RPAC2_YEAST
ID RPAC2_YEAST Reviewed; 142 AA.
AC P28000; D6W168;
DT 01-AUG-1992, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1992, sequence version 1.
DT 03-AUG-2022, entry version 204.
DE RecName: Full=DNA-directed RNA polymerases I and III subunit RPAC2;
DE Short=RNA polymerases I and III subunit AC2;
DE AltName: Full=AC19;
DE AltName: Full=DNA-directed RNA polymerases I and III 16 kDa polypeptide;
DE AltName: Full=RPA19;
GN Name=RPC19; OrderedLocusNames=YNL113W; ORFNames=N1937;
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], AND PARTIAL PROTEIN SEQUENCE.
RX PubMed=1869554; DOI=10.1016/s0021-9258(18)98616-3;
RA Dequard-Chablat M., Riva M., Carles C., Sentenac A.;
RT "RPC19, the gene for a subunit common to yeast RNA polymerases A (I) and C
RT (III).";
RL J. Biol. Chem. 266:15300-15307(1991).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=9090055;
RX DOI=10.1002/(sici)1097-0061(19970315)13:3<261::aid-yea64>3.0.co;2-l;
RA de Antoni A., D'Angelo M., Dal Pero F., Sartorello F., Pandolfo D.,
RA Pallavicini A., Lanfranchi G., Valle G.;
RT "The DNA sequence of cosmid 14-13b from chromosome XIV of Saccharomyces
RT cerevisiae reveals an unusually high number of overlapping open reading
RT frames.";
RL Yeast 13:261-266(1997).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169873;
RA Philippsen P., Kleine K., Poehlmann R., Duesterhoeft A., Hamberg K.,
RA Hegemann J.H., Obermaier B., Urrestarazu L.A., Aert R., Albermann K.,
RA Altmann R., Andre B., Baladron V., Ballesta J.P.G., Becam A.-M.,
RA Beinhauer J.D., Boskovic J., Buitrago M.J., Bussereau F., Coster F.,
RA Crouzet M., D'Angelo M., Dal Pero F., De Antoni A., del Rey F., Doignon F.,
RA Domdey H., Dubois E., Fiedler T.A., Fleig U., Floeth M., Fritz C.,
RA Gaillardin C., Garcia-Cantalejo J.M., Glansdorff N., Goffeau A.,
RA Gueldener U., Herbert C.J., Heumann K., Heuss-Neitzel D., Hilbert H.,
RA Hinni K., Iraqui Houssaini I., Jacquet M., Jimenez A., Jonniaux J.-L.,
RA Karpfinger-Hartl L., Lanfranchi G., Lepingle A., Levesque H., Lyck R.,
RA Maftahi M., Mallet L., Maurer C.T.C., Messenguy F., Mewes H.-W., Moestl D.,
RA Nasr F., Nicaud J.-M., Niedenthal R.K., Pandolfo D., Pierard A.,
RA Piravandi E., Planta R.J., Pohl T.M., Purnelle B., Rebischung C.,
RA Remacha M.A., Revuelta J.L., Rinke M., Saiz J.E., Sartorello F.,
RA Scherens B., Sen-Gupta M., Soler-Mira A., Urbanus J.H.M., Valle G.,
RA Van Dyck L., Verhasselt P., Vierendeels F., Vissers S., Voet M.,
RA Volckaert G., Wach A., Wambutt R., Wedler H., Zollner A., Hani J.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XIV and its
RT evolutionary implications.";
RL Nature 387:93-98(1997).
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 NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=17322287; DOI=10.1101/gr.6037607;
RA Hu Y., Rolfs A., Bhullar B., Murthy T.V.S., Zhu C., Berger M.F.,
RA Camargo A.A., Kelley F., McCarron S., Jepson D., Richardson A., Raphael J.,
RA Moreira D., Taycher E., Zuo D., Mohr S., Kane M.F., Williamson J.,
RA Simpson A.J.G., Bulyk M.L., Harlow E., Marsischky G., Kolodner R.D.,
RA LaBaer J.;
RT "Approaching a complete repository of sequence-verified protein-encoding
RT clones for Saccharomyces cerevisiae.";
RL Genome Res. 17:536-543(2007).
RN [6]
RP REVIEW ON THE RNA POL III COMPLEX.
RX PubMed=10384303; DOI=10.1101/sqb.1998.63.381;
RA Chedin S., Ferri M.L., Peyroche G., Andrau J.-C., Jourdain S., Lefebvre O.,
RA Werner M., Carles C., Sentenac A.;
RT "The yeast RNA polymerase III transcription machinery: a paradigm for
RT eukaryotic gene activation.";
RL Cold Spring Harb. Symp. Quant. Biol. 63:381-389(1998).
RN [7]
RP IDENTIFICATION IN THE RNA POL I COMPLEX.
RX PubMed=11717393; DOI=10.1073/pnas.231181398;
RA Fath S., Milkereit P., Peyroche G., Riva M., Carles C., Tschochner H.;
RT "Differential roles of phosphorylation in the formation of transcriptional
RT active RNA polymerase I.";
RL Proc. Natl. Acad. Sci. U.S.A. 98:14334-14339(2001).
RN [8]
RP INTERACTION WITH AC40.
RX PubMed=8516295; DOI=10.1073/pnas.90.12.5524;
RA Lalo D., Carles C., Sentenac A., Thuriaux P.;
RT "Interactions between three common subunits of yeast RNA polymerases I and
RT III.";
RL Proc. Natl. Acad. Sci. U.S.A. 90:5524-5528(1993).
RN [9]
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 [10]
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 [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-33, 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 THR-15 AND THR-33, AND
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 [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-15 AND THR-33, 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-134, 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 [15]
RP 3D-STRUCTURE MODELING OF THE POL III CORE COMPLEX.
RX PubMed=16818233; DOI=10.1016/j.molcel.2006.05.013;
RA Jasiak A.J., Armache K.J., Martens B., Jansen R.P., Cramer P.;
RT "Structural biology of RNA polymerase III: subcomplex C17/25 X-ray
RT structure and 11 subunit enzyme model.";
RL Mol. Cell 23:71-81(2006).
RN [16]
RP STRUCTURE BY ELECTRON MICROSCOPY (12.00 ANGSTROMS) OF THE POL I COMPLEX,
RP FUNCTION, AND SUBUNIT.
RX PubMed=18160037; DOI=10.1016/j.cell.2007.10.051;
RA Kuhn C.D., Geiger S.R., Baumli S., Gartmann M., Gerber J., Jennebach S.,
RA Mielke T., Tschochner H., Beckmann R., Cramer P.;
RT "Functional architecture of RNA polymerase I.";
RL Cell 131:1260-1272(2007).
RN [17]
RP X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS) OF THE POL I COMPLEX, FUNCTION, AND
RP SUBUNIT.
RX PubMed=24153184; DOI=10.1038/nature12636;
RA Fernandez-Tornero C., Moreno-Morcillo M., Rashid U.J., Taylor N.M.,
RA Ruiz F.M., Gruene T., Legrand P., Steuerwald U., Muller C.W.;
RT "Crystal structure of the 14-subunit RNA polymerase I.";
RL Nature 502:644-649(2013).
RN [18]
RP X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF THE POL I COMPLEX, FUNCTION, AND
RP SUBUNIT.
RX PubMed=24153182; DOI=10.1038/nature12712;
RA Engel C., Sainsbury S., Cheung A.C., Kostrewa D., Cramer P.;
RT "RNA polymerase I structure and transcription regulation.";
RL Nature 502:650-655(2013).
CC -!- FUNCTION: DNA-dependent RNA polymerases catalyze the transcription of
CC DNA into RNA using the four ribonucleoside triphosphates as substrates.
CC Common core component of RNA polymerases I and III which synthesize
CC ribosomal RNA precursors and small RNAs, such as 5S rRNA and tRNAs,
CC respectively. {ECO:0000269|PubMed:18160037,
CC ECO:0000269|PubMed:24153182, ECO:0000269|PubMed:24153184}.
CC -!- SUBUNIT: Component of the RNA polymerase I (Pol I) and RNA polymerase
CC III (Pol III) complexes. Component of the RNA polymerase I (Pol I)
CC complex consisting of 14 subunits: RPA135, RPA190, RPC40, RPA14, RPB5,
CC RPO26, RPA43, RPB8, RPA12, RPB10, RPC19, RPC10, RPA49 and RPA34. The
CC complex is composed of a horseshoe-shaped core containing ten subunits
CC (RPA135, RPA190, RPB5, RPO26, RPB8, RPB10, RPC10, RPA12, RPC19 and
CC RPC40) where RPA135 and RPA190 form the DNA-binding cleft. Outside of
CC the core, RPA14 and RPA43 form the stalk that mediates interactions
CC with transcription initiation factors and newly synthesized RNA.
CC Component of the RNA polymerase III (Pol III) complex consisting of 17
CC subunits. Directly interacts with the RPC40 subunit.
CC {ECO:0000269|PubMed:11717393, ECO:0000269|PubMed:18160037,
CC ECO:0000269|PubMed:24153182, ECO:0000269|PubMed:24153184,
CC ECO:0000269|PubMed:8516295}.
CC -!- INTERACTION:
CC P28000; P07703: RPC40; NbExp=5; IntAct=EBI-15846, EBI-15831;
CC -!- SUBCELLULAR LOCATION: Nucleus, nucleolus {ECO:0000269|PubMed:14562095}.
CC -!- MISCELLANEOUS: Present with 8680 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the archaeal Rpo11/eukaryotic RPB11/RPC19 RNA
CC polymerase subunit family. {ECO:0000305}.
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DR EMBL; M64991; AAA34998.1; -; Genomic_DNA.
DR EMBL; Z69382; CAA93394.1; -; Genomic_DNA.
DR EMBL; Z71390; CAA95994.1; -; Genomic_DNA.
DR EMBL; AY558001; AAS56327.1; -; Genomic_DNA.
DR EMBL; BK006947; DAA10434.1; -; Genomic_DNA.
DR PIR; A39418; A39418.
DR RefSeq; NP_014286.1; NM_001182951.1.
DR PDB; 4C2M; X-ray; 2.80 A; K/Z=1-142.
DR PDB; 4C3H; X-ray; 3.27 A; K=1-142.
DR PDB; 4C3I; X-ray; 3.00 A; K=1-142.
DR PDB; 4C3J; X-ray; 3.35 A; K=1-142.
DR PDB; 4YM7; X-ray; 5.50 A; AK/BK/CK/DK/EK/FK=1-142.
DR PDB; 5FJ8; EM; 3.90 A; K=1-142.
DR PDB; 5FJ9; EM; 4.60 A; K=1-142.
DR PDB; 5FJA; EM; 4.65 A; K=1-142.
DR PDB; 5G5L; EM; 4.80 A; K=1-142.
DR PDB; 5LMX; EM; 4.90 A; K=1-142.
DR PDB; 5M3F; EM; 3.80 A; K=1-142.
DR PDB; 5M3M; EM; 4.00 A; K=1-142.
DR PDB; 5M5W; EM; 3.80 A; K=1-142.
DR PDB; 5M5X; EM; 4.00 A; K=1-142.
DR PDB; 5M5Y; EM; 4.00 A; K=1-142.
DR PDB; 5M64; EM; 4.60 A; K=1-142.
DR PDB; 5N5Y; EM; 7.70 A; K=1-142.
DR PDB; 5N5Z; EM; 7.70 A; K=1-142.
DR PDB; 5N60; EM; 7.70 A; K=1-142.
DR PDB; 5N61; EM; 3.40 A; K=1-142.
DR PDB; 5OA1; EM; 4.40 A; K=1-142.
DR PDB; 5W5Y; EM; 3.80 A; K=1-142.
DR PDB; 5W64; EM; 4.20 A; K=1-142.
DR PDB; 5W65; EM; 4.30 A; K=1-142.
DR PDB; 5W66; EM; 3.90 A; K=1-142.
DR PDB; 6CNB; EM; 4.10 A; K=1-142.
DR PDB; 6CNC; EM; 4.10 A; K=1-142.
DR PDB; 6CND; EM; 4.80 A; K=1-142.
DR PDB; 6CNF; EM; 4.50 A; K=1-142.
DR PDB; 6EU0; EM; 4.00 A; K=1-142.
DR PDB; 6EU1; EM; 3.40 A; K=1-142.
DR PDB; 6EU2; EM; 3.40 A; K=1-142.
DR PDB; 6EU3; EM; 3.30 A; K=1-142.
DR PDB; 6F40; EM; 3.70 A; K=1-142.
DR PDB; 6F41; EM; 4.30 A; K=1-142.
DR PDB; 6F42; EM; 5.50 A; K=1-142.
DR PDB; 6F44; EM; 4.20 A; K=1-142.
DR PDB; 6H67; EM; 3.60 A; K=1-142.
DR PDB; 6H68; EM; 4.60 A; K=1-142.
DR PDB; 6HKO; EM; 3.42 A; K=1-142.
DR PDB; 6HLQ; EM; 3.18 A; K=1-142.
DR PDB; 6HLR; EM; 3.18 A; K=1-142.
DR PDB; 6HLS; EM; 3.21 A; K=1-142.
DR PDB; 6RQH; EM; 3.70 A; K=1-142.
DR PDB; 6RQL; EM; 2.90 A; K=1-142.
DR PDB; 6RQT; EM; 4.00 A; K=1-142.
DR PDB; 6RRD; EM; 3.10 A; K=1-142.
DR PDB; 6RUI; EM; 2.70 A; K=1-142.
DR PDB; 6RUO; EM; 3.50 A; K=1-142.
DR PDB; 6RWE; EM; 3.00 A; K=1-142.
DR PDB; 6TPS; EM; 3.54 A; K=1-142.
DR PDB; 6TUT; EM; 3.25 A; K=1-142.
DR PDBsum; 4C2M; -.
DR PDBsum; 4C3H; -.
DR PDBsum; 4C3I; -.
DR PDBsum; 4C3J; -.
DR PDBsum; 4YM7; -.
DR PDBsum; 5FJ8; -.
DR PDBsum; 5FJ9; -.
DR PDBsum; 5FJA; -.
DR PDBsum; 5G5L; -.
DR PDBsum; 5LMX; -.
DR PDBsum; 5M3F; -.
DR PDBsum; 5M3M; -.
DR PDBsum; 5M5W; -.
DR PDBsum; 5M5X; -.
DR PDBsum; 5M5Y; -.
DR PDBsum; 5M64; -.
DR PDBsum; 5N5Y; -.
DR PDBsum; 5N5Z; -.
DR PDBsum; 5N60; -.
DR PDBsum; 5N61; -.
DR PDBsum; 5OA1; -.
DR PDBsum; 5W5Y; -.
DR PDBsum; 5W64; -.
DR PDBsum; 5W65; -.
DR PDBsum; 5W66; -.
DR PDBsum; 6CNB; -.
DR PDBsum; 6CNC; -.
DR PDBsum; 6CND; -.
DR PDBsum; 6CNF; -.
DR PDBsum; 6EU0; -.
DR PDBsum; 6EU1; -.
DR PDBsum; 6EU2; -.
DR PDBsum; 6EU3; -.
DR PDBsum; 6F40; -.
DR PDBsum; 6F41; -.
DR PDBsum; 6F42; -.
DR PDBsum; 6F44; -.
DR PDBsum; 6H67; -.
DR PDBsum; 6H68; -.
DR PDBsum; 6HKO; -.
DR PDBsum; 6HLQ; -.
DR PDBsum; 6HLR; -.
DR PDBsum; 6HLS; -.
DR PDBsum; 6RQH; -.
DR PDBsum; 6RQL; -.
DR PDBsum; 6RQT; -.
DR PDBsum; 6RRD; -.
DR PDBsum; 6RUI; -.
DR PDBsum; 6RUO; -.
DR PDBsum; 6RWE; -.
DR PDBsum; 6TPS; -.
DR PDBsum; 6TUT; -.
DR AlphaFoldDB; P28000; -.
DR SMR; P28000; -.
DR BioGRID; 35712; 340.
DR ComplexPortal; CPX-1664; DNA-directed RNA Polymerase I complex.
DR ComplexPortal; CPX-2660; DNA-directed RNA polymerase III complex.
DR DIP; DIP-130N; -.
DR IntAct; P28000; 33.
DR MINT; P28000; -.
DR STRING; 4932.YNL113W; -.
DR iPTMnet; P28000; -.
DR MaxQB; P28000; -.
DR PaxDb; P28000; -.
DR PRIDE; P28000; -.
DR EnsemblFungi; YNL113W_mRNA; YNL113W; YNL113W.
DR GeneID; 855609; -.
DR KEGG; sce:YNL113W; -.
DR SGD; S000005057; RPC19.
DR VEuPathDB; FungiDB:YNL113W; -.
DR eggNOG; KOG3438; Eukaryota.
DR GeneTree; ENSGT00550000075160; -.
DR HOGENOM; CLU_090381_3_0_1; -.
DR InParanoid; P28000; -.
DR OMA; CGYTMPH; -.
DR BioCyc; YEAST:G3O-33137-MON; -.
DR PRO; PR:P28000; -.
DR Proteomes; UP000002311; Chromosome XIV.
DR RNAct; P28000; protein.
DR GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
DR GO; GO:0005634; C:nucleus; IDA:ComplexPortal.
DR GO; GO:0005736; C:RNA polymerase I complex; IDA:UniProtKB.
DR GO; GO:0005666; C:RNA polymerase III complex; IDA:SGD.
DR GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR GO; GO:0046983; F:protein dimerization activity; IEA:InterPro.
DR GO; GO:0001054; F:RNA polymerase I activity; IDA:UniProtKB.
DR GO; GO:0042790; P:nucleolar large rRNA transcription by RNA polymerase I; IDA:ComplexPortal.
DR GO; GO:0042254; P:ribosome biogenesis; IEA:UniProtKB-KW.
DR GO; GO:0006363; P:termination of RNA polymerase I transcription; IDA:ComplexPortal.
DR GO; GO:0006386; P:termination of RNA polymerase III transcription; IDA:ComplexPortal.
DR GO; GO:0006360; P:transcription by RNA polymerase I; IDA:UniProtKB.
DR GO; GO:0006383; P:transcription by RNA polymerase III; IDA:ComplexPortal.
DR GO; GO:0006362; P:transcription elongation from RNA polymerase I promoter; IDA:ComplexPortal.
DR GO; GO:0006361; P:transcription initiation from RNA polymerase I promoter; IDA:ComplexPortal.
DR GO; GO:0006384; P:transcription initiation from RNA polymerase III promoter; IDA:ComplexPortal.
DR GO; GO:0042797; P:tRNA transcription by RNA polymerase III; IDA:SGD.
DR CDD; cd07029; RNAP_I_III_AC19; 1.
DR Gene3D; 3.30.1360.10; -; 1.
DR HAMAP; MF_00261; RNApol_arch_Rpo11; 1.
DR InterPro; IPR036603; RBP11-like.
DR InterPro; IPR009025; RBP11-like_dimer.
DR InterPro; IPR008193; RNA_pol_Rpb11_13-16kDa_CS.
DR InterPro; IPR033898; RNAP_AC19.
DR Pfam; PF13656; RNA_pol_L_2; 1.
DR SUPFAM; SSF55257; SSF55257; 1.
DR PROSITE; PS01154; RNA_POL_L_13KD; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Direct protein sequencing; DNA-directed RNA polymerase;
KW Isopeptide bond; Nucleus; Phosphoprotein; Reference proteome;
KW Ribosome biogenesis; Transcription; Ubl conjugation.
FT CHAIN 1..142
FT /note="DNA-directed RNA polymerases I and III subunit
FT RPAC2"
FT /id="PRO_0000149319"
FT REGION 1..45
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..27
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 15
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:18407956,
FT ECO:0007744|PubMed:19779198"
FT MOD_RES 33
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:17330950,
FT ECO:0007744|PubMed:18407956, ECO:0007744|PubMed:19779198"
FT CROSSLNK 134
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0007744|PubMed:22106047"
FT STRAND 46..49
FT /evidence="ECO:0007829|PDB:6RUI"
FT TURN 51..53
FT /evidence="ECO:0007829|PDB:4C3I"
FT STRAND 56..67
FT /evidence="ECO:0007829|PDB:6RUI"
FT HELIX 70..80
FT /evidence="ECO:0007829|PDB:6RUI"
FT STRAND 86..92
FT /evidence="ECO:0007829|PDB:6RUI"
FT STRAND 96..98
FT /evidence="ECO:0007829|PDB:6RQL"
FT STRAND 100..107
FT /evidence="ECO:0007829|PDB:6RUI"
FT STRAND 109..111
FT /evidence="ECO:0007829|PDB:6RUI"
FT HELIX 113..139
FT /evidence="ECO:0007829|PDB:6RUI"
SQ SEQUENCE 142 AA; 16151 MW; 0B048299A787EEDB CRC64;
MTEDIEQKKT ATEVTPQEPK HIQEEEEQDV DMTGDEEQEE EPDREKIKLL TQATSEDGTS
ASFQIVEEDH TLGNALRYVI MKNPDVEFCG YSIPHPSENL LNIRIQTYGE TTAVDALQKG
LKDLMDLCDV VESKFTEKIK SM
