SHS1_YEAST
ID SHS1_YEAST Reviewed; 551 AA.
AC Q07657; D6VRD0;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 1.
DT 03-AUG-2022, entry version 194.
DE RecName: Full=Seventh homolog of septin 1;
DE AltName: Full=Septation protein 7;
GN Name=SHS1; Synonyms=SEP7; OrderedLocusNames=YDL225W;
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 [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169867;
RA Jacq C., Alt-Moerbe J., Andre B., Arnold W., Bahr A., Ballesta J.P.G.,
RA Bargues M., Baron L., Becker A., Biteau N., Bloecker H., Blugeon C.,
RA Boskovic J., Brandt P., Brueckner M., Buitrago M.J., Coster F.,
RA Delaveau T., del Rey F., Dujon B., Eide L.G., Garcia-Cantalejo J.M.,
RA Goffeau A., Gomez-Peris A., Granotier C., Hanemann V., Hankeln T.,
RA Hoheisel J.D., Jaeger W., Jimenez A., Jonniaux J.-L., Kraemer C.,
RA Kuester H., Laamanen P., Legros Y., Louis E.J., Moeller-Rieker S.,
RA Monnet A., Moro M., Mueller-Auer S., Nussbaumer B., Paricio N., Paulin L.,
RA Perea J., Perez-Alonso M., Perez-Ortin J.E., Pohl T.M., Prydz H.,
RA Purnelle B., Rasmussen S.W., Remacha M.A., Revuelta J.L., Rieger M.,
RA Salom D., Saluz H.P., Saiz J.E., Saren A.-M., Schaefer M., Scharfe M.,
RA Schmidt E.R., Schneider C., Scholler P., Schwarz S., Soler-Mira A.,
RA Urrestarazu L.A., Verhasselt P., Vissers S., Voet M., Volckaert G.,
RA Wagner G., Wambutt R., Wedler E., Wedler H., Woelfl S., Harris D.E.,
RA Bowman S., Brown D., Churcher C.M., Connor R., Dedman K., Gentles S.,
RA Hamlin N., Hunt S., Jones L., McDonald S., Murphy L.D., Niblett D.,
RA Odell C., Oliver K., Rajandream M.A., Richards C., Shore L., Walsh S.V.,
RA Barrell B.G., Dietrich F.S., Mulligan J.T., Allen E., Araujo R., Aviles E.,
RA Berno A., Carpenter J., Chen E., Cherry J.M., Chung E., Duncan M.,
RA Hunicke-Smith S., Hyman R.W., Komp C., Lashkari D., Lew H., Lin D.,
RA Mosedale D., Nakahara K., Namath A., Oefner P., Oh C., Petel F.X.,
RA Roberts D., Schramm S., Schroeder M., Shogren T., Shroff N., Winant A.,
RA Yelton M.A., Botstein D., Davis R.W., Johnston M., Andrews S., Brinkman R.,
RA Cooper J., Ding H., Du Z., Favello A., Fulton L., Gattung S., Greco T.,
RA Hallsworth K., Hawkins J., Hillier L.W., Jier M., Johnson D., Johnston L.,
RA Kirsten J., Kucaba T., Langston Y., Latreille P., Le T., Mardis E.,
RA Menezes S., Miller N., Nhan M., Pauley A., Peluso D., Rifkin L., Riles L.,
RA Taich A., Trevaskis E., Vignati D., Wilcox L., Wohldman P., Vaudin M.,
RA Wilson R., Waterston R., Albermann K., Hani J., Heumann K., Kleine K.,
RA Mewes H.-W., Zollner A., Zaccaria P.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome IV.";
RL Nature 387:75-78(1997).
RN [2]
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 [3]
RP CHARACTERIZATION, AND INTERACTION WITH GIN4.
RX PubMed=9813092; DOI=10.1083/jcb.143.3.709;
RA Carroll C.W., Altman R., Schieltz D., Yates J.R. III, Kellogg D.;
RT "The septins are required for the mitosis-specific activation of the Gin4
RT kinase.";
RL J. Cell Biol. 143:709-717(1998).
RN [4]
RP FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH SPA2.
RX PubMed=9790978; DOI=10.1006/bbrc.1998.9541;
RA Mino A., Tanaka K., Kamei T., Umikawa M., Fujiwara T., Takai Y.;
RT "Shs1p: a novel member of septin that interacts with spa2p, involved in
RT polarized growth in Saccharomyces cerevisiae.";
RL Biochem. Biophys. Res. Commun. 251:732-736(1998).
RN [5]
RP SUMOYLATION AT LYS-426 AND LYS-437, AND MUTAGENESIS OF LYS-426 AND LYS-437.
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 PHOSPHORYLATION BY GIN4, IDENTIFICATION BY MASS SPECTROMETRY, AND
RP IDENTIFICATION IN THE GIN4 COMPLEX.
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 [7]
RP PHOSPHORYLATION.
RX PubMed=12636916; DOI=10.1016/s1534-5807(03)00061-3;
RA Dobbelaere J., Gentry M.S., Hallberg R.L., Barral Y.;
RT "Phosphorylation-dependent regulation of septin dynamics during the cell
RT cycle.";
RL Dev. Cell 4:345-357(2003).
RN [8]
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 [9]
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 [10]
RP INTERACTION WITH CDC11, 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 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-447, AND IDENTIFICATION BY
RP 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 [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-416; SER-447; SER-519;
RP SER-525; SER-545 AND SER-548, AND IDENTIFICATION BY MASS SPECTROMETRY
RP [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 [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-408; SER-416; SER-447;
RP SER-545 AND SER-548, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP 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 [14]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-400; SER-408; SER-416;
RP SER-447; SER-460; SER-519; SER-520; SER-522; SER-525; THR-539; SER-545 AND
RP SER-548, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE 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 [15]
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 min before bud emergence, which transforms into an
CC hour-glass shaped collar of cortical filaments that spans both sides of
CC 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:9790978}.
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 CDC11 and SPA2.
CC {ECO:0000269|PubMed:12058072, ECO:0000269|PubMed:15282341,
CC ECO:0000269|PubMed:9790978, ECO:0000269|PubMed:9813092}.
CC -!- INTERACTION:
CC Q07657; P32458: CDC11; NbExp=5; IntAct=EBI-22083, EBI-4178;
CC Q07657; P32468: CDC12; NbExp=4; IntAct=EBI-22083, EBI-4182;
CC Q07657; Q12263: GIN4; NbExp=7; IntAct=EBI-22083, EBI-7595;
CC Q07657; P40075: SCS2; NbExp=4; IntAct=EBI-22083, EBI-16735;
CC Q07657; P39523: YMR124W; NbExp=5; IntAct=EBI-22083, EBI-27256;
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000250}; Peripheral membrane
CC protein {ECO:0000250}. Bud neck {ECO:0000269|PubMed:14562095,
CC ECO:0000269|PubMed:9790978}. Note=Present at the bud neck during cell
CC division. Probably interacts with phosphoinosides such as
CC phosphatidylinositol 4-phosphate or phosphatidylinositol 5-phosphate
CC (By similarity). {ECO:0000250}.
CC -!- PTM: Phosphorylated by GIN4 and CLA4. Phosphorylation state is
CC essential for septin ring dynamics during telophase.
CC {ECO:0000269|PubMed:12058072, ECO:0000269|PubMed:12636916}.
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 5620 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; Z74273; CAA98804.1; -; Genomic_DNA.
DR EMBL; BK006938; DAA11640.1; -; Genomic_DNA.
DR PIR; S67788; S67788.
DR RefSeq; NP_010056.1; NM_001180285.1.
DR AlphaFoldDB; Q07657; -.
DR SMR; Q07657; -.
DR BioGRID; 31885; 276.
DR ComplexPortal; CPX-1675; Septin complex.
DR ComplexPortal; CPX-1712; Gin4 serine/threonine kinase complex.
DR DIP; DIP-5596N; -.
DR ELM; Q07657; -.
DR IntAct; Q07657; 54.
DR MINT; Q07657; -.
DR STRING; 4932.YDL225W; -.
DR iPTMnet; Q07657; -.
DR MaxQB; Q07657; -.
DR PaxDb; Q07657; -.
DR PRIDE; Q07657; -.
DR EnsemblFungi; YDL225W_mRNA; YDL225W; YDL225W.
DR GeneID; 851373; -.
DR KEGG; sce:YDL225W; -.
DR SGD; S000002384; SHS1.
DR VEuPathDB; FungiDB:YDL225W; -.
DR eggNOG; KOG2655; Eukaryota.
DR HOGENOM; CLU_017718_7_4_1; -.
DR InParanoid; Q07657; -.
DR OMA; IQECKFL; -.
DR BioCyc; YEAST:G3O-29605-MON; -.
DR Reactome; R-SCE-111457; Release of apoptotic factors from the mitochondria.
DR Reactome; R-SCE-5687128; MAPK6/MAPK4 signaling.
DR PRO; PR:Q07657; -.
DR Proteomes; UP000002311; Chromosome IV.
DR RNAct; Q07657; protein.
DR GO; GO:0005619; C:ascospore wall; IC:ComplexPortal.
DR GO; GO:0032153; C:cell division site; IBA:GO_Central.
DR GO; GO:0005935; C:cellular bud neck; IPI: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:0043332; C:mating projection tip; HDA:SGD.
DR GO; GO:0015630; C:microtubule cytoskeleton; IBA:GO_Central.
DR GO; GO:0005628; C:prospore membrane; HDA:SGD.
DR GO; GO:0031105; C:septin complex; IPI:ComplexPortal.
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: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; IMP:SGD.
DR GO; GO:0061640; P:cytoskeleton-dependent cytokinesis; IBA:GO_Central.
DR GO; GO:0000917; P:division septum assembly; IMP:SGD.
DR GO; GO:0061163; P:endoplasmic reticulum polarization; IDA:SGD.
DR GO; GO:0010458; P:exit from mitosis; IMP:SGD.
DR GO; GO:0000082; P:G1/S transition of mitotic cell cycle; IGI:SGD.
DR GO; GO:1903475; P:mitotic actomyosin contractile ring assembly; IMP: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; IGI: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:22814378"
FT CHAIN 2..551
FT /note="Seventh homolog of septin 1"
FT /id="PRO_0000173545"
FT DOMAIN 20..339
FT /note="Septin-type G"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01056"
FT REGION 30..37
FT /note="G1 motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01056"
FT REGION 135..138
FT /note="G3 motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01056"
FT REGION 217..220
FT /note="G4 motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01056"
FT REGION 381..417
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 515..551
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 418..518
FT /evidence="ECO:0000255"
FT COMPBIAS 381..397
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 398..417
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 515..544
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 30..37
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 138
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 218..226
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 288
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:22814378"
FT MOD_RES 400
FT /note="Phosphotyrosine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 408
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18407956,
FT ECO:0007744|PubMed:19779198"
FT MOD_RES 416
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17330950,
FT ECO:0007744|PubMed:18407956, ECO:0007744|PubMed:19779198"
FT MOD_RES 447
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:15665377,
FT ECO:0007744|PubMed:17330950, ECO:0007744|PubMed:18407956,
FT ECO:0007744|PubMed:19779198"
FT MOD_RES 460
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 519
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17330950,
FT ECO:0007744|PubMed:19779198"
FT MOD_RES 520
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 522
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 525
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17330950,
FT ECO:0007744|PubMed:19779198"
FT MOD_RES 539
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 545
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17330950,
FT ECO:0007744|PubMed:18407956, ECO:0007744|PubMed:19779198"
FT MOD_RES 548
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17330950,
FT ECO:0007744|PubMed:18407956, ECO:0007744|PubMed:19779198"
FT CROSSLNK 426
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO)"
FT CROSSLNK 437
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO)"
FT MUTAGEN 426
FT /note="K->R: Abolishes sumoylation in vitro; when
FT associated with R-437."
FT /evidence="ECO:0000269|PubMed:10579719"
FT MUTAGEN 437
FT /note="K->R: Abolishes sumoylation in vitro; when
FT associated with R-426."
FT /evidence="ECO:0000269|PubMed:10579719"
SQ SEQUENCE 551 AA; 62630 MW; BDA2631061A278F9 CRC64;
MSTASTPPIN LFRRKKEHKR GITYTMLLCG PAGTGKTAFA NNLLETKIFP HKYQYGKSNA
SISSNPEVKV IAPTKVVSFN SKNGIPSYVS EFDPMRANLE PGITITSTSL ELGGNKDQGK
PEMNEDDTVF FNLIMTHGIG ENLDDSLCSE EVMSYLEQQF DIVLAEETRI KRNPRFEDTR
VHVALYFIEP TGHGLREVDV ELMKSISKYT NVLPIITRAD SFTKEELTQF RKNIMFDVER
YNVPIYKFEV DPEDDDLESM EENQALASLQ PFAIITSDTR DSEGRYVREY PWGIISIDDD
KISDLKVLKN VLFGSHLQEF KDTTQNLLYE NYRSEKLSSV ANAEEIGPNS TKRQSNAPSL
SNFASLISTG QFNSSQTLAN NLRADTPRNQ VSGNFKENEY EDNGEHDSAE NEQEMSPVRQ
LGREIKQENE NLIRSIKTES SPKFLNSPDL PERTKLRNIS ETVPYVLRHE RILARQQKLE
ELEAQSAKEL QKRIQELERK AHELKLREKL INQNKLNGSS SSINSLQQST RSQIKKNDTY
TDLASIASGR D
