ID   SNF2_YEAST              Reviewed;        1703 AA.
AC   P22082; D6W2Y8;
DT   01-AUG-1991, integrated into UniProtKB/Swiss-Prot.
DT   01-AUG-1991, sequence version 1.
DT   27-MAR-2024, entry version 224.
DE   RecName: Full=Transcription regulatory protein SNF2;
DE            EC=3.6.4.-;
DE   AltName: Full=ATP-dependent helicase SNF2;
DE   AltName: Full=Regulatory protein GAM1;
DE   AltName: Full=Regulatory protein SWI2;
DE   AltName: Full=SWI/SNF complex component SNF2;
DE   AltName: Full=Transcription factor TYE3;
GN   Name=SNF2; Synonyms=GAM1, RIC1, SWI2, TYE3; OrderedLocusNames=YOR290C;
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 204508 / S288c;
RX   PubMed=1901413; DOI=10.1073/pnas.88.7.2687;
RA   Laurent B.C., Treitel M.A., Carlson M.;
RT   "Functional interdependence of the yeast SNF2, SNF5, and SNF6 proteins in
RT   transcriptional activation.";
RL   Proc. Natl. Acad. Sci. U.S.A. 88:2687-2691(1991).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 38626 / AH22 / NRRL Y-12843;
RX   PubMed=1886612; DOI=10.1007/bf00282476;
RA   Yoshimoto H., Yamashita I.;
RT   "The GAM1/SNF2 gene of Saccharomyces cerevisiae encodes a highly charged
RT   nuclear protein required for transcription of the STA1 gene.";
RL   Mol. Gen. Genet. 228:270-280(1991).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 26787 / X2180-1B;
RX   PubMed=7608126; DOI=10.1093/jb/117.2.362;
RA   Kodaki T., Hosaka K., Nikawa J., Yamashita S.;
RT   "The SNF2/SWI2/GAM1/TYE3/RIC1 gene is involved in the coordinate regulation
RT   of phospholipid synthesis in Saccharomyces cerevisiae.";
RL   J. Biochem. 117:362-368(1995).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=8896271;
RX   DOI=10.1002/(sici)1097-0061(199609)12:10b%3c1059::aid-yea994%3e3.0.co;2-7;
RA   Cheret G., Bernardi A., Sor F.J.;
RT   "DNA sequence analysis of the VPH1-SNF2 region on chromosome XV of
RT   Saccharomyces cerevisiae.";
RL   Yeast 12:1059-1064(1996).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=9169874;
RA   Dujon B., Albermann K., Aldea M., Alexandraki D., Ansorge W., Arino J.,
RA   Benes V., Bohn C., Bolotin-Fukuhara M., Bordonne R., Boyer J., Camasses A.,
RA   Casamayor A., Casas C., Cheret G., Cziepluch C., Daignan-Fornier B.,
RA   Dang V.-D., de Haan M., Delius H., Durand P., Fairhead C., Feldmann H.,
RA   Gaillon L., Galisson F., Gamo F.-J., Gancedo C., Goffeau A., Goulding S.E.,
RA   Grivell L.A., Habbig B., Hand N.J., Hani J., Hattenhorst U., Hebling U.,
RA   Hernando Y., Herrero E., Heumann K., Hiesel R., Hilger F., Hofmann B.,
RA   Hollenberg C.P., Hughes B., Jauniaux J.-C., Kalogeropoulos A.,
RA   Katsoulou C., Kordes E., Lafuente M.J., Landt O., Louis E.J., Maarse A.C.,
RA   Madania A., Mannhaupt G., Marck C., Martin R.P., Mewes H.-W., Michaux G.,
RA   Paces V., Parle-McDermott A.G., Pearson B.M., Perrin A., Pettersson B.,
RA   Poch O., Pohl T.M., Poirey R., Portetelle D., Pujol A., Purnelle B.,
RA   Ramezani Rad M., Rechmann S., Schwager C., Schweizer M., Sor F., Sterky F.,
RA   Tarassov I.A., Teodoru C., Tettelin H., Thierry A., Tobiasch E.,
RA   Tzermia M., Uhlen M., Unseld M., Valens M., Vandenbol M., Vetter I.,
RA   Vlcek C., Voet M., Volckaert G., Voss H., Wambutt R., Wedler H.,
RA   Wiemann S., Winsor B., Wolfe K.H., Zollner A., Zumstein E., Kleine K.;
RT   "The nucleotide sequence of Saccharomyces cerevisiae chromosome XV.";
RL   Nature 387:98-102(1997).
RN   [6]
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   [7]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-309.
RC   STRAIN=ATCC 96604 / S288c / FY1679;
RX   PubMed=9153758;
RX   DOI=10.1002/(sici)1097-0061(199704)13:5<479::aid-yea104>3.0.co;2-g;
RA   Poirey R., Cziepluch C., Tobiasch E., Pujol A., Kordes E., Jauniaux J.-C.;
RT   "Sequence and analysis of a 36.2 kb fragment from the right arm of yeast
RT   chromosome XV reveals 19 open reading frames including SNF2 (5' end), CPA1,
RT   SLY41, a putative transport ATPase, a putative ribosomal protein and an
RT   SNF2 homologue.";
RL   Yeast 13:479-482(1997).
RN   [8]
RP   MUTAGENESIS.
RX   PubMed=8871545; DOI=10.1093/nar/24.19.3685;
RA   Richmond E., Peterson C.L.;
RT   "Functional analysis of the DNA-stimulated ATPase domain of yeast
RT   SWI2/SNF2.";
RL   Nucleic Acids Res. 24:3685-3692(1996).
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   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-358, AND IDENTIFICATION BY
RP   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   [11]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-358; SER-716 AND SER-1340,
RP   AND 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   [12]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-358; THR-383 AND SER-716, AND
RP   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   [13]
RP   UBIQUITINATION [LARGE SCALE ANALYSIS] AT LYS-543, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=22106047; DOI=10.1002/pmic.201100166;
RA   Starita L.M., Lo R.S., Eng J.K., von Haller P.D., Fields S.;
RT   "Sites of ubiquitin attachment in Saccharomyces cerevisiae.";
RL   Proteomics 12:236-240(2012).
RN   [14]
RP   3D-STRUCTURE MODELING OF THE SWI/SNF COMPLEX, AND ELECTRON MICROSCOPY OF
RP   THE SWI/SNF COMPLEX.
RX   PubMed=12524530; DOI=10.1038/nsb888;
RA   Smith C.L., Horowitz-Scherer R., Flanagan J.F., Woodcock C.L.,
RA   Peterson C.L.;
RT   "Structural analysis of the yeast SWI/SNF chromatin remodeling complex.";
RL   Nat. Struct. Biol. 10:141-145(2003).
CC   -!- FUNCTION: Involved in transcriptional activation. Catalytic component
CC       of the SWI/SNF complex, an ATP-dependent chromatin-remodeling complex,
CC       which is required for the positive and negative regulation of gene
CC       expression of a large number of genes. It changes chromatin structure
CC       by altering DNA-histone contacts within a nucleosome, leading
CC       eventually to a change in nucleosome position, thus facilitating or
CC       repressing binding of gene-specific transcription factors.
CC   -!- SUBUNIT: Component of the SWI/SNF global transcription activator
CC       complex. The 1.14 MDa SWI/SNF complex is composed of 11 different
CC       subunits: one copy each of SWI1, SNF2/SWI2, SNF5, SNF12/SWP73,
CC       ARP7/SWP61, ARP9/SWP59; two copies each of SWI3, SNF6, SNF11, SWP82;
CC       and three copies of TAF14/SWP29.
CC   -!- INTERACTION:
CC       P22082; P02309: HHF2; NbExp=2; IntAct=EBI-17526, EBI-8113;
CC       P22082; P38074: HMT1; NbExp=3; IntAct=EBI-17526, EBI-8394;
CC       P22082; P38956: SNF11; NbExp=3; IntAct=EBI-17526, EBI-17560;
CC       P22082; P32591: SWI3; NbExp=8; IntAct=EBI-17526, EBI-18622;
CC   -!- SUBCELLULAR LOCATION: Nucleus.
CC   -!- MISCELLANEOUS: Present with 217 molecules/cell in log phase SD medium.
CC       {ECO:0000269|PubMed:14562106}.
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DR   EMBL; M61703; AAA35059.1; -; Genomic_DNA.
DR   EMBL; X57837; CAA40969.1; -; Genomic_DNA.
DR   EMBL; D90459; BAA14423.1; -; Genomic_DNA.
DR   EMBL; X89633; CAA61793.1; -; Genomic_DNA.
DR   EMBL; Z75198; CAA99517.1; -; Genomic_DNA.
DR   EMBL; Z75199; CAA99519.1; -; Genomic_DNA.
DR   EMBL; BK006948; DAA11054.1; -; Genomic_DNA.
DR   PIR; S15047; S15047.
DR   RefSeq; NP_014933.3; NM_001183709.3.
DR   PDB; 4I6M; X-ray; 2.80 A; C=575-667.
DR   PDB; 5X0X; EM; 3.97 A; O=666-1400.
DR   PDB; 5X0Y; EM; 3.97 A; O=666-1400.
DR   PDB; 5Z3L; EM; 4.31 A; O=666-1400.
DR   PDB; 5Z3O; EM; 3.62 A; O=666-1400.
DR   PDB; 5Z3U; EM; 4.31 A; O=666-1400.
DR   PDB; 5Z3V; EM; 4.22 A; O=666-1400.
DR   PDB; 6IY2; EM; 3.47 A; O=670-1348.
DR   PDB; 6IY3; EM; 3.67 A; O=670-1348.
DR   PDB; 6UXV; EM; 4.70 A; A=1-1703.
DR   PDB; 6UXW; EM; 8.96 A; A=1-1703.
DR   PDB; 7C4J; EM; 2.89 A; H=1-1703.
DR   PDB; 7EGM; EM; 3.60 A; A=430-1400.
DR   PDB; 7EGP; EM; 6.90 A; A=430-1400.
DR   PDB; 7VRC; X-ray; 2.15 A; B/D=248-308.
DR   PDBsum; 4I6M; -.
DR   PDBsum; 5X0X; -.
DR   PDBsum; 5X0Y; -.
DR   PDBsum; 5Z3L; -.
DR   PDBsum; 5Z3O; -.
DR   PDBsum; 5Z3U; -.
DR   PDBsum; 5Z3V; -.
DR   PDBsum; 6IY2; -.
DR   PDBsum; 6IY3; -.
DR   PDBsum; 6UXV; -.
DR   PDBsum; 6UXW; -.
DR   PDBsum; 7C4J; -.
DR   PDBsum; 7EGM; -.
DR   PDBsum; 7EGP; -.
DR   PDBsum; 7VRC; -.
DR   AlphaFoldDB; P22082; -.
DR   EMDB; EMD-20933; -.
DR   EMDB; EMD-20934; -.
DR   EMDB; EMD-30285; -.
DR   EMDB; EMD-31136; -.
DR   EMDB; EMD-31137; -.
DR   EMDB; EMD-6699; -.
DR   EMDB; EMD-6700; -.
DR   EMDB; EMD-6879; -.
DR   EMDB; EMD-6880; -.
DR   EMDB; EMD-6882; -.
DR   EMDB; EMD-6883; -.
DR   EMDB; EMD-9748; -.
DR   SMR; P22082; -.
DR   BioGRID; 34678; 261.
DR   ComplexPortal; CPX-1150; SWI/SNF chromatin remodelling complex.
DR   DIP; DIP-1150N; -.
DR   IntAct; P22082; 47.
DR   MINT; P22082; -.
DR   STRING; 4932.YOR290C; -.
DR   GlyGen; P22082; 3 sites, 1 O-linked glycan (3 sites).
DR   iPTMnet; P22082; -.
DR   MaxQB; P22082; -.
DR   PaxDb; 4932-YOR290C; -.
DR   PeptideAtlas; P22082; -.
DR   EnsemblFungi; YOR290C_mRNA; YOR290C; YOR290C.
DR   GeneID; 854465; -.
DR   KEGG; sce:YOR290C; -.
DR   AGR; SGD:S000005816; -.
DR   SGD; S000005816; SNF2.
DR   VEuPathDB; FungiDB:YOR290C; -.
DR   eggNOG; KOG0386; Eukaryota.
DR   GeneTree; ENSGT00940000169728; -.
DR   HOGENOM; CLU_000315_15_2_1; -.
DR   InParanoid; P22082; -.
DR   OMA; NPTRETN; -.
DR   OrthoDB; 5482994at2759; -.
DR   BioCyc; YEAST:G3O-33775-MONOMER; -.
DR   BioGRID-ORCS; 854465; 2 hits in 10 CRISPR screens.
DR   PRO; PR:P22082; -.
DR   Proteomes; UP000002311; Chromosome XV.
DR   RNAct; P22082; Protein.
DR   GO; GO:0000785; C:chromatin; NAS:ComplexPortal.
DR   GO; GO:0005634; C:nucleus; IDA:SGD.
DR   GO; GO:0016514; C:SWI/SNF complex; IDA:SGD.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0008094; F:ATP-dependent activity, acting on DNA; IBA:GO_Central.
DR   GO; GO:0140658; F:ATP-dependent chromatin remodeler activity; IDA:SGD.
DR   GO; GO:0003677; F:DNA binding; IBA:GO_Central.
DR   GO; GO:0004386; F:helicase activity; IEA:UniProtKB-KW.
DR   GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR   GO; GO:0070577; F:lysine-acetylated histone binding; IDA:SGD.
DR   GO; GO:0031492; F:nucleosomal DNA binding; IDA:SGD.
DR   GO; GO:0000182; F:rDNA binding; IDA:SGD.
DR   GO; GO:0061629; F:RNA polymerase II-specific DNA-binding transcription factor binding; IPI:SGD.
DR   GO; GO:0035973; P:aggrephagy; IMP:SGD.
DR   GO; GO:0006338; P:chromatin remodeling; IDA:SGD.
DR   GO; GO:0042148; P:DNA strand invasion; IMP:SGD.
DR   GO; GO:0006261; P:DNA-templated DNA replication; IMP:SGD.
DR   GO; GO:0006302; P:double-strand break repair; IMP:SGD.
DR   GO; GO:1900189; P:positive regulation of cell adhesion involved in single-species biofilm formation; IMP:SGD.
DR   GO; GO:2000219; P:positive regulation of invasive growth in response to glucose limitation; IMP:SGD.
DR   GO; GO:0031496; P:positive regulation of mating type switching; IMP:SGD.
DR   GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IMP:SGD.
DR   GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IDA:ComplexPortal.
DR   CDD; cd05519; Bromo_SNF2; 1.
DR   CDD; cd17996; DEXHc_SMARCA2_SMARCA4; 1.
DR   CDD; cd18793; SF2_C_SNF; 1.
DR   Gene3D; 1.20.5.170; -; 1.
DR   Gene3D; 1.20.920.10; Bromodomain-like; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR   Gene3D; 3.40.50.10810; Tandem AAA-ATPase domain; 1.
DR   InterPro; IPR017956; AT_hook_DNA-bd_motif.
DR   InterPro; IPR001487; Bromodomain.
DR   InterPro; IPR036427; Bromodomain-like_sf.
DR   InterPro; IPR018359; Bromodomain_CS.
DR   InterPro; IPR014978; Gln-Leu-Gln_QLQ.
DR   InterPro; IPR014001; Helicase_ATP-bd.
DR   InterPro; IPR001650; Helicase_C.
DR   InterPro; IPR014012; HSA_dom.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR029295; SnAC.
DR   InterPro; IPR038718; SNF2-like_sf.
DR   InterPro; IPR049730; SNF2/RAD54-like_C.
DR   InterPro; IPR000330; SNF2_N.
DR   PANTHER; PTHR10799:SF973; ATP-DEPENDENT HELICASE BRM; 1.
DR   PANTHER; PTHR10799; SNF2/RAD54 HELICASE FAMILY; 1.
DR   Pfam; PF00439; Bromodomain; 1.
DR   Pfam; PF00271; Helicase_C; 1.
DR   Pfam; PF08880; QLQ; 1.
DR   Pfam; PF14619; SnAC; 1.
DR   Pfam; PF00176; SNF2-rel_dom; 1.
DR   PRINTS; PR00503; BROMODOMAIN.
DR   SMART; SM00384; AT_hook; 2.
DR   SMART; SM00297; BROMO; 1.
DR   SMART; SM00487; DEXDc; 1.
DR   SMART; SM00490; HELICc; 1.
DR   SMART; SM00951; QLQ; 1.
DR   SMART; SM01314; SnAC; 1.
DR   SUPFAM; SSF47370; Bromodomain; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 2.
DR   PROSITE; PS00633; BROMODOMAIN_1; 1.
DR   PROSITE; PS50014; BROMODOMAIN_2; 1.
DR   PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR   PROSITE; PS51194; HELICASE_CTER; 1.
DR   PROSITE; PS51204; HSA; 1.
DR   PROSITE; PS51666; QLQ; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Activator; ATP-binding; Bromodomain; Helicase; Hydrolase;
KW   Isopeptide bond; Nucleotide-binding; Nucleus; Phosphoprotein;
KW   Reference proteome; Repeat; Transcription; Transcription regulation;
KW   Ubl conjugation.
FT   CHAIN           1..1703
FT                   /note="Transcription regulatory protein SNF2"
FT                   /id="PRO_0000074358"
FT   DOMAIN          247..282
FT                   /note="QLQ"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01001"
FT   DOMAIN          588..661
FT                   /note="HSA"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00549"
FT   DOMAIN          779..944
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT   DOMAIN          1091..1254
FT                   /note="Helicase C-terminal"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT   DOMAIN          1568..1638
FT                   /note="Bromo"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00035"
FT   DNA_BIND        1446..1456
FT                   /note="A.T hook 1"
FT   DNA_BIND        1502..1513
FT                   /note="A.T hook 2"
FT   DNA_BIND        1516..1526
FT                   /note="A.T hook 3"
FT   REGION          57..176
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          193..212
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          305..426
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1338..1531
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           894..897
FT                   /note="DEGH box"
FT   COMPBIAS        305..388
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        399..418
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1370..1412
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1419..1443
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1464..1478
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1504..1524
FT                   /note="Basic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         792..799
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT   MOD_RES         358
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:17330950,
FT                   ECO:0007744|PubMed:18407956, ECO:0007744|PubMed:19779198"
FT   MOD_RES         383
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0007744|PubMed:19779198"
FT   MOD_RES         716
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:18407956,
FT                   ECO:0007744|PubMed:19779198"
FT   MOD_RES         1340
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:18407956"
FT   CROSSLNK        543
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in ubiquitin)"
FT                   /evidence="ECO:0007744|PubMed:22106047"
FT   HELIX           250..267
FT                   /evidence="ECO:0007829|PDB:7VRC"
FT   HELIX           274..285
FT                   /evidence="ECO:0007829|PDB:7VRC"
FT   HELIX           290..295
FT                   /evidence="ECO:0007829|PDB:7VRC"
FT   HELIX           427..434
FT                   /evidence="ECO:0007829|PDB:7C4J"
FT   STRAND          439..441
FT                   /evidence="ECO:0007829|PDB:7C4J"
FT   STRAND          451..453
FT                   /evidence="ECO:0007829|PDB:7C4J"
FT   HELIX           465..471
FT                   /evidence="ECO:0007829|PDB:7C4J"
FT   TURN            474..476
FT                   /evidence="ECO:0007829|PDB:7C4J"
FT   TURN            481..483
FT                   /evidence="ECO:0007829|PDB:7C4J"
FT   HELIX           490..517
FT                   /evidence="ECO:0007829|PDB:7C4J"
FT   HELIX           523..556
FT                   /evidence="ECO:0007829|PDB:7C4J"
FT   HELIX           560..563
FT                   /evidence="ECO:0007829|PDB:7C4J"
FT   HELIX           593..657
FT                   /evidence="ECO:0007829|PDB:4I6M"
FT   HELIX           672..681
FT                   /evidence="ECO:0007829|PDB:6IY2"
FT   HELIX           685..688
FT                   /evidence="ECO:0007829|PDB:6IY2"
FT   HELIX           744..747
FT                   /evidence="ECO:0007829|PDB:6IY2"
FT   HELIX           769..783
FT                   /evidence="ECO:0007829|PDB:6IY2"
FT   HELIX           798..811
FT                   /evidence="ECO:0007829|PDB:6IY2"
FT   STRAND          819..822
FT                   /evidence="ECO:0007829|PDB:6IY2"
FT   HELIX           825..827
FT                   /evidence="ECO:0007829|PDB:6IY2"
FT   HELIX           828..838
FT                   /evidence="ECO:0007829|PDB:6IY2"
FT   HELIX           851..861
FT                   /evidence="ECO:0007829|PDB:6IY2"
FT   TURN            862..864
FT                   /evidence="ECO:0007829|PDB:6IY2"
FT   STRAND          867..869
FT                   /evidence="ECO:0007829|PDB:6IY2"
FT   HELIX           874..878
FT                   /evidence="ECO:0007829|PDB:6IY2"
FT   TURN            879..881
FT                   /evidence="ECO:0007829|PDB:6IY2"
FT   HELIX           882..885
FT                   /evidence="ECO:0007829|PDB:6IY2"
FT   STRAND          890..893
FT                   /evidence="ECO:0007829|PDB:6IY2"
FT   HELIX           896..899
FT                   /evidence="ECO:0007829|PDB:6IY2"
FT   HELIX           905..911
FT                   /evidence="ECO:0007829|PDB:6IY2"
FT   STRAND          917..922
FT                   /evidence="ECO:0007829|PDB:6IY2"
FT   STRAND          929..933
FT                   /evidence="ECO:0007829|PDB:6IY2"
FT   HELIX           934..937
FT                   /evidence="ECO:0007829|PDB:6IY2"
FT   TURN            938..940
FT                   /evidence="ECO:0007829|PDB:6IY2"
FT   HELIX           944..947
FT                   /evidence="ECO:0007829|PDB:6IY2"
FT   TURN            948..952
FT                   /evidence="ECO:0007829|PDB:6IY2"
FT   HELIX           953..956
FT                   /evidence="ECO:0007829|PDB:6IY2"
FT   TURN            957..959
FT                   /evidence="ECO:0007829|PDB:6IY2"
FT   HELIX           970..974
FT                   /evidence="ECO:0007829|PDB:6IY2"
FT   HELIX           977..986
FT                   /evidence="ECO:0007829|PDB:6IY2"
FT   TURN            996..1000
FT                   /evidence="ECO:0007829|PDB:6IY2"
FT   STRAND          1007..1013
FT                   /evidence="ECO:0007829|PDB:6IY2"
FT   TURN            1017..1020
FT                   /evidence="ECO:0007829|PDB:6IY2"
FT   HELIX           1021..1030
FT                   /evidence="ECO:0007829|PDB:6IY2"
FT   HELIX           1051..1060
FT                   /evidence="ECO:0007829|PDB:6IY2"
FT   STRAND          1064..1066
FT                   /evidence="ECO:0007829|PDB:6IY2"
FT   HELIX           1069..1072
FT                   /evidence="ECO:0007829|PDB:6IY2"
FT   TURN            1080..1082
FT                   /evidence="ECO:0007829|PDB:6IY2"
FT   HELIX           1087..1102
FT                   /evidence="ECO:0007829|PDB:6IY2"
FT   STRAND          1106..1109
FT                   /evidence="ECO:0007829|PDB:6IY2"
FT   HELIX           1113..1125
FT                   /evidence="ECO:0007829|PDB:6IY2"
FT   STRAND          1130..1132
FT                   /evidence="ECO:0007829|PDB:6IY2"
FT   HELIX           1140..1149
FT                   /evidence="ECO:0007829|PDB:6IY2"
FT   STRAND          1158..1160
FT                   /evidence="ECO:0007829|PDB:6IY2"
FT   STRAND          1177..1182
FT                   /evidence="ECO:0007829|PDB:6IY2"
FT   STRAND          1185..1187
FT                   /evidence="ECO:0007829|PDB:6IY2"
FT   HELIX           1188..1197
FT                   /evidence="ECO:0007829|PDB:6IY2"
FT   STRAND          1207..1213
FT                   /evidence="ECO:0007829|PDB:6IY2"
FT   HELIX           1217..1228
FT                   /evidence="ECO:0007829|PDB:6IY2"
FT   HELIX           1233..1238
FT                   /evidence="ECO:0007829|PDB:6IY2"
FT   HELIX           1240..1242
FT                   /evidence="ECO:0007829|PDB:6IY2"
FT   TURN            1247..1251
FT                   /evidence="ECO:0007829|PDB:6IY2"
FT   HELIX           1252..1258
FT                   /evidence="ECO:0007829|PDB:6IY2"
FT   TURN            1259..1262
FT                   /evidence="ECO:0007829|PDB:6IY2"
FT   HELIX           1264..1268
FT                   /evidence="ECO:0007829|PDB:6IY2"
FT   HELIX           1280..1286
FT                   /evidence="ECO:0007829|PDB:6IY2"
FT   HELIX           1291..1306
FT                   /evidence="ECO:0007829|PDB:6IY2"
FT   HELIX           1338..1345
FT                   /evidence="ECO:0007829|PDB:6IY2"
SQ   SEQUENCE   1703 AA;  194051 MW;  84B8BC595C8F3E6D CRC64;
     MNIPQRQFSN EEVNRCYLRW QHLRNEHGMN APSVPEFIYL TKVLQFAAKQ RQELQMQRQQ
     QGISGSQQNI VPNSSDQAEL PNNASSHISA SASPHLAPNM QLNGNETFST SAHQSPIMQT
     QMPLNSNGGN NMLPQRQSSV GSLNATNFSP TPANNGENAA EKPDNSNHNN LNLNNSELQP
     QNRSLQEHNI QDSNVMPGSQ INSPMPQQAQ MQQAQFQAQQ AQQAQQAQQA QQAQARLQQG
     RRLPMTMFTA EQSELLKAQI TSLKCLVNRK PIPFEFQAVI QKSINHPPDF KRMLLSLSEF
     ARRRQPTDQN NQSNLNGGNN TQQPGTNSHY NNTNTDNVSG LTRNAPLDSK DENFASVSPA
     GPSSVHNAKN GTLDKNSQTV SGTPITQTES KKEENETISN VAKTAPNSNK THTEQNNPPK
     PQKPVPLNVL QDQYKEGIKV VDIDDPDMMV DSFTMPNISH SNIDYQTLLA NSDHAKFTIE
     PGVLPVGIDT HTATDIYQTL IALNLDTTVN DCLDKLLNDE CTESTRENAL YDYYALQLLP
     LQKAVRGHVL QFEWHQNSLL TNTHPNFLSK IRNINVQDAL LTNQLYKNHE LLKLERKKTE
     AVARLKSMNK SAINQYNRRQ DKKNKRLKFG HRLIATHTNL ERDEQKRAEK KAKERLQALK
     ANDEEAYIKL LDQTKDTRIT HLLRQTNAFL DSLTRAVKDQ QKYTKEMIDS HIKEASEEVD
     DLSMVPKMKD EEYDDDDDNS NVDYYNVAHR IKEDIKKQPS ILVGGTLKDY QIKGLQWMVS
     LFNNHLNGIL ADEMGLGKTI QTISLLTYLY EMKNIRGPYL VIVPLSTLSN WSSEFAKWAP
     TLRTISFKGS PNERKAKQAK IRAGEFDVVL TTFEYIIKER ALLSKVKWVH MIIDEGHRMK
     NAQSKLSLTL NTHYHADYRL ILTGTPLQNN LPELWALLNF VLPKIFNSVK SFDEWFNTPF
     ANTGGQDKIE LSEEETLLVI RRLHKVLRPF LLRRLKKDVE KELPDKVEKV VKCKMSALQQ
     IMYQQMLKYR RLFIGDQNNK KMVGLRGFNN QIMQLKKICN HPFVFEEVED QINPTRETND
     DIWRVAGKFE LLDRILPKLK ATGHRVLIFF QMTQIMDIME DFLRYINIKY LRLDGHTKSD
     ERSELLRLFN APDSEYLCFI LSTRAGGLGL NLQTADTVII FDTDWNPHQD LQAQDRAHRI
     GQKNEVRILR LITTNSVEEV ILERAYKKLD IDGKVIQAGK FDNKSTSEEQ EALLRSLLDA
     EEERRKKRES GVEEEEELKD SEINEILARN DEEMAVLTRM DEDRSKKEEE LGVKSRLLEK
     SELPDIYSRD IGAELKREES ESAAVYNGRG ARERKTATYN DNMSEEQWLR QFEVSDDEKN
     DKQARKQRTK KEDKSEAIDG NGEIKGENID ADNDGPRINN ISAEDRADTD LAMNDDDFLS
     KKRKAGRPRG RPKKVKLEGS ENSEPPALES SPVTGDNSPS EDFMDIPKPR TAGKTSVKSA
     RTSTRGRGRG RGRGRGRGRG RGRPPKARNG LDYVRTPAAA TSPIDIREKV AKQALDLYHF
     ALNYENEAGR KLSDIFLSKP SKALYPDYYM IIKYPVAFDN INTHIETLAY NSLKETLQDF
     HLIFSNARIY NTEGSVVYED SLELEKVVTK KYCEIMGDNS QLDFTEFDEQ YGTRPLVLPP
     VVTSSVAESF TDEADSSMTE ASV
//