Did you know ? If you order before Friday 14h we deliver 90PCT of the the time next Tuesday, GENTAUR another in time delivery

E3 SUMO-protein ligase RanBP2 (EC 6.3.2.-) (358 kDa nucleoporin) (Nuclear pore complex protein Nup358) (Nucleoporin Nup358) (Ran-binding protein 2) (RanBP2) (p270)

 RBP2_HUMAN              Reviewed;        3224 AA.
P49792; Q13074; Q15280; Q53TE2; Q59FH7;
01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
06-DEC-2005, sequence version 2.
30-AUG-2017, entry version 200.
RecName: Full=E3 SUMO-protein ligase RanBP2;
EC=6.3.2.-;
AltName: Full=358 kDa nucleoporin;
AltName: Full=Nuclear pore complex protein Nup358;
AltName: Full=Nucleoporin Nup358;
AltName: Full=Ran-binding protein 2;
Short=RanBP2;
AltName: Full=p270;
Name=RANBP2; Synonyms=NUP358;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND SUBCELLULAR LOCATION.
PubMed=7775481; DOI=10.1074/jbc.270.23.14209;
Wu J., Matunis M.J., Kraemer D., Blobel G., Coutavas E.;
"Nup358, a cytoplasmically exposed nucleoporin with peptide repeats,
Ran-GTP binding sites, zinc fingers, a cyclophilin A homologous
domain, and a leucine-rich region.";
J. Biol. Chem. 270:14209-14213(1995).
[2]
NUCLEOTIDE SEQUENCE [MRNA], VARIANT LYS-784, AND SUBCELLULAR LOCATION.
TISSUE=Blood;
PubMed=7603572; DOI=10.1038/376184a0;
Yokoyama N., Hayashi N., Seki T., Nishii K., Hayashida T., Kuma K.,
Miyata T., Fukui M., Nishimoto T., Pante N., Aebi U.;
"A giant nucleopore protein that binds Ran/TC4.";
Nature 376:184-188(1995).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=15815621; DOI=10.1038/nature03466;
Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H.,
Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M.,
Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E.,
Kremitzki C., Oddy L., Du H., Sun H., Bradshaw-Cordum H., Ali J.,
Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C.,
Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J.,
Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A.,
Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K.,
Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M.,
Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K.,
McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C.,
Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N.,
Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M.,
Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E.,
Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P.,
Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A.,
Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A.,
Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T.,
Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D.,
Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X.,
McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C.,
Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S.,
Miller W., Eichler E.E., Bork P., Suyama M., Torrents D.,
Waterston R.H., Wilson R.K.;
"Generation and annotation of the DNA sequences of human chromosomes 2
and 4.";
Nature 434:724-731(2005).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 87-3224.
TISSUE=Brain;
Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S.,
Ohara O., Nagase T., Kikuno R.F.;
Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases.
[5]
NUCLEOTIDE SEQUENCE [MRNA] OF 2205-2546.
TISSUE=Hippocampus;
PubMed=7724562; DOI=10.1073/pnas.92.8.3328;
Beddow A.L., Richards S.A., Orem N.R., Macara I.G.;
"The Ran/TC4 GTPase-binding domain: identification by expression
cloning and characterization of a conserved sequence motif.";
Proc. Natl. Acad. Sci. U.S.A. 92:3328-3332(1995).
[6]
FUNCTION, AND SUMOYLATION.
PubMed=11792325; DOI=10.1016/S0092-8674(01)00633-X;
Pichler A., Gast A., Seeler J.S., Dejean A., Melchior F.;
"The nucleoporin RanBP2 has SUMO1 E3 ligase activity.";
Cell 108:109-120(2002).
[7]
FUNCTION.
PubMed=12032081; DOI=10.1093/emboj/21.11.2682;
Kirsh O., Seeler J.-S., Pichler A., Gast A., Mueller S., Miska E.,
Mathieu M., Harel-Bellan A., Kouzarides T., Melchior F., Dejean A.;
"The SUMO E3 ligase RanBP2 promotes modification of the HDAC4
deacetylase.";
EMBO J. 21:2682-2691(2002).
[8]
SUBCELLULAR LOCATION.
PubMed=11839768; DOI=10.1083/jcb.200106046;
Frosst P., Guan T., Subauste C., Hahn K., Gerace L.;
"Tpr is localized within the nuclear basket of the pore complex and
has a role in nuclear protein export.";
J. Cell Biol. 156:617-630(2002).
[9]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Leukemic T-cell;
PubMed=15144186; DOI=10.1021/ac035352d;
Brill L.M., Salomon A.R., Ficarro S.B., Mukherji M., Stettler-Gill M.,
Peters E.C.;
"Robust phosphoproteomic profiling of tyrosine phosphorylation sites
from human T cells using immobilized metal affinity chromatography and
tandem mass spectrometry.";
Anal. Chem. 76:2763-2772(2004).
[10]
FUNCTION, INTERACTION WITH UBE2I, SUMOYLATION AT LYS-2592, AND
MUTAGENESIS OF PRO-2640; LYS-2645; LEU-2651; LYS-2652; LEU-2653;
PRO-2654; PRO-2655; THR-2656; PHE-2657; PHE-2658; CYS-2659; ASP-2676;
PHE-2677 AND TYR-2689.
PubMed=15378033; DOI=10.1038/nsmb834;
Pichler A., Knipscheer P., Saitoh H., Sixma T.K., Melchior F.;
"The RanBP2 SUMO E3 ligase is neither HECT- nor RING-type.";
Nat. Struct. Mol. Biol. 11:984-991(2004).
[11]
INTERACTION WITH SUMOYLATED RANGAP1, AND MUTAGENESIS OF VAL-2632;
ILE-2634 AND VAL-2635.
PubMed=15388847; DOI=10.1073/pnas.0403498101;
Song J., Durrin L.K., Wilkinson T.A., Krontiris T.G., Chen Y.;
"Identification of a SUMO-binding motif that recognizes SUMO-modified
proteins.";
Proc. Natl. Acad. Sci. U.S.A. 101:14373-14378(2004).
[12]
INTERACTION WITH SUMO1 AND UBE2I.
PubMed=15608651; DOI=10.1038/nsmb878;
Tatham M.H., Kim S., Jaffray E., Song J., Chen Y., Hay R.T.;
"Unique binding interactions among Ubc9, SUMO and RanBP2 reveal a
mechanism for SUMO paralog selection.";
Nat. Struct. Mol. Biol. 12:67-74(2005).
[13]
IDENTIFICATION BY MASS SPECTROMETRY.
PubMed=16620772; DOI=10.1016/j.abb.2006.03.002;
Li T., Santockyte R., Shen R.-F., Tekle E., Wang G., Yang D.C.H.,
Chock P.B.;
"A general approach for investigating enzymatic pathways and
substrates for ubiquitin-like modifiers.";
Arch. Biochem. Biophys. 453:70-74(2006).
[14]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,
Mann M.;
"Global, in vivo, and site-specific phosphorylation dynamics in
signaling networks.";
Cell 127:635-648(2006).
[15]
INTERACTION WITH PRKN, AND UBIQUITINATION.
PubMed=16332688; DOI=10.1074/jbc.M504994200;
Um J.W., Min D.S., Rhim H., Kim J., Paik S.R., Chung K.C.;
"Parkin ubiquitinates and promotes the degradation of RanBP2.";
J. Biol. Chem. 281:3595-3603(2006).
[16]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-21 AND THR-1144, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=16964243; DOI=10.1038/nbt1240;
Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.;
"A probability-based approach for high-throughput protein
phosphorylation analysis and site localization.";
Nat. Biotechnol. 24:1285-1292(2006).
[17]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18220336; DOI=10.1021/pr0705441;
Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D.,
Yates J.R. III;
"Combining protein-based IMAC, peptide-based IMAC, and MudPIT for
efficient phosphoproteomic analysis.";
J. Proteome Res. 7:1346-1351(2008).
[18]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007;
Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,
Greff Z., Keri G., Stemmann O., Mann M.;
"Kinase-selective enrichment enables quantitative phosphoproteomics of
the kinome across the cell cycle.";
Mol. Cell 31:438-448(2008).
[19]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-19; SER-21; SER-781;
SER-948; SER-955; SER-1110; THR-1144; SER-1160; THR-1396; SER-1443;
SER-1456; SER-1509; SER-1573; SER-1869; SER-2270; THR-2613; SER-2668;
SER-2741; THR-2743 AND SER-2900, AND IDENTIFICATION BY MASS
SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18669648; DOI=10.1073/pnas.0805139105;
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
Elledge S.J., Gygi S.P.;
"A quantitative atlas of mitotic phosphorylation.";
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
[20]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=18318008; DOI=10.1002/pmic.200700884;
Han G., Ye M., Zhou H., Jiang X., Feng S., Jiang X., Tian R., Wan D.,
Zou H., Gu J.;
"Large-scale phosphoproteome analysis of human liver tissue by
enrichment and fractionation of phosphopeptides with strong anion
exchange chromatography.";
Proteomics 8:1346-1361(2008).
[21]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19413330; DOI=10.1021/ac9004309;
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,
Mohammed S.;
"Lys-N and trypsin cover complementary parts of the phosphoproteome in
a refined SCX-based approach.";
Anal. Chem. 81:4493-4501(2009).
[22]
INTERACTION WITH CDCA8.
PubMed=18946085; DOI=10.1091/mbc.E08-05-0511;
Klein U.R., Haindl M., Nigg E.A., Muller S.;
"RanBP2 and SENP3 function in a mitotic SUMO2/3 conjugation-
deconjugation cycle on Borealin.";
Mol. Biol. Cell 20:410-418(2009).
[23]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-19; SER-21; SER-955;
SER-1107; THR-1396; SER-1871; SER-2270; SER-2668 AND SER-2900, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Leukemic T-cell;
PubMed=19690332; DOI=10.1126/scisignal.2000007;
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
Rodionov V., Han D.K.;
"Quantitative phosphoproteomic analysis of T cell receptor signaling
reveals system-wide modulation of protein-protein interactions.";
Sci. Signal. 2:RA46-RA46(2009).
[24]
FUNCTION, INTERACTION WITH BICD2, AND SUBCELLULAR LOCATION.
PubMed=20386726; DOI=10.1371/journal.pbio.1000350;
Splinter D., Tanenbaum M.E., Lindqvist A., Jaarsma D., Flotho A.,
Yu K.L., Grigoriev I., Engelsma D., Haasdijk E.D., Keijzer N.,
Demmers J., Fornerod M., Melchior F., Hoogenraad C.C., Medema R.H.,
Akhmanova A.;
"Bicaudal D2, dynein, and kinesin-1 associate with nuclear pore
complexes and regulate centrosome and nuclear positioning during
mitotic entry.";
PLoS Biol. 8:E1000350-E1000350(2010).
[25]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-19; SER-21; SER-781;
SER-837; SER-948; SER-955; SER-1110; SER-1160; THR-1412; SER-1509;
SER-1835; SER-2900 AND SER-3207, AND IDENTIFICATION BY MASS
SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=20068231; DOI=10.1126/scisignal.2000475;
Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S.,
Mann M.;
"Quantitative phosphoproteomics reveals widespread full
phosphorylation site occupancy during mitosis.";
Sci. Signal. 3:RA3-RA3(2010).
[26]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21269460; DOI=10.1186/1752-0509-5-17;
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
"Initial characterization of the human central proteome.";
BMC Syst. Biol. 5:17-17(2011).
[27]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1160; SER-1456;
SER-2668; SER-2900 AND SER-3207, AND IDENTIFICATION BY MASS
SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21406692; DOI=10.1126/scisignal.2001570;
Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J.,
Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V.,
Blagoev B.;
"System-wide temporal characterization of the proteome and
phosphoproteome of human embryonic stem cell differentiation.";
Sci. Signal. 4:RS3-RS3(2011).
[28]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-21; THR-779; SER-781;
SER-948; SER-955; THR-1098; SER-1103; SER-1107; SER-1110; THR-1144;
SER-1160; SER-1249; THR-1396; THR-1412; SER-1450; SER-1456; SER-1509;
SER-1520; SER-1573; SER-1833; SER-1835; SER-1869; SER-2270; SER-2526;
THR-2613; TYR-2666; SER-2668; SER-2805 AND SER-3207, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma, and Erythroleukemia;
PubMed=23186163; DOI=10.1021/pr300630k;
Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
Mohammed S.;
"Toward a comprehensive characterization of a human cancer cell
phosphoproteome.";
J. Proteome Res. 12:260-271(2013).
[29]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-955; SER-1160; SER-1450;
SER-1456; SER-1509; SER-2668 AND SER-2900, AND IDENTIFICATION BY MASS
SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D.,
Wang L., Ye M., Zou H.;
"An enzyme assisted RP-RPLC approach for in-depth analysis of human
liver phosphoproteome.";
J. Proteomics 96:253-262(2014).
[30]
METHYLATION [LARGE SCALE ANALYSIS] AT ARG-945 AND ARG-1016, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Colon carcinoma;
PubMed=24129315; DOI=10.1074/mcp.O113.027870;
Guo A., Gu H., Zhou J., Mulhern D., Wang Y., Lee K.A., Yang V.,
Aguiar M., Kornhauser J., Jia X., Ren J., Beausoleil S.A., Silva J.C.,
Vemulapalli V., Bedford M.T., Comb M.J.;
"Immunoaffinity enrichment and mass spectrometry analysis of protein
methylation.";
Mol. Cell. Proteomics 13:372-387(2014).
[31]
SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-1414, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=25218447; DOI=10.1038/nsmb.2890;
Hendriks I.A., D'Souza R.C., Yang B., Verlaan-de Vries M., Mann M.,
Vertegaal A.C.;
"Uncovering global SUMOylation signaling networks in a site-specific
manner.";
Nat. Struct. Mol. Biol. 21:927-936(2014).
[32]
SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-1605; LYS-1664; LYS-1723;
LYS-2594 AND LYS-2792, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE
SCALE ANALYSIS].
PubMed=25114211; DOI=10.1073/pnas.1413825111;
Impens F., Radoshevich L., Cossart P., Ribet D.;
"Mapping of SUMO sites and analysis of SUMOylation changes induced by
external stimuli.";
Proc. Natl. Acad. Sci. U.S.A. 111:12432-12437(2014).
[33]
SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-1414, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=25772364; DOI=10.1016/j.celrep.2015.02.033;
Hendriks I.A., Treffers L.W., Verlaan-de Vries M., Olsen J.V.,
Vertegaal A.C.;
"SUMO-2 orchestrates chromatin modifiers in response to DNA damage.";
Cell Rep. 10:1778-1791(2015).
[34]
SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-1414; LYS-1605; LYS-1664 AND
LYS-1723, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
ANALYSIS].
PubMed=25755297; DOI=10.1074/mcp.O114.044792;
Xiao Z., Chang J.G., Hendriks I.A., Sigurdsson J.O., Olsen J.V.,
Vertegaal A.C.;
"System-wide analysis of SUMOylation dynamics in response to
replication stress reveals novel small ubiquitin-like modified target
proteins and acceptor lysines relevant for genome stability.";
Mol. Cell. Proteomics 14:1419-1434(2015).
[35]
SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-1350; LYS-1414; LYS-1596;
LYS-1605; LYS-1655; LYS-1664; LYS-1714; LYS-1723; LYS-2022; LYS-2522;
LYS-2594; LYS-2612; LYS-2792 AND LYS-2815, AND IDENTIFICATION BY MASS
SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=28112733; DOI=10.1038/nsmb.3366;
Hendriks I.A., Lyon D., Young C., Jensen L.J., Vertegaal A.C.,
Nielsen M.L.;
"Site-specific mapping of the human SUMO proteome reveals co-
modification with phosphorylation.";
Nat. Struct. Mol. Biol. 24:325-336(2017).
[36]
X-RAY CRYSTALLOGRAPHY (2.96 ANGSTROMS) OF 1171-1304.
PubMed=10078529; DOI=10.1038/17969;
Vetter I.R., Nowak C., Nishimoto T., Kuhlmann J., Wittinghofer A.;
"Structure of a Ran-binding domain complexed with Ran bound to a GTP
analogue: implications for nuclear transport.";
Nature 398:39-46(1999).
[37]
STRUCTURE BY NMR OF 2028-2154.
PubMed=15826666; DOI=10.1016/j.jmb.2005.02.033;
Geyer J.P., Doker R., Kremer W., Zhao X., Kuhlmann J., Kalbitzer H.R.;
"Solution structure of the Ran-binding domain 2 of RanBP2 and its
interaction with the C terminus of Ran.";
J. Mol. Biol. 348:711-725(2005).
[38]
X-RAY CRYSTALLOGRAPHY (3.01 ANGSTROMS) OF 2631-2711 IN COMPLEX WITH
SUMO1; RANGAP1 AND UBE2I, SUBUNIT, AND FUNCTION.
PubMed=15931224; DOI=10.1038/nature03588;
Reverter D., Lima C.D.;
"Insights into E3 ligase activity revealed by a SUMO-RanGAP1-Ubc9-
Nup358 complex.";
Nature 435:687-692(2005).
[39]
X-RAY CRYSTALLOGRAPHY (2.29 ANGSTROMS) OF 2631-2695 IN COMPLEX WITH
SUMO1; RANGAP1 AND UBE2I, SUBUNIT, AND FUNCTION.
PubMed=22194619; DOI=10.1074/jbc.M111.321141;
Gareau J.R., Reverter D., Lima C.D.;
"Determinants of small ubiquitin-like modifier 1 (SUMO1) protein
specificity, E3 ligase, and SUMO-RanGAP1 binding activities of
nucleoporin RanBP2.";
J. Biol. Chem. 287:4740-4751(2012).
[40]
X-RAY CRYSTALLOGRAPHY (1.15 ANGSTROMS) OF 1-145, AND TPR REPEATS.
PubMed=22959972; DOI=10.1016/j.jmb.2012.08.026;
Kassube S.A., Stuwe T., Lin D.H., Antonuk C.D., Napetschnig J.,
Blobel G., Hoelz A.;
"Crystal structure of the N-terminal domain of Nup358/RanBP2.";
J. Mol. Biol. 423:752-765(2012).
[41]
X-RAY CRYSTALLOGRAPHY (1.75 ANGSTROMS) OF 3062-3224, DOMAIN, ABSENCE
OF ROTAMASE ACTIVITY, AND SUBCELLULAR LOCATION.
PubMed=23353830; DOI=10.1016/j.jmb.2013.01.021;
Lin D.H., Zimmermann S., Stuwe T., Stuwe E., Hoelz A.;
"Structural and functional analysis of the C-terminal domain of
Nup358/RanBP2.";
J. Mol. Biol. 425:1318-1329(2013).
[42]
VARIANTS IIAE3 MET-585; ILE-653 AND VAL-656.
PubMed=19118815; DOI=10.1016/j.ajhg.2008.12.009;
Neilson D.E., Adams M.D., Orr C.M.D., Schelling D.K., Eiben R.M.,
Kerr D.S., Anderson J., Bassuk A.G., Bye A.M., Childs A.-M.,
Clarke A., Crow Y.J., Di Rocco M., Dohna-Schwake C., Dueckers G.,
Fasano A.E., Gika A.D., Gionnis D., Gorman M.P., Grattan-Smith P.J.,
Hackenberg A., Kuster A., Lentschig M.G., Lopez-Laso E., Marco E.J.,
Mastroyianni S., Perrier J., Schmitt-Mechelke T., Servidei S.,
Skardoutsou A., Uldall P., van der Knaap M.S., Goglin K.C.,
Tefft D.L., Aubin C., de Jager P., Hafler D., Warman M.L.;
"Infection-triggered familial or recurrent cases of acute necrotizing
encephalopathy caused by mutations in a component of the nuclear pore,
RANBP2.";
Am. J. Hum. Genet. 84:44-51(2009).
-!- FUNCTION: E3 SUMO-protein ligase which facilitates SUMO1 and SUMO2
conjugation by UBE2I. Involved in transport factor (Ran-GTP,
karyopherin)-mediated protein import via the F-G repeat-containing
domain which acts as a docking site for substrates. Binds single-
stranded RNA (in vitro). May bind DNA. Component of the nuclear
export pathway. Specific docking site for the nuclear export
factor exportin-1. Sumoylates PML at 'Lys-490' which is essential
for the proper assembly of PML-NB. Recruits BICD2 to the nuclear
envelope and cytoplasmic stacks of nuclear pore complex known as
annulate lamellae during G2 phase of cell cycle (PubMed:20386726).
{ECO:0000269|PubMed:11792325, ECO:0000269|PubMed:12032081,
ECO:0000269|PubMed:15378033, ECO:0000269|PubMed:15931224,
ECO:0000269|PubMed:20386726, ECO:0000269|PubMed:22194619}.
-!- PATHWAY: Protein modification; protein sumoylation.
-!- SUBUNIT: Forms a tight complex with RANBP1 and UBE2I. Interacts
with SUMO1 but not SUMO2. Interacts with PRKN. Interacts with
sumoylated RANGAP1. Interacts with CDCA8. Interacts with PML
(isoform PML-4). Interacts with BICD2 (PubMed:20386726).
{ECO:0000269|PubMed:15378033, ECO:0000269|PubMed:15388847,
ECO:0000269|PubMed:15608651, ECO:0000269|PubMed:15931224,
ECO:0000269|PubMed:16332688, ECO:0000269|PubMed:18946085,
ECO:0000269|PubMed:20386726, ECO:0000269|PubMed:22194619}.
-!- INTERACTION:
P04626:ERBB2; NbExp=3; IntAct=EBI-973138, EBI-641062;
Q53GG5:PDLIM3; NbExp=3; IntAct=EBI-973138, EBI-5658852;
O60260:PRKN; NbExp=11; IntAct=EBI-973138, EBI-716346;
-!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:7775481}.
Nucleus membrane {ECO:0000269|PubMed:11839768}. Nucleus, nuclear
pore complex {ECO:0000269|PubMed:11839768,
ECO:0000269|PubMed:20386726, ECO:0000269|PubMed:23353830,
ECO:0000269|PubMed:7603572}. Nucleus envelope
{ECO:0000269|PubMed:20386726}. Note=Detected in diffuse and
discrete intranuclear foci (PubMed:11839768). Cytoplasmic
filaments (PubMed:7775481). {ECO:0000269|PubMed:11839768,
ECO:0000269|PubMed:7775481}.
-!- DOMAIN: Contains a dozen F-X-F-G repeats in the C-terminal half.
{ECO:0000269|PubMed:23353830}.
-!- DOMAIN: The PPIase cyclophilin-type domain has high structural
similarity with PPIA, but has extremely low and barely detectable
proline isomerase activity (in vitro) (PubMed:23353830). Only
about half of the residues that surround the PPIA active site
cleft are conserved. {ECO:0000269|PubMed:23353830}.
-!- PTM: Polyubiquitinated by PRKN, which leads to proteasomal
degradation. {ECO:0000269|PubMed:16332688}.
-!- PTM: The the inner channel of the NPC has a different redox
environment from the cytoplasm and allows the formation of
interchain disulfide bonds between some nucleoporins, the
significant increase of these linkages upon oxidative stress
reduces the permeability of the NPC.
{ECO:0000250|UniProtKB:Q9ERU9}.
-!- DISEASE: Encephalopathy, acute, infection-induced, 3 (IIAE3)
[MIM:608033]: A rapidly progressive encephalopathy manifesting in
susceptible individuals with seizures and coma. It can occur
within days in otherwise healthy children after common viral
infections such as influenza and parainfluenza, without evidence
of viral infection of the brain or inflammatory cell infiltration.
Brain T2-weighted magnetic resonance imaging reveals
characteristic symmetric lesions present in the thalami, pons and
brainstem. {ECO:0000269|PubMed:19118815}. Note=The disease is
caused by mutations affecting the gene represented in this entry.
Mutations in the RANBP2 gene predispose to IIAE3, but by
themselves are insufficient to make the phenotype fully penetrant;
additional genetic and environmental factors are required
(PubMed:19118815). {ECO:0000269|PubMed:19118815}.
-!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology
and Haematology;
URL="http://atlasgeneticsoncology.org/Genes/RANBP2ID483.html";
-----------------------------------------------------------------------
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
Distributed under the Creative Commons Attribution-NoDerivs License
-----------------------------------------------------------------------
EMBL; L41840; AAC41758.1; -; Genomic_DNA.
EMBL; D42063; BAA07662.1; -; mRNA.
EMBL; AC010095; AAY14984.1; -; Genomic_DNA.
EMBL; AB209483; BAD92720.1; -; mRNA.
EMBL; U19248; AAA85838.1; -; mRNA.
CCDS; CCDS2079.1; -.
PIR; S58884; S58884.
RefSeq; NP_006258.3; NM_006267.4.
UniGene; Hs.199561; -.
UniGene; Hs.715056; -.
PDB; 1RRP; X-ray; 2.96 A; B/D=1171-1304.
PDB; 1XKE; NMR; -; A=2028-2154.
PDB; 1Z5S; X-ray; 3.01 A; D=2631-2711.
PDB; 2LAS; NMR; -; B=2705-2717.
PDB; 3UIN; X-ray; 2.60 A; D=2629-2695.
PDB; 3UIO; X-ray; 2.60 A; D=2631-2695.
PDB; 3UIP; X-ray; 2.29 A; D=2631-2695.
PDB; 4GA0; X-ray; 1.15 A; A=1-145.
PDB; 4I9Y; X-ray; 1.75 A; A/B/C/D/E/F=3062-3224.
PDB; 4L6E; X-ray; 2.50 A; A=2907-3050.
PDB; 4LQW; X-ray; 1.95 A; A/B=3057-3224.
PDB; 5CLL; X-ray; 2.45 A; B/D=1155-1321.
PDB; 5CLQ; X-ray; 3.20 A; B/D=1155-1321.
PDBsum; 1RRP; -.
PDBsum; 1XKE; -.
PDBsum; 1Z5S; -.
PDBsum; 2LAS; -.
PDBsum; 3UIN; -.
PDBsum; 3UIO; -.
PDBsum; 3UIP; -.
PDBsum; 4GA0; -.
PDBsum; 4I9Y; -.
PDBsum; 4L6E; -.
PDBsum; 4LQW; -.
PDBsum; 5CLL; -.
PDBsum; 5CLQ; -.
ProteinModelPortal; P49792; -.
SMR; P49792; -.
BioGrid; 111839; 153.
DIP; DIP-37654N; -.
IntAct; P49792; 63.
MINT; MINT-191403; -.
STRING; 9606.ENSP00000283195; -.
TCDB; 1.I.1.1.3; the nuclear pore complex (npc) family.
iPTMnet; P49792; -.
PhosphoSitePlus; P49792; -.
SwissPalm; P49792; -.
BioMuta; RANBP2; -.
DMDM; 83305554; -.
OGP; P49792; -.
EPD; P49792; -.
MaxQB; P49792; -.
PaxDb; P49792; -.
PeptideAtlas; P49792; -.
PRIDE; P49792; -.
Ensembl; ENST00000283195; ENSP00000283195; ENSG00000153201.
GeneID; 5903; -.
KEGG; hsa:5903; -.
UCSC; uc002tem.4; human.
CTD; 5903; -.
DisGeNET; 5903; -.
GeneCards; RANBP2; -.
H-InvDB; HIX0002358; -.
HGNC; HGNC:9848; RANBP2.
HPA; CAB034063; -.
HPA; HPA018437; -.
HPA; HPA023960; -.
HPA; HPA049497; -.
HPA; HPA051675; -.
HPA; HPA067564; -.
MalaCards; RANBP2; -.
MIM; 601181; gene.
MIM; 608033; phenotype.
neXtProt; NX_P49792; -.
OpenTargets; ENSG00000153201; -.
Orphanet; 263524; Acute necrotizing encephalopathy of childhood.
Orphanet; 88619; Familial acute necrotizing encephalopathy.
Orphanet; 178342; Inflammatory myofibroblastic tumor.
PharmGKB; PA34209; -.
eggNOG; KOG0864; Eukaryota.
eggNOG; KOG0865; Eukaryota.
eggNOG; COG0652; LUCA.
eggNOG; COG5171; LUCA.
GeneTree; ENSGT00880000137938; -.
HOGENOM; HOG000089994; -.
HOVERGEN; HBG092361; -.
InParanoid; P49792; -.
KO; K12172; -.
OMA; TKKEGQW; -.
OrthoDB; EOG091G0BGL; -.
PhylomeDB; P49792; -.
TreeFam; TF314797; -.
Reactome; R-HSA-1169408; ISG15 antiviral mechanism.
Reactome; R-HSA-159227; Transport of the SLBP independent Mature mRNA.
Reactome; R-HSA-159230; Transport of the SLBP Dependant Mature mRNA.
Reactome; R-HSA-159231; Transport of Mature mRNA Derived from an Intronless Transcript.
Reactome; R-HSA-159236; Transport of Mature mRNA derived from an Intron-Containing Transcript.
Reactome; R-HSA-165054; Rev-mediated nuclear export of HIV RNA.
Reactome; R-HSA-168271; Transport of Ribonucleoproteins into the Host Nucleus.
Reactome; R-HSA-168276; NS1 Mediated Effects on Host Pathways.
Reactome; R-HSA-168325; Viral Messenger RNA Synthesis.
Reactome; R-HSA-168333; NEP/NS2 Interacts with the Cellular Export Machinery.
Reactome; R-HSA-170822; Regulation of Glucokinase by Glucokinase Regulatory Protein.
Reactome; R-HSA-180746; Nuclear import of Rev protein.
Reactome; R-HSA-180910; Vpr-mediated nuclear import of PICs.
Reactome; R-HSA-191859; snRNP Assembly.
Reactome; R-HSA-2467813; Separation of Sister Chromatids.
Reactome; R-HSA-2500257; Resolution of Sister Chromatid Cohesion.
Reactome; R-HSA-3108214; SUMOylation of DNA damage response and repair proteins.
Reactome; R-HSA-3301854; Nuclear Pore Complex (NPC) Disassembly.
Reactome; R-HSA-3371453; Regulation of HSF1-mediated heat shock response.
Reactome; R-HSA-4551638; SUMOylation of chromatin organization proteins.
Reactome; R-HSA-4570464; SUMOylation of RNA binding proteins.
Reactome; R-HSA-4615885; SUMOylation of DNA replication proteins.
Reactome; R-HSA-5578749; Transcriptional regulation by small RNAs.
Reactome; R-HSA-5663220; RHO GTPases Activate Formins.
Reactome; R-HSA-6784531; tRNA processing in the nucleus.
Reactome; R-HSA-68877; Mitotic Prometaphase.
UniPathway; UPA00886; -.
ChiTaRS; RANBP2; human.
EvolutionaryTrace; P49792; -.
GeneWiki; RANBP2; -.
GenomeRNAi; 5903; -.
PRO; PR:P49792; -.
Proteomes; UP000005640; Chromosome 2.
Bgee; ENSG00000153201; -.
CleanEx; HS_RANBP2; -.
ExpressionAtlas; P49792; baseline and differential.
Genevisible; P49792; HS.
GO; GO:0005642; C:annulate lamellae; IDA:UniProtKB.
GO; GO:0005813; C:centrosome; IBA:GO_Central.
GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
GO; GO:1990723; C:cytoplasmic periphery of the nuclear pore complex; IEA:Ensembl.
GO; GO:0005829; C:cytosol; TAS:Reactome.
GO; GO:0043657; C:host cell; IEA:GOC.
GO; GO:0043231; C:intracellular membrane-bounded organelle; IDA:HPA.
GO; GO:0016020; C:membrane; IDA:UniProtKB.
GO; GO:0005739; C:mitochondrion; IEA:Ensembl.
GO; GO:0005635; C:nuclear envelope; IDA:UniProtKB.
GO; GO:0042405; C:nuclear inclusion body; IDA:UniProtKB.
GO; GO:0031965; C:nuclear membrane; IDA:UniProtKB.
GO; GO:0005643; C:nuclear pore; IDA:UniProtKB.
GO; GO:0044614; C:nuclear pore cytoplasmic filaments; IDA:GO_Central.
GO; GO:0044615; C:nuclear pore nuclear basket; IDA:UniProtKB.
GO; GO:0016874; F:ligase activity; IEA:UniProtKB-KW.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0003755; F:peptidyl-prolyl cis-trans isomerase activity; IEA:InterPro.
GO; GO:0032403; F:protein complex binding; IEA:Ensembl.
GO; GO:0008536; F:Ran GTPase binding; IPI:GO_Central.
GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
GO; GO:0019789; F:SUMO transferase activity; EXP:Reactome.
GO; GO:0051642; P:centrosome localization; IMP:UniProtKB.
GO; GO:0000082; P:G1/S transition of mitotic cell cycle; IBA:GO_Central.
GO; GO:0075733; P:intracellular transport of virus; TAS:Reactome.
GO; GO:0007077; P:mitotic nuclear envelope disassembly; TAS:Reactome.
GO; GO:0006406; P:mRNA export from nucleus; TAS:Reactome.
GO; GO:0006607; P:NLS-bearing protein import into nucleus; IMP:GO_Central.
GO; GO:0033133; P:positive regulation of glucokinase activity; IEA:Ensembl.
GO; GO:0043547; P:positive regulation of GTPase activity; IEA:GOC.
GO; GO:0046604; P:positive regulation of mitotic centrosome separation; IBA:GO_Central.
GO; GO:0006457; P:protein folding; IEA:InterPro.
GO; GO:0016925; P:protein sumoylation; IDA:UniProtKB.
GO; GO:1900034; P:regulation of cellular response to heat; TAS:Reactome.
GO; GO:0060964; P:regulation of gene silencing by miRNA; TAS:Reactome.
GO; GO:0090526; P:regulation of gluconeogenesis involved in cellular glucose homeostasis; IEA:Ensembl.
GO; GO:0010827; P:regulation of glucose transport; TAS:Reactome.
GO; GO:0001975; P:response to amphetamine; IEA:Ensembl.
GO; GO:0006405; P:RNA export from nucleus; IBA:GO_Central.
GO; GO:0007062; P:sister chromatid cohesion; TAS:Reactome.
GO; GO:0007051; P:spindle organization; IBA:GO_Central.
GO; GO:0006409; P:tRNA export from nucleus; TAS:Reactome.
GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; IBA:GO_Central.
GO; GO:0016032; P:viral process; TAS:Reactome.
GO; GO:0019083; P:viral transcription; TAS:Reactome.
Gene3D; 1.25.40.10; -; 1.
Gene3D; 2.30.29.30; -; 4.
Gene3D; 2.40.100.10; -; 1.
InterPro; IPR029000; Cyclophilin-like_dom.
InterPro; IPR020892; Cyclophilin-type_PPIase_CS.
InterPro; IPR002130; Cyclophilin-type_PPIase_dom.
InterPro; IPR022011; IR1-M.
InterPro; IPR011993; PH_dom-like.
InterPro; IPR000156; Ran_bind_dom.
InterPro; IPR013026; TPR-contain_dom.
InterPro; IPR011990; TPR-like_helical_dom.
InterPro; IPR019734; TPR_repeat.
InterPro; IPR001876; Znf_RanBP2.
Pfam; PF12185; IR1-M; 2.
Pfam; PF00160; Pro_isomerase; 1.
Pfam; PF00638; Ran_BP1; 4.
Pfam; PF00641; zf-RanBP; 8.
PRINTS; PR00153; CSAPPISMRASE.
SMART; SM00160; RanBD; 4.
SMART; SM00028; TPR; 1.
SMART; SM00547; ZnF_RBZ; 8.
SUPFAM; SSF48452; SSF48452; 1.
SUPFAM; SSF50729; SSF50729; 4.
SUPFAM; SSF50891; SSF50891; 1.
SUPFAM; SSF90209; SSF90209; 7.
PROSITE; PS00170; CSA_PPIASE_1; 1.
PROSITE; PS50072; CSA_PPIASE_2; 1.
PROSITE; PS50196; RANBD1; 4.
PROSITE; PS50005; TPR; 1.
PROSITE; PS50293; TPR_REGION; 1.
PROSITE; PS01358; ZF_RANBP2_1; 8.
PROSITE; PS50199; ZF_RANBP2_2; 8.
1: Evidence at protein level;
3D-structure; Acetylation; Complete proteome; Disulfide bond;
Isopeptide bond; Ligase; Membrane; Metal-binding; Methylation;
mRNA transport; Nuclear pore complex; Nucleus; Phosphoprotein;
Polymorphism; Protein transport; Reference proteome; Repeat;
RNA-binding; TPR repeat; Translocation; Transport; Ubl conjugation;
Ubl conjugation pathway; Zinc; Zinc-finger.
CHAIN 1 3224 E3 SUMO-protein ligase RanBP2.
/FTId=PRO_0000204913.
REPEAT 26 59 TPR 1. {ECO:0000255|PROSITE-
ProRule:PRU00339,
ECO:0000269|PubMed:22959972}.
REPEAT 60 93 TPR 2. {ECO:0000255|PROSITE-
ProRule:PRU00339,
ECO:0000269|PubMed:22959972}.
REPEAT 94 128 TPR 3. {ECO:0000255|PROSITE-
ProRule:PRU00339,
ECO:0000269|PubMed:22959972}.
REPEAT 165 201 TPR 4. {ECO:0000255|PROSITE-
ProRule:PRU00339,
ECO:0000269|PubMed:22959972}.
REPEAT 287 319 TPR 5. {ECO:0000255|PROSITE-
ProRule:PRU00339,
ECO:0000269|PubMed:22959972}.
REPEAT 583 616 TPR 6. {ECO:0000255|PROSITE-
ProRule:PRU00339,
ECO:0000269|PubMed:22959972}.
REPEAT 648 681 TPR 7. {ECO:0000255|PROSITE-
ProRule:PRU00339,
ECO:0000269|PubMed:22959972}.
DOMAIN 1171 1307 RanBD1 1. {ECO:0000255|PROSITE-
ProRule:PRU00164}.
DOMAIN 2012 2148 RanBD1 2. {ECO:0000255|PROSITE-
ProRule:PRU00164}.
DOMAIN 2309 2445 RanBD1 3. {ECO:0000255|PROSITE-
ProRule:PRU00164}.
REPEAT 2633 2685 1. {ECO:0000269|PubMed:22959972}.
REPEAT 2711 2761 2. {ECO:0000269|PubMed:22959972}.
DOMAIN 2911 3046 RanBD1 4. {ECO:0000255|PROSITE-
ProRule:PRU00164}.
DOMAIN 3067 3223 PPIase cyclophilin-type.
{ECO:0000255|PROSITE-ProRule:PRU00156}.
ZN_FING 1351 1381 RanBP2-type 1. {ECO:0000255|PROSITE-
ProRule:PRU00322}.
ZN_FING 1415 1444 RanBP2-type 2. {ECO:0000255|PROSITE-
ProRule:PRU00322}.
ZN_FING 1479 1508 RanBP2-type 3. {ECO:0000255|PROSITE-
ProRule:PRU00322}.
ZN_FING 1543 1572 RanBP2-type 4. {ECO:0000255|PROSITE-
ProRule:PRU00322}.
ZN_FING 1606 1635 RanBP2-type 5. {ECO:0000255|PROSITE-
ProRule:PRU00322}.
ZN_FING 1665 1694 RanBP2-type 6. {ECO:0000255|PROSITE-
ProRule:PRU00322}.
ZN_FING 1724 1753 RanBP2-type 7. {ECO:0000255|PROSITE-
ProRule:PRU00322}.
ZN_FING 1781 1810 RanBP2-type 8. {ECO:0000255|PROSITE-
ProRule:PRU00322}.
REGION 2147 2287 Interaction with BICD2.
{ECO:0000269|PubMed:20386726}.
REGION 2631 2635 Interaction with sumoylated RANGAP1.
REGION 2633 2761 2 X 50 AA approximate repeats.
REGION 2633 2710 Required for E3 SUMO-ligase activity.
REGION 2633 2685 Interaction with UBE2I.
REGION 2686 2761 Interaction with SUMO1.
{ECO:0000269|PubMed:15608651}.
MOD_RES 19 19 Phosphothreonine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:19690332,
ECO:0000244|PubMed:20068231}.
MOD_RES 21 21 Phosphoserine.
{ECO:0000244|PubMed:16964243,
ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:19690332,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:23186163}.
MOD_RES 779 779 Phosphothreonine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 781 781 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:23186163}.
MOD_RES 788 788 Phosphoserine.
{ECO:0000250|UniProtKB:Q9ERU9}.
MOD_RES 837 837 Phosphoserine.
{ECO:0000244|PubMed:20068231}.
MOD_RES 945 945 Asymmetric dimethylarginine.
{ECO:0000244|PubMed:24129315}.
MOD_RES 948 948 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:23186163}.
MOD_RES 955 955 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:19690332,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:23186163,
ECO:0000244|PubMed:24275569}.
MOD_RES 1016 1016 Asymmetric dimethylarginine; alternate.
{ECO:0000250|UniProtKB:Q9ERU9}.
MOD_RES 1016 1016 Omega-N-methylarginine; alternate.
{ECO:0000244|PubMed:24129315}.
MOD_RES 1098 1098 Phosphothreonine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 1103 1103 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 1107 1107 Phosphoserine.
{ECO:0000244|PubMed:19690332,
ECO:0000244|PubMed:23186163}.
MOD_RES 1110 1110 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:23186163}.
MOD_RES 1144 1144 Phosphothreonine.
{ECO:0000244|PubMed:16964243,
ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:23186163}.
MOD_RES 1160 1160 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:21406692,
ECO:0000244|PubMed:23186163,
ECO:0000244|PubMed:24275569}.
MOD_RES 1249 1249 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 1396 1396 Phosphothreonine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:19690332,
ECO:0000244|PubMed:23186163}.
MOD_RES 1412 1412 Phosphothreonine.
{ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:23186163}.
MOD_RES 1443 1443 Phosphoserine.
{ECO:0000244|PubMed:18669648}.
MOD_RES 1450 1450 Phosphoserine.
{ECO:0000244|PubMed:23186163,
ECO:0000244|PubMed:24275569}.
MOD_RES 1456 1456 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:21406692,
ECO:0000244|PubMed:23186163,
ECO:0000244|PubMed:24275569}.
MOD_RES 1509 1509 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:23186163,
ECO:0000244|PubMed:24275569}.
MOD_RES 1520 1520 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 1573 1573 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:23186163}.
MOD_RES 1833 1833 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 1835 1835 Phosphoserine.
{ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:23186163}.
MOD_RES 1869 1869 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:23186163}.
MOD_RES 1871 1871 Phosphoserine.
{ECO:0000244|PubMed:19690332}.
MOD_RES 1977 1977 N6-acetyllysine.
{ECO:0000250|UniProtKB:Q9ERU9}.
MOD_RES 2005 2005 Phosphothreonine.
{ECO:0000250|UniProtKB:Q9ERU9}.
MOD_RES 2008 2008 Phosphoserine.
{ECO:0000250|UniProtKB:Q9ERU9}.
MOD_RES 2153 2153 Phosphothreonine.
{ECO:0000250|UniProtKB:Q9ERU9}.
MOD_RES 2246 2246 Phosphoserine.
{ECO:0000250|UniProtKB:Q9ERU9}.
MOD_RES 2251 2251 Phosphoserine.
{ECO:0000250|UniProtKB:Q9ERU9}.
MOD_RES 2270 2270 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:19690332,
ECO:0000244|PubMed:23186163}.
MOD_RES 2280 2280 Phosphoserine.
{ECO:0000250|UniProtKB:Q9ERU9}.
MOD_RES 2290 2290 Phosphoserine.
{ECO:0000250|UniProtKB:Q9ERU9}.
MOD_RES 2293 2293 Phosphothreonine.
{ECO:0000250|UniProtKB:Q9ERU9}.
MOD_RES 2297 2297 Phosphoserine.
{ECO:0000250|UniProtKB:Q9ERU9}.
MOD_RES 2462 2462 Phosphoserine.
{ECO:0000250|UniProtKB:Q9ERU9}.
MOD_RES 2493 2493 Phosphoserine.
{ECO:0000250|UniProtKB:Q9ERU9}.
MOD_RES 2510 2510 Phosphoserine.
{ECO:0000250|UniProtKB:Q9ERU9}.
MOD_RES 2526 2526 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 2613 2613 Phosphothreonine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:23186163}.
MOD_RES 2666 2666 Phosphotyrosine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 2668 2668 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:19690332,
ECO:0000244|PubMed:21406692,
ECO:0000244|PubMed:23186163,
ECO:0000244|PubMed:24275569}.
MOD_RES 2741 2741 Phosphoserine.
{ECO:0000244|PubMed:18669648}.
MOD_RES 2743 2743 Phosphothreonine.
{ECO:0000244|PubMed:18669648}.
MOD_RES 2805 2805 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 2900 2900 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:19690332,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:21406692,
ECO:0000244|PubMed:24275569}.
MOD_RES 3207 3207 Phosphoserine.
{ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:21406692,
ECO:0000244|PubMed:23186163}.
CROSSLNK 1350 1350 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:28112733}.
CROSSLNK 1414 1414 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:25218447,
ECO:0000244|PubMed:25755297,
ECO:0000244|PubMed:25772364,
ECO:0000244|PubMed:28112733}.
CROSSLNK 1596 1596 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:28112733}.
CROSSLNK 1605 1605 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO1).
{ECO:0000244|PubMed:25114211}.
CROSSLNK 1605 1605 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:25755297,
ECO:0000244|PubMed:28112733}.
CROSSLNK 1655 1655 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:28112733}.
CROSSLNK 1664 1664 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO1).
{ECO:0000244|PubMed:25114211}.
CROSSLNK 1664 1664 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:25755297,
ECO:0000244|PubMed:28112733}.
CROSSLNK 1714 1714 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:28112733}.
CROSSLNK 1723 1723 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO1).
{ECO:0000244|PubMed:25114211}.
CROSSLNK 1723 1723 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:25755297,
ECO:0000244|PubMed:28112733}.
CROSSLNK 2022 2022 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:28112733}.
CROSSLNK 2522 2522 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:28112733}.
CROSSLNK 2592 2592 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO).
{ECO:0000269|PubMed:15378033}.
CROSSLNK 2594 2594 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO1).
{ECO:0000244|PubMed:25114211}.
CROSSLNK 2594 2594 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:28112733}.
CROSSLNK 2612 2612 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:28112733}.
CROSSLNK 2792 2792 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:25114211,
ECO:0000244|PubMed:28112733}.
CROSSLNK 2815 2815 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:28112733}.
VARIANT 548 548 V -> L (in dbSNP:rs1057954).
/FTId=VAR_029765.
VARIANT 580 580 E -> K (in dbSNP:rs4012065).
/FTId=VAR_029766.
VARIANT 581 581 C -> Y (in dbSNP:rs1057957).
/FTId=VAR_029767.
VARIANT 585 585 T -> M (in IIAE3; dbSNP:rs121434502).
{ECO:0000269|PubMed:19118815}.
/FTId=VAR_054997.
VARIANT 653 653 T -> I (in IIAE3; dbSNP:rs121434503).
{ECO:0000269|PubMed:19118815}.
/FTId=VAR_054998.
VARIANT 656 656 I -> V (in IIAE3; dbSNP:rs121434504).
{ECO:0000269|PubMed:19118815}.
/FTId=VAR_054999.
VARIANT 725 725 S -> G (in dbSNP:rs17414315).
/FTId=VAR_050575.
VARIANT 784 784 R -> K (in dbSNP:rs2912838).
{ECO:0000269|PubMed:7603572}.
/FTId=VAR_023939.
VARIANT 1870 1870 P -> L (in dbSNP:rs2889846).
/FTId=VAR_029768.
VARIANT 1892 1892 P -> A (in dbSNP:rs12770).
/FTId=VAR_014886.
VARIANT 1892 1892 P -> R (in dbSNP:rs12770).
/FTId=VAR_050576.
MUTAGEN 2632 2632 V->K: Abolishes interaction with
sumoylated RANGAP1.
{ECO:0000269|PubMed:15388847}.
MUTAGEN 2634 2634 I->K: Abolishes interaction with
sumoylated RANGAP1.
{ECO:0000269|PubMed:15388847}.
MUTAGEN 2635 2635 V->K: Abolishes interaction with
sumoylated RANGAP1.
{ECO:0000269|PubMed:15388847}.
MUTAGEN 2640 2640 P->A: No effect on SUMO E3 ligase
activity. {ECO:0000269|PubMed:15378033}.
MUTAGEN 2645 2645 K->A: No effect on SUMO E3 ligase
activity. {ECO:0000269|PubMed:15378033}.
MUTAGEN 2651 2651 L->A: Abolishes binding to UBE2I and SUMO
E3 ligase activity.
{ECO:0000269|PubMed:15378033}.
MUTAGEN 2652 2652 K->A: No effect on SUMO E3 ligase
activity. {ECO:0000269|PubMed:15378033}.
MUTAGEN 2653 2653 L->A: Abolishes binding to UBE2I and SUMO
E3 ligase activity.
{ECO:0000269|PubMed:15378033}.
MUTAGEN 2654 2654 P->A: Impairs SUMO E3 ligase activity.
{ECO:0000269|PubMed:15378033}.
MUTAGEN 2655 2655 P->A: No effect on SUMO E3 ligase
activity. {ECO:0000269|PubMed:15378033}.
MUTAGEN 2656 2656 T->A: Impairs SUMO E3 ligase activity.
{ECO:0000269|PubMed:15378033}.
MUTAGEN 2657 2657 F->A: Abolishes binding to UBE2I and SUMO
E3 ligase activity.
{ECO:0000269|PubMed:15378033}.
MUTAGEN 2658 2658 F->A: Abolishes binding to UBE2I and SUMO
E3 ligase activity.
{ECO:0000269|PubMed:15378033}.
MUTAGEN 2659 2659 C->S,A: Impairs SUMO E3 ligase activity.
{ECO:0000269|PubMed:15378033}.
MUTAGEN 2676 2676 D->A: Impairs SUMO E3 ligase activity.
{ECO:0000269|PubMed:15378033}.
MUTAGEN 2677 2677 F->A: Impairs SUMO E3 ligase activity.
{ECO:0000269|PubMed:15378033}.
MUTAGEN 2689 2689 Y->A: Impairs SUMO E3 ligase activity.
{ECO:0000269|PubMed:15378033}.
CONFLICT 777 777 H -> R (in Ref. 1; AAC41758).
{ECO:0000305}.
CONFLICT 2207 2207 S -> A (in Ref. 5; AAA85838).
{ECO:0000305}.
CONFLICT 2210 2210 T -> P (in Ref. 5; AAA85838).
{ECO:0000305}.
CONFLICT 2216 2216 E -> V (in Ref. 5; AAA85838).
{ECO:0000305}.
CONFLICT 2436 2436 F -> C (in Ref. 5; AAA85838).
{ECO:0000305}.
CONFLICT 2475 2475 T -> P (in Ref. 5; AAA85838).
{ECO:0000305}.
CONFLICT 2531 2531 K -> N (in Ref. 5; AAA85838).
{ECO:0000305}.
CONFLICT 2545 2545 F -> C (in Ref. 5). {ECO:0000305}.
HELIX 5 18 {ECO:0000244|PDB:4GA0}.
HELIX 22 26 {ECO:0000244|PDB:4GA0}.
HELIX 29 38 {ECO:0000244|PDB:4GA0}.
HELIX 42 55 {ECO:0000244|PDB:4GA0}.
HELIX 60 72 {ECO:0000244|PDB:4GA0}.
HELIX 76 89 {ECO:0000244|PDB:4GA0}.
HELIX 94 107 {ECO:0000244|PDB:4GA0}.
HELIX 112 124 {ECO:0000244|PDB:4GA0}.
HELIX 129 141 {ECO:0000244|PDB:4GA0}.
STRAND 1191 1205 {ECO:0000244|PDB:5CLL}.
TURN 1206 1209 {ECO:0000244|PDB:5CLL}.
STRAND 1210 1224 {ECO:0000244|PDB:5CLL}.
TURN 1225 1227 {ECO:0000244|PDB:5CLL}.
STRAND 1230 1236 {ECO:0000244|PDB:5CLL}.
TURN 1237 1239 {ECO:0000244|PDB:5CLL}.
STRAND 1242 1247 {ECO:0000244|PDB:5CLL}.
STRAND 1255 1257 {ECO:0000244|PDB:5CLL}.
STRAND 1260 1270 {ECO:0000244|PDB:5CLL}.
STRAND 1277 1284 {ECO:0000244|PDB:5CLL}.
HELIX 1288 1302 {ECO:0000244|PDB:5CLL}.
STRAND 2028 2030 {ECO:0000244|PDB:1XKE}.
STRAND 2032 2046 {ECO:0000244|PDB:1XKE}.
TURN 2047 2050 {ECO:0000244|PDB:1XKE}.
STRAND 2051 2065 {ECO:0000244|PDB:1XKE}.
STRAND 2071 2077 {ECO:0000244|PDB:1XKE}.
TURN 2078 2081 {ECO:0000244|PDB:1XKE}.
STRAND 2082 2088 {ECO:0000244|PDB:1XKE}.
STRAND 2095 2097 {ECO:0000244|PDB:1XKE}.
STRAND 2105 2111 {ECO:0000244|PDB:1XKE}.
STRAND 2113 2115 {ECO:0000244|PDB:1XKE}.
STRAND 2117 2125 {ECO:0000244|PDB:1XKE}.
HELIX 2129 2145 {ECO:0000244|PDB:1XKE}.
TURN 2146 2148 {ECO:0000244|PDB:1XKE}.
STRAND 2632 2637 {ECO:0000244|PDB:3UIP}.
HELIX 2642 2650 {ECO:0000244|PDB:3UIP}.
HELIX 2657 2661 {ECO:0000244|PDB:3UIP}.
STRAND 2663 2665 {ECO:0000244|PDB:3UIN}.
HELIX 2677 2682 {ECO:0000244|PDB:3UIP}.
TURN 2683 2686 {ECO:0000244|PDB:3UIP}.
STRAND 2710 2712 {ECO:0000244|PDB:2LAS}.
TURN 2926 2929 {ECO:0000244|PDB:4L6E}.
STRAND 2930 2944 {ECO:0000244|PDB:4L6E}.
TURN 2945 2948 {ECO:0000244|PDB:4L6E}.
STRAND 2949 2963 {ECO:0000244|PDB:4L6E}.
TURN 2964 2967 {ECO:0000244|PDB:4L6E}.
STRAND 2968 2974 {ECO:0000244|PDB:4L6E}.
TURN 2976 2978 {ECO:0000244|PDB:4L6E}.
STRAND 2981 2986 {ECO:0000244|PDB:4L6E}.
STRAND 2994 2996 {ECO:0000244|PDB:4L6E}.
STRAND 3000 3009 {ECO:0000244|PDB:4L6E}.
STRAND 3016 3026 {ECO:0000244|PDB:4L6E}.
HELIX 3027 3047 {ECO:0000244|PDB:4L6E}.
STRAND 3065 3072 {ECO:0000244|PDB:4I9Y}.
STRAND 3075 3084 {ECO:0000244|PDB:4I9Y}.
TURN 3086 3088 {ECO:0000244|PDB:4I9Y}.
HELIX 3090 3101 {ECO:0000244|PDB:4I9Y}.
TURN 3102 3104 {ECO:0000244|PDB:4I9Y}.
STRAND 3112 3117 {ECO:0000244|PDB:4I9Y}.
TURN 3118 3120 {ECO:0000244|PDB:4I9Y}.
STRAND 3121 3124 {ECO:0000244|PDB:4I9Y}.
TURN 3127 3129 {ECO:0000244|PDB:4I9Y}.
STRAND 3130 3133 {ECO:0000244|PDB:4I9Y}.
STRAND 3157 3160 {ECO:0000244|PDB:4I9Y}.
STRAND 3168 3170 {ECO:0000244|PDB:4LQW}.
STRAND 3172 3177 {ECO:0000244|PDB:4I9Y}.
HELIX 3180 3182 {ECO:0000244|PDB:4I9Y}.
TURN 3183 3185 {ECO:0000244|PDB:4I9Y}.
STRAND 3188 3194 {ECO:0000244|PDB:4I9Y}.
HELIX 3196 3203 {ECO:0000244|PDB:4I9Y}.
STRAND 3216 3223 {ECO:0000244|PDB:4I9Y}.
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


Related products :

Catalog number Product name Quantity
EIAAB34052 358 kDa nucleoporin,E3 SUMO-protein ligase RanBP2,Homo sapiens,Human,Nuclear pore complex protein Nup358,Nucleoporin Nup358,NUP358,p270,Ran-binding protein 2,RanBP2,RANBP2
EIAAB34050 358 kDa nucleoporin,Bos taurus,Bovine,E3 SUMO-protein ligase RanBP2,Nuclear pore complex protein Nup358,Nucleoporin Nup358,p270,Ran-binding protein 2,RanBP2,RANBP2
EIAAB34051 E3 SUMO-protein ligase RanBP2,Mouse,Mus musculus,Ran-binding protein 2,RanBP2,Ranbp2
CSB-EL019311MO Mouse E3 SUMO-protein ligase RanBP2(RANBP2) ELISA kit SpeciesMouse 96T
CSB-EL019311BO Bovine E3 SUMO-protein ligase RanBP2(RANBP2) ELISA kit SpeciesBovine 96T
CSB-EL019311HU Human E3 SUMO-protein ligase RanBP2(RANBP2) ELISA kit SpeciesHuman 96T
CSB-EL019311MO Mouse E3 SUMO-protein ligase RanBP2(RANBP2) ELISA kit 96T
CSB-EL019311HU Human E3 SUMO-protein ligase RanBP2(RANBP2) ELISA kit 96T
CSB-EL019311BO Bovine E3 SUMO-protein ligase RanBP2(RANBP2) ELISA kit 96T
RBP2_MOUSE ELISA Kit FOR E3 SUMO-protein ligase RanBP2; organism: Mouse; gene name: Ranbp2 96T
RBP2_BOVIN ELISA Kit FOR E3 SUMO-protein ligase RanBP2; organism: Bovine; gene name: RANBP2 96T
EIAAB28281 50 kDa nucleoporin,Homo sapiens,Human,NPAP60L,Nuclear pore complex protein Nup50,Nuclear pore-associated protein 60 kDa-like,Nucleoporin Nup50,NUP50,PRO1146
EIAAB28282 50 kDa nucleoporin,Mouse,Mus musculus,Npap60,Nuclear pore complex protein Nup50,Nuclear pore-associated protein 60 kDa-like,Nucleoporin Nup50,Nup50
EIAAB28280 50 kDa nucleoporin,Npap60,Nuclear pore complex protein Nup50,Nuclear pore-associated protein 60 kDa-like,Nucleoporin Nup50,Nup50,Rat,Rattus norvegicus
EIAAB28295 85 kDa nucleoporin,FROUNT,Homo sapiens,Human,Nuclear pore complex protein Nup85,Nucleoporin Nup75,Nucleoporin Nup85,NUP75,NUP85,PCNT1,Pericentrin-1
EIAAB28283 35 kDa nucleoporin,Homo sapiens,Human,Mitotic phosphoprotein 44,MP44,MP-44,Nuclear pore complex protein Nup53,Nucleoporin Nup35,Nucleoporin NUP53,NUP35,NUP53
EIAAB28096 160 kDa nucleoporin,Gene trap locus 1-13 protein,Gtl1-13,GTL-13,Kiaa0197,Mouse,Mus musculus,Nuclear pore complex protein Nup160,Nucleoporin Nup160,Nup160
EIAAB28285 35 kDa nucleoporin,Mitotic phosphoprotein 44,Mouse,Mp44,MP-44,Mus musculus,Nuclear pore complex protein Nup53,Nucleoporin Nup35,Nucleoporin NUP53,Nup35,Nup53
EIAAB28109 214 kDa nucleoporin,CAIN,CAN,Homo sapiens,Human,KIAA0023,Nuclear pore complex protein Nup214,Nucleoporin Nup214,NUP214,Protein CAN
EIAAB28301 93 kDa nucleoporin,CBP-interacting protein 4,Cip4,Kiaa0095,Mouse,Mus musculus,Nuclear pore complex protein Nup93,Nucleoporin Nup93,Nup93
EIAAB28284 35 kDa nucleoporin,Nuclear pore complex protein Nup53,Nucleoporin Nup35,Nucleoporin NUP53,Nup35,Nup53,Rat,Rattus norvegicus
EIAAB28298 88 kDa nucleoporin,Nuclear pore complex protein Nup88,Nucleoporin Nup84,Nucleoporin Nup88,Nup84,Nup88,Rat,Rattus norvegicus
EIAAB28097 160 kDa nucleoporin,Homo sapiens,Human,KIAA0197,Nuclear pore complex protein Nup160,Nucleoporin Nup160,NUP120,NUP160
EIAAB28108 205 kDa nucleoporin,C7orf14,Homo sapiens,Human,KIAA0225,Nuclear pore complex protein Nup205,Nucleoporin Nup205,NUP205
EIAAB28292 85 kDa nucleoporin,FROUNT,Mouse,Mus musculus,Nuclear pore complex protein Nup85,Nucleoporin Nup85,Nup85,Pcnt1,Pericentrin-1


 

GENTAUR Belgium BVBA BE0473327336
Voortstraat 49, 1910 Kampenhout BELGIUM
Tel 0032 16 58 90 45

Fax 0032 16 50 90 45
info@gentaur.com | Gentaur





GENTAUR Ltd.
Howard Frank Turnberry House
1404-1410 High Road
Whetstone London N20 9BH
Tel 020 3393 8531 Fax 020 8445 9411
uk@gentaur.com | Gentaur

 

 




GENTAUR France SARL
9, rue Lagrange, 75005 Paris
Tel 01 43 25 01 50

Fax 01 43 25 01 60
RCS Paris B 484 237 888

SIRET 48423788800017

BNP PARIBAS PARIS PL MAUBERT BIC BNPAFRPPPRG

france@gentaur.com | Gentaur

GENTAUR GmbH
Marienbongard 20
52062 Aachen Deutschland
Support Karolina Elandt
Tel: 0035929830070
Fax: (+49) 241 56 00 47 88

Logistic :0241 40 08 90 86
Bankleitzahl 39050000
IBAN lautet DE8839050000107569353
Handelsregister Aachen HR B 16058
Umsatzsteuer-Identifikationsnummer *** DE 815175831
Steuernummer 201/5961/3925
de@gentaur.com | Gentaur

GENTAUR U.S.A
Genprice Inc, Logistics
547, Yurok Circle
San Jose, CA 95123
CA 95123
Tel (408) 780-0908,
Fax (408) 780-0908,
sales@genprice.com

Genprice Inc, Invoices and accounting
6017 Snell Ave, Ste 357
San Jose, CA 95123




GENTAUR Nederland BV
NL850396268B01 KVK nummer 52327027
Kuiper 1
5521 DG Eersel Nederland
Tel:  0208-080893  Fax: 0497-517897
nl@gentaur.com | Gentaur
IBAN: NL04 RABO 0156 9854 62   SWIFT RABONL2U






GENTAUR Spain
tel:0911876558
spain@gentaur.com | Gentaur






ГЕНТАУЪР БЪЛГАРИЯ
ID # 201 358 931 /BULSTAT
София 1000, ул. "Граф Игнатиев" 53 вх. В, ет. 2
Tel 0035924682280 Fax 0035924808322
e-mail: Sofia@gentaur.com | Gentaur
IBAN: BG11FINV91501014771636
BIC: FINVBGSF

GENTAUR Poland Sp. z o.o.


ul. Grunwaldzka 88/A m.2
81-771 Sopot, Poland
TEL Gdansk 058 710 33 44 FAX  058 710 33 48              

poland@gentaur.com | Gentaur

Other countries

Österreich +43720880899

Canada Montreal +15149077481

Ceská republika Praha +420246019719

Danmark +4569918806

Finland Helsset +358942419041

Magyarország Budapest +3619980547

Ireland Dublin+35316526556

Luxembourg+35220880274

Norge Oslo+4721031366

Sverige Stockholm+46852503438

Schweiz Züri+41435006251

US New York+17185132983

GENTAUR Italy
SRL IVA IT03841300167
Piazza Giacomo Matteotti, 6
24122 Bergamo Tel 02 36 00 65 93
Fax 02 36 00 65 94
italia@gentaur.com | Gentaur