RBP2_HUMAN
ID RBP2_HUMAN Reviewed; 3224 AA.
AC P49792; Q13074; Q15280; Q53TE2; Q59FH7;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 06-DEC-2005, sequence version 2.
DT 03-AUG-2022, entry version 237.
DE RecName: Full=E3 SUMO-protein ligase RanBP2;
DE EC=2.3.2.- {ECO:0000269|PubMed:11792325, ECO:0000269|PubMed:12032081, ECO:0000269|PubMed:15378033, ECO:0000269|PubMed:15931224, ECO:0000269|PubMed:22194619};
DE AltName: Full=358 kDa nucleoporin;
DE AltName: Full=Nuclear pore complex protein Nup358;
DE AltName: Full=Nucleoporin Nup358;
DE AltName: Full=Ran-binding protein 2;
DE Short=RanBP2;
DE AltName: Full=p270;
GN Name=RANBP2; Synonyms=NUP358;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, DOMAIN, AND SUBCELLULAR
RP LOCATION.
RX PubMed=7775481; DOI=10.1074/jbc.270.23.14209;
RA Wu J., Matunis M.J., Kraemer D., Blobel G., Coutavas E.;
RT "Nup358, a cytoplasmically exposed nucleoporin with peptide repeats, Ran-
RT GTP binding sites, zinc fingers, a cyclophilin A homologous domain, and a
RT leucine-rich region.";
RL J. Biol. Chem. 270:14209-14213(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], IDENTIFICATION IN THE NUCLEAR PORE COMPLEX,
RP SUBCELLULAR LOCATION, AND VARIANT LYS-784.
RC TISSUE=Blood;
RX PubMed=7603572; DOI=10.1038/376184a0;
RA Yokoyama N., Hayashi N., Seki T., Nishii K., Hayashida T., Kuma K.,
RA Miyata T., Fukui M., Nishimoto T., Pante N., Aebi U.;
RT "A giant nucleopore protein that binds Ran/TC4.";
RL Nature 376:184-188(1995).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15815621; DOI=10.1038/nature03466;
RA Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P.,
RA Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C.,
RA Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L.,
RA Du H., Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A.,
RA Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J.,
RA Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M.,
RA Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T.,
RA Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S.,
RA Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K.,
RA McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C.,
RA Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S.,
RA Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C.,
RA Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M.,
RA Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C.,
RA Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J.,
RA Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E.,
RA Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X.,
RA Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M.,
RA Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C.,
RA Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S.,
RA Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H.,
RA Wilson R.K.;
RT "Generation and annotation of the DNA sequences of human chromosomes 2 and
RT 4.";
RL Nature 434:724-731(2005).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 87-3224.
RC TISSUE=Brain;
RA Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S.,
RA Ohara O., Nagase T., Kikuno R.F.;
RL Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 2205-2546.
RC TISSUE=Hippocampus;
RX PubMed=7724562; DOI=10.1073/pnas.92.8.3328;
RA Beddow A.L., Richards S.A., Orem N.R., Macara I.G.;
RT "The Ran/TC4 GTPase-binding domain: identification by expression cloning
RT and characterization of a conserved sequence motif.";
RL Proc. Natl. Acad. Sci. U.S.A. 92:3328-3332(1995).
RN [6]
RP FUNCTION, CATALYTIC ACTIVITY, AND SUMOYLATION.
RX PubMed=11792325; DOI=10.1016/s0092-8674(01)00633-x;
RA Pichler A., Gast A., Seeler J.S., Dejean A., Melchior F.;
RT "The nucleoporin RanBP2 has SUMO1 E3 ligase activity.";
RL Cell 108:109-120(2002).
RN [7]
RP FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=12032081; DOI=10.1093/emboj/21.11.2682;
RA Kirsh O., Seeler J.-S., Pichler A., Gast A., Mueller S., Miska E.,
RA Mathieu M., Harel-Bellan A., Kouzarides T., Melchior F., Dejean A.;
RT "The SUMO E3 ligase RanBP2 promotes modification of the HDAC4
RT deacetylase.";
RL EMBO J. 21:2682-2691(2002).
RN [8]
RP IDENTIFICATION IN THE NUCLEAR PORE COMPLEX, AND SUBCELLULAR LOCATION.
RX PubMed=11839768; DOI=10.1083/jcb.200106046;
RA Frosst P., Guan T., Subauste C., Hahn K., Gerace L.;
RT "Tpr is localized within the nuclear basket of the pore complex and has a
RT role in nuclear protein export.";
RL J. Cell Biol. 156:617-630(2002).
RN [9]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Leukemic T-cell;
RX PubMed=15144186; DOI=10.1021/ac035352d;
RA Brill L.M., Salomon A.R., Ficarro S.B., Mukherji M., Stettler-Gill M.,
RA Peters E.C.;
RT "Robust phosphoproteomic profiling of tyrosine phosphorylation sites from
RT human T cells using immobilized metal affinity chromatography and tandem
RT mass spectrometry.";
RL Anal. Chem. 76:2763-2772(2004).
RN [10]
RP IDENTIFICATION IN A COMPLEX WITH RANGAP1; NXF1 AND NXT1.
RX PubMed=14729961; DOI=10.1128/mcb.24.3.1155-1167.2004;
RA Forler D., Rabut G., Ciccarelli F.D., Herold A., Koecher T., Niggeweg R.,
RA Bork P., Ellenberg J., Izaurralde E.;
RT "RanBP2/Nup358 provides a major binding site for NXF1-p15 dimers at the
RT nuclear pore complex and functions in nuclear mRNA export.";
RL Mol. Cell. Biol. 24:1155-1167(2004).
RN [11]
RP FUNCTION, CATALYTIC ACTIVITY, INTERACTION WITH UBE2I, SUMOYLATION AT
RP LYS-2592, AND MUTAGENESIS OF PRO-2640; LYS-2645; LEU-2651; LYS-2652;
RP LEU-2653; PRO-2654; PRO-2655; THR-2656; PHE-2657; PHE-2658; CYS-2659;
RP ASP-2676; PHE-2677 AND TYR-2689.
RX PubMed=15378033; DOI=10.1038/nsmb834;
RA Pichler A., Knipscheer P., Saitoh H., Sixma T.K., Melchior F.;
RT "The RanBP2 SUMO E3 ligase is neither HECT- nor RING-type.";
RL Nat. Struct. Mol. Biol. 11:984-991(2004).
RN [12]
RP INTERACTION WITH SUMOYLATED RANGAP1, AND MUTAGENESIS OF VAL-2632; ILE-2634
RP AND VAL-2635.
RX PubMed=15388847; DOI=10.1073/pnas.0403498101;
RA Song J., Durrin L.K., Wilkinson T.A., Krontiris T.G., Chen Y.;
RT "Identification of a SUMO-binding motif that recognizes SUMO-modified
RT proteins.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:14373-14378(2004).
RN [13]
RP INTERACTION WITH SUMO1 AND UBE2I.
RX PubMed=15608651; DOI=10.1038/nsmb878;
RA Tatham M.H., Kim S., Jaffray E., Song J., Chen Y., Hay R.T.;
RT "Unique binding interactions among Ubc9, SUMO and RanBP2 reveal a mechanism
RT for SUMO paralog selection.";
RL Nat. Struct. Mol. Biol. 12:67-74(2005).
RN [14]
RP IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=16620772; DOI=10.1016/j.abb.2006.03.002;
RA Li T., Santockyte R., Shen R.-F., Tekle E., Wang G., Yang D.C.H.,
RA Chock P.B.;
RT "A general approach for investigating enzymatic pathways and substrates for
RT ubiquitin-like modifiers.";
RL Arch. Biochem. Biophys. 453:70-74(2006).
RN [15]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
RA Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.;
RT "Global, in vivo, and site-specific phosphorylation dynamics in signaling
RT networks.";
RL Cell 127:635-648(2006).
RN [16]
RP INTERACTION WITH PRKN, AND UBIQUITINATION.
RX PubMed=16332688; DOI=10.1074/jbc.m504994200;
RA Um J.W., Min D.S., Rhim H., Kim J., Paik S.R., Chung K.C.;
RT "Parkin ubiquitinates and promotes the degradation of RanBP2.";
RL J. Biol. Chem. 281:3595-3603(2006).
RN [17]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-21 AND THR-1144, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=16964243; DOI=10.1038/nbt1240;
RA Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.;
RT "A probability-based approach for high-throughput protein phosphorylation
RT analysis and site localization.";
RL Nat. Biotechnol. 24:1285-1292(2006).
RN [18]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18220336; DOI=10.1021/pr0705441;
RA Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D., Yates J.R. III;
RT "Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient
RT phosphoproteomic analysis.";
RL J. Proteome Res. 7:1346-1351(2008).
RN [19]
RP IDENTIFICATION 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 the
RT kinome across the cell cycle.";
RL Mol. Cell 31:438-448(2008).
RN [20]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-19; SER-21; SER-781; SER-948;
RP SER-955; SER-1110; THR-1144; SER-1160; THR-1396; SER-1443; SER-1456;
RP SER-1509; SER-1573; SER-1869; SER-2270; THR-2613; SER-2668; SER-2741;
RP THR-2743 AND SER-2900, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP 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 [21]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=18318008; DOI=10.1002/pmic.200700884;
RA Han G., Ye M., Zhou H., Jiang X., Feng S., Jiang X., Tian R., Wan D.,
RA Zou H., Gu J.;
RT "Large-scale phosphoproteome analysis of human liver tissue by enrichment
RT and fractionation of phosphopeptides with strong anion exchange
RT chromatography.";
RL Proteomics 8:1346-1361(2008).
RN [22]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a
RT refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [23]
RP INTERACTION WITH CDCA8.
RX PubMed=18946085; DOI=10.1091/mbc.e08-05-0511;
RA Klein U.R., Haindl M., Nigg E.A., Muller S.;
RT "RanBP2 and SENP3 function in a mitotic SUMO2/3 conjugation-deconjugation
RT cycle on Borealin.";
RL Mol. Biol. Cell 20:410-418(2009).
RN [24]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-19; SER-21; SER-955;
RP SER-1107; THR-1396; SER-1871; SER-2270; SER-2668 AND SER-2900, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Leukemic T-cell;
RX PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA Rodionov V., Han D.K.;
RT "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT reveals system-wide modulation of protein-protein interactions.";
RL Sci. Signal. 2:RA46-RA46(2009).
RN [25]
RP INTERACTION WITH MCM3AP.
RX PubMed=20005110; DOI=10.1016/j.cub.2009.10.078;
RA Wickramasinghe V.O., McMurtrie P.I., Mills A.D., Takei Y., Penrhyn-Lowe S.,
RA Amagase Y., Main S., Marr J., Stewart M., Laskey R.A.;
RT "mRNA export from mammalian cell nuclei is dependent on GANP.";
RL Curr. Biol. 20:25-31(2010).
RN [26]
RP FUNCTION, IDENTIFICATION IN THE NUCLEAR PORE COMPLEX, INTERACTION WITH
RP BICD2, AND SUBCELLULAR LOCATION.
RX PubMed=20386726; DOI=10.1371/journal.pbio.1000350;
RA Splinter D., Tanenbaum M.E., Lindqvist A., Jaarsma D., Flotho A., Yu K.L.,
RA Grigoriev I., Engelsma D., Haasdijk E.D., Keijzer N., Demmers J.,
RA Fornerod M., Melchior F., Hoogenraad C.C., Medema R.H., Akhmanova A.;
RT "Bicaudal D2, dynein, and kinesin-1 associate with nuclear pore complexes
RT and regulate centrosome and nuclear positioning during mitotic entry.";
RL PLoS Biol. 8:E1000350-E1000350(2010).
RN [27]
RP FUNCTION, AND CAUTION.
RX PubMed=20676357; DOI=10.1371/journal.pbio.1000439;
RA Davis T.L., Walker J.R., Campagna-Slater V., Finerty P.J., Paramanathan R.,
RA Bernstein G., MacKenzie F., Tempel W., Ouyang H., Lee W.H.,
RA Eisenmesser E.Z., Dhe-Paganon S.;
RT "Structural and biochemical characterization of the human cyclophilin
RT family of peptidyl-prolyl isomerases.";
RL PLoS Biol. 8:E1000439-E1000439(2010).
RN [28]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-19; SER-21; SER-781; SER-837;
RP SER-948; SER-955; SER-1110; SER-1160; THR-1412; SER-1509; SER-1835;
RP SER-2900 AND SER-3207, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP 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., Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [29]
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., Buerckstuemmer T.,
RA 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 [30]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1160; SER-1456; SER-2668;
RP SER-2900 AND SER-3207, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP ANALYSIS].
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T.,
RA Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.;
RT "System-wide temporal characterization of the proteome and phosphoproteome
RT of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [31]
RP FUNCTION, AND INTERACTION WITH PML.
RX PubMed=22155184; DOI=10.1053/j.gastro.2011.11.041;
RA Satow R., Shitashige M., Jigami T., Fukami K., Honda K., Kitabayashi I.,
RA Yamada T.;
RT "Beta-catenin inhibits promyelocytic leukemia protein tumor suppressor
RT function in colorectal cancer cells.";
RL Gastroenterology 142:572-581(2012).
RN [32]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-21; THR-779; SER-781;
RP SER-948; SER-955; THR-1098; SER-1103; SER-1107; SER-1110; THR-1144;
RP SER-1160; SER-1249; THR-1396; THR-1412; SER-1450; SER-1456; SER-1509;
RP SER-1520; SER-1573; SER-1833; SER-1835; SER-1869; SER-2270; SER-2526;
RP THR-2613; TYR-2666; SER-2668; SER-2805 AND SER-3207, AND IDENTIFICATION BY
RP 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 [33]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-955; SER-1160; SER-1450;
RP SER-1456; SER-1509; SER-2668 AND SER-2900, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [34]
RP METHYLATION [LARGE SCALE ANALYSIS] AT ARG-945 AND ARG-1016, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Colon carcinoma;
RX PubMed=24129315; DOI=10.1074/mcp.o113.027870;
RA Guo A., Gu H., Zhou J., Mulhern D., Wang Y., Lee K.A., Yang V., Aguiar M.,
RA Kornhauser J., Jia X., Ren J., Beausoleil S.A., Silva J.C., Vemulapalli V.,
RA Bedford M.T., Comb M.J.;
RT "Immunoaffinity enrichment and mass spectrometry analysis of protein
RT methylation.";
RL Mol. Cell. Proteomics 13:372-387(2014).
RN [35]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-1414, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25218447; DOI=10.1038/nsmb.2890;
RA Hendriks I.A., D'Souza R.C., Yang B., Verlaan-de Vries M., Mann M.,
RA Vertegaal A.C.;
RT "Uncovering global SUMOylation signaling networks in a site-specific
RT manner.";
RL Nat. Struct. Mol. Biol. 21:927-936(2014).
RN [36]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-1605; LYS-1664; LYS-1723;
RP LYS-2594 AND LYS-2792, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP 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 [37]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-1414, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25772364; DOI=10.1016/j.celrep.2015.02.033;
RA Hendriks I.A., Treffers L.W., Verlaan-de Vries M., Olsen J.V.,
RA Vertegaal A.C.;
RT "SUMO-2 orchestrates chromatin modifiers in response to DNA damage.";
RL Cell Rep. 10:1778-1791(2015).
RN [38]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-1414; LYS-1605; LYS-1664 AND
RP LYS-1723, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25755297; DOI=10.1074/mcp.o114.044792;
RA Xiao Z., Chang J.G., Hendriks I.A., Sigurdsson J.O., Olsen J.V.,
RA Vertegaal A.C.;
RT "System-wide analysis of SUMOylation dynamics in response to replication
RT stress reveals novel small ubiquitin-like modified target proteins and
RT acceptor lysines relevant for genome stability.";
RL Mol. Cell. Proteomics 14:1419-1434(2015).
RN [39]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-1350; LYS-1414; LYS-1596;
RP LYS-1605; LYS-1655; LYS-1664; LYS-1714; LYS-1723; LYS-2022; LYS-2522;
RP LYS-2594; LYS-2612; LYS-2792 AND LYS-2815, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE 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-modification
RT with phosphorylation.";
RL Nat. Struct. Mol. Biol. 24:325-336(2017).
RN [40]
RP X-RAY CRYSTALLOGRAPHY (2.96 ANGSTROMS) OF 1171-1304, AND FUNCTION.
RX PubMed=10078529; DOI=10.1038/17969;
RA Vetter I.R., Nowak C., Nishimoto T., Kuhlmann J., Wittinghofer A.;
RT "Structure of a Ran-binding domain complexed with Ran bound to a GTP
RT analogue: implications for nuclear transport.";
RL Nature 398:39-46(1999).
RN [41]
RP STRUCTURE BY NMR OF 2028-2154.
RX PubMed=15826666; DOI=10.1016/j.jmb.2005.02.033;
RA Geyer J.P., Doker R., Kremer W., Zhao X., Kuhlmann J., Kalbitzer H.R.;
RT "Solution structure of the Ran-binding domain 2 of RanBP2 and its
RT interaction with the C terminus of Ran.";
RL J. Mol. Biol. 348:711-725(2005).
RN [42]
RP X-RAY CRYSTALLOGRAPHY (3.01 ANGSTROMS) OF 2631-2711 IN COMPLEX WITH SUMO1;
RP RANGAP1 AND UBE2I, FUNCTION, CATALYTIC ACTIVITY, AND SUBUNIT.
RX PubMed=15931224; DOI=10.1038/nature03588;
RA Reverter D., Lima C.D.;
RT "Insights into E3 ligase activity revealed by a SUMO-RanGAP1-Ubc9-Nup358
RT complex.";
RL Nature 435:687-692(2005).
RN [43]
RP X-RAY CRYSTALLOGRAPHY (2.29 ANGSTROMS) OF 2631-2695 IN COMPLEX WITH SUMO1;
RP RANGAP1 AND UBE2I, FUNCTION, CATALYTIC ACTIVITY, AND SUBUNIT.
RX PubMed=22194619; DOI=10.1074/jbc.m111.321141;
RA Gareau J.R., Reverter D., Lima C.D.;
RT "Determinants of small ubiquitin-like modifier 1 (SUMO1) protein
RT specificity, E3 ligase, and SUMO-RanGAP1 binding activities of nucleoporin
RT RanBP2.";
RL J. Biol. Chem. 287:4740-4751(2012).
RN [44]
RP X-RAY CRYSTALLOGRAPHY (1.15 ANGSTROMS) OF 1-145, AND TPR REPEATS.
RX PubMed=22959972; DOI=10.1016/j.jmb.2012.08.026;
RA Kassube S.A., Stuwe T., Lin D.H., Antonuk C.D., Napetschnig J., Blobel G.,
RA Hoelz A.;
RT "Crystal structure of the N-terminal domain of Nup358/RanBP2.";
RL J. Mol. Biol. 423:752-765(2012).
RN [45]
RP X-RAY CRYSTALLOGRAPHY (1.75 ANGSTROMS) OF 3062-3224, FUNCTION,
RP IDENTIFICATION IN THE NUCLEAR PORE COMPLEX, SUBCELLULAR LOCATION, DOMAIN,
RP AND CAUTION.
RX PubMed=23353830; DOI=10.1016/j.jmb.2013.01.021;
RA Lin D.H., Zimmermann S., Stuwe T., Stuwe E., Hoelz A.;
RT "Structural and functional analysis of the C-terminal domain of
RT Nup358/RanBP2.";
RL J. Mol. Biol. 425:1318-1329(2013).
RN [46]
RP VARIANTS IIAE3 MET-585; ILE-653 AND VAL-656.
RX PubMed=19118815; DOI=10.1016/j.ajhg.2008.12.009;
RA Neilson D.E., Adams M.D., Orr C.M.D., Schelling D.K., Eiben R.M.,
RA Kerr D.S., Anderson J., Bassuk A.G., Bye A.M., Childs A.-M., Clarke A.,
RA Crow Y.J., Di Rocco M., Dohna-Schwake C., Dueckers G., Fasano A.E.,
RA Gika A.D., Gionnis D., Gorman M.P., Grattan-Smith P.J., Hackenberg A.,
RA Kuster A., Lentschig M.G., Lopez-Laso E., Marco E.J., Mastroyianni S.,
RA Perrier J., Schmitt-Mechelke T., Servidei S., Skardoutsou A., Uldall P.,
RA van der Knaap M.S., Goglin K.C., Tefft D.L., Aubin C., de Jager P.,
RA Hafler D., Warman M.L.;
RT "Infection-triggered familial or recurrent cases of acute necrotizing
RT encephalopathy caused by mutations in a component of the nuclear pore,
RT RANBP2.";
RL Am. J. Hum. Genet. 84:44-51(2009).
RN [47]
RP CHROMOSOMAL TRANSLOCATION WITH FGFR1.
RX PubMed=23041776; DOI=10.1038/leu.2012.286;
RA Gervais C., Dano L., Perrusson N., Helias C., Jeandidier E., Galoisy A.C.,
RA Ittel A., Herbrecht R., Bilger K., Mauvieux L.;
RT "A translocation t(2;8)(q12;p11) fuses FGFR1 to a novel partner gene,
RT RANBP2/NUP358, in a myeloproliferative/myelodysplastic neoplasm.";
RL Leukemia 27:1186-1188(2013).
RN [48]
RP VARIANT IIAE3 MET-585, CHARACTERIZATION OF VARIANT IIAE3 MET-585, AND
RP INTERACTION WITH COX11.
RX PubMed=34400285; DOI=10.1016/j.neulet.2021.136173;
RA Shibata A., Kasai M., Hoshino A., Tanaka T., Mizuguchi M.;
RT "RANBP2 mutation causing autosomal dominant acute necrotizing
RT encephalopathy attenuates its interaction with COX11.";
RL Neurosci. Lett. 763:136173-136173(2021).
CC -!- FUNCTION: E3 SUMO-protein ligase which facilitates SUMO1 and SUMO2
CC conjugation by UBE2I (PubMed:11792325, PubMed:12032081,
CC PubMed:15378033, PubMed:22194619, PubMed:15931224). Involved in
CC transport factor (Ran-GTP, karyopherin)-mediated protein import via the
CC F-G repeat-containing domain which acts as a docking site for
CC substrates (PubMed:7775481). Binds single-stranded RNA (in vitro)
CC (PubMed:7775481). May bind DNA (PubMed:7775481). Component of the
CC nuclear export pathway (PubMed:10078529). Specific docking site for the
CC nuclear export factor exportin-1 (PubMed:10078529). Sumoylates PML at
CC 'Lys-490' which is essential for the proper assembly of PML-NB
CC (PubMed:22155184). Recruits BICD2 to the nuclear envelope and
CC cytoplasmic stacks of nuclear pore complex known as annulate lamellae
CC during G2 phase of cell cycle (PubMed:20386726). Probable inactive
CC PPIase with no peptidyl-prolyl cis-trans isomerase activity
CC (PubMed:20676357, PubMed:23353830). {ECO:0000269|PubMed:11792325,
CC ECO:0000269|PubMed:12032081, ECO:0000269|PubMed:15378033,
CC ECO:0000269|PubMed:15931224, ECO:0000269|PubMed:20386726,
CC ECO:0000269|PubMed:20676357, ECO:0000269|PubMed:22155184,
CC ECO:0000269|PubMed:22194619, ECO:0000269|PubMed:23353830,
CC ECO:0000269|PubMed:7775481, ECO:0000303|PubMed:10078529}.
CC -!- PATHWAY: Protein modification; protein sumoylation.
CC -!- SUBUNIT: Part of the nuclear pore complex (PubMed:11839768,
CC PubMed:20386726, PubMed:23353830, PubMed:7603572). Forms a complex with
CC NXT1, NXF1 and RANGAP1 (PubMed:14729961). Forms a tight complex with
CC RANBP1 and UBE2I (PubMed:15388847, PubMed:10078529, PubMed:15826666).
CC Interacts with SUMO1 but not SUMO2 (PubMed:15388847, PubMed:10078529,
CC PubMed:15826666). Interacts with PRKN (PubMed:16332688). Interacts with
CC sumoylated RANGAP1 (PubMed:15378033, PubMed:10078529, PubMed:15826666).
CC Interacts with CDCA8 (PubMed:19413330). Interacts with PML (isoform
CC PML-4) (PubMed:22155184). Interacts with BICD2 (PubMed:20386726).
CC Interacts with MCM3AP isoform GANP (PubMed:20005110). Interacts with
CC COX11 (PubMed:34400285). {ECO:0000269|PubMed:10078529,
CC ECO:0000269|PubMed:11839768, ECO:0000269|PubMed:14729961,
CC ECO:0000269|PubMed:15378033, ECO:0000269|PubMed:15388847,
CC ECO:0000269|PubMed:15826666, ECO:0000269|PubMed:16332688,
CC ECO:0000269|PubMed:20005110, ECO:0000269|PubMed:20386726,
CC ECO:0000269|PubMed:22155184, ECO:0000269|PubMed:23353830,
CC ECO:0000269|PubMed:34400285, ECO:0000269|PubMed:7603572}.
CC -!- INTERACTION:
CC P49792; Q8TD16: BICD2; NbExp=2; IntAct=EBI-973138, EBI-2372628;
CC P49792; P04626: ERBB2; NbExp=3; IntAct=EBI-973138, EBI-641062;
CC P49792; Q53GG5: PDLIM3; NbExp=3; IntAct=EBI-973138, EBI-5658852;
CC P49792; O60260: PRKN; NbExp=11; IntAct=EBI-973138, EBI-716346;
CC P49792; P62826: RAN; NbExp=4; IntAct=EBI-973138, EBI-286642;
CC P49792; P46060: RANGAP1; NbExp=4; IntAct=EBI-973138, EBI-396091;
CC P49792; P63279: UBE2I; NbExp=3; IntAct=EBI-973138, EBI-80168;
CC P49792; Q921C5-1: Bicd2; Xeno; NbExp=4; IntAct=EBI-973138, EBI-642995;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:7775481}. Nucleus
CC membrane {ECO:0000269|PubMed:11839768}. Nucleus, nuclear pore complex
CC {ECO:0000269|PubMed:11839768, ECO:0000269|PubMed:20386726,
CC ECO:0000269|PubMed:23353830, ECO:0000269|PubMed:7603572}. Nucleus
CC envelope {ECO:0000269|PubMed:20386726}. Note=Detected in diffuse and
CC discrete intranuclear foci (PubMed:11839768). Cytoplasmic filaments
CC (PubMed:7775481). {ECO:0000269|PubMed:11839768,
CC ECO:0000269|PubMed:7775481}.
CC -!- DOMAIN: Contains FG repeats. FG repeats are interaction sites for
CC karyopherins (importins, exportins) and form probably an affinity
CC gradient, guiding the transport proteins unidirectionally with their
CC cargo through the NPC. FG repeat regions are highly flexible and lack
CC ordered secondary structure. The overall conservation of FG repeats
CC regarding exact sequence, spacing, and repeat unit length is limited.
CC {ECO:0000305}.
CC -!- DOMAIN: The PPIase cyclophilin-type domain has high structural
CC similarity with PPIA, but has extremely low and barely detectable
CC proline isomerase activity (in vitro) (PubMed:23353830). Only about
CC half of the residues that surround the PPIA active site cleft are
CC conserved. {ECO:0000269|PubMed:23353830}.
CC -!- PTM: Polyubiquitinated by PRKN, which leads to proteasomal degradation.
CC {ECO:0000269|PubMed:16332688}.
CC -!- PTM: The inner channel of the NPC has a different redox environment
CC from the cytoplasm and allows the formation of interchain disulfide
CC bonds between some nucleoporins, the significant increase of these
CC linkages upon oxidative stress reduces the permeability of the NPC.
CC {ECO:0000250|UniProtKB:Q9ERU9}.
CC -!- DISEASE: Encephalopathy, acute, infection-induced, 3 (IIAE3)
CC [MIM:608033]: A rapidly progressive encephalopathy manifesting in
CC susceptible individuals with seizures and coma. It can occur within
CC days in otherwise healthy children after common viral infections such
CC as influenza and parainfluenza, without evidence of viral infection of
CC the brain or inflammatory cell infiltration. Brain T2-weighted magnetic
CC resonance imaging reveals characteristic symmetric lesions present in
CC the thalami, pons and brainstem. {ECO:0000269|PubMed:19118815,
CC ECO:0000269|PubMed:34400285}. Note=The disease is caused by variants
CC affecting the gene represented in this entry. Mutations in the RANBP2
CC gene predispose to IIAE3, but by themselves are insufficient to make
CC the phenotype fully penetrant; additional genetic and environmental
CC factors are required (PubMed:19118815). {ECO:0000269|PubMed:19118815}.
CC -!- DISEASE: Note=A chromosomal aberration involving RANBP2 is a cause of
CC chromosome 8p11 myeloproliferative syndrome. Translocation
CC t(2;8)(q12;p11) with FGFR1. Chromosome 8p11 myeloproliferative syndrome
CC is characterized by myeloid hyperplasia, eosinophilia and T-cell or B-
CC cell lymphoblastic lymphoma. In general it progresses to acute myeloid
CC leukemia. {ECO:0000269|PubMed:23041776}.
CC -!- SIMILARITY: Belongs to the RanBP2 E3 ligase family. {ECO:0000305}.
CC -!- CAUTION: Despite the presence of a PPIase cyclophilin-type domain, it
CC has probably no peptidyl-prolyl cis-trans isomerase activity.
CC {ECO:0000269|PubMed:20676357, ECO:0000269|PubMed:23353830}.
CC -!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology and
CC Haematology;
CC URL="http://atlasgeneticsoncology.org/Genes/RANBP2ID483.html";
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DR EMBL; L41840; AAC41758.1; -; Genomic_DNA.
DR EMBL; D42063; BAA07662.1; -; mRNA.
DR EMBL; AC010095; AAY14984.1; -; Genomic_DNA.
DR EMBL; AB209483; BAD92720.1; -; mRNA.
DR EMBL; U19248; AAA85838.1; -; mRNA.
DR CCDS; CCDS2079.1; -.
DR PIR; S58884; S58884.
DR RefSeq; NP_006258.3; NM_006267.4.
DR PDB; 1RRP; X-ray; 2.96 A; B/D=1171-1304.
DR PDB; 1XKE; NMR; -; A=2028-2154.
DR PDB; 1Z5S; X-ray; 3.01 A; D=2631-2711.
DR PDB; 2LAS; NMR; -; B=2705-2717.
DR PDB; 3UIN; X-ray; 2.60 A; D=2629-2695.
DR PDB; 3UIO; X-ray; 2.60 A; D=2631-2695.
DR PDB; 3UIP; X-ray; 2.29 A; D=2631-2695.
DR PDB; 4GA0; X-ray; 1.15 A; A=1-145.
DR PDB; 4I9Y; X-ray; 1.75 A; A/B/C/D/E/F=3062-3224.
DR PDB; 4L6E; X-ray; 2.50 A; A=2907-3050.
DR PDB; 4LQW; X-ray; 1.95 A; A/B=3057-3224.
DR PDB; 5CLL; X-ray; 2.45 A; B/D=1155-1321.
DR PDB; 5CLQ; X-ray; 3.20 A; B/D=1155-1321.
DR PDBsum; 1RRP; -.
DR PDBsum; 1XKE; -.
DR PDBsum; 1Z5S; -.
DR PDBsum; 2LAS; -.
DR PDBsum; 3UIN; -.
DR PDBsum; 3UIO; -.
DR PDBsum; 3UIP; -.
DR PDBsum; 4GA0; -.
DR PDBsum; 4I9Y; -.
DR PDBsum; 4L6E; -.
DR PDBsum; 4LQW; -.
DR PDBsum; 5CLL; -.
DR PDBsum; 5CLQ; -.
DR SMR; P49792; -.
DR BioGRID; 111839; 246.
DR ComplexPortal; CPX-4747; E3 ligase (RANBP2) complex.
DR ComplexPortal; CPX-873; Nuclear pore complex.
DR DIP; DIP-37654N; -.
DR IntAct; P49792; 101.
DR MINT; P49792; -.
DR STRING; 9606.ENSP00000283195; -.
DR TCDB; 1.I.1.1.3; the nuclear pore complex (npc) family.
DR GlyConnect; 2890; 1 O-Linked glycan (1 site).
DR GlyGen; P49792; 36 sites, 1 N-linked glycan (1 site), 2 O-linked glycans (35 sites).
DR iPTMnet; P49792; -.
DR MetOSite; P49792; -.
DR PhosphoSitePlus; P49792; -.
DR SwissPalm; P49792; -.
DR BioMuta; RANBP2; -.
DR DMDM; 83305554; -.
DR OGP; P49792; -.
DR CPTAC; CPTAC-996; -.
DR EPD; P49792; -.
DR jPOST; P49792; -.
DR MassIVE; P49792; -.
DR MaxQB; P49792; -.
DR PaxDb; P49792; -.
DR PeptideAtlas; P49792; -.
DR PRIDE; P49792; -.
DR ProteomicsDB; 56121; -.
DR Antibodypedia; 33105; 209 antibodies from 24 providers.
DR DNASU; 5903; -.
DR Ensembl; ENST00000283195.11; ENSP00000283195.6; ENSG00000153201.16.
DR GeneID; 5903; -.
DR KEGG; hsa:5903; -.
DR MANE-Select; ENST00000283195.11; ENSP00000283195.6; NM_006267.5; NP_006258.3.
DR UCSC; uc002tem.4; human.
DR CTD; 5903; -.
DR DisGeNET; 5903; -.
DR GeneCards; RANBP2; -.
DR HGNC; HGNC:9848; RANBP2.
DR HPA; ENSG00000153201; Low tissue specificity.
DR MalaCards; RANBP2; -.
DR MIM; 601181; gene.
DR MIM; 608033; phenotype.
DR neXtProt; NX_P49792; -.
DR OpenTargets; ENSG00000153201; -.
DR Orphanet; 263524; Acute necrotizing encephalopathy of childhood.
DR Orphanet; 88619; Familial acute necrotizing encephalopathy.
DR Orphanet; 178342; Inflammatory myofibroblastic tumor.
DR PharmGKB; PA34209; -.
DR VEuPathDB; HostDB:ENSG00000153201; -.
DR eggNOG; KOG0864; Eukaryota.
DR eggNOG; KOG0865; Eukaryota.
DR GeneTree; ENSGT00940000154389; -.
DR HOGENOM; CLU_000378_1_0_1; -.
DR InParanoid; P49792; -.
DR OMA; FRFVDKE; -.
DR OrthoDB; 201737at2759; -.
DR PhylomeDB; P49792; -.
DR TreeFam; TF314797; -.
DR PathwayCommons; P49792; -.
DR Reactome; R-HSA-1169408; ISG15 antiviral mechanism.
DR Reactome; R-HSA-141444; Amplification of signal from unattached kinetochores via a MAD2 inhibitory signal.
DR Reactome; R-HSA-159227; Transport of the SLBP independent Mature mRNA.
DR Reactome; R-HSA-159230; Transport of the SLBP Dependant Mature mRNA.
DR Reactome; R-HSA-159231; Transport of Mature mRNA Derived from an Intronless Transcript.
DR Reactome; R-HSA-159236; Transport of Mature mRNA derived from an Intron-Containing Transcript.
DR Reactome; R-HSA-165054; Rev-mediated nuclear export of HIV RNA.
DR Reactome; R-HSA-168271; Transport of Ribonucleoproteins into the Host Nucleus.
DR Reactome; R-HSA-168276; NS1 Mediated Effects on Host Pathways.
DR Reactome; R-HSA-168325; Viral Messenger RNA Synthesis.
DR Reactome; R-HSA-168333; NEP/NS2 Interacts with the Cellular Export Machinery.
DR Reactome; R-HSA-170822; Regulation of Glucokinase by Glucokinase Regulatory Protein.
DR Reactome; R-HSA-180746; Nuclear import of Rev protein.
DR Reactome; R-HSA-180910; Vpr-mediated nuclear import of PICs.
DR Reactome; R-HSA-191859; snRNP Assembly.
DR Reactome; R-HSA-2467813; Separation of Sister Chromatids.
DR Reactome; R-HSA-2500257; Resolution of Sister Chromatid Cohesion.
DR Reactome; R-HSA-3108214; SUMOylation of DNA damage response and repair proteins.
DR Reactome; R-HSA-3232142; SUMOylation of ubiquitinylation proteins.
DR Reactome; R-HSA-3301854; Nuclear Pore Complex (NPC) Disassembly.
DR Reactome; R-HSA-3371453; Regulation of HSF1-mediated heat shock response.
DR Reactome; R-HSA-4085377; SUMOylation of SUMOylation proteins.
DR Reactome; R-HSA-4551638; SUMOylation of chromatin organization proteins.
DR Reactome; R-HSA-4570464; SUMOylation of RNA binding proteins.
DR Reactome; R-HSA-4615885; SUMOylation of DNA replication proteins.
DR Reactome; R-HSA-5578749; Transcriptional regulation by small RNAs.
DR Reactome; R-HSA-5619107; Defective TPR may confer susceptibility towards thyroid papillary carcinoma (TPC).
DR Reactome; R-HSA-5663220; RHO GTPases Activate Formins.
DR Reactome; R-HSA-6784531; tRNA processing in the nucleus.
DR Reactome; R-HSA-68877; Mitotic Prometaphase.
DR Reactome; R-HSA-9609690; HCMV Early Events.
DR Reactome; R-HSA-9610379; HCMV Late Events.
DR Reactome; R-HSA-9648025; EML4 and NUDC in mitotic spindle formation.
DR Reactome; R-HSA-9705671; SARS-CoV-2 activates/modulates innate and adaptive immune responses.
DR Reactome; R-HSA-9725370; Signaling by ALK fusions and activated point mutants.
DR SignaLink; P49792; -.
DR SIGNOR; P49792; -.
DR UniPathway; UPA00886; -.
DR BioGRID-ORCS; 5903; 409 hits in 1078 CRISPR screens.
DR ChiTaRS; RANBP2; human.
DR EvolutionaryTrace; P49792; -.
DR GeneWiki; RANBP2; -.
DR GenomeRNAi; 5903; -.
DR Pharos; P49792; Tbio.
DR PRO; PR:P49792; -.
DR Proteomes; UP000005640; Chromosome 2.
DR RNAct; P49792; protein.
DR Bgee; ENSG00000153201; Expressed in endothelial cell and 214 other tissues.
DR ExpressionAtlas; P49792; baseline and differential.
DR Genevisible; P49792; HS.
DR GO; GO:0005642; C:annulate lamellae; IDA:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; IDA:HPA.
DR GO; GO:0016020; C:membrane; HDA:UniProtKB.
DR GO; GO:0005635; C:nuclear envelope; IDA:UniProtKB.
DR GO; GO:0042405; C:nuclear inclusion body; IDA:UniProtKB.
DR GO; GO:0031965; C:nuclear membrane; IDA:UniProtKB.
DR GO; GO:0005643; C:nuclear pore; IDA:UniProtKB.
DR GO; GO:0044614; C:nuclear pore cytoplasmic filaments; IDA:GO_Central.
DR GO; GO:0044615; C:nuclear pore nuclear basket; IDA:UniProtKB.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0106068; C:SUMO ligase complex; IPI:ComplexPortal.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR GO; GO:0031267; F:small GTPase binding; IPI:GO_Central.
DR GO; GO:0061665; F:SUMO ligase activity; IDA:UniProtKB.
DR GO; GO:0019789; F:SUMO transferase activity; EXP:Reactome.
DR GO; GO:0051642; P:centrosome localization; IMP:UniProtKB.
DR GO; GO:0051028; P:mRNA transport; IEA:UniProtKB-KW.
DR GO; GO:0006607; P:NLS-bearing protein import into nucleus; IMP:GO_Central.
DR GO; GO:0051168; P:nuclear export; IC:ComplexPortal.
DR GO; GO:0006913; P:nucleocytoplasmic transport; IC:ComplexPortal.
DR GO; GO:0033133; P:positive regulation of glucokinase activity; IEA:Ensembl.
DR GO; GO:0006457; P:protein folding; IEA:InterPro.
DR GO; GO:0000413; P:protein peptidyl-prolyl isomerization; IEA:InterPro.
DR GO; GO:0016925; P:protein sumoylation; IDA:UniProtKB.
DR GO; GO:0006111; P:regulation of gluconeogenesis; IEA:Ensembl.
DR Gene3D; 1.25.40.10; -; 1.
DR Gene3D; 2.30.29.30; -; 4.
DR Gene3D; 2.40.100.10; -; 1.
DR IDEAL; IID00151; -.
DR InterPro; IPR029000; Cyclophilin-like_dom_sf.
DR InterPro; IPR020892; Cyclophilin-type_PPIase_CS.
DR InterPro; IPR002130; Cyclophilin-type_PPIase_dom.
DR InterPro; IPR022011; IR1-M.
DR InterPro; IPR011993; PH-like_dom_sf.
DR InterPro; IPR000156; Ran_bind_dom.
DR InterPro; IPR045255; RanBP1-like.
DR InterPro; IPR011990; TPR-like_helical_dom_sf.
DR InterPro; IPR019734; TPR_repeat.
DR InterPro; IPR001876; Znf_RanBP2.
DR InterPro; IPR036443; Znf_RanBP2_sf.
DR PANTHER; PTHR23138; PTHR23138; 4.
DR Pfam; PF12185; IR1-M; 2.
DR Pfam; PF00160; Pro_isomerase; 1.
DR Pfam; PF00638; Ran_BP1; 4.
DR Pfam; PF00641; zf-RanBP; 8.
DR PRINTS; PR00153; CSAPPISMRASE.
DR SMART; SM00160; RanBD; 4.
DR SMART; SM00028; TPR; 1.
DR SMART; SM00547; ZnF_RBZ; 8.
DR SUPFAM; SSF48452; SSF48452; 1.
DR SUPFAM; SSF50891; SSF50891; 1.
DR SUPFAM; SSF90209; SSF90209; 7.
DR PROSITE; PS00170; CSA_PPIASE_1; 1.
DR PROSITE; PS50072; CSA_PPIASE_2; 1.
DR PROSITE; PS50196; RANBD1; 4.
DR PROSITE; PS50005; TPR; 1.
DR PROSITE; PS50293; TPR_REGION; 1.
DR PROSITE; PS01358; ZF_RANBP2_1; 8.
DR PROSITE; PS50199; ZF_RANBP2_2; 8.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Chromosomal rearrangement; Disulfide bond;
KW Isopeptide bond; Membrane; Metal-binding; Methylation; mRNA transport;
KW Nuclear pore complex; Nucleus; Phosphoprotein; Protein transport;
KW Reference proteome; Repeat; RNA-binding; TPR repeat; Transferase;
KW Translocation; Transport; Ubl conjugation; Ubl conjugation pathway; Zinc;
KW Zinc-finger.
FT CHAIN 1..3224
FT /note="E3 SUMO-protein ligase RanBP2"
FT /id="PRO_0000204913"
FT REPEAT 26..59
FT /note="TPR 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00339,
FT ECO:0000269|PubMed:22959972"
FT REPEAT 60..93
FT /note="TPR 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00339,
FT ECO:0000269|PubMed:22959972"
FT REPEAT 94..128
FT /note="TPR 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00339,
FT ECO:0000269|PubMed:22959972"
FT REPEAT 165..201
FT /note="TPR 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00339,
FT ECO:0000269|PubMed:22959972"
FT REPEAT 287..319
FT /note="TPR 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00339,
FT ECO:0000269|PubMed:22959972"
FT REPEAT 583..616
FT /note="TPR 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00339,
FT ECO:0000269|PubMed:22959972"
FT REPEAT 648..681
FT /note="TPR 7"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00339,
FT ECO:0000269|PubMed:22959972"
FT REPEAT 1001..1002
FT /note="1"
FT /evidence="ECO:0000305"
FT REPEAT 1101..1102
FT /note="2"
FT /evidence="ECO:0000305"
FT REPEAT 1142..1143
FT /note="3"
FT /evidence="ECO:0000305"
FT DOMAIN 1171..1307
FT /note="RanBD1 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00164"
FT REPEAT 1459..1460
FT /note="4"
FT /evidence="ECO:0000305"
FT REPEAT 1523..1524
FT /note="5"
FT /evidence="ECO:0000305"
FT REPEAT 1586..1587
FT /note="6"
FT /evidence="ECO:0000305"
FT REPEAT 1852..1853
FT /note="7"
FT /evidence="ECO:0000305"
FT REPEAT 1861..1862
FT /note="8"
FT /evidence="ECO:0000305"
FT REPEAT 1900..1901
FT /note="9"
FT /evidence="ECO:0000305"
FT REPEAT 1938..1939
FT /note="10"
FT /evidence="ECO:0000305"
FT REPEAT 1961..1962
FT /note="11"
FT /evidence="ECO:0000305"
FT DOMAIN 2012..2148
FT /note="RanBD1 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00164"
FT REPEAT 2260..2261
FT /note="12"
FT /evidence="ECO:0000305"
FT DOMAIN 2309..2445
FT /note="RanBD1 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00164"
FT REPEAT 2516..2517
FT /note="13"
FT /evidence="ECO:0000305"
FT REPEAT 2535..2536
FT /note="14"
FT /evidence="ECO:0000305"
FT REPEAT 2545..2546
FT /note="15"
FT /evidence="ECO:0000305"
FT REPEAT 2633..2685
FT /note="1"
FT /evidence="ECO:0000269|PubMed:22959972"
FT REPEAT 2711..2761
FT /note="2"
FT /evidence="ECO:0000269|PubMed:22959972"
FT REPEAT 2840..2841
FT /note="16"
FT /evidence="ECO:0000305"
FT REPEAT 2842..2843
FT /note="17"
FT /evidence="ECO:0000305"
FT REPEAT 2863..2864
FT /note="18"
FT /evidence="ECO:0000305"
FT REPEAT 2880..2881
FT /note="19"
FT /evidence="ECO:0000305"
FT DOMAIN 2911..3046
FT /note="RanBD1 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00164"
FT DOMAIN 3067..3223
FT /note="PPIase cyclophilin-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00156"
FT REPEAT 3106..3107
FT /note="20"
FT /evidence="ECO:0000305"
FT REPEAT 3189..3190
FT /note="21"
FT /evidence="ECO:0000305"
FT REPEAT 3205..3206
FT /note="22"
FT /evidence="ECO:0000305"
FT ZN_FING 1351..1381
FT /note="RanBP2-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00322"
FT ZN_FING 1415..1444
FT /note="RanBP2-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00322"
FT ZN_FING 1479..1508
FT /note="RanBP2-type 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00322"
FT ZN_FING 1543..1572
FT /note="RanBP2-type 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00322"
FT ZN_FING 1606..1635
FT /note="RanBP2-type 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00322"
FT ZN_FING 1665..1694
FT /note="RanBP2-type 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00322"
FT ZN_FING 1724..1753
FT /note="RanBP2-type 7"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00322"
FT ZN_FING 1781..1810
FT /note="RanBP2-type 8"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00322"
FT REGION 760..802
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1001..3206
FT /note="22 X 2 AA repeats of F-G"
FT /evidence="ECO:0000305"
FT REGION 1138..1174
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1569..1595
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1633..1657
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1692..1716
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1903..1928
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2147..2287
FT /note="Interaction with BICD2"
FT /evidence="ECO:0000269|PubMed:20386726"
FT REGION 2188..2224
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2273..2307
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2486..2509
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2556..2584
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2631..2635
FT /note="Interaction with sumoylated RANGAP1"
FT REGION 2633..2761
FT /note="2 X 50 AA approximate repeats"
FT REGION 2633..2710
FT /note="Required for E3 SUMO-ligase activity"
FT REGION 2633..2685
FT /note="Interaction with UBE2I"
FT REGION 2686..2761
FT /note="Interaction with SUMO1"
FT /evidence="ECO:0000269|PubMed:15608651"
FT REGION 2793..2818
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 772..795
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1155..1174
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1633..1654
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1692..1713
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2202..2221
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2273..2295
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2493..2507
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2795..2815
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT SITE 932..933
FT /note="Breakpoint for translocation to form RANBP2-FGFR1
FT protein"
FT /evidence="ECO:0000269|PubMed:23041776"
FT MOD_RES 19
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231"
FT MOD_RES 21
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:16964243,
FT ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:19690332,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163"
FT MOD_RES 779
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 781
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163"
FT MOD_RES 788
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9ERU9"
FT MOD_RES 837
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231"
FT MOD_RES 945
FT /note="Asymmetric dimethylarginine"
FT /evidence="ECO:0007744|PubMed:24129315"
FT MOD_RES 948
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163"
FT MOD_RES 955
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569"
FT MOD_RES 1016
FT /note="Asymmetric dimethylarginine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q9ERU9"
FT MOD_RES 1016
FT /note="Omega-N-methylarginine; alternate"
FT /evidence="ECO:0007744|PubMed:24129315"
FT MOD_RES 1098
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 1103
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 1107
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19690332,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 1110
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163"
FT MOD_RES 1144
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:16964243,
FT ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:23186163"
FT MOD_RES 1160
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
FT ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569"
FT MOD_RES 1249
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 1396
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:23186163"
FT MOD_RES 1412
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 1443
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 1450
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163,
FT ECO:0007744|PubMed:24275569"
FT MOD_RES 1456
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163,
FT ECO:0007744|PubMed:24275569"
FT MOD_RES 1509
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163,
FT ECO:0007744|PubMed:24275569"
FT MOD_RES 1520
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 1573
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 1833
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 1835
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 1869
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 1871
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19690332"
FT MOD_RES 1977
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q9ERU9"
FT MOD_RES 2005
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q9ERU9"
FT MOD_RES 2008
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9ERU9"
FT MOD_RES 2153
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q9ERU9"
FT MOD_RES 2246
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9ERU9"
FT MOD_RES 2251
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9ERU9"
FT MOD_RES 2270
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:23186163"
FT MOD_RES 2280
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9ERU9"
FT MOD_RES 2290
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9ERU9"
FT MOD_RES 2293
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q9ERU9"
FT MOD_RES 2297
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9ERU9"
FT MOD_RES 2462
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9ERU9"
FT MOD_RES 2493
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9ERU9"
FT MOD_RES 2510
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9ERU9"
FT MOD_RES 2526
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 2613
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 2666
FT /note="Phosphotyrosine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 2668
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:21406692,
FT ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569"
FT MOD_RES 2741
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 2743
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 2805
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 2900
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:24275569"
FT MOD_RES 3207
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163"
FT CROSSLNK 1350
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 1414
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:25218447,
FT ECO:0007744|PubMed:25755297, ECO:0007744|PubMed:25772364,
FT ECO:0007744|PubMed:28112733"
FT CROSSLNK 1596
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 1605
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO1); alternate"
FT /evidence="ECO:0007744|PubMed:25114211"
FT CROSSLNK 1605
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2); alternate"
FT /evidence="ECO:0007744|PubMed:25755297,
FT ECO:0007744|PubMed:28112733"
FT CROSSLNK 1655
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 1664
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO1); alternate"
FT /evidence="ECO:0007744|PubMed:25114211"
FT CROSSLNK 1664
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2); alternate"
FT /evidence="ECO:0007744|PubMed:25755297,
FT ECO:0007744|PubMed:28112733"
FT CROSSLNK 1714
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 1723
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO1); alternate"
FT /evidence="ECO:0007744|PubMed:25114211"
FT CROSSLNK 1723
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2); alternate"
FT /evidence="ECO:0007744|PubMed:25755297,
FT ECO:0007744|PubMed:28112733"
FT CROSSLNK 2022
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 2522
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 2592
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO)"
FT /evidence="ECO:0000269|PubMed:15378033"
FT CROSSLNK 2594
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO1); alternate"
FT /evidence="ECO:0007744|PubMed:25114211"
FT CROSSLNK 2594
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2); alternate"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 2612
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 2792
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:25114211,
FT ECO:0007744|PubMed:28112733"
FT CROSSLNK 2815
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT VARIANT 548
FT /note="V -> L (in dbSNP:rs1057954)"
FT /id="VAR_029765"
FT VARIANT 580
FT /note="E -> K (in dbSNP:rs1057956)"
FT /id="VAR_029766"
FT VARIANT 581
FT /note="C -> Y (in dbSNP:rs1057957)"
FT /id="VAR_029767"
FT VARIANT 585
FT /note="T -> M (in IIAE3; decreased interaction with COX11;
FT dbSNP:rs121434502)"
FT /evidence="ECO:0000269|PubMed:19118815,
FT ECO:0000269|PubMed:34400285"
FT /id="VAR_054997"
FT VARIANT 653
FT /note="T -> I (in IIAE3; dbSNP:rs121434503)"
FT /evidence="ECO:0000269|PubMed:19118815"
FT /id="VAR_054998"
FT VARIANT 656
FT /note="I -> V (in IIAE3; dbSNP:rs121434504)"
FT /evidence="ECO:0000269|PubMed:19118815"
FT /id="VAR_054999"
FT VARIANT 725
FT /note="S -> G (in dbSNP:rs17414315)"
FT /id="VAR_050575"
FT VARIANT 784
FT /note="R -> K (in dbSNP:rs2912838)"
FT /evidence="ECO:0000269|PubMed:7603572"
FT /id="VAR_023939"
FT VARIANT 1870
FT /note="P -> L (in dbSNP:rs2889846)"
FT /id="VAR_029768"
FT VARIANT 1892
FT /note="P -> A (in dbSNP:rs12770)"
FT /id="VAR_014886"
FT VARIANT 1892
FT /note="P -> R (in dbSNP:rs12770)"
FT /id="VAR_050576"
FT MUTAGEN 2632
FT /note="V->K: Abolishes interaction with sumoylated
FT RANGAP1."
FT /evidence="ECO:0000269|PubMed:15388847"
FT MUTAGEN 2634
FT /note="I->K: Abolishes interaction with sumoylated
FT RANGAP1."
FT /evidence="ECO:0000269|PubMed:15388847"
FT MUTAGEN 2635
FT /note="V->K: Abolishes interaction with sumoylated
FT RANGAP1."
FT /evidence="ECO:0000269|PubMed:15388847"
FT MUTAGEN 2640
FT /note="P->A: No effect on SUMO E3 ligase activity."
FT /evidence="ECO:0000269|PubMed:15378033"
FT MUTAGEN 2645
FT /note="K->A: No effect on SUMO E3 ligase activity."
FT /evidence="ECO:0000269|PubMed:15378033"
FT MUTAGEN 2651
FT /note="L->A: Abolishes binding to UBE2I and SUMO E3 ligase
FT activity."
FT /evidence="ECO:0000269|PubMed:15378033"
FT MUTAGEN 2652
FT /note="K->A: No effect on SUMO E3 ligase activity."
FT /evidence="ECO:0000269|PubMed:15378033"
FT MUTAGEN 2653
FT /note="L->A: Abolishes binding to UBE2I and SUMO E3 ligase
FT activity."
FT /evidence="ECO:0000269|PubMed:15378033"
FT MUTAGEN 2654
FT /note="P->A: Impairs SUMO E3 ligase activity."
FT /evidence="ECO:0000269|PubMed:15378033"
FT MUTAGEN 2655
FT /note="P->A: No effect on SUMO E3 ligase activity."
FT /evidence="ECO:0000269|PubMed:15378033"
FT MUTAGEN 2656
FT /note="T->A: Impairs SUMO E3 ligase activity."
FT /evidence="ECO:0000269|PubMed:15378033"
FT MUTAGEN 2657
FT /note="F->A: Abolishes binding to UBE2I and SUMO E3 ligase
FT activity."
FT /evidence="ECO:0000269|PubMed:15378033"
FT MUTAGEN 2658
FT /note="F->A: Abolishes binding to UBE2I and SUMO E3 ligase
FT activity."
FT /evidence="ECO:0000269|PubMed:15378033"
FT MUTAGEN 2659
FT /note="C->S,A: Impairs SUMO E3 ligase activity."
FT /evidence="ECO:0000269|PubMed:15378033"
FT MUTAGEN 2676
FT /note="D->A: Impairs SUMO E3 ligase activity."
FT /evidence="ECO:0000269|PubMed:15378033"
FT MUTAGEN 2677
FT /note="F->A: Impairs SUMO E3 ligase activity."
FT /evidence="ECO:0000269|PubMed:15378033"
FT MUTAGEN 2689
FT /note="Y->A: Impairs SUMO E3 ligase activity."
FT /evidence="ECO:0000269|PubMed:15378033"
FT CONFLICT 777
FT /note="H -> R (in Ref. 1; AAC41758)"
FT /evidence="ECO:0000305"
FT CONFLICT 2207
FT /note="S -> A (in Ref. 5; AAA85838)"
FT /evidence="ECO:0000305"
FT CONFLICT 2210
FT /note="T -> P (in Ref. 5; AAA85838)"
FT /evidence="ECO:0000305"
FT CONFLICT 2216
FT /note="E -> V (in Ref. 5; AAA85838)"
FT /evidence="ECO:0000305"
FT CONFLICT 2436
FT /note="F -> C (in Ref. 5; AAA85838)"
FT /evidence="ECO:0000305"
FT CONFLICT 2475
FT /note="T -> P (in Ref. 5; AAA85838)"
FT /evidence="ECO:0000305"
FT CONFLICT 2531
FT /note="K -> N (in Ref. 5; AAA85838)"
FT /evidence="ECO:0000305"
FT CONFLICT 2545
FT /note="F -> C (in Ref. 5)"
FT /evidence="ECO:0000305"
FT HELIX 5..18
FT /evidence="ECO:0007829|PDB:4GA0"
FT HELIX 22..26
FT /evidence="ECO:0007829|PDB:4GA0"
FT HELIX 29..38
FT /evidence="ECO:0007829|PDB:4GA0"
FT HELIX 42..55
FT /evidence="ECO:0007829|PDB:4GA0"
FT HELIX 60..72
FT /evidence="ECO:0007829|PDB:4GA0"
FT HELIX 76..89
FT /evidence="ECO:0007829|PDB:4GA0"
FT HELIX 94..107
FT /evidence="ECO:0007829|PDB:4GA0"
FT HELIX 112..124
FT /evidence="ECO:0007829|PDB:4GA0"
FT HELIX 129..141
FT /evidence="ECO:0007829|PDB:4GA0"
FT STRAND 1191..1205
FT /evidence="ECO:0007829|PDB:5CLL"
FT TURN 1206..1209
FT /evidence="ECO:0007829|PDB:5CLL"
FT STRAND 1210..1224
FT /evidence="ECO:0007829|PDB:5CLL"
FT TURN 1225..1227
FT /evidence="ECO:0007829|PDB:5CLL"
FT STRAND 1230..1236
FT /evidence="ECO:0007829|PDB:5CLL"
FT TURN 1237..1239
FT /evidence="ECO:0007829|PDB:5CLL"
FT STRAND 1242..1247
FT /evidence="ECO:0007829|PDB:5CLL"
FT STRAND 1255..1257
FT /evidence="ECO:0007829|PDB:5CLL"
FT STRAND 1260..1270
FT /evidence="ECO:0007829|PDB:5CLL"
FT STRAND 1277..1284
FT /evidence="ECO:0007829|PDB:5CLL"
FT HELIX 1288..1302
FT /evidence="ECO:0007829|PDB:5CLL"
FT STRAND 2028..2030
FT /evidence="ECO:0007829|PDB:1XKE"
FT STRAND 2032..2046
FT /evidence="ECO:0007829|PDB:1XKE"
FT TURN 2047..2050
FT /evidence="ECO:0007829|PDB:1XKE"
FT STRAND 2051..2065
FT /evidence="ECO:0007829|PDB:1XKE"
FT STRAND 2071..2077
FT /evidence="ECO:0007829|PDB:1XKE"
FT TURN 2078..2081
FT /evidence="ECO:0007829|PDB:1XKE"
FT STRAND 2082..2088
FT /evidence="ECO:0007829|PDB:1XKE"
FT STRAND 2095..2097
FT /evidence="ECO:0007829|PDB:1XKE"
FT STRAND 2105..2111
FT /evidence="ECO:0007829|PDB:1XKE"
FT STRAND 2113..2115
FT /evidence="ECO:0007829|PDB:1XKE"
FT STRAND 2117..2125
FT /evidence="ECO:0007829|PDB:1XKE"
FT HELIX 2129..2145
FT /evidence="ECO:0007829|PDB:1XKE"
FT TURN 2146..2148
FT /evidence="ECO:0007829|PDB:1XKE"
FT STRAND 2632..2637
FT /evidence="ECO:0007829|PDB:3UIP"
FT HELIX 2642..2650
FT /evidence="ECO:0007829|PDB:3UIP"
FT HELIX 2657..2661
FT /evidence="ECO:0007829|PDB:3UIP"
FT STRAND 2663..2665
FT /evidence="ECO:0007829|PDB:3UIN"
FT HELIX 2677..2682
FT /evidence="ECO:0007829|PDB:3UIP"
FT TURN 2683..2686
FT /evidence="ECO:0007829|PDB:3UIP"
FT STRAND 2710..2712
FT /evidence="ECO:0007829|PDB:2LAS"
FT TURN 2926..2929
FT /evidence="ECO:0007829|PDB:4L6E"
FT STRAND 2930..2944
FT /evidence="ECO:0007829|PDB:4L6E"
FT TURN 2945..2948
FT /evidence="ECO:0007829|PDB:4L6E"
FT STRAND 2949..2963
FT /evidence="ECO:0007829|PDB:4L6E"
FT TURN 2964..2967
FT /evidence="ECO:0007829|PDB:4L6E"
FT STRAND 2968..2974
FT /evidence="ECO:0007829|PDB:4L6E"
FT TURN 2976..2978
FT /evidence="ECO:0007829|PDB:4L6E"
FT STRAND 2981..2986
FT /evidence="ECO:0007829|PDB:4L6E"
FT STRAND 2994..2996
FT /evidence="ECO:0007829|PDB:4L6E"
FT STRAND 3000..3009
FT /evidence="ECO:0007829|PDB:4L6E"
FT STRAND 3016..3026
FT /evidence="ECO:0007829|PDB:4L6E"
FT HELIX 3027..3047
FT /evidence="ECO:0007829|PDB:4L6E"
FT STRAND 3065..3072
FT /evidence="ECO:0007829|PDB:4I9Y"
FT STRAND 3075..3084
FT /evidence="ECO:0007829|PDB:4I9Y"
FT TURN 3086..3088
FT /evidence="ECO:0007829|PDB:4I9Y"
FT HELIX 3090..3101
FT /evidence="ECO:0007829|PDB:4I9Y"
FT TURN 3102..3104
FT /evidence="ECO:0007829|PDB:4I9Y"
FT STRAND 3112..3117
FT /evidence="ECO:0007829|PDB:4I9Y"
FT TURN 3118..3120
FT /evidence="ECO:0007829|PDB:4I9Y"
FT STRAND 3121..3124
FT /evidence="ECO:0007829|PDB:4I9Y"
FT TURN 3127..3129
FT /evidence="ECO:0007829|PDB:4I9Y"
FT STRAND 3130..3133
FT /evidence="ECO:0007829|PDB:4I9Y"
FT STRAND 3157..3160
FT /evidence="ECO:0007829|PDB:4I9Y"
FT STRAND 3168..3170
FT /evidence="ECO:0007829|PDB:4LQW"
FT STRAND 3172..3177
FT /evidence="ECO:0007829|PDB:4I9Y"
FT HELIX 3180..3182
FT /evidence="ECO:0007829|PDB:4I9Y"
FT TURN 3183..3185
FT /evidence="ECO:0007829|PDB:4I9Y"
FT STRAND 3188..3194
FT /evidence="ECO:0007829|PDB:4I9Y"
FT HELIX 3196..3203
FT /evidence="ECO:0007829|PDB:4I9Y"
FT STRAND 3216..3223
FT /evidence="ECO:0007829|PDB:4I9Y"
SQ SEQUENCE 3224 AA; 358199 MW; 4CD9A3D5E77183FB CRC64;
MRRSKADVER YIASVQGSTP SPRQKSMKGF YFAKLYYEAK EYDLAKKYIC TYINVQERDP
KAHRFLGLLY ELEENTDKAV ECYRRSVELN PTQKDLVLKI AELLCKNDVT DGRAKYWLER
AAKLFPGSPA IYKLKEQLLD CEGEDGWNKL FDLIQSELYV RPDDVHVNIR LVEVYRSTKR
LKDAVAHCHE AERNIALRSS LEWNSCVVQT LKEYLESLQC LESDKSDWRA TNTDLLLAYA
NLMLLTLSTR DVQESRELLQ SFDSALQSVK SLGGNDELSA TFLEMKGHFY MHAGSLLLKM
GQHSSNVQWR ALSELAALCY LIAFQVPRPK IKLIKGEAGQ NLLEMMACDR LSQSGHMLLN
LSRGKQDFLK EIVETFANKS GQSALYDALF SSQSPKDTSF LGSDDIGNID VREPELEDLT
RYDVGAIRAH NGSLQHLTWL GLQWNSLPAL PGIRKWLKQL FHHLPHETSR LETNAPESIC
ILDLEVFLLG VVYTSHLQLK EKCNSHHSSY QPLCLPLPVC KQLCTERQKS WWDAVCTLIH
RKAVPGNVAK LRLLVQHEIN TLRAQEKHGL QPALLVHWAE CLQKTGSGLN SFYDQREYIG
RSVHYWKKVL PLLKIIKKKN SIPEPIDPLF KHFHSVDIQA SEIVEYEEDA HITFAILDAV
NGNIEDAVTA FESIKSVVSY WNLALIFHRK AEDIENDALS PEEQEECKNY LRKTRDYLIK
IIDDSDSNLS VVKKLPVPLE SVKEMLNSVM QELEDYSEGG PLYKNGSLRN ADSEIKHSTP
SPTRYSLSPS KSYKYSPKTP PRWAEDQNSL LKMICQQVEA IKKEMQELKL NSSNSASPHR
WPTENYGPDS VPDGYQGSQT FHGAPLTVAT TGPSVYYSQS PAYNSQYLLR PAANVTPTKG
PVYGMNRLPP QQHIYAYPQQ MHTPPVQSSS ACMFSQEMYG PPALRFESPA TGILSPRGDD
YFNYNVQQTS TNPPLPEPGY FTKPPIAAHA SRSAESKTIE FGKTNFVQPM PGEGLRPSLP
TQAHTTQPTP FKFNSNFKSN DGDFTFSSPQ VVTQPPPAAY SNSESLLGLL TSDKPLQGDG
YSGAKPIPGG QTIGPRNTFN FGSKNVSGIS FTENMGSSQQ KNSGFRRSDD MFTFHGPGKS
VFGTPTLETA NKNHETDGGS AHGDDDDDGP HFEPVVPLPD KIEVKTGEED EEEFFCNRAK
LFRFDVESKE WKERGIGNVK ILRHKTSGKI RLLMRREQVL KICANHYISP DMKLTPNAGS
DRSFVWHALD YADELPKPEQ LAIRFKTPEE AALFKCKFEE AQSILKAPGT NVAMASNQAV
RIVKEPTSHD NKDICKSDAG NLNFEFQVAK KEGSWWHCNS CSLKNASTAK KCVSCQNLNP
SNKELVGPPL AETVFTPKTS PENVQDRFAL VTPKKEGHWD CSICLVRNEP TVSRCIACQN
TKSANKSGSS FVHQASFKFG QGDLPKPINS DFRSVFSTKE GQWDCSACLV QNEGSSTKCA
ACQNPRKQSL PATSIPTPAS FKFGTSETSK TLKSGFEDMF AKKEGQWDCS SCLVRNEANA
TRCVACQNPD KPSPSTSVPA PASFKFGTSE TSKAPKSGFE GMFTKKEGQW DCSVCLVRNE
ASATKCIACQ NPGKQNQTTS AVSTPASSET SKAPKSGFEG MFTKKEGQWD CSVCLVRNEA
SATKCIACQN PGKQNQTTSA VSTPASSETS KAPKSGFEGM FTKKEGQWDC SVCLVRNEAS
ATKCIACQCP SKQNQTTAIS TPASSEISKA PKSGFEGMFI RKGQWDCSVC CVQNESSSLK
CVACDASKPT HKPIAEAPSA FTLGSEMKLH DSSGSQVGTG FKSNFSEKAS KFGNTEQGFK
FGHVDQENSP SFMFQGSSNT EFKSTKEGFS IPVSADGFKF GISEPGNQEK KSEKPLENGT
GFQAQDISGQ KNGRGVIFGQ TSSTFTFADL AKSTSGEGFQ FGKKDPNFKG FSGAGEKLFS
SQYGKMANKA NTSGDFEKDD DAYKTEDSDD IHFEPVVQMP EKVELVTGEE DEKVLYSQRV
KLFRFDAEVS QWKERGLGNL KILKNEVNGK LRMLMRREQV LKVCANHWIT TTMNLKPLSG
SDRAWMWLAS DFSDGDAKLE QLAAKFKTPE LAEEFKQKFE ECQRLLLDIP LQTPHKLVDT
GRAAKLIQRA EEMKSGLKDF KTFLTNDQTK VTEEENKGSG TGAAGASDTT IKPNPENTGP
TLEWDNYDLR EDALDDSVSS SSVHASPLAS SPVRKNLFRF GESTTGFNFS FKSALSPSKS
PAKLNQSGTS VGTDEESDVT QEEERDGQYF EPVVPLPDLV EVSSGEENEQ VVFSHRAKLY
RYDKDVGQWK ERGIGDIKIL QNYDNKQVRI VMRRDQVLKL CANHRITPDM TLQNMKGTER
VWLWTACDFA DGERKVEHLA VRFKLQDVAD SFKKIFDEAK TAQEKDSLIT PHVSRSSTPR
ESPCGKIAVA VLEETTRERT DVIQGDDVAD ATSEVEVSST SETTPKAVVS PPKFVFGSES
VKSIFSSEKS KPFAFGNSSA TGSLFGFSFN APLKSNNSET SSVAQSGSES KVEPKKCELS
KNSDIEQSSD SKVKNLFASF PTEESSINYT FKTPEKAKEK KKPEDSPSDD DVLIVYELTP
TAEQKALATK LKLPPTFFCY KNRPDYVSEE EEDDEDFETA VKKLNGKLYL DGSEKCRPLE
ENTADNEKEC IIVWEKKPTV EEKAKADTLK LPPTFFCGVC SDTDEDNGNG EDFQSELQKV
QEAQKSQTEE ITSTTDSVYT GGTEVMVPSF CKSEEPDSIT KSISSPSVSS ETMDKPVDLS
TRKEIDTDST SQGESKIVSF GFGSSTGLSF ADLASSNSGD FAFGSKDKNF QWANTGAAVF
GTQSVGTQSA GKVGEDEDGS DEEVVHNEDI HFEPIVSLPE VEVKSGEEDE EILFKERAKL
YRWDRDVSQW KERGVGDIKI LWHTMKNYYR ILMRRDQVFK VCANHVITKT MELKPLNVSN
NALVWTASDY ADGEAKVEQL AVRFKTKEVA DCFKKTFEEC QQNLMKLQKG HVSLAAELSK
ETNPVVFFDV CADGEPLGRI TMELFSNIVP RTAENFRALC TGEKGFGFKN SIFHRVIPDF
VCQGGDITKH DGTGGQSIYG DKFEDENFDV KHTGPGLLSM ANQGQNTNNS QFVITLKKAE
HLDFKHVVFG FVKDGMDTVK KIESFGSPKG SVCRRITITE CGQI
