Ranbp2 RAN binding protein 2 [Mus musculus (house mouse)] - Gene

Summary

Official Symbol: Ranbp2provided by MGI
Official Full Name: RAN binding protein 2provided by MGI
Primary source: MGI:MGI:894323
See related: Ensembl:ENSMUSG00000003226 AllianceGenome:MGI:894323
Gene type: protein coding
RefSeq status: VALIDATED
Organism: Mus musculus
Lineage: Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae; Murinae; Mus; Mus
Also known as: NUP358; A430087B05Rik
Summary: Enables SUMO transferase activity. Involved in nuclear export. Acts upstream of or within positive regulation of glucokinase activity and regulation of gluconeogenesis. Predicted to be located in annulate lamellae; cytoplasmic periphery of the nuclear pore complex; and nucleus. Predicted to be part of SUMO ligase complex; nuclear pore cytoplasmic filaments; and nuclear pore nuclear basket. Predicted to be active in cytoplasm. Is expressed in several structures, including alimentary system; eye; genitourinary system; hemolymphoid system; and nervous system. Human ortholog(s) of this gene implicated in brain disease and inflammatory myofibroblastic tumor. Orthologous to several human genes including RANBP2 (RAN binding protein 2). [provided by Alliance of Genome Resources, Dec 2024]
Expression: Ubiquitous expression in liver E14 (RPKM 9.3), placenta adult (RPKM 8.8) and 26 other tissues See more
Orthologs: human all
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Genomic context

Location:: 10 B4; 10 29.34 cM

Exon count:: 29

Annotation release	Status	Assembly	Chr	Location
RS_2024_02	current	GRCm39 (GCF_000001635.27)	10	NC_000076.7 (58282674..58329977)
108.20200622	previous assembly	GRCm38.p6 (GCF_000001635.26)	10	NC_000076.6 (58446852..58494155)

Chromosome 10 - NC_000076.7 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

Bibliography

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GeneRIFs: Gene References Into Functions

What's a GeneRIF?

Proteostatic Remodeling of Small Heat Shock Chaperones horizontal line Crystallins by Ran-Binding Protein 2 horizontal line and the Peptidyl-Prolyl cis-trans Isomerase and Chaperone Activities of Its Cyclophilin Domain.
Title: Proteostatic Remodeling of Small Heat Shock Chaperones─Crystallins by Ran-Binding Protein 2─and the Peptidyl-Prolyl cis-trans Isomerase and Chaperone Activities of Its Cyclophilin Domain.
Nucleoporin Nup358 drives the differentiation of myeloid-biased multipotent progenitors by modulating HDAC3 nuclear translocation.
Title: Nucleoporin Nup358 drives the differentiation of myeloid-biased multipotent progenitors by modulating HDAC3 nuclear translocation.
T-cell receptor (TCR) signaling promotes the assembly of RanBP2/RanGAP1-SUMO1/Ubc9 nuclear pore subcomplex via PKC-theta-mediated phosphorylation of RanGAP1.
Title: T-cell receptor (TCR) signaling promotes the assembly of RanBP2/RanGAP1-SUMO1/Ubc9 nuclear pore subcomplex via PKC-θ-mediated phosphorylation of RanGAP1.
Ankyrin-G induces nucleoporin Nup358 to associate with the axon initial segment of neurons.
Title: Ankyrin-G induces nucleoporin Nup358 to associate with the axon initial segment of neurons.
data support that Ran GTPase-dependent and independent and moonlighting roles of Ranbp2 or domains thereof and ubc9 control selectively age-dependent, neural-type and mitochondrial functions
Title: Impairments in age-dependent ubiquitin proteostasis and structural integrity of selective neurons by uncoupling Ran GTPase from the Ran-binding domain 3 of Ranbp2 and identification of novel mitochondrial isoforms of ubiquitin-conjugating enzyme E2I (ubc9) and Ranbp2.
Ranbp2 is a major regulator of Acc1 and Mmp28 expressions and that Acc1 and Mmp28 may play a central role in neuroimmunity by controlling non-autonomous (paracrine) cell signaling between retinal ganglion neurons and microglia upon loss of Ranbp2 in retinal ganglion neurons.
Title: Microglial activation in an amyotrophic lateral sclerosis-like model caused by Ranbp2 loss and nucleocytoplasmic transport impairment in retinal ganglion neurons.
These results demonstrate a function of RanBP2-mediated SUMOylation of SHP in maintaining bile acids (BA) homoeostasis and protecting from the BA hepatotoxicity.
Title: Critical role of RanBP2-mediated SUMOylation of Small Heterodimer Partner in maintaining bile acid homeostasis.
results demonstrate that Ranbp2 controls nucleocytoplasmic, chemokine and metalloproteinase 28 signaling, and proteostasis of substrates that are crucial to motoneuronal homeostasis and whose impairments by loss of Ranbp2 drive ALS-like syndromes
Title: Loss of Ranbp2 in motoneurons causes disruption of nucleocytoplasmic and chemokine signaling, proteostasis of hnRNPH3 and Mmp28, and development of amyotrophic lateral sclerosis-like syndromes.
RanBP2 expression was regulated by Zap70.
Title: Zap70 and downstream RanBP2 are required for the exact timing of the meiotic cell cycle in oocytes.
Data (including data from studies in transgenic/knockout mice) suggest that Ranbp2 in photoreceptor neurons participates in coupling of photoreceptor degeneration (neural dysmorphology) and apoptosis (neural death) caused by toxic exposure to light.
Title: Uncoupling phototoxicity-elicited neural dysmorphology and death by insidious function and selective impairment of Ran-binding protein 2 (Ranbp2).

Submit: New GeneRIF Correction See all GeneRIFs (29)

Variation

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Alleles

Alleles of this type are documented at Mouse Genome Informatics (MGI)

Endonuclease-mediated (3)
Gene trapped (2) 1 citation
Targeted (5) 1 citation

Interactions

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Products	Interactant	Other Gene	Complex	Source	Pubs	Description

General gene information

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Markers

RH136086 (e-PCR)
- UniSTS:210081

Ranbp2 (e-PCR), detects polymorphism
- UniSTS:256955

Gene Ontology Provided by MGI

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	IEA Inferred from Electronic Annotation more info
enables SUMO ligase activity	ISO Inferred from Sequence Orthology more info
enables SUMO transferase activity	EXP Inferred from Experiment more info	PubMed
enables SUMO transferase activity	ISO Inferred from Sequence Orthology more info
enables kinase activator activity	IDA Inferred from Direct Assay more info	PubMed
enables metal ion binding	IEA Inferred from Electronic Annotation more info
enables peptidyl-prolyl cis-trans isomerase activity	IEA Inferred from Electronic Annotation more info
enables protein binding	IPI Inferred from Physical Interaction more info	PubMed
enables protein-containing complex binding	IEA Inferred from Electronic Annotation more info
enables protein-containing complex binding	ISO Inferred from Sequence Orthology more info
enables small GTPase binding	IEA Inferred from Electronic Annotation more info

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	IEA Inferred from Electronic Annotation more info
involved_in centrosome localization	IEA Inferred from Electronic Annotation more info
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 sumoylation	IEA Inferred from Electronic Annotation more info
involved_in protein sumoylation	ISO Inferred from Sequence Orthology more info
involved_in protein sumoylation	ISS Inferred from Sequence or Structural Similarity more info
acts_upstream_of_or_within regulation of gluconeogenesis	IMP Inferred from Mutant Phenotype more info	PubMed
involved_in response to amphetamine	IEA Inferred from Electronic Annotation more info

Component	Evidence Code	Pubs
part_of SUMO ligase complex	ISO Inferred from Sequence Orthology more info
located_in annulate lamellae	ISO Inferred from Sequence Orthology more info
located_in annulate lamellae	ISS Inferred from Sequence or Structural Similarity more info
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 cytoplasmic periphery of the nuclear pore complex	ISO Inferred from Sequence Orthology more info
located_in intracellular membrane-bounded organelle	ISO Inferred from Sequence Orthology more info
located_in nuclear envelope	ISO Inferred from Sequence Orthology more info
located_in nuclear envelope	ISS Inferred from Sequence or Structural Similarity more info
located_in nuclear envelope	TAS Traceable Author Statement more info
located_in nuclear inclusion body	ISO Inferred from Sequence Orthology more info
located_in nuclear inclusion body	ISS Inferred from Sequence or Structural Similarity more info
located_in nuclear membrane	ISO Inferred from Sequence Orthology more info
located_in nuclear membrane	ISS Inferred from Sequence or Structural Similarity more info
part_of nuclear pore	IBA Inferred from Biological aspect of Ancestor more info
part_of nuclear pore	ISO Inferred from Sequence Orthology more info
part_of nuclear pore	ISS Inferred from Sequence or Structural Similarity more info
part_of nuclear pore	NAS Non-traceable Author Statement more info	PubMed
part_of nuclear pore cytoplasmic filaments	IEA Inferred from Electronic Annotation more info
part_of nuclear pore cytoplasmic filaments	ISO Inferred from Sequence Orthology more info
part_of nuclear pore nuclear basket	ISO Inferred from Sequence Orthology more info
part_of nuclear pore nuclear basket	ISS Inferred from Sequence or Structural Similarity more info
located_in nucleoplasm	IEA Inferred from Electronic Annotation more info
located_in nucleoplasm	ISO Inferred from Sequence Orthology more info

General protein information

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Preferred Names: E3 SUMO-protein ligase RanBP2

Names: E3 SUMO-protein transferase RanBP2; ran-binding protein 2

NP_035370.2

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.

mRNA and Protein(s)

NM_011240.3 → NP_035370.2 E3 SUMO-protein ligase RanBP2

See identical proteins and their annotated locations for NP_035370.2

Status: VALIDATED

Source sequence(s)

AC158593

Consensus CDS

CCDS23861.1

UniProtKB/Swiss-Prot

E9QM01, Q61992, Q8C9K9, Q9ERU9

Related

ENSMUSP00000003310.6, ENSMUST00000003310.7

Conserved Domains (12) summary

cd01926
Location:2893 → 3051

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:1864 → 1980

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

cd13178
Location:2754 → 2870

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

cd14684
Location:1180 → 1296

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

cd14685
Location:2161 → 2277

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

sd00025
Location:1350 → 1369

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

sd00006
Location:59 → 89

TPR; TPR repeat [structural motif]

pfam00515
Location:60 → 92

TPR_1; Tetratricopeptide repeat

pfam00641
Location:1469 → 1498

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

pfam12185
Location:2544 → 2602

IR1-M; Nup358/RanBP2 E3 ligase domain

pfam13414
Location:59 → 126

TPR_11; TPR repeat

cl23782
Location:839 → 925

RCR; Chitin synthesis regulation, resistance to Congo red