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Search results 401 to 500 out of 511 for Ranbp2

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Type Details Score
UniProt Feature
UniProt Feature
Begin: 57
Description: Interaction with RANBP2
Type: site
End: 57
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UniProt Feature
UniProt Feature
Begin: 25
Description: Interaction with RANBP2
Type: site
End: 25
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UniProt Feature
UniProt Feature
Begin: 4
Description: Interaction with RANBP2
Type: site
End: 4
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Gene
749339 | RGPD8
Type: gene
Organism: chimpanzee
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Publication
30333138 | J:266974
 
First Author: Wu K
Year: 2018
Journal: J Cell Sci
Title: GCN5L1 interacts with αTAT1 and RanBP2 to regulate hepatic α-tubulin acetylation and lysosome trafficking.
Volume: 131
Issue: 22
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GXD Expression
GXD Expression
 
Probe: MGI:7643699
Assay Type: Immunohistochemistry
Annotation Date: 2024-07-23
Strength: Present
Sex: Not Specified
Emaps: EMAPS:1857728
Pattern: Not Specified
Stage: TS28
Assay Id: MGI:7703257
Age: postnatal adult
Note: Coexpressed with Ranbp2 at the paranodes.
Specimen Label: S3C upper
Detected: true
Specimen Num: 1
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GXD Expression
GXD Expression
 
Probe: MGI:7643699
Assay Type: Immunohistochemistry
Annotation Date: 2024-07-23
Strength: Present
Sex: Not Specified
Emaps: EMAPS:1857728
Pattern: Not Specified
Stage: TS28
Assay Id: MGI:7703257
Age: postnatal adult
Note: Coexpressed with Ranbp2 at the paranodes.
Specimen Label: S3C lower
Detected: true
Specimen Num: 2
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GXD Expression
GXD Expression
 
Probe: MGI:7703153
Assay Type: Immunohistochemistry
Annotation Date: 2024-07-23
Strength: Present
Sex: Not Specified
Emaps: EMAPS:1857728
Pattern: Not Specified
Stage: TS28
Assay Id: MGI:7703256
Age: postnatal adult
Note: Coexpressed with Ranbp2 at nodes of Ranvier.
Specimen Label: S3B
Detected: true
Specimen Num: 1
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Interaction Experiment
Pichler A (2002)
Description: The nucleoporin RanBP2 has SUMO1 E3 ligase activity.
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Publication
11792325 | -
First Author: Pichler A
Year: 2002
Journal: Cell
Title: The nucleoporin RanBP2 has SUMO1 E3 ligase activity.
Volume: 108
Issue: 1
Pages: 109-20
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Allele
Ranbp2<tm1Smoc> | MGI:7291970
Name: RAN binding protein 2; targeted mutation 1, Shanghai Model Organisms Center
Allele Type: Targeted
Attribute String: Conditional ready, No functional change
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Publication
23641069 | -
First Author: Yoshimura SH
Year: 2013
Journal: J Cell Sci
Title: Intermolecular disulfide bonds between nucleoporins regulate karyopherin-dependent nuclear transport.
Volume: 126
Issue: Pt 14
Pages: 3141-50
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Publication
15037602 | -
First Author: Swaminathan S
Year: 2004
Journal: J Cell Biol
Title: RanGAP1*SUMO1 is phosphorylated at the onset of mitosis and remains associated with RanBP2 upon NPC disassembly.
Volume: 164
Issue: 7
Pages: 965-71
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Publication
12032081 | -
First Author: Kirsh O
Year: 2002
Journal: EMBO J
Title: The SUMO E3 ligase RanBP2 promotes modification of the HDAC4 deacetylase.
Volume: 21
Issue: 11
Pages: 2682-91
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Publication
12874105 | -
First Author: Castagnet P
Year: 2003
Journal: Hum Mol Genet
Title: RPGRIP1s with distinct neuronal localization and biochemical properties associate selectively with RanBP2 in amacrine neurons.
Volume: 12
Issue: 15
Pages: 1847-63
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Publication
18946085 | -
First Author: Klein UR
Year: 2009
Journal: Mol Biol Cell
Title: RanBP2 and SENP3 function in a mitotic SUMO2/3 conjugation-deconjugation cycle on Borealin.
Volume: 20
Issue: 1
Pages: 410-8
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Strain
MGI:6429461 | C57BL/6J-Ranbp2<tm1Smoc>/Smoc
Attribute String: targeted mutation, mutant stock
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Publication
9019411 | J:38226
First Author: Mahajan R
Year: 1997
Journal: Cell
Title: A small ubiquitin-related polypeptide involved in targeting RanGAP1 to nuclear pore complex protein RanBP2.
Volume: 88
Issue: 1
Pages: 97-107
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Publication
26321253 | J:228091
First Author: Liu H
Year: 2015
Journal: Mol Cell
Title: The Immune Adaptor SLP-76 Binds to SUMO-RANGAP1 at Nuclear Pore Complex Filaments to Regulate Nuclear Import of Transcription Factors in T Cells.
Volume: 59
Issue: 5
Pages: 840-9
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Protein
Q9R020
Organism: Mus musculus/domesticus
Length: 330  
Fragment?: false
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Protein
Q9D9Z2
Organism: Mus musculus/domesticus
Length: 185  
Fragment?: false
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Protein
A2AFS9
Organism: Mus musculus/domesticus
Length: 377  
Fragment?: false
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Protein
A0A0G2JGA3
Organism: Mus musculus/domesticus
Length: 530  
Fragment?: false
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Protein
A0A0G2JGE3
Organism: Mus musculus/domesticus
Length: 38  
Fragment?: false
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Protein
B2RRT9
Organism: Mus musculus/domesticus
Length: 330  
Fragment?: false
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Protein
A0A1D5RLI7
Organism: Mus musculus/domesticus
Length: 502  
Fragment?: false
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Protein
D3Z4U0
Organism: Mus musculus/domesticus
Length: 320  
Fragment?: false
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Protein
Q3USF2
Organism: Mus musculus/domesticus
Length: 255  
Fragment?: true
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Protein
Q3TQH3
Organism: Mus musculus/domesticus
Length: 254  
Fragment?: true
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Protein
V9GX51
Organism: Mus musculus/domesticus
Length: 40  
Fragment?: false
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Protein
E9PUD0
Organism: Mus musculus/domesticus
Length: 293  
Fragment?: false
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Publication
10318915 | -
First Author: Yaseen NR
Year: 1999
Journal: Proc Natl Acad Sci U S A
Title: Two distinct classes of Ran-binding sites on the nucleoporin Nup-358.
Volume: 96
Issue: 10
Pages: 5516-21
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Protein Domain
IPR001876 | Znf_RanBP2
Type: Domain
Description: Zinc finger (Znf) domains are relatively small protein motifs which contain multiple finger-like protrusions that make tandem contacts with their target molecule. Some of these domains bind zinc, but many do not; instead binding other metals such as iron, or no metal at all. For example, some family members form salt bridges to stabilise the finger-like folds. They were first identified as a DNA-binding motif in transcription factor TFIIIA from Xenopus laevis (African clawed frog), however they are now recognised to bind DNA, RNA, protein and/or lipid substrates [, , , , ]. Their binding properties depend on the amino acid sequence of the finger domains and of the linker between fingers, as well as on the higher-order structures and the number of fingers. Znf domains are often found in clusters, where fingers can have different binding specificities. There are many superfamilies of Znf motifs, varying in both sequence and structure. They display considerable versatility in binding modes, even between members of the same class (e.g. some bind DNA, others protein), suggesting that Znf motifs are stable scaffolds that have evolved specialised functions. For example, Znf-containing proteins function in gene transcription, translation, mRNA trafficking, cytoskeleton organisation, epithelial development, cell adhesion, protein folding, chromatin remodelling and zinc sensing, to name but a few []. Zinc-binding motifs are stable structures, and they rarely undergo conformational changes upon binding their target. This entry representsthe zinc finger domain found in RanBP2 proteins. Ran is an evolutionary conserved member of the Ras superfamily that regulates all receptor-mediated transport between the nucleus and the cytoplasm. Ran binding protein 2 (RanBP2) is a 358kDa nucleoporin located on the cytoplasmic side of the nuclear pore complex which plays a role in nuclear protein import []. RanBP2 contains multiple zinc fingers which mediate binding to RanGDP [].
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Protein Domain
IPR036443 | Znf_RanBP2_sf
Type: Homologous_superfamily
Description: Zinc finger (Znf) domains are relatively small protein motifs which contain multiple finger-like protrusions that make tandem contacts with their target molecule. Some of these domains bind zinc, but many do not; instead binding other metals such as iron, or no metal at all. For example, some family members form salt bridges to stabilise the finger-like folds. They were first identified as a DNA-binding motif in transcription factor TFIIIA from Xenopus laevis (African clawed frog), however they are now recognised to bind DNA, RNA, protein and/or lipid substrates [, , , , ]. Their binding properties depend on the amino acid sequence of the finger domains and of the linker between fingers, as well as on the higher-order structures and the number of fingers. Znf domains are often found in clusters, where fingers can have different binding specificities. There are many superfamilies of Znf motifs, varying in both sequence and structure. They display considerable versatility in binding modes, even between members of the same class (e.g. some bind DNA, others protein), suggesting that Znf motifs are stable scaffolds that have evolved specialised functions. For example, Znf-containing proteins function in gene transcription, translation, mRNA trafficking, cytoskeleton organisation, epithelial development, cell adhesion, protein folding, chromatin remodelling and zinc sensing, to name but a few []. Zinc-binding motifs are stable structures, and they rarely undergo conformational changes upon binding their target. This entry represents the zinc finger domain superfamily found in RanBP2 proteins. Ran is an evolutionary conserved member of the Ras superfamily that regulates all receptor-mediated transport between the nucleus and the cytoplasm. Ran binding protein 2 (RanBP2) is a 358kDa nucleoporin located on the cytoplasmic side of the nuclear pore complex which plays a role in nuclear protein import []. RanBP2 contains multiple zinc fingers which mediate binding to RanGDP [].
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Publication
20386726 | J:236956
First Author: Splinter D
Year: 2010
Journal: PLoS Biol
Title: Bicaudal D2, dynein, and kinesin-1 associate with nuclear pore complexes and regulate centrosome and nuclear positioning during mitotic entry.
Volume: 8
Issue: 4
Pages: e1000350
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Publication
9365272 | J:45030
 
First Author: Nicolás FJ
Year: 1997
Journal: J Cell Sci
Title: Xenopus Ran-binding protein 1: molecular interactions and effects on nuclear assembly in Xenopus egg extracts.
Volume: 110 ( Pt 24)
Pages: 3019-30
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Protein
Q8CCI5
Organism: Mus musculus/domesticus
Length: 228  
Fragment?: false
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Protein
Q571K4
Organism: Mus musculus/domesticus
Length: 716  
Fragment?: false
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Protein
Q91WA6
Organism: Mus musculus/domesticus
Length: 380  
Fragment?: false
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Protein
Q99K90
Organism: Mus musculus/domesticus
Length: 693  
Fragment?: false
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Protein
Q99LW6
Organism: Mus musculus/domesticus
Length: 179  
Fragment?: false
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Protein
Q80WR0
Organism: Mus musculus/domesticus
Length: 1462  
Fragment?: false
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Protein
Q80UN3
Organism: Mus musculus/domesticus
Length: 928  
Fragment?: true
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Protein
E9Q3G8
Organism: Mus musculus/domesticus
Length: 1462  
Fragment?: false
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Protein
A0A1B0GQZ6
Organism: Mus musculus/domesticus
Length: 372  
Fragment?: false
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Protein
Q8BRF6
Organism: Mus musculus/domesticus
Length: 666  
Fragment?: true
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Protein
Q8BQK6
Organism: Mus musculus/domesticus
Length: 516  
Fragment?: true
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Protein
G3UZD2
Organism: Mus musculus/domesticus
Length: 104  
Fragment?: true
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Protein
F6UHH8
Organism: Mus musculus/domesticus
Length: 83  
Fragment?: true
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Protein
A0A286YE24
Organism: Mus musculus/domesticus
Length: 303  
Fragment?: true
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Protein
B1ASY9
Organism: Mus musculus/domesticus
Length: 716  
Fragment?: false
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Protein
Q91VQ2
Organism: Mus musculus/domesticus
Length: 280  
Fragment?: false
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Publication
24998930 | -
First Author: Stingele J
Year: 2014
Journal: Cell
Title: A DNA-dependent protease involved in DNA-protein crosslink repair.
Volume: 158
Issue: 2
Pages: 327-338
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Protein Domain
IPR013536 | WLM_dom
Type: Domain
Description: The WLM (WSS1-like metalloprotease) domain is a globular domain related to the zincin-like superfamily of Zn-dependent peptidase. Since the WLM domain contains all known active site residues of zincins, it is predicted to be a catalytically active peptidase domain. The WLM domain is a eukaryotic domain represented in plants, fungi, Plasmodium, and kinetoplastids. By contrast, it is absent in animals, Cryptosporidium, and Microsporidia, suggesting that it has been lost on multiple occasions during the evolution of eukaryotes. The WLM domain is found either in stand-alone form or in association with other domains such as the RanBP2 zinc finger , the ubiquitin domain, or the PUB/PUG domain. This domain could function as a specific de-SUMOylating domain of distinct protein complexes in the nucleus and the cytoplasm []. It has been suggested to form a segregated alpha/beta structure with eight helices and five strands. Proteins containing this domain include yeast WSS1 (also known as weak suppressor of SMT3) which is involved in the repair of toxic DNA-protein cross-links (DPCs) such as covalently trapped topoisomerase 1 (TOP1) adducts on DNA lesions or DPCs induced by reactive compounds [], WSS1 homologues and various putative metalloproteases from plant and fungal species. This domain is also found in an uncharacterised protein from Acanthamoeba polyphaga mimivirus.
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Protein
P60670
Organism: Mus musculus/domesticus
Length: 608  
Fragment?: false
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Protein
Q3UE06
Organism: Mus musculus/domesticus
Length: 608  
Fragment?: false
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Protein
Q05CY7
Organism: Mus musculus/domesticus
Length: 444  
Fragment?: true
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Protein
S4R1U7
Organism: Mus musculus/domesticus
Length: 251  
Fragment?: true
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Protein
Q3UDU9
Organism: Mus musculus/domesticus
Length: 608  
Fragment?: false
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Protein
Q61545
Organism: Mus musculus/domesticus
Length: 655  
Fragment?: false
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Protein
P56959
Organism: Mus musculus/domesticus
Length: 518  
Fragment?: false
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Protein
Q7M760
Organism: Mus musculus/domesticus
Length: 708  
Fragment?: false
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Protein
Q6NZP1
Organism: Mus musculus/domesticus
Length: 1069  
Fragment?: false
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Protein
Q8BQ46
Organism: Mus musculus/domesticus
Length: 557  
Fragment?: false
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Protein
Q3UK30
Organism: Mus musculus/domesticus
Length: 518  
Fragment?: false
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Protein
Q566J0
Organism: Mus musculus/domesticus
Length: 591  
Fragment?: true
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Protein
Q9CRS5
Organism: Mus musculus/domesticus
Length: 333  
Fragment?: true
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Protein
Q3UI30
Organism: Mus musculus/domesticus
Length: 655  
Fragment?: false
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Protein
A0A1L1SQ24
Organism: Mus musculus/domesticus
Length: 734  
Fragment?: false
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Protein
Q3USY4
Organism: Mus musculus/domesticus
Length: 518  
Fragment?: false
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Protein
Q8BY56
Organism: Mus musculus/domesticus
Length: 557  
Fragment?: true
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Protein
Q3TLE4
Organism: Mus musculus/domesticus
Length: 518  
Fragment?: false
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Protein
Q5SUT0
Organism: Mus musculus/domesticus
Length: 618  
Fragment?: false
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Protein
G3UXT7
Organism: Mus musculus/domesticus
Length: 130  
Fragment?: true
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Protein
Q5SUS9
Organism: Mus musculus/domesticus
Length: 661  
Fragment?: false
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Protein
F6QCI0
Organism: Mus musculus/domesticus
Length: 324  
Fragment?: true
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Protein
Q6NVA3
Organism: Mus musculus/domesticus
Length: 656  
Fragment?: false
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Protein
Q564D0
Organism: Mus musculus/domesticus
Length: 518  
Fragment?: false
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Protein
Q8CFQ9
Organism: Mus musculus/domesticus
Length: 517  
Fragment?: false
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Publication
12019565 | -
 
First Author: Steggerda SM
Year: 2002
Journal: Int Rev Cytol
Title: Regulation of nuclear import and export by the GTPase Ran.
Volume: 217
Pages: 41-91
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Protein
Q99KG3
Organism: Mus musculus/domesticus
Length: 930  
Fragment?: false
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Protein
O35618
Organism: Mus musculus/domesticus
Length: 489  
Fragment?: false
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Protein
Q91YE7
Organism: Mus musculus/domesticus
Length: 815  
Fragment?: false
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Protein
Q924T7
Organism: Mus musculus/domesticus
Length: 1066  
Fragment?: false
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Protein
Q6WIZ9
Organism: Mus musculus/domesticus
Length: 1067  
Fragment?: false
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Protein
Q99L86
Organism: Mus musculus/domesticus
Length: 490  
Fragment?: false
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Protein
F6XVP7
Organism: Mus musculus/domesticus
Length: 912  
Fragment?: true
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Protein
Q3UTC9
Organism: Mus musculus/domesticus
Length: 490  
Fragment?: false
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Publication
15483401 | -
First Author: Iyer LM
Year: 2004
Journal: Cell Cycle
Title: Novel predicted peptidases with a potential role in the ubiquitin signaling pathway.
Volume: 3
Issue: 11
Pages: 1440-50
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Protein
Q9JLG8
Organism: Mus musculus/domesticus
Length: 1095  
Fragment?: false
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Protein
Q8K203
Organism: Mus musculus/domesticus
Length: 606  
Fragment?: false
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Protein
P23804
Organism: Mus musculus/domesticus
Length: 489  
Fragment?: false
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Protein
Q9WUB0
Organism: Mus musculus/domesticus
Length: 508  
Fragment?: false
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Protein
Q3TVL4
Organism: Mus musculus/domesticus
Length: 489  
Fragment?: false
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Protein
Q569X0
Organism: Mus musculus/domesticus
Length: 487  
Fragment?: false
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Protein
A0A1D5RLS3
Organism: Mus musculus/domesticus
Length: 1196  
Fragment?: false
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Protein
A0A1D5RLJ4
Organism: Mus musculus/domesticus
Length: 955  
Fragment?: false
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Publication
19131326 | -
First Author: Sweet SM
Year: 2009
Journal: Mol Cell Proteomics
Title: Large scale localization of protein phosphorylation by use of electron capture dissociation mass spectrometry.
Volume: 8
Issue: 5
Pages: 904-12
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Publication
16452087 | J:263376
First Author: Trinidad JC
Year: 2006
Journal: Mol Cell Proteomics
Title: Comprehensive identification of phosphorylation sites in postsynaptic density preparations.
Volume: 5
Issue: 5
Pages: 914-22
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Publication
24129315 | J:306378
First Author: Guo A
Year: 2014
Journal: Mol Cell Proteomics
Title: Immunoaffinity enrichment and mass spectrometry analysis of protein methylation.
Volume: 13
Issue: 1
Pages: 372-87
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MouseMine is a collaboration between MGI at The Jackson Laboratory and the InterMine project at the Cambridge Systems Biology Centre. MouseMine is funded through a grant from the NIH/NHGRI.The Jackson Laboratory makes no representation about the suitability or accuracy of this software or data for any purpose, and makes no warranties, either express or implied, including merchantability and fitness for a particular purpose or that the use of this software or data will not infringe any third party patents, copyrights, trademarks, or other rights. the software and data are provided "as is". This software and data are provided to enhance knowledge and encourage progress in the scientific community and are to be used only for research and educational purposes. Any reproduction or use for commercial purpose is prohibited without the prior express written permission of the Jackson Laboratory.

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