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Protein Page:
TIMP3 (human)

Overview
TIMP3 Complexes with metalloproteinases (such as collagenases) and irreversibly inactivates them by binding to their catalytic zinc cofactor. May form part of a tissue-specific acute response to remodeling stimuli. Known to act on MMP-1, MMP-2, MMP-3, MMP-7, MMP-9, MMP-13, MMP-14 and MMP-15. Interacts with EFEMP1. Belongs to the protease inhibitor I35 (TIMP) family. Note: This description may include information from UniProtKB.
Protein type: Secreted, signal peptide; Secreted; Motility/polarity/chemotaxis
Chromosomal Location of Human Ortholog: 22q12.3
Cellular Component: extracellular matrix; basement membrane; nucleus
Molecular Function: metalloendopeptidase inhibitor activity; protein binding; metal ion binding
Biological Process: visual perception; negative regulation of membrane protein ectodomain proteolysis
Reference #:  P35625 (UniProtKB)
Alt. Names/Synonyms: HSMRK222; K222; K222TA2; Metalloproteinase inhibitor 3; MIG-5 protein; Protein MIG-5; SFD; TIMP metallopeptidase inhibitor 3; TIMP-3; TIMP3; Tissue inhibitor of metalloproteinases 3
Gene Symbols: TIMP3
Molecular weight: 24,145 Da
Basal Isoelectric point: Predict pI for various phosphorylation states
Protein-Specific Antibodies or siRNAs from Cell Signaling Technology® Total Proteins
Select Structure to View Below

TIMP3

Protein Structure Not Found.


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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 Y100-p LKLEVNKyQYLLTGR
0 1 Y177-p SNFGYPGyQSKHyAC
0 1 Y182-p PGyQSKHyACIRQKG
0 2 Y195-p KGGYCSWyRGWAPPD
  mouse

 
Y100 LKLEVNKYQYLLTGR
Y177 SNFGYPGYQSKHYAC
Y182 PGYQSKHYACIRQKG
Y195 KGGYCSWYRGWAPPD
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