ID SUMO1_MOUSE Reviewed; 101 AA. AC P63166; P55856; Q3TX92; Q93068; DT 27-SEP-2004, integrated into UniProtKB/Swiss-Prot. DT 27-SEP-2004, sequence version 1. DT 27-MAR-2024, entry version 178. DE RecName: Full=Small ubiquitin-related modifier 1; DE Short=SUMO-1; DE AltName: Full=SMT3 homolog 3; DE AltName: Full=Ubiquitin-homology domain protein PIC1; DE AltName: Full=Ubiquitin-like protein SMT3C; DE Short=Smt3C; DE Flags: Precursor; GN Name=Sumo1; Synonyms=Smt3c, Smt3h3, Ubl1; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae; OC Murinae; Mus; Mus. OX NCBI_TaxID=10090; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RC STRAIN=ICR; RX PubMed=9465300; DOI=10.1006/geno.1997.5091; RA Howe K., Williamson J., Boddy M.N., Sheer D., Freemont P.S., Solomon E.; RT "The ubiquitin-homology gene PIC1: characterization of mouse (Pic1) and RT human (UBL1) genes and pseudogenes."; RL Genomics 47:92-100(1998). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=C57BL/6J, and NOD; TISSUE=Kidney, Liver, and Thymus; RX PubMed=16141072; DOI=10.1126/science.1112014; RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J., RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.; RT "The transcriptional landscape of the mammalian genome."; RL Science 309:1559-1563(2005). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=C57BL/6J, and FVB/N; TISSUE=Colon, and Eye; 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 [4] RP SUBCELLULAR LOCATION, INDUCTION, AND INTERACTION WITH HIF1A. RX PubMed=15225651; DOI=10.1016/j.febslet.2004.05.079; RA Shao R., Zhang F.-P., Tian F., Anders Friberg P., Wang X., Sjoeland H., RA Billig H.; RT "Increase of SUMO-1 expression in response to hypoxia: direct interaction RT with HIF-1alpha in adult mouse brain and heart in vivo."; RL FEBS Lett. 569:293-300(2004). RN [5] RP INTERACTION WITH IKFZ1. RX PubMed=15767674; DOI=10.1128/mcb.25.7.2688-2697.2005; RA Gomez-del Arco P., Koipally J., Georgopoulos K.; RT "Ikaros SUMOylation: switching out of repression."; RL Mol. Cell. Biol. 25:2688-2697(2005). RN [6] RP FUNCTION, AND DEVELOPMENTAL STAGE. RX PubMed=16990542; DOI=10.1126/science.1128406; RA Alkuraya F.S., Saadi I., Lund J.J., Turbe-Doan A., Morton C.C., Maas R.L.; RT "SUMO1 haploinsufficiency leads to cleft lip and palate."; RL Science 313:1751-1751(2006). RN [7] RP SUBCELLULAR LOCATION. RX PubMed=18681895; DOI=10.1111/j.1365-2443.2008.01216.x; RA Kuwata T., Nakamura T.; RT "BCL11A is a SUMOylated protein and recruits SUMO-conjugation enzymes in RT its nuclear body."; RL Genes Cells 13:931-940(2008). RN [8] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2, AND IDENTIFICATION BY MASS RP SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Embryonic fibroblast; RX PubMed=19131326; DOI=10.1074/mcp.m800451-mcp200; RA Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.; RT "Large scale localization of protein phosphorylation by use of electron RT capture dissociation mass spectrometry."; RL Mol. Cell. Proteomics 8:904-912(2009). RN [9] RP INTERACTION WITH HINT1. RX PubMed=31088288; DOI=10.1089/ars.2019.7724; RA Cortes-Montero E., Rodriguez-Munoz M., Sanchez-Blazquez P., Garzon J.; RT "The Axonal Motor Neuropathy-Related HINT1 Protein Is a Zinc- and RT Calmodulin-Regulated Cysteine SUMO Protease."; RL Antioxid. Redox Signal. 31:503-520(2019). CC -!- FUNCTION: Ubiquitin-like protein that can be covalently attached to CC proteins as a monomer or a lysine-linked polymer. Covalent attachment CC via an isopeptide bond to its substrates requires prior activation by CC the E1 complex SAE1-SAE2 and linkage to the E2 enzyme UBE2I, and can be CC promoted by E3 ligases such as PIAS1-4, RANBP2 or CBX4. This post- CC translational modification on lysine residues of proteins plays a CC crucial role in a number of cellular processes such as nuclear CC transport, DNA replication and repair, mitosis and signal transduction. CC Involved for instance in targeting RANGAP1 to the nuclear pore complex CC protein RANBP2. Covalently attached to the voltage-gated potassium CC channel KCNB1; this modulates the gating characteristics of KCNB1. CC Polymeric SUMO1 chains are also susceptible to polyubiquitination which CC functions as a signal for proteasomal degradation of modified proteins. CC May also regulate a network of genes involved in palate development. CC Covalently attached to ZFHX3 (By similarity). CC {ECO:0000250|UniProtKB:P63165, ECO:0000269|PubMed:16990542}. CC -!- SUBUNIT: Covalently attached to KCNB1; UBE2I increases cross-linking CC with KCNB1 and PIAS1 decreases cross-links with KCNB1 (By similarity). CC Interacts with SAE2, RANBP2, PIAS1 and PIAS2 (By similarity). Interacts CC with PRKN (By similarity). Covalently attached to a number of proteins CC such as IKFZ1, PML, RANGAP1, HIPK2, SP100, p53, p73-alpha, MDM2, JUN, CC DNMT3B and TDG (By similarity). Also interacts with HIF1A, HIPK2, CC HIPK3, CHD3, EXOSC9, RAD51 and RAD52 (By similarity). Interacts with CC USP25 (via ts SIM domain); the interaction weakly sumoylates USP25 (By CC similarity). Interacts with SIMC1, CASP8AP2, RNF111 and SOBP (via SIM CC domains) (By similarity). Interacts with BHLHE40/DEC1 (By similarity). CC Interacts with RWDD3 (By similarity). Interacts with UBE2I/UBC9 and CC this interaction is enhanced in the presence of RWDD3 (By similarity). CC Interacts with MTA1 (By similarity). Interacts with SENP2 (By CC similarity). Interacts with HINT1 (PubMed:31088288). CC {ECO:0000250|UniProtKB:P63165, ECO:0000269|PubMed:31088288}. CC -!- INTERACTION: CC P63166; Q03267: Ikzf1; NbExp=2; IntAct=EBI-80152, EBI-908572; CC P63166; Q505F1: Nr2c1; NbExp=5; IntAct=EBI-80152, EBI-15617004; CC P63166; P63015: Pax6; NbExp=2; IntAct=EBI-80152, EBI-1395428; CC P63166; P26367-1: PAX6; Xeno; NbExp=2; IntAct=EBI-80152, EBI-15892945; CC P63166; P18031: PTPN1; Xeno; NbExp=2; IntAct=EBI-80152, EBI-968788; CC -!- SUBCELLULAR LOCATION: Nucleus membrane {ECO:0000250|UniProtKB:P63165}. CC Nucleus speckle {ECO:0000269|PubMed:18681895}. Cytoplasm CC {ECO:0000250|UniProtKB:P63165}. Nucleus, PML body CC {ECO:0000250|UniProtKB:P63165}. Cell membrane CC {ECO:0000250|UniProtKB:P63165}. Nucleus {ECO:0000250|UniProtKB:P63165}. CC Note=Recruited by BCL11A into the nuclear body (PubMed:18681895). In CC the presence of ZFHX3, sequesterd to nuclear body (NB)-like dots in the CC nucleus some of which overlap or closely associate with PML body (By CC similarity). {ECO:0000250|UniProtKB:P63165, CC ECO:0000269|PubMed:18681895}. CC -!- TISSUE SPECIFICITY: Ubiquitous. CC -!- DEVELOPMENTAL STAGE: Expressed at 13.5 dpc strongly in the upper lip, CC primary palate and medial edge epithelia of the secondary palate. At CC 14.5 dpc expression could be seen in the medial edge epithelial seam. CC {ECO:0000269|PubMed:16990542}. CC -!- INDUCTION: By hypoxia. {ECO:0000269|PubMed:15225651}. CC -!- PTM: Cleavage of precursor form by SENP1 or SENP2 is necessary for CC function. {ECO:0000250|UniProtKB:P63165}. CC -!- PTM: Polymeric SUMO1 chains undergo polyubiquitination by RNF4. CC {ECO:0000250|UniProtKB:P63165}. CC -!- SIMILARITY: Belongs to the ubiquitin family. SUMO subfamily. 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 EMBL; AF033353; AAC39959.1; -; mRNA. DR EMBL; AK002536; BAB22172.1; -; mRNA. DR EMBL; AK011074; BAB27379.1; -; mRNA. DR EMBL; AK089081; BAC40739.1; -; mRNA. DR EMBL; AK159366; BAE35024.1; -; mRNA. DR EMBL; BC082566; AAH82566.1; -; mRNA. DR EMBL; BC083158; AAH83158.1; -; mRNA. DR CCDS; CCDS35586.1; -. DR RefSeq; NP_033486.1; NM_009460.2. DR AlphaFoldDB; P63166; -. DR BMRB; P63166; -. DR SMR; P63166; -. DR BioGRID; 204420; 16. DR CORUM; P63166; -. DR DIP; DIP-29278N; -. DR IntAct; P63166; 14. DR MINT; P63166; -. DR STRING; 10090.ENSMUSP00000088935; -. DR ChEMBL; CHEMBL4879447; -. DR GlyGen; P63166; 1 site, 1 O-linked glycan (1 site). DR iPTMnet; P63166; -. DR PhosphoSitePlus; P63166; -. DR SwissPalm; P63166; -. DR EPD; P63166; -. DR jPOST; P63166; -. DR MaxQB; P63166; -. DR PaxDb; 10090-ENSMUSP00000088935; -. DR PeptideAtlas; P63166; -. DR ProteomicsDB; 257507; -. DR Pumba; P63166; -. DR Antibodypedia; 3793; 1288 antibodies from 45 providers. DR DNASU; 22218; -. DR Ensembl; ENSMUST00000091374.9; ENSMUSP00000088935.3; ENSMUSG00000026021.16. DR GeneID; 22218; -. DR KEGG; mmu:22218; -. DR UCSC; uc007bdx.1; mouse. DR AGR; MGI:1197010; -. DR CTD; 7341; -. DR MGI; MGI:1197010; Sumo1. DR VEuPathDB; HostDB:ENSMUSG00000026021; -. DR eggNOG; KOG1769; Eukaryota. DR GeneTree; ENSGT00940000154319; -. DR HOGENOM; CLU_148322_0_0_1; -. DR InParanoid; P63166; -. DR OMA; TIECHIE; -. DR OrthoDB; 5132985at2759; -. DR PhylomeDB; P63166; -. DR TreeFam; TF315116; -. DR Reactome; R-MMU-3065676; SUMO is conjugated to E1 (UBA2:SAE1). DR Reactome; R-MMU-3065678; SUMO is transferred from E1 to E2 (UBE2I, UBC9). DR Reactome; R-MMU-3065679; SUMO is proteolytically processed. DR Reactome; R-MMU-3108214; SUMOylation of DNA damage response and repair proteins. DR Reactome; R-MMU-3232118; SUMOylation of transcription factors. DR Reactome; R-MMU-3232142; SUMOylation of ubiquitinylation proteins. DR Reactome; R-MMU-3899300; SUMOylation of transcription cofactors. DR Reactome; R-MMU-4085377; SUMOylation of SUMOylation proteins. DR Reactome; R-MMU-4090294; SUMOylation of intracellular receptors. DR Reactome; R-MMU-4551638; SUMOylation of chromatin organization proteins. DR Reactome; R-MMU-4570464; SUMOylation of RNA binding proteins. DR Reactome; R-MMU-4615885; SUMOylation of DNA replication proteins. DR Reactome; R-MMU-4655427; SUMOylation of DNA methylation proteins. DR Reactome; R-MMU-4755510; SUMOylation of immune response proteins. DR Reactome; R-MMU-5693565; Recruitment and ATM-mediated phosphorylation of repair and signaling proteins at DNA double strand breaks. DR Reactome; R-MMU-5696395; Formation of Incision Complex in GG-NER. DR Reactome; R-MMU-877312; Regulation of IFNG signaling. DR Reactome; R-MMU-8866904; Negative regulation of activity of TFAP2 (AP-2) family transcription factors. DR Reactome; R-MMU-9615933; Postmitotic nuclear pore complex (NPC) reformation. DR Reactome; R-MMU-9793242; SUMOylation of nuclear envelope proteins. DR BioGRID-ORCS; 22218; 4 hits in 75 CRISPR screens. DR ChiTaRS; Sumo1; mouse. DR PRO; PR:P63166; -. DR Proteomes; UP000000589; Chromosome 1. DR RNAct; P63166; Protein. DR Bgee; ENSMUSG00000026021; Expressed in blastoderm cell in morula and 72 other cell types or tissues. DR ExpressionAtlas; P63166; baseline and differential. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0030425; C:dendrite; ISO:MGI. DR GO; GO:0001650; C:fibrillar center; ISO:MGI. DR GO; GO:0000792; C:heterochromatin; ISO:MGI. DR GO; GO:0016604; C:nuclear body; IDA:UniProtKB. DR GO; GO:0031965; C:nuclear membrane; ISO:MGI. DR GO; GO:0016607; C:nuclear speck; IEA:UniProtKB-SubCell. DR GO; GO:0097165; C:nuclear stress granule; ISS:UniProtKB. DR GO; GO:0005730; C:nucleolus; ISO:MGI. DR GO; GO:0005654; C:nucleoplasm; ISO:MGI. DR GO; GO:0005634; C:nucleus; IDA:MGI. DR GO; GO:0005886; C:plasma membrane; ISS:UniProtKB. DR GO; GO:0016605; C:PML body; ISS:UniProtKB. DR GO; GO:0001741; C:XY body; IDA:MGI. DR GO; GO:0019899; F:enzyme binding; ISO:MGI. DR GO; GO:0015459; F:potassium channel regulator activity; ISS:UniProtKB. DR GO; GO:0031386; F:protein tag activity; IBA:GO_Central. DR GO; GO:0044388; F:small protein activating enzyme binding; ISO:MGI. DR GO; GO:0008134; F:transcription factor binding; IMP:AgBase. DR GO; GO:0031625; F:ubiquitin protein ligase binding; ISS:UniProtKB. DR GO; GO:0044389; F:ubiquitin-like protein ligase binding; IBA:GO_Central. DR GO; GO:1990381; F:ubiquitin-specific protease binding; ISO:MGI. DR GO; GO:0071276; P:cellular response to cadmium ion; ISS:UniProtKB. DR GO; GO:0034605; P:cellular response to heat; ISS:UniProtKB. DR GO; GO:0045759; P:negative regulation of action potential; ISS:UniProtKB. DR GO; GO:1902260; P:negative regulation of delayed rectifier potassium channel activity; ISS:UniProtKB. DR GO; GO:0045892; P:negative regulation of DNA-templated transcription; ISO:MGI. DR GO; GO:0042308; P:negative regulation of protein import into nucleus; ISO:MGI. DR GO; GO:0010621; P:negative regulation of transcription by transcription factor localization; ISO:MGI. DR GO; GO:0030578; P:PML body organization; IMP:MGI. DR GO; GO:1901896; P:positive regulation of ATPase-coupled calcium transmembrane transporter activity; IMP:BHF-UCL. DR GO; GO:0032436; P:positive regulation of proteasomal ubiquitin-dependent protein catabolic process; ISO:MGI. DR GO; GO:0031334; P:positive regulation of protein-containing complex assembly; ISO:MGI. DR GO; GO:0090204; P:protein localization to nuclear pore; IMP:MGI. DR GO; GO:0050821; P:protein stabilization; ISO:MGI. DR GO; GO:0016925; P:protein sumoylation; IDA:MGI. DR GO; GO:1903169; P:regulation of calcium ion transmembrane transport; IMP:BHF-UCL. DR GO; GO:0086004; P:regulation of cardiac muscle cell contraction; IMP:BHF-UCL. DR GO; GO:0006355; P:regulation of DNA-templated transcription; IDA:MGI. DR GO; GO:0031647; P:regulation of protein stability; IMP:BHF-UCL. DR GO; GO:0060021; P:roof of mouth development; IMP:UniProtKB. DR CDD; cd16114; Ubl_SUMO1; 1. DR InterPro; IPR022617; Rad60/SUMO-like_dom. DR InterPro; IPR046332; SUMO1_Ubl. DR InterPro; IPR000626; Ubiquitin-like_dom. DR InterPro; IPR029071; Ubiquitin-like_domsf. DR PANTHER; PTHR10562; SMALL UBIQUITIN-RELATED MODIFIER; 1. DR PANTHER; PTHR10562:SF14; SMALL UBIQUITIN-RELATED MODIFIER 1; 1. DR Pfam; PF11976; Rad60-SLD; 1. DR SMART; SM00213; UBQ; 1. DR SUPFAM; SSF54236; Ubiquitin-like; 1. DR PROSITE; PS50053; UBIQUITIN_2; 1. DR Genevisible; P63166; MM. PE 1: Evidence at protein level; KW Acetylation; Cell membrane; Cytoplasm; Isopeptide bond; Membrane; Nucleus; KW Phosphoprotein; Reference proteome; Stress response; Ubl conjugation; KW Ubl conjugation pathway. FT INIT_MET 1 FT /note="Removed" FT /evidence="ECO:0000250|UniProtKB:P63165" FT CHAIN 2..97 FT /note="Small ubiquitin-related modifier 1" FT /id="PRO_0000035941" FT PROPEP 98..101 FT /evidence="ECO:0000250" FT /id="PRO_0000035942" FT DOMAIN 20..97 FT /note="Ubiquitin-like" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00214" FT SITE 36 FT /note="Interaction with PIAS2" FT /evidence="ECO:0000250" FT MOD_RES 2 FT /note="N-acetylserine" FT /evidence="ECO:0000250|UniProtKB:P63165" FT MOD_RES 2 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:19131326" FT MOD_RES 9 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:P63165" FT MOD_RES 32 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:P63165" FT CROSSLNK 7 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO1); alternate" FT /evidence="ECO:0000250|UniProtKB:P63165" FT CROSSLNK 7 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2); alternate" FT /evidence="ECO:0000250|UniProtKB:P63165" FT CROSSLNK 16 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0000250|UniProtKB:P63165" FT CROSSLNK 17 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0000250|UniProtKB:P63165" FT CROSSLNK 23 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0000250|UniProtKB:P63165" FT CROSSLNK 25 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO1)" FT /evidence="ECO:0000250|UniProtKB:P63165" FT CROSSLNK 37 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0000250|UniProtKB:P63165" FT CROSSLNK 39 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0000250|UniProtKB:P63165" FT CROSSLNK 45 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0000250|UniProtKB:P63165" FT CROSSLNK 46 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0000250|UniProtKB:P63165" FT CROSSLNK 97 FT /note="Glycyl lysine isopeptide (Gly-Lys) (interchain with FT K-? in acceptor proteins)" SQ SEQUENCE 101 AA; 11557 MW; 89BE97D2D054FB33 CRC64; MSDQEAKPST EDLGDKKEGE YIKLKVIGQD SSEIHFKVKM TTHLKKLKES YCQRQGVPMN SLRFLFEGQR IADNHTPKEL GMEEEDVIEV YQEQTGGHST V //