ID RL13_HUMAN Reviewed; 211 AA. AC P26373; B4DLX3; F5H1S2; Q3KQT8; Q567Q8; Q9BPX0; DT 01-AUG-1992, integrated into UniProtKB/Swiss-Prot. DT 23-JAN-2007, sequence version 4. DT 28-MAR-2018, entry version 178. DE RecName: Full=60S ribosomal protein L13; DE AltName: Full=Breast basic conserved protein 1; DE AltName: Full=Large ribosomal subunit protein eL13 {ECO:0000303|PubMed:24524803}; GN Name=RPL13; Synonyms=BBC1; ORFNames=OK/SW-cl.46; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND VARIANT THR-112. RX PubMed=1301162; DOI=10.1093/hmg/1.2.91; RA Adams S.M., Helps N.R., Sharp M.G.F., Brammar W.J., Walker R.A., RA Varley J.M.; RT "Isolation and characterization of a novel gene with differential RT expression in benign and malignant human breast tumours."; RL Hum. Mol. Genet. 1:91-96(1992). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RC TISSUE=Colon adenocarcinoma; RA Shichijo S., Itoh K.; RT "Identification of immuno-peptidmics that are recognized by tumor- RT reactive CTL generated from TIL of colon cancer patients."; RL Submitted (MAY-2001) to the EMBL/GenBank/DDBJ databases. RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2). RC TISSUE=Brain; RX PubMed=14702039; DOI=10.1038/ng1285; RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S., RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., RA Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., RA Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.; RT "Complete sequencing and characterization of 21,243 full-length human RT cDNAs."; RL Nat. Genet. 36:40-45(2004). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=15616553; DOI=10.1038/nature03187; RA Martin J., Han C., Gordon L.A., Terry A., Prabhakar S., She X., RA Xie G., Hellsten U., Chan Y.M., Altherr M., Couronne O., Aerts A., RA Bajorek E., Black S., Blumer H., Branscomb E., Brown N.C., Bruno W.J., RA Buckingham J.M., Callen D.F., Campbell C.S., Campbell M.L., RA Campbell E.W., Caoile C., Challacombe J.F., Chasteen L.A., RA Chertkov O., Chi H.C., Christensen M., Clark L.M., Cohn J.D., RA Denys M., Detter J.C., Dickson M., Dimitrijevic-Bussod M., Escobar J., RA Fawcett J.J., Flowers D., Fotopulos D., Glavina T., Gomez M., RA Gonzales E., Goodstein D., Goodwin L.A., Grady D.L., Grigoriev I., RA Groza M., Hammon N., Hawkins T., Haydu L., Hildebrand C.E., Huang W., RA Israni S., Jett J., Jewett P.B., Kadner K., Kimball H., Kobayashi A., RA Krawczyk M.-C., Leyba T., Longmire J.L., Lopez F., Lou Y., Lowry S., RA Ludeman T., Manohar C.F., Mark G.A., McMurray K.L., Meincke L.J., RA Morgan J., Moyzis R.K., Mundt M.O., Munk A.C., Nandkeshwar R.D., RA Pitluck S., Pollard M., Predki P., Parson-Quintana B., Ramirez L., RA Rash S., Retterer J., Ricke D.O., Robinson D.L., Rodriguez A., RA Salamov A., Saunders E.H., Scott D., Shough T., Stallings R.L., RA Stalvey M., Sutherland R.D., Tapia R., Tesmer J.G., Thayer N., RA Thompson L.S., Tice H., Torney D.C., Tran-Gyamfi M., Tsai M., RA Ulanovsky L.E., Ustaszewska A., Vo N., White P.S., Williams A.L., RA Wills P.L., Wu J.-R., Wu K., Yang J., DeJong P., Bruce D., RA Doggett N.A., Deaven L., Schmutz J., Grimwood J., Richardson P., RA Rokhsar D.S., Eichler E.E., Gilna P., Lucas S.M., Myers R.M., RA Rubin E.M., Pennacchio L.A.; RT "The sequence and analysis of duplication-rich human chromosome 16."; RL Nature 432:988-994(2004). RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANT RP THR-112. RC TISSUE=Blood vessel, Brain, Cervix, Lung, Lymph, Pancreas, Placenta, RC and Uterus; 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 RT project: the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [6] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-77, AND IDENTIFICATION RP BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007; RA Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., RA Greff Z., Keri G., Stemmann O., Mann M.; RT "Kinase-selective enrichment enables quantitative phosphoproteomics of RT the kinome across the cell cycle."; RL Mol. Cell 31:438-448(2008). RN [7] RP IDENTIFICATION BY 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 [8] RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-16 AND LYS-177, AND RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=19608861; DOI=10.1126/science.1175371; RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., RA Walther T.C., Olsen J.V., Mann M.; RT "Lysine acetylation targets protein complexes and co-regulates major RT cellular functions."; RL Science 325:834-840(2009). RN [9] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-106, AND IDENTIFICATION RP BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=20068231; DOI=10.1126/scisignal.2000475; RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., RA Mann M.; RT "Quantitative phosphoproteomics reveals widespread full RT phosphorylation site occupancy during mitosis."; RL Sci. Signal. 3:RA3-RA3(2010). RN [10] 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., RA Buerckstuemmer T., 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 [11] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=21406692; DOI=10.1126/scisignal.2001570; RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., RA Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., RA Blagoev B.; RT "System-wide temporal characterization of the proteome and RT phosphoproteome of human embryonic stem cell differentiation."; RL Sci. Signal. 4:RS3-RS3(2011). RN [12] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-52; SER-77 AND SER-106, RP AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma, and 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 [13] 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 [14] RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-174, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=25114211; DOI=10.1073/pnas.1413825111; RA Impens F., Radoshevich L., Cossart P., Ribet D.; RT "Mapping of SUMO sites and analysis of SUMOylation changes induced by RT external stimuli."; RL Proc. Natl. Acad. Sci. U.S.A. 111:12432-12437(2014). RN [15] 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., RA Ayoub D., 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 [16] RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-123; LYS-145; LYS-174 AND RP LYS-177, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE RP 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- RT modification with phosphorylation."; RL Nat. Struct. Mol. Biol. 24:325-336(2017). RN [17] 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 Q8NHQ1:CEP70; NbExp=3; IntAct=EBI-356849, EBI-739624; CC Q5S007:LRRK2; NbExp=2; IntAct=EBI-356849, EBI-5323863; CC P16333:NCK1; NbExp=2; IntAct=EBI-356849, EBI-389883; CC P27986:PIK3R1; NbExp=2; IntAct=EBI-356849, EBI-79464; CC Q15554:TERF2; NbExp=2; IntAct=EBI-356849, EBI-706637; CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=1; CC IsoId=P26373-1; Sequence=Displayed; CC Name=2; CC IsoId=P26373-2; Sequence=VSP_046028; CC Note=No experimental confirmation available.; CC -!- TISSUE SPECIFICITY: Higher levels of expression in benign breast CC lesions than in carcinomas. CC -!- SIMILARITY: Belongs to the eukaryotic ribosomal protein eL13 CC family. {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; X64707; CAA45963.1; -; mRNA. DR EMBL; AB062392; BAB93479.1; -; mRNA. DR EMBL; AK297198; BAG59685.1; -; mRNA. DR EMBL; AC092123; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; BC004954; AAH04954.1; -; mRNA. DR EMBL; BC007345; AAH07345.1; -; mRNA. DR EMBL; BC007563; AAH07563.1; -; mRNA. DR EMBL; BC007805; AAH07805.1; -; mRNA. DR EMBL; BC010994; AAH10994.1; -; mRNA. DR EMBL; BC013078; AAH13078.1; -; mRNA. DR EMBL; BC014167; AAH14167.1; -; mRNA. DR EMBL; BC020804; AAH20804.1; -; mRNA. DR EMBL; BC027463; AAH27463.1; -; mRNA. DR EMBL; BC063378; AAH63378.1; -; mRNA. DR EMBL; BC093063; AAH93063.1; -; mRNA. DR EMBL; BC106058; AAI06059.1; -; mRNA. DR CCDS; CCDS10979.1; -. [P26373-1] DR CCDS; CCDS58492.1; -. [P26373-2] DR PIR; S23753; S23753. DR RefSeq; NP_000968.2; NM_000977.3. [P26373-1] DR RefSeq; NP_001230059.1; NM_001243130.1. DR RefSeq; NP_001230060.1; NM_001243131.1. [P26373-2] DR RefSeq; NP_150254.1; NM_033251.2. [P26373-1] DR UniGene; Hs.410817; -. DR PDB; 4UG0; EM; -; LL=1-211. DR PDB; 4V6X; EM; 5.00 A; CL=1-211. DR PDB; 5AJ0; EM; 3.50 A; AL=1-211. DR PDB; 5LKS; EM; 3.60 A; LL=1-211. DR PDB; 5T2C; EM; 3.60 A; r=1-211. DR PDB; 6EK0; EM; 2.90 A; LL=1-211. DR PDBsum; 4UG0; -. DR PDBsum; 4V6X; -. DR PDBsum; 5AJ0; -. DR PDBsum; 5LKS; -. DR PDBsum; 5T2C; -. DR PDBsum; 6EK0; -. DR ProteinModelPortal; P26373; -. DR SMR; P26373; -. DR BioGrid; 112057; 227. DR CORUM; P26373; -. DR IntAct; P26373; 53. DR MINT; P26373; -. DR STRING; 9606.ENSP00000307889; -. DR iPTMnet; P26373; -. DR PhosphoSitePlus; P26373; -. DR SwissPalm; P26373; -. DR BioMuta; RPL13; -. DR DMDM; 21903462; -. DR EPD; P26373; -. DR MaxQB; P26373; -. DR PaxDb; P26373; -. DR PeptideAtlas; P26373; -. DR PRIDE; P26373; -. DR TopDownProteomics; P26373-1; -. [P26373-1] DR TopDownProteomics; P26373-2; -. [P26373-2] DR DNASU; 6137; -. DR Ensembl; ENST00000311528; ENSP00000307889; ENSG00000167526. [P26373-1] DR Ensembl; ENST00000393099; ENSP00000376811; ENSG00000167526. [P26373-1] DR Ensembl; ENST00000452368; ENSP00000438959; ENSG00000167526. [P26373-2] DR Ensembl; ENST00000567815; ENSP00000455009; ENSG00000167526. [P26373-1] DR GeneID; 6137; -. DR KEGG; hsa:6137; -. DR UCSC; uc002fnm.3; human. [P26373-1] DR CTD; 6137; -. DR DisGeNET; 6137; -. DR EuPathDB; HostDB:ENSG00000167526.13; -. DR GeneCards; RPL13; -. DR HGNC; HGNC:10303; RPL13. DR HPA; HPA051702; -. DR MIM; 113703; gene. DR neXtProt; NX_P26373; -. DR OpenTargets; ENSG00000167526; -. DR PharmGKB; PA34670; -. DR eggNOG; KOG3295; Eukaryota. DR eggNOG; COG4352; LUCA. DR GeneTree; ENSGT00390000007818; -. DR HOGENOM; HOG000170452; -. DR HOVERGEN; HBG001156; -. DR InParanoid; P26373; -. DR KO; K02873; -. DR OMA; IVVDHRR; -. DR OrthoDB; EOG091G0KGO; -. DR PhylomeDB; P26373; -. DR TreeFam; TF300073; -. 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-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 ChiTaRS; RPL13; human. DR GeneWiki; RPL13; -. DR GenomeRNAi; 6137; -. DR PMAP-CutDB; P26373; -. DR PRO; PR:P26373; -. DR Proteomes; UP000005640; Chromosome 16. DR Bgee; ENSG00000167526; -. DR CleanEx; HS_RPL13; -. DR ExpressionAtlas; P26373; baseline and differential. DR Genevisible; P26373; HS. DR GO; GO:0005829; C:cytosol; IDA:HPA. DR GO; GO:0022625; C:cytosolic large ribosomal subunit; HDA:UniProtKB. DR GO; GO:0022626; C:cytosolic ribosome; TAS:ProtInc. DR GO; GO:0005783; C:endoplasmic reticulum; IDA:HPA. DR GO; GO:0016020; C:membrane; HDA:UniProtKB. DR GO; GO:0005730; C:nucleolus; IDA:HPA. DR GO; GO:0005634; C:nucleus; HDA:UniProtKB. DR GO; GO:0003723; F:RNA binding; HDA:UniProtKB. DR GO; GO:0003735; F:structural constituent of ribosome; IBA:GO_Central. DR GO; GO:0000184; P:nuclear-transcribed mRNA catabolic process, nonsense-mediated decay; TAS:Reactome. DR GO; GO:0006364; P:rRNA processing; TAS:Reactome. DR GO; GO:0006614; P:SRP-dependent cotranslational protein targeting to membrane; TAS:Reactome. DR GO; GO:0006412; P:translation; IBA:GO_Central. DR GO; GO:0006413; P:translational initiation; TAS:Reactome. DR GO; GO:0019083; P:viral transcription; TAS:Reactome. DR HAMAP; MF_00499; Ribosomal_L13e; 1. DR InterPro; IPR001380; Ribosomal_L13e. DR InterPro; IPR018256; Ribosomal_L13e_CS. DR PANTHER; PTHR11722; PTHR11722; 1. DR Pfam; PF01294; Ribosomal_L13e; 1. DR PROSITE; PS01104; RIBOSOMAL_L13E; 1. PE 1: Evidence at protein level; KW 3D-structure; Acetylation; Alternative splicing; Complete proteome; KW Isopeptide bond; Phosphoprotein; Polymorphism; Reference proteome; KW Ribonucleoprotein; Ribosomal protein; Ubl conjugation. FT CHAIN 1 211 60S ribosomal protein L13. FT /FTId=PRO_0000192919. FT MOD_RES 16 16 N6-acetyllysine. FT {ECO:0000244|PubMed:19608861}. FT MOD_RES 52 52 Phosphoserine. FT {ECO:0000244|PubMed:23186163}. FT MOD_RES 77 77 Phosphoserine. FT {ECO:0000244|PubMed:18691976, FT ECO:0000244|PubMed:23186163}. FT MOD_RES 106 106 Phosphoserine. FT {ECO:0000244|PubMed:20068231, FT ECO:0000244|PubMed:23186163}. FT MOD_RES 177 177 N6-acetyllysine; alternate. FT {ECO:0000244|PubMed:19608861}. FT CROSSLNK 123 123 Glycyl lysine isopeptide (Lys-Gly) FT (interchain with G-Cter in SUMO2). FT {ECO:0000244|PubMed:28112733}. FT CROSSLNK 145 145 Glycyl lysine isopeptide (Lys-Gly) FT (interchain with G-Cter in SUMO2). FT {ECO:0000244|PubMed:28112733}. FT CROSSLNK 174 174 Glycyl lysine isopeptide (Lys-Gly) FT (interchain with G-Cter in SUMO1); FT alternate. {ECO:0000244|PubMed:25114211}. FT CROSSLNK 174 174 Glycyl lysine isopeptide (Lys-Gly) FT (interchain with G-Cter in SUMO2); FT alternate. {ECO:0000244|PubMed:28112733}. FT CROSSLNK 177 177 Glycyl lysine isopeptide (Lys-Gly) FT (interchain with G-Cter in SUMO2); FT alternate. {ECO:0000244|PubMed:28112733}. FT VAR_SEQ 88 134 Missing (in isoform 2). FT {ECO:0000303|PubMed:14702039}. FT /FTId=VSP_046028. FT VARIANT 112 112 A -> T (in dbSNP:rs9930567). FT {ECO:0000269|PubMed:1301162, FT ECO:0000269|PubMed:15489334}. FT /FTId=VAR_051801. FT VARIANT 170 170 T -> P (in dbSNP:rs1062450). FT /FTId=VAR_051802. FT CONFLICT 9 9 V -> A (in Ref. 3; BAG59685). FT {ECO:0000305}. SQ SEQUENCE 211 AA; 24261 MW; DB9FC57768E6BEDE CRC64; MAPSRNGMVL KPHFHKDWQR RVATWFNQPA RKIRRRKARQ AKARRIAPRP ASGPIRPIVR CPTVRYHTKV RAGRGFSLEE LRVAGIHKKV ARTIGISVDP RRRNKSTESL QANVQRLKEY RSKLILFPRK PSAPKKGDSS AEELKLATQL TGPVMPVRNV YKKEKARVIT EEEKNFKAFA SLRMARANAR LFGIRAKRAK EAAEQDVEKK K //