CDC11_YEAST
ID CDC11_YEAST Reviewed; 415 AA.
AC P32458; D6VWP6;
DT 01-OCT-1993, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1993, sequence version 1.
DT 03-AUG-2022, entry version 198.
DE RecName: Full=Cell division control protein 11;
GN Name=CDC11; Synonyms=PSL9; OrderedLocusNames=YJR076C; ORFNames=J1833;
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=DBY939;
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 [GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=8840504;
RX DOI=10.1002/(sici)1097-0061(199607)12:9<869::aid-yea964>3.0.co;2-1;
RA Huang M.-E., Manus V., Chuat J.-C., Galibert F.;
RT "Analysis of a 62 kb DNA sequence of chromosome X reveals 36 open reading
RT frames and a gene cluster with a counterpart on chromosome XI.";
RL Yeast 12:869-875(1996).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=8641269; DOI=10.1002/j.1460-2075.1996.tb00557.x;
RA Galibert F., Alexandraki D., Baur A., Boles E., Chalwatzis N., Chuat J.-C.,
RA Coster F., Cziepluch C., de Haan M., Domdey H., Durand P., Entian K.-D.,
RA Gatius M., Goffeau A., Grivell L.A., Hennemann A., Herbert C.J.,
RA Heumann K., Hilger F., Hollenberg C.P., Huang M.-E., Jacq C.,
RA Jauniaux J.-C., Katsoulou C., Kirchrath L., Kleine K., Kordes E.,
RA Koetter P., Liebl S., Louis E.J., Manus V., Mewes H.-W., Miosga T.,
RA Obermaier B., Perea J., Pohl T.M., Portetelle D., Pujol A., Purnelle B.,
RA Ramezani Rad M., Rasmussen S.W., Rose M., Rossau R.,
RA Schaaff-Gerstenschlaeger I., Smits P.H.M., Scarcez T., Soriano N.,
RA To Van D., Tzermia M., Van Broekhoven A., Vandenbol M., Wedler H.,
RA von Wettstein D., Wambutt R., Zagulski M., Zollner A., Karpfinger-Hartl L.;
RT "Complete nucleotide sequence of Saccharomyces cerevisiae chromosome X.";
RL EMBO J. 15:2031-2049(1996).
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 INTERACTION WITH SPR28.
RX PubMed=8885406; DOI=10.1099/13500872-142-10-2897;
RA de Virgilio C., DeMarini D.J., Pringle J.R.;
RT "SPR28, a sixth member of the septin gene family in Saccharomyces
RT cerevisiae that is expressed specifically in sporulating cells.";
RL Microbiology 142:2897-2905(1996).
RN [6]
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 [7]
RP SUMOYLATION AT LYS-412, AND MUTAGENESIS OF LYS-412.
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 [8]
RP INTERACTION WITH KCC4.
RX PubMed=11165249; DOI=10.1016/s0014-5793(01)02104-4;
RA Okuzaki D., Nojima H.;
RT "Kcc4 associates with septin proteins of Saccharomyces cerevisiae.";
RL FEBS Lett. 489:197-201(2001).
RN [9]
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 [10]
RP FUNCTION, DOMAIN, INTERACTION WITH CDC3 AND BEM4, AND MUTAGENESIS OF
RP 12-ARG--HIS-16; GLY-29; GLY-32; GLY-34; ARG-35; ASN-40 AND GLY-230.
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 [11]
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 [12]
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 [13]
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 [14]
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 [15]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-305 AND THR-327, AND
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 [16]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-327, AND IDENTIFICATION BY
RP MASS 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 [17]
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 [18]
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 [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. {ECO:0000269|PubMed:12665577}.
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 BEM4, KCC4, SPR28
CC and SYP1. {ECO:0000269|PubMed:11165249, ECO:0000269|PubMed:12058072,
CC ECO:0000269|PubMed:12665577, ECO:0000269|PubMed:18791237,
CC ECO:0000269|PubMed:8885406, ECO:0000269|PubMed:9813094}.
CC -!- INTERACTION:
CC P32458; P32458: CDC11; NbExp=2; IntAct=EBI-4178, EBI-4178;
CC P32458; P32468: CDC12; NbExp=11; IntAct=EBI-4178, EBI-4182;
CC P32458; P38785: GIC1; NbExp=2; IntAct=EBI-4178, EBI-7575;
CC P32458; Q06648: GIC2; NbExp=2; IntAct=EBI-4178, EBI-7585;
CC P32458; Q12263: GIN4; NbExp=7; IntAct=EBI-4178, EBI-7595;
CC P32458; Q07657: SHS1; NbExp=5; IntAct=EBI-4178, EBI-22083;
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000269|PubMed:14562095}. Bud neck
CC {ECO:0000269|PubMed:14562095}. Note=Present at the bud neck during cell
CC division. Interacts with phosphatidylinositol 4-phosphate and
CC phosphatidylinositol 5-phosphate (PI(4)P and PI(5)P).
CC -!- DOMAIN: The coiled coil domain is required for the interaction with
CC CDC3 and BEM4, but not for interaction with CDC12 or with itself.
CC {ECO:0000269|PubMed:12665577}.
CC -!- DOMAIN: The basic motif is essential for the association with PI(4)P
CC and PI(5)P. {ECO:0000269|PubMed:12665577}.
CC -!- PTM: Sumoylated during mitosis on the mother cell side of the bud neck.
CC Sumoylation probably plays a central role in regulating septin ring
CC disassembly during the cell cycle. {ECO:0000269|PubMed:10579719}.
CC -!- MISCELLANEOUS: Present with 9280 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
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; L16550; AAB50035.1; -; Genomic_DNA.
DR EMBL; L47993; AAB39301.1; -; Genomic_DNA.
DR EMBL; Z49576; CAA89604.1; -; Genomic_DNA.
DR EMBL; BK006943; DAA08862.1; -; Genomic_DNA.
DR PIR; S40911; S40911.
DR RefSeq; NP_012610.1; NM_001181734.1.
DR PDB; 5AR1; X-ray; 2.85 A; A=20-298.
DR PDBsum; 5AR1; -.
DR AlphaFoldDB; P32458; -.
DR SMR; P32458; -.
DR BioGRID; 33832; 1246.
DR ComplexPortal; CPX-1675; Septin complex.
DR ComplexPortal; CPX-1712; Gin4 serine/threonine kinase complex.
DR DIP; DIP-1656N; -.
DR ELM; P32458; -.
DR IntAct; P32458; 44.
DR MINT; P32458; -.
DR STRING; 4932.YJR076C; -.
DR iPTMnet; P32458; -.
DR MaxQB; P32458; -.
DR PaxDb; P32458; -.
DR PRIDE; P32458; -.
DR EnsemblFungi; YJR076C_mRNA; YJR076C; YJR076C.
DR GeneID; 853539; -.
DR KEGG; sce:YJR076C; -.
DR SGD; S000003837; CDC11.
DR VEuPathDB; FungiDB:YJR076C; -.
DR eggNOG; KOG2655; Eukaryota.
DR HOGENOM; CLU_017718_7_4_1; -.
DR InParanoid; P32458; -.
DR OMA; VNCEDSW; -.
DR BioCyc; YEAST:G3O-31706-MON; -.
DR Reactome; R-SCE-111457; Release of apoptotic factors from the mitochondria.
DR Reactome; R-SCE-5687128; MAPK6/MAPK4 signaling.
DR PRO; PR:P32458; -.
DR Proteomes; UP000002311; Chromosome X.
DR RNAct; P32458; 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:0005881; C:cytoplasmic microtubule; IDA:SGD.
DR GO; GO:1990317; C:Gin4 complex; IPI:ComplexPortal.
DR GO; GO:0001400; C:mating projection base; IDA:SGD.
DR GO; GO:0043332; C:mating projection tip; HDA:SGD.
DR GO; GO:0072687; C:meiotic spindle; 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:0005876; C:spindle microtubule; IDA:SGD.
DR GO; GO:0005525; F:GTP binding; IDA:SGD.
DR GO; GO:0003924; F:GTPase activity; IBA:GO_Central.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
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:0000915; P:actomyosin contractile ring assembly; IBA:GO_Central.
DR GO; GO:0032186; P:cellular bud neck septin ring organization; IBA:GO_Central.
DR GO; GO:0061640; P:cytoskeleton-dependent cytokinesis; IBA:GO_Central.
DR GO; GO:0000917; P:division septum assembly; IBA:GO_Central.
DR GO; GO:0030011; P:maintenance of cell polarity; IC:SGD.
DR GO; GO:0000281; P:mitotic cytokinesis; IMP:SGD.
DR GO; GO:0045860; P:positive regulation of protein kinase activity; 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:0097271; P:protein localization to bud neck; IGI:SGD.
DR GO; GO:0000921; P:septin ring assembly; IC:ComplexPortal.
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 3D-structure; Acetylation; Cell cycle; Cell division; Coiled coil;
KW GTP-binding; 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..415
FT /note="Cell division control protein 11"
FT /id="PRO_0000173499"
FT DOMAIN 19..298
FT /note="Septin-type G"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01056"
FT REGION 29..36
FT /note="G1 motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01056"
FT REGION 89..92
FT /note="G3 motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01056"
FT REGION 171..174
FT /note="G4 motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01056"
FT REGION 307..360
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 354..414
FT /evidence="ECO:0000255"
FT MOTIF 12..19
FT /note="Basic motif"
FT COMPBIAS 307..359
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 29..36
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 92
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 172..180
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 230
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 247
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
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 305
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17330950"
FT MOD_RES 327
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:17287358,
FT ECO:0007744|PubMed:17330950"
FT CROSSLNK 412
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO)"
FT MUTAGEN 12..16
FT /note="RKRKH->QQEQQ: Loss of function; abolishes
FT association with PI(4)P and PI(5)P."
FT /evidence="ECO:0000269|PubMed:12665577"
FT MUTAGEN 12..16
FT /note="RKRKH->QQQQQ: Loss of function; strongly decreases
FT association with PI(4)P and PI(5)P."
FT /evidence="ECO:0000269|PubMed:12665577"
FT MUTAGEN 29
FT /note="G->A: Abolishes GTP-binding; no strong effect in
FT vivo."
FT /evidence="ECO:0000269|PubMed:12665577"
FT MUTAGEN 32
FT /note="G->A: Abolishes GTP-binding; no strong effect in
FT vivo."
FT /evidence="ECO:0000269|PubMed:12665577"
FT MUTAGEN 34
FT /note="G->A: Abolishes GTP-binding; no strong effect in
FT vivo."
FT /evidence="ECO:0000269|PubMed:12665577"
FT MUTAGEN 35
FT /note="R->A: Abolishes GTP-binding; no strong effect in
FT vivo."
FT /evidence="ECO:0000269|PubMed:12665577"
FT MUTAGEN 40
FT /note="N->E: Temperature-sensitive; no effect at 23 degrees
FT Celsius but loss of function at 37 degrees Celsius;
FT abolishes interaction with itself."
FT /evidence="ECO:0000269|PubMed:12665577"
FT MUTAGEN 230
FT /note="G->E: Temperature-sensitive; no effect at 23 degrees
FT Celsius but loss of function at 37 degrees Celsius."
FT /evidence="ECO:0000269|PubMed:12665577"
FT MUTAGEN 412
FT /note="K->R: Abolishes sumoylation in vitro."
FT /evidence="ECO:0000269|PubMed:10579719"
FT STRAND 23..29
FT /evidence="ECO:0007829|PDB:5AR1"
FT STRAND 31..33
FT /evidence="ECO:0007829|PDB:5AR1"
FT TURN 36..40
FT /evidence="ECO:0007829|PDB:5AR1"
FT STRAND 69..73
FT /evidence="ECO:0007829|PDB:5AR1"
FT STRAND 79..81
FT /evidence="ECO:0007829|PDB:5AR1"
FT STRAND 85..89
FT /evidence="ECO:0007829|PDB:5AR1"
FT HELIX 104..120
FT /evidence="ECO:0007829|PDB:5AR1"
FT STRAND 137..142
FT /evidence="ECO:0007829|PDB:5AR1"
FT STRAND 145..148
FT /evidence="ECO:0007829|PDB:5AR1"
FT HELIX 151..160
FT /evidence="ECO:0007829|PDB:5AR1"
FT TURN 161..163
FT /evidence="ECO:0007829|PDB:5AR1"
FT STRAND 166..172
FT /evidence="ECO:0007829|PDB:5AR1"
FT HELIX 173..175
FT /evidence="ECO:0007829|PDB:5AR1"
FT HELIX 178..194
FT /evidence="ECO:0007829|PDB:5AR1"
FT STRAND 206..209
FT /evidence="ECO:0007829|PDB:5AR1"
FT HELIX 213..223
FT /evidence="ECO:0007829|PDB:5AR1"
FT STRAND 230..232
FT /evidence="ECO:0007829|PDB:5AR1"
FT STRAND 263..265
FT /evidence="ECO:0007829|PDB:5AR1"
FT HELIX 269..285
FT /evidence="ECO:0007829|PDB:5AR1"
FT HELIX 287..295
FT /evidence="ECO:0007829|PDB:5AR1"
SQ SEQUENCE 415 AA; 47649 MW; 5CFFD4CD1F6C57D4 CRC64;
MSGIIDASSA LRKRKHLKRG ITFTVMIVGQ SGSGRSTFIN TLCGQQVVDT STTILLPTDT
STEIDLQLRE ETVELEDDEG VKIQLNIIDT PGFGDSLDNS PSFEIISDYI RHQYDEILLE
ESRVRRNPRF KDGRVHCCLY LINPTGHGLK EIDVEFIRQL GSLVNIIPVI SKSDSLTRDE
LKLNKKLIME DIDRWNLPIY NFPFDEDEIS DEDYETNMYL RTLLPFAIIG SNEVYEMGGD
VGTIRGRKYP WGILDVEDSS ISDFVILRNA LLISHLHDLK NYTHEILYER YRTEALSGES
VAAESIRPNL TKLNGSSSSS TTTRRNTNPF KQSNNINNDV LNPASDMHGQ STGENNETYM
TREEQIRLEE ERLKAFEERV QQELLLKRQE LLQREKELRE IEARLEKEAK IKQEE
