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Search results 201 to 300 out of 1806 for Ranbp1

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Type Details Score
Publication
- | J:155721
     
First Author: Mouse Genome Informatics (MGI) and The National Center for Biotechnology Information (NCBI)
Year: 2010
Journal: Database Download
Title: Consensus CDS project
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Publication
- | J:85324
     
First Author: Mouse Genome Informatics Group
Year: 2003
Journal: Database Procedure
Title: Automatic Encodes (AutoE) Reference
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Publication
- | J:53168
     
First Author: Bairoch A
Year: 1999
Journal: Database Release
Title: SWISS-PROT Annotated protein sequence database
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Publication
- | J:91388
       
First Author: Mouse Genome Informatics Scientific Curators
Year: 2005
Title: Obtaining and Loading Genome Assembly Coordinates from Ensembl Annotations
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Publication
- | J:155221
     
First Author: Mouse Genome Informatics
Year: 2010
Journal: Database Release
Title: Protein Ontology Association Load.
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Publication
- | J:90438
       
First Author: Mouse Genome Informatics Scientific Curators
Year: 2005
Title: Obtaining and loading genome assembly coordinates from NCBI annotations
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Publication
- | J:144087
     
First Author: Mouse Genome Informatics Scientific Curators
Year: 2009
Journal: Database Download
Title: Mouse Microarray Data Integration in Mouse Genome Informatics, the Affymetrix GeneChip Mouse Genome 430 2.0 Array Platform
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Publication
9883880 | J:51858
First Author: Callebaut I
Year: 1998
Journal: FEBS Lett
Title: EVH1/WH1 domains of VASP and WASP proteins belong to a large family including Ran-binding domains of the RanBP1 family.
Volume: 441
Issue: 2
Pages: 181-5
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Publication
9111043 | J:39773
First Author: Zolotukhin AS
Year: 1997
Journal: J Biol Chem
Title: Mutations in the nuclear export signal of human ran-binding protein RanBP1 block the Rev-mediated posttranscriptional regulation of human immunodeficiency virus type 1.
Volume: 272
Issue: 17
Pages: 11356-60
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Protein
P34022
Organism: Mus musculus/domesticus
Length: 203  
Fragment?: false
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Interaction Experiment
Bischoff FR (1997)
Description: RanBP1 is crucial for the release of RanGTP from importin beta-related nuclear transport factors.
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Interaction Experiment
Li Y (2019)
Description: Distinct RanBP1 nuclear export and cargo dissociation mechanisms between fungi and animals.
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Publication
9428644 | -
First Author: Bischoff FR
Year: 1997
Journal: FEBS Lett
Title: RanBP1 is crucial for the release of RanGTP from importin beta-related nuclear transport factors.
Volume: 419
Issue: 2-3
Pages: 249-54
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Publication
31021318 | -
   
First Author: Li Y
Year: 2019
Journal: Elife
Title: Distinct RanBP1 nuclear export and cargo dissociation mechanisms between fungi and animals.
Volume: 8
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Publication
7616957 | J:28336
First Author: Hayashi N
Year: 1995
Journal: Mol Gen Genet
Title: RanBP1, a Ras-like nuclear G protein binding to Ran/TC4, inhibits RCC1 via Ran/TC4.
Volume: 247
Issue: 6
Pages: 661-9
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Protein Domain
IPR045256 | RanBP1_RanBD
Type: Domain
Description: This entry represents the Ran-binding domain (RBD) found in RanBP1 from humans and Yrb1 from budding yeasts. RanBP1 and Yrb1 are involved in nuclear import and export. RanBP1 and Yrb1 have been shown to shuttle between the nucleus and cytoplasm and the conserved RBD is necessary and sufficient for the essential function and nucleocytoplasmic shuttling []. RanBP1/Yrb1 acts as a negative regulator of Regulator of chromosome condensation 1 (RCC1) by inhibiting RCC1-stimulated guanine nucleotide release from Ran [].
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Publication
22730302 | J:199697
First Author: Chao HW
Year: 2012
Journal: Nucleic Acids Res
Title: NMDAR signaling facilitates the IPO5-mediated nuclear import of CPEB3.
Volume: 40
Issue: 17
Pages: 8484-98
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Publication
10825193 | -
First Author: Künzler M
Year: 2000
Journal: Mol Cell Biol
Title: Yeast Ran-binding protein 1 (Yrb1) shuttles between the nucleus and cytoplasm and is exported from the nucleus via a CRM1 (XPO1)-dependent pathway.
Volume: 20
Issue: 12
Pages: 4295-308
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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
H7BX22
Organism: Mus musculus/domesticus
Length: 153  
Fragment?: false
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Protein
Q3U6M5
Organism: Mus musculus/domesticus
Length: 203  
Fragment?: false
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Publication
10404224 | -
First Author: Fedorov AA
Year: 1999
Journal: Nat Struct Biol
Title: Structure of EVH1, a novel proline-rich ligand-binding module involved in cytoskeletal dynamics and neural function.
Volume: 6
Issue: 7
Pages: 661-5
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Protein Domain
IPR000156 | Ran_bind_dom
Type: Domain
Description: 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 1 (RanBP1) has guanine nucleotide dissociation inhibitory activity, specific for the GTP form of Ran and also functions to stimulate Ran GTPase activating protein(GAP)-mediated GTP hydrolysis by Ran. RanBP1 contributes to maintaining the gradient of RanGTP across the nuclear envelope high (GDI activity) or the cytoplasmic levels of RanGTP low (GAP cofactor) [].All RanBP1 proteins contain an approx 150 amino acid residue Ran binding domain. Ran BP1 binds directly to RanGTP with high affinity.There are four sites of contact between Ran and the Ran binding domain. One of these involves binding of the C-terminal segment of Ran to a groove on the Ran binding domain that is analogous to the surface utilised in the EVH1-peptide interaction []. Nup358 contains four Ran binding domains. The structure of the first of these is known [].
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Protein Domain
IPR045255 | RanBP1-like
Type: Family
Description: This entry represents a group of RanGTP-binding proteins that contain a conserved RanGTP-binding motif, also called a Ran-binding domain (RBD). They have been implicated in nucleocytoplasmic transport. NUP358 (RanBP2) is localised to the cytoplasmic filaments protruding from the nuclear pore complex (NPC) into the cytoplasm, while RanBP3/Hba1 are localised to the nucleoplasm and Nup2 is localised to the NPC. In general, RanBP1 and other members of this protein family increase, via their conserved RBDs, the rate of RanGAP1-mediated GTP hydrolysis on Ran [].
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Publication
10078529 | -
First Author: Vetter IR
Year: 1999
Journal: Nature
Title: Structure of a Ran-binding domain complexed with Ran bound to a GTP analogue: implications for nuclear transport.
Volume: 398
Issue: 6722
Pages: 39-46
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Protein
Q9CT10
Organism: Mus musculus/domesticus
Length: 491  
Fragment?: false
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Protein
Q6PDH4
Organism: Mus musculus/domesticus
Length: 491  
Fragment?: false
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Protein
A0A2I3BQU7
Organism: Mus musculus/domesticus
Length: 354  
Fragment?: true
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Protein
A0A3B2WCL5
Organism: Mus musculus/domesticus
Length: 558  
Fragment?: false
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Protein
O08846
Organism: Mus musculus/domesticus
Length: 52  
Fragment?: true
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Publication
12578832 | -
First Author: Braunwarth A
Year: 2003
Journal: J Biol Chem
Title: Identification and characterization of a novel RanGTP-binding protein in the yeast Saccharomyces cerevisiae.
Volume: 278
Issue: 17
Pages: 15397-405
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Protein Domain
IPR008812 | Ran_GTP-bd-rel
Type: Family
Description: The small Ras-like GTPase Ran plays an essential role in the transport of macromolecules in and out of the nucleus and has been implicated in spindle and nuclear envelope formation during mitosis in higher eukaryotes. The Saccharomyces cerevisiae ORF YGL164c encoding a novel RanGTP-binding protein, termed Yrb30p was identified. The protein competes with S. cerevisiae RanBP1 (Yrb1p) for binding to the GTP-bound form of S. cerevisiae Ran (Gsp1p) and is, like Yrb1p, able to form trimeric complexes with RanGTP and some of the karyopherins [].
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Protein Domain
IPR009109 | Ran_GTPase_activating_1_C
Type: Domain
Description: Ran GTPase is a ubiquitous protein required for nuclear transport, spindle assembly, nuclear assembly and mitotic cell cycle regulation. RanGTPase activating protein 1 (RanGAP1) is one of several RanGTPase accessory proteins. During interphase, RanGAP1 is located in the cytoplasm, while during mitosis it becomes associated with the kinetochores []. Cytoplasmic RanGAP1 is required for RanGTPase-directed nuclear transport. The activity of RanGAP1 requires the accessory protein RanBP1. RanBP1 facilitates RanGAP1 hydrolysis of Ran-GTP, both directly and by promoting the dissociation of Ran-GTP from transport receptors, which would otherwise block RanGAP1-mediated hydrolysis. RanGAP1 is thought to bind to the Switch 1 and Switch 2 regions of RanGTPase. The Switch 2 region can be buried in complexes with karyopherin-beta2, and requires the interaction with RanBP1 to permit RanGAP1 function. RanGAP1 can undergo SUMO (small ubiquitin-like modifier) modification, which targets RanGAP1 to RanBP2/Nup358 in the nuclear pore complex, and is required for association with the nuclear pore complex and for nuclear transport []. The enzymes involved in SUMO modification are located on the filaments of the nuclear pore complex.The RanGAP1 N-terminal domain is fairly well conserved between vertebrate and fungal proteins, but yeast does not contain the C-terminal domain. The C-terminal domain is SUMO-modified and required for the localisation of RanGAP1 at the nuclear pore complex. The structure of the C-terminal domain is multihelical, consisting of two curved alpha/alpha layers in a right-handed superhelix.
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Protein Domain
IPR036720 | RanGAP1_C_sf
Type: Homologous_superfamily
Description: Ran GTPase is a ubiquitous protein required for nuclear transport, spindle assembly, nuclear assembly and mitotic cell cycle regulation. RanGTPase activating protein 1 (RanGAP1) is one of several RanGTPase accessory proteins. During interphase, RanGAP1 is located in the cytoplasm, while during mitosis it becomes associated with the kinetochores []. Cytoplasmic RanGAP1 is required for RanGTPase-directed nuclear transport. The activity of RanGAP1 requires the accessory protein RanBP1. RanBP1 facilitates RanGAP1 hydrolysis of Ran-GTP, both directly and by promoting the dissociation of Ran-GTP from transport receptors, which would otherwise block RanGAP1-mediated hydrolysis. RanGAP1 is thought to bind to the Switch 1 and Switch 2 regions of RanGTPase. The Switch 2 region can be buried in complexes with karyopherin-beta2, and requires the interaction with RanBP1 to permit RanGAP1 function. RanGAP1 can undergo SUMO (small ubiquitin-like modifier) modification, which targets RanGAP1 to RanBP2/Nup358 in the nuclear pore complex, and is required for association with the nuclear pore complex and for nuclear transport []. The enzymes involved in SUMO modification are located on the filaments of the nuclear pore complex.The RanGAP1 N-terminal domain is fairly well conserved between vertebrate and fungal proteins, but yeast does not contain the C-terminal domain. The C-terminal domain is SUMO-modified and required for the localisation of RanGAP1 at the nuclear pore complex. The structure of the C-terminal domain is multihelical, consisting of two curved alpha/alpha layers in a right-handed superhelix.
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Protein
Q9JIH2
Organism: Mus musculus/domesticus
Length: 466  
Fragment?: false
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Publication
11853669 | -
First Author: Bernier-Villamor V
Year: 2002
Journal: Cell
Title: Structural basis for E2-mediated SUMO conjugation revealed by a complex between ubiquitin-conjugating enzyme Ubc9 and RanGAP1.
Volume: 108
Issue: 3
Pages: 345-56
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Protein
Q9CW20
Organism: Mus musculus/domesticus
Length: 58  
Fragment?: true
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Protein
Q76N02
Organism: Mus musculus/domesticus
Length: 46  
Fragment?: true
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Protein
Q3V2K7
Organism: Mus musculus/domesticus
Length: 440  
Fragment?: false
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Protein
Q9DAQ0
Organism: Mus musculus/domesticus
Length: 117  
Fragment?: false
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Protein
H3BJX0
Organism: Mus musculus/domesticus
Length: 67  
Fragment?: true
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Protein
F6S7E8
Organism: Mus musculus/domesticus
Length: 99  
Fragment?: true
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Protein
A0A140LIM7
Organism: Mus musculus/domesticus
Length: 105  
Fragment?: true
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Protein
D3Z2C8
Organism: Mus musculus/domesticus
Length: 36  
Fragment?: true
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Protein
D3Z3L8
Organism: Mus musculus/domesticus
Length: 95  
Fragment?: true
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Protein
J3QPK7
Organism: Mus musculus/domesticus
Length: 160  
Fragment?: false
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Protein
J3QMC0
Organism: Mus musculus/domesticus
Length: 123  
Fragment?: false
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Protein
Q3TXD6
Organism: Mus musculus/domesticus
Length: 48  
Fragment?: true
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Protein
D6RJL7
Organism: Mus musculus/domesticus
Length: 51  
Fragment?: false
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Protein
Q3UW93
Organism: Mus musculus/domesticus
Length: 243  
Fragment?: true
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Protein
F6W980
Organism: Mus musculus/domesticus
Length: 200  
Fragment?: true
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Protein
S4R2V0
Organism: Mus musculus/domesticus
Length: 146  
Fragment?: true
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Protein
J3JS29
Organism: Mus musculus/domesticus
Length: 147  
Fragment?: true
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Protein
Q9D4E1
Organism: Mus musculus/domesticus
Length: 193  
Fragment?: false
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Protein
J3QNW2
Organism: Mus musculus/domesticus
Length: 99  
Fragment?: false
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Protein
E9PXM2
Organism: Mus musculus/domesticus
Length: 192  
Fragment?: false
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Publication
12852855 | -
First Author: Arnaoutov A
Year: 2003
Journal: Dev Cell
Title: The Ran GTPase regulates kinetochore function.
Volume: 5
Issue: 1
Pages: 99-111
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Publication
12429733 | -
First Author: Smith WJ
Year: 2003
Journal: J Biol Chem
Title: Structure of the active N-terminal domain of Ezrin. Conformational and mobility changes identify keystone interactions.
Volume: 278
Issue: 7
Pages: 4949-56
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Protein Domain
IPR011993 | PH-like_dom_sf
Type: Homologous_superfamily
Description: Pleckstrin homology (PH) domains are small modular domains that occur in a large variety of signalling proteins, where they serve as simple targeting domains that bind lipids [, , ]. PH domains have a partly opened β-barrel topology that is capped by an alpha helix. The structure of PH domains is similar to the phosphotyrosine-binding domain (PTB) found in IRS-1 (insulin receptor substrate 1) [], Shc adaptor and Numb []; to the Ran-binding domain, found in Nup nuclear pore complex and Ranbp1 []; to the Enabled/VASP homology domain 1 (EVH1 domain), found in Enabled, VASP (vasodilator-stimulated phosphoprotein), Homer and WASP actin regulatory protein []; and to the third domain of FERM, found in moesin, radixin, ezrin, merlin and talin [].This superfamily represents the PH domain and structurally related domains.
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Protein
Q03173
Organism: Mus musculus/domesticus
Length: 802  
Fragment?: false
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Protein
A0A0A6YXC8
Organism: Mus musculus/domesticus
Length: 524  
Fragment?: false
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Protein
A0A140LHR9
Organism: Mus musculus/domesticus
Length: 179  
Fragment?: true
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Protein
E9QLZ9
Organism: Mus musculus/domesticus
Length: 804  
Fragment?: false
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Protein
A0A140LJ06
Organism: Mus musculus/domesticus
Length: 252  
Fragment?: false
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Protein
A0A0A6YW06
Organism: Mus musculus/domesticus
Length: 785  
Fragment?: false
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Protein
A0A2R8W753
Organism: Mus musculus/domesticus
Length: 144  
Fragment?: true
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Protein
E9QKR1
Organism: Mus musculus/domesticus
Length: 562  
Fragment?: false
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Protein
J3QNM3
Organism: Mus musculus/domesticus
Length: 789  
Fragment?: false
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Protein
E9Q4F9
Organism: Mus musculus/domesticus
Length: 290  
Fragment?: false
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Protein
E9QKQ9
Organism: Mus musculus/domesticus
Length: 789  
Fragment?: false
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Protein
Q6PEM6
Organism: Mus musculus/domesticus
Length: 445  
Fragment?: false
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Protein
Q8VCC6
Organism: Mus musculus/domesticus
Length: 481  
Fragment?: false
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Protein
P46061
Organism: Mus musculus/domesticus
Length: 589  
Fragment?: false
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Protein
Q3V3G7
Organism: Mus musculus/domesticus
Length: 320  
Fragment?: false
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Protein
E0CZH2
Organism: Mus musculus/domesticus
Length: 157  
Fragment?: false
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Protein
F7BJ98
Organism: Mus musculus/domesticus
Length: 734  
Fragment?: true
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Protein
Q7TMW1
Organism: Mus musculus/domesticus
Length: 589  
Fragment?: false
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Protein
A4FUT6
Organism: Mus musculus/domesticus
Length: 200  
Fragment?: true
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Protein
Q9D318
Organism: Mus musculus/domesticus
Length: 514  
Fragment?: false
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Protein
Q8CAP5
Organism: Mus musculus/domesticus
Length: 334  
Fragment?: false
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Protein
Q5RJB9
Organism: Mus musculus/domesticus
Length: 194  
Fragment?: true
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Protein
Q3UZD8
Organism: Mus musculus/domesticus
Length: 396  
Fragment?: false
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Protein
D3YWU9
Organism: Mus musculus/domesticus
Length: 199  
Fragment?: true
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Protein
A0A087WPB6
Organism: Mus musculus/domesticus
Length: 224  
Fragment?: true
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Protein
A0A286YCN4
Organism: Mus musculus/domesticus
Length: 177  
Fragment?: true
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Protein
Q3ULJ9
Organism: Mus musculus/domesticus
Length: 483  
Fragment?: false
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Protein
S4R1K4
Organism: Mus musculus/domesticus
Length: 128  
Fragment?: true
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Protein
E0CYY2
Organism: Mus musculus/domesticus
Length: 126  
Fragment?: false
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Protein
Q6ZPH4
Organism: Mus musculus/domesticus
Length: 646  
Fragment?: true
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Protein
Q8C2E3
Organism: Mus musculus/domesticus
Length: 589  
Fragment?: false
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Protein
Q3TTJ8
Organism: Mus musculus/domesticus
Length: 323  
Fragment?: false
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Protein
F6X8K3
Organism: Mus musculus/domesticus
Length: 60  
Fragment?: true
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Protein
E0CZ84
Organism: Mus musculus/domesticus
Length: 113  
Fragment?: true
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Protein
A0A5F8MQ15
Organism: Mus musculus/domesticus
Length: 133  
Fragment?: true
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Protein
Q91YS2
Organism: Mus musculus/domesticus
Length: 589  
Fragment?: false
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Protein
A0A571BF92
Organism: Mus musculus/domesticus
Length: 192  
Fragment?: false
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Protein
A0A286YDC8
Organism: Mus musculus/domesticus
Length: 419  
Fragment?: true
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Protein
D3Z1T6
Organism: Mus musculus/domesticus
Length: 176  
Fragment?: true
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Protein
A0A087WRK8
Organism: Mus musculus/domesticus
Length: 161  
Fragment?: true
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Protein
D3YVC0
Organism: Mus musculus/domesticus
Length: 245  
Fragment?: true
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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.

Copyright © 2017 by The Jackson Laboratory. All Rights Reserved

© 2002 - 2017 Department of Genetics, University of Cambridge, Downing Street,
Cambridge CB2 3EH, United Kingdom