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Protein Page:
pyrin (human)

Overview
pyrin Probably controls the inflammatory response in myelomonocytic cells at the level of the cytoskeleton organization. Defects in MEFV are the cause of familial Mediterranean fever autosomal recessive (ARFMF). ARFMF is an inherited disorder characterized by recurrent episodic fever, serosal inflammation and pain in the abdomen, chest or joints. ARFMF is frequently complicated by amyloidosis, which leads to renal failure and can be prophylactically treated with colchicine. ARFMF primarily affects ancestral ethnic groups living around the Mediterranean basin: North African Jews, Armenians, Arabs and Turks. The disease is also distributed in other populations including Greeks, Cypriots, Italians and Spanish, although at a lower prevalence. Defects in MEFV are the cause of familial Mediterranean fever autosomal dominant (ADFMF). ADFMF is characterized by periodic fever, serosal inflammation and pain in the abdomen, chest or joints as seen also in the autosomal recessive form of the disease. It is associated with renal amyloidosis and characterized by colchicine unresponsiveness. 2 isoforms of the human protein are produced by alternative splicing. Note: This description may include information from UniProtKB.
Cellular Component: ruffle; microtubule; microtubule associated complex; lamellipodium; nucleus; cytosol
Molecular Function: zinc ion binding; actin binding
Biological Process: negative regulation of interleukin-12 production; negative regulation of inflammatory response; innate immune response; negative regulation of interleukin-1 beta production; inflammatory response
Reference #:  O15553 (UniProtKB)
Alt. Names/Synonyms: FMF; Marenostrin; Mediterranean fever; Mediterranean fever protein; MEF; MEFV; MGC126560; MGC126586; Pyrin; TRIM20
Gene Symbols: MEFV
Molecular weight: 86,444 Da
Basal Isoelectric point: 8.3  Predict pI for various phosphorylation states
Select Structure to View Below

pyrin

Protein Structure Not Found.


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Sites Implicated In
intracellular localization: S208‑p, S209‑p, S242‑p
molecular association, regulation: S208‑p, S209‑p, S242‑p

Modification Sites and Domains  

Modification Sites in Parent Protein, Orthologs, and Isoforms  
 

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 2 S6-p __MAKTPsDHLLstL
0 2 S11-p TPsDHLLstLEELVP
0 2 T12-p PsDHLLstLEELVPY
1 2 S208-p VRLRRNAssAGRLQG
1 0 S209-p RLRRNAssAGRLQGL
1 2 S242-p SGKMRPRsLEVTIST
  mouse

 
G6 __MAKTLGDHLLNTL
N11 TLGDHLLNTLEELLP
T12 LGDHLLNTLEELLPY
S205 AQLRRNVSSAGRLQG
S206 QLRRNVSSAGRLQGL
S241-p SGKKRPRsLEITTYS
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