CDC3_YEAST
ID CDC3_YEAST Reviewed; 520 AA.
AC P32457; D6VYV8; Q06161;
DT 01-OCT-1993, integrated into UniProtKB/Swiss-Prot.
DT 21-SEP-2011, sequence version 3.
DT 03-AUG-2022, entry version 201.
DE RecName: Full=Cell division control protein 3;
GN Name=CDC3; OrderedLocusNames=YLR314C; ORFNames=L8543.7;
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=ATCC 204510 / AB320;
RX PubMed=8791410; DOI=10.1016/s0955-0674(96)80054-8;
RA Longtine M.S., DeMarini D.J., Valencik M.L., Al-Awar O.S., Fares H.,
RA De Virgilio C., Pringle J.R.;
RT "The septins: roles in cytokinesis and other processes.";
RL Curr. Opin. Cell Biol. 8:106-119(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169871;
RA Johnston M., Hillier L.W., Riles L., Albermann K., Andre B., Ansorge W.,
RA Benes V., Brueckner M., Delius H., Dubois E., Duesterhoeft A.,
RA Entian K.-D., Floeth M., Goffeau A., Hebling U., Heumann K.,
RA Heuss-Neitzel D., Hilbert H., Hilger F., Kleine K., Koetter P., Louis E.J.,
RA Messenguy F., Mewes H.-W., Miosga T., Moestl D., Mueller-Auer S.,
RA Nentwich U., Obermaier B., Piravandi E., Pohl T.M., Portetelle D.,
RA Purnelle B., Rechmann S., Rieger M., Rinke M., Rose M., Scharfe M.,
RA Scherens B., Scholler P., Schwager C., Schwarz S., Underwood A.P.,
RA Urrestarazu L.A., Vandenbol M., Verhasselt P., Vierendeels F., Voet M.,
RA Volckaert G., Voss H., Wambutt R., Wedler E., Wedler H., Zimmermann F.K.,
RA Zollner A., Hani J., Hoheisel J.D.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XII.";
RL Nature 387:87-90(1997).
RN [3]
RP GENOME REANNOTATION, AND SEQUENCE REVISION TO 431.
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 IDENTIFICATION IN THE SEPTIN COMPLEX.
RX PubMed=9813094; DOI=10.1083/jcb.143.3.737;
RA Frazier J.A., Wong M.L., Longtine M.S., Pringle J.R., Mann M.,
RA Mitchison T.J., Field C.;
RT "Polymerization of purified yeast septins: evidence that organized filament
RT arrays may not be required for septin function.";
RL J. Cell Biol. 143:737-749(1998).
RN [5]
RP SUMOYLATION AT LYS-4; LYS-11; LYS-30; LYS-63 AND LYS-287, MUTAGENESIS OF
RP LYS-4; LYS-11; LYS-287; LYS-415 AND LYS-443, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RX PubMed=10579719; DOI=10.1083/jcb.147.5.981;
RA Johnson E.S., Blobel G.;
RT "Cell cycle-regulated attachment of the ubiquitin-related protein SUMO to
RT the yeast septins.";
RL J. Cell Biol. 147:981-994(1999).
RN [6]
RP SUMOYLATION, AND INTERACTION WITH SIZ1.
RX PubMed=11587849; DOI=10.1016/s0378-1119(01)00662-x;
RA Takahashi Y., Toh-e A., Kikuchi Y.;
RT "A novel factor required for the SUMO1/Smt3 conjugation of yeast septins.";
RL Gene 275:223-231(2001).
RN [7]
RP PHOSPHORYLATION BY CDC28.
RX PubMed=12429908;
RA Tang C.S., Reed S.I.;
RT "Phosphorylation of the septin cdc3 in G1 by the cdc28 kinase is essential
RT for efficient septin ring disassembly.";
RL Cell Cycle 1:42-49(2002).
RN [8]
RP IDENTIFICATION IN THE GIN4 COMPLEX, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RX PubMed=12058072; DOI=10.1091/mbc.01-10-0500;
RA Mortensen E.M., McDonald H., Yates J. III, Kellogg D.R.;
RT "Cell cycle-dependent assembly of a Gin4-septin complex.";
RL Mol. Biol. Cell 13:2091-2105(2002).
RN [9]
RP ASSOCIATION WITH PHOSPHOINOSIDES LIPIDS, AND INTERACTION WITH CDC11.
RX PubMed=12665577; DOI=10.1128/mcb.23.8.2762-2777.2003;
RA Casamayor A., Snyder M.;
RT "Molecular dissection of a yeast septin: distinct domains are required for
RT septin interaction, localization, and function.";
RL Mol. Cell. Biol. 23:2762-2777(2003).
RN [10]
RP SELF-ASSOCIATION, AND ASSEMBLY OF THE SEPTIN FILAMENTS.
RX PubMed=15282341; DOI=10.1091/mbc.e04-04-0330;
RA Versele M., Gullbrand B., Shulewitz M.J., Cid V.J., Bahmanyar S.,
RA Chen R.E., Barth P., Alber T., Thorner J.;
RT "Protein-protein interactions governing septin heteropentamer assembly and
RT septin filament organization in Saccharomyces cerevisiae.";
RL Mol. Biol. Cell 15:4568-4583(2004).
RN [11]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-63, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RX PubMed=15166219; DOI=10.1074/jbc.m404173200;
RA Zhou W., Ryan J.J., Zhou H.;
RT "Global analyses of sumoylated proteins in Saccharomyces cerevisiae.
RT Induction of protein sumoylation by cellular stresses.";
RL J. Biol. Chem. 279:32262-32268(2004).
RN [12]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-63, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RC STRAIN=EJY251-11b;
RX PubMed=15542864; DOI=10.1074/mcp.m400154-mcp200;
RA Denison C., Rudner A.D., Gerber S.A., Bakalarski C.E., Moazed D.,
RA Gygi S.P.;
RT "A proteomic strategy for gaining insights into protein sumoylation in
RT yeast.";
RL Mol. Cell. Proteomics 4:246-254(2005).
RN [13]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, PHOSPHORYLATION [LARGE SCALE
RP ANALYSIS] AT SER-2, CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE
RP ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=YAL6B;
RX PubMed=15665377; DOI=10.1074/mcp.m400219-mcp200;
RA Gruhler A., Olsen J.V., Mohammed S., Mortensen P., Faergeman N.J., Mann M.,
RA Jensen O.N.;
RT "Quantitative phosphoproteomics applied to the yeast pheromone signaling
RT pathway.";
RL Mol. Cell. Proteomics 4:310-327(2005).
RN [14]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=ADR376;
RX PubMed=17330950; DOI=10.1021/pr060559j;
RA Li X., Gerber S.A., Rudner A.D., Beausoleil S.A., Haas W., Villen J.,
RA Elias J.E., Gygi S.P.;
RT "Large-scale phosphorylation analysis of alpha-factor-arrested
RT Saccharomyces cerevisiae.";
RL J. Proteome Res. 6:1190-1197(2007).
RN [15]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-9, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=17287358; DOI=10.1073/pnas.0607084104;
RA Chi A., Huttenhower C., Geer L.Y., Coon J.J., Syka J.E.P., Bai D.L.,
RA Shabanowitz J., Burke D.J., Troyanskaya O.G., Hunt D.F.;
RT "Analysis of phosphorylation sites on proteins from Saccharomyces
RT cerevisiae by electron transfer dissociation (ETD) mass spectrometry.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:2193-2198(2007).
RN [16]
RP INTERACTION WITH SYP1.
RX PubMed=18791237; DOI=10.1534/genetics.108.091900;
RA Qiu W., Neo S.P., Yu X., Cai M.;
RT "A novel septin-associated protein, Syp1p, is required for normal cell
RT cycle-dependent septin cytoskeleton dynamics in yeast.";
RL Genetics 180:1445-1457(2008).
RN [17]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-9; SER-175 AND THR-468, AND
RP IDENTIFICATION BY 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).
RN [18]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-47; SER-60; SER-77; SER-175
RP AND SER-509, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP 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 [19]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-terminal
RT acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
CC -!- FUNCTION: Septins are GTPases involved in cytokinesis that assemble
CC early in the cell cycle as a patch at the incipient bud site and form a
CC ring approximate 15 minutes before bud emergence, which transforms into
CC an hour-glass shaped collar of cortical filaments that spans both sides
CC of the mother-bud neck. This collar persists until just before
CC cytokinesis, when it splits into two rings that occupy opposite sides
CC of the neck. The septins at the bud neck serve as a structural scaffold
CC that recruits different components involved in diverse processes at
CC specific stages during the cell cycle. Many proteins bind
CC asymmetrically to the septin collar. The septin assembly is regulated
CC by protein kinases GIN4 and/or CLA4. May act by recruiting MYO1 and
CC HOF1, a protein involved in septation, to the site of cleavage. Septins
CC are also involved in cell morphogenesis, bud site selection, chitin
CC deposition, cell cycle regulation, cell compartmentalization and spore
CC wall formation.
CC -!- SUBUNIT: Component of the septin complex which consists of CDC3, CDC10,
CC CDC11, CDC12 and probably SHS1 and rearranges to a cortical collar of
CC highly ordered filaments at the mother-bud-neck. A complex formed by
CC CDC3, CDC10, CDC11 and CDC12 is capable of forming long filaments in
CC vitro and the components seem to be present in a 2:2:2:2 arrangement in
CC vivo. The filaments are proposed to be formed by the end-to-end
CC polymerization of CDC3-CDC12-CDC11 complexes with CDC10 serving as a
CC bridge to bundle the polymers into paired filaments. Component of the
CC GIN4 complex composed of at least BNI5, CDC3, CDC10, CDC11, CDC12,
CC GIN4, NAP1 and SHS1. Self-associates. Interacts with SIZ1 and SYP1.
CC {ECO:0000269|PubMed:11587849, ECO:0000269|PubMed:12058072,
CC ECO:0000269|PubMed:12665577, ECO:0000269|PubMed:18791237,
CC ECO:0000269|PubMed:9813094}.
CC -!- INTERACTION:
CC P32457; P25342: CDC10; NbExp=11; IntAct=EBI-4429, EBI-4174;
CC P32457; P38785: GIC1; NbExp=2; IntAct=EBI-4429, EBI-7575;
CC P32457; Q06648: GIC2; NbExp=3; IntAct=EBI-4429, EBI-7585;
CC -!- SUBCELLULAR LOCATION: Membrane; Peripheral membrane protein. Bud neck.
CC Note=Present at the bud neck during cell division. Probably interacts
CC with phosphoinosides such as phosphatidylinositol 4-phosphate or
CC phosphatidylinositol 5-phosphate.
CC -!- PTM: Phosphorylated by CDC28. Phosphorylation at the end of G1 may
CC facilitate initiation of a new cell cycle by promoting disassembly of
CC the obsolete septin ring from the previous cell cycle.
CC {ECO:0000269|PubMed:12429908}.
CC -!- PTM: Sumoylated during mitosis on the mother cell side of the bud neck
CC by UBC9/SIZ1. Sumoylation probably plays a central role in regulating
CC septin ring disassembly during the cell cycle.
CC {ECO:0000269|PubMed:10579719, ECO:0000269|PubMed:11587849,
CC ECO:0000269|PubMed:15166219, ECO:0000269|PubMed:15542864}.
CC -!- SIMILARITY: Belongs to the TRAFAC class TrmE-Era-EngA-EngB-Septin-like
CC GTPase superfamily. Septin GTPase family. {ECO:0000255|PROSITE-
CC ProRule:PRU01056}.
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DR EMBL; L16548; AAB50034.1; -; Genomic_DNA.
DR EMBL; U20618; AAB64515.1; -; Genomic_DNA.
DR EMBL; BK006945; DAA09624.2; -; Genomic_DNA.
DR PIR; S53393; S53393.
DR RefSeq; NP_013418.2; NM_001182203.2.
DR AlphaFoldDB; P32457; -.
DR SMR; P32457; -.
DR BioGRID; 31579; 787.
DR ComplexPortal; CPX-1675; Septin complex.
DR ComplexPortal; CPX-1712; Gin4 serine/threonine kinase complex.
DR DIP; DIP-3010N; -.
DR ELM; P32457; -.
DR IntAct; P32457; 36.
DR MINT; P32457; -.
DR STRING; 4932.YLR314C; -.
DR iPTMnet; P32457; -.
DR MaxQB; P32457; -.
DR PaxDb; P32457; -.
DR PRIDE; P32457; -.
DR EnsemblFungi; YLR314C_mRNA; YLR314C; YLR314C.
DR GeneID; 851024; -.
DR KEGG; sce:YLR314C; -.
DR SGD; S000004306; CDC3.
DR VEuPathDB; FungiDB:YLR314C; -.
DR eggNOG; KOG2655; Eukaryota.
DR GeneTree; ENSGT00940000154222; -.
DR HOGENOM; CLU_017718_8_0_1; -.
DR InParanoid; P32457; -.
DR OMA; HTNNFLY; -.
DR BioCyc; YEAST:G3O-32400-MON; -.
DR Reactome; R-SCE-111457; Release of apoptotic factors from the mitochondria.
DR Reactome; R-SCE-5687128; MAPK6/MAPK4 signaling.
DR PRO; PR:P32457; -.
DR Proteomes; UP000002311; Chromosome XII.
DR RNAct; P32457; protein.
DR GO; GO:0005619; C:ascospore wall; IDA:SGD.
DR GO; GO:0032153; C:cell division site; IBA:GO_Central.
DR GO; GO:0005935; C:cellular bud neck; HDA:SGD.
DR GO; GO:0000144; C:cellular bud neck septin ring; IDA:SGD.
DR GO; GO:1990317; C:Gin4 complex; IPI:ComplexPortal.
DR GO; GO:0001400; C:mating projection base; IDA:SGD.
DR GO; GO:0015630; C:microtubule cytoskeleton; IBA:GO_Central.
DR GO; GO:0005628; C:prospore membrane; IDA:SGD.
DR GO; GO:0031105; C:septin complex; IDA:SGD.
DR GO; GO:0032160; C:septin filament array; IDA:SGD.
DR GO; GO:0005940; C:septin ring; IBA:GO_Central.
DR GO; GO:0005525; F:GTP binding; IDA:SGD.
DR GO; GO:0003924; F:GTPase activity; IBA:GO_Central.
DR GO; GO:0060090; F:molecular adaptor activity; IBA:GO_Central.
DR GO; GO:0070273; F:phosphatidylinositol-4-phosphate binding; IDA:SGD.
DR GO; GO:0010314; F:phosphatidylinositol-5-phosphate binding; IDA:SGD.
DR GO; GO:0005200; F:structural constituent of cytoskeleton; IDA:SGD.
DR GO; GO:0032186; P:cellular bud neck septin ring organization; IC:ComplexPortal.
DR GO; GO:0061640; P:cytoskeleton-dependent cytokinesis; IBA:GO_Central.
DR GO; GO:0030011; P:maintenance of cell polarity; IC:SGD.
DR GO; GO:0000281; P:mitotic cytokinesis; IDA:SGD.
DR GO; GO:0071902; P:positive regulation of protein serine/threonine kinase activity; IDA:ComplexPortal.
DR GO; GO:0008104; P:protein localization; IBA:GO_Central.
DR GO; GO:0000921; P:septin ring assembly; IMP:SGD.
DR GO; GO:0031107; P:septin ring disassembly; IMP:SGD.
DR GO; GO:0000920; P:septum digestion after cytokinesis; IC:ComplexPortal.
DR CDD; cd01850; CDC_Septin; 1.
DR Gene3D; 3.40.50.300; -; 1.
DR InterPro; IPR030379; G_SEPTIN_dom.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR016491; Septin.
DR Pfam; PF00735; Septin; 1.
DR PIRSF; PIRSF006698; Septin; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR PROSITE; PS51719; G_SEPTIN; 1.
PE 1: Evidence at protein level;
KW Acetylation; Cell cycle; Cell division; Coiled coil; GTP-binding;
KW Isopeptide bond; Membrane; Nucleotide-binding; Phosphoprotein;
KW Reference proteome; Ubl conjugation.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0007744|PubMed:15665377,
FT ECO:0007744|PubMed:22814378"
FT CHAIN 2..520
FT /note="Cell division control protein 3"
FT /id="PRO_0000173496"
FT DOMAIN 116..411
FT /note="Septin-type G"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01056"
FT REGION 1..83
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 126..133
FT /note="G1 motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01056"
FT REGION 156..181
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 204..207
FT /note="G3 motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01056"
FT REGION 286..289
FT /note="G4 motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01056"
FT REGION 496..520
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 427..508
FT /evidence="ECO:0000255"
FT COMPBIAS 1..37
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 126..133
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 207
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 287..295
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 344
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 360
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT SITE 415
FT /note="Not sumoylated"
FT SITE 443
FT /note="Not sumoylated"
FT MOD_RES 2
FT /note="N-acetylserine"
FT /evidence="ECO:0007744|PubMed:15665377,
FT ECO:0007744|PubMed:22814378"
FT MOD_RES 2
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:15665377"
FT MOD_RES 9
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17287358,
FT ECO:0007744|PubMed:18407956"
FT MOD_RES 47
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 60
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 77
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 175
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18407956,
FT ECO:0007744|PubMed:19779198"
FT MOD_RES 468
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:18407956"
FT MOD_RES 509
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT CROSSLNK 4
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO)"
FT CROSSLNK 11
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO)"
FT CROSSLNK 30
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO)"
FT CROSSLNK 63
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO)"
FT /evidence="ECO:0000269|PubMed:15166219,
FT ECO:0000269|PubMed:15542864"
FT CROSSLNK 287
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO)"
FT MUTAGEN 4
FT /note="K->R: Abolishes sumoylation."
FT /evidence="ECO:0000269|PubMed:10579719"
FT MUTAGEN 11
FT /note="K->R: Abolishes sumoylation."
FT /evidence="ECO:0000269|PubMed:10579719"
FT MUTAGEN 287
FT /note="K->R: Abolishes sumoylation."
FT /evidence="ECO:0000269|PubMed:10579719"
FT MUTAGEN 415
FT /note="K->R: No effect on sumoylation."
FT /evidence="ECO:0000269|PubMed:10579719"
FT MUTAGEN 443
FT /note="K->R: No effect on sumoylation."
FT /evidence="ECO:0000269|PubMed:10579719"
FT CONFLICT 431
FT /note="Q -> L (in Ref. 2; AAB64515)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 520 AA; 60054 MW; DCCD4C8C16AA5E25 CRC64;
MSLKEEQVSI KQDPEQEERQ HDQFNDVQIK QESQDHDGVD SQYTNGTQND DSERFEAAES
DVKVEPGLGM GITSSQSEKG QVLPDQPEIK FIRRQINGYV GFANLPKQWH RRSIKNGFSF
NLLCVGPDGI GKTTLMKTLF NNDDIEANLV KDYEEELAND QEEEEGQGEG HENQSQEQRH
KVKIKSYESV IEENGVKLNL NVIDTEGFGD FLNNDQKSWD PIIKEIDSRF DQYLDAENKI
NRHSINDKRI HACLYFIEPT GHYLKPLDLK FMQSVYEKCN LIPVIAKSDI LTDEEILSFK
KTIMNQLIQS NIELFKPPIY SNDDAENSHL SERLFSSLPY AVIGSNDIVE NYSGNQVRGR
SYPWGVIEVD NDNHSDFNLL KNLLIKQFME ELKERTSKIL YENYRSSKLA KLGIKQDNSV
FKEFDPISKQ QEEKTLHEAK LAKLEIEMKT VFQQKVSEKE KKLQKSETEL FARHKEMKEK
LTKQLKALED KKKQLELSIN SASPNVNHSP VPTKKKGFLR
