HUMAN:RBP2

Species (Taxon ID)	Homo sapiens (Human). (9606)
Gene Name(s)	RANBP2 (synonyms: NUP358)
Protein Name(s)	E3 SUMO-protein ligase RanBP2 358 kDa nucleoporin Nuclear pore complex protein Nup358 Nucleoporin Nup358 Ran-binding protein 2 RanBP2 p270
External Links
UniProt	P49792
EMBL	L41840 D42063 AC010095 AB209483 U19248
CCDS	CCDS2079.1
PIR	S58884
RefSeq	NP_006258.3
UniGene	Hs.199561 Hs.715056
PDB	1RRP 1XKE 1Z5S 3UIN 3UIO 3UIP 4GA0 4I9Y 4L6E 4LQW 5CLL 5CLQ
PDBsum	1RRP 1XKE 1Z5S 3UIN 3UIO 3UIP 4GA0 4I9Y 4L6E 4LQW 5CLL 5CLQ
ProteinModelPortal	P49792
SMR	P49792
BioGrid	111839
DIP	DIP-37654N
IntAct	P49792
MINT	MINT-191403
STRING	9606.ENSP00000283195
TCDB	1.I.1.1.3
iPTMnet	P49792
PhosphoSite	P49792
SwissPalm	P49792
BioMuta	RANBP2
DMDM	83305554
OGP	P49792
EPD	P49792
MaxQB	P49792
PaxDb	P49792
PeptideAtlas	P49792
PRIDE	P49792
Ensembl	ENST00000283195
GeneID	5903
KEGG	hsa:5903
UCSC	uc002tem.4
CTD	5903
GeneCards	RANBP2
H-InvDB	HIX0002358
HGNC	HGNC:9848
HPA	CAB034063 HPA018437 HPA023960 HPA049497 HPA051675
MalaCards	RANBP2
MIM	601181 608033
neXtProt	NX_P49792
Orphanet	263524 88619 178342
PharmGKB	PA34209
eggNOG	KOG0864 KOG0865 COG0652 COG5171
GeneTree	ENSGT00760000119119
HOGENOM	HOG000089994
HOVERGEN	HBG092361
InParanoid	P49792
KO	K12172
OMA	PGKQNQT
OrthoDB	EOG7X0VG5
PhylomeDB	P49792
TreeFam	TF314797
Reactome	R-HSA-1169408 R-HSA-165054 R-HSA-168276 R-HSA-168325 R-HSA-170822 R-HSA-180746 R-HSA-180910 R-HSA-2467813 R-HSA-2500257 R-HSA-3108214 R-HSA-3301854 R-HSA-3371453 R-HSA-4570464 R-HSA-4615885 R-HSA-5578749 R-HSA-5663220 R-HSA-6784531 R-HSA-68877
UniPathway	UPA00886
ChiTaRS	RANBP2
EvolutionaryTrace	P49792
GeneWiki	RANBP2
GenomeRNAi	5903
NextBio	22964
PRO	PR:P49792
Proteomes	UP000005640
Bgee	P49792
CleanEx	HS_RANBP2
ExpressionAtlas	P49792
Genevisible	P49792
GO	GO:1990723 GO:0005829 GO:0016020 GO:0005739 GO:0005635 GO:0042405 GO:0031965 GO:0005643 GO:0044614 GO:0044615 GO:0016874 GO:0003755 GO:0008536 GO:0003723 GO:0008270 GO:0005975 GO:0044267 GO:0034605 GO:0019221 GO:0010467 GO:0031047 GO:0015758 GO:0008645 GO:0000278 GO:0007077 GO:0019048 GO:0019054 GO:0051028 GO:0033132 GO:0006607 GO:0043687 GO:0006457 GO:0016925 GO:1900034 GO:0090526 GO:0010827 GO:0001975 GO:0007264 GO:0044281 GO:0055085 GO:0008033 GO:0019058 GO:0016032 GO:0019083
Gene3D	1.25.40.10 2.30.29.30 2.40.100.10
InterPro	IPR029000 IPR020892 IPR002130 IPR022011 IPR011993 IPR000156 IPR013026 IPR011990 IPR019734 IPR001876
Pfam	PF12185 PF00160 PF00638 PF13181 PF00641
PRINTS	PR00153
SMART	SM00160 SM00547
SUPFAM	SSF48452 SSF50729 SSF50891 SSF90209
PROSITE	PS00170 PS50072 PS50196 PS50005 PS50293 PS01358 PS50199

Annotations

Qualifier	GO ID	GO term name	Reference	ECO ID	ECO term name	with/from	Aspect	Notes	Status
involved_in	GO:0051642	centrosome localization	PMID:20386726^[1]	ECO:0000315	mutant phenotype evidence used in manual assertion		P	Seeded From UniProt	complete
part_of	GO:0005643	nuclear pore	PMID:20386726^[1]	ECO:0000314	direct assay evidence used in manual assertion		C	Seeded From UniProt	complete
part_of	GO:0005642	annulate lamellae	PMID:20386726^[1]	ECO:0000314	direct assay evidence used in manual assertion		C	Seeded From UniProt	complete
part_of	GO:0005635	nuclear envelope	PMID:20386726^[1]	ECO:0000314	direct assay evidence used in manual assertion		C	Seeded From UniProt	complete
enables	GO:0008536	Ran GTPase binding	PMID:7603572^[2]	ECO:0000353	physical interaction evidence used in manual assertion	UniProtKB:P62826	F	Seeded From UniProt	complete
part_of	GO:0016020	membrane	PMID:19946888^[3]	ECO:0007005	high throughput direct assay evidence used in manual assertion		C	Seeded From UniProt	complete
NOT\|enables	GO:0016018	cyclosporin A binding	PMID:20676357^[4]	ECO:0000314	direct assay evidence used in manual assertion		F	Seeded From UniProt	complete
NOT\|enables	GO:0003755	peptidyl-prolyl cis-trans isomerase activity	PMID:20676357^[4]	ECO:0000314	direct assay evidence used in manual assertion		F	Seeded From UniProt	complete
involved_in	GO:0006607	NLS-bearing protein import into nucleus	PMID:7603572^[2]	ECO:0000315	mutant phenotype evidence used in manual assertion		P	Seeded From UniProt	complete
part_of	GO:0044614	nuclear pore cytoplasmic filaments	PMID:7603572^[2]	ECO:0000314	direct assay evidence used in manual assertion		C	Seeded From UniProt	complete
part_of	GO:0044615	nuclear pore nuclear basket	PMID:11839768^[5]	ECO:0000314	direct assay evidence used in manual assertion		C	Seeded From UniProt	complete
part_of	GO:0042405	nuclear inclusion body	PMID:11839768^[5]	ECO:0000314	direct assay evidence used in manual assertion		C	Seeded From UniProt	complete
part_of	GO:0031965	nuclear membrane	PMID:11839768^[5]	ECO:0000314	direct assay evidence used in manual assertion		C	Seeded From UniProt	complete
involved_in	GO:0016925	protein sumoylation	PMID:17264123^[6]	ECO:0000314	direct assay evidence used in manual assertion		P	Seeded From UniProt	complete
involved_in	GO:0016925	protein sumoylation	PMID:22155184^[7]	ECO:0000314	direct assay evidence used in manual assertion		P	Seeded From UniProt	complete
part_of	GO:0005643	nuclear pore	PMID:17098863^[8]	ECO:0000314	direct assay evidence used in manual assertion		C	Seeded From UniProt	complete
enables	GO:0008536	Ran GTPase binding	PMID:21873635^[9]	ECO:0000318	biological aspect of ancestor evidence used in manual assertion	PANTHER:PTN000566604 SGD:S000002409 SGD:S000004327 UniProtKB:P49792 UniProtKB:Q9H6Z4	F	Seeded From UniProt	complete
involved_in	GO:0006607	NLS-bearing protein import into nucleus	PMID:21873635^[9]	ECO:0000318	biological aspect of ancestor evidence used in manual assertion	PANTHER:PTN002751291 UniProtKB:P49792	P	Seeded From UniProt	complete
part_of	GO:0005737	cytoplasm	PMID:21873635^[9]	ECO:0000318	biological aspect of ancestor evidence used in manual assertion	MGI:MGI:96269 PANTHER:PTN000566604 RGD:1310521 SGD:S000002409 UniProtKB:P43487	C	Seeded From UniProt	complete
part_of	GO:0005643	nuclear pore	PMID:21873635^[9]	ECO:0000318	biological aspect of ancestor evidence used in manual assertion	MGI:MGI:1351502 PANTHER:PTN000566604 PomBase:SPCC18B5.07c RGD:1560047 RGD:3191 UniProtKB:P49792 WB:WBGene00003795	C	Seeded From UniProt	complete
part_of	GO:0005643	nuclear pore	PMID:21873635^[9]	ECO:0000318	biological aspect of ancestor evidence used in manual assertion	MGI:MGI:1351502 PANTHER:PTN000566604 PomBase:SPCC18B5.07c RGD:1560047 RGD:3191 SGD:S000001325 UniProtKB:P49792 WB:WBGene00003795	C	Seeded From UniProt	complete
part_of	GO:0005634	nucleus	PMID:21873635^[9]	ECO:0000318	biological aspect of ancestor evidence used in manual assertion	PANTHER:PTN000566604 PomBase:SPBC365.13c RGD:1310521 SGD:S000001325 SGD:S000002409 TAIR:locus:2018204 UniProtKB:Q9H6Z4	C	Seeded From UniProt	complete
contributes_to	GO:0005096	GTPase activator activity	PMID:21873635^[9]	ECO:0000318	biological aspect of ancestor evidence used in manual assertion	PANTHER:PTN000566604 PomBase:SPBC1773.07c	F	Seeded From UniProt	complete
enables	GO:0019789	SUMO transferase activity	PMID:16688858^[10]	ECO:0000269	experimental evidence used in manual assertion		F	Seeded From UniProt	complete
enables	GO:0019789	SUMO transferase activity	PMID:15608651^[11]	ECO:0000269	experimental evidence used in manual assertion		F	Seeded From UniProt	complete
enables	GO:0019789	SUMO transferase activity	PMID:15378033^[12]	ECO:0000269	experimental evidence used in manual assertion		F	Seeded From UniProt	complete
enables	GO:0019789	SUMO transferase activity	PMID:11792325^[13]	ECO:0000269	experimental evidence used in manual assertion		F	Seeded From UniProt	complete
involved_in	GO:0043547	positive regulation of GTPase activity	GO_REF:0000108	ECO:0000364	evidence based on logical inference from manual annotation used in automatic assertion	GO:0005096	P	Seeded From UniProt	complete
part_of	GO:0043657	host cell	GO_REF:0000108	ECO:0000364	evidence based on logical inference from manual annotation used in automatic assertion	GO:0075733	C	Seeded From UniProt	complete
part_of	GO:1990723	cytoplasmic periphery of the nuclear pore complex	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:M0R3M4 ensembl:ENSRNOP00000063941	C	Seeded From UniProt	complete
enables	GO:0044877	protein-containing complex binding	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:M0R3M4 ensembl:ENSRNOP00000063941	F	Seeded From UniProt	complete
part_of	GO:0044614	nuclear pore cytoplasmic filaments	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:M0R3M4 ensembl:ENSRNOP00000063941	C	Seeded From UniProt	complete
part_of	GO:0005643	nuclear pore	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:M0R3M4 ensembl:ENSRNOP00000063941	C	Seeded From UniProt	complete
involved_in	GO:0001975	response to amphetamine	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:M0R3M4 ensembl:ENSRNOP00000063941	P	Seeded From UniProt	complete
involved_in	GO:0033133	positive regulation of glucokinase activity	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:Q9ERU9 ensembl:ENSMUSP00000003310	P	Seeded From UniProt	complete
involved_in	GO:0006111	regulation of gluconeogenesis	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:Q9ERU9 ensembl:ENSMUSP00000003310	P	Seeded From UniProt	complete
part_of	GO:0005739	mitochondrion	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:Q9ERU9 ensembl:ENSMUSP00000003310	C	Seeded From UniProt	complete
involved_in	GO:0000413	protein peptidyl-prolyl isomerization	GO_REF:0000002	ECO:0000256	match to sequence model evidence used in automatic assertion	InterPro:IPR002130	P	Seeded From UniProt	complete
involved_in	GO:0006457	protein folding	GO_REF:0000002	ECO:0000256	match to sequence model evidence used in automatic assertion	InterPro:IPR020892	P	Seeded From UniProt	complete
	GO:0005635	nuclear envelope	PMID:25294810^[14]	ECO:0000314			C	Figure 2B shows immunostaining of RanBP2 in the nuclear envelope.	complete CACAO 11505
involved_in	GO:0046907	intracellular transport	GO_REF:0000002	ECO:0000256	match to sequence model evidence used in automatic assertion	InterPro:IPR000156	P	Seeded From UniProt	complete
involved_in	GO:1900034	regulation of cellular response to heat	Reactome:R-HSA-3371453	ECO:0000304	author statement supported by traceable reference used in manual assertion		P	Seeded From UniProt	complete
involved_in	GO:0075733	intracellular transport of virus	Reactome:R-HSA-1176059	ECO:0000304	author statement supported by traceable reference used in manual assertion		P	Seeded From UniProt	complete
involved_in	GO:0060964	regulation of gene silencing by miRNA	Reactome:R-HSA-5578749	ECO:0000304	author statement supported by traceable reference used in manual assertion		P	Seeded From UniProt	complete
involved_in	GO:0019083	viral transcription	Reactome:R-HSA-168325	ECO:0000304	author statement supported by traceable reference used in manual assertion		P	Seeded From UniProt	complete
involved_in	GO:0016925	protein sumoylation	Reactome:R-HSA-4655355	ECO:0000304	author statement supported by traceable reference used in manual assertion		P	Seeded From UniProt	complete
involved_in	GO:0016032	viral process	Reactome:R-HSA-162599	ECO:0000304	author statement supported by traceable reference used in manual assertion		P	Seeded From UniProt	complete
involved_in	GO:0006409	tRNA export from nucleus	Reactome:R-HSA-6783483	ECO:0000304	author statement supported by traceable reference used in manual assertion		P	Seeded From UniProt	complete
involved_in	GO:0006406	mRNA export from nucleus	Reactome:R-HSA-75098 Reactome:R-HSA-75097 Reactome:R-HSA-75096	ECO:0000304	author statement supported by traceable reference used in manual assertion		P	Seeded From UniProt	complete
involved_in	GO:0006110	regulation of glycolytic process	Reactome:R-HSA-170822	ECO:0000304	author statement supported by traceable reference used in manual assertion		P	Seeded From UniProt	complete
part_of	GO:0005829	cytosol	Reactome:R-HSA-75098 Reactome:R-HSA-75097 Reactome:R-HSA-75096 Reactome:R-HSA-6783483 Reactome:R-HSA-5666169 Reactome:R-HSA-5666160 Reactome:R-HSA-5666129 Reactome:R-HSA-5578744 Reactome:R-HSA-5252041 Reactome:R-HSA-5228523 Reactome:R-HSA-5228508 Reactome:R-HSA-4615987 Reactome:R-HSA-4615872 Reactome:R-HSA-4570493 Reactome:R-HSA-4551679 Reactome:R-HSA-4551649 Reactome:R-HSA-375302 Reactome:R-HSA-3000411 Reactome:R-HSA-3000399 Reactome:R-HSA-3000348 Reactome:R-HSA-2990882 Reactome:R-HSA-2990880 Reactome:R-HSA-2484822 Reactome:R-HSA-2468287 Reactome:R-HSA-2467811 Reactome:R-HSA-2467809 Reactome:R-HSA-192925 Reactome:R-HSA-192627 Reactome:R-HSA-180622 Reactome:R-HSA-170796 Reactome:R-HSA-165047 Reactome:R-HSA-165043 Reactome:R-HSA-1638821 Reactome:R-HSA-1638803 Reactome:R-HSA-141439 Reactome:R-HSA-141431 Reactome:R-HSA-141422 Reactome:R-HSA-141409 Reactome:R-HSA-1176059	ECO:0000304	author statement supported by traceable reference used in manual assertion		C	Seeded From UniProt	complete
part_of	GO:0005635	nuclear envelope	Reactome:R-HSA-4655355 Reactome:R-HSA-4551679 Reactome:R-HSA-4551649	ECO:0000304	author statement supported by traceable reference used in manual assertion		C	Seeded From UniProt	complete
part_of	GO:0005634	nucleus	GO_REF:0000037 GO_REF:0000039	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0539 UniProtKB-SubCell:SL-0191	C	Seeded From UniProt	complete
part_of	GO:0016020	membrane	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0472	C	Seeded From UniProt	complete
involved_in	GO:0015031	protein transport	GO_REF:0000037 GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0653 UniProtKB-KW:KW-0811	P	Seeded From UniProt	complete
involved_in	GO:0051028	mRNA transport	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0509	P	Seeded From UniProt	complete
enables	GO:0046872	metal ion binding	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0479	F	Seeded From UniProt	complete
enables	GO:0003723	RNA binding	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0694	F	Seeded From UniProt	complete
enables	GO:0016740	transferase activity	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0808	F	Seeded From UniProt	complete
part_of	GO:0005643	nuclear pore	GO_REF:0000037 GO_REF:0000039	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0906 UniProtKB-SubCell:SL-0185	C	Seeded From UniProt	complete
part_of	GO:0005635	nuclear envelope	GO_REF:0000039	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-SubCell:SL-0178	C	Seeded From UniProt	complete
part_of	GO:0031965	nuclear membrane	GO_REF:0000039	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-SubCell:SL-0182	C	Seeded From UniProt	complete
involved_in	GO:0016925	protein sumoylation	GO_REF:0000041	ECO:0000322	imported manually asserted information used in automatic assertion	UniPathway:UPA00886	P	Seeded From UniProt	complete
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Notes

References

See Help:References for how to manage references in GONUTS.

↑ ^1.0 ^1.1 ^1.2 ^1.3 Splinter, D et al. (2010) Bicaudal D2, dynein, and kinesin-1 associate with nuclear pore complexes and regulate centrosome and nuclear positioning during mitotic entry. PLoS Biol. 8 e1000350 PubMed GONUTS page
↑ ^2.0 ^2.1 ^2.2 Yokoyama, N et al. (1995) A giant nucleopore protein that binds Ran/TC4. Nature 376 184-8 PubMed GONUTS page
↑ Ghosh, D et al. (2010) Defining the membrane proteome of NK cells. J Mass Spectrom 45 1-25 PubMed GONUTS page
↑ ^4.0 ^4.1 Davis, TL et al. (2010) Structural and biochemical characterization of the human cyclophilin family of peptidyl-prolyl isomerases. PLoS Biol. 8 e1000439 PubMed GONUTS page
↑ ^5.0 ^5.1 ^5.2 Frosst, P et al. (2002) Tpr is localized within the nuclear basket of the pore complex and has a role in nuclear protein export. J. Cell Biol. 156 617-30 PubMed GONUTS page
↑ Hamard, PJ et al. (2007) Sumoylation delays the ATF7 transcription factor subcellular localization and inhibits its transcriptional activity. Nucleic Acids Res. 35 1134-44 PubMed GONUTS page
↑ Satow, R et al. (2012) β-catenin inhibits promyelocytic leukemia protein tumor suppressor function in colorectal cancer cells. Gastroenterology 142 572-81 PubMed GONUTS page
↑ Rasala, BA et al. (2006) ELYS is a dual nucleoporin/kinetochore protein required for nuclear pore assembly and proper cell division. Proc. Natl. Acad. Sci. U.S.A. 103 17801-6 PubMed GONUTS page
↑ ^9.0 ^9.1 ^9.2 ^9.3 ^9.4 ^9.5 ^9.6 Gaudet, P et al. (2011) Phylogenetic-based propagation of functional annotations within the Gene Ontology consortium. Brief. Bioinformatics 12 449-62 PubMed GONUTS page
↑ Saitoh, N et al. (2006) In situ SUMOylation analysis reveals a modulatory role of RanBP2 in the nuclear rim and PML bodies. Exp. Cell Res. 312 1418-30 PubMed GONUTS page
↑ Tatham, MH et al. (2005) Unique binding interactions among Ubc9, SUMO and RanBP2 reveal a mechanism for SUMO paralog selection. Nat. Struct. Mol. Biol. 12 67-74 PubMed GONUTS page
↑ Pichler, A et al. (2004) The RanBP2 SUMO E3 ligase is neither HECT- nor RING-type. Nat. Struct. Mol. Biol. 11 984-91 PubMed GONUTS page
↑ Pichler, A et al. (2002) The nucleoporin RanBP2 has SUMO1 E3 ligase activity. Cell 108 109-20 PubMed GONUTS page
↑ Kazyken, D et al. (2014) The nuclear import of ribosomal proteins is regulated by mTOR. Oncotarget 5 9577-93 PubMed GONUTS page

[PMID:20386726-1] 1.0 ^1.1 ^1.2 ^1.3 Splinter, D et al. (2010) Bicaudal D2, dynein, and kinesin-1 associate with nuclear pore complexes and regulate centrosome and nuclear positioning during mitotic entry. PLoS Biol. 8 e1000350 PubMed GONUTS page

[PMID:7603572-2] 2.0 ^2.1 ^2.2 Yokoyama, N et al. (1995) A giant nucleopore protein that binds Ran/TC4. Nature 376 184-8 PubMed GONUTS page

[PMID:19946888-3] Ghosh, D et al. (2010) Defining the membrane proteome of NK cells. J Mass Spectrom 45 1-25 PubMed GONUTS page

[PMID:20676357-4] 4.0 ^4.1 Davis, TL et al. (2010) Structural and biochemical characterization of the human cyclophilin family of peptidyl-prolyl isomerases. PLoS Biol. 8 e1000439 PubMed GONUTS page

[PMID:11839768-5] 5.0 ^5.1 ^5.2 Frosst, P et al. (2002) Tpr is localized within the nuclear basket of the pore complex and has a role in nuclear protein export. J. Cell Biol. 156 617-30 PubMed GONUTS page

[PMID:17264123-6] Hamard, PJ et al. (2007) Sumoylation delays the ATF7 transcription factor subcellular localization and inhibits its transcriptional activity. Nucleic Acids Res. 35 1134-44 PubMed GONUTS page

[PMID:22155184-7] Satow, R et al. (2012) β-catenin inhibits promyelocytic leukemia protein tumor suppressor function in colorectal cancer cells. Gastroenterology 142 572-81 PubMed GONUTS page

[PMID:17098863-8] Rasala, BA et al. (2006) ELYS is a dual nucleoporin/kinetochore protein required for nuclear pore assembly and proper cell division. Proc. Natl. Acad. Sci. U.S.A. 103 17801-6 PubMed GONUTS page

[PMID:21873635-9] 9.0 ^9.1 ^9.2 ^9.3 ^9.4 ^9.5 ^9.6 Gaudet, P et al. (2011) Phylogenetic-based propagation of functional annotations within the Gene Ontology consortium. Brief. Bioinformatics 12 449-62 PubMed GONUTS page

[PMID:16688858-10] Saitoh, N et al. (2006) In situ SUMOylation analysis reveals a modulatory role of RanBP2 in the nuclear rim and PML bodies. Exp. Cell Res. 312 1418-30 PubMed GONUTS page

[PMID:15608651-11] Tatham, MH et al. (2005) Unique binding interactions among Ubc9, SUMO and RanBP2 reveal a mechanism for SUMO paralog selection. Nat. Struct. Mol. Biol. 12 67-74 PubMed GONUTS page

[PMID:15378033-12] Pichler, A et al. (2004) The RanBP2 SUMO E3 ligase is neither HECT- nor RING-type. Nat. Struct. Mol. Biol. 11 984-91 PubMed GONUTS page

[PMID:11792325-13] Pichler, A et al. (2002) The nucleoporin RanBP2 has SUMO1 E3 ligase activity. Cell 108 109-20 PubMed GONUTS page

[PMID:25294810-14] Kazyken, D et al. (2014) The nuclear import of ribosomal proteins is regulated by mTOR. Oncotarget 5 9577-93 PubMed GONUTS page

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HUMAN:RBP2

Contents

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