SCC2_YEAST
ID SCC2_YEAST Reviewed; 1493 AA.
AC Q04002; D6VSG3;
DT 10-OCT-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 179.
DE RecName: Full=Sister chromatid cohesion protein 2;
GN Name=SCC2; OrderedLocusNames=YDR180W; ORFNames=YD9395.14;
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 200060 / W303;
RX PubMed=9335333; DOI=10.1016/s0092-8674(01)80007-6;
RA Michaelis C., Ciosk R., Nasmyth K.;
RT "Cohesins: chromosomal proteins that prevent premature separation of sister
RT chromatids.";
RL Cell 91:35-45(1997).
RN [2]
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 [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 INTERACTION WITH THE COHESIN COMPLEX, AND FUNCTION.
RX PubMed=9990856; DOI=10.1101/gad.13.3.320;
RA Toth A., Ciosk R., Uhlmann F., Galova M., Schleiffer A., Nasmyth K.;
RT "Yeast cohesin complex requires a conserved protein, Eco1p(Ctf7), to
RT establish cohesion between sister chromatids during DNA replication.";
RL Genes Dev. 13:320-333(1999).
RN [5]
RP FUNCTION, INTERACTION WITH SCC4, AND SUBCELLULAR LOCATION.
RX PubMed=10882066; DOI=10.1016/s1097-2765(00)80420-7;
RA Ciosk R., Shirayama M., Shevchenko A., Tanaka T., Toth A., Shevchenko A.,
RA Nasmyth K.;
RT "Cohesin's binding to chromosomes depends on a separate complex consisting
RT of Scc2 and Scc4 proteins.";
RL Mol. Cell 5:243-254(2000).
RN [6]
RP FUNCTION.
RX PubMed=14614819; DOI=10.1016/j.cub.2003.10.036;
RA Arumugam P., Gruber S., Tanaka K., Haering C.H., Mechtler K., Nasmyth K.;
RT "ATP hydrolysis is required for cohesin's association with chromosomes.";
RL Curr. Biol. 13:1941-1953(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, AND SUBCELLULAR LOCATION.
RC STRAIN=ATCC 200060 / W303 {ECO:0000303|PubMed:25173104};
RX PubMed=25173104; DOI=10.1038/ng.3080;
RA Lopez-Serra L., Kelly G., Patel H., Stewart A., Uhlmann F.;
RT "The Scc2-Scc4 complex acts in sister chromatid cohesion and
RT transcriptional regulation by maintaining nucleosome-free regions.";
RL Nat. Genet. 46:1147-1151(2014).
RN [9]
RP FUNCTION, PHOSPHORYLATION AT SER-43; THR-67; SER-74; SER-127; SER-157;
RP SER-162; SER-163; THR-231; THR-236; SER-305; SER-320; THR-360; SER-753;
RP SER-1179; SER-1182; SER-1183 AND SER-1185, AND MUTAGENESIS OF THR-67;
RP SER-127; SER-157; SER-163; THR-231; THR-236; SER-305; SER-320; SER-753;
RP SER-1182 AND SER-1185.
RX PubMed=26354421; DOI=10.1091/mbc.e15-03-0165;
RA Woodman J., Hoffman M., Dzieciatkowska M., Hansen K.C., Megee P.C.;
RT "Phosphorylation of the Scc2 cohesin deposition complex subunit regulates
RT chromosome condensation through cohesin integrity.";
RL Mol. Biol. Cell 26:3754-3767(2015).
RN [10]
RP X-RAY CRYSTALLOGRAPHY (2.08 ANGSTROMS) OF 1-181 IN COMPLEX WITH SCC4,
RP DOMAIN, AND SUBCELLULAR LOCATION.
RX PubMed=26038942; DOI=10.7554/elife.06057;
RA Hinshaw S.M., Makrantoni V., Kerr A., Marston A.L., Harrison S.C.;
RT "Structural evidence for Scc4-dependent localization of cohesin loading.";
RL Elife 4:E06057-E06057(2015).
CC -!- FUNCTION: Plays a structural role in chromatin and is involved in
CC sister chromatid cohesion (PubMed:9990856, PubMed:14614819,
CC PubMed:25173104, PubMed:26354421). Forms a complex with SCC4 required
CC for the stable association of the cohesin complex with chromatin, which
CC may act by hydrolyzing ATP from SMC1 and SMC3 heads (PubMed:10882066,
CC PubMed:14614819). Binds to the nucleosome-free promoter regions of
CC ribosomal protein genes and tRNA genes. Involved in transcriptional
CC regulation by cooperating with the RSC complex to maintain nucleosome
CC exhaustion at its binding sites (PubMed:25173104).
CC {ECO:0000269|PubMed:10882066, ECO:0000269|PubMed:14614819,
CC ECO:0000269|PubMed:25173104, ECO:0000269|PubMed:26354421,
CC ECO:0000269|PubMed:9990856}.
CC -!- SUBUNIT: Interacts with SCC4 (PubMed:9990856, PubMed:10882066,
CC PubMed:26038942). Interacts with the cohesin complex, which is composed
CC of: the SMC1 and SMC3 heterodimer attached via their hinge domain,
CC MCD1/SCC1 which link them, and IRR1/SCC3, which interacts with MCD1
CC (PubMed:9990856). {ECO:0000269|PubMed:10882066,
CC ECO:0000269|PubMed:26038942, ECO:0000269|PubMed:9990856}.
CC -!- INTERACTION:
CC Q04002; P40090: SCC4; NbExp=5; IntAct=EBI-16662, EBI-16679;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:10882066,
CC ECO:0000269|PubMed:25173104, ECO:0000269|PubMed:26038942}. Chromosome,
CC centromere {ECO:0000269|PubMed:26038942}. Note=Associates with
CC chromatin. {ECO:0000269|PubMed:10882066, ECO:0000269|PubMed:25173104,
CC ECO:0000269|PubMed:26038942}.
CC -!- DOMAIN: The N-terminus (residues 1-181) is sufficient for the
CC interaction with SCC4 (PubMed:26038942). {ECO:0000269|PubMed:26038942}.
CC -!- PTM: Phosphorylated at alternative sites Ser-43, Ser-74, Ser-162, Thr-
CC 360, Ser-1179 and Ser-1183 when the principal phosphorylation sites
CC Thr-67, Ser-127, Ser-157, Ser-163, Thr-231, Thr-236, Ser-305 and Ser-
CC 320 are mutated to alanines. {ECO:0000269|PubMed:26354421}.
CC -!- MISCELLANEOUS: Present with 3310 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the SCC2/Nipped-B family. {ECO:0000305}.
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DR EMBL; Y14279; CAA74656.1; -; Genomic_DNA.
DR EMBL; Z46727; CAA86687.1; -; Genomic_DNA.
DR EMBL; BK006938; DAA12023.1; -; Genomic_DNA.
DR PIR; S49777; S49777.
DR RefSeq; NP_010466.3; NM_001180488.3.
DR PDB; 4XDN; X-ray; 2.08 A; B=1-181.
DR PDB; 5W94; X-ray; 3.19 A; B/D=1-181.
DR PDB; 6ZZ6; EM; 3.40 A; D=1-1493.
DR PDBsum; 4XDN; -.
DR PDBsum; 5W94; -.
DR PDBsum; 6ZZ6; -.
DR AlphaFoldDB; Q04002; -.
DR SMR; Q04002; -.
DR BioGRID; 32234; 279.
DR ComplexPortal; CPX-1868; SCC2-SCC4 cohesin loader complex.
DR DIP; DIP-831N; -.
DR IntAct; Q04002; 2.
DR MINT; Q04002; -.
DR STRING; 4932.YDR180W; -.
DR CarbonylDB; Q04002; -.
DR iPTMnet; Q04002; -.
DR MaxQB; Q04002; -.
DR PaxDb; Q04002; -.
DR PRIDE; Q04002; -.
DR EnsemblFungi; YDR180W_mRNA; YDR180W; YDR180W.
DR GeneID; 851761; -.
DR KEGG; sce:YDR180W; -.
DR SGD; S000002588; SCC2.
DR VEuPathDB; FungiDB:YDR180W; -.
DR eggNOG; KOG1020; Eukaryota.
DR GeneTree; ENSGT00390000010427; -.
DR HOGENOM; CLU_259053_0_0_1; -.
DR InParanoid; Q04002; -.
DR OMA; YVTKCLL; -.
DR BioCyc; YEAST:G3O-29769-MON; -.
DR PRO; PR:Q04002; -.
DR Proteomes; UP000002311; Chromosome IV.
DR RNAct; Q04002; protein.
DR GO; GO:0005729; C:2-micrometer circle DNA; IDA:SGD.
DR GO; GO:0000785; C:chromatin; IDA:UniProtKB.
DR GO; GO:0000775; C:chromosome, centromeric region; IEA:UniProtKB-SubCell.
DR GO; GO:0005829; C:cytosol; IDA:SGD.
DR GO; GO:0005634; C:nucleus; IDA:SGD.
DR GO; GO:0090694; C:Scc2-Scc4 cohesin loading complex; IBA:GO_Central.
DR GO; GO:0032116; C:SMC loading complex; IPI:SGD.
DR GO; GO:0003682; F:chromatin binding; IBA:GO_Central.
DR GO; GO:0043565; F:sequence-specific DNA binding; IDA:UniProtKB.
DR GO; GO:0030543; P:2-micrometer plasmid partitioning; IC:SGD.
DR GO; GO:0006302; P:double-strand break repair; IMP:SGD.
DR GO; GO:0034087; P:establishment of mitotic sister chromatid cohesion; IDA:ComplexPortal.
DR GO; GO:0071169; P:establishment of protein localization to chromatin; IMP:SGD.
DR GO; GO:0007076; P:mitotic chromosome condensation; IMP:SGD.
DR GO; GO:0061780; P:mitotic cohesin loading; IEA:InterPro.
DR GO; GO:0007064; P:mitotic sister chromatid cohesion; IDA:UniProtKB.
DR GO; GO:1905309; P:positive regulation of cohesin loading; IDA:ComplexPortal.
DR GO; GO:0071168; P:protein localization to chromatin; IMP:SGD.
DR GO; GO:0070550; P:rDNA chromatin condensation; IMP:SGD.
DR GO; GO:0010468; P:regulation of gene expression; IMP:UniProtKB.
DR GO; GO:1990414; P:replication-born double-strand break repair via sister chromatid exchange; IMP:SGD.
DR GO; GO:0000972; P:transcription-dependent tethering of RNA polymerase II gene DNA at nuclear periphery; IMP:SGD.
DR GO; GO:0070058; P:tRNA gene clustering; IMP:SGD.
DR InterPro; IPR016024; ARM-type_fold.
DR InterPro; IPR026003; Cohesin_HEAT.
DR InterPro; IPR024986; Nipped-B_C.
DR InterPro; IPR033031; Scc2/Nipped-B.
DR PANTHER; PTHR21704; PTHR21704; 1.
DR Pfam; PF12765; Cohesin_HEAT; 1.
DR Pfam; PF12830; Nipped-B_C; 1.
DR SUPFAM; SSF48371; SSF48371; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cell cycle; Centromere; Chromosome; Nucleus; Phosphoprotein;
KW Reference proteome; Repeat; Transcription; Transcription regulation.
FT CHAIN 1..1493
FT /note="Sister chromatid cohesion protein 2"
FT /id="PRO_0000218603"
FT REPEAT 695..732
FT /note="HEAT 1"
FT REPEAT 734..771
FT /note="HEAT 2"
FT REPEAT 806..843
FT /note="HEAT 3"
FT REPEAT 1132..1169
FT /note="HEAT 4"
FT REPEAT 1244..1281
FT /note="HEAT 5"
FT REGION 151..170
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 43
FT /note="Phosphoserine; in mutant scc2-8A"
FT /evidence="ECO:0000269|PubMed:26354421"
FT MOD_RES 67
FT /note="Phosphothreonine"
FT /evidence="ECO:0000269|PubMed:26354421"
FT MOD_RES 74
FT /note="Phosphoserine; in mutant scc2-8A"
FT /evidence="ECO:0000269|PubMed:26354421"
FT MOD_RES 127
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:26354421"
FT MOD_RES 157
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:26354421"
FT MOD_RES 162
FT /note="Phosphoserine; in mutant scc2-8A"
FT /evidence="ECO:0000269|PubMed:26354421"
FT MOD_RES 163
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:26354421"
FT MOD_RES 231
FT /note="Phosphothreonine"
FT /evidence="ECO:0000269|PubMed:26354421"
FT MOD_RES 236
FT /note="Phosphothreonine"
FT /evidence="ECO:0000269|PubMed:26354421"
FT MOD_RES 305
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:26354421"
FT MOD_RES 320
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:26354421"
FT MOD_RES 360
FT /note="Phosphothreonine; in mutant scc2-8A"
FT /evidence="ECO:0000269|PubMed:26354421"
FT MOD_RES 753
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:26354421"
FT MOD_RES 1179
FT /note="Phosphoserine; in mutant scc2-8A"
FT /evidence="ECO:0000269|PubMed:26354421"
FT MOD_RES 1182
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:26354421"
FT MOD_RES 1183
FT /note="Phosphoserine; in mutant scc2-8A"
FT /evidence="ECO:0000269|PubMed:26354421"
FT MOD_RES 1185
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:26354421"
FT MUTAGEN 67
FT /note="T->A: In scc2-8A; mimics unphosphorylated form and
FT leads to novel phosphorylation sites at Ser-43, Ser-74,
FT Ser-162, Ser-360, Ser-1179 and Ser-1183; when associated
FT with A-127; A-157; A-163; A-231; A-236; A-305 and A-320."
FT /evidence="ECO:0000269|PubMed:26354421"
FT MUTAGEN 67
FT /note="T->E: In scc2-8E; mimics constitutive
FT phosphorylation, retains normal SCC2-SCC4 interactions and
FT chromatin association, but exhibits decreased viability,
FT sensitivity to genotoxic agents methyl methanesulfonate
FT (MMS) and hydroxyurea (HU), and decreased stability of the
FT MCD1 cohesin subunit in mitotic cells; when associated with
FT E-127; E-157; E-163; E-231; E-236; E-305 and E-320."
FT /evidence="ECO:0000269|PubMed:26354421"
FT MUTAGEN 127
FT /note="S->A: In scc2-8A; mimics unphosphorylated form and
FT leads to novel phosphorylation sites at Ser-43, Ser-74,
FT Ser-162, Ser-360, Ser-1179 and Ser-1183; when associated
FT with A-67; A-157; A-163; A-231; A-236; A-305 and A-320."
FT /evidence="ECO:0000269|PubMed:26354421"
FT MUTAGEN 127
FT /note="S->E: In scc2-8E; mimics constitutive
FT phosphorylation, retains normal SCC2-SCC4 interactions and
FT chromatin association, but exhibits decreased viability,
FT sensitivity to genotoxic agents methyl methanesulfonate
FT (MMS) and hydroxyurea (HU), and decreased stability of the
FT MCD1 cohesin subunit in mitotic cells; when associated with
FT E-67; E-157; E-163; E-231; E-236; E-305 and E-320."
FT /evidence="ECO:0000269|PubMed:26354421"
FT MUTAGEN 157
FT /note="S->A: In scc2-8A; mimics unphosphorylated form and
FT leads to novel phosphorylation sites at Ser-43, Ser-74,
FT Ser-162, Ser-360, Ser-1179 and Ser-1183; when associated
FT with A-67; A-127; A-163; A-231; A-236; A-305 and A-320."
FT /evidence="ECO:0000269|PubMed:26354421"
FT MUTAGEN 157
FT /note="S->E: In scc2-8E; mimics constitutive
FT phosphorylation, retains normal SCC2-SCC4 interactions and
FT chromatin association, but exhibits decreased viability,
FT sensitivity to genotoxic agents methyl methanesulfonate
FT (MMS) and hydroxyurea (HU), and decreased stability of the
FT MCD1 cohesin subunit in mitotic cells; when associated with
FT E-67; E-127; E-163; E-231; E-236; E-305 and E-320."
FT /evidence="ECO:0000269|PubMed:26354421"
FT MUTAGEN 163
FT /note="S->A: In scc2-8A; mimics unphosphorylated form and
FT leads to novel phosphorylation sites at Ser-43, Ser-74,
FT Ser-162, Ser-360, Ser-1179 and Ser-1183; when associated
FT with A-67; A-127; A-157; A-231; A-236; A-305 and A-320."
FT /evidence="ECO:0000269|PubMed:26354421"
FT MUTAGEN 163
FT /note="S->E: In scc2-8E; mimics constitutive
FT phosphorylation, retains normal SCC2-SCC4 interactions and
FT chromatin association, but exhibits decreased viability,
FT sensitivity to genotoxic agents methyl methanesulfonate
FT (MMS) and hydroxyurea (HU), and decreased stability of the
FT MCD1 cohesin subunit in mitotic cells; when associated with
FT E-67; E-127; E-157; E-231; E-236; E-305 and E-320."
FT /evidence="ECO:0000269|PubMed:26354421"
FT MUTAGEN 231
FT /note="T->A: In scc2-8A; mimics unphosphorylated form and
FT leads to novel phosphorylation sites at Ser-43, Ser-74,
FT Ser-162, Ser-360, Ser-1179 and Ser-1183; when associated
FT with A-67; A-127; A-157; A-163; A-236; A-305 and A-320."
FT /evidence="ECO:0000269|PubMed:26354421"
FT MUTAGEN 231
FT /note="T->E: In scc2-8E; mimics constitutive
FT phosphorylation, retains normal SCC2-SCC4 interactions and
FT chromatin association, but exhibits decreased viability,
FT sensitivity to genotoxic agents methyl methanesulfonate
FT (MMS) and hydroxyurea (HU), and decreased stability of the
FT MCD1 cohesin subunit in mitotic cells; when associated with
FT E-67; E-127; E-157; E-163; E-236; E-305 and E-320. In scc2-
FT 2NE; mimics constitutive phosphorylation, retains normal
FT SCC2-SCC4 interactions and chromatin association, but
FT exhibits decreased viability, sensitivity to genotoxic
FT agents methyl methanesulfonate (MMS) and hydroxyurea (HU),
FT and decreased stability of the MCD1 cohesin subunit in
FT mitotic cells; when associated with E-236; E-305 and E-
FT 320."
FT /evidence="ECO:0000269|PubMed:26354421"
FT MUTAGEN 236
FT /note="T->A: In scc2-8A; mimics unphosphorylated form and
FT leads to novel phosphorylation sites at Ser-43, Ser-74,
FT Ser-162, Ser-360, Ser-1179 and Ser-1183; when associated
FT with A-67; A-127; A-157; A-163; A-231; A-305 and A-320."
FT /evidence="ECO:0000269|PubMed:26354421"
FT MUTAGEN 236
FT /note="T->E: In scc2-8E; mimics constitutive
FT phosphorylation, retains normal SCC2-SCC4 interactions and
FT chromatin association, but exhibits decreased viability,
FT sensitivity to genotoxic agents methyl methanesulfonate
FT (MMS) and hydroxyurea (HU), and decreased stability of the
FT MCD1 cohesin subunit in mitotic cells; when associated with
FT E-67; E-127; E-157; E-163; E-231; E-305 and E-320. In scc2-
FT 2NE; mimics constitutive phosphorylation, retains normal
FT SCC2-SCC4 interactions and chromatin association, but
FT exhibits decreased viability, sensitivity to genotoxic
FT agents methyl methanesulfonate (MMS) and hydroxyurea (HU),
FT and decreased stability of the MCD1 cohesin subunit in
FT mitotic cells; when associated with E-231; E-305 and E-
FT 320."
FT /evidence="ECO:0000269|PubMed:26354421"
FT MUTAGEN 305
FT /note="S->A: In scc2-8A; mimics unphosphorylated form and
FT leads to novel phosphorylation sites at Ser-43; S-74; S-
FT 162; S-360; S-1179 and Ser-1183; when associated with A-67;
FT A-127; A-157; A-163; A-231; A-236 and A-320."
FT /evidence="ECO:0000269|PubMed:26354421"
FT MUTAGEN 305
FT /note="S->E: In scc2-8E; mimics constitutive
FT phosphorylation, retains normal SCC2-SCC4 interactions and
FT chromatin association, but exhibits decreased viability,
FT sensitivity to genotoxic agents methyl methanesulfonate
FT (MMS) and hydroxyurea (HU), and decreased stability of the
FT MCD1 cohesin subunit in mitotic cells; when associated with
FT E-67; E-127; E-157; E-163; E-231; E-236 and E-320. In scc2-
FT 2NE; mimics constitutive phosphorylation, retains normal
FT SCC2-SCC4 interactions and chromatin association, but
FT exhibits decreased viability, sensitivity to genotoxic
FT agents methyl methanesulfonate (MMS) and hydroxyurea (HU),
FT and decreased stability of the MCD1 cohesin subunit in
FT mitotic cells; when associated with E-231; E-236 and E-
FT 320."
FT /evidence="ECO:0000269|PubMed:26354421"
FT MUTAGEN 320
FT /note="S->A: In scc2-8A; mimics unphosphorylated form and
FT leads to novel phosphorylation sites at S-43; S-74; S-162;
FT S-360; S-1179 and S-1183; when associated with A-67; A-127;
FT A-157; A-163; A-231; A-236 and A-305."
FT /evidence="ECO:0000269|PubMed:26354421"
FT MUTAGEN 320
FT /note="S->E: In scc2-8E; mimics constitutive
FT phosphorylation, retains normal SCC2-SCC4 interactions and
FT chromatin association, but exhibits decreased viability,
FT sensitivity to genotoxic agents methyl methanesulfonate
FT (MMS) and hydroxyurea (HU), and decreased stability of the
FT MCD1 cohesin subunit in mitotic cells; when associated with
FT E-67; E-127; E-157; E-163; E-231; E-236 and E-305. In scc2-
FT 2NE; mimics constitutive phosphorylation, retains normal
FT SCC2-SCC4 interactions and chromatin association, but
FT exhibits decreased viability, sensitivity to genotoxic
FT agents methyl methanesulfonate (MMS) and hydroxyurea (HU),
FT and decreased stability of the MCD1 cohesin subunit in
FT mitotic cells; when associated with E-231; E-236 and E-
FT 305."
FT /evidence="ECO:0000269|PubMed:26354421"
FT MUTAGEN 753
FT /note="S->E: Mimics constitutive phosphorylation and causes
FT inviability through protein instability."
FT /evidence="ECO:0000269|PubMed:26354421"
FT MUTAGEN 1182
FT /note="S->E: In scc2-CE; mimics constitutive
FT phosphorylation, retains normal SCC2-SCC4 interactions and
FT chromatin association, but exhibits decreased viability,
FT sensitivity to genotoxic agents methyl methanesulfonate
FT (MMS) and hydroxyurea (HU); when associated with E-1185."
FT /evidence="ECO:0000269|PubMed:26354421"
FT MUTAGEN 1185
FT /note="S->E: In scc2-CE; mimics constitutive
FT phosphorylation, retains normal SCC2-SCC4 interactions and
FT chromatin association, but exhibits decreased viability,
FT sensitivity to genotoxic agents methyl methanesulfonate
FT (MMS) and hydroxyurea (HU); when associated with E-1182."
FT /evidence="ECO:0000269|PubMed:26354421"
FT TURN 4..7
FT /evidence="ECO:0007829|PDB:4XDN"
FT HELIX 14..17
FT /evidence="ECO:0007829|PDB:4XDN"
FT TURN 18..20
FT /evidence="ECO:0007829|PDB:4XDN"
FT HELIX 32..37
FT /evidence="ECO:0007829|PDB:4XDN"
FT STRAND 41..43
FT /evidence="ECO:0007829|PDB:4XDN"
FT STRAND 59..61
FT /evidence="ECO:0007829|PDB:4XDN"
FT HELIX 79..81
FT /evidence="ECO:0007829|PDB:4XDN"
FT STRAND 85..87
FT /evidence="ECO:0007829|PDB:4XDN"
FT TURN 106..109
FT /evidence="ECO:0007829|PDB:4XDN"
FT HELIX 112..120
FT /evidence="ECO:0007829|PDB:4XDN"
FT TURN 121..124
FT /evidence="ECO:0007829|PDB:5W94"
FT STRAND 128..130
FT /evidence="ECO:0007829|PDB:4XDN"
FT HELIX 222..235
FT /evidence="ECO:0007829|PDB:6ZZ6"
FT HELIX 251..261
FT /evidence="ECO:0007829|PDB:6ZZ6"
FT HELIX 279..290
FT /evidence="ECO:0007829|PDB:6ZZ6"
FT HELIX 305..321
FT /evidence="ECO:0007829|PDB:6ZZ6"
FT HELIX 339..351
FT /evidence="ECO:0007829|PDB:6ZZ6"
FT HELIX 357..372
FT /evidence="ECO:0007829|PDB:6ZZ6"
FT HELIX 387..405
FT /evidence="ECO:0007829|PDB:6ZZ6"
FT HELIX 410..419
FT /evidence="ECO:0007829|PDB:6ZZ6"
FT HELIX 420..423
FT /evidence="ECO:0007829|PDB:6ZZ6"
FT HELIX 445..455
FT /evidence="ECO:0007829|PDB:6ZZ6"
FT HELIX 460..465
FT /evidence="ECO:0007829|PDB:6ZZ6"
FT HELIX 476..505
FT /evidence="ECO:0007829|PDB:6ZZ6"
FT TURN 507..509
FT /evidence="ECO:0007829|PDB:6ZZ6"
FT HELIX 511..523
FT /evidence="ECO:0007829|PDB:6ZZ6"
FT HELIX 532..547
FT /evidence="ECO:0007829|PDB:6ZZ6"
FT HELIX 556..578
FT /evidence="ECO:0007829|PDB:6ZZ6"
FT HELIX 598..615
FT /evidence="ECO:0007829|PDB:6ZZ6"
FT HELIX 619..633
FT /evidence="ECO:0007829|PDB:6ZZ6"
FT HELIX 648..661
FT /evidence="ECO:0007829|PDB:6ZZ6"
FT HELIX 679..687
FT /evidence="ECO:0007829|PDB:6ZZ6"
FT TURN 688..690
FT /evidence="ECO:0007829|PDB:6ZZ6"
FT HELIX 692..695
FT /evidence="ECO:0007829|PDB:6ZZ6"
FT HELIX 697..708
FT /evidence="ECO:0007829|PDB:6ZZ6"
FT HELIX 713..729
FT /evidence="ECO:0007829|PDB:6ZZ6"
FT TURN 731..734
FT /evidence="ECO:0007829|PDB:6ZZ6"
FT HELIX 737..748
FT /evidence="ECO:0007829|PDB:6ZZ6"
FT HELIX 752..764
FT /evidence="ECO:0007829|PDB:6ZZ6"
FT HELIX 769..771
FT /evidence="ECO:0007829|PDB:6ZZ6"
FT HELIX 772..777
FT /evidence="ECO:0007829|PDB:6ZZ6"
FT TURN 778..780
FT /evidence="ECO:0007829|PDB:6ZZ6"
FT HELIX 784..800
FT /evidence="ECO:0007829|PDB:6ZZ6"
FT HELIX 804..816
FT /evidence="ECO:0007829|PDB:6ZZ6"
FT HELIX 823..837
FT /evidence="ECO:0007829|PDB:6ZZ6"
FT HELIX 839..844
FT /evidence="ECO:0007829|PDB:6ZZ6"
FT TURN 848..850
FT /evidence="ECO:0007829|PDB:6ZZ6"
FT HELIX 851..865
FT /evidence="ECO:0007829|PDB:6ZZ6"
FT STRAND 867..869
FT /evidence="ECO:0007829|PDB:6ZZ6"
FT HELIX 871..882
FT /evidence="ECO:0007829|PDB:6ZZ6"
FT TURN 883..885
FT /evidence="ECO:0007829|PDB:6ZZ6"
FT TURN 887..889
FT /evidence="ECO:0007829|PDB:6ZZ6"
FT HELIX 893..916
FT /evidence="ECO:0007829|PDB:6ZZ6"
FT HELIX 928..941
FT /evidence="ECO:0007829|PDB:6ZZ6"
FT STRAND 943..945
FT /evidence="ECO:0007829|PDB:6ZZ6"
FT HELIX 950..961
FT /evidence="ECO:0007829|PDB:6ZZ6"
FT HELIX 968..980
FT /evidence="ECO:0007829|PDB:6ZZ6"
FT HELIX 988..1000
FT /evidence="ECO:0007829|PDB:6ZZ6"
FT TURN 1001..1004
FT /evidence="ECO:0007829|PDB:6ZZ6"
FT HELIX 1007..1021
FT /evidence="ECO:0007829|PDB:6ZZ6"
FT STRAND 1024..1026
FT /evidence="ECO:0007829|PDB:6ZZ6"
FT HELIX 1028..1048
FT /evidence="ECO:0007829|PDB:6ZZ6"
FT HELIX 1061..1074
FT /evidence="ECO:0007829|PDB:6ZZ6"
FT HELIX 1093..1103
FT /evidence="ECO:0007829|PDB:6ZZ6"
FT HELIX 1111..1127
FT /evidence="ECO:0007829|PDB:6ZZ6"
FT HELIX 1129..1133
FT /evidence="ECO:0007829|PDB:6ZZ6"
FT HELIX 1135..1146
FT /evidence="ECO:0007829|PDB:6ZZ6"
FT HELIX 1152..1174
FT /evidence="ECO:0007829|PDB:6ZZ6"
FT STRAND 1179..1182
FT /evidence="ECO:0007829|PDB:6ZZ6"
FT HELIX 1204..1211
FT /evidence="ECO:0007829|PDB:6ZZ6"
FT HELIX 1213..1220
FT /evidence="ECO:0007829|PDB:6ZZ6"
FT HELIX 1225..1241
FT /evidence="ECO:0007829|PDB:6ZZ6"
FT HELIX 1246..1248
FT /evidence="ECO:0007829|PDB:6ZZ6"
FT HELIX 1250..1257
FT /evidence="ECO:0007829|PDB:6ZZ6"
FT HELIX 1262..1285
FT /evidence="ECO:0007829|PDB:6ZZ6"
FT HELIX 1287..1301
FT /evidence="ECO:0007829|PDB:6ZZ6"
FT STRAND 1303..1305
FT /evidence="ECO:0007829|PDB:6ZZ6"
FT TURN 1306..1308
FT /evidence="ECO:0007829|PDB:6ZZ6"
FT HELIX 1313..1319
FT /evidence="ECO:0007829|PDB:6ZZ6"
FT HELIX 1326..1340
FT /evidence="ECO:0007829|PDB:6ZZ6"
FT HELIX 1356..1367
FT /evidence="ECO:0007829|PDB:6ZZ6"
FT HELIX 1374..1397
FT /evidence="ECO:0007829|PDB:6ZZ6"
FT HELIX 1414..1433
FT /evidence="ECO:0007829|PDB:6ZZ6"
FT HELIX 1449..1453
FT /evidence="ECO:0007829|PDB:6ZZ6"
FT HELIX 1467..1472
FT /evidence="ECO:0007829|PDB:6ZZ6"
SQ SEQUENCE 1493 AA; 171102 MW; 94CC2E8D2F4208D0 CRC64;
MSYPGKDKNI PGRIIEALED LPLSYLVPKD GLAALVNAPM RVSLPFDKTI FTSADDGRDV
NINVLGTANS TTSSIKNEAE KERLVFKRPS NFTSSANSVD YVPTNFLEGL SPLAQSVLST
HKGLNDSINI EKKSEIVSRP EAKHKLESVT SNAGNLSFND NSSNKKTKTS TGVTMTQANL
AEQYLNDLKN ILDIVGFDQN SAEIGNIEYW LQLPNKKFVL TTNCLTKLQM TIKNITDNPQ
LSNSIEITWL LRLLDVMVCN IKFSKSSLKM GLDDSMLRYI ALLSTIVLFN IFLLGKNDSN
LHRESYIMEP VNFLSDLIES LKILTIEYGS LKIEFDTFQE ALELLPKYIR NGPFLDDNVT
AKLVYIFSDL LMNNDIEATT NIQFQSFWDN VKRISSDILV SLFGSFDQQR GFIIEELLSH
IEKLPTKRIQ KKLRKVGNQN IYITDFTFTL MSMLENINCY SFCNQMKDIA PENIDLLKNE
YKKQEEFLFN IVEHINDTIL ERFFKNPSAL RYVIDNFVQD LLLLISSPQW PVTEKILSSL
LKRLLSVYSP SMQVSANIET ICLQLIGNIG STIFDIKCST RDHEDNNLIK MINYPETLPH
FFKSFEECIA YNETIKCRRS ATRFLWNLRL GTILILEEYT KDAKEQIITV DNELKKILEQ
IKDGGLGPEL ENREADFSTI KLDYFSILHA FELLNLYDPY LKLILSLLAK DKIKLRSTAI
KCLSMLASKD KVILSNPMVK ETIHRRLNDS SASVKDAILD LVSINSSYFE FYQQINNNYN
DDSIMVRKHV LRINEKMYDE TNDIVTKVYV IARILMKIED EEDNIIDMAR LILLNRWILK
VHEVLDQPEK LKEISSSVLL VMSRVAIMNE KCSQLFDLFL NFYLLNKEAH SKEAYDKITH
VLTILTDFLV QKIVELNSDD TNEKNSIVDK QNFLNLLAKF ADSTVSFLTK DHITALYPYM
VSDEKSDFHY YILQVFRCTF EKLANFKQKF LYDLETTLLS RLPKMNVREI DEAMPLIWSV
ATHRHDTARV AKACSSCLSH LHPYINKANN EEAAIVVDGK LQRLIYLSTG FARFCFPKPS
NDKIAFLQEG ETLYEHITKC LLVLSKDKIT HVIRRVAVKN LTKLCGNHPK LFNSRHVLHL
LDKEFQSDQL DIKLVILESL YDLFLLEERK SVRNTGVNST LSSNSILKKK LLKTNRVEFA
NDGVCSALAT RFLDNILQLC LLRDLKNSLV AIRLLKLILK FGYTNPSHSI PTVIALFAST
SQYIRHVAYE LLEDLFEKYE TLVFSSLSRG VTKAIHYSIH TDEKYYYKHD HFLSLLEKLC
GTGKKNGPKF FKVLKRIMQS YLDDITDLTS TNSSVQKSIF VLCTNISNIT FVSQYDLVSL
LKTIDLTTDR LKEVIMDEIG DNVSSLSVSE EKLSGIILIQ LSLQDLGTYL LHLYGLRDDV
LLLDIVEESE LKNKQLPAKK PDISKFSAQL ENIEQYSSNG KLLTYFRKHV KDT
