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E3 SUMO-protein ligase RanBP2 (EC 6.3.2.-) (Ran-binding protein 2) (RanBP2)

 RBP2_MOUSE              Reviewed;        3053 AA.
Q9ERU9; E9QM01; Q61992; Q8C9K9;
06-DEC-2005, integrated into UniProtKB/Swiss-Prot.
27-JUL-2011, sequence version 2.
30-AUG-2017, entry version 144.
RecName: Full=E3 SUMO-protein ligase RanBP2;
EC=6.3.2.-;
AltName: Full=Ran-binding protein 2;
Short=RanBP2;
Name=Ranbp2;
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
STRAIN=129/Ola;
PubMed=11353387; DOI=10.1007/s003350010291;
Fauser S., Aslanukov A., Roepman R., Ferreira P.A.;
"Genomic organization, expression, and localization of murine Ran-
binding protein 2 (RanBP2) gene.";
Mamm. Genome 12:406-415(2001).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=C57BL/6J;
PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
Lindblad-Toh K., Eichler E.E., Ponting C.P.;
"Lineage-specific biology revealed by a finished genome assembly of
the mouse.";
PLoS Biol. 7:E1000112-E1000112(2009).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-222.
STRAIN=C57BL/6J; TISSUE=Thymus;
PubMed=16141072; DOI=10.1126/science.1112014;
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
Hayashizaki Y.;
"The transcriptional landscape of the mammalian genome.";
Science 309:1559-1563(2005).
[4]
NUCLEOTIDE SEQUENCE [MRNA] OF 985-2249.
PubMed=8603673;
Wilken N., Senecal J.L., Scheer U., Dabauvalle M.C.;
"Localization of the Ran-GTP binding protein RanBP2 at the cytoplasmic
side of the nuclear pore complex.";
Eur. J. Cell Biol. 68:211-219(1995).
[5]
INTERACTION WITH PRKN.
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).
[6]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Brain;
PubMed=16452087; DOI=10.1074/mcp.T500041-MCP200;
Trinidad J.C., Specht C.G., Thalhammer A., Schoepfer R.,
Burlingame A.L.;
"Comprehensive identification of phosphorylation sites in postsynaptic
density preparations.";
Mol. Cell. Proteomics 5:914-922(2006).
[7]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-21; SER-954; SER-2083;
THR-2130; SER-2134; SER-2348; SER-2505; SER-2576; THR-2578 AND
SER-2729, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
ANALYSIS].
TISSUE=Liver;
PubMed=17242355; DOI=10.1073/pnas.0609836104;
Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
"Large-scale phosphorylation analysis of mouse liver.";
Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
[8]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-954; SER-1154 AND
SER-2729, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
ANALYSIS].
PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
Thibault P.;
"The phagosomal proteome in interferon-gamma-activated macrophages.";
Immunity 30:143-154(2009).
[9]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-781; SER-788 AND
SER-2505, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
ANALYSIS].
TISSUE=Embryonic fibroblast;
PubMed=19131326; DOI=10.1074/mcp.M800451-MCP200;
Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.;
"Large scale localization of protein phosphorylation by use of
electron capture dissociation mass spectrometry.";
Mol. Cell. Proteomics 8:904-912(2009).
[10]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-21; SER-781; SER-788;
SER-954; SER-1101; SER-1154; THR-1842; SER-1845; THR-1990; SER-2083;
SER-2088; SER-2107; SER-2117; SER-2127; THR-2130; SER-2134; SER-2299;
SER-2330; SER-2505; SER-2576; THR-2578 AND SER-2729, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung,
Pancreas, Spleen, and Testis;
PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
"A tissue-specific atlas of mouse protein phosphorylation and
expression.";
Cell 143:1174-1189(2010).
[11]
DISULFIDE BOND.
PubMed=23641069; DOI=10.1242/jcs.124172;
Yoshimura S.H., Otsuka S., Kumeta M., Taga M., Takeyasu K.;
"Intermolecular disulfide bonds between nucleoporins regulate
karyopherin-dependent nuclear transport.";
J. Cell Sci. 126:3141-3150(2013).
[12]
ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-1814, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Embryonic fibroblast;
PubMed=23806337; DOI=10.1016/j.molcel.2013.06.001;
Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z.,
Zhang Y., Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.;
"SIRT5-mediated lysine desuccinylation impacts diverse metabolic
pathways.";
Mol. Cell 50:919-930(2013).
[13]
METHYLATION [LARGE SCALE ANALYSIS] AT ARG-1015, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Brain, and Embryo;
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).
-!- 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 (By similarity). 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. {ECO:0000250|UniProtKB:P49792}.
-!- PATHWAY: Protein modification; protein sumoylation.
-!- SUBUNIT: Forms a tight complex with RANBP1 and UBE2I. Interacts
with SUMO1 but not SUMO2. Interacts with sumoylated RANGAP1.
Interacts with CDCA8. Interacts with PML. Interacts with BICD2 (By
similarity). Interacts with PRKN (PubMed:16332688).
{ECO:0000250|UniProtKB:P49792, ECO:0000269|PubMed:16332688}.
-!- INTERACTION:
Q9WVS6:Prkn; NbExp=2; IntAct=EBI-643756, EBI-973635;
-!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:P49792}.
Nucleus membrane {ECO:0000250|UniProtKB:P49792}. Nucleus, nuclear
pore complex {ECO:0000250|UniProtKB:P49792}. Nucleus envelope
{ECO:0000250|UniProtKB:P49792}. Note=Detected in diffuse and
discrete intranuclear foci. Cytoplasmic filaments.
{ECO:0000250|UniProtKB:P49792}.
-!- DOMAIN: Contains a dozen F-X-F-G repeats in the C-terminal half.
-!- DOMAIN: The PPIase cyclophilin-type domain has high structural
similarity with PPIA, but has extremely low and barely detectable
proline isomerase activity (in vitro) (By similarity). Only about
half of the residues that surround the PPIA active site cleft are
conserved. {ECO:0000250|UniProtKB:P49792}.
-!- PTM: Polyubiquitinated by PRKN, which leads to proteasomal
degradation. {ECO:0000250|UniProtKB:P49792}.
-!- 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:0000269|PubMed:23641069}.
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EMBL; AF279458; AAG17403.1; -; Genomic_DNA.
EMBL; AC158593; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AK041932; BAC31101.1; -; mRNA.
EMBL; X87337; CAA60778.1; -; mRNA.
CCDS; CCDS23861.1; -.
PIR; S57968; S57968.
RefSeq; NP_035370.2; NM_011240.3.
UniGene; Mm.431695; -.
ProteinModelPortal; Q9ERU9; -.
SMR; Q9ERU9; -.
BioGrid; 202582; 82.
IntAct; Q9ERU9; 88.
MINT; MINT-1659128; -.
STRING; 10090.ENSMUSP00000003310; -.
iPTMnet; Q9ERU9; -.
PhosphoSitePlus; Q9ERU9; -.
EPD; Q9ERU9; -.
MaxQB; Q9ERU9; -.
PaxDb; Q9ERU9; -.
PeptideAtlas; Q9ERU9; -.
PRIDE; Q9ERU9; -.
Ensembl; ENSMUST00000003310; ENSMUSP00000003310; ENSMUSG00000003226.
GeneID; 19386; -.
KEGG; mmu:19386; -.
UCSC; uc007fdd.1; mouse.
CTD; 5903; -.
MGI; MGI:894323; Ranbp2.
eggNOG; KOG0864; Eukaryota.
eggNOG; KOG0865; Eukaryota.
eggNOG; COG0652; LUCA.
eggNOG; COG5171; LUCA.
GeneTree; ENSGT00880000137938; -.
HOGENOM; HOG000089994; -.
HOVERGEN; HBG092361; -.
InParanoid; Q9ERU9; -.
KO; K12172; -.
OMA; TKKEGQW; -.
OrthoDB; EOG091G0BGL; -.
TreeFam; TF314797; -.
Reactome; R-MMU-159236; Transport of Mature mRNA derived from an Intron-Containing Transcript.
Reactome; R-MMU-170822; Regulation of Glucokinase by Glucokinase Regulatory Protein.
Reactome; R-MMU-191859; snRNP Assembly.
Reactome; R-MMU-2467813; Separation of Sister Chromatids.
Reactome; R-MMU-2500257; Resolution of Sister Chromatid Cohesion.
Reactome; R-MMU-3108214; SUMOylation of DNA damage response and repair proteins.
Reactome; R-MMU-3301854; Nuclear Pore Complex (NPC) Disassembly.
Reactome; R-MMU-3371453; Regulation of HSF1-mediated heat shock response.
Reactome; R-MMU-4551638; SUMOylation of chromatin organization proteins.
Reactome; R-MMU-4570464; SUMOylation of RNA binding proteins.
Reactome; R-MMU-4615885; SUMOylation of DNA replication proteins.
Reactome; R-MMU-5578749; Transcriptional regulation by small RNAs.
Reactome; R-MMU-5663220; RHO GTPases Activate Formins.
Reactome; R-MMU-68877; Mitotic Prometaphase.
UniPathway; UPA00886; -.
ChiTaRS; Ranbp2; mouse.
PRO; PR:Q9ERU9; -.
Proteomes; UP000000589; Chromosome 10.
Bgee; ENSMUSG00000003226; -.
CleanEx; MM_RANBP2; -.
Genevisible; Q9ERU9; MM.
GO; GO:0005642; C:annulate lamellae; ISS:UniProtKB.
GO; GO:0005813; C:centrosome; IBA:GO_Central.
GO; GO:1990723; C:cytoplasmic periphery of the nuclear pore complex; IEA:Ensembl.
GO; GO:0005739; C:mitochondrion; IDA:MGI.
GO; GO:0005635; C:nuclear envelope; ISS:UniProtKB.
GO; GO:0042405; C:nuclear inclusion body; ISS:UniProtKB.
GO; GO:0031965; C:nuclear membrane; ISS:UniProtKB.
GO; GO:0005643; C:nuclear pore; ISS:UniProtKB.
GO; GO:0044614; C:nuclear pore cytoplasmic filaments; IEA:Ensembl.
GO; GO:0044615; C:nuclear pore nuclear basket; ISS:UniProtKB.
GO; GO:0005634; C:nucleus; IBA:GO_Central.
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; IBA: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; IEA:Ensembl.
GO; GO:0000082; P:G1/S transition of mitotic cell cycle; IBA:GO_Central.
GO; GO:0051028; P:mRNA transport; IEA:UniProtKB-KW.
GO; GO:0006607; P:NLS-bearing protein import into nucleus; IEA:Ensembl.
GO; GO:0033133; P:positive regulation of glucokinase activity; IDA:MGI.
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:0006606; P:protein import into nucleus; IBA:GO_Central.
GO; GO:0016925; P:protein sumoylation; ISS:UniProtKB.
GO; GO:0090526; P:regulation of gluconeogenesis involved in cellular glucose homeostasis; IMP:MGI.
GO; GO:0001975; P:response to amphetamine; IEA:Ensembl.
GO; GO:0006405; P:RNA export from nucleus; IBA:GO_Central.
GO; GO:0007051; P:spindle organization; IBA:GO_Central.
GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; IBA:GO_Central.
Gene3D; 1.25.40.10; -; 3.
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; 6.
PRINTS; PR00153; CSAPPISMRASE.
SMART; SM00160; RanBD; 4.
SMART; SM00028; TPR; 1.
SMART; SM00547; ZnF_RBZ; 6.
SUPFAM; SSF48452; SSF48452; 1.
SUPFAM; SSF50729; SSF50729; 4.
SUPFAM; SSF50891; SSF50891; 1.
SUPFAM; SSF90209; SSF90209; 4.
PROSITE; PS00170; CSA_PPIASE_1; 1.
PROSITE; PS50072; CSA_PPIASE_2; 1.
PROSITE; PS50196; RANBD1; 4.
PROSITE; PS50005; TPR; 2.
PROSITE; PS50293; TPR_REGION; 1.
PROSITE; PS01358; ZF_RANBP2_1; 6.
PROSITE; PS50199; ZF_RANBP2_2; 6.
1: Evidence at protein level;
Acetylation; Complete proteome; Disulfide bond; Isopeptide bond;
Ligase; Membrane; Metal-binding; Methylation; mRNA transport;
Nuclear pore complex; Nucleus; Phosphoprotein; Protein transport;
Reference proteome; Repeat; RNA-binding; TPR repeat; Translocation;
Transport; Ubl conjugation; Ubl conjugation pathway; Zinc;
Zinc-finger.
CHAIN 1 3053 E3 SUMO-protein ligase RanBP2.
/FTId=PRO_0000204914.
REPEAT 26 59 TPR 1.
REPEAT 60 93 TPR 2.
REPEAT 94 128 TPR 3.
REPEAT 165 201 TPR 4.
REPEAT 288 319 TPR 5.
REPEAT 583 616 TPR 6.
REPEAT 648 681 TPR 7.
DOMAIN 1165 1301 RanBD1 1. {ECO:0000255|PROSITE-
ProRule:PRU00164}.
DOMAIN 1849 1985 RanBD1 2. {ECO:0000255|PROSITE-
ProRule:PRU00164}.
DOMAIN 2146 2282 RanBD1 3. {ECO:0000255|PROSITE-
ProRule:PRU00164}.
REPEAT 2470 2522 1.
REPEAT 2546 2596 2.
DOMAIN 2740 2875 RanBD1 4. {ECO:0000255|PROSITE-
ProRule:PRU00164}.
DOMAIN 2896 3052 PPIase cyclophilin-type.
{ECO:0000255|PROSITE-ProRule:PRU00156}.
ZN_FING 1345 1375 RanBP2-type 1. {ECO:0000255|PROSITE-
ProRule:PRU00322}.
ZN_FING 1410 1439 RanBP2-type 2. {ECO:0000255|PROSITE-
ProRule:PRU00322}.
ZN_FING 1469 1498 RanBP2-type 3. {ECO:0000255|PROSITE-
ProRule:PRU00322}.
ZN_FING 1494 1527 RanBP2-type 4. {ECO:0000255|PROSITE-
ProRule:PRU00322}.
ZN_FING 1558 1587 RanBP2-type 5. {ECO:0000255|PROSITE-
ProRule:PRU00322}.
ZN_FING 1617 1646 RanBP2-type 6. {ECO:0000255|PROSITE-
ProRule:PRU00322}.
REGION 1984 2124 Interaction with BICD2.
{ECO:0000250|UniProtKB:P49792}.
REGION 2468 2472 Interaction with sumoylated RANGAP1.
{ECO:0000250}.
REGION 2470 2596 2 X 50 AA approximate repeats.
REGION 2470 2545 Required for E3 SUMO-ligase activity.
{ECO:0000250}.
REGION 2470 2522 Interaction with UBE2I. {ECO:0000250}.
REGION 2523 2596 Interaction with SUMO1. {ECO:0000250}.
COMPBIAS 2074 2079 Poly-Ser.
COMPBIAS 2506 2509 Poly-Glu.
COMPBIAS 2638 2641 Poly-Ser.
MOD_RES 21 21 Phosphoserine.
{ECO:0000244|PubMed:17242355,
ECO:0000244|PubMed:21183079}.
MOD_RES 779 779 Phosphothreonine.
{ECO:0000250|UniProtKB:P49792}.
MOD_RES 781 781 Phosphoserine.
{ECO:0000244|PubMed:19131326,
ECO:0000244|PubMed:21183079}.
MOD_RES 788 788 Phosphoserine.
{ECO:0000244|PubMed:19131326,
ECO:0000244|PubMed:21183079}.
MOD_RES 837 837 Phosphoserine.
{ECO:0000250|UniProtKB:P49792}.
MOD_RES 944 944 Asymmetric dimethylarginine.
{ECO:0000250|UniProtKB:P49792}.
MOD_RES 947 947 Phosphoserine.
{ECO:0000250|UniProtKB:P49792}.
MOD_RES 954 954 Phosphoserine.
{ECO:0000244|PubMed:17242355,
ECO:0000244|PubMed:19144319,
ECO:0000244|PubMed:21183079}.
MOD_RES 1015 1015 Asymmetric dimethylarginine; alternate.
{ECO:0000244|PubMed:24129315}.
MOD_RES 1015 1015 Omega-N-methylarginine; alternate.
{ECO:0000250|UniProtKB:P49792}.
MOD_RES 1096 1096 Phosphothreonine.
{ECO:0000250|UniProtKB:P49792}.
MOD_RES 1101 1101 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 1138 1138 Phosphothreonine.
{ECO:0000250|UniProtKB:P49792}.
MOD_RES 1154 1154 Phosphoserine.
{ECO:0000244|PubMed:19144319,
ECO:0000244|PubMed:21183079}.
MOD_RES 1243 1243 Phosphoserine.
{ECO:0000250|UniProtKB:P49792}.
MOD_RES 1407 1407 Phosphothreonine.
{ECO:0000250|UniProtKB:P49792}.
MOD_RES 1438 1438 Phosphoserine.
{ECO:0000250|UniProtKB:P49792}.
MOD_RES 1441 1441 Phosphoserine.
{ECO:0000250|UniProtKB:P49792}.
MOD_RES 1446 1446 Phosphoserine.
{ECO:0000250|UniProtKB:P49792}.
MOD_RES 1528 1528 Phosphoserine.
{ECO:0000250|UniProtKB:P49792}.
MOD_RES 1670 1670 Phosphoserine.
{ECO:0000250|UniProtKB:P49792}.
MOD_RES 1706 1706 Phosphoserine.
{ECO:0000250|UniProtKB:P49792}.
MOD_RES 1814 1814 N6-acetyllysine.
{ECO:0000244|PubMed:23806337}.
MOD_RES 1842 1842 Phosphothreonine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 1845 1845 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 1990 1990 Phosphothreonine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 2083 2083 Phosphoserine.
{ECO:0000244|PubMed:17242355,
ECO:0000244|PubMed:21183079}.
MOD_RES 2088 2088 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 2107 2107 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 2117 2117 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 2127 2127 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 2130 2130 Phosphothreonine.
{ECO:0000244|PubMed:17242355,
ECO:0000244|PubMed:21183079}.
MOD_RES 2134 2134 Phosphoserine.
{ECO:0000244|PubMed:17242355,
ECO:0000244|PubMed:21183079}.
MOD_RES 2299 2299 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 2330 2330 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 2348 2348 Phosphoserine.
{ECO:0000244|PubMed:17242355}.
MOD_RES 2364 2364 Phosphoserine.
{ECO:0000250|UniProtKB:P49792}.
MOD_RES 2450 2450 Phosphothreonine.
{ECO:0000250|UniProtKB:P49792}.
MOD_RES 2503 2503 Phosphotyrosine.
{ECO:0000250|UniProtKB:P49792}.
MOD_RES 2505 2505 Phosphoserine.
{ECO:0000244|PubMed:17242355,
ECO:0000244|PubMed:19131326,
ECO:0000244|PubMed:21183079}.
MOD_RES 2576 2576 Phosphoserine.
{ECO:0000244|PubMed:17242355,
ECO:0000244|PubMed:21183079}.
MOD_RES 2578 2578 Phosphothreonine.
{ECO:0000244|PubMed:17242355,
ECO:0000244|PubMed:21183079}.
MOD_RES 2640 2640 Phosphoserine.
{ECO:0000250|UniProtKB:P49792}.
MOD_RES 2729 2729 Phosphoserine.
{ECO:0000244|PubMed:17242355,
ECO:0000244|PubMed:19144319,
ECO:0000244|PubMed:21183079}.
MOD_RES 3036 3036 Phosphoserine.
{ECO:0000250|UniProtKB:P49792}.
CROSSLNK 1344 1344 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000250|UniProtKB:P49792}.
CROSSLNK 1557 1557 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO1).
{ECO:0000250|UniProtKB:P49792}.
CROSSLNK 1557 1557 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000250|UniProtKB:P49792}.
CROSSLNK 1607 1607 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000250|UniProtKB:P49792}.
CROSSLNK 1616 1616 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO1).
{ECO:0000250|UniProtKB:P49792}.
CROSSLNK 1616 1616 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000250|UniProtKB:P49792}.
CROSSLNK 1859 1859 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000250|UniProtKB:P49792}.
CROSSLNK 2360 2360 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000250|UniProtKB:P49792}.
CROSSLNK 2430 2430 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO).
{ECO:0000250}.
CROSSLNK 2432 2432 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO1).
{ECO:0000250|UniProtKB:P49792}.
CROSSLNK 2432 2432 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000250|UniProtKB:P49792}.
CROSSLNK 2449 2449 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000250|UniProtKB:P49792}.
CROSSLNK 2627 2627 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000250|UniProtKB:P49792}.
CROSSLNK 2649 2649 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000250|UniProtKB:P49792}.
CONFLICT 213 222 EYLESLQCLD -> VGETYFSTVF (in Ref. 3;
BAC31101). {ECO:0000305}.
CONFLICT 985 1001 LVAHASRSAESKVIEFG -> IPGSRFKVSRIKGYRIWL
(in Ref. 4; CAA60778). {ECO:0000305}.
CONFLICT 1086 1089 ISGQ -> YLA (in Ref. 4; CAA60778).
{ECO:0000305}.
CONFLICT 1269 1269 L -> F (in Ref. 4; CAA60778).
{ECO:0000305}.
CONFLICT 1273 1273 E -> G (in Ref. 4; CAA60778).
{ECO:0000305}.
CONFLICT 1276 1276 A -> S (in Ref. 4; CAA60778).
{ECO:0000305}.
CONFLICT 1280 1280 K -> Q (in Ref. 4; CAA60778).
{ECO:0000305}.
CONFLICT 1293 1293 E -> G (in Ref. 4; CAA60778).
{ECO:0000305}.
CONFLICT 1297 1297 N -> D (in Ref. 4; CAA60778).
{ECO:0000305}.
CONFLICT 1861 1861 E -> D (in Ref. 4; CAA60778).
{ECO:0000305}.
CONFLICT 2868 2869 EC -> DS (in Ref. 1; AAG17403).
{ECO:0000305}.
SEQUENCE 3053 AA; 341121 MW; 62FD4249DEE466AE CRC64;
MRRSKADVER YIASVQGSAP SPREKSMKGF YFAKLYYEAK EYDLAKKYIS TYINVQERDP
KAHRFLGLLY EVEENIDKAV ECYKRSVELN PTQKDLVLKI AELLCKNDVT DGRAKYWVER
AAKLFPGSPA IYKLKEQLLD CKGEDGWNKL FDLIQSELYA RPDDIHVNIR LVELYRSNKR
LKDAVAHCHE ADRNTALRSS LEWNLCVVQT LKEYLESLQC LDSDKSTWRA TNKDLLLAYA
NLMLLTLSTR DVQEGRELLE SFDSALQSVK SSVGGNDELS ATFLETKGHF YMHVGSLLLK
MGQQSDIQWR ALSELAALCY LVAFQVPRPK VKLIKGEAGQ NLLETMAHDR LSQSGHMLLN
LSRGKQDFLK EVVESFANKS GQSALCDALF SSQSSKERSF LGNDDIGNLD GQVPDPDDLA
RYDTGAVRAH NGSLQHLTWL GLQWNSLSTL PAIRKWLKQL FHHLPQETSR LETNAPESIC
ILDLEVFLLG VIYTSHLQLK EKCNSHHTSY QPLCLPLPVC RQLCTERQKT WWDAVCTLIH
RKALPGTSAK LRLLVQREIN SLRGQEKHGL QPALLVHWAQ SLQKTGSSLN SFYDQREYIG
RSVHYWRKVL PLLKMIRKKN SIPEPIDPLF KHFHSVDIQA SEIGEYEEDA HITFAILDAV
NGNIEDAMTA FESIKNVVSY WNLALIFHRK AEDIENDALS PEEQEECKNY LRKTRDYLIR
ILDDSDSNTS VVQKLPVPLE SVKEMLNSVM QELEDYSEGG TLYKNGCWRS ADSELKHSTP
SPTKYSLSPS KSYKYSPKTP PRWAEDQNSL LKMICQQVEA IKKEMQELKL NSNNSASPHR
WPAEPYGQDP APDGYQGSQT FHGAPLTVAT TGPSVYYSQS PAYNSQYLLR PAANVTPTKG
PVYGMNRLPP QQHIYAYSQQ MHTPPVQSSS ACMFSQEMYG PPLRFESPAT GILSPRGDDY
FNYNVQQTST NPPLPEPGYF TKPPLVAHAS RSAESKVIEF GKSNFVQPMQ GEVIRPPLTT
PAHTTQPTPF KFNSNFKSND GDFTFSSPQV VAQPPSTAYS NSESLLGLLT SDKPLQGDGY
SGLKPISGQA SGSRNTFSFG SKNTLTENMG PNQQKNFGFH RSDDMFAFHG PGKSVFTTAA
SELANKSHET DGGSAHGDEE DDGPHFEPVV PLPDKIEVKT GEEDEEEFFC NRAKLFRFDG
ESKEWKERGI GNVKILRHKT SGKIRLLMRR EQVLKICANH YISPDMKLTP NAGSDRSFVW
HALDYADELP KPEQLAIRFK TPEEAALFKC KFEEAQNILK ALGTNTSTAP NHTLRIVKES
ATQDNKDICK ADGGNLNFEF QIVKKEGPYW NCNSCSFKNA ATAKKCVSCQ NTNPTSNKEL
LGPPLVENGF APKTGLENAQ DRFATMTANK EGHWDCSVCL VRNEPTVSRC IACQNTKSAS
SFVQTSFKFG QGDLPKSVDS DFRSVFSKKE GQWECSVCLV RNERSAKKCV ACENPGKQFK
EWHCSLCSVK NEAHAIKCVA CNNPVTPSLS TAPPSFKFGT SEMSKPFRIG FEGMFAKKEG
QWDCSLCFVR NEASATHCIA CQYPNKQNQP TSCVSAPASS ETSRSPKSGF EGLFPKKEGE
WECAVCSVQN ESSSLKCVAC EASKPTHKPH EAPSAFTVGS KSQSNESAGS QVGTEFKSNF
PEKNFKVGIS EQKFKFGHVD QEKTPSFAFQ GGSNTEFKSI KDGFSFCIPV SADGFKFGIQ
EKGNQEKKSE KHLENDPSFQ AHDTSGQKNG SGVVFGQTSS TFTFADLAKS TSREGFQFGK
KDPNFKGFSG AGEKLFSSQS GKVAEKANTS SDLEKDDDAY KTEDSDDIHF EPVVQMPEKV
ELVTGEEDEK VLYSQRVKLF RFDAEISQWK ERGLGNLKIL KNEVNGKLRM LMRREQVLKV
CANHWITTTM NLKPLSGSDR AWMWLASDFS DGDAKLEQLA AKFKTPELAE EFKQKFEECQ
RLLLDIPLQT PHKLVDTGRA AKLIQRAEEM KSGLKDFKTF LTNDQVKVTD EENASSGADA
PSASDTTAKQ NPDNTGPALE WDNYDLREDA LDDSVSSSSV HASPLASSPV RKNLFRFGES
TTGFNFSFKS ALSPSKSPAK LNQSGASVGT DEESDVTQEE ERDGQYFEPV VPLPDLVEVS
SGEENEQVVF SHRAKLYRYD KDVGQWKERG IGDIKILQNY DNKQVRIVMR RDQVLKLCAN
HRITPDMTLQ TMKGTERVWV WTACDFADGE RKIEHLAVRF KLQDVADSFK KIFDEAKTAQ
EKDSLITPHV SHLSTPRESP CGKIAIAVLE ETTRERTDLT QGDEVIDTTS EAGETSSTSE
TTPKAVVSPP KFVFGSESVK SIFSSEKSKP FAFGNSSATG SLFGFSFNAP LKNSNSEMTS
RVQSGSEGKV KPDKCELPQN SDIKQSSDGK VKNLSAFSKE NSSTSYTFKT PEKAQEKSKP
EDLPSDNDIL IVYELTPTPE QKALAEKLLL PSTFFCYKNR PGYVSEEEED DEDYEMAVKK
LNGKLYLDDS EKPLEENLAD NDKECVIVWE KKPTVEERAK ADTLKLPPTF FCGVCSDTDE
DNGNGEDFQS ELRKVCEAQK SQNEKVTDRV GIEHIGETEV TNPVGCKSEE PDSDTKHSSS
SPVSGTMDKP VDLSTRKETD MEFPSKGENK PVLFGFGSGT GLSFADLASS NSGDFAFGSK
DKNFQWANTG AAVFGTQTTS KGGEDEDGSD EDVVHNEDIH FEPIVSLPEV EVKSGEEDEE
VLFKERAKLY RWDRDVSQWK ERGIGDIKIL WHTMKKYYRI LMRRDQVFKV CANHVITKAM
ELKPLNVSNN ALVWTASDYA DGEAKVEQLA VRFKTKEMTE SFKKKFEECQ QNIIKLQNGH
TSLAAELSKD TNPVVFFDVC ADGEPLGRII MELFSNIVPQ TAENFRALCT GEKGFGFKNS
IFHRVVPDFI CQGGDITKYN GTGGQSIYGD KFDDENFDLK HTGPGLLSMA NYGQNTNSSQ
FFITLKKAEH LDFKHVVFGF VKDGMDTVRK IESFGSPKGS VSRRICITEC GQL


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