Javascript is not enabled on this browser. This site will not work properly without Javascript.
PhosphoSitePlus Homepage Cell Signaling Technology
PhosphoSitePlus
HomeAbout PhosphoSiteUsing PhosphoSiteCuration ProcessContact
NIH-logos NIGMS Logo NIAAA Logo NCI Logo NIH Logo
Protein Page:
FANCA (human)
p Phosphorylation
a Acetylation
m Methylation
m1 Mono-methylation
m2 Di-methylation
m3 Tri-methylation
u Ubiquitination
s Sumoylation
n Neddylation
gl O-GlcNAc
ga O-GalNAc
h Palmitoylation
ad Adenylylation
sn S-Nitrosylation
ca Caspase cleavage

Overview
FANCA DNA repair protein that may operate in a postreplication repair or a cell cycle checkpoint function. May be involved in interstrand DNA cross-link repair and in the maintenance of normal chromosome stability. Defects in FANCA are a cause of Fanconi anemia (FA). FA is a genetically heterogeneous, autosomal recessive disorder characterized by progressive pancytopenia, a diverse assortment of congenital malformations, 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. 2 isoforms of the human protein are produced by alternative splicing. Note: This description may include information from UniProtKB.
Protein type: DNA repair, damage
Cellular Component: nucleoplasm; cytoplasm; nucleolus; nucleus
Molecular Function: protein binding
Biological Process: male gonad development; protein complex assembly; DNA repair; male meiosis; female gonad development; regulation of cell proliferation
Reference #:  O15360 (UniProtKB)
Alt. Names/Synonyms: FA; FA-H; FA1; FAA; FACA; FAH; FANCA; FANCH; Fanconi anemia group A protein; Fanconi anemia, complementation group A; Fanconi anemia, complementation group H; Fanconi anemia, type 1; MGC75158; Protein FACA
Gene Symbols: FANCA
Molecular weight: 162,775 Da
Basal Isoelectric point: 6.13  Predict pI for various phosphorylation states
Select Structure to View Below

FANCA

Protein Structure Not Found.


STRING  |  Scansite  |  Phospho.ELM  |  NetworKIN  |  Pfam  |  DISEASE  |  Source  |  GeneCards  |  UniProtKB  |  Entrez-Gene  |  Ensembl Gene


Sites Implicated In
chromatin organization, altered: S1449‑p
molecular association, regulation: S1149‑p, S1449‑p
ubiquitination: S1449‑p

Modification Sites and Domains Show Modification Legend
Click here to view phosphorylation modifications only

Modification Sites in Parent Protein, Orthologs, and Isoforms Show Modification Legend
 

Show Multiple Sequence Alignment


 SS 

SS: 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.


 MS 

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


       human

 
0 1 K44-u PERAQKLkESAVRLL
0 1 S46 RAQKLkESAVRLLRS
0 1 K249-u FVLRGFQkNSDLRRT
0 1 K261-u RRTVEPEkMPQVTVD
0 1 K335-u LTHSPVLkASDAVQM
1 1 T351-p REWSFARtHPLLTSL
0 2 K515-u TDYISLAkTRLADLk
0 1 K522-u kTRLADLkVSIENMG
0 1 S536 GLYEDLSSAGDITEP
0 1 K608-u VAFIESLkRADKIPP
0 1 K701-u DSSVEISkIQLSINT
0 1 M1077 QRQRELLMYKRILLR
1 0 S1149-p CLRSRDPsLMVDFIL
0 2 K1199-u PLPRELQkLQEGRQF
0 1 K1387-u AGRSLELkGQGNPVE
0 1 K1398-u NPVELITkARLFLLQ
1 21 S1449-p AAPDADLsQEPHLF_
  mouse

 
K44 PEREQKLKDsALKLL
S46-p REQKLKDsALKLLRY
G246 LISRGFQGSSDPRRL
R258 RRLVEPERLPQVATD
K331 LTHKPVLKVSDAIQM
T347 KEWSFAKTHHLLTDL
K511 TDYISLAKTRLADLK
K518 KTRLADLKVSLENVG
S532-p GLYEDLSsPGDIAER
K604 VALIETLKRADKIPS
K698 GGSLQRAKIQLSVLP
T1071-p RRQQELLtCKRLLLC
A1142 CLRSQDPALVANQTL
R1192 PLPRELRRLQEAREF
- gap
K1382 SPVQLITKARVFLLQ
Y1433 ADPSFDLYQEPQLF_
Home  |  Curator Login With enhanced literature mining using Linguamatics I2E I2E Logo Produced by 3rd Millennium  |  Design by Digizyme
©2003-2013 Cell Signaling Technology, Inc.