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Conserved domains on  [gi|209870086|ref|NP_001129587|]
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F-box only protein 28 isoform b [Homo sapiens]

Protein Classification

F-box only protein 28( domain architecture ID 17778309)

F-box only protein 28 (FBXO28) may recognize and bind to some phosphorylated proteins and promotes their ubiquitination and degradation

CATH:  1.20.1280.50
Gene Ontology:  GO:0005515|GO:0000209
PubMed:  31898225|11178263
SCOP:  4001927

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
F-box_FBXO28 cd22100
F-box domain found in F-box only protein 28 (FBXO28) and similar proteins; FBXO28, also called ...
 64-108 1.28e-20

F-box domain found in F-box only protein 28 (FBXO28) and similar proteins; FBXO28, also called FBX28, is part of an SCF (SKP1-cullin-F-box) protein ligase complex. It probably recognizes and binds to some phosphorylated proteins and promotes their ubiquitination and degradation. It promotes mitotic progression and regulates topoisomerase IIalpha-dependent DNA decatenation. FBXO28 plays a crucial role in the pathogenesis of the 1q41q42 microdeletion syndrome. The F-box domain has a role in mediating protein-protein interactions in a variety of contexts, such as polyubiquitination, transcription elongation, centromere binding and translational repression.


:

Pssm-ID: 438872  Cd Length: 45  Bit Score: 79.90  E-value: 1.28e-20
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*
gi 209870086  64 LVALPIVAIENILSFMSYDEISQLRLVCKRMDLVCQRMLNQGFLK 108
Cdd:cd22100    1 LLELPDEIIEKILSYLSYDEISKLRLVCRRFNEVCQRILNQGFKK 45
 
Name Accession Description Interval E-value
F-box_FBXO28 cd22100
F-box domain found in F-box only protein 28 (FBXO28) and similar proteins; FBXO28, also called ...
 64-108 1.28e-20

F-box domain found in F-box only protein 28 (FBXO28) and similar proteins; FBXO28, also called FBX28, is part of an SCF (SKP1-cullin-F-box) protein ligase complex. It probably recognizes and binds to some phosphorylated proteins and promotes their ubiquitination and degradation. It promotes mitotic progression and regulates topoisomerase IIalpha-dependent DNA decatenation. FBXO28 plays a crucial role in the pathogenesis of the 1q41q42 microdeletion syndrome. The F-box domain has a role in mediating protein-protein interactions in a variety of contexts, such as polyubiquitination, transcription elongation, centromere binding and translational repression.


Pssm-ID: 438872  Cd Length: 45  Bit Score: 79.90  E-value: 1.28e-20
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*
gi 209870086  64 LVALPIVAIENILSFMSYDEISQLRLVCKRMDLVCQRMLNQGFLK 108
Cdd:cd22100    1 LLELPDEIIEKILSYLSYDEISKLRLVCRRFNEVCQRILNQGFKK 45
F-box pfam00646
F-box domain; This domain is approximately 50 amino acids long, and is usually found in the ...
 67-94 2.16e-03

F-box domain; This domain is approximately 50 amino acids long, and is usually found in the N-terminal half of a variety of proteins. Two motifs that are commonly found associated with the F-box domain are the leucine rich repeats (LRRs; pfam00560 and pfam07723) and the WD repeat (pfam00400). The F-box domain has a role in mediating protein-protein interactions in a variety of contexts, such as polyubiquitination, transcription elongation, centromere binding and translational repression.


Pssm-ID: 425796  Cd Length: 43  Bit Score: 34.44  E-value: 2.16e-03
                          10        20
                  ....*....|....*....|....*...
gi 209870086   67 LPIVAIENILSFMSYDEISQLRLVCKRM 94
Cdd:pfam00646   4 LPDDLLLEILSRLDPKDLLRLSLVSKRW 31
 
Name Accession Description Interval E-value
F-box_FBXO28 cd22100
F-box domain found in F-box only protein 28 (FBXO28) and similar proteins; FBXO28, also called ...
 64-108 1.28e-20

F-box domain found in F-box only protein 28 (FBXO28) and similar proteins; FBXO28, also called FBX28, is part of an SCF (SKP1-cullin-F-box) protein ligase complex. It probably recognizes and binds to some phosphorylated proteins and promotes their ubiquitination and degradation. It promotes mitotic progression and regulates topoisomerase IIalpha-dependent DNA decatenation. FBXO28 plays a crucial role in the pathogenesis of the 1q41q42 microdeletion syndrome. The F-box domain has a role in mediating protein-protein interactions in a variety of contexts, such as polyubiquitination, transcription elongation, centromere binding and translational repression.


Pssm-ID: 438872  Cd Length: 45  Bit Score: 79.90  E-value: 1.28e-20
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*
gi 209870086  64 LVALPIVAIENILSFMSYDEISQLRLVCKRMDLVCQRMLNQGFLK 108
Cdd:cd22100    1 LLELPDEIIEKILSYLSYDEISKLRLVCRRFNEVCQRILNQGFKK 45
F-box pfam00646
F-box domain; This domain is approximately 50 amino acids long, and is usually found in the ...
 67-94 2.16e-03

F-box domain; This domain is approximately 50 amino acids long, and is usually found in the N-terminal half of a variety of proteins. Two motifs that are commonly found associated with the F-box domain are the leucine rich repeats (LRRs; pfam00560 and pfam07723) and the WD repeat (pfam00400). The F-box domain has a role in mediating protein-protein interactions in a variety of contexts, such as polyubiquitination, transcription elongation, centromere binding and translational repression.


Pssm-ID: 425796  Cd Length: 43  Bit Score: 34.44  E-value: 2.16e-03
                          10        20
                  ....*....|....*....|....*...
gi 209870086   67 LPIVAIENILSFMSYDEISQLRLVCKRM 94
Cdd:pfam00646   4 LPDDLLLEILSRLDPKDLLRLSLVSKRW 31
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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