Version 5.4
Homo sapiens Gene: ADAMTS4
Summary
InnateDB Gene IDBG-104221.6
Last Modified 2014-10-13 [Report errors or provide feedback]
Gene Symbol ADAMTS4
Gene Name ADAM metallopeptidase with thrombospondin type 1 motif, 4
Synonyms ADAMTS-2; ADAMTS-4; ADMP-1
Species Homo sapiens
Ensembl Gene ENSG00000158859
Encoded Proteins
IDBP-104223
ADAM metallopeptidase with thrombospondin type 1 motif, 4
IDBP-104225
ADAM metallopeptidase with thrombospondin type 1 motif, 4
Protein Structure
Useful resources Stemformatics EHFPI ImmGen
Entrez Gene
Summary This gene encodes a member of the ADAMTS (a disintegrin and metalloproteinase with thrombospondin motifs) protein family. Members of the family share several distinct protein modules, including a propeptide region, a metalloproteinase domain, a disintegrin-like domain, and a thrombospondin type 1 (TS) motif. Individual members of this family differ in the number of C-terminal TS motifs, and some have unique C-terminal domains. The enzyme encoded by this gene lacks a C-terminal TS motif. It is responsible for the degradation of aggrecan, a major proteoglycan of cartilage, and brevican, a brain-specific extracellular matrix protein. The cleavage of aggrecan and brevican suggests key roles of this enzyme in arthritic disease and in the central nervous system, potentially, in the progression of glioma. [provided by RefSeq, Jul 2008]
Gene Information
Type Protein coding
Genomic Location Chromosome 1:161184308-161199056
Strand Reverse strand
Band q23.3
Transcripts
ENST00000367996 ENSP00000356975
ENST00000367995 ENSP00000356974
ENST00000478394
Interactions
Number of Interactions This gene and/or its encoded proteins are associated with 7 experimentally validated interaction(s) in this database.
Experimentally validated
Total 7 [view]
Protein-Protein 6 [view]
Protein-DNA 0
Protein-RNA 1 [view]
DNA-DNA 0
RNA-RNA 0
DNA-RNA 0
Gene Ontology

Molecular Function
Accession GO Term
GO:0002020 protease binding
GO:0004222 metalloendopeptidase activity
GO:0005515 protein binding
GO:0008233 peptidase activity
GO:0008237 metallopeptidase activity
GO:0008270 zinc ion binding
Biological Process
GO:0001501 skeletal system development
GO:0006508 proteolysis
GO:0022617 extracellular matrix disassembly
GO:0030198 extracellular matrix organization
GO:0042742 defense response to bacterium
Cellular Component
GO:0005576 extracellular region
GO:0005578 proteinaceous extracellular matrix
GO:0005615 extracellular space
GO:0031012 extracellular matrix
Orthologs
Species
Mus musculus
Bos taurus
Gene ID
Gene Order
ENSMUSG00000006403
View Gene Order
ENSBTAG00000013210
Not yet available
Pathways
NETPATH
REACTOME
REACT_22161
Post-translational protein modification pathway
REACT_118779
Extracellular matrix organization pathway
REACT_118572
Degradation of the extracellular matrix pathway
REACT_200727
O-linked glycosylation pathway
REACT_17015
Metabolism of proteins pathway
REACT_200626
O-glycosylation of TSR domain-containing proteins pathway
KEGG
INOH
PID NCI
Cross-References
SwissProt
TrEMBL Q5VTW1
UniProt Splice Variant
Entrez Gene 9507
UniGene Hs.211604
RefSeq NM_005099
HUGO HGNC:220
OMIM 603876
CCDS CCDS1223
HPRD 04853
IMGT
EMBL AL590714
GenPept
RNA Seq Atlas 9507

If you use InnateDB for your research, please cite the following publication:

Breuer et al., InnateDB: systems biology of innate immunity and beyond - recent updates and continuing curation. Nucl. Acids Res. (2013) 41 (D1) 

InnateDB is being developed jointly by the Brinkman Laboratory (Simon Fraser University, British Columbia, Canada), the Hancock Laboratory (University of British Columbia, Vancouver, British Columbia) and the Lynn EMBL Australia Group (South Australian Health & Medical Research Institute and Flinders University, Adelaide, Australia).

Funding is currently provided by Allergen and EMBL Australia. Previous funding has been provided by Genome Canada, the Foundation for the National Institutes of Health through the Grand Challenges in Global Health initiative and by Teagasc. InnateDB curated interactions are licensed under the Design Science License. All other data is licensed under the terms of the originating database. Contact: innatedb-mail@sfu.ca