Protein detail

CYBR1

Plasma membrane ascorbate-dependent reductase CYBRD1 (EC 7.2.1.3) (Cytochrome b reductase 1) (Duodenal cytochrome b) (Ferric-chelate reductase 3)

Entry name
CYBR1
UniProt ID
Q53TN4
EVMP confidence score
0.53
Supporting publications (n)
1
Transmembrane count
6
Protein classification
EnzymesMetabolic proteinsPredicted membrane proteinsTransporters
Basic Information
Protein Names
Plasma membrane ascorbate-dependent reductase CYBRD1 (EC 7.2.1.3) (Cytochrome b reductase 1) (Duodenal cytochrome b) (Ferric-chelate reductase 3)
Protein Class (4)
EnzymesMetabolic proteinsPredicted membrane proteinsTransporters
Protein Function (3)
  • Transporters:Transport Electron Carriers
  • Enzymes
  • ENZYME proteins
Transmembrane
8..32; Helical; Name=1; 48..69; Helical; Name=2; 79..105; Helical; Name=3; 119..144; Helical; Name=4; 152..179; Helical; Name=5; 198..222; Helical; Name=6
Transmembrane Count
6
Ensembl
ENSG00000071967
Entrez Gene Symbol
CYBRD1
Gene Synonym (4)
CYB561A2DCYTBFLJ23462FRRS3
Gene Description
Cytochrome b reductase 1
Chromosome
2
Position
171522247-171558129
Supporting publications (n)
1
EVMP confidence score
0.53
Fluorescence & Localization
Cell SpecificEpendymal cellsSingle-Nuclei Brain Specificependymal cell
Function & Pathway
Protein Function (3)
  • Transporters:Transport Electron Carriers
  • Enzymes
  • ENZYME proteins
Cellular Component (6)
Molecular Function (7)
Biological Process (3)
KEGG
hsa04978 Mineral absorption
Reactome (2)
Canonical Pathways (3)
  • M16801 Sig regulation of the actin cytoskeleton by rho gtpases
  • M5193 Sig chemotaxis
  • M276 Pid fgf pathway
Mediation Categories (2)
Fusion and delivery mediationMetabolism mediation
Relations & Evidence18

Ligand-Receptor Signaling (13)

13 records.

CategoryParentDatabaseTransmitterReceiverSecretedPlasma Membrane (Transmembrane)Plasma Membrane (Peripheral)
intracellularintracellularComPPI
intracellularintracellularGO_Intercell
intracellularintracellularOmniPath
transmembranetransmembraneUniProt_location
transmembranetransmembraneUniProt_topology
transmembranetransmembraneUniProt_keyword
transmembranetransmembraneTopDB
transmembranetransmembraneRamilowski_location
transmembranetransmembraneOmniPath
plasma_membraneplasma_membraneUniProt_location
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Protein Complex Composition (4)

4 records.

Component NameComponent Gene SymbolsComponent UniProt IDStoichiometryDatabaseDatabase IDsReferences
CDYLCDYL2CYBRD1MIER1MIER2Q53TN4Q8N108Q8N344Q8N8U2Q9Y2320:0:0:0:0hu.MAP2
CDYLCYBRD1MIER1Q53TN4Q8N108Q9Y2320:0:0hu.MAP2
CDYLCDYL2CYBRD1MIER2Q53TN4Q8N344Q8N8U2Q9Y2320:0:0:0hu.MAP2
CDYLCYBRD1Q53TN4Q9Y2320:0hu.MAP2

Isolation & Detection Technology (1)

1 record.

EV Isolation MethodDetection MethodNumber of ReferencesReferences
Differential UltracentrifugationSize Exclusion ChromatographyImmunoaffinity CaptureMass spectrometry [LTQ-FT Ultra]113786238131508500398737264106344138731868306087004009834630760538369823124031161640091455
Sequence, Structure & Domains

Sequences

Length
286
Mass
31,641
Sequence
MAMEGYWRFLALLGSALLVGFLSVIFALVWVLHYREGLGWDGSALEFNWHPVLMVTGFVFIQGIAIIVYRLPWTWKCSKLLMKSIHAGLNAVAAILAIISVVAVFENHNVNNIANMYSLHSWVGLIAVICYLLQLLSGFSVFLLPWAPLSLRAFLMPIHVYSGIVIFGTVIATALMGLTEKLIFSLRDPAYSTFPPEGVFVNTLGLLILVFGALIFWIVTRPQWKRPKEPNSTILHPNGGTEQGARGSMPAYSGNNMDKSDSELNSEVAARKRNLALDEAGQRSTM
Alternative Products
Event=Alternative splicing; Named isoforms=3; Name=1; IsoId=Q53TN4-1; Sequence=Displayed; Name=2; IsoId=Q53TN4-2; Sequence=VSP_042039; Name=3; IsoId=Q53TN4-3; Sequence=VSP_044945
Alternative Sequence
1..64; MAMEGYWRFLALLGSALLVGFLSVIFALVWVLHYREGLGWDGSALEFNWHPVLMVTGFVFIQGI -> MLDEGE (in isoform 3); 66..286; IIVYRLPWTWKCSKLLMKSIHAGLNAVAAILAIISVVAVFENHNVNNIANMYSLHSWVGLIAVICYLLQLLSGFSVFLLPWAPLSLRAFLMPIHVYSGIVIFGTVIATALMGLTEKLIFSLRDPAYSTFPPEGVFVNTLGLLILVFGALIFWIVTRPQWKRPKEPNSTILHPNGGTEQGARGSMPAYSGNNMDKSDSELNSEVAARKRNLALDEAGQRSTM -> SFRFFSLSASMGSAFSPSISHAHTCLFWNCHLWNSDCNSTYGIDRETDFFPERSCIQYIPARRCFRKYAWPSDPGVRGPHFLDSHQTAMETS (in isoform 2)

3D Structural Models

Turn
187..190
Helix
7..33; 44..47; 49..57; 60..66; 67..70; 72..74; 79..111; 119..142; 149..185; 191..193; 196..219; 222..224
Beta Strand
40..43
3D Structure
X-ray crystallography (2)

Domain & Motif Annotations

Domain (FT)
15..220; Cytochrome b561
Region
229..268; Disordered
Clinical Relevance
Antibody
HPA014757
Supporting Publications1
PMIDTitleRelated sentences
37459063Phosphorylation of αB-Crystallin Involves Interleukin-1β-Mediated Intracellular Retention in Retinal Müller Cells: A New Mechanism Underlying Fibrovascular Membrane Formation.The phosphorylation of αB-crystallin/CRYAB modulates its molecular dynamics and chaperone activity, and attenuates αB-crystallin secretion via exosomes.