ID RS6_RABIT Reviewed; 249 AA. AC G1TM55; G1SJH6; DT 27-MAR-2024, integrated into UniProtKB/Swiss-Prot. DT 27-MAR-2024, sequence version 3. DT 27-MAR-2024, entry version 108. DE RecName: Full=Small ribosomal subunit protein eS6; DE AltName: Full=40S ribosomal protein S6; GN Name=RPS6; OS Oryctolagus cuniculus (Rabbit). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Glires; Lagomorpha; Leporidae; Oryctolagus. OX NCBI_TaxID=9986; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Thorbecke; RX PubMed=21993624; DOI=10.1038/nature10530; RA Lindblad-Toh K., Garber M., Zuk O., Lin M.F., Parker B.J., Washietl S., RA Kheradpour P., Ernst J., Jordan G., Mauceli E., Ward L.D., Lowe C.B., RA Holloway A.K., Clamp M., Gnerre S., Alfoldi J., Beal K., Chang J., RA Clawson H., Cuff J., Di Palma F., Fitzgerald S., Flicek P., Guttman M., RA Hubisz M.J., Jaffe D.B., Jungreis I., Kent W.J., Kostka D., Lara M., RA Martins A.L., Massingham T., Moltke I., Raney B.J., Rasmussen M.D., RA Robinson J., Stark A., Vilella A.J., Wen J., Xie X., Zody M.C., Baldwin J., RA Bloom T., Chin C.W., Heiman D., Nicol R., Nusbaum C., Young S., RA Wilkinson J., Worley K.C., Kovar C.L., Muzny D.M., Gibbs R.A., Cree A., RA Dihn H.H., Fowler G., Jhangiani S., Joshi V., Lee S., Lewis L.R., RA Nazareth L.V., Okwuonu G., Santibanez J., Warren W.C., Mardis E.R., RA Weinstock G.M., Wilson R.K., Delehaunty K., Dooling D., Fronik C., RA Fulton L., Fulton B., Graves T., Minx P., Sodergren E., Birney E., RA Margulies E.H., Herrero J., Green E.D., Haussler D., Siepel A., Goldman N., RA Pollard K.S., Pedersen J.S., Lander E.S., Kellis M.; RT "A high-resolution map of human evolutionary constraint using 29 mammals."; RL Nature 478:476-482(2011). RN [2] {ECO:0007744|PDB:4KZX, ECO:0007744|PDB:4KZY} RP X-RAY CRYSTALLOGRAPHY (7.01 ANGSTROMS) OF 40S RIBOSOME, FUNCTION, SUBUNIT, RP AND SUBCELLULAR LOCATION. RX PubMed=23873042; DOI=10.1038/nature12355; RA Lomakin I.B., Steitz T.A.; RT "The initiation of mammalian protein synthesis and mRNA scanning RT mechanism."; RL Nature 500:307-311(2013). RN [3] {ECO:0007744|PDB:4D5L, ECO:0007744|PDB:4D61} RP STRUCTURE BY ELECTRON MICROSCOPY (9.00 ANGSTROMS) OF RIBOSOME, FUNCTION, RP SUBUNIT, AND SUBCELLULAR LOCATION. RX PubMed=25601755; DOI=10.1016/j.molcel.2014.12.016; RA Muhs M., Hilal T., Mielke T., Skabkin M.A., Sanbonmatsu K.Y., Pestova T.V., RA Spahn C.M.; RT "Cryo-EM of ribosomal 80S complexes with termination factors reveals the RT translocated cricket paralysis virus IRES."; RL Mol. Cell 57:422-432(2015). RN [4] {ECO:0007744|PDB:3JAG, ECO:0007744|PDB:3JAH} RP STRUCTURE BY ELECTRON MICROSCOPY (3.45 ANGSTROMS) OF 1-235 OF RIBOSOME, RP FUNCTION, SUBCELLULAR LOCATION, AND SUBUNIT. RX PubMed=26245381; DOI=10.1038/nature14896; RA Brown A., Shao S., Murray J., Hegde R.S., Ramakrishnan V.; RT "Structural basis for stop codon recognition in eukaryotes."; RL Nature 524:493-496(2015). RN [5] {ECO:0007744|PDB:5LZS, ECO:0007744|PDB:5LZT} RP STRUCTURE BY ELECTRON MICROSCOPY (3.31 ANGSTROMS) OF RIBOSOME, FUNCTION, RP SUBCELLULAR LOCATION, AND SUBUNIT. RX PubMed=27863242; DOI=10.1016/j.cell.2016.10.046; RA Shao S., Murray J., Brown A., Taunton J., Ramakrishnan V., Hegde R.S.; RT "Decoding mammalian ribosome-mRNA states by translational GTPase RT complexes."; RL Cell 167:1229-1240(2016). RN [6] {ECO:0007744|PDB:6GZ3} RP STRUCTURE BY ELECTRON MICROSCOPY (3.60 ANGSTROMS) OF 1-230 OF RIBOSOME, RP FUNCTION, SUBCELLULAR LOCATION, AND SUBUNIT. RX PubMed=30517857; DOI=10.1016/j.celrep.2018.11.040; RA Flis J., Holm M., Rundlet E.J., Loerke J., Hilal T., Dabrowski M., RA Burger J., Mielke T., Blanchard S.C., Spahn C.M.T., Budkevich T.V.; RT "tRNA translocation by the eukaryotic 80S ribosome and the impact of GTP RT hydrolysis."; RL Cell Rep. 25:2676-2688(2018). RN [7] {ECO:0007744|PDB:6D90, ECO:0007744|PDB:6D9J} RP STRUCTURE BY ELECTRON MICROSCOPY (3.20 ANGSTROMS) OF RIBOSOME, SUBCELLULAR RP LOCATION, AND SUBUNIT. RX PubMed=29856316; DOI=10.7554/elife.34062; RA Pisareva V.P., Pisarev A.V., Fernandez I.S.; RT "Dual tRNA mimicry in the Cricket paralysis virus IRES uncovers an RT unexpected similarity with the Hepatitis C Virus IRES."; RL Elife 7:0-0(2018). RN [8] {ECO:0007744|PDB:6MTB, ECO:0007744|PDB:6MTC} RP STRUCTURE BY ELECTRON MICROSCOPY (3.30 ANGSTROMS) OF 1-235 OF RIBOSOME, RP SUBCELLULAR LOCATION, AND SUBUNIT. RX PubMed=30355441; DOI=10.7554/elife.40486; RA Brown A., Baird M.R., Yip M.C., Murray J., Shao S.; RT "Structures of translationally inactive mammalian ribosomes."; RL Elife 7:e40486-e40486(2018). RN [9] {ECO:0007744|PDB:6HCF, ECO:0007744|PDB:6HCJ} RP STRUCTURE BY ELECTRON MICROSCOPY (3.80 ANGSTROMS) OF RIBOSOME, SUBCELLULAR RP LOCATION, AND SUBUNIT. RX PubMed=30293783; DOI=10.1016/j.molcel.2018.08.037; RA Juszkiewicz S., Chandrasekaran V., Lin Z., Kraatz S., Ramakrishnan V., RA Hegde R.S.; RT "ZNF598 is a quality control sensor of collided ribosomes."; RL Mol. Cell 72:469-481(2018). RN [10] {ECO:0007744|PDB:6R5Q, ECO:0007744|PDB:6R6G} RP STRUCTURE BY ELECTRON MICROSCOPY (3.00 ANGSTROMS) OF 1-235 OF RIBOSOME, RP SUBCELLULAR LOCATION, AND SUBUNIT. RX PubMed=31246176; DOI=10.7554/elife.46267; RA Shanmuganathan V., Schiller N., Magoulopoulou A., Cheng J., Braunger K., RA Cymer F., Berninghausen O., Beatrix B., Kohno K., von Heijne G., RA Beckmann R.; RT "Structural and mutational analysis of the ribosome-arresting human RT XBP1u."; RL Elife 8:0-0(2019). RN [11] {ECO:0007744|PDB:6P4G, ECO:0007744|PDB:6P4H} RP STRUCTURE BY ELECTRON MICROSCOPY (3.10 ANGSTROMS) OF RIBOSOME, SUBUNIT, AND RP SUBCELLULAR LOCATION. RX PubMed=31609474; DOI=10.15252/embj.2019102226; RA Acosta-Reyes F., Neupane R., Frank J., Fernandez I.S.; RT "The Israeli acute paralysis virus IRES captures host ribosomes by RT mimicking a ribosomal state with hybrid tRNAs."; RL EMBO J. 38:e102226-e102226(2019). RN [12] {ECO:0007744|PDB:6SGC} RP STRUCTURE BY ELECTRON MICROSCOPY (2.80 ANGSTROMS) OF RIBOSOME, SUBCELLULAR RP LOCATION, AND SUBUNIT. RX PubMed=31768042; DOI=10.1038/s41594-019-0331-x; RA Chandrasekaran V., Juszkiewicz S., Choi J., Puglisi J.D., Brown A., RA Shao S., Ramakrishnan V., Hegde R.S.; RT "Mechanism of ribosome stalling during translation of a poly(A) tail."; RL Nat. Struct. Mol. Biol. 26:1132-1140(2019). RN [13] {ECO:0007744|PDB:6ZVK, ECO:0007744|PDB:7A01} RP STRUCTURE BY ELECTRON MICROSCOPY (3.49 ANGSTROMS) OF RIBOSOME, SUBCELLULAR RP LOCATION, AND SUBUNIT. RX PubMed=33296660; DOI=10.1016/j.celrep.2020.108476; RA Abaeva I.S., Vicens Q., Bochler A., Soufari H., Simonetti A., Pestova T.V., RA Hashem Y., Hellen C.U.T.; RT "The Halastavi arva virus intergenic region IRES promotes translation by RT the simplest possible initiation mechanism."; RL Cell Rep. 33:108476-108476(2020). RN [14] {ECO:0007744|PDB:6W2S, ECO:0007744|PDB:6W2T} RP STRUCTURE BY ELECTRON MICROSCOPY (3.00 ANGSTROMS) OF RIBOSOME, SUBUNIT, AND RP SUBCELLULAR LOCATION. RX PubMed=32286223; DOI=10.7554/elife.54575; RA Neupane R., Pisareva V.P., Rodriguez C.F., Pisarev A.V., Fernandez I.S.; RT "A complex IRES at the 5'-UTR of a viral mRNA assembles a functional 48S RT complex via an uAUG intermediate."; RL Elife 9:0-0(2020). RN [15] {ECO:0007744|PDB:7UCJ, ECO:0007744|PDB:7UCK} RP STRUCTURE BY ELECTRON MICROSCOPY (2.80 ANGSTROMS) OF RIBOSOME, SUBCELLULAR RP LOCATION, AND SUBUNIT. RX PubMed=35679869; DOI=10.1016/j.molcel.2022.05.016; RA Arango D., Sturgill D., Yang R., Kanai T., Bauer P., Roy J., Wang Z., RA Hosogane M., Schiffers S., Oberdoerffer S.; RT "Direct epitranscriptomic regulation of mammalian translation initiation RT through N4-acetylcytidine."; RL Mol. Cell 82:2797-2814(2022). RN [16] {ECO:0007744|PDB:7OYD} RP STRUCTURE BY ELECTRON MICROSCOPY (2.30 ANGSTROMS) OF RIBOSOME, SUBCELLULAR RP LOCATION, AND SUBUNIT. RX PubMed=36653451; DOI=10.1038/s41586-022-05623-y; RA Leesch F., Lorenzo-Orts L., Pribitzer C., Grishkovskaya I., Roehsner J., RA Chugunova A., Matzinger M., Roitinger E., Belacic K., Kandolf S., Lin T.Y., RA Mechtler K., Meinhart A., Haselbach D., Pauli A.; RT "A molecular network of conserved factors keeps ribosomes dormant in the RT egg."; RL Nature 613:712-720(2023). CC -!- FUNCTION: Component of the 40S small ribosomal subunit CC (PubMed:23873042, PubMed:25601755, PubMed:26245381, PubMed:27863242, CC PubMed:30517857). Plays an important role in controlling cell growth CC and proliferation through the selective translation of particular CC classes of mRNA (PubMed:23873042, PubMed:25601755, PubMed:26245381, CC PubMed:27863242, PubMed:30517857). Part of the small subunit (SSU) CC processome, first precursor of the small eukaryotic ribosomal subunit CC (PubMed:23873042, PubMed:25601755, PubMed:26245381, PubMed:27863242, CC PubMed:30517857). During the assembly of the SSU processome in the CC nucleolus, many ribosome biogenesis factors, an RNA chaperone and CC ribosomal proteins associate with the nascent pre-rRNA and work in CC concert to generate RNA folding, modifications, rearrangements and CC cleavage as well as targeted degradation of pre-ribosomal RNA by the CC RNA exosome (PubMed:23873042, PubMed:25601755, PubMed:26245381, CC PubMed:27863242, PubMed:30517857). {ECO:0000269|PubMed:23873042, CC ECO:0000269|PubMed:25601755, ECO:0000269|PubMed:26245381, CC ECO:0000269|PubMed:27863242, ECO:0000269|PubMed:30517857}. CC -!- SUBUNIT: Component of the small ribosomal subunit (PubMed:23873042, CC PubMed:25601755, PubMed:26245381, PubMed:27863242, PubMed:30517857, CC PubMed:29856316, PubMed:30355441, PubMed:30293783, PubMed:31246176, CC PubMed:31609474, PubMed:31768042, PubMed:33296660, PubMed:32286223, CC PubMed:35679869, PubMed:36653451). Part of the small subunit (SSU) CC processome, composed of more than 70 proteins and the RNA chaperone CC small nucleolar RNA (snoRNA) U3 (PubMed:23873042, PubMed:25601755, CC PubMed:26245381, PubMed:27863242, PubMed:30517857, PubMed:29856316, CC PubMed:30355441, PubMed:30293783, PubMed:31246176, PubMed:31609474, CC PubMed:31768042, PubMed:33296660, PubMed:32286223, PubMed:35679869, CC PubMed:36653451). {ECO:0000269|PubMed:23873042, CC ECO:0000269|PubMed:25601755, ECO:0000269|PubMed:26245381, CC ECO:0000269|PubMed:27863242, ECO:0000269|PubMed:29856316, CC ECO:0000269|PubMed:30293783, ECO:0000269|PubMed:30355441, CC ECO:0000269|PubMed:30517857, ECO:0000269|PubMed:31246176, CC ECO:0000269|PubMed:31609474, ECO:0000269|PubMed:31768042, CC ECO:0000269|PubMed:32286223, ECO:0000269|PubMed:33296660, CC ECO:0000269|PubMed:35679869, ECO:0000269|PubMed:36653451}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:23873042, CC ECO:0000269|PubMed:25601755, ECO:0000269|PubMed:26245381, CC ECO:0000269|PubMed:27863242, ECO:0000269|PubMed:29856316, CC ECO:0000269|PubMed:30293783, ECO:0000269|PubMed:30355441, CC ECO:0000269|PubMed:30517857, ECO:0000269|PubMed:31246176, CC ECO:0000269|PubMed:31609474, ECO:0000269|PubMed:31768042, CC ECO:0000269|PubMed:32286223, ECO:0000269|PubMed:33296660, CC ECO:0000269|PubMed:35679869, ECO:0000269|PubMed:36653451}. Nucleus, CC nucleolus {ECO:0000250|UniProtKB:P62753}. CC -!- PTM: Ribosomal protein S6 is the major substrate of protein kinases in CC eukaryote ribosomes. The phosphorylation is stimulated by growth CC factors, tumor promoting agents, and mitogens. It is dephosphorylated CC at growth arrest. Phosphorylated at Ser-235 and Ser-236 by RPS6KA1 and CC RPS6KA3; phosphorylation at these sites facilitates the assembly of the CC pre-initiation complex. {ECO:0000250|UniProtKB:P62753}. CC -!- PTM: Specifically hydroxylated (with R stereochemistry) at C-3 of Arg- CC 137 by KDM8. {ECO:0000250|UniProtKB:P62753}. CC -!- PTM: Mono-ADP-ribosylation at Glu-35 by PARP16 inhibits polysome CC assembly and mRNA loading, thereby inhibiting protein translation. CC {ECO:0000250|UniProtKB:P62753}. CC -!- SIMILARITY: Belongs to the eukaryotic ribosomal protein eS6 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 PDB; 3JAG; EM; 3.65 A; GG=1-201. DR PDB; 3JAH; EM; 3.45 A; GG=1-201. DR PDB; 3JAI; EM; 3.65 A; GG=1-201. DR PDB; 4D5L; EM; 9.00 A; G=1-201. DR PDB; 4D61; EM; 9.00 A; G=1-201. DR PDB; 4KZX; X-ray; 7.81 A; G=1-201. DR PDB; 4KZY; X-ray; 7.01 A; G=1-201. DR PDB; 4KZZ; X-ray; 7.03 A; G=1-201. DR PDB; 5K0Y; EM; 5.80 A; q=1-201. DR PDB; 5LZS; EM; 3.31 A; GG=1-201. DR PDB; 5LZT; EM; 3.65 A; GG=1-201. DR PDB; 5LZU; EM; 3.75 A; GG=1-201. DR PDB; 5LZV; EM; 3.35 A; GG=1-201. DR PDB; 5LZW; EM; 3.53 A; GG=1-201. DR PDB; 5LZX; EM; 3.67 A; GG=1-201. DR PDB; 5LZY; EM; 3.99 A; GG=1-201. DR PDB; 5LZZ; EM; 3.47 A; GG=1-201. DR PDB; 6D90; EM; 3.20 A; HH=1-201. DR PDB; 6D9J; EM; 3.20 A; HH=1-201. DR PDB; 6GZ3; EM; 3.60 A; BG=1-201. DR PDB; 6HCF; EM; 3.90 A; H1=1-201. DR PDB; 6HCJ; EM; 3.80 A; H2=1-201. DR PDB; 6HCM; EM; 6.80 A; H1=1-201. DR PDB; 6HCQ; EM; 6.50 A; H2=1-201. DR PDB; 6MTB; EM; 3.60 A; GG=1-201. DR PDB; 6MTC; EM; 3.40 A; GG=1-201. DR PDB; 6MTD; EM; 3.30 A; GG=1-201. DR PDB; 6MTE; EM; 3.40 A; GG=1-201. DR PDB; 6P4G; EM; 3.10 A; H=1-201. DR PDB; 6P4H; EM; 3.20 A; H=1-201. DR PDB; 6P5I; EM; 3.10 A; H=1-201. DR PDB; 6P5J; EM; 3.10 A; H=1-201. DR PDB; 6P5K; EM; 3.10 A; H=1-201. DR PDB; 6P5N; EM; 3.20 A; H=1-201. DR PDB; 6R5Q; EM; 3.00 A; z=1-201. DR PDB; 6R6G; EM; 3.70 A; z=1-201. DR PDB; 6R6P; EM; 3.10 A; z=1-201. DR PDB; 6R7Q; EM; 3.90 A; z=1-201. DR PDB; 6SGC; EM; 2.80 A; H1=1-201. DR PDB; 6W2S; EM; 3.00 A; H=1-201. DR PDB; 6W2T; EM; 3.36 A; H=1-201. DR PDB; 6YAM; EM; 3.60 A; I=1-201. DR PDB; 6ZVK; EM; 3.49 A; b3=1-201. DR PDB; 7A01; EM; 3.60 A; b3=1-201. DR PDB; 7MDZ; EM; 3.20 A; GG=1-201. DR PDB; 7O7Y; EM; 2.20 A; Af=1-201. DR PDB; 7O7Z; EM; 2.40 A; Af=1-201. DR PDB; 7O80; EM; 2.90 A; Af=1-201. DR PDB; 7O81; EM; 3.10 A; Af=1-201. DR PDB; 7OYD; EM; 2.30 A; GG=1-201. DR PDB; 7TOQ; EM; 3.10 A; AS06=1-201. DR PDB; 7TOR; EM; 2.90 A; AS06=1-201. DR PDB; 7UCJ; EM; 3.10 A; GG=1-201. DR PDB; 7UCK; EM; 2.80 A; GG=1-201. DR PDB; 8BHF; EM; 3.10 A; H3=1-201. DR PDB; 8BTK; EM; 3.50 A; Af=1-201. DR PDB; 8P2K; EM; 2.90 A; Af=1-201. DR PDBsum; 3JAG; -. DR PDBsum; 3JAH; -. DR PDBsum; 3JAI; -. DR PDBsum; 4D5L; -. DR PDBsum; 4D61; -. DR PDBsum; 4KZX; -. DR PDBsum; 4KZY; -. DR PDBsum; 4KZZ; -. DR PDBsum; 5K0Y; -. DR PDBsum; 5LZS; -. DR PDBsum; 5LZT; -. DR PDBsum; 5LZU; -. DR PDBsum; 5LZV; -. DR PDBsum; 5LZW; -. DR PDBsum; 5LZX; -. DR PDBsum; 5LZY; -. DR PDBsum; 5LZZ; -. DR PDBsum; 6D90; -. DR PDBsum; 6D9J; -. DR PDBsum; 6GZ3; -. DR PDBsum; 6HCF; -. DR PDBsum; 6HCJ; -. DR PDBsum; 6HCM; -. DR PDBsum; 6HCQ; -. DR PDBsum; 6MTB; -. DR PDBsum; 6MTC; -. DR PDBsum; 6MTD; -. DR PDBsum; 6MTE; -. DR PDBsum; 6P4G; -. DR PDBsum; 6P4H; -. DR PDBsum; 6P5I; -. DR PDBsum; 6P5J; -. DR PDBsum; 6P5K; -. DR PDBsum; 6P5N; -. DR PDBsum; 6R5Q; -. DR PDBsum; 6R6G; -. DR PDBsum; 6R6P; -. DR PDBsum; 6R7Q; -. DR PDBsum; 6SGC; -. DR PDBsum; 6W2S; -. DR PDBsum; 6W2T; -. DR PDBsum; 6YAM; -. DR PDBsum; 6ZVK; -. DR PDBsum; 7A01; -. DR PDBsum; 7MDZ; -. DR PDBsum; 7O7Y; -. DR PDBsum; 7O7Z; -. DR PDBsum; 7O80; -. DR PDBsum; 7O81; -. DR PDBsum; 7OYD; -. DR PDBsum; 7TOQ; -. DR PDBsum; 7TOR; -. DR PDBsum; 7UCJ; -. DR PDBsum; 7UCK; -. DR PDBsum; 8BHF; -. DR PDBsum; 8BTK; -. DR PDBsum; 8P2K; -. DR AlphaFoldDB; G1TM55; -. DR IntAct; G1TM55; 1. DR STRING; 9986.ENSOCUP00000018062; -. DR Ensembl; ENSOCUT00000030834.2; ENSOCUP00000018062.2; ENSOCUG00000025205.2. DR eggNOG; KOG1646; Eukaryota. DR HOGENOM; CLU_046346_0_1_1; -. DR InParanoid; G1TM55; -. DR TreeFam; TF300035; -. DR Proteomes; UP000001811; Unplaced. DR Bgee; ENSOCUG00000025205; Expressed in uterus and 10 other cell types or tissues. DR PROSITE; PS00578; RIBOSOMAL_S6E; 1. PE 1: Evidence at protein level; KW 3D-structure; Acetylation; ADP-ribosylation; Cytoplasm; Hydroxylation; KW Isopeptide bond; Nucleus; Phosphoprotein; Reference proteome; KW Ribonucleoprotein; Ribosomal protein; Ubl conjugation. FT CHAIN 1..249 FT /note="Small ribosomal subunit protein eS6" FT /id="PRO_0000460056" FT MOD_RES 35 FT /note="ADP-ribosyl glutamic acid" FT /evidence="ECO:0000250|UniProtKB:P62753" FT MOD_RES 137 FT /note="(3R)-3-hydroxyarginine" FT /evidence="ECO:0000250|UniProtKB:P62753" FT MOD_RES 148 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:P62753" FT MOD_RES 211 FT /note="N6-acetyllysine" FT /evidence="ECO:0000250|UniProtKB:P62753" FT MOD_RES 235 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:P62753" FT MOD_RES 236 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:P62753" FT MOD_RES 240 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:P62753" FT MOD_RES 242 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:P62753" FT MOD_RES 244 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:P62753" FT MOD_RES 247 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:P62753" FT CROSSLNK 14 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0000250|UniProtKB:P62753" SQ SEQUENCE 249 AA; 28681 MW; A61E435884E636AE CRC64; MKLNISFPAT GCQKLIEVDD ERKLRTFYEK RMATEVAADA LGEEWKGYVV RISGGNDKQG FPMKQGVLTH GRVRLLLSKG HSCYRPRRTG ERKRKSVRGC IVDANLSVLN LVIVKKGEKD IPGLTDTTVP RRLGPKRASR IRKLFNLSKE DDVRQYVVRK PLNKEGKKPR TKAPKIQRLV TPRVLQHKRR RIALKKQRTK KNKEEAAEYA KLLAKRMKEA KEKRQEQIAK RRRLSSLRAS TSKSESSQK //