MATR3_MOUSE
ID MATR3_MOUSE Reviewed; 846 AA.
AC Q8K310;
DT 23-NOV-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2002, sequence version 1.
DT 03-AUG-2022, entry version 171.
DE RecName: Full=Matrin-3;
GN Name=Matr3;
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].
RC STRAIN=NOD; TISSUE=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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Czech II; TISSUE=Mammary tumor;
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 [3]
RP PROTEIN SEQUENCE OF 4-12; 20-44; 93-127; 133-146; 193-223; 230-245;
RP 271-304; 399-407; 413-433; 497-515; 525-530; 533-542; 556-562; 719-735;
RP 780-797 AND 804-816, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC STRAIN=OF1; TISSUE=Hippocampus;
RA Lubec G., Sunyer B., Chen W.-Q.;
RL Submitted (JAN-2009) to UniProtKB.
RN [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-188, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain;
RX PubMed=16452087; DOI=10.1074/mcp.t500041-mcp200;
RA Trinidad J.C., Specht C.G., Thalhammer A., Schoepfer R., Burlingame A.L.;
RT "Comprehensive identification of phosphorylation sites in postsynaptic
RT density preparations.";
RL Mol. Cell. Proteomics 5:914-922(2006).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-188, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT "Large-scale phosphorylation analysis of mouse liver.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-188, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
RA Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
RA Thibault P.;
RT "The phagosomal proteome in interferon-gamma-activated macrophages.";
RL Immunity 30:143-154(2009).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-598, AND IDENTIFICATION BY
RP MASS 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 [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-150; SER-188; SER-195;
RP SER-533; SER-598 AND SER-604, AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Lung, Pancreas, Spleen,
RC and Testis;
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 [9]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-835, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic fibroblast;
RX PubMed=23806337; DOI=10.1016/j.molcel.2013.06.001;
RA Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y.,
RA Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.;
RT "SIRT5-mediated lysine desuccinylation impacts diverse metabolic
RT pathways.";
RL Mol. Cell 50:919-930(2013).
RN [10]
RP STRUCTURE BY NMR OF 390-576.
RG RIKEN structural genomics initiative (RSGI);
RT "Solution structure of RRM domains in matrin 3.";
RL Submitted (NOV-2005) to the PDB data bank.
CC -!- FUNCTION: May play a role in transcription or may interact with other
CC nuclear matrix proteins to form the internal fibrogranular network. In
CC association with the SFPQ-NONO heteromer may play a role in nuclear
CC retention of defective RNAs. Plays a role in the regulation of DNA
CC virus-mediated innate immune response by assembling into the HDP-RNP
CC complex, a complex that serves as a platform for IRF3 phosphorylation
CC and subsequent innate immune response activation through the cGAS-STING
CC pathway. Binds to N6-methyladenosine (m6A)-containing mRNAs and
CC contributes to MYC stability by binding to m6A-containing MYC mRNAs.
CC May bind to specific miRNA hairpins. {ECO:0000250|UniProtKB:P43243}.
CC -!- SUBUNIT: Part of a complex consisting of SFPQ, NONO and MATR3.
CC Interacts with AGO1 and AGO2 (By similarity). Part of a complex
CC composed at least of ASCL2, EMSY, HCFC1, HSPA8, CCAR2, MATR3, MKI67,
CC RBBP5, TUBB2A, WDR5 and ZNF335; this complex may have a histone H3-
CC specific methyltransferase activity. Interacts with TARDBP. Part of the
CC HDP-RNP complex composed of at least HEXIM1, PRKDC, XRCC5, XRCC6,
CC paraspeckle proteins (SFPQ, NONO, PSPC1, RBM14, and MATR3) and NEAT1
CC RNA. Interacts with FUS. Interacts with IGF2BP1. Interacts with IGF2BP2
CC and IGF2BP3. {ECO:0000250|UniProtKB:P43243}.
CC -!- SUBCELLULAR LOCATION: Nucleus matrix {ECO:0000255|PROSITE-
CC ProRule:PRU00130}.
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DR EMBL; AK087939; BAC40050.1; -; mRNA.
DR EMBL; BC029070; AAH29070.1; -; mRNA.
DR CCDS; CCDS29142.1; -.
DR RefSeq; NP_034901.2; NM_010771.6.
DR PDB; 1X4D; NMR; -; A=390-478.
DR PDB; 1X4F; NMR; -; A=478-576.
DR PDB; 7FBR; NMR; -; A=390-478.
DR PDB; 7FBV; NMR; -; A=478-576.
DR PDBsum; 1X4D; -.
DR PDBsum; 1X4F; -.
DR PDBsum; 7FBR; -.
DR PDBsum; 7FBV; -.
DR AlphaFoldDB; Q8K310; -.
DR SMR; Q8K310; -.
DR BioGRID; 201324; 37.
DR IntAct; Q8K310; 22.
DR MINT; Q8K310; -.
DR STRING; 10090.ENSMUSP00000125761; -.
DR iPTMnet; Q8K310; -.
DR PhosphoSitePlus; Q8K310; -.
DR SwissPalm; Q8K310; -.
DR EPD; Q8K310; -.
DR jPOST; Q8K310; -.
DR MaxQB; Q8K310; -.
DR PaxDb; Q8K310; -.
DR PRIDE; Q8K310; -.
DR ProteomicsDB; 292271; -.
DR DNASU; 17184; -.
DR Ensembl; ENSMUST00000166793; ENSMUSP00000125761; ENSMUSG00000037236.
DR Ensembl; ENSMUST00000235199; ENSMUSP00000158074; ENSMUSG00000037236.
DR Ensembl; ENSMUST00000237744; ENSMUSP00000158537; ENSMUSG00000037236.
DR GeneID; 17184; -.
DR KEGG; mmu:17184; -.
DR UCSC; uc008emg.2; mouse.
DR CTD; 9782; -.
DR MGI; MGI:1298379; Matr3.
DR VEuPathDB; HostDB:ENSMUSG00000037236; -.
DR eggNOG; ENOG502QRVG; Eukaryota.
DR GeneTree; ENSGT00940000153322; -.
DR HOGENOM; CLU_015917_0_0_1; -.
DR InParanoid; Q8K310; -.
DR OMA; CFCMLNS; -.
DR OrthoDB; 200901at2759; -.
DR PhylomeDB; Q8K310; -.
DR TreeFam; TF333921; -.
DR BioGRID-ORCS; 17184; 12 hits in 75 CRISPR screens.
DR ChiTaRS; Matr3; mouse.
DR EvolutionaryTrace; Q8K310; -.
DR PRO; PR:Q8K310; -.
DR Proteomes; UP000000589; Chromosome 18.
DR RNAct; Q8K310; protein.
DR Bgee; ENSMUSG00000037236; Expressed in renal medulla interstitium and 251 other tissues.
DR ExpressionAtlas; Q8K310; baseline and differential.
DR Genevisible; Q8K310; MM.
DR GO; GO:0005737; C:cytoplasm; ISO:MGI.
DR GO; GO:0016363; C:nuclear matrix; ISO:MGI.
DR GO; GO:0005634; C:nucleus; IDA:MGI.
DR GO; GO:0042802; F:identical protein binding; ISO:MGI.
DR GO; GO:0035198; F:miRNA binding; ISS:UniProtKB.
DR GO; GO:0003723; F:RNA binding; IBA:GO_Central.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0002218; P:activation of innate immune response; ISO:MGI.
DR GO; GO:0001825; P:blastocyst formation; IMP:MGI.
DR GO; GO:0003170; P:heart valve development; IMP:MGI.
DR GO; GO:0045087; P:innate immune response; IEA:UniProtKB-KW.
DR GO; GO:0010608; P:post-transcriptional regulation of gene expression; ISO:MGI.
DR GO; GO:0003281; P:ventricular septum development; IMP:MGI.
DR CDD; cd12714; RRM1_MATR3; 1.
DR CDD; cd12715; RRM2_MATR3; 1.
DR Gene3D; 3.30.70.330; -; 2.
DR InterPro; IPR034928; MATR3_RRM1.
DR InterPro; IPR034930; MATR3_RRM2.
DR InterPro; IPR000690; Matrin/U1-C_Znf_C2H2.
DR InterPro; IPR003604; Matrin/U1-like-C_Znf_C2H2.
DR InterPro; IPR012677; Nucleotide-bd_a/b_plait_sf.
DR InterPro; IPR035979; RBD_domain_sf.
DR InterPro; IPR000504; RRM_dom.
DR SMART; SM00360; RRM; 2.
DR SMART; SM00451; ZnF_U1; 2.
DR SUPFAM; SSF54928; SSF54928; 2.
DR PROSITE; PS50102; RRM; 2.
DR PROSITE; PS50171; ZF_MATRIN; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Direct protein sequencing; Immunity;
KW Innate immunity; Isopeptide bond; Metal-binding; Nucleus; Phosphoprotein;
KW Reference proteome; Repeat; RNA-binding; Ubl conjugation; Zinc;
KW Zinc-finger.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:P43243"
FT CHAIN 2..846
FT /note="Matrin-3"
FT /id="PRO_0000081623"
FT DOMAIN 398..473
FT /note="RRM 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT DOMAIN 496..571
FT /note="RRM 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT ZN_FING 800..831
FT /note="Matrin-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00130"
FT REGION 147..174
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 187..213
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 342..394
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 588..779
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 709..717
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000255"
FT COMPBIAS 588..646
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 647..663
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 689..734
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 748..776
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 2
FT /note="N-acetylserine"
FT /evidence="ECO:0000250|UniProtKB:P43243"
FT MOD_RES 3
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P43243"
FT MOD_RES 4
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P43243"
FT MOD_RES 9
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P43243"
FT MOD_RES 14
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P43243"
FT MOD_RES 22
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P43243"
FT MOD_RES 41
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P43243"
FT MOD_RES 118
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P43243"
FT MOD_RES 126
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P43243"
FT MOD_RES 150
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 157
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P43243"
FT MOD_RES 158
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:P43243"
FT MOD_RES 164
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P43243"
FT MOD_RES 188
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:16452087,
FT ECO:0007744|PubMed:17242355, ECO:0007744|PubMed:19144319,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 195
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 202
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:P43243"
FT MOD_RES 206
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P43243"
FT MOD_RES 208
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P43243"
FT MOD_RES 211
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P43243"
FT MOD_RES 219
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:P43243"
FT MOD_RES 234
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P43243"
FT MOD_RES 264
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P43243"
FT MOD_RES 275
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P43243"
FT MOD_RES 509
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P43243"
FT MOD_RES 511
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P43243"
FT MOD_RES 522
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P43243"
FT MOD_RES 533
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 571
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P43243"
FT MOD_RES 596
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P43243"
FT MOD_RES 598
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19131326,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 604
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 606
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P43243"
FT MOD_RES 653
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P43243"
FT MOD_RES 670
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P43243"
FT MOD_RES 672
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P43243"
FT MOD_RES 673
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P43243"
FT MOD_RES 678
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P43243"
FT MOD_RES 688
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P43243"
FT MOD_RES 740
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P43243"
FT MOD_RES 746
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P43243"
FT MOD_RES 758
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P43244"
FT MOD_RES 835
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0007744|PubMed:23806337"
FT CROSSLNK 3
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2); alternate"
FT /evidence="ECO:0000250|UniProtKB:P43243"
FT CROSSLNK 132
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P43243"
FT CROSSLNK 146
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P43243"
FT CROSSLNK 245
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P43243"
FT CROSSLNK 269
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P43243"
FT CROSSLNK 478
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P43243"
FT CROSSLNK 487
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P43243"
FT CROSSLNK 491
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P43243"
FT CROSSLNK 515
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P43243"
FT CROSSLNK 522
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2); alternate"
FT /evidence="ECO:0000250|UniProtKB:P43243"
FT CROSSLNK 554
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P43243"
FT CROSSLNK 555
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P43243"
FT CROSSLNK 616
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P43243"
FT CROSSLNK 629
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P43243"
FT CROSSLNK 718
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P43243"
FT CROSSLNK 735
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P43243"
FT CROSSLNK 769
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P43243"
FT CROSSLNK 835
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2); alternate"
FT /evidence="ECO:0000250|UniProtKB:P43243"
FT STRAND 399..404
FT /evidence="ECO:0007829|PDB:1X4D"
FT STRAND 408..410
FT /evidence="ECO:0007829|PDB:1X4D"
FT HELIX 411..416
FT /evidence="ECO:0007829|PDB:1X4D"
FT TURN 417..419
FT /evidence="ECO:0007829|PDB:1X4D"
FT HELIX 420..422
FT /evidence="ECO:0007829|PDB:1X4D"
FT STRAND 425..430
FT /evidence="ECO:0007829|PDB:1X4D"
FT STRAND 432..435
FT /evidence="ECO:0007829|PDB:1X4D"
FT STRAND 437..443
FT /evidence="ECO:0007829|PDB:1X4D"
FT HELIX 444..456
FT /evidence="ECO:0007829|PDB:1X4D"
FT STRAND 467..471
FT /evidence="ECO:0007829|PDB:1X4D"
FT STRAND 497..502
FT /evidence="ECO:0007829|PDB:1X4F"
FT HELIX 511..514
FT /evidence="ECO:0007829|PDB:1X4F"
FT TURN 515..520
FT /evidence="ECO:0007829|PDB:1X4F"
FT STRAND 524..529
FT /evidence="ECO:0007829|PDB:1X4F"
FT TURN 530..533
FT /evidence="ECO:0007829|PDB:1X4F"
FT STRAND 534..538
FT /evidence="ECO:0007829|PDB:1X4F"
FT HELIX 542..554
FT /evidence="ECO:0007829|PDB:1X4F"
FT STRAND 559..562
FT /evidence="ECO:0007829|PDB:1X4F"
FT STRAND 565..569
FT /evidence="ECO:0007829|PDB:1X4F"
FT STRAND 573..576
FT /evidence="ECO:0007829|PDB:1X4F"
SQ SEQUENCE 846 AA; 94630 MW; 59C30E63D55093AF CRC64;
MSKSFQQSSL GRDSQGHGRD LSAAGIGLLA AATQSLSMPA SLGRMNQGTA RLASLMNLGM
SSSLNQQGAH SALSSASTSS HNLQSIFNIG SRGPLPLSSQ HRGDTDQASN ILASFGLSAR
DLDELSRYPE DKITPENLPQ ILLQLKRRRT EEGPTLSYGR DGRSATREPP YRVPRDDWEE
KRHFRRDSFD DRGPSLNPVL DYDHGSRSQE SGYYDRMDYE DDRLRDGERC RDDSFFGETS
HNYHKFDSEY ERMGRGPGPL QERSLFEKKR GAPPSSNIED FHGLLPKGYP HLCSICDLPV
HSNKEWSQHI NGASHSRRCQ LLLEIYPEWN PDNDTGHTMG DPFMLQQSTN PAPGILGPPP
PSFHLGGPAV GPRGNLGAGN GNLQGPRHMQ KGRVETSRVV HIMDFQRGKN LRYQLLQLVE
PFGVISNHLI LNKINEAFIE MATTEDAQAA VDYYTTTPAL VFGKPVRVHL SQKYKRIKKP
EGKPDQKFDQ KQELGRVIHL SNLPHSGYSD SAVLKLAEPY GKIKNYILMR MKSQAFIEME
TREDAMAMVD HCLKKALWFQ GRCVKVDLSE KYKKLVLRIP NRGIDLLKKD KSRKRSYSPD
GKESPSDKKS KTDAQKTESP AEGKEQEEKS GEDGEKDTKD DQTEQEPSML LESEDELLVD
EEEAAALLES GSSVGDETDL ANLGDVSSDG KKEPSDKAVK KDPSASATSK KKLKKVDKIE
ELDQENEAAL ENGIKNEENT EPGAESAENA DDPNKDTSEN ADGQNDENKE DYTIPDEYRI
GPYQPNVPVG IDYVIPKTGF YCKLCSLFYT NEEVAKNTHC SSLPHYQKLK KFLNKLAEER
RQKKET
