:cytoplasm; HDA:SGD.
DR GO; GO:0005635; C:nuclear envelope; IDA:SGD.
DR GO; GO:0005634; C:nucleus; HDA:SGD.
DR GO; GO:0030915; C:Smc5-Smc6 complex; IDA:SGD.
DR GO; GO:0030291; F:protein serine/threonine kinase inhibitor activity; IMP:SGD.
DR GO; GO:0061665; F:SUMO ligase activity; IBA:GO_Central.
DR GO; GO:0019789; F:SUMO transferase activity; IDA:SGD.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:1990683; P:DNA double-strand break attachment to nuclear envelope; IMP:SGD.
DR GO; GO:0006281; P:DNA repair; IMP:SGD.
DR GO; GO:0000724; P:double-strand break repair via homologous recombination; IBA:GO_Central.
DR GO; GO:0016925; P:protein sumoylation; IBA:GO_Central.
DR GO; GO:0032204; P:regulation of telomere maintenance; IC:ComplexPortal.
DR CDD; cd16651; SPL-RING_NSE2; 1.
DR Gene3D; 3.30.40.10; -; 1.
DR InterPro; IPR026846; Nse2(Mms21).
DR InterPro; IPR004181; Znf_MIZ.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR PANTHER; PTHR21330; PTHR21330; 1.
DR Pfam; PF11789; zf-Nse; 1.
DR PROSITE; PS51044; ZF_SP_RING; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cytoplasm; DNA damage; DNA recombination; DNA repair;
KW Metal-binding; Nucleus; Reference proteome; Transferase;
KW Ubl conjugation pathway; Zinc; Zinc-finger.
FT CHAIN 1..267
FT /note="E3 SUMO-protein ligase MMS21"
FT /id="PRO_0000218991"
FT ZN_FING 169..256
FT /note="SP-RING-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00452"
FT BINDING 200
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00452"
FT BINDING 202
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00452"
FT BINDING 221
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00452"
FT BINDING 226
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00452"
FT CONFLICT 124
FT /note="E -> D (in Ref. 1; AAA20471)"
FT /evidence="ECO:0000305"
FT HELIX 16..18
FT /evidence="ECO:0007829|PDB:3HTK"
FT HELIX 19..24
FT /evidence="ECO:0007829|PDB:3HTK"
FT HELIX 31..51
FT /evidence="ECO:0007829|PDB:3HTK"
FT HELIX 60..99
FT /evidence="ECO:0007829|PDB:3HTK"
FT HELIX 108..114
FT /evidence="ECO:0007829|PDB:3HTK"
FT STRAND 115..117
FT /evidence="ECO:0007829|PDB:3HTK"
FT HELIX 122..127
FT /evidence="ECO:0007829|PDB:3HTK"
FT HELIX 142..155
FT /evidence="ECO:0007829|PDB:3HTK"
FT STRAND 177..179
FT /evidence="ECO:0007829|PDB:3HTK"
FT TURN 185..187
FT /evidence="ECO:0007829|PDB:3HTK"
FT STRAND 188..190
FT /evidence="ECO:0007829|PDB:3HTK"
FT STRAND 192..200
FT /evidence="ECO:0007829|PDB:3HTK"
FT STRAND 203..205
FT /evidence="ECO:0007829|PDB:3HTK"
FT HELIX 206..212
FT /evidence="ECO:0007829|PDB:3HTK"
FT STRAND 217..220
FT /evidence="ECO:0007829|PDB:7P47"
FT HELIX 223..225
FT /evidence="ECO:0007829|PDB:3HTK"
FT STRAND 229..231
FT /evidence="ECO:0007829|PDB:7P47"
FT HELIX 232..234
FT /evidence="ECO:0007829|PDB:3HTK"
FT STRAND 235..237
FT /evidence="ECO:0007829|PDB:3HTK"
FT HELIX 239..256
FT /evidence="ECO:0007829|PDB:3HTK"
SQ SEQUENCE 267 AA; 30354 MW; F200378289B1CEE4 CRC64;
MALNDNPIPK SVPLHPKSGK YFHNLHARDL SNIYQQCYKQ IDETINQLVD STSPSTIGIE
EQVADITSTY KLLSTYESES NSFDEHIKDL KKNFKQSSDA CPQIDLSTWD KYRTGELTAP
KLSELYLNMP TPEPATMVNN TDTLKILKVL PYIWNDPTCV IPDLQNPADE DDLQIEGGKI
ELTCPITCKP YEAPLISRKC NHVFDRDGIQ NYLQGYTTRD CPQAACSQVV SMRDFVRDPI
MELRCKIAKM KESQEQDKRS SQAIDVL
