SUMO1_MOUSE
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 03-AUG-2022, entry version 169.
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}.
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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 iPTMnet; P63166; -.
DR PhosphoSitePlus; P63166; -.
DR SwissPalm; P63166; -.
DR EPD; P63166; -.
DR jPOST; P63166; -.
DR MaxQB; P63166; -.
DR PaxDb; P63166; -.
DR PeptideAtlas; P63166; -.
DR PRIDE; P63166; -.
DR ProteomicsDB; 257507; -.
DR Antibodypedia; 3793; 1185 antibodies from 45 providers.
DR DNASU; 22218; -.
DR Ensembl; ENSMUST00000091374; ENSMUSP00000088935; ENSMUSG00000026021.
DR GeneID; 22218; -.
DR KEGG; mmu:22218; -.
DR UCSC; uc007bdx.1; mouse.
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; 1583700at2759; -.
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-3108232; SUMO E3 ligases SUMOylate target 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 BioGRID-ORCS; 22218; 4 hits in 70 CRISPR screens.
DR ChiTaRS; Sumo1; mouse.
DR PRO; PR:P63166; -.
DR Proteomes; UP000000589; Chromosome 1.
DR RNAct; P63166; protein.
DR Bgee; ENSMUSG00000026021; Expressed in morula and 70 other tissues.
DR ExpressionAtlas; P63166; baseline and differential.
DR Genevisible; P63166; MM.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
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:0045202; C:synapse; ISO:MGI.
DR GO; GO:0008076; C:voltage-gated potassium channel complex; ISO:MGI.
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; 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:0043392; P:negative regulation of DNA binding; ISO:MGI.
DR GO; GO:0043433; P:negative regulation of DNA-binding transcription factor activity; 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:0045892; P:negative regulation of transcription, DNA-templated; 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:0031647; P:regulation of protein stability; IMP:BHF-UCL.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; IDA:MGI.
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 Pfam; PF11976; Rad60-SLD; 1.
DR SMART; SM00213; UBQ; 1.
DR SUPFAM; SSF54236; SSF54236; 1.
DR PROSITE; PS50053; UBIQUITIN_2; 1.
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
