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Search results 601 to 700 out of 716 for Rbp1

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Type Details Score
Publication
- | J:326541
       
First Author: Cyagen Biosciences Inc.
Year: 2022
Title: Cyagen Biosciences Website.
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Publication
- | J:342587
       
First Author: AgBase, BHF-UCL, Parkinson's UK-UCL, dictyBase, HGNC, Roslin Institute, FlyBase and UniProtKB curators
Year: 2011
Title: Manual transfer of experimentally-verified manual GO annotation data to orthologs by curator judgment of sequence similarity
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Publication
- | J:60000
       
First Author: UniProt-GOA
Year: 2012
Title: Gene Ontology annotation based on UniProtKB/Swiss-Prot keyword mapping
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Publication
- | J:342605
       
First Author: GOA curators
Year: 2016
Title: Automatic transfer of experimentally verified manual GO annotation data to orthologs using Ensembl Compara
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Publication
- | J:68900
     
First Author: The Jackson Laboratory Mouse Radiation Hybrid Database
Year: 2004
Journal: Database Release
Title: Mouse T31 Radiation Hybrid Data Load
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Publication
- | J:164563
       
First Author: The Gene Ontology Consortium
Year: 2010
Title: Automated transfer of experimentally-verified manual GO annotation data to mouse-human orthologs
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Publication
21267068 | J:153498
First Author: Diez-Roux G
Year: 2011
Journal: PLoS Biol
Title: A high-resolution anatomical atlas of the transcriptome in the mouse embryo.
Volume: 9
Issue: 1
Pages: e1000582
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Publication
- | J:75000
       
First Author: Mouse Genome Informatics Scientific Curators
Year: 2002
Title: Mouse Genome Informatics Computational Sequence to Gene Associations
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Publication
- | J:157972
     
First Author: Mouse Genome Informatics Scientific Curators
Year: 2010
Journal: Database Download
Title: Mouse Microarray Data Integration in Mouse Genome Informatics, the Affymetrix GeneChip Mouse Genome U74 Array Platform (A, B, C v2).
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Publication
- | J:57747
     
First Author: MGI Genome Annotation Group and UniGene Staff
Year: 2015
Journal: Database Download
Title: MGI-UniGene Interconnection Effort
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Publication
- | J:161428
       
First Author: Marc Feuermann, Huaiyu Mi, Pascale Gaudet, Dustin Ebert, Anushya Muruganujan, Paul Thomas
Year: 2010
Title: Annotation inferences using phylogenetic trees
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Publication
- | J:63103
     
First Author: Mouse Genome Database and National Center for Biotechnology Information
Year: 2000
Journal: Database Release
Title: Entrez Gene Load
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Publication
- | J:262123
     
First Author: Allen Institute for Brain Science
Year: 2004
Journal: Allen Institute
Title: Allen Brain Atlas: mouse riboprobes
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Publication
- | J:144086
     
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 Gene 1.0 ST Array Platform
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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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Protein
F8VPQ2
Organism: Mus musculus/domesticus
Length: 1261  
Fragment?: false
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Protein
Q7TNF8
Organism: Mus musculus/domesticus
Length: 1846  
Fragment?: false
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Protein
Q7TNF8-2
Organism: Mus musculus/domesticus
Length: 1566  
Fragment?: false
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Protein
Q7TNF8-4
Organism: Mus musculus/domesticus
Length: 1833  
Fragment?: false
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Protein
Q7TNF8-3
Organism: Mus musculus/domesticus
Length: 264  
Fragment?: false
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Allele
Tg(Rbp1-EGFP)GX31Gsat | MGI:4847369
Name: transgene insertion GX31, GENSAT Project at Rockefeller University
Allele Type: Transgenic
Attribute String: Reporter
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Allele
Tg(Rbp1-cre)MJ72Gsat | MGI:5051758
Name: transgene insertion MJ72, GENSAT Project at Rockefeller University
Allele Type: Transgenic
Attribute String: Recombinase
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Strain
MGI:5003661 | STOCK Tg(Rbp1-EGFP)GX31Gsat/Mmucd
Attribute String: mutant stock, transgenic
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Strain
MGI:5519928 | STOCK Tg(Rbp1-cre)MJ72Gsat/Mmucd
Attribute String: transgenic, mutant stock
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Publication
18295589 | J:135646
First Author: Fierce Y
Year: 2008
Journal: Arch Biochem Biophys
Title: In vitro and in vivo characterization of retinoid synthesis from beta-carotene.
Volume: 472
Issue: 2
Pages: 126-38
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Publication
28663132 | J:248708
First Author: Hoffmeister M
Year: 2017
Journal: Dev Biol
Title: Developmental neurogenesis in mouse and Xenopus is impaired in the absence of Nosip.
Volume: 429
Issue: 1
Pages: 200-212
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Protein
Q3U108
Organism: Mus musculus/domesticus
Length: 590  
Fragment?: false
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Protein
D3Z085
Organism: Mus musculus/domesticus
Length: 256  
Fragment?: true
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Protein
D3Z0W0
Organism: Mus musculus/domesticus
Length: 619  
Fragment?: false
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Protein
Q8BWM4
Organism: Mus musculus/domesticus
Length: 264  
Fragment?: true
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Protein
Q8BV50
Organism: Mus musculus/domesticus
Length: 270  
Fragment?: true
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Protein
Q9D982
Organism: Mus musculus/domesticus
Length: 145  
Fragment?: false
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Publication
10545119 | -
First Author: Iwahara J
Year: 1999
Journal: EMBO J
Title: Solution structure of the DNA binding domain from Dead ringer, a sequence-specific AT-rich interaction domain (ARID).
Volume: 18
Issue: 21
Pages: 6084-94
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Publication
11867548 | -
First Author: Iwahara J
Year: 2002
Journal: EMBO J
Title: The structure of the Dead ringer-DNA complex reveals how AT-rich interaction domains (ARIDs) recognize DNA.
Volume: 21
Issue: 5
Pages: 1197-209
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Publication
11959810 | -
First Author: Wilsker D
Year: 2002
Journal: Cell Growth Differ
Title: ARID proteins: a diverse family of DNA binding proteins implicated in the control of cell growth, differentiation, and development.
Volume: 13
Issue: 3
Pages: 95-106
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Publication
14722072 | -
First Author: Kim S
Year: 2004
Journal: J Biol Chem
Title: Structure and DNA-binding sites of the SWI1 AT-rich interaction domain (ARID) suggest determinants for sequence-specific DNA recognition.
Volume: 279
Issue: 16
Pages: 16670-6
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Protein
Q8CGM7
Organism: Mus musculus/domesticus
Length: 31  
Fragment?: true
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Protein
D3Z7U1
Organism: Mus musculus/domesticus
Length: 120  
Fragment?: true
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Protein Domain
IPR036431 | ARID_dom_sf
Type: Homologous_superfamily
Description: The AT-rich interaction domain (ARID) is an ~100-amino acid DNA-binding module found in a large number of eukaryotic transcription factors that regulate cellproliferation, differentiation and development [, ]. The ARID domain appearsas a single-copy motif and can be found in association with other domains,such as JmjC, JmjN, Tudor and PHD-type zinc finger [].The basic structure of the ARID domain domain appears to be a series of sixα-helices separated by β-strands, loops, or turns, but the structuredregion may extend to an additional helix at either or both ends of the basicsix. Based on primary sequence homology, they can be partitioned into threestructural classes:Minimal ARID proteins that consist of a core domain formed by six alpha-helices;ARID proteins that supplement the core domain with an N-terminal alpha-helix;Extended-ARID proteins, which contain the core domain and additional alpha-helices at their N- and C-termini.Minimal ARIDs are distributed in all eukaryotes, while extended ARIDs arerestricted to metazoans. The ARID domain binds DNA as a monomer, recognizingthe duplex through insertion of a loop and an α-helix into the majorgroove, and by extensive non-specific anchoring contacts to the adjacentsugar-phosphate backbone [, , ].Some proteins known to contain a ARID domain are listed below:Eukaryotic transcription factors of the jumonji family.Mammalian Bright, a B-cell-specific trans-activator of IgH transcription.Mammalian PLU-1, a protein that is upregulated in breast cancer cells.Mammalian RBP1 and RBP2, retinoblastoma binding factors.Mammalian Mrf-1 and Mrf-2, transcriptional modulators of thecytomegalovirus major intermediate-early promoter.Drosophila melanogaster Dead ringer protein, a transcriptional regulatoryprotein required for early embryonic development.Yeast SWI1 protein, from the SWI/SNF complex involved in chromatinremodeling and broad aspects of transcription regulation.Drosophila melanogaster Osa. It is structurally related to SWI1 andassociates with the brahma complex, which is the Drosophila equivalent ofthe SWI/SNF complex.
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Protein Domain
IPR001606 | ARID_dom
Type: Domain
Description: The AT-rich interaction domain (ARID) is an ~100-amino acid DNA-binding module found in a large number of eukaryotic transcription factors that regulate cellproliferation, differentiation and development [, ]. The ARID domain appearsas a single-copy motif and can be found in association with other domains,such as JmjC, JmjN, Tudor and PHD-type zinc finger [].The basic structure of the ARID domain domain appears to be a series of sixα-helices separated by β-strands, loops, or turns, but the structuredregion may extend to an additional helix at either or both ends of the basicsix. Based on primary sequence homology, they can be partitioned into threestructural classes:Minimal ARID proteins that consist of a core domain formed by six alpha-helices;ARID proteins that supplement the core domain with an N-terminal alpha-helix;Extended-ARID proteins, which contain the core domain and additional alpha-helices at their N- and C-termini.Minimal ARIDs are distributed in all eukaryotes, while extended ARIDs arerestricted to metazoans. The ARID domain binds DNA as a monomer, recognizingthe duplex through insertion of a loop and an α-helix into the majorgroove, and by extensive non-specific anchoring contacts to the adjacentsugar-phosphate backbone [, , ].Some proteins known to contain a ARID domain are listed below:Eukaryotic transcription factors of the jumonji family.Mammalian Bright, a B-cell-specific trans-activator of IgH transcription.Mammalian PLU-1, a protein that is upregulated in breast cancer cells.Mammalian RBP1 and RBP2, retinoblastoma binding factors.Mammalian Mrf-1 and Mrf-2, transcriptional modulators of thecytomegalovirus major intermediate-early promoter.Drosophila melanogaster Dead ringer protein, a transcriptional regulatoryprotein required for early embryonic development.Yeast SWI1 protein, from the SWI/SNF complex involved in chromatinremodeling and broad aspects of transcription regulation.Drosophila melanogaster Osa. It is structurally related to SWI1 andassociates with the brahma complex, which is the Drosophila equivalent ofthe SWI/SNF complex.
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Protein
E9PW42
Organism: Mus musculus/domesticus
Length: 240  
Fragment?: false
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Protein
Q62431
Organism: Mus musculus/domesticus
Length: 601  
Fragment?: false
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Protein
Q9Z1N7
Organism: Mus musculus/domesticus
Length: 568  
Fragment?: false
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Protein
A6PWV5
Organism: Mus musculus/domesticus
Length: 409  
Fragment?: false
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Protein
Q8BM75
Organism: Mus musculus/domesticus
Length: 1188  
Fragment?: false
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Protein
A0A087WR43
Organism: Mus musculus/domesticus
Length: 271  
Fragment?: false
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Protein
Q8CGG4
Organism: Mus musculus/domesticus
Length: 263  
Fragment?: true
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Protein
Q3UT97
Organism: Mus musculus/domesticus
Length: 137  
Fragment?: false
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Protein
Q3TRJ5
Organism: Mus musculus/domesticus
Length: 158  
Fragment?: false
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Protein
A0A0R4J1A7
Organism: Mus musculus/domesticus
Length: 599  
Fragment?: false
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Protein
Q05CE7
Organism: Mus musculus/domesticus
Length: 263  
Fragment?: true
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Protein
F8WIN2
Organism: Mus musculus/domesticus
Length: 536  
Fragment?: false
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Protein
Z4YMH1
Organism: Mus musculus/domesticus
Length: 540  
Fragment?: true
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Protein
Z4YL44
Organism: Mus musculus/domesticus
Length: 473  
Fragment?: false
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Protein
B2RWY2
Organism: Mus musculus/domesticus
Length: 568  
Fragment?: false
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Protein
Q3V3E9
Organism: Mus musculus/domesticus
Length: 215  
Fragment?: true
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Protein
G3UZT8
Organism: Mus musculus/domesticus
Length: 1029  
Fragment?: true
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Protein
Q3U4V8
Organism: Mus musculus/domesticus
Length: 264  
Fragment?: true
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Protein
B7ZP08
Organism: Mus musculus/domesticus
Length: 379  
Fragment?: false
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Protein
A0A1B0GRY1
Organism: Mus musculus/domesticus
Length: 85  
Fragment?: false
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Publication
1633439 | -
First Author: Weinmann R
Year: 1992
Journal: Gene Expr
Title: The basic RNA polymerase II transcriptional machinery.
Volume: 2
Issue: 2
Pages: 81-91
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Publication
8516312 | -
First Author: Buratowski S
Year: 1993
Journal: Proc Natl Acad Sci U S A
Title: Functional domains of transcription factor TFIIB.
Volume: 90
Issue: 12
Pages: 5633-7
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Publication
8504927 | -
First Author: Ha I
Year: 1993
Journal: Genes Dev
Title: Multiple functional domains of human transcription factor IIB: distinct interactions with two general transcription factors and RNA polymerase II.
Volume: 7
Issue: 6
Pages: 1021-32
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Publication
8564536 | -
First Author: Zhu W
Year: 1996
Journal: Nat Struct Biol
Title: The N-terminal domain of TFIIB from Pyrococcus furiosus forms a zinc ribbon.
Volume: 3
Issue: 2
Pages: 122-4
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Publication
15024075 | -
First Author: Tubon TC
Year: 2004
Journal: Mol Cell Biol
Title: A nonconserved surface of the TFIIB zinc ribbon domain plays a direct role in RNA polymerase II recruitment.
Volume: 24
Issue: 7
Pages: 2863-74
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Protein Domain
IPR013137 | Znf_TFIIB
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 represents a zinc finger motif found in transcription factor IIB (TFIIB). In eukaryotes the initiation of transcription of protein encoding genes by the polymerase II complexe (Pol II) is modulated by general and specific transcription factors. The general transcription factors operate through common promoters elements (such as the TATA box). At least seven different proteins associate to form the general transcription factors: TFIIA, -IIB, -IID, -IIE, -IIF, -IIG, and -IIH [].TFIIB and TFIID are responsible for promoter recognition and interaction with pol II; together with Pol II, they form a minimal initiation complex capable of transcription under certain conditions. The TATA box of a Pol II promoter is bound in the initiation complex by the TBP subunit of TFIID, which bends the DNA around the C-terminal domain of TFIIB whereas the N-terminal zinc finger of TFIIB interacts with Pol II [, ].The TFIIB zinc finger adopts a zinc ribbon fold characterised by two β-hairpins forming two structurally similar zinc-binding sub-sites []. The zinc finger contacts the rbp1 subunit of Pol II through its dock domain, a conserved region of about 70 amino acids located close to the polymerase active site []. In the Pol II complex this surface is located near the RNA exit groove. Interestingly this sequence is best conserved in the three polymerases that utilise a TFIIB-like general transcription factor (Pol II, Pol III, and archaeal RNA polymerase) but not in Pol I [].
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Protein
A2CG63
Organism: Mus musculus/domesticus
Length: 1314  
Fragment?: false
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Protein
E9Q4N7
Organism: Mus musculus/domesticus
Length: 2306  
Fragment?: false
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Protein
A2BH40
Organism: Mus musculus/domesticus
Length: 2283  
Fragment?: false
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Protein
Q62315
Organism: Mus musculus/domesticus
Length: 1234  
Fragment?: false
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Protein
Q1LZL9
Organism: Mus musculus/domesticus
Length: 914  
Fragment?: true
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Protein
A0A0N4SUK6
Organism: Mus musculus/domesticus
Length: 153  
Fragment?: true
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Protein
E9QAQ7
Organism: Mus musculus/domesticus
Length: 2287  
Fragment?: false
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Protein
E9Q9V1
Organism: Mus musculus/domesticus
Length: 531  
Fragment?: true
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Protein
A0A338P6U8
Organism: Mus musculus/domesticus
Length: 2296  
Fragment?: false
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Protein
E9Q4N6
Organism: Mus musculus/domesticus
Length: 1762  
Fragment?: false
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Protein
E9Q6R4
Organism: Mus musculus/domesticus
Length: 2243  
Fragment?: false
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Protein
E9Q7E2
Organism: Mus musculus/domesticus
Length: 1828  
Fragment?: false
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Protein
Q3UAW9
Organism: Mus musculus/domesticus
Length: 420  
Fragment?: false
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Protein
P62915
Organism: Mus musculus/domesticus
Length: 316  
Fragment?: false
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Protein
Q3UNY0
Organism: Mus musculus/domesticus
Length: 316  
Fragment?: false
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Protein
Q3UZJ3
Organism: Mus musculus/domesticus
Length: 316  
Fragment?: false
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Protein
A0A0R4J0C6
Organism: Mus musculus/domesticus
Length: 420  
Fragment?: false
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Protein
Q3ULN2
Organism: Mus musculus/domesticus
Length: 316  
Fragment?: false
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Protein
Q8BQM3
Organism: Mus musculus/domesticus
Length: 476  
Fragment?: false
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Protein
Q3TQL9
Organism: Mus musculus/domesticus
Length: 600  
Fragment?: false
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Protein
Q3URX5
Organism: Mus musculus/domesticus
Length: 399  
Fragment?: false
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Protein
Q8CFK2
Organism: Mus musculus/domesticus
Length: 676  
Fragment?: false
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Protein
G3X8S2
Organism: Mus musculus/domesticus
Length: 676  
Fragment?: false
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Protein
Q9D0D5
Organism: Mus musculus/domesticus
Length: 440  
Fragment?: false
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Protein
Q8BV40
Organism: Mus musculus/domesticus
Length: 421  
Fragment?: false
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Protein
Q3UXZ9
Organism: Mus musculus/domesticus
Length: 1690  
Fragment?: false
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Protein
P41230
Organism: Mus musculus/domesticus
Length: 1554  
Fragment?: false
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Protein
Q80Y84
Organism: Mus musculus/domesticus
Length: 1544  
Fragment?: false
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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