RS15_HUMAN
ID RS15_HUMAN Reviewed; 145 AA.
AC P62841; A5D8V9; P11174; Q3KRA1; Q9UDC2;
DT 16-AUG-2004, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 179.
DE RecName: Full=40S ribosomal protein S15;
DE AltName: Full=RIG protein;
DE AltName: Full=Small ribosomal subunit protein uS19 {ECO:0000303|PubMed:24524803};
GN Name=RPS15; Synonyms=RIG;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=2821540; DOI=10.1073/pnas.84.19.6659;
RA Inoue C., Shiga K., Takasawa S., Kitagawa M., Yamamoto H., Okamoto H.;
RT "Evolutionary conservation of the insulinoma gene rig and its possible
RT function.";
RL Proc. Natl. Acad. Sci. U.S.A. 84:6659-6662(1987).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=2159154; DOI=10.1073/pnas.87.9.3594;
RA Shiga K., Yamamoto H., Okamoto H.;
RT "Isolation and characterization of the human homologue of rig and its
RT pseudogenes: the functional gene has features characteristic of
RT housekeeping genes.";
RL Proc. Natl. Acad. Sci. U.S.A. 87:3594-3598(1990).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Yu L., Zhao S.Y.;
RT "Cloning and characterization of human insulinoma protein.";
RL Submitted (APR-1999) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Pancreas;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [5]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 11-145.
RC TISSUE=Brain;
RX PubMed=1466847; DOI=10.1097/00002030-199210000-00014;
RA Rosenblatt J.D., Tomkins P., Rosenthal M., Kacena A., Chan G.,
RA Valderama R., Harrington W. Jr., Saxton E., Diagne A., Zhao J.-Q.,
RA Mitsuyasu R.T., Weisbart R.H.;
RT "Progressive spastic myelopathy in a patient co-infected with HIV-1 and
RT HTLV-II: autoantibodies to the human homologue of rig in blood and
RT cerebrospinal fluid.";
RL AIDS 6:1151-1158(1992).
RN [6]
RP PROTEIN SEQUENCE OF 101-116.
RC TISSUE=Placenta;
RX PubMed=8706699; DOI=10.1111/j.1432-1033.1996.0144u.x;
RA Vladimirov S.N., Ivanov A.V., Karpova G.G., Musolyamov A.K., Egorov T.A.,
RA Thiede B., Wittmann-Liebold B., Otto A.;
RT "Characterization of the human small-ribosomal-subunit proteins by N-
RT terminal and internal sequencing, and mass spectrometry.";
RL Eur. J. Biochem. 239:144-149(1996).
RN [7]
RP IDENTIFICATION BY MASS SPECTROMETRY.
RC TISSUE=Lymphoblast;
RX PubMed=14654843; DOI=10.1038/nature02166;
RA Andersen J.S., Wilkinson C.J., Mayor T., Mortensen P., Nigg E.A., Mann M.;
RT "Proteomic characterization of the human centrosome by protein correlation
RT profiling.";
RL Nature 426:570-574(2003).
RN [8]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a
RT refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [9]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [10]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-terminal
RT acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN [11]
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 [12]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [13]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25944712; DOI=10.1002/pmic.201400617;
RA Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., Ayoub D.,
RA Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
RT "N-terminome analysis of the human mitochondrial proteome.";
RL Proteomics 15:2519-2524(2015).
RN [14]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-108, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=28112733; DOI=10.1038/nsmb.3366;
RA Hendriks I.A., Lyon D., Young C., Jensen L.J., Vertegaal A.C.,
RA Nielsen M.L.;
RT "Site-specific mapping of the human SUMO proteome reveals co-modification
RT with phosphorylation.";
RL Nat. Struct. Mol. Biol. 24:325-336(2017).
RN [15]
RP STRUCTURE BY ELECTRON MICROSCOPY (5.0 ANGSTROMS).
RX PubMed=23636399; DOI=10.1038/nature12104;
RA Anger A.M., Armache J.P., Berninghausen O., Habeck M., Subklewe M.,
RA Wilson D.N., Beckmann R.;
RT "Structures of the human and Drosophila 80S ribosome.";
RL Nature 497:80-85(2013).
CC -!- INTERACTION:
CC P62841; Q7L622: G2E3; NbExp=3; IntAct=EBI-372635, EBI-751757;
CC P62841; Q5S007: LRRK2; NbExp=9; IntAct=EBI-372635, EBI-5323863;
CC P62841; P62937: PPIA; NbExp=3; IntAct=EBI-372635, EBI-437708;
CC -!- SIMILARITY: Belongs to the universal ribosomal protein uS19 family.
CC {ECO:0000305}.
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DR EMBL; J02984; AAA36036.1; -; mRNA.
DR EMBL; M32405; AAA36568.1; -; Genomic_DNA.
DR EMBL; AF145025; AAP97277.1; -; mRNA.
DR EMBL; BC064908; AAH64908.1; -; mRNA.
DR EMBL; BC105810; AAI05811.1; -; mRNA.
DR EMBL; BC141832; AAI41833.1; -; mRNA.
DR CCDS; CCDS12067.1; -.
DR PIR; A35908; R3HU15.
DR RefSeq; NP_001009.1; NM_001018.4.
DR PDB; 4UG0; EM; -; SP=1-145.
DR PDB; 4V6X; EM; 5.00 A; AP=1-145.
DR PDB; 5A2Q; EM; 3.90 A; P=1-145.
DR PDB; 5AJ0; EM; 3.50 A; BP=1-145.
DR PDB; 5FLX; EM; 3.90 A; P=1-145.
DR PDB; 5LKS; EM; 3.60 A; SP=1-145.
DR PDB; 5OA3; EM; 4.30 A; P=1-145.
DR PDB; 5T2C; EM; 3.60 A; Ax=1-145.
DR PDB; 5VYC; X-ray; 6.00 A; P1/P2/P3/P4/P5/P6=1-145.
DR PDB; 6FEC; EM; 6.30 A; n=4-130.
DR PDB; 6G18; EM; 3.60 A; P=1-145.
DR PDB; 6G4S; EM; 4.00 A; P=1-145.
DR PDB; 6G4W; EM; 4.50 A; P=1-145.
DR PDB; 6G51; EM; 4.10 A; P=1-145.
DR PDB; 6G53; EM; 4.50 A; P=1-145.
DR PDB; 6G5H; EM; 3.60 A; P=1-145.
DR PDB; 6G5I; EM; 3.50 A; P=1-145.
DR PDB; 6IP5; EM; 3.90 A; 2w=1-145.
DR PDB; 6IP6; EM; 4.50 A; 2w=1-145.
DR PDB; 6IP8; EM; 3.90 A; 2w=1-145.
DR PDB; 6OLE; EM; 3.10 A; SP=10-136.
DR PDB; 6OLF; EM; 3.90 A; SP=10-136.
DR PDB; 6OLG; EM; 3.40 A; BP=12-131.
DR PDB; 6OLI; EM; 3.50 A; SP=10-136.
DR PDB; 6OLZ; EM; 3.90 A; BP=12-131.
DR PDB; 6OM0; EM; 3.10 A; SP=10-136.
DR PDB; 6OM7; EM; 3.70 A; SP=10-136.
DR PDB; 6QZP; EM; 2.90 A; SP=10-136.
DR PDB; 6XA1; EM; 2.80 A; SP=13-143.
DR PDB; 6Y0G; EM; 3.20 A; SP=1-145.
DR PDB; 6Y2L; EM; 3.00 A; SP=1-145.
DR PDB; 6Y57; EM; 3.50 A; SP=1-145.
DR PDB; 6YBS; EM; 3.10 A; b=1-145.
DR PDB; 6Z6L; EM; 3.00 A; SP=1-145.
DR PDB; 6Z6M; EM; 3.10 A; SP=1-145.
DR PDB; 6Z6N; EM; 2.90 A; SP=1-145.
DR PDB; 6ZLW; EM; 2.60 A; Q=1-145.
DR PDB; 6ZM7; EM; 2.70 A; SP=1-145.
DR PDB; 6ZME; EM; 3.00 A; SP=1-145.
DR PDB; 6ZMI; EM; 2.60 A; SP=1-145.
DR PDB; 6ZMO; EM; 3.10 A; SP=1-145.
DR PDB; 6ZMT; EM; 3.00 A; Q=1-145.
DR PDB; 6ZMW; EM; 3.70 A; b=1-145.
DR PDB; 6ZN5; EM; 3.20 A; Q=15-134.
DR PDB; 6ZOJ; EM; 2.80 A; P=1-145.
DR PDB; 6ZOL; EM; 2.80 A; P=1-145.
DR PDB; 6ZON; EM; 3.00 A; o=1-145.
DR PDB; 6ZP4; EM; 2.90 A; o=1-145.
DR PDB; 6ZUO; EM; 3.10 A; P=1-145.
DR PDB; 6ZV6; EM; 2.90 A; P=1-145.
DR PDB; 6ZVH; EM; 2.90 A; P=10-138.
DR PDB; 6ZVJ; EM; 3.80 A; o=15-133.
DR PDB; 6ZXD; EM; 3.20 A; P=1-145.
DR PDB; 6ZXE; EM; 3.00 A; P=1-145.
DR PDB; 6ZXF; EM; 3.70 A; P=1-145.
DR PDB; 6ZXG; EM; 2.60 A; P=1-145.
DR PDB; 6ZXH; EM; 2.70 A; P=1-145.
DR PDB; 7A09; EM; 3.50 A; o=1-145.
DR PDB; 7K5I; EM; 2.90 A; P=1-145.
DR PDBsum; 4UG0; -.
DR PDBsum; 4V6X; -.
DR PDBsum; 5A2Q; -.
DR PDBsum; 5AJ0; -.
DR PDBsum; 5FLX; -.
DR PDBsum; 5LKS; -.
DR PDBsum; 5OA3; -.
DR PDBsum; 5T2C; -.
DR PDBsum; 5VYC; -.
DR PDBsum; 6FEC; -.
DR PDBsum; 6G18; -.
DR PDBsum; 6G4S; -.
DR PDBsum; 6G4W; -.
DR PDBsum; 6G51; -.
DR PDBsum; 6G53; -.
DR PDBsum; 6G5H; -.
DR PDBsum; 6G5I; -.
DR PDBsum; 6IP5; -.
DR PDBsum; 6IP6; -.
DR PDBsum; 6IP8; -.
DR PDBsum; 6OLE; -.
DR PDBsum; 6OLF; -.
DR PDBsum; 6OLG; -.
DR PDBsum; 6OLI; -.
DR PDBsum; 6OLZ; -.
DR PDBsum; 6OM0; -.
DR PDBsum; 6OM7; -.
DR PDBsum; 6QZP; -.
DR PDBsum; 6XA1; -.
DR PDBsum; 6Y0G; -.
DR PDBsum; 6Y2L; -.
DR PDBsum; 6Y57; -.
DR PDBsum; 6YBS; -.
DR PDBsum; 6Z6L; -.
DR PDBsum; 6Z6M; -.
DR PDBsum; 6Z6N; -.
DR PDBsum; 6ZLW; -.
DR PDBsum; 6ZM7; -.
DR PDBsum; 6ZME; -.
DR PDBsum; 6ZMI; -.
DR PDBsum; 6ZMO; -.
DR PDBsum; 6ZMT; -.
DR PDBsum; 6ZMW; -.
DR PDBsum; 6ZN5; -.
DR PDBsum; 6ZOJ; -.
DR PDBsum; 6ZOL; -.
DR PDBsum; 6ZON; -.
DR PDBsum; 6ZP4; -.
DR PDBsum; 6ZUO; -.
DR PDBsum; 6ZV6; -.
DR PDBsum; 6ZVH; -.
DR PDBsum; 6ZVJ; -.
DR PDBsum; 6ZXD; -.
DR PDBsum; 6ZXE; -.
DR PDBsum; 6ZXF; -.
DR PDBsum; 6ZXG; -.
DR PDBsum; 6ZXH; -.
DR PDBsum; 7A09; -.
DR PDBsum; 7K5I; -.
DR AlphaFoldDB; P62841; -.
DR SMR; P62841; -.
DR BioGRID; 112123; 311.
DR ComplexPortal; CPX-5223; 40S cytosolic small ribosomal subunit.
DR CORUM; P62841; -.
DR IntAct; P62841; 88.
DR MINT; P62841; -.
DR STRING; 9606.ENSP00000467466; -.
DR GlyGen; P62841; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; P62841; -.
DR MetOSite; P62841; -.
DR PhosphoSitePlus; P62841; -.
DR SwissPalm; P62841; -.
DR BioMuta; RPS15; -.
DR DMDM; 51338641; -.
DR EPD; P62841; -.
DR jPOST; P62841; -.
DR MassIVE; P62841; -.
DR MaxQB; P62841; -.
DR PaxDb; P62841; -.
DR PeptideAtlas; P62841; -.
DR PRIDE; P62841; -.
DR ProteomicsDB; 57433; -.
DR TopDownProteomics; P62841; -.
DR Antibodypedia; 22700; 220 antibodies from 28 providers.
DR DNASU; 6209; -.
DR Ensembl; ENST00000592588.7; ENSP00000467466.3; ENSG00000115268.10.
DR GeneID; 6209; -.
DR KEGG; hsa:6209; -.
DR MANE-Select; ENST00000592588.7; ENSP00000467466.3; NM_001018.5; NP_001009.1.
DR UCSC; uc002lsp.2; human.
DR CTD; 6209; -.
DR DisGeNET; 6209; -.
DR GeneCards; RPS15; -.
DR HGNC; HGNC:10388; RPS15.
DR HPA; ENSG00000115268; Low tissue specificity.
DR MalaCards; RPS15; -.
DR MIM; 180535; gene.
DR neXtProt; NX_P62841; -.
DR OpenTargets; ENSG00000115268; -.
DR Orphanet; 67038; B-cell chronic lymphocytic leukemia.
DR PharmGKB; PA34787; -.
DR VEuPathDB; HostDB:ENSG00000115268; -.
DR eggNOG; KOG0898; Eukaryota.
DR GeneTree; ENSGT00390000000475; -.
DR InParanoid; P62841; -.
DR OMA; VIRTHCR; -.
DR PhylomeDB; P62841; -.
DR PathwayCommons; P62841; -.
DR Reactome; R-HSA-156827; L13a-mediated translational silencing of Ceruloplasmin expression.
DR Reactome; R-HSA-156902; Peptide chain elongation.
DR Reactome; R-HSA-1799339; SRP-dependent cotranslational protein targeting to membrane.
DR Reactome; R-HSA-192823; Viral mRNA Translation.
DR Reactome; R-HSA-2408557; Selenocysteine synthesis.
DR Reactome; R-HSA-6791226; Major pathway of rRNA processing in the nucleolus and cytosol.
DR Reactome; R-HSA-72649; Translation initiation complex formation.
DR Reactome; R-HSA-72689; Formation of a pool of free 40S subunits.
DR Reactome; R-HSA-72695; Formation of the ternary complex, and subsequently, the 43S complex.
DR Reactome; R-HSA-72702; Ribosomal scanning and start codon recognition.
DR Reactome; R-HSA-72706; GTP hydrolysis and joining of the 60S ribosomal subunit.
DR Reactome; R-HSA-72764; Eukaryotic Translation Termination.
DR Reactome; R-HSA-9010553; Regulation of expression of SLITs and ROBOs.
DR Reactome; R-HSA-9633012; Response of EIF2AK4 (GCN2) to amino acid deficiency.
DR Reactome; R-HSA-9754678; SARS-CoV-2 modulates host translation machinery.
DR Reactome; R-HSA-975956; Nonsense Mediated Decay (NMD) independent of the Exon Junction Complex (EJC).
DR Reactome; R-HSA-975957; Nonsense Mediated Decay (NMD) enhanced by the Exon Junction Complex (EJC).
DR SignaLink; P62841; -.
DR SIGNOR; P62841; -.
DR BioGRID-ORCS; 6209; 785 hits in 1031 CRISPR screens.
DR ChiTaRS; RPS15; human.
DR EvolutionaryTrace; P62841; -.
DR GeneWiki; RPS15; -.
DR GenomeRNAi; 6209; -.
DR Pharos; P62841; Tbio.
DR PRO; PR:P62841; -.
DR Proteomes; UP000005640; Chromosome 19.
DR RNAct; P62841; protein.
DR Bgee; ENSG00000115268; Expressed in pituitary gland and 99 other tissues.
DR ExpressionAtlas; P62841; baseline and differential.
DR Genevisible; P62841; HS.
DR GO; GO:0005737; C:cytoplasm; IC:ComplexPortal.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0022626; C:cytosolic ribosome; IDA:FlyBase.
DR GO; GO:0022627; C:cytosolic small ribosomal subunit; IDA:UniProtKB.
DR GO; GO:0005925; C:focal adhesion; HDA:UniProtKB.
DR GO; GO:0016020; C:membrane; HDA:UniProtKB.
DR GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
DR GO; GO:0005634; C:nucleus; NAS:UniProtKB.
DR GO; GO:0003677; F:DNA binding; NAS:UniProtKB.
DR GO; GO:0097371; F:MDM2/MDM4 family protein binding; IPI:FlyBase.
DR GO; GO:0003723; F:RNA binding; HDA:UniProtKB.
DR GO; GO:0003735; F:structural constituent of ribosome; IDA:FlyBase.
DR GO; GO:1990948; F:ubiquitin ligase inhibitor activity; IDA:FlyBase.
DR GO; GO:0002181; P:cytoplasmic translation; IC:FlyBase.
DR GO; GO:0001649; P:osteoblast differentiation; HDA:UniProtKB.
DR GO; GO:1901798; P:positive regulation of signal transduction by p53 class mediator; IDA:FlyBase.
DR GO; GO:0000028; P:ribosomal small subunit assembly; IBA:GO_Central.
DR GO; GO:0042274; P:ribosomal small subunit biogenesis; IMP:UniProtKB.
DR GO; GO:0000056; P:ribosomal small subunit export from nucleus; IMP:UniProtKB.
DR GO; GO:0006364; P:rRNA processing; IMP:UniProtKB.
DR GO; GO:0006412; P:translation; IC:UniProtKB.
DR Gene3D; 3.30.860.10; -; 1.
DR HAMAP; MF_00531; Ribosomal_S19; 1.
DR InterPro; IPR020934; Ribosomal_S15/S19_CS.
DR InterPro; IPR002222; Ribosomal_S19.
DR InterPro; IPR023575; Ribosomal_S19_S15_SF.
DR InterPro; IPR005713; Ribosomal_S19A/S15e.
DR PANTHER; PTHR11880; PTHR11880; 1.
DR Pfam; PF00203; Ribosomal_S19; 1.
DR PIRSF; PIRSF002144; Ribosomal_S19; 1.
DR PRINTS; PR00975; RIBOSOMALS19.
DR SUPFAM; SSF54570; SSF54570; 1.
DR TIGRFAMs; TIGR01025; uS19_arch; 1.
DR PROSITE; PS00323; RIBOSOMAL_S19; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Direct protein sequencing; Isopeptide bond;
KW Reference proteome; Ribonucleoprotein; Ribosomal protein; Ubl conjugation.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0007744|PubMed:19413330,
FT ECO:0007744|PubMed:22814378"
FT CHAIN 2..145
FT /note="40S ribosomal protein S15"
FT /id="PRO_0000130027"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0007744|PubMed:19413330,
FT ECO:0007744|PubMed:22814378"
FT CROSSLNK 108
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT STRAND 16..19
FT /evidence="ECO:0007829|PDB:6ZXH"
FT HELIX 22..26
FT /evidence="ECO:0007829|PDB:6ZLW"
FT HELIX 33..36
FT /evidence="ECO:0007829|PDB:6ZLW"
FT HELIX 39..47
FT /evidence="ECO:0007829|PDB:6ZLW"
FT HELIX 51..65
FT /evidence="ECO:0007829|PDB:6ZLW"
FT STRAND 69..71
FT /evidence="ECO:0007829|PDB:6ZV6"
FT STRAND 76..79
FT /evidence="ECO:0007829|PDB:6ZLW"
FT HELIX 87..89
FT /evidence="ECO:0007829|PDB:6ZLW"
FT STRAND 93..97
FT /evidence="ECO:0007829|PDB:6ZLW"
FT STRAND 99..106
FT /evidence="ECO:0007829|PDB:6ZLW"
FT HELIX 109..111
FT /evidence="ECO:0007829|PDB:6ZLW"
FT STRAND 112..115
FT /evidence="ECO:0007829|PDB:6ZV6"
FT HELIX 116..118
FT /evidence="ECO:0007829|PDB:6ZLW"
FT STRAND 133..136
FT /evidence="ECO:0007829|PDB:6ZVH"
FT HELIX 139..141
FT /evidence="ECO:0007829|PDB:6ZXG"
SQ SEQUENCE 145 AA; 17040 MW; CA2C682302C7B387 CRC64;
MAEVEQKKKR TFRKFTYRGV DLDQLLDMSY EQLMQLYSAR QRRRLNRGLR RKQHSLLKRL
RKAKKEAPPM EKPEVVKTHL RDMIILPEMV GSMVGVYNGK TFNQVEIKPE MIGHYLGEFS
ITYKPVKHGR PGIGATHSSR FIPLK
