logo
  Home | Contact us | Browse | Quick Search by UniProtKB ID, Keyword, PDBID

Menu:

Latest news:

Sep. 10, 2014:
A total of 174 experimentally verified S-nitrosylation sites on 94 S-nitrosylated proteins from individualized human colorectal cancer tissues using a label-free quantitation strategy.

Read more...


Protein Name: Filamin-C

UniprotKB/SwissProt ID: FLNC_HUMAN (Q14315)

Gene Name: FLNC

Synonyms: ABPL, FLN2

Organism: Homo sapiens (Human).

Function: Muscle-specific filamin, which plays a central role in muscle cells, probably by functioning as a large actin-cross- linking protein. May be involved in reorganizing the actin cytoskeleton in response to signaling events, and may also display structural functions at the Z lines in muscle cells. Critical for normal myogenesis and for maintaining the structural integrity of the muscle fibers.

Other Modifications: View all modification sites in dbPTM

Protein Subcellular Localization: Cytoplasm. Membrane; Peripheral membrane protein. Cytoplasm, cytoskeleton. Cytoplasm, myofibril, sarcomere, Z line. Note=A small amount localizes at membranes. In striated muscle cells, it predominantly localizes in myofibrillar Z lines, while a minor fr

PDB :
( If your security settings prevent Jmol from running, please register http://140.138.144.145/ as a safe location in your Java settings. )

Protein disease:
Disease database Database Entry Disease information
KEGGH00595 Myofibrillar myopathies (MFM), including: Desminopathy (MFM1); alpha-B Crystallinopathy (MFM2); Myot
OMIM102565FILAMIN C; FLNC ;;FILAMIN, GAMMA;; FILAMIN 2; FLN2;; ACTIN-BINDING PROTEIN 280, AUTOSOMAL FO
OMIM609524MYOPATHY, MYOFIBRILLAR, FILAMIN C-RELATED ;;MFM, FILAMIN C-RELATED;; FILAMINOPATHY, AUTOSOMA
OMIM614065MYOPATHY, DISTAL, 4; MPD4
HPRD00018Filaminopathy, autosomal dominant
Network with metabolic pathway:
Kegg map ID Pathway Link
map04010MAPK signaling pathway
map04510Focal adhesion
map05132Salmonella infection
Graphical Visualization of S-nitrosylation Sites:
Overview of Protein S-nitrosylation Sites with Functional and Structural Information
InterPro ID Domain
IPR001298
IPR001589
IPR001715
IPR013783
IPR014756

3D Structure Databases:
3D structure databases
EntryMethodResolution (A)ChainPositionsView
1V05 X-ray 1.43 A A2633-2725Link
2D7M NMR - A1536-1637Link
2D7N NMR - A1782-1861Link
2D7O NMR - A1856-1953Link
2D7P NMR - A2405-2500Link
2D7Q NMR - A2502-2599Link
2K9U NMR - A2302-2415Link
2NQC X-ray 2.05 A A2495-2598Link
3V8O X-ray 2.80 A A/B569-761Link
4MGX X-ray 3.16 A A572-756Link

The S-nitrosylation sites of FLNC_HUMAN

No. Position S-nitrosylated Peptide Secondary Structure of S-nitrosylated Peptide Solvent Accessibility of nitrosylated Site Substrate Motifs PubMed ID Experiment
11103GGLGLTVEGP C EAKIECQDNG CCEEEEEEEC C CCCEEEEECC 13.44%HC0620140087in vivo
21348SPFRVGVTEG C DPTRVRAFGP CCEEEEEECC C CCEEEEEECC 4.63%HC012212679in vitro