RL18A_HUMAN
ID RL18A_HUMAN Reviewed; 176 AA.
AC Q02543;
DT 01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1995, sequence version 2.
DT 03-AUG-2022, entry version 206.
DE RecName: Full=60S ribosomal protein L18a;
DE AltName: Full=Large ribosomal subunit protein eL20 {ECO:0000303|PubMed:24524803};
GN Name=RPL18A;
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].
RA Bhat K.S.;
RL Submitted (NOV-1992) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Zenz K.I.;
RL Submitted (AUG-1994) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15057824; DOI=10.1038/nature02399;
RA Grimwood J., Gordon L.A., Olsen A.S., Terry A., Schmutz J., Lamerdin J.E.,
RA Hellsten U., Goodstein D., Couronne O., Tran-Gyamfi M., Aerts A.,
RA Altherr M., Ashworth L., Bajorek E., Black S., Branscomb E., Caenepeel S.,
RA Carrano A.V., Caoile C., Chan Y.M., Christensen M., Cleland C.A.,
RA Copeland A., Dalin E., Dehal P., Denys M., Detter J.C., Escobar J.,
RA Flowers D., Fotopulos D., Garcia C., Georgescu A.M., Glavina T., Gomez M.,
RA Gonzales E., Groza M., Hammon N., Hawkins T., Haydu L., Ho I., Huang W.,
RA Israni S., Jett J., Kadner K., Kimball H., Kobayashi A., Larionov V.,
RA Leem S.-H., Lopez F., Lou Y., Lowry S., Malfatti S., Martinez D.,
RA McCready P.M., Medina C., Morgan J., Nelson K., Nolan M., Ovcharenko I.,
RA Pitluck S., Pollard M., Popkie A.P., Predki P., Quan G., Ramirez L.,
RA Rash S., Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A.,
RA She X., Smith D., Slezak T., Solovyev V., Thayer N., Tice H., Tsai M.,
RA Ustaszewska A., Vo N., Wagner M., Wheeler J., Wu K., Xie G., Yang J.,
RA Dubchak I., Furey T.S., DeJong P., Dickson M., Gordon D., Eichler E.E.,
RA Pennacchio L.A., Richardson P., Stubbs L., Rokhsar D.S., Myers R.M.,
RA Rubin E.M., Lucas S.M.;
RT "The DNA sequence and biology of human chromosome 19.";
RL Nature 428:529-535(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain, and Muscle;
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 INTERACTION WITH IPO9.
RX PubMed=11823430; DOI=10.1093/emboj/21.3.377;
RA Jaekel S., Mingot J.-M., Schwarzmaier P., Hartmann E., Goerlich D.;
RT "Importins fulfill a dual function as nuclear import receptors and
RT cytoplasmic chaperones for exposed basic domains.";
RL EMBO J. 21:377-386(2002).
RN [6]
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 [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-63, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=15592455; DOI=10.1038/nbt1046;
RA Rush J., Moritz A., Lee K.A., Guo A., Goss V.L., Spek E.J., Zhang H.,
RA Zha X.-M., Polakiewicz R.D., Comb M.J.;
RT "Immunoaffinity profiling of tyrosine phosphorylation in cancer cells.";
RL Nat. Biotechnol. 23:94-101(2005).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-71, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-71, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19369195; DOI=10.1074/mcp.m800588-mcp200;
RA Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G.,
RA Mann M., Daub H.;
RT "Large-scale proteomics analysis of the human kinome.";
RL Mol. Cell. Proteomics 8:1751-1764(2009).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-71, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Leukemic T-cell;
RX PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA Rodionov V., Han D.K.;
RT "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT reveals system-wide modulation of protein-protein interactions.";
RL Sci. Signal. 2:RA46-RA46(2009).
RN [11]
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 [12]
RP IDENTIFICATION BY MASS SPECTROMETRY [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 [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-71, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [14]
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 [15]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-11, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25218447; DOI=10.1038/nsmb.2890;
RA Hendriks I.A., D'Souza R.C., Yang B., Verlaan-de Vries M., Mann M.,
RA Vertegaal A.C.;
RT "Uncovering global SUMOylation signaling networks in a site-specific
RT manner.";
RL Nat. Struct. Mol. Biol. 21:927-936(2014).
RN [16]
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 [17]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-128 AND LYS-170, AND
RP IDENTIFICATION BY MASS 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 [18]
RP STRUCTURE BY ELECTRON MICROSCOPY (5.0 ANGSTROMS), FUNCTION, SUBUNIT, AND
RP SUBCELLULAR LOCATION.
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).
RN [19] {ECO:0007744|PDB:6LQM, ECO:0007744|PDB:6LSR, ECO:0007744|PDB:6LSS, ECO:0007744|PDB:6LU8}
RP STRUCTURE BY ELECTRON MICROSCOPY (3.09 ANGSTROMS), FUNCTION, AND SUBUNIT.
RX PubMed=32669547; DOI=10.1038/s41467-020-17237-x;
RA Liang X., Zuo M.Q., Zhang Y., Li N., Ma C., Dong M.Q., Gao N.;
RT "Structural snapshots of human pre-60S ribosomal particles before and after
RT nuclear export.";
RL Nat. Commun. 11:3542-3542(2020).
CC -!- FUNCTION: Component of the large ribosomal subunit. The ribosome is a
CC large ribonucleoprotein complex responsible for the synthesis of
CC proteins in the cell. {ECO:0000269|PubMed:23636399,
CC ECO:0000269|PubMed:32669547}.
CC -!- SUBUNIT: Component of the large ribosomal subunit (PubMed:23636399,
CC PubMed:32669547). Binds IPO9 with high affinity (PubMed:11823430).
CC {ECO:0000269|PubMed:11823430, ECO:0000269|PubMed:23636399,
CC ECO:0000269|PubMed:32669547}.
CC -!- INTERACTION:
CC Q02543; P36578: RPL4; NbExp=2; IntAct=EBI-350523, EBI-348313;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:23636399}.
CC -!- SIMILARITY: Belongs to the eukaryotic ribosomal protein eL20 family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAA56788.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; L05093; AAC18781.1; -; mRNA.
DR EMBL; X80822; CAA56788.1; ALT_FRAME; mRNA.
DR EMBL; AC005796; AAC62828.1; -; Genomic_DNA.
DR EMBL; BC007512; AAH07512.1; -; mRNA.
DR EMBL; BC066319; AAH66319.1; -; mRNA.
DR EMBL; BC071920; AAH71920.1; -; mRNA.
DR CCDS; CCDS12367.1; -.
DR PIR; S47353; S47353.
DR RefSeq; NP_000971.1; NM_000980.3.
DR PDB; 4UG0; EM; -; LS=1-176.
DR PDB; 4V6X; EM; 5.00 A; CS=1-176.
DR PDB; 5AJ0; EM; 3.50 A; AS=1-176.
DR PDB; 5LKS; EM; 3.60 A; LS=1-176.
DR PDB; 5T2C; EM; 3.60 A; M=1-176.
DR PDB; 6IP5; EM; 3.90 A; 2M=1-176.
DR PDB; 6IP6; EM; 4.50 A; 2M=1-176.
DR PDB; 6IP8; EM; 3.90 A; 2M=1-176.
DR PDB; 6LQM; EM; 3.09 A; b=1-176.
DR PDB; 6LSR; EM; 3.13 A; b=1-176.
DR PDB; 6LSS; EM; 3.23 A; b=1-176.
DR PDB; 6LU8; EM; 3.13 A; b=1-176.
DR PDB; 6OLE; EM; 3.10 A; T=1-175.
DR PDB; 6OLF; EM; 3.90 A; T=1-175.
DR PDB; 6OLG; EM; 3.40 A; AS=1-175.
DR PDB; 6OLI; EM; 3.50 A; T=1-175.
DR PDB; 6OLZ; EM; 3.90 A; AS=1-175.
DR PDB; 6OM0; EM; 3.10 A; T=1-175.
DR PDB; 6OM7; EM; 3.70 A; T=1-175.
DR PDB; 6QZP; EM; 2.90 A; LS=2-176.
DR PDB; 6W6L; EM; 3.84 A; T=1-176.
DR PDB; 6XA1; EM; 2.80 A; LS=2-176.
DR PDB; 6Y0G; EM; 3.20 A; LS=1-176.
DR PDB; 6Y2L; EM; 3.00 A; LS=1-176.
DR PDB; 6Y57; EM; 3.50 A; LS=1-176.
DR PDB; 6Y6X; EM; 2.80 A; LS=2-176.
DR PDB; 6Z6L; EM; 3.00 A; LS=1-176.
DR PDB; 6Z6M; EM; 3.10 A; LS=1-176.
DR PDB; 6Z6N; EM; 2.90 A; LS=1-176.
DR PDB; 6ZM7; EM; 2.70 A; LS=1-176.
DR PDB; 6ZME; EM; 3.00 A; LS=1-176.
DR PDB; 6ZMI; EM; 2.60 A; LS=1-176.
DR PDB; 6ZMO; EM; 3.10 A; LS=1-176.
DR PDB; 7BHP; EM; 3.30 A; LS=1-176.
DR PDBsum; 4UG0; -.
DR PDBsum; 4V6X; -.
DR PDBsum; 5AJ0; -.
DR PDBsum; 5LKS; -.
DR PDBsum; 5T2C; -.
DR PDBsum; 6IP5; -.
DR PDBsum; 6IP6; -.
DR PDBsum; 6IP8; -.
DR PDBsum; 6LQM; -.
DR PDBsum; 6LSR; -.
DR PDBsum; 6LSS; -.
DR PDBsum; 6LU8; -.
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; 6W6L; -.
DR PDBsum; 6XA1; -.
DR PDBsum; 6Y0G; -.
DR PDBsum; 6Y2L; -.
DR PDBsum; 6Y57; -.
DR PDBsum; 6Y6X; -.
DR PDBsum; 6Z6L; -.
DR PDBsum; 6Z6M; -.
DR PDBsum; 6Z6N; -.
DR PDBsum; 6ZM7; -.
DR PDBsum; 6ZME; -.
DR PDBsum; 6ZMI; -.
DR PDBsum; 6ZMO; -.
DR PDBsum; 7BHP; -.
DR AlphaFoldDB; Q02543; -.
DR SMR; Q02543; -.
DR BioGRID; 112062; 389.
DR ComplexPortal; CPX-5183; 60S cytosolic large ribosomal subunit.
DR CORUM; Q02543; -.
DR IntAct; Q02543; 156.
DR MINT; Q02543; -.
DR STRING; 9606.ENSP00000222247; -.
DR GlyGen; Q02543; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q02543; -.
DR MetOSite; Q02543; -.
DR PhosphoSitePlus; Q02543; -.
DR SwissPalm; Q02543; -.
DR BioMuta; RPL18A; -.
DR SWISS-2DPAGE; Q02543; -.
DR EPD; Q02543; -.
DR jPOST; Q02543; -.
DR MassIVE; Q02543; -.
DR MaxQB; Q02543; -.
DR PaxDb; Q02543; -.
DR PeptideAtlas; Q02543; -.
DR PRIDE; Q02543; -.
DR ProteomicsDB; 58108; -.
DR TopDownProteomics; Q02543; -.
DR Antibodypedia; 27861; 164 antibodies from 28 providers.
DR DNASU; 6142; -.
DR Ensembl; ENST00000222247.10; ENSP00000222247.4; ENSG00000105640.13.
DR GeneID; 6142; -.
DR KEGG; hsa:6142; -.
DR MANE-Select; ENST00000222247.10; ENSP00000222247.4; NM_000980.4; NP_000971.1.
DR UCSC; uc002nhp.4; human.
DR CTD; 6142; -.
DR DisGeNET; 6142; -.
DR GeneCards; RPL18A; -.
DR HGNC; HGNC:10311; RPL18A.
DR HPA; ENSG00000105640; Low tissue specificity.
DR MIM; 604178; gene.
DR neXtProt; NX_Q02543; -.
DR OpenTargets; ENSG00000105640; -.
DR PharmGKB; PA34680; -.
DR VEuPathDB; HostDB:ENSG00000105640; -.
DR eggNOG; KOG0829; Eukaryota.
DR GeneTree; ENSGT00390000015797; -.
DR HOGENOM; CLU_080773_2_0_1; -.
DR InParanoid; Q02543; -.
DR OMA; RFWYFMK; -.
DR OrthoDB; 1265349at2759; -.
DR PhylomeDB; Q02543; -.
DR TreeFam; TF300086; -.
DR PathwayCommons; Q02543; -.
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-72689; Formation of a pool of free 40S subunits.
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-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; Q02543; -.
DR SIGNOR; Q02543; -.
DR BioGRID-ORCS; 6142; 800 hits in 1046 CRISPR screens.
DR ChiTaRS; RPL18A; human.
DR GeneWiki; RPL18A; -.
DR GenomeRNAi; 6142; -.
DR Pharos; Q02543; Tbio.
DR PRO; PR:Q02543; -.
DR Proteomes; UP000005640; Chromosome 19.
DR RNAct; Q02543; protein.
DR Bgee; ENSG00000105640; Expressed in skin of leg and 109 other tissues.
DR ExpressionAtlas; Q02543; baseline and differential.
DR Genevisible; Q02543; HS.
DR GO; GO:0005737; C:cytoplasm; IC:ComplexPortal.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0022625; C:cytosolic large ribosomal subunit; IDA:UniProtKB.
DR GO; GO:0022626; C:cytosolic ribosome; IDA:FlyBase.
DR GO; GO:0016020; C:membrane; HDA:UniProtKB.
DR GO; GO:0042788; C:polysomal ribosome; IDA:UniProtKB.
DR GO; GO:0003723; F:RNA binding; HDA:UniProtKB.
DR GO; GO:0003735; F:structural constituent of ribosome; IDA:FlyBase.
DR GO; GO:0002181; P:cytoplasmic translation; IDA:UniProtKB.
DR GO; GO:0006412; P:translation; TAS:ProtInc.
DR HAMAP; MF_00273; Ribosomal_L18Ae; 1.
DR InterPro; IPR028877; 50S_L18Ae/Ribosomal_L18a/L20.
DR InterPro; IPR023573; Ribosomal_L18a//L18Ae/LX.
DR InterPro; IPR021138; Ribosomal_L18a/L20_eukaryotes.
DR PANTHER; PTHR10052; PTHR10052; 1.
DR Pfam; PF01775; Ribosomal_L18A; 1.
DR PIRSF; PIRSF002190; Ribosomal_L18a; 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..176
FT /note="60S ribosomal protein L18a"
FT /id="PRO_0000213925"
FT MOD_RES 63
FT /note="Phosphotyrosine"
FT /evidence="ECO:0007744|PubMed:15592455"
FT MOD_RES 71
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:19369195, ECO:0007744|PubMed:19690332,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 76
FT /note="N6-succinyllysine"
FT /evidence="ECO:0000250|UniProtKB:P62717"
FT MOD_RES 123
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P62717"
FT CROSSLNK 11
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:25218447"
FT CROSSLNK 128
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 170
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CONFLICT 83
FT /note="R -> S (in Ref. 2; CAA56788)"
FT /evidence="ECO:0000305"
FT CONFLICT 134
FT /note="A -> V (in Ref. 2; CAA56788)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 176 AA; 20762 MW; 5E501C6D835BE580 CRC64;
MKASGTLREY KVVGRCLPTP KCHTPPLYRM RIFAPNHVVA KSRFWYFVSQ LKKMKKSSGE
IVYCGQVFEK SPLRVKNFGI WLRYDSRSGT HNMYREYRDL TTAGAVTQCY RDMGARHRAR
AHSIQIMKVE EIAASKCRRP AVKQFHDSKI KFPLPHRVLR RQHKPRFTTK RPNTFF
