MYSM1_MOUSE
ID MYSM1_MOUSE Reviewed; 819 AA.
AC Q69Z66; A2AJE3; B9EKJ6; Q3TPV7; Q8BRP5; Q8C4N1;
DT 02-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT 02-MAY-2006, sequence version 2.
DT 03-AUG-2022, entry version 150.
DE RecName: Full=Deubiquitinase MYSM1;
DE Short=2A-DUB;
DE EC=3.4.19.- {ECO:0000269|PubMed:26474655};
DE AltName: Full=Myb-like, SWIRM and MPN domain-containing protein 1;
GN Name=Mysm1; Synonyms=Kiaa1915;
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 [LARGE SCALE MRNA] (ISOFORM 2), AND NUCLEOTIDE SEQUENCE
RP [LARGE SCALE MRNA] OF 1-354.
RC STRAIN=C57BL/6J; TISSUE=Brain cortex, Head, and Spinal cord;
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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain;
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 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 75-819.
RC TISSUE=Pancreatic islet;
RX PubMed=15368895; DOI=10.1093/dnares/11.3.205;
RA Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S.,
RA Saga Y., Seino S., Nishimura M., Kaisho T., Hoshino K., Kitamura H.,
RA Nagase T., Ohara O., Koga H.;
RT "Prediction of the coding sequences of mouse homologues of KIAA gene: IV.
RT The complete nucleotide sequences of 500 mouse KIAA-homologous cDNAs
RT identified by screening of terminal sequences of cDNA clones randomly
RT sampled from size-fractionated libraries.";
RL DNA Res. 11:205-218(2004).
RN [5]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Pancreas, and Spleen;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [6]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=22169041; DOI=10.1016/j.immuni.2011.11.010;
RA Jiang X.X., Nguyen Q., Chou Y., Wang T., Nandakumar V., Yates P., Jones L.,
RA Wang L., Won H., Lee H.R., Jung J.U., Mueschen M., Huang X.F., Chen S.Y.;
RT "Control of B cell development by the histone H2A deubiquitinase MYSM1.";
RL Immunity 35:883-896(2011).
RN [7]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=24062447; DOI=10.1073/pnas.1308888110;
RA Nandakumar V., Chou Y., Zang L., Huang X.F., Chen S.Y.;
RT "Epigenetic control of natural killer cell maturation by histone H2A
RT deubiquitinase, MYSM1.";
RL Proc. Natl. Acad. Sci. U.S.A. 110:E3927-E3936(2013).
RN [8]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=25217698; DOI=10.1182/blood-2013-10-534313;
RA Won H., Nandakumar V., Yates P., Sanchez S., Jones L., Huang X.F.,
RA Chen S.Y.;
RT "Epigenetic control of dendritic cell development and fate determination of
RT common myeloid progenitor by Mysm1.";
RL Blood 124:2647-2656(2014).
RN [9]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=26348977; DOI=10.1038/srep13755;
RA Jiang X.X., Chou Y., Jones L., Wang T., Sanchez S., Huang X.F., Zhang L.,
RA Wang C., Chen S.Y.;
RT "Epigenetic Regulation of Antibody Responses by the Histone H2A
RT Deubiquitinase MYSM1.";
RL Sci. Rep. 5:13755-13755(2015).
RN [10]
RP FUNCTION, DISRUPTION PHENOTYPE, SUBCELLULAR LOCATION, AND CATALYTIC
RP ACTIVITY.
RX PubMed=26474655; DOI=10.1016/j.immuni.2015.09.010;
RA Panda S., Nilsson J.A., Gekara N.O.;
RT "Deubiquitinase MYSM1 Regulates Innate Immunity through Inactivation of
RT TRAF3 and TRAF6 Complexes.";
RL Immunity 43:647-659(2015).
RN [11]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=27895164; DOI=10.1189/jlb.1ab0415-177rr;
RA Foerster M., Farrington K., Petrov J.C., Belle J.I., Mindt B.C.,
RA Witalis M., Duerr C.U., Fritz J.H., Nijnik A.;
RT "MYSM1-dependent checkpoints in B cell lineage differentiation and B cell-
RT mediated immune response.";
RL J. Leukoc. Biol. 101:643-654(2017).
RN [12]
RP FUNCTION, SUBCELLULAR LOCATION, AND DISRUPTION PHENOTYPE.
RX PubMed=30405132; DOI=10.1038/s41467-018-07016-0;
RA Panda S., Gekara N.O.;
RT "The deubiquitinase MYSM1 dampens NOD2-mediated inflammation and tissue
RT damage by inactivating the RIP2 complex.";
RL Nat. Commun. 9:4654-4654(2018).
RN [13]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=33086059; DOI=10.1016/j.celrep.2020.108297;
RA Tian M., Liu W., Zhang Q., Huang Y., Li W., Wang W., Zhao P., Huang S.,
RA Song Y., Shereen M.A., Qin M., Liu Y., Wu K., Wu J.;
RT "MYSM1 Represses Innate Immunity and Autoimmunity through Suppressing the
RT cGAS-STING Pathway.";
RL Cell Rep. 33:108297-108297(2020).
CC -!- FUNCTION: Metalloprotease with deubiquitinase activity that plays
CC important regulator roles in hematopoietic stem cell function, blood
CC cell production and immune response (PubMed:26474655, PubMed:27895164,
CC PubMed:30405132). Participates in the normal programming of B-cell
CC responses to antigen after the maturation process (PubMed:27895164).
CC Within the cytoplasm, plays critical roles in the repression of innate
CC immunity and autoimmunity (PubMed:26474655, PubMed:30405132). Removes
CC 'Lys-63'-linked polyubiquitins from TRAF3 and TRAF6 complexes
CC (PubMed:26474655). Attenuates NOD2-mediated inflammation and tissue
CC injury by promoting 'Lys-63'-linked deubiquitination of RIPK2 component
CC (PubMed:30405132). Suppresses the CGAS-STING1 signaling pathway by
CC cleaving STING1 'Lys-63'-linked ubiquitin chains (PubMed:33086059). In
CC the nucleus, acts as a hematopoietic transcription regulator
CC derepressing a range of genes essential for normal stem cell
CC differentiation including EBF1 and PAX5 in B-cells, ID2 in NK-cell
CC progenitor or FLT3 in dendritic cell precursors (PubMed:22169041,
CC PubMed:24062447, PubMed:25217698 PubMed:26348977). Deubiquitinates
CC monoubiquitinated histone H2A, a specific tag for epigenetic
CC transcriptional repression, leading to dissociation of histone H1 from
CC the nucleosome (By similarity). {ECO:0000250|UniProtKB:Q5VVJ2,
CC ECO:0000269|PubMed:22169041, ECO:0000269|PubMed:24062447,
CC ECO:0000269|PubMed:25217698, ECO:0000269|PubMed:26348977,
CC ECO:0000269|PubMed:26474655, ECO:0000269|PubMed:27895164,
CC ECO:0000269|PubMed:30405132}.
CC -!- SUBUNIT: Component of a large chromatin remodeling complex, at least
CC composed of MYSM1, PCAF, RBM10 and KIF11/TRIP5. Binds histones (By
CC similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:26474655,
CC ECO:0000269|PubMed:30405132}. Cytoplasm {ECO:0000269|PubMed:26474655,
CC ECO:0000269|PubMed:30405132}. Note=Localizes to the cytoplasm in
CC response to bacterial infection. {ECO:0000269|PubMed:26474655}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q69Z66-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q69Z66-2; Sequence=VSP_018212;
CC -!- DOMAIN: Contains an N-terminal SANT domain that mediates histone/DNA
CC binding, a central SWIRM domain to mediate interaction with chromatin
CC associated proteins, and a C-terminal MPN domain that contains the
CC metalloprotease activity. {ECO:0000250|UniProtKB:Q5VVJ2}.
CC -!- DISRUPTION PHENOTYPE: Deficient mice elicit hyper-inflammatory
CC responses, are more susceptible to septic shock, more resistant to RNA
CC virus replication but exhibit early death upon DNA viral infection
CC (PubMed:26474655, PubMed:33086059). They also show an impaired B-cell
CC development (PubMed:22169041, PubMed:26348977, PubMed:27895164). In a
CC similar way, NK-cell and dendritic cell development is impaired in
CC deletion mutant (PubMed:25217698, PubMed:24062447). An enhanced
CC systemic inflammation can be observed characterized by higher cytokine
CC levels, as well as the hepatocellular enzyme alanine aminotransferase,
CC a marker of liver damage (PubMed:30405132).
CC {ECO:0000269|PubMed:22169041, ECO:0000269|PubMed:24062447,
CC ECO:0000269|PubMed:25217698, ECO:0000269|PubMed:26348977,
CC ECO:0000269|PubMed:26474655, ECO:0000269|PubMed:27895164,
CC ECO:0000269|PubMed:30405132, ECO:0000269|PubMed:33086059}.
CC -!- SIMILARITY: Belongs to the peptidase M67A family. MYSM1 subfamily.
CC {ECO:0000305}.
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DR EMBL; AK043802; BAC31657.1; -; mRNA.
DR EMBL; AK081684; BAC38291.1; -; mRNA.
DR EMBL; AK164103; BAE37628.1; -; mRNA.
DR EMBL; AL732611; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC150946; AAI50947.1; -; mRNA.
DR EMBL; BC151172; AAI51173.1; -; mRNA.
DR EMBL; AK173300; BAD32578.1; -; mRNA.
DR CCDS; CCDS18363.1; -. [Q69Z66-1]
DR RefSeq; NP_796213.2; NM_177239.2. [Q69Z66-1]
DR AlphaFoldDB; Q69Z66; -.
DR SMR; Q69Z66; -.
DR BioGRID; 236236; 11.
DR STRING; 10090.ENSMUSP00000075269; -.
DR MEROPS; M67.005; -.
DR iPTMnet; Q69Z66; -.
DR PhosphoSitePlus; Q69Z66; -.
DR EPD; Q69Z66; -.
DR MaxQB; Q69Z66; -.
DR PaxDb; Q69Z66; -.
DR PeptideAtlas; Q69Z66; -.
DR PRIDE; Q69Z66; -.
DR ProteomicsDB; 287600; -. [Q69Z66-1]
DR ProteomicsDB; 287601; -. [Q69Z66-2]
DR Antibodypedia; 46901; 281 antibodies from 30 providers.
DR DNASU; 320713; -.
DR Ensembl; ENSMUST00000075872; ENSMUSP00000075269; ENSMUSG00000062627. [Q69Z66-1]
DR GeneID; 320713; -.
DR KEGG; mmu:320713; -.
DR UCSC; uc008tsn.1; mouse. [Q69Z66-1]
DR CTD; 114803; -.
DR MGI; MGI:2444584; Mysm1.
DR VEuPathDB; HostDB:ENSMUSG00000062627; -.
DR eggNOG; KOG1279; Eukaryota.
DR eggNOG; KOG1555; Eukaryota.
DR GeneTree; ENSGT00940000157721; -.
DR HOGENOM; CLU_018854_0_0_1; -.
DR InParanoid; Q69Z66; -.
DR OMA; SWRTDNS; -.
DR OrthoDB; 590811at2759; -.
DR PhylomeDB; Q69Z66; -.
DR TreeFam; TF324811; -.
DR Reactome; R-MMU-5689901; Metalloprotease DUBs.
DR BioGRID-ORCS; 320713; 0 hits in 61 CRISPR screens.
DR ChiTaRS; Mysm1; mouse.
DR PRO; PR:Q69Z66; -.
DR Proteomes; UP000000589; Chromosome 4.
DR RNAct; Q69Z66; protein.
DR Bgee; ENSMUSG00000062627; Expressed in animal zygote and 219 other tissues.
DR Genevisible; Q69Z66; MM.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005730; C:nucleolus; ISO:MGI.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0032991; C:protein-containing complex; ISO:MGI.
DR GO; GO:0004843; F:cysteine-type deubiquitinase activity; IEA:InterPro.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0042393; F:histone binding; ISS:UniProtKB.
DR GO; GO:0070122; F:isopeptidase activity; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0140492; F:metal-dependent deubiquitinase activity; ISS:UniProtKB.
DR GO; GO:0003713; F:transcription coactivator activity; ISS:UniProtKB.
DR GO; GO:0006338; P:chromatin remodeling; ISS:UniProtKB.
DR GO; GO:0002376; P:immune system process; IEA:UniProtKB-KW.
DR GO; GO:0035522; P:monoubiquitinated histone H2A deubiquitination; ISS:UniProtKB.
DR GO; GO:0043473; P:pigmentation; IMP:MGI.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; ISS:UniProtKB.
DR GO; GO:0030334; P:regulation of cell migration; IMP:MGI.
DR GO; GO:0051797; P:regulation of hair follicle development; IMP:MGI.
DR GO; GO:1903706; P:regulation of hemopoiesis; ISS:UniProtKB.
DR CDD; cd00167; SANT; 1.
DR Gene3D; 1.10.10.10; -; 1.
DR InterPro; IPR009057; Homeobox-like_sf.
DR InterPro; IPR000555; JAMM/MPN+_dom.
DR InterPro; IPR037518; MPN.
DR InterPro; IPR017930; Myb_dom.
DR InterPro; IPR033497; MYSM1.
DR InterPro; IPR001005; SANT/Myb.
DR InterPro; IPR017884; SANT_dom.
DR InterPro; IPR007526; SWIRM.
DR InterPro; IPR036388; WH-like_DNA-bd_sf.
DR PANTHER; PTHR12802:SF67; PTHR12802:SF67; 1.
DR Pfam; PF01398; JAB; 1.
DR Pfam; PF00249; Myb_DNA-binding; 1.
DR Pfam; PF04433; SWIRM; 1.
DR SMART; SM00232; JAB_MPN; 1.
DR SMART; SM00717; SANT; 1.
DR SUPFAM; SSF46689; SSF46689; 2.
DR PROSITE; PS50249; MPN; 1.
DR PROSITE; PS50934; SWIRM; 1.
PE 1: Evidence at protein level;
KW Activator; Alternative splicing; Chromatin regulator; Cytoplasm;
KW DNA-binding; Hydrolase; Immunity; Isopeptide bond; Metal-binding;
KW Metalloprotease; Nucleus; Phosphoprotein; Protease; Reference proteome;
KW Transcription; Transcription regulation; Ubl conjugation;
KW Ubl conjugation pathway; Zinc.
FT CHAIN 1..819
FT /note="Deubiquitinase MYSM1"
FT /id="PRO_0000234074"
FT DOMAIN 113..164
FT /note="SANT"
FT DOMAIN 363..461
FT /note="SWIRM"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00247"
FT DOMAIN 568..700
FT /note="MPN"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01182"
FT REGION 1..29
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 228..247
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 260..279
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 318..347
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 647..660
FT /note="JAMM motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01182"
FT MOTIF 765..769
FT /note="LXXLL motif"
FT COMPBIAS 318..335
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 647
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01182"
FT BINDING 649
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01182"
FT BINDING 660
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01182"
FT MOD_RES 107
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q5VVJ2"
FT MOD_RES 215
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q5VVJ2"
FT MOD_RES 233
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q5VVJ2"
FT MOD_RES 332
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q5VVJ2"
FT CROSSLNK 184
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q5VVJ2"
FT VAR_SEQ 412..819
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_018212"
FT CONFLICT 7
FT /note="D -> G (in Ref. 1; BAE37628)"
FT /evidence="ECO:0000305"
FT CONFLICT 175
FT /note="Q -> H (in Ref. 1; BAC31657)"
FT /evidence="ECO:0000305"
FT CONFLICT 221
FT /note="D -> H (in Ref. 1; BAE37628)"
FT /evidence="ECO:0000305"
FT CONFLICT 265
FT /note="A -> P (in Ref. 1; BAE37628)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 819 AA; 93475 MW; B5A720311CD9C779 CRC64;
MEAEEADVDV EGDVAAAAQP GNDESTASVF QDHYLDSTWR RENGCLPWTL DSTISDENRA
IIEKMLLEEE YYLSNKSLPG KFWVNQKEDN KKYTNSLQKS SKAMVDSPAK PASHSVKWTV
EEKELFEQGL AKFGRRWTKI ATLLKSRTVL QVKSYARQYF KNKVKWDVEK ETPTQKSSSD
LQVKNKDDRT KAWAAACLRG SADPCLNAVK IEKLSDDEDV DITDELDELT SQTSQNSGSH
LTLDVPNSKM YTTNQGELCQ EGPLAKSSGE SLQNVKQGEG EACSSSEIAS WAEKQKSTDK
NSAELNEKYN KVVEEHTLHR GEVREEAKHS PSPEPCERQD SSGNEMLLPP CQIEEENHEG
EELKPPEQEV EIDRNVIQEE EKQAIPEFFE GRQTKTPERY LKIRNYILDQ WEICKPKYLN
KTSVRPGLKN CGDVNCIGRI HTYLELIGAI NFGCEQAVYN RPQPLDKVRA ADRKDAEAAY
QLAWRLQSMR TRRRRVRDPW GNWCDAKDLE GQTFEHLSVE EMARRKEEEK CKPIKFSKAS
KLPKSSLDPF QLIPCNFFSE EKQEPFQVKV AAEALLIMNL HAHVSMAEVI GLLGGRYSEA
DKVLEVCAAE PCNSLSTGLQ CEMDPVSQTQ ASETLALRGY SVIGWYHSHP AFDPNPSLRD
IDTQAKYQSY FSRGGAKFIG MIVSPYNRSN PLPYSQITCL VISEEVSPDG TYRLPYKFEV
QQMLEEPQWE LVFEKTRWII EKYRLSNSSV PMDRIFRRDS DLTCLQKLLE CLRKTLSKVA
NCFIAEEFLT QIENLFLSNY KSKEENGLAE EDSTKELFM
