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Search results 1 to 100 out of 773 for 472

Category restricted to UniProtFeature (x)

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Categories

Category: UniProtFeature
Type Details Score
UniProt Feature
Begin: 472
Description: Nuclear localization signal 2
Type: short sequence motif
End: 479
UniProt Feature
Begin: 472
Description: In Ref. 4; AAL91174.
Type: sequence conflict
End: 472
UniProt Feature  
Begin: 472
Type: helix
End: 487
UniProt Feature
Begin: 472
Description: Contributes to redox potential value
Type: site
End: 472
UniProt Feature
Begin: 472
Description: In isoform 2.
Type: splice variant
End: 499
UniProt Feature  
Begin: 472
Type: binding site
End: 474
UniProt Feature
Begin: 472
Description: In isoform 2.
Type: splice variant
End: 488
UniProt Feature  
Begin: 472
Type: binding site
End: 472
UniProt Feature  
Begin: 472
Type: binding site
End: 472
UniProt Feature  
Begin: 472
Type: binding site
End: 472
UniProt Feature
Begin: 472
Description: Phosphothreonine
Type: modified residue
End: 472
UniProt Feature  
Begin: 472
Type: binding site
End: 474
UniProt Feature
Begin: 472
Description: Phosphothreonine
Type: modified residue
End: 472
UniProt Feature  
Begin: 472
Type: binding site
End: 476
UniProt Feature  
Begin: 472
Type: binding site
End: 472
UniProt Feature
Begin: 472
Description: Helical
Type: transmembrane region
End: 492
UniProt Feature
Begin: 472
Description: LRR 16
Type: repeat
End: 495
UniProt Feature  
Begin: 472
Type: binding site
End: 472
UniProt Feature  
Begin: 472
Type: binding site
End: 483
UniProt Feature
Begin: 472
Description: Proton acceptor
Type: active site
End: 472
UniProt Feature
Begin: 472
Description: Proton acceptor
Type: active site
End: 472
UniProt Feature
Begin: 472
Description: Proton acceptor
Type: active site
End: 472
UniProt Feature  
Begin: 472
Type: binding site
End: 472
UniProt Feature
Begin: 472
Description: EF-hand 4
Type: domain
End: 507
UniProt Feature
Begin: 472
Description: PLD phosphodiesterase 1
Type: domain
End: 499
UniProt Feature  
Begin: 472
Type: binding site
End: 472
UniProt Feature
Begin: 472
Description: Helical
Type: transmembrane region
End: 492
UniProt Feature  
Begin: 472
Type: binding site
End: 472
UniProt Feature  
Begin: 472
Type: binding site
End: 472
UniProt Feature
Begin: 472
Description: LRR 17
Type: repeat
End: 493
UniProt Feature  
Begin: 472
Type: binding site
End: 472
UniProt Feature  
Begin: 472
Type: strand
End: 477
UniProt Feature
Begin: 472
Description: N-linked (GlcNAc...) asparagine
Type: glycosylation site
End: 472
UniProt Feature
Begin: 472
Description: Lumenal
Type: topological domain
End: 482
UniProt Feature  
Begin: 472
Type: disulfide bond
End: 492
UniProt Feature
Begin: 472
Description: In Ref. 3; BAF00665.
Type: sequence conflict
End: 472
UniProt Feature  
Begin: 472
Type: binding site
End: 472
UniProt Feature  
Begin: 472
Type: binding site
End: 479
UniProt Feature
Begin: 472
Description: Proton acceptor
Type: active site
End: 472
UniProt Feature
Begin: 472
Description: Cytoplasmic
Type: topological domain
End: 514
UniProt Feature
Begin: 472
Description: PPR 8
Type: repeat
End: 506
UniProt Feature
Begin: 472
Description: Cytoplasmic
Type: topological domain
End: 496
UniProt Feature  
Begin: 472
Type: binding site
End: 472
UniProt Feature  
Begin: 472
Type: binding site
End: 472
UniProt Feature
Begin: 472
Description: In zif1-3; zinc sensitivity.
Type: mutagenesis site
End: 472
UniProt Feature
Begin: 472
Description: Proton acceptor
Type: active site
End: 472
UniProt Feature
Begin: 472
Description: PPR
Type: repeat
End: 506
UniProt Feature
Begin: 472
Description: Basic and acidic residues
Type: compositionally biased region
End: 486
UniProt Feature
Begin: 472
Description: Zinc finger PHD-type
Type: domain
End: 540
UniProt Feature
Begin: 472
Description: Basic and acidic residues
Type: compositionally biased region
End: 489
UniProt Feature
Begin: 472
Description: EF-hand
Type: domain
End: 507
UniProt Feature
Begin: 472
Description: Helical
Type: transmembrane region
End: 492
UniProt Feature
Begin: 472
Description: Disordered
Type: region of interest
End: 534
UniProt Feature
Begin: 472
Description: Polar residues
Type: compositionally biased region
End: 527
UniProt Feature
Begin: 472
Description: Disordered
Type: region of interest
End: 492
UniProt Feature
Begin: 472
Description: Disordered
Type: region of interest
End: 493
UniProt Feature
Begin: 472
Description: Polar residues
Type: compositionally biased region
End: 488
UniProt Feature
Begin: 472
Description: Helical
Type: transmembrane region
End: 493
UniProt Feature
Begin: 472
Description: Polar residues
Type: compositionally biased region
End: 486
UniProt Feature
Begin: 472
Description: Disordered
Type: region of interest
End: 501
UniProt Feature
Begin: 472
Description: Acidic residues
Type: compositionally biased region
End: 490
UniProt Feature
Begin: 472
Description: PPR
Type: repeat
End: 506
UniProt Feature
Begin: 472
Description: Basic and acidic residues
Type: compositionally biased region
End: 501
UniProt Feature
Begin: 472
Description: PPR
Type: repeat
End: 506
UniProt Feature
Begin: 472
Description: Basic and acidic residues
Type: compositionally biased region
End: 505
UniProt Feature
Begin: 472
Description: Pumilio
Type: repeat
End: 509
UniProt Feature
Begin: 472
Description: Basic and acidic residues
Type: compositionally biased region
End: 496
UniProt Feature  
Begin: 472
Type: binding site
End: 472
UniProt Feature
Begin: 472
Description: PPR
Type: repeat
End: 506
UniProt Feature
Begin: 472
Description: Helical
Type: transmembrane region
End: 496
UniProt Feature
Begin: 472
Description: Disordered
Type: region of interest
End: 505
UniProt Feature
Begin: 472
Description: Helical
Type: transmembrane region
End: 492
UniProt Feature
Begin: 472
Description: EF-hand
Type: domain
End: 507
UniProt Feature
Begin: 472
Description: RRM
Type: domain
End: 549
UniProt Feature
Begin: 472
Description: Polar residues
Type: compositionally biased region
End: 488
UniProt Feature
Begin: 472
Description: Disordered
Type: region of interest
End: 493
UniProt Feature
Begin: 472
Description: Basic and acidic residues
Type: compositionally biased region
End: 505
UniProt Feature
Begin: 472
Description: Basic and acidic residues
Type: compositionally biased region
End: 501
UniProt Feature
Begin: 472
Description: HTH myb-type
Type: domain
End: 529
UniProt Feature
Begin: 472
Description: Disordered
Type: region of interest
End: 492
UniProt Feature
Begin: 472
Description: Helical
Type: transmembrane region
End: 496
UniProt Feature  
Begin: 472
Type: binding site
End: 472
UniProt Feature
Begin: 472
Description: Helical
Type: transmembrane region
End: 493
UniProt Feature
Begin: 472
Description: Helical
Type: transmembrane region
End: 493
UniProt Feature
Begin: 472
Description: Polar residues
Type: compositionally biased region
End: 494
UniProt Feature
Begin: 472
Description: Polar residues
Type: compositionally biased region
End: 494
UniProt Feature
Begin: 472
Description: Polar residues
Type: compositionally biased region
End: 494
UniProt Feature
Begin: 472
Description: Disordered
Type: region of interest
End: 516
UniProt Feature
Begin: 472
Description: Acidic residues
Type: compositionally biased region
End: 508
UniProt Feature
Begin: 472
Description: PHD-type
Type: domain
End: 517
UniProt Feature
Begin: 472
Description: Disordered
Type: region of interest
End: 498
UniProt Feature
Begin: 472
Description: PPR
Type: repeat
End: 506
UniProt Feature
Begin: 472
Description: PPR
Type: repeat
End: 506
UniProt Feature
Begin: 472
Description: PPR
Type: repeat
End: 506
UniProt Feature
Begin: 472
Description: Basic and acidic residues
Type: compositionally biased region
End: 490
UniProt Feature  
Begin: 472
Type: binding site
End: 472
UniProt Feature
Begin: 472
Description: Disordered
Type: region of interest
End: 493
UniProt Feature
Begin: 472
Description: Polar residues
Type: compositionally biased region
End: 488
UniProt Feature
Begin: 472
Description: EF-hand
Type: domain
End: 507
UniProt Feature
Begin: 472
Description: Helicase C-terminal
Type: domain
End: 624