Home

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; Motility/polarity/chemotaxis; Secreted, signal peptide Cellular Component: extracellular matrix; cytoplasm; basement membrane Molecular Function: metalloendopeptidase inhibitor activity; protein binding; metal ion binding Biological Process: central nervous system development; visual perception; response to mechanical stimulus; tissue regeneration; response to estrogen stimulus; response to folic acid; negative regulation of membrane protein ectodomain proteolysis; aging 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: 9  Predict pI for various phosphorylation states Protein-Specific Antibodies or siRNAs from Cell Signaling Technology®

Select Structure to View Below TIMP3 3CKI - B=24-144 (human)

STRING  |  Scansite  |  Phospho.ELM  |  NetworKIN  |  Pfam  |  RCSB PDB  |  Phospho3D  |  DISEASE 136900 188826  |  InnateDB  |  UCSD-Nature  |  UniProtKB  |  Entrez-Gene  |  GenPept  |  Ensembl Gene

	Modification Sites and Domains

	Modification Sites in Parent Protein, Orthologs, and Isoforms

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

Home  |  Curator Login With enhanced literature mining using Linguamatics I2E Produced by 3rd Millennium  |  Design by Digizyme ©2003-2013 Cell Signaling Technology, Inc.