RANBP2 RAN binding protein 2 [Homo sapiens (human)] - Gene

Summary

Official Symbol: RANBP2provided by HGNC
Official Full Name: RAN binding protein 2provided by HGNC
Primary source: HGNC:HGNC:9848
See related: Ensembl:ENSG00000153201 MIM:601181; AllianceGenome:HGNC:9848
Gene type: protein coding
RefSeq status: REVIEWED
Organism: Homo sapiens
Lineage: Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; Homo
Also known as: ANE1; TRP1; TRP2; ADANE; IIAE3; NUP358
Summary: RAN is a small GTP-binding protein of the RAS superfamily that is associated with the nuclear membrane and is thought to control a variety of cellular functions through its interactions with other proteins. This gene encodes a very large RAN-binding protein that immunolocalizes to the nuclear pore complex. The protein is a giant scaffold and mosaic cyclophilin-related nucleoporin implicated in the Ran-GTPase cycle. The encoded protein directly interacts with the E2 enzyme UBC9 and strongly enhances SUMO1 transfer from UBC9 to the SUMO1 target SP100. These findings place sumoylation at the cytoplasmic filaments of the nuclear pore complex and suggest that, for some substrates, modification and nuclear import are linked events. This gene is partially duplicated in a gene cluster that lies in a hot spot for recombination on chromosome 2q. [provided by RefSeq, Jul 2008]
Annotation information: Note: This gene has been reviewed for its involvement in coronavirus biology, and is locus in the vicinity of disease-associated variant(s).
Expression: Ubiquitous expression in testis (RPKM 18.7), thyroid (RPKM 17.9) and 25 other tissues See more
Orthologs: mouse all
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Genomic context

Location:: 2q13

Exon count:: 32

Annotation release	Status	Assembly	Chr	Location
RS_2024_08	current	GRCh38.p14 (GCF_000001405.40)	2	NC_000002.12 (108719482..109842301)
RS_2024_08	current	T2T-CHM13v2.0 (GCF_009914755.1)	2	NC_060926.1 (109180084..110303989)
RS_2024_09	previous assembly	GRCh37.p13 (GCF_000001405.25)	2	NC_000002.11 (109335938..109402265)

Chromosome 2 - NC_000002.12 Genomic Context describing neighboring genes

Genomic regions, transcripts, and products

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Go to reference sequence details

Genomic Sequence:

Go to nucleotide: Graphics FASTA GenBank

Expression

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See details

Project title: HPA RNA-seq normal tissues HPA RNA-seq normal tissues
Description: RNA-seq was performed of tissue samples from 95 human individuals representing 27 different tissues in order to determine tissue-specificity of all protein-coding genes
BioProject: PRJEB4337
Publication: PMID 24309898
Analysis date: Wed Apr 4 07:08:55 2018

Bibliography

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GeneRIFs: Gene References Into Functions

What's a GeneRIF?

Association of RAN and RANBP2 Gene Polymorphisms With Glioma Susceptibility in Chinese Children.
Title: Association of RAN and RANBP2 Gene Polymorphisms With Glioma Susceptibility in Chinese Children.
Intense work-up is required for pediatric COVID-related acute necrotizing encephalopathy with RANBP2 variants.
Title: Intense work-up is required for pediatric COVID-related acute necrotizing encephalopathy with RANBP2 variants.
Role of Nesprin-2 and RanBP2 in BICD2-associated brain developmental disorders.
Title: Role of Nesprin-2 and RanBP2 in BICD2-associated brain developmental disorders.
Aurora B SUMOylation Is Restricted to Centromeres in Early Mitosis and Requires RANBP2.
Title: Aurora B SUMOylation Is Restricted to Centromeres in Early Mitosis and Requires RANBP2.
Outcomes in influenza and RANBP2 mutation-associated acute necrotizing encephalopathy of childhood.
Title: Outcomes in influenza and RANBP2 mutation-associated acute necrotizing encephalopathy of childhood.
Roles of Nucleoporin RanBP2/Nup358 in Acute Necrotizing Encephalopathy Type 1 (ANE1) and Viral Infection.
Title: Roles of Nucleoporin RanBP2/Nup358 in Acute Necrotizing Encephalopathy Type 1 (ANE1) and Viral Infection.
RANBP2 mutation causing autosomal dominant acute necrotizing encephalopathy attenuates its interaction with COX11.
Title: RANBP2 mutation causing autosomal dominant acute necrotizing encephalopathy attenuates its interaction with COX11.
The RanBP2/RanGAP1-SUMO complex gates beta-arrestin2 nuclear entry to regulate the Mdm2-p53 signaling axis.
Title: The RanBP2/RanGAP1-SUMO complex gates β-arrestin2 nuclear entry to regulate the Mdm2-p53 signaling axis.
Acute necrotizing encephalopathy-linked mutations in Nup358 impair interaction of Nup358 with TNRC6/GW182 and miRNA function.
Title: Acute necrotizing encephalopathy-linked mutations in Nup358 impair interaction of Nup358 with TNRC6/GW182 and miRNA function.
Genetic Acute Necrotizing Encephalopathy Associated with RANBP2: Clinical and Therapeutic Implications in Pediatrics.
Title: Genetic Acute Necrotizing Encephalopathy Associated with RANBP2: Clinical and Therapeutic Implications in Pediatrics.

Submit: New GeneRIF Correction See all GeneRIFs (83)

Phenotypes

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Find tests for this gene in the NIH Genetic Testing Registry (GTR)

Review eQTL and phenotype association data in this region using PheGenI

Associated conditions

Description	Tests
Familial acute necrotizing encephalopathy MedGen: C2675556 OMIM: 608033 GeneReviews: Not available	Compare labs

Variation

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See variants in ClinVar

See studies and variants in dbVar

See Variation Viewer (GRCh37.p13)

See Variation Viewer (GRCh38)

HIV-1 interactions

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Replication interactions

Interaction	Pubs
HIV-1 replication, specifically uncoating and nuclear import, requires RANBP2 (NUP358) and KIF5B as shown through siRNA knockdown of each protein	PubMed
shRNA knockdown of RANBP2 renders cells less permissive to HIV-1 WT; HIV-1 is enhanced by RANBP2 [HOWEVER HIV-1 with CA mutations S41A, Q67H, V165I and V172I in combination and/or CA mutation N74D exhibit reduced dependence on RANBP2 for infectivity]	PubMed
Knockdown of RAN binding protein 2 (RANBP2) by siRNA inhibits HIV-1 replication in HeLa-derived TZM-bl cells	PubMed
Knockdown of RAN binding protein 2 (RANBP2) by siRNA inhibits the early stages of HIV-1 replication in 293T cells infected with VSV-G pseudotyped HIV-1	PubMed

Protein interactions

Protein	Gene	Interaction	Pubs
Rev	rev	SiRNA-mediated depletion of RanBP2 impairs biological activities of ectopically expressed HIV-1 Tat and Rev proteins. RanBP2 depletion also inhibits HIV-1 replication by blocking nuclear import of HIV-1 DNA PIC	PubMed
Tat	tat	Interaction of HIV-1 Tat with Nup358 in T-cells is identified by a proteomic strategy based on affinity chromatography	PubMed
	tat	SiRNA-mediated depletion of RanBP2 impairs biological activities of ectopically expressed HIV-1 Tat and Rev proteins. RanBP2 depletion also inhibits HIV-1 replication by blocking nuclear import of HIV-1 DNA PIC	PubMed
capsid	gag	HIV-1 CA relocalizes RANBP2 (NUP358) into the cytoplasm of infected cells	PubMed
	gag	NUP358 is involved in HIV-1 nuclear entry and HIV-1 CA protein is the determinant for NUP358-dependent nuclear import	PubMed
	gag	HIV-1 CA mutants N74D and P90A fail to bind to CPSF6 and cyclophilins (Nup358 and CypA), respectively, and trigger innate sensors, leading to nuclear translocation of NFkappaB and IRF3, production of type 1 IFN and induction of an antiviral state	PubMed
	gag	HIV-1 CA mutant virus N74D infection is inhibited in the Nup358 null cells, but rescued by Nup358 (1-1340) expression	PubMed
	gag	Residues N57, M66, Q67, K70, N74, and T107 in the N-terminal domain of HIV-1 CA are important for the binding to CPSF6. Mutations on these residues lead to the loss or reduction of dependency on TNPO3 and RanBP2	PubMed
	gag	CypA-CA interactions dictate the use of a NUP358/NUP153 dependent nuclear entry pathway	PubMed
	gag	The crystal structure of the C-terminal domain (CTD; residues 3062-3224) of NUP358 reveals that the CTD possesses weak peptidyl-prolyl isomerase activity and mediates a weak association with CA. The V3173W mutant abolishes its association with CA	PubMed
	gag	NUP358 V61M mutation abolishes its interaction with the HIV-1 CA N-terminal domain, while V113F preserves its binding to CA	PubMed
	gag	NUP358 interacts with HIV-1 CA via its cyclophilin domain (residues 3064-3222). Replacement of HIV-1 CA with SIVmac CA renders HIV-1 largely insensitive to NUP358 depletion	PubMed
integrase	gag-pol	Depletion of the nuclear transport factor RANBP2 by RNAi blocks HIV-1 nuclear import and integration efficiency as assayed by the appearance of circular viral DNAs, suggesting HIV-1 IN interacts with RANBP2 in cells	PubMed

Go to the HIV-1, Human Interaction Database

Interactions

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Products	Interactant	Other Gene	Complex	Source	Pubs	Description

General gene information

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Markers

RH16188 (e-PCR)
- UniSTS:91661

SHGC-36406 (e-PCR)
- UniSTS:1088

RH67924 (e-PCR)
- UniSTS:27717

RH18435 (e-PCR)
- UniSTS:67670

RH98799 (e-PCR)
- UniSTS:88151

RH78999 (e-PCR)
- UniSTS:22361

RH79061 (e-PCR)
- UniSTS:82615

Gene Ontology Provided by GOA

Function	Evidence Code	Pubs
contributes_to GTPase activator activity	IBA Inferred from Biological aspect of Ancestor more info
enables RNA binding	IEA Inferred from Electronic Annotation more info
enables SUMO ligase activity	IDA Inferred from Direct Assay more info	PubMed
enables SUMO transferase activity	EXP Inferred from Experiment more info	PubMed
enables metal ion binding	IEA Inferred from Electronic Annotation more info
NOT enables peptidyl-prolyl cis-trans isomerase activity	IDA Inferred from Direct Assay more info	PubMed
enables protein binding	IPI Inferred from Physical Interaction more info	PubMed
enables protein-containing complex binding	IEA Inferred from Electronic Annotation more info
enables small GTPase binding	IPI Inferred from Physical Interaction more info	PubMed

Process	Evidence Code	Pubs
involved_in NLS-bearing protein import into nucleus	IBA Inferred from Biological aspect of Ancestor more info
involved_in NLS-bearing protein import into nucleus	IMP Inferred from Mutant Phenotype more info	PubMed
involved_in centrosome localization	IMP Inferred from Mutant Phenotype more info	PubMed
involved_in mRNA transport	IEA Inferred from Electronic Annotation more info
involved_in nuclear export	EXP Inferred from Experiment more info	PubMed
involved_in nucleocytoplasmic transport	NAS Non-traceable Author Statement more info	PubMed
involved_in protein folding	IEA Inferred from Electronic Annotation more info
involved_in protein peptidyl-prolyl isomerization	IEA Inferred from Electronic Annotation more info
involved_in protein sumoylation	IDA Inferred from Direct Assay more info	PubMed
involved_in protein sumoylation	IEA Inferred from Electronic Annotation more info
involved_in protein sumoylation	TAS Traceable Author Statement more info
involved_in regulation of gluconeogenesis	IEA Inferred from Electronic Annotation more info
involved_in response to amphetamine	IEA Inferred from Electronic Annotation more info

Component	Evidence Code	Pubs
part_of SUMO ligase complex	IPI Inferred from Physical Interaction more info	PubMed
located_in annulate lamellae	IDA Inferred from Direct Assay more info	PubMed
is_active_in cytoplasm	IBA Inferred from Biological aspect of Ancestor more info
located_in cytoplasmic periphery of the nuclear pore complex	IEA Inferred from Electronic Annotation more info
located_in cytosol	TAS Traceable Author Statement more info
located_in intracellular membrane-bounded organelle	IDA Inferred from Direct Assay more info
located_in membrane	HDA more info	PubMed
located_in nuclear envelope	IDA Inferred from Direct Assay more info	PubMed
located_in nuclear envelope	TAS Traceable Author Statement more info
located_in nuclear inclusion body	IDA Inferred from Direct Assay more info	PubMed
located_in nuclear membrane	IDA Inferred from Direct Assay more info	PubMed
part_of nuclear pore	IBA Inferred from Biological aspect of Ancestor more info
part_of nuclear pore	IDA Inferred from Direct Assay more info	PubMed
part_of nuclear pore	NAS Non-traceable Author Statement more info	PubMed
part_of nuclear pore cytoplasmic filaments	IDA Inferred from Direct Assay more info	PubMed
part_of nuclear pore nuclear basket	IDA Inferred from Direct Assay more info	PubMed
located_in nucleoplasm	IDA Inferred from Direct Assay more info

General protein information

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Preferred Names: E3 SUMO-protein ligase RanBP2

Names: 358 kDa nucleoporin; E3 SUMO-protein transferase RanBP2; P270; acute necrotizing encephalopathy 1 (autosomal dominant); nuclear pore complex protein Nup358; nucleoporin 358; nucleoporin Nup358; ran-binding protein 2; transformation-related protein 2

NP_001402800.1

EC 5.2.1.8

NP_001402801.1

EC 5.2.1.8

NP_001402802.1

EC 5.2.1.8

NP_006258.3

EC 5.2.1.8

XP_005264059.1

EC 5.2.1.8

XP_005264064.1

EC 5.2.1.8

XP_011509877.1

EC 5.2.1.8

XP_011509878.1

EC 5.2.1.8

XP_011509880.1

EC 5.2.1.8

XP_016860113.1

EC 5.2.1.8

XP_016860114.1

EC 5.2.1.8

XP_047301323.1

EC 5.2.1.8

XP_054199233.1

EC 5.2.1.8

XP_054199234.1

EC 5.2.1.8

XP_054199235.1

EC 5.2.1.8

XP_054199236.1

EC 5.2.1.8

XP_054199237.1

EC 5.2.1.8

XP_054199238.1

EC 5.2.1.8

XP_054199239.1

EC 5.2.1.8

XP_054199240.1

EC 5.2.1.8

NCBI Reference Sequences (RefSeq)

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RefSeqs maintained independently of Annotated Genomes

These reference sequences exist independently of genome builds. Explain

These reference sequences are curated independently of the genome annotation cycle, so their versions may not match the RefSeq versions in the current genome build. Identify version mismatches by comparing the version of the RefSeq in this section to the one reported in Genomic regions, transcripts, and products above.

Genomic

NG_012210.2 RefSeqGene

Range

5002..71329

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GenBank, FASTA, Sequence Viewer (Graphics)

mRNA and Protein(s)

NM_001415871.1 → NP_001402800.1 E3 SUMO-protein ligase RanBP2 isoform 2

Status: REVIEWED

Source sequence(s)

AC010095
NM_001415872.1 → NP_001402801.1 E3 SUMO-protein ligase RanBP2 isoform 3

Status: REVIEWED

Source sequence(s)

AC010095
NM_001415873.1 → NP_001402802.1 E3 SUMO-protein ligase RanBP2 isoform 4

Status: REVIEWED

Source sequence(s)

AC010095
NM_006267.5 → NP_006258.3 E3 SUMO-protein ligase RanBP2 isoform 1

See identical proteins and their annotated locations for NP_006258.3

Status: REVIEWED

Source sequence(s)

AC010095

Consensus CDS

CCDS2079.1

UniProtKB/Swiss-Prot

P49792, Q13074, Q15280, Q53TE2, Q59FH7

Related

ENSP00000283195.6, ENST00000283195.11

Conserved Domains (12) summary

smart00028
Location:60 → 92

TPR; Tetratricopeptide repeats

COG5171
Location:1951 → 2143

YRB1; Ran GTPase-activating protein (Ran-binding protein) [Intracellular trafficking and secretion]

cd01926
Location:3064 → 3222

cyclophilin_ABH_like; cyclophilin_ABH_like: Cyclophilin A, B and H-like cyclophilin-type peptidylprolyl cis- trans isomerase (PPIase) domain. This family represents the archetypal cystolic cyclophilin similar to human cyclophilins A, B and H. PPIase is an enzyme which ...

cd13177
Location:2027 → 2143

RanBD2_RanBP2-like; Ran-binding protein 2, Ran binding domain repeat 2

cd13178
Location:2925 → 3041

RanBD4_RanBP2-like; Ran-binding protein 2, Ran binding domain repeat 4

cd14684
Location:1186 → 1302

RanBD1_RanBP2-like; Ran-binding protein 2, Ran binding domain repeat 1

cd14685
Location:2324 → 2440

RanBD3_RanBP2-like; Ran-binding protein 2, Ran binding domain repeat 3

sd00025
Location:1419 → 1438

zf-RanBP2; RanBP2-type Zn finger [structural motif]

sd00006
Location:59 → 89

TPR; TPR repeat [structural motif]

pfam00641
Location:1781 → 1809

zf-RanBP; Zn-finger in Ran binding protein and others

pfam12185
Location:2709 → 2768

IR1-M; Nup358/RanBP2 E3 ligase domain

pfam13414
Location:59 → 126

TPR_11; TPR repeat

RefSeqs of Annotated Genomes: GCF_000001405.40-RS_2024_08

The following sections contain reference sequences that belong to a specific genome build. Explain

Reference GRCh38.p14 Primary Assembly

Genomic

NC_000002.12 Reference GRCh38.p14 Primary Assembly

Range

108719482..109842301

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GenBank, FASTA, Sequence Viewer (Graphics)

mRNA and Protein(s)

XM_047445367.1 → XP_047301323.1 E3 SUMO-protein ligase RanBP2 isoform X4
XM_005264002.4 → XP_005264059.1 E3 SUMO-protein ligase RanBP2 isoform X1

Conserved Domains (10) summary

smart00547
Location:1608 → 1632

ZnF_RBZ; Zinc finger domain

COG0457
Location:30 → 126

TPR; Tetratricopeptide (TPR) repeat [General function prediction only]

cd01926
Location:3098 → 3256

cyclophilin_ABH_like; Cyclophilin A, B and H-like cyclophilin-type peptidylprolyl cis- trans isomerase (PPIase) domain. This family represents the archetypal cystolic cyclophilin similar to human cyclophilins A, B and H. PPIase is an enzyme which accelerates protein folding ...

cd13177
Location:2027 → 2143

RanBD2_RanBP2-like; Ran-binding protein 2, Ran binding domain repeat 2

cd13178
Location:2959 → 3075

RanBD4_RanBP2-like; Ran-binding protein 2, Ran binding domain repeat 4

cd14684
Location:1186 → 1302

RanBD1_RanBP2-like; Ran-binding protein 2, Ran binding domain repeat 1

cd14685
Location:2324 → 2440

RanBD3_RanBP2-like; Ran-binding protein 2, Ran binding domain repeat 3

TIGR02917
Location:30 → 291

PEP_TPR_lipo; putative PEP-CTERM system TPR-repeat lipoprotein

sd00025
Location:1419 → 1438

zf-RanBP2; RanBP2-type Zn finger [structural motif]

sd00006
Location:59 → 89

TPR; TPR repeat [structural motif]
XM_011511576.4 → XP_011509878.1 E3 SUMO-protein ligase RanBP2 isoform X3

Conserved Domains (12) summary

smart00028
Location:60 → 92

TPR; Tetratricopeptide repeats

COG5171
Location:1892 → 2084

YRB1; Ran GTPase-activating protein (Ran-binding protein) [Intracellular trafficking and secretion]

cd01926
Location:3039 → 3197

cyclophilin_ABH_like; cyclophilin_ABH_like: Cyclophilin A, B and H-like cyclophilin-type peptidylprolyl cis- trans isomerase (PPIase) domain. This family represents the archetypal cystolic cyclophilin similar to human cyclophilins A, B and H. PPIase is an enzyme which ...

cd13177
Location:1968 → 2084

RanBD2_RanBP2-like; Ran-binding protein 2, Ran binding domain repeat 2

cd13178
Location:2900 → 3016

RanBD4_RanBP2-like; Ran-binding protein 2, Ran binding domain repeat 4

cd14684
Location:1186 → 1302

RanBD1_RanBP2-like; Ran-binding protein 2, Ran binding domain repeat 1

cd14685
Location:2265 → 2381

RanBD3_RanBP2-like; Ran-binding protein 2, Ran binding domain repeat 3

sd00025
Location:1419 → 1438

zf-RanBP2; RanBP2-type Zn finger [structural motif]

sd00006
Location:59 → 89

TPR; TPR repeat [structural motif]

pfam00641
Location:1722 → 1750

zf-RanBP; Zn-finger in Ran binding protein and others

pfam12185
Location:2676 → 2732

IR1-M; Nup358/RanBP2 E3 ligase domain

pfam13414
Location:59 → 126

TPR_11; TPR repeat
XM_005264007.4 → XP_005264064.1 E3 SUMO-protein ligase RanBP2 isoform X5

Conserved Domains (9) summary

smart00028
Location:60 → 92

TPR; Tetratricopeptide repeats

COG5171
Location:975 → 1167

YRB1; Ran GTPase-activating protein (Ran-binding protein) [Intracellular trafficking and secretion]

cd01926
Location:2122 → 2280

cyclophilin_ABH_like; cyclophilin_ABH_like: Cyclophilin A, B and H-like cyclophilin-type peptidylprolyl cis- trans isomerase (PPIase) domain. This family represents the archetypal cystolic cyclophilin similar to human cyclophilins A, B and H. PPIase is an enzyme which ...

cd13177
Location:1051 → 1167

RanBD2_RanBP2-like; Ran-binding protein 2, Ran binding domain repeat 2

cd13178
Location:1983 → 2099

RanBD4_RanBP2-like; Ran-binding protein 2, Ran binding domain repeat 4

cd14685
Location:1348 → 1464

RanBD3_RanBP2-like; Ran-binding protein 2, Ran binding domain repeat 3

sd00006
Location:59 → 89

TPR; TPR repeat [structural motif]

pfam12185
Location:1759 → 1815

IR1-M; Nup358/RanBP2 E3 ligase domain

pfam13414
Location:59 → 126

TPR_11; TPR repeat
XM_011511575.3 → XP_011509877.1 E3 SUMO-protein ligase RanBP2 isoform X2

Conserved Domains (12) summary

smart00028
Location:59 → 91

TPR; Tetratricopeptide repeats

COG5171
Location:1950 → 2142

YRB1; Ran GTPase-activating protein (Ran-binding protein) [Intracellular trafficking and secretion]

cd01926
Location:3097 → 3255

cyclophilin_ABH_like; cyclophilin_ABH_like: Cyclophilin A, B and H-like cyclophilin-type peptidylprolyl cis- trans isomerase (PPIase) domain. This family represents the archetypal cystolic cyclophilin similar to human cyclophilins A, B and H. PPIase is an enzyme which ...

cd13177
Location:2026 → 2142

RanBD2_RanBP2-like; Ran-binding protein 2, Ran binding domain repeat 2

cd13178
Location:2958 → 3074

RanBD4_RanBP2-like; Ran-binding protein 2, Ran binding domain repeat 4

cd14684
Location:1185 → 1301

RanBD1_RanBP2-like; Ran-binding protein 2, Ran binding domain repeat 1

cd14685
Location:2323 → 2439

RanBD3_RanBP2-like; Ran-binding protein 2, Ran binding domain repeat 3

sd00025
Location:1418 → 1437

zf-RanBP2; RanBP2-type Zn finger [structural motif]

sd00006
Location:58 → 88

TPR; TPR repeat [structural motif]

pfam00641
Location:1780 → 1808

zf-RanBP; Zn-finger in Ran binding protein and others

pfam12185
Location:2734 → 2790

IR1-M; Nup358/RanBP2 E3 ligase domain

pfam13414
Location:58 → 125

TPR_11; TPR repeat
XM_011511578.3 → XP_011509880.1 E3 SUMO-protein ligase RanBP2 isoform X6

Conserved Domains (9) summary

smart00028
Location:59 → 91

TPR; Tetratricopeptide repeats

COG5171
Location:974 → 1166

YRB1; Ran GTPase-activating protein (Ran-binding protein) [Intracellular trafficking and secretion]

cd01926
Location:2121 → 2279

cyclophilin_ABH_like; cyclophilin_ABH_like: Cyclophilin A, B and H-like cyclophilin-type peptidylprolyl cis- trans isomerase (PPIase) domain. This family represents the archetypal cystolic cyclophilin similar to human cyclophilins A, B and H. PPIase is an enzyme which ...

cd13177
Location:1050 → 1166

RanBD2_RanBP2-like; Ran-binding protein 2, Ran binding domain repeat 2

cd13178
Location:1982 → 2098

RanBD4_RanBP2-like; Ran-binding protein 2, Ran binding domain repeat 4

cd14685
Location:1347 → 1463

RanBD3_RanBP2-like; Ran-binding protein 2, Ran binding domain repeat 3

sd00006
Location:58 → 88

TPR; TPR repeat [structural motif]

pfam12185
Location:1758 → 1814

IR1-M; Nup358/RanBP2 E3 ligase domain

pfam13414
Location:58 → 125

TPR_11; TPR repeat
XM_017004624.3 → XP_016860113.1 E3 SUMO-protein ligase RanBP2 isoform X7
XM_017004625.2 → XP_016860114.1 E3 SUMO-protein ligase RanBP2 isoform X8