RLA0_YEAST
ID RLA0_YEAST Reviewed; 312 AA.
AC P05317; D6VYX8;
DT 01-NOV-1988, integrated into UniProtKB/Swiss-Prot.
DT 05-OCT-2010, sequence version 2.
DT 03-AUG-2022, entry version 208.
DE RecName: Full=60S acidic ribosomal protein P0 {ECO:0000303|PubMed:9559554};
DE Short=A0;
DE AltName: Full=L10e;
DE AltName: Full=Large ribosomal subunit protein uL10 {ECO:0000303|PubMed:24524803};
GN Name=RPP0 {ECO:0000303|PubMed:9559554}; Synonyms=L10E, RPA0, RPL10E, RPLA0;
GN OrderedLocusNames=YLR340W; ORFNames=L8300.8;
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 [MRNA].
RC STRAIN=IFO 40028;
RX PubMed=3287327; DOI=10.1093/nar/16.8.3573;
RA Mitsui K., Tsurugi K.;
RT "cDNA and deduced amino acid sequence of 38 kDa-type acidic ribosomal
RT protein A0 from Saccharomyces cerevisiae.";
RL Nucleic Acids Res. 16:3573-3573(1988).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=2681177; DOI=10.1093/oxfordjournals.jbchem.a122836;
RA Mitsui K., Nakagawa T., Tsurugi K.;
RT "The gene and the primary structure of acidic ribosomal protein A0 from
RT yeast Saccharomyces cerevisiae which shows partial homology to bacterial
RT ribosomal protein L10.";
RL J. Biochem. 106:223-227(1989).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=SR26-12C;
RX PubMed=2404943; DOI=10.1128/jb.172.2.579-588.1990;
RA Newton C.H., Shimmin L.C., Yee J., Dennis P.P.;
RT "A family of genes encode the multiple forms of the Saccharomyces
RT cerevisiae ribosomal proteins equivalent to the Escherichia coli L12
RT protein and a single form of the L10-equivalent ribosomal protein.";
RL J. Bacteriol. 172:579-588(1990).
RN [4]
RP ERRATUM OF PUBMED:2404943.
RX PubMed=2188966; DOI=10.1128/jb.172.6.3535.1990;
RA Newton C.H., Shimmin L.C., Yee J., Dennis P.P.;
RL J. Bacteriol. 172:3535-3535(1990).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169871;
RA Johnston M., Hillier L.W., Riles L., Albermann K., Andre B., Ansorge W.,
RA Benes V., Brueckner M., Delius H., Dubois E., Duesterhoeft A.,
RA Entian K.-D., Floeth M., Goffeau A., Hebling U., Heumann K.,
RA Heuss-Neitzel D., Hilbert H., Hilger F., Kleine K., Koetter P., Louis E.J.,
RA Messenguy F., Mewes H.-W., Miosga T., Moestl D., Mueller-Auer S.,
RA Nentwich U., Obermaier B., Piravandi E., Pohl T.M., Portetelle D.,
RA Purnelle B., Rechmann S., Rieger M., Rinke M., Rose M., Scharfe M.,
RA Scherens B., Scholler P., Schwager C., Schwarz S., Underwood A.P.,
RA Urrestarazu L.A., Vandenbol M., Verhasselt P., Vierendeels F., Voet M.,
RA Volckaert G., Voss H., Wambutt R., Wedler E., Wedler H., Zimmermann F.K.,
RA Zollner A., Hani J., Hoheisel J.D.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XII.";
RL Nature 387:87-90(1997).
RN [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 NOMENCLATURE, AND SUBUNIT.
RX PubMed=9559554;
RX DOI=10.1002/(sici)1097-0061(19980330)14:5<471::aid-yea241>3.0.co;2-u;
RA Planta R.J., Mager W.H.;
RT "The list of cytoplasmic ribosomal proteins of Saccharomyces cerevisiae.";
RL Yeast 14:471-477(1998).
RN [8]
RP PHOSPHORYLATION AT SER-302.
RX PubMed=9843429; DOI=10.1021/bi981396i;
RA Rodriguez-Gabriel M.A., Remacha M., Ballesta J.P.G.;
RT "Phosphorylation of ribosomal protein P0 is not essential for ribosome
RT function but can affect translation.";
RL Biochemistry 37:16620-16626(1998).
RN [9]
RP INTERACTION WITH YFL034W.
RX PubMed=15286401; DOI=10.1007/bf02702559;
RA Aruna K., Chakraborty T., Nambeesan S., Mannan A.B., Sehgal A.,
RA Balachandara S.R., Sharma S.;
RT "Identification of a hypothetical membrane protein interactor of ribosomal
RT phosphoprotein P0.";
RL J. Biosci. 29:33-43(2004).
RN [10]
RP INTERACTION WITH RPP1A; RPP1B; RPP2A AND RPP2B.
RX PubMed=16573688; DOI=10.1111/j.1365-2958.2006.05117.x;
RA Krokowski D., Boguszewska A., Abramczyk D., Liljas A., Tchorzewski M.,
RA Grankowski N.;
RT "Yeast ribosomal P0 protein has two separate binding sites for P1/P2
RT proteins.";
RL Mol. Microbiol. 60:386-400(2006).
RN [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-302, 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 [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-302, AND IDENTIFICATION BY
RP 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 [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-68 AND SER-302, 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 [14]
RP UBIQUITINATION [LARGE SCALE ANALYSIS] AT LYS-14; LYS-97 AND LYS-144, AND
RP IDENTIFICATION BY 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 [15]
RP NOMENCLATURE.
RX PubMed=24524803; DOI=10.1016/j.sbi.2014.01.002;
RA Ban N., Beckmann R., Cate J.H.D., Dinman J.D., Dragon F., Ellis S.R.,
RA Lafontaine D.L.J., Lindahl L., Liljas A., Lipton J.M., McAlear M.A.,
RA Moore P.B., Noller H.F., Ortega J., Panse V.G., Ramakrishnan V.,
RA Spahn C.M.T., Steitz T.A., Tchorzewski M., Tollervey D., Warren A.J.,
RA Williamson J.R., Wilson D., Yonath A., Yusupov M.;
RT "A new system for naming ribosomal proteins.";
RL Curr. Opin. Struct. Biol. 24:165-169(2014).
RN [16]
RP X-RAY CRYSTALLOGRAPHY (4.00 ANGSTROMS).
RX PubMed=21109664; DOI=10.1126/science.1194294;
RA Ben-Shem A., Jenner L., Yusupova G., Yusupov M.;
RT "Crystal structure of the eukaryotic ribosome.";
RL Science 330:1203-1209(2010).
RN [17]
RP X-RAY CRYSTALLOGRAPHY (3.00 ANGSTROMS), SUBUNIT, AND SUBCELLULAR LOCATION.
RX PubMed=22096102; DOI=10.1126/science.1212642;
RA Ben-Shem A., Garreau de Loubresse N., Melnikov S., Jenner L., Yusupova G.,
RA Yusupov M.;
RT "The structure of the eukaryotic ribosome at 3.0 A resolution.";
RL Science 334:1524-1529(2011).
CC -!- FUNCTION: Component of the ribosome, a large ribonucleoprotein complex
CC responsible for the synthesis of proteins in the cell. The small
CC ribosomal subunit (SSU) binds messenger RNAs (mRNAs) and translates the
CC encoded message by selecting cognate aminoacyl-transfer RNA (tRNA)
CC molecules. The large subunit (LSU) contains the ribosomal catalytic
CC site termed the peptidyl transferase center (PTC), which catalyzes the
CC formation of peptide bonds, thereby polymerizing the amino acids
CC delivered by tRNAs into a polypeptide chain. The nascent polypeptides
CC leave the ribosome through a tunnel in the LSU and interact with
CC protein factors that function in enzymatic processing, targeting, and
CC the membrane insertion of nascent chains at the exit of the ribosomal
CC tunnel. uL10 forms part of the P stalk that participates in recruiting
CC G proteins to the ribosome. {ECO:0000305|PubMed:22096102}.
CC -!- SUBUNIT: Component of the large ribosomal subunit (LSU). Mature yeast
CC ribosomes consist of a small (40S) and a large (60S) subunit. The 40S
CC small subunit contains 1 molecule of ribosomal RNA (18S rRNA) and 33
CC different proteins (encoded by 57 genes). The large 60S subunit
CC contains 3 rRNA molecules (25S, 5.8S and 5S rRNA) and 46 different
CC proteins (encoded by 81 genes) (PubMed:9559554, PubMed:22096102). The 5
CC acidic ribosomal P-proteins form the stalk structure of the 60S
CC subunit. They are organized as a pentameric complex in which uL10/P0
CC interacts with 2 heterodimers, P1A-P2B and P1B-P2A. uL10 directly
CC interacts with 28S rRNA (PubMed:16573688). uL10 interacts with YFL034W
CC (PubMed:15286401). {ECO:0000269|PubMed:15286401,
CC ECO:0000269|PubMed:16573688, ECO:0000269|PubMed:22096102,
CC ECO:0000305|PubMed:9559554}.
CC -!- INTERACTION:
CC P05317; P32324: EFT2; NbExp=3; IntAct=EBI-15447, EBI-6333;
CC P05317; P05318: RPP1A; NbExp=3; IntAct=EBI-15447, EBI-15452;
CC P05317; P10622: RPP1B; NbExp=2; IntAct=EBI-15447, EBI-15460;
CC P05317; P05319: RPP2A; NbExp=2; IntAct=EBI-15447, EBI-15456;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:22096102}.
CC -!- SIMILARITY: Belongs to the universal ribosomal protein uL10 family.
CC {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; X06959; CAA30029.1; -; mRNA.
DR EMBL; D00529; BAA00415.1; -; Genomic_DNA.
DR EMBL; X13328; CAA31703.1; -; Genomic_DNA.
DR EMBL; M26506; AAA34730.1; -; Genomic_DNA.
DR EMBL; M37326; AAA34729.1; -; Genomic_DNA.
DR EMBL; U19028; AAB67258.1; -; Genomic_DNA.
DR EMBL; BK006945; DAA09644.1; -; Genomic_DNA.
DR PIR; S51343; R5BY0E.
DR RefSeq; NP_013444.1; NM_001182229.1.
DR PDB; 3J16; EM; -; G=1-312.
DR PDB; 3J77; EM; 6.20 A; P0=1-312.
DR PDB; 3J78; EM; 6.30 A; P0=1-312.
DR PDB; 4U3M; X-ray; 3.00 A; p0=2-311.
DR PDB; 4U3N; X-ray; 3.20 A; p0=2-312.
DR PDB; 4U3U; X-ray; 2.90 A; p0=2-312.
DR PDB; 4U4N; X-ray; 3.10 A; p0=2-312.
DR PDB; 4U4O; X-ray; 3.60 A; p0=2-312.
DR PDB; 4U4Q; X-ray; 3.00 A; p0=2-312.
DR PDB; 4U4R; X-ray; 2.80 A; p0=2-312.
DR PDB; 4U4U; X-ray; 3.00 A; p0=2-312.
DR PDB; 4U4Y; X-ray; 3.20 A; p0=2-312.
DR PDB; 4U4Z; X-ray; 3.10 A; p0=2-312.
DR PDB; 4U50; X-ray; 3.20 A; p0=2-312.
DR PDB; 4U51; X-ray; 3.20 A; p0=2-312.
DR PDB; 4U52; X-ray; 3.00 A; p0=2-312.
DR PDB; 4U53; X-ray; 3.30 A; p0=2-312.
DR PDB; 4U55; X-ray; 3.20 A; p0=2-312.
DR PDB; 4U56; X-ray; 3.45 A; p0=2-312.
DR PDB; 4U6F; X-ray; 3.10 A; p0=2-312.
DR PDB; 4V6I; EM; 8.80 A; Bs=1-312.
DR PDB; 4V7R; X-ray; 4.00 A; DM=1-312.
DR PDB; 4V88; X-ray; 3.00 A; Dq=1-312.
DR PDB; 4V8T; EM; 8.10 A; q=1-312.
DR PDB; 4V8Y; EM; 4.30 A; Bq=1-312.
DR PDB; 4V8Z; EM; 6.60 A; Bq=1-237.
DR PDB; 5APN; EM; 3.91 A; q=1-312.
DR PDB; 5APO; EM; 3.41 A; q=1-312.
DR PDB; 5DAT; X-ray; 3.15 A; p0=2-221.
DR PDB; 5DC3; X-ray; 3.25 A; p0=2-312.
DR PDB; 5DGE; X-ray; 3.45 A; p0=2-312.
DR PDB; 5DGV; X-ray; 3.10 A; p0=2-312.
DR PDB; 5FCI; X-ray; 3.40 A; p0=2-311.
DR PDB; 5FCJ; X-ray; 3.10 A; p0=2-312.
DR PDB; 5I4L; X-ray; 3.10 A; p0=1-312.
DR PDB; 5JUO; EM; 4.00 A; VA=1-312.
DR PDB; 5JUP; EM; 3.50 A; VA=1-312.
DR PDB; 5JUS; EM; 4.20 A; VA=1-312.
DR PDB; 5JUT; EM; 4.00 A; VA=1-312.
DR PDB; 5JUU; EM; 4.00 A; VA=1-312.
DR PDB; 5LYB; X-ray; 3.25 A; p0=3-198.
DR PDB; 5MEI; X-ray; 3.50 A; p0=2-221.
DR PDB; 5NDG; X-ray; 3.70 A; p0=1-312.
DR PDB; 5OBM; X-ray; 3.40 A; p0=1-312.
DR PDB; 5ON6; X-ray; 3.10 A; p0=2-312.
DR PDB; 5TBW; X-ray; 3.00 A; p0=3-221.
DR PDB; 5TGA; X-ray; 3.30 A; p0=3-221.
DR PDB; 6GQ1; EM; 4.40 A; P0=5-193.
DR PDB; 6GQB; EM; 3.90 A; P0=5-193.
DR PDB; 6GQV; EM; 4.00 A; P0=5-193.
DR PDB; 6HHQ; X-ray; 3.10 A; p0=1-312.
DR PDB; 6I7O; EM; 5.30 A; BU/YU=1-312.
DR PDB; 6OIG; EM; 3.80 A; q=3-198.
DR PDB; 6R84; EM; 3.60 A; r=3-199.
DR PDB; 6R86; EM; 3.40 A; r=3-199.
DR PDB; 6R87; EM; 3.40 A; r=3-199.
DR PDB; 6SV4; EM; 3.30 A; BU/YU/ZU=1-312.
DR PDB; 6T83; EM; 4.00 A; ba=2-312.
DR PDB; 6WOO; EM; 2.90 A; r=6-200.
DR PDBsum; 3J16; -.
DR PDBsum; 3J77; -.
DR PDBsum; 3J78; -.
DR PDBsum; 4U3M; -.
DR PDBsum; 4U3N; -.
DR PDBsum; 4U3U; -.
DR PDBsum; 4U4N; -.
DR PDBsum; 4U4O; -.
DR PDBsum; 4U4Q; -.
DR PDBsum; 4U4R; -.
DR PDBsum; 4U4U; -.
DR PDBsum; 4U4Y; -.
DR PDBsum; 4U4Z; -.
DR PDBsum; 4U50; -.
DR PDBsum; 4U51; -.
DR PDBsum; 4U52; -.
DR PDBsum; 4U53; -.
DR PDBsum; 4U55; -.
DR PDBsum; 4U56; -.
DR PDBsum; 4U6F; -.
DR PDBsum; 4V6I; -.
DR PDBsum; 4V7R; -.
DR PDBsum; 4V88; -.
DR PDBsum; 4V8T; -.
DR PDBsum; 4V8Y; -.
DR PDBsum; 4V8Z; -.
DR PDBsum; 5APN; -.
DR PDBsum; 5APO; -.
DR PDBsum; 5DAT; -.
DR PDBsum; 5DC3; -.
DR PDBsum; 5DGE; -.
DR PDBsum; 5DGV; -.
DR PDBsum; 5FCI; -.
DR PDBsum; 5FCJ; -.
DR PDBsum; 5I4L; -.
DR PDBsum; 5JUO; -.
DR PDBsum; 5JUP; -.
DR PDBsum; 5JUS; -.
DR PDBsum; 5JUT; -.
DR PDBsum; 5JUU; -.
DR PDBsum; 5LYB; -.
DR PDBsum; 5MEI; -.
DR PDBsum; 5NDG; -.
DR PDBsum; 5OBM; -.
DR PDBsum; 5ON6; -.
DR PDBsum; 5TBW; -.
DR PDBsum; 5TGA; -.
DR PDBsum; 6GQ1; -.
DR PDBsum; 6GQB; -.
DR PDBsum; 6GQV; -.
DR PDBsum; 6HHQ; -.
DR PDBsum; 6I7O; -.
DR PDBsum; 6OIG; -.
DR PDBsum; 6R84; -.
DR PDBsum; 6R86; -.
DR PDBsum; 6R87; -.
DR PDBsum; 6SV4; -.
DR PDBsum; 6T83; -.
DR PDBsum; 6WOO; -.
DR AlphaFoldDB; P05317; -.
DR SMR; P05317; -.
DR BioGRID; 31602; 382.
DR ComplexPortal; CPX-1601; 60S cytosolic large ribosomal subunit.
DR DIP; DIP-1582N; -.
DR IntAct; P05317; 289.
DR MINT; P05317; -.
DR STRING; 4932.YLR340W; -.
DR iPTMnet; P05317; -.
DR SWISS-2DPAGE; P05317; -.
DR MaxQB; P05317; -.
DR PaxDb; P05317; -.
DR PRIDE; P05317; -.
DR TopDownProteomics; P05317; -.
DR EnsemblFungi; YLR340W_mRNA; YLR340W; YLR340W.
DR GeneID; 851052; -.
DR KEGG; sce:YLR340W; -.
DR SGD; S000004332; RPP0.
DR VEuPathDB; FungiDB:YLR340W; -.
DR eggNOG; KOG0815; Eukaryota.
DR GeneTree; ENSGT00390000017839; -.
DR HOGENOM; CLU_053173_1_1_1; -.
DR InParanoid; P05317; -.
DR OMA; MAHVAEW; -.
DR BioCyc; YEAST:G3O-32417-MON; -.
DR Reactome; R-SCE-156827; L13a-mediated translational silencing of Ceruloplasmin expression.
DR Reactome; R-SCE-1799339; SRP-dependent cotranslational protein targeting to membrane.
DR Reactome; R-SCE-72689; Formation of a pool of free 40S subunits.
DR Reactome; R-SCE-72706; GTP hydrolysis and joining of the 60S ribosomal subunit.
DR Reactome; R-SCE-975956; Nonsense Mediated Decay (NMD) independent of the Exon Junction Complex (EJC).
DR Reactome; R-SCE-975957; Nonsense Mediated Decay (NMD) enhanced by the Exon Junction Complex (EJC).
DR PRO; PR:P05317; -.
DR Proteomes; UP000002311; Chromosome XII.
DR RNAct; P05317; protein.
DR GO; GO:0030686; C:90S preribosome; HDA:SGD.
DR GO; GO:0005737; C:cytoplasm; IDA:SGD.
DR GO; GO:0022625; C:cytosolic large ribosomal subunit; IDA:SGD.
DR GO; GO:0070180; F:large ribosomal subunit rRNA binding; IDA:SGD.
DR GO; GO:0003735; F:structural constituent of ribosome; IDA:SGD.
DR GO; GO:0002181; P:cytoplasmic translation; IMP:SGD.
DR GO; GO:0000027; P:ribosomal large subunit assembly; IMP:SGD.
DR Gene3D; 3.30.70.1730; -; 1.
DR Gene3D; 3.90.105.20; -; 1.
DR InterPro; IPR030670; L10E_eukaryotes.
DR InterPro; IPR043141; Ribosomal_L10-like_sf.
DR InterPro; IPR001790; Ribosomal_L10P.
DR InterPro; IPR043164; RL10_insert_sf.
DR InterPro; IPR040637; RL10P_insert.
DR Pfam; PF00466; Ribosomal_L10; 1.
DR Pfam; PF17777; RL10P_insert; 1.
DR PIRSF; PIRSF039087; L10E; 1.
DR SUPFAM; SSF160369; SSF160369; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cytoplasm; Isopeptide bond; Phosphoprotein;
KW Reference proteome; Ribonucleoprotein; Ribosomal protein; Ubl conjugation.
FT CHAIN 1..312
FT /note="60S acidic ribosomal protein P0"
FT /id="PRO_0000154786"
FT REGION 199..230
FT /note="Interaction with P1A-P2B"
FT REGION 231..258
FT /note="Interaction with P1B-P2A"
FT REGION 278..312
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 292..312
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 68
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 302
FT /note="Phosphoserine; by CK2"
FT /evidence="ECO:0000269|PubMed:9843429,
FT ECO:0007744|PubMed:17330950, ECO:0007744|PubMed:18407956,
FT ECO:0007744|PubMed:19779198"
FT CROSSLNK 14
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0007744|PubMed:22106047"
FT CROSSLNK 97
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0007744|PubMed:22106047"
FT CROSSLNK 144
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0007744|PubMed:22106047"
FT CONFLICT 83
FT /note="N -> Y (in Ref. 1; CAA30029 and 2; BAA00415/
FT CAA31703)"
FT /evidence="ECO:0000305"
FT HELIX 4..21
FT /evidence="ECO:0007829|PDB:4U4R"
FT STRAND 23..29
FT /evidence="ECO:0007829|PDB:4U4R"
FT HELIX 35..43
FT /evidence="ECO:0007829|PDB:4U4R"
FT STRAND 46..48
FT /evidence="ECO:0007829|PDB:4U3U"
FT STRAND 50..53
FT /evidence="ECO:0007829|PDB:4U4R"
FT HELIX 56..64
FT /evidence="ECO:0007829|PDB:4U4R"
FT STRAND 68..70
FT /evidence="ECO:0007829|PDB:4U4R"
FT HELIX 72..74
FT /evidence="ECO:0007829|PDB:4U4R"
FT HELIX 77..79
FT /evidence="ECO:0007829|PDB:4U4R"
FT STRAND 82..89
FT /evidence="ECO:0007829|PDB:4U4R"
FT HELIX 93..102
FT /evidence="ECO:0007829|PDB:4U4R"
FT STRAND 186..194
FT /evidence="ECO:0007829|PDB:4U4R"
FT STRAND 195..197
FT /evidence="ECO:0007829|PDB:4U3M"
FT TURN 200..202
FT /evidence="ECO:0007829|PDB:4U4R"
FT HELIX 210..213
FT /evidence="ECO:0007829|PDB:4U4R"
FT TURN 214..219
FT /evidence="ECO:0007829|PDB:4U4R"
SQ SEQUENCE 312 AA; 33717 MW; 109ECC90F7C8B68E CRC64;
MGGIREKKAE YFAKLREYLE EYKSLFVVGV DNVSSQQMHE VRKELRGRAV VLMGKNTMVR
RAIRGFLSDL PDFEKLLPFV KGNVGFVFTN EPLTEIKNVI VSNRVAAPAR AGAVAPEDIW
VRAVNTGMEP GKTSFFQALG VPTKIARGTI EIVSDVKVVD AGNKVGQSEA SLLNLLNISP
FTFGLTVVQV YDNGQVFPSS ILDITDEELV SHFVSAVSTI ASISLAIGYP TLPSVGHTLI
NNYKDLLAVA IAASYHYPEI EDLVDRIENP EKYAAAAPAA TSAASGDAAP AEEAAAEEEE
ESDDDMGFGL FD
