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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
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Type Details Score
UniProt Feature
UniProt Feature
 
Begin: 472
Type: helix
End: 476
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UniProt Feature
UniProt Feature
 
Begin: 472
Type: helix
End: 476
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UniProt Feature
UniProt Feature
Begin: 472
Description: ADD
Type: domain
End: 601
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UniProt Feature
UniProt Feature
 
Begin: 472
Type: binding site
End: 472
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UniProt Feature
UniProt Feature
Begin: 472
Description: DEVH box
Type: short sequence motif
End: 475
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UniProt Feature
UniProt Feature
Begin: 472
Description: N-linked (GlcNAc...) asparagine
Type: glycosylation site
End: 472
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UniProt Feature
UniProt Feature
Begin: 472
Description: N-linked (GlcNAc...) asparagine
Type: glycosylation site
End: 472
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UniProt Feature
UniProt Feature
Begin: 472
Description: Proton acceptor
Type: active site
End: 472
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UniProt Feature
UniProt Feature
Begin: 472
Description: Helical
Type: transmembrane region
End: 492
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UniProt Feature
UniProt Feature
Begin: 472
Description: Phosphothreonine
Type: modified residue
End: 472
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UniProt Feature
UniProt Feature
Begin: 472
Description: EF-hand 3
Type: domain
End: 507
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UniProt Feature
UniProt Feature
 
Begin: 472
Type: turn
End: 474
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UniProt Feature
UniProt Feature
Begin: 472
Description: PPR 13
Type: repeat
End: 502
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UniProt Feature
UniProt Feature
Begin: 472
Description: Extracellular
Type: topological domain
End: 485
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UniProt Feature
UniProt Feature
Begin: 472
Description: In strain: cv. BG-4, cv. KNO2, cv. Po-1 and cv. Zu-0.
Type: sequence variant
End: 472
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UniProt Feature
UniProt Feature
Begin: 472
Description: In Ref. 2; AAC49807 and 3; AAC17732.
Type: sequence conflict
End: 473
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UniProt Feature
UniProt Feature
 
Begin: 472
Type: binding site
End: 472
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UniProt Feature
UniProt Feature
 
Begin: 472
Type: binding site
End: 472
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UniProt Feature
UniProt Feature
Begin: 472
Description: Helical; Name=12
Type: transmembrane region
End: 492
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UniProt Feature
UniProt Feature
 
Begin: 472
Type: strand
End: 485
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UniProt Feature
UniProt Feature
Begin: 472
Description: N-linked (GlcNAc...) asparagine
Type: glycosylation site
End: 472
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UniProt Feature
UniProt Feature
 
Begin: 472
Type: binding site
End: 472
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UniProt Feature
UniProt Feature
 
Begin: 472
Type: binding site
End: 472
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UniProt Feature
UniProt Feature
Begin: 472
Description: WD 10
Type: repeat
End: 512
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UniProt Feature
UniProt Feature
Begin: 472
Description: No effect on the recruitment of ADO3 to the cytoplasm; when associated with R-283; R-335; R-410; R-463 and R-553.
Type: mutagenesis site
End: 472
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UniProt Feature
UniProt Feature
 
Begin: 472
Type: binding site
End: 472
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UniProt Feature
UniProt Feature
Begin: 472
Description: Helical
Type: transmembrane region
End: 492
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UniProt Feature
UniProt Feature
 
Begin: 472
Type: helix
End: 481
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UniProt Feature
UniProt Feature
Begin: 472
Description: Bromo
Type: domain
End: 543
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UniProt Feature
UniProt Feature
Begin: 472
Description: Proton acceptor
Type: active site
End: 472
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UniProt Feature
UniProt Feature
Begin: 472
Description: Triggers nucleus envelope localization
Type: region of interest
End: 548
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UniProt Feature
UniProt Feature
Begin: 472
Description: Nuclear localization signal 2
Type: short sequence motif
End: 479
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UniProt Feature
UniProt Feature
Begin: 472
Description: In Ref. 4; AAL91174.
Type: sequence conflict
End: 472
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UniProt Feature
UniProt Feature
 
Begin: 472
Type: helix
End: 487
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UniProt Feature
UniProt Feature
Begin: 472
Description: Contributes to redox potential value
Type: site
End: 472
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UniProt Feature
UniProt Feature
Begin: 472
Description: In isoform 2.
Type: splice variant
End: 499
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UniProt Feature
UniProt Feature
 
Begin: 472
Type: binding site
End: 474
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UniProt Feature
UniProt Feature
Begin: 472
Description: In isoform 2.
Type: splice variant
End: 488
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UniProt Feature
UniProt Feature
 
Begin: 472
Type: binding site
End: 472
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UniProt Feature
UniProt Feature
 
Begin: 472
Type: binding site
End: 472
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UniProt Feature
UniProt Feature
 
Begin: 472
Type: binding site
End: 472
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UniProt Feature
UniProt Feature
Begin: 472
Description: Phosphothreonine
Type: modified residue
End: 472
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UniProt Feature
UniProt Feature
 
Begin: 472
Type: binding site
End: 474
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UniProt Feature
UniProt Feature
Begin: 472
Description: Phosphothreonine
Type: modified residue
End: 472
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UniProt Feature
UniProt Feature
 
Begin: 472
Type: binding site
End: 476
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UniProt Feature
UniProt Feature
 
Begin: 472
Type: binding site
End: 472
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UniProt Feature
UniProt Feature
Begin: 472
Description: Helical
Type: transmembrane region
End: 492
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UniProt Feature
UniProt Feature
Begin: 472
Description: LRR 16
Type: repeat
End: 495
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UniProt Feature
UniProt Feature
 
Begin: 472
Type: binding site
End: 472
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UniProt Feature
UniProt Feature
 
Begin: 472
Type: binding site
End: 483
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UniProt Feature
UniProt Feature
Begin: 472
Description: Proton acceptor
Type: active site
End: 472
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UniProt Feature
UniProt Feature
Begin: 472
Description: Proton acceptor
Type: active site
End: 472
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UniProt Feature
UniProt Feature
Begin: 472
Description: Proton acceptor
Type: active site
End: 472
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UniProt Feature
UniProt Feature
 
Begin: 472
Type: binding site
End: 472
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UniProt Feature
UniProt Feature
Begin: 472
Description: EF-hand 4
Type: domain
End: 507
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UniProt Feature
UniProt Feature
Begin: 472
Description: PLD phosphodiesterase 1
Type: domain
End: 499
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UniProt Feature
UniProt Feature
 
Begin: 472
Type: binding site
End: 472
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UniProt Feature
UniProt Feature
Begin: 472
Description: Helical
Type: transmembrane region
End: 492
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UniProt Feature
UniProt Feature
 
Begin: 472
Type: binding site
End: 472
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UniProt Feature
UniProt Feature
 
Begin: 472
Type: binding site
End: 472
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UniProt Feature
UniProt Feature
Begin: 472
Description: LRR 17
Type: repeat
End: 493
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UniProt Feature
UniProt Feature
 
Begin: 472
Type: binding site
End: 472
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UniProt Feature
UniProt Feature
 
Begin: 472
Type: strand
End: 477
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UniProt Feature
UniProt Feature
Begin: 472
Description: N-linked (GlcNAc...) asparagine
Type: glycosylation site
End: 472
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UniProt Feature
UniProt Feature
Begin: 472
Description: Lumenal
Type: topological domain
End: 482
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UniProt Feature
UniProt Feature
 
Begin: 472
Type: disulfide bond
End: 492
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UniProt Feature
UniProt Feature
Begin: 472
Description: In Ref. 3; BAF00665.
Type: sequence conflict
End: 472
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UniProt Feature
UniProt Feature
 
Begin: 472
Type: binding site
End: 472
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UniProt Feature
UniProt Feature
 
Begin: 472
Type: binding site
End: 479
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UniProt Feature
UniProt Feature
Begin: 472
Description: Proton acceptor
Type: active site
End: 472
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UniProt Feature
UniProt Feature
Begin: 472
Description: Cytoplasmic
Type: topological domain
End: 514
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UniProt Feature
UniProt Feature
Begin: 472
Description: PPR 8
Type: repeat
End: 506
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UniProt Feature
UniProt Feature
Begin: 472
Description: Cytoplasmic
Type: topological domain
End: 496
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UniProt Feature
UniProt Feature
 
Begin: 472
Type: binding site
End: 472
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UniProt Feature
UniProt Feature
 
Begin: 472
Type: binding site
End: 472
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UniProt Feature
UniProt Feature
Begin: 472
Description: In zif1-3; zinc sensitivity.
Type: mutagenesis site
End: 472
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UniProt Feature
UniProt Feature
Begin: 472
Description: Proton acceptor
Type: active site
End: 472
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UniProt Feature
UniProt Feature
Begin: 472
Description: N-linked (GlcNAc...) asparagine
Type: glycosylation site
End: 472
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UniProt Feature
UniProt Feature
 
Begin: 472
Type: binding site
End: 472
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UniProt Feature
UniProt Feature
Begin: 472
Description: Disordered
Type: region of interest
End: 494
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UniProt Feature
UniProt Feature
Begin: 472
Description: Proton acceptor
Type: active site
End: 472
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UniProt Feature
UniProt Feature
Begin: 472
Description: Removed in mature form
Type: propeptide
End: 506
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UniProt Feature
UniProt Feature
Begin: 472
Description: type 3 copper site
Type: binding site
End: 472
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UniProt Feature
UniProt Feature
 
Begin: 472
Type: helix
End: 474
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UniProt Feature
UniProt Feature
Begin: 472
Description: Nuclear export signal
Type: short sequence motif
End: 480
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UniProt Feature
UniProt Feature
Begin: 472
Description: Proton acceptor
Type: active site
End: 472
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UniProt Feature
UniProt Feature
 
Begin: 472
Type: helix
End: 477
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UniProt Feature
UniProt Feature
Begin: 472
Description: Disordered
Type: region of interest
End: 545
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UniProt Feature
UniProt Feature
Begin: 472
Description: N-linked (GlcNAc...) asparagine
Type: glycosylation site
End: 472
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UniProt Feature
UniProt Feature
 
Begin: 472
Type: helix
End: 474
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UniProt Feature
UniProt Feature
Begin: 472
Description: Polar residues
Type: compositionally biased region
End: 513
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UniProt Feature
UniProt Feature
Begin: 472
Description: type 1 copper site
Type: binding site
End: 472
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UniProt Feature
UniProt Feature
Begin: 472
Description: Kinesin motor
Type: domain
End: 800
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UniProt Feature
UniProt Feature
Begin: 472
Description: Basic and acidic residues
Type: compositionally biased region
End: 499
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UniProt Feature
UniProt Feature
 
Begin: 472
Type: binding site
End: 479
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UniProt Feature
UniProt Feature
 
Begin: 472
Type: coiled-coil region
End: 534
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UniProt Feature
UniProt Feature
Begin: 472
Description: Polar residues
Type: compositionally biased region
End: 488
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UniProt Feature
UniProt Feature
Begin: 472
Description: Extracellular
Type: topological domain
End: 477
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UniProt Feature
UniProt Feature
Begin: 472
Description: Helical
Type: transmembrane region
End: 492
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UniProt Feature
UniProt Feature
 
Begin: 472
Type: helix
End: 477
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