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Database: UniProt
Entry: P49792
LinkDB: P49792
Original site: P49792 
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   29-SEP-2021, entry version 234.
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).
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).
CC       {ECO:0000269|PubMed:10078529, ECO:0000269|PubMed:11839768,
CC       ECO:0000269|PubMed:14729961, ECO:0000269|PubMed:15378033,
CC       ECO:0000269|PubMed:15388847, ECO:0000269|PubMed:15826666,
CC       ECO:0000269|PubMed:16332688, ECO:0000269|PubMed:20005110,
CC       ECO:0000269|PubMed:20386726, ECO:0000269|PubMed:22155184,
CC       ECO:0000269|PubMed:23353830, 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       Note=The disease is caused by variants affecting the gene represented
CC       in this entry. Mutations in the RANBP2 gene predispose to IIAE3, but by
CC       themselves are insufficient to make the phenotype fully penetrant;
CC       additional genetic and environmental factors are required
CC       (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; 224.
DR   ComplexPortal; CPX-4747; E3 ligase (RANBP2) complex.
DR   ComplexPortal; CPX-873; Nuclear pore complex.
DR   DIP; DIP-37654N; -.
DR   IntAct; P49792; 91.
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; 203 antibodies.
DR   DNASU; 5903; -.
DR   Ensembl; ENST00000283195; ENSP00000283195; ENSG00000153201.
DR   GeneID; 5903; -.
DR   KEGG; hsa:5903; -.
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; HKLCANH; -.
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   SIGNOR; P49792; -.
DR   UniPathway; UPA00886; -.
DR   BioGRID-ORCS; 5903; 405 hits in 1017 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 biceps brachii and 256 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:1990723; C:cytoplasmic periphery of the nuclear pore complex; IEA:Ensembl.
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:0005739; C:mitochondrion; IEA:Ensembl.
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:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0044877; F:protein-containing complex binding; IEA:Ensembl.
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: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   GO; GO:0001975; P:response to amphetamine; 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; IPR011990; TPR-like_helical_dom_sf.
DR   InterPro; IPR019734; TPR_repeat.
DR   InterPro; IPR001876; Znf_RanBP2.
DR   InterPro; IPR036443; Znf_RanBP2_sf.
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; dbSNP:rs121434502)"
FT                   /evidence="ECO:0000269|PubMed:19118815"
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
//
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