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Protein Page:
FANCB (human)

Overview
FANCB DNA repair protein required for FANCD2 ubiquitination. Defects in FANCB are the cause of Fanconi anemia complementation group B (FANCB). It is a disorder affecting all bone marrow elements and resulting in anemia, leukopenia and thrombopenia. It is associated with cardiac, renal and limb malformations, dermal pigmentary changes, and a predisposition to the development of malignancies. At the cellular level it is associated with hypersensitivity to DNA-damaging agents, chromosomal instability (increased chromosome breakage) and defective DNA repair. Some severe FANCB cases manifest features of VACTERL syndrome with hydrocephalus. Note: This description may include information from UniProtKB.
Chromosomal Location of Human Ortholog: Xp22.2
Cellular Component: nucleoplasm
Molecular Function: protein binding
Biological Process: DNA repair
Disease: Fanconi Anemia, Complementation Group B; Tracheoesophageal Fistula With Or Without Esophageal Atresia; Vacterl Association, X-linked, With Or Without Hydrocephalus
Reference #:  Q8NB91 (UniProtKB)
Alt. Names/Synonyms: FA2; FAAP90; FAAP95; FAB; FACB; FANCB; Fanconi anemia group B protein; Fanconi anemia, complementation group B; Fanconi anemia-associated polypeptide of 95 kDa; Protein FACB; type 2 Fanconi pancytopenia
Gene Symbols: FANCB
Molecular weight: 97,726 Da
Basal Isoelectric point: 7.79  Predict pI for various phosphorylation states
Protein-Specific Antibodies or siRNAs from Cell Signaling Technology® Total Proteins
Select Structure to View Below

FANCB

Protein Structure Not Found.


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Modification Sites and Domains  

Modification Sites in Parent Protein, Orthologs, and Isoforms  
 

Show Multiple Sequence Alignment


 LTP 

LTP: The number of records in which this modification site was determined using site-specific methods. SS methods include amino acid sequencing, site-directed mutagenesis, modification site-specific antibodies, specific MS strategies, etc.


 HTP 

HTP: The number of records in which this modification site was assigned using ONLY proteomic discovery-mode mass spectrometry.


       human

 
0 1 Y205‑p QEPSKSDyAIWNTKF
0 1 S456‑p LCGEEENsVHILDEK
0 1 S465‑p HILDEKLsDNFQDSE
0 4 T555‑p EAKRVTLtPDSKKEE
0 1 S795‑p CEVSKGKssVVAAAL
0 1 S796‑p EVSKGKssVVAAALs
0 1 S803‑p sVVAAALsDRRENIH
0 1 T839‑p GALYREItLKVAEVQ
  mouse

 
Y196 QKLSESDYEFSNSSL
S450 FCDEGEDSVPTPEEN
P459 PTPEENLPDNFPEPE
- gap
N638 CRIRRTDNRAMTFLG
- gap
L644 DNRAMTFLGRRAKIR
T679 GSSYAEMTLALAEIQ
  rat

 
Y201 RKLSESDYEFSNSSF
S455 FCDEDENSVPTPEEN
P464 PTPEENLPDNFPEPE
T552 EIKRMKLTSGSQEEE
N792 CSTSKTDNRATTFSG
- gap
S798 DNRATTFSGRRAKIR
T833 VSSYAEMTLALAEIQ
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