ADAM15
entrez
8751
canonical
uniprot
Q13444
canonical
ensembl
ENSG00000143537
resolver
ensp
ENSP00000271836
resolver
ensp
ENSP00000348227
resolver
ensp
ENSP00000349436
resolver
ensp
ENSP00000352226
resolver
ensp
ENSP00000353892
resolver
ensp
ENSP00000357397
resolver
ensp
ENSP00000403843
resolver
ensp
ENSP00000432927
resolver
ensp
ENSP00000476000
resolver
genesymbol
ADAM15
resolver
genesymbol_syn
MDC15
resolver
hgnc
HGNC:193
resolver
uniprot
B3KQU5
resolver
uniprot
B4DLB5
resolver
uniprot
B4DMH8
resolver
uniprot
E9PN65
resolver
uniprot
Q13493
resolver
uniprot
Q53XQ0
resolver
uniprot
Q5SR68
resolver
uniprot
Q5SR69
resolver
uniprot
Q6R267
resolver
uniprot
Q71S61
resolver
uniprot
Q71S62
resolver
uniprot
Q71S63
resolver
uniprot
Q71S64
resolver
uniprot
Q71S65
resolver
uniprot
Q71S66
resolver
uniprot
Q71S67
resolver
uniprot
Q71S68
resolver
uniprot
Q71S69
resolver
uniprot
Q96C78
resolver
uniprot
U3KQL5
resolver
uniprot_entry
ADA15_HUMAN
resolver
uniprot_sec
B3KQU5
resolver
uniprot_sec
B4DLB5
resolver
uniprot_sec
B4DMH8
resolver
uniprot_sec
E9PN65
resolver
uniprot_sec
Q13493
resolver
uniprot_sec
Q53XQ0
resolver
uniprot_sec
Q5SR68
resolver
uniprot_sec
Q5SR69
resolver
uniprot_sec
Q6R267
resolver
uniprot_sec
Q71S61
resolver
uniprot_sec
Q71S62
resolver
uniprot_sec
Q71S63
resolver
uniprot_sec
Q71S64
resolver
uniprot_sec
Q71S65
resolver
uniprot_sec
Q71S66
resolver
uniprot_sec
Q71S67
resolver
uniprot_sec
Q71S68
resolver
uniprot_sec
Q71S69
resolver
uniprot_sec
Q96C78
resolver
uniprot_sec
U3KQL5
resolver
activity_regulation
ACTIVITY REGULATION: Inhibited by hydroxamate-type metalloproteinase inhibitors such as marimastat. Inhibited by metalloproteinase inhibitor 2 (TIMP-2) and TIMP-3 at nanomolar concentrations. Not significantly inhibited by TIMP-1 at concentrations of up to 100 nM. Not activated by PMA or ionomycin. {ECO:0000269|PubMed:19207106}.
uniprot
proteins
amino_acid_sequence
MRLALLWALGLLGAGSPLPSWPLPNIGGTEEQQAESEKAPREPLEPQVLQDDLPISLKKVLQTSLPEPLRIKLELDGDSHILELLQNRELVPGRPTLVWYQPDGTRVVSEGHTLENCCYQGRVRGYAGSWVSICTCSGLRGLVVLTPERSYTLEQGPGDLQGPPIISRIQDLHLPGHTCALSWRESVHTQKPPEHPLGQRHIRRRRDVVTETKTVELVIVADHSEAQKYRDFQHLLNRTLEVALLLDTFFRPLNVRVALVGLEAWTQRDLVEISPNPAVTLENFLHWRRAHLLPRLPHDSAQLVTGTSFSGPTVGMAIQNSICSPDFSGGVNMDHSTSILGVASSIAHELGHSLGLDHDLPGNSCPCPGPAPAKTCIMEASTDFLPGLNFSNCSRRALEKALLDGMGSCLFERLPSLPPMAAFCGNMFVEPGEQCDCGFLDDCVDPCCDSLTCQLRPGAQCASDGPCCQNCQLRPSGWQCRPTRGDCDLPEFCPGDSSQCPPDVSLGDGEPCAGGQAVCMHGRCASYAQQCQSLWGPGAQPAAPLCLQTANTRGNAFGSCGRNPSGSYVSCTPRDAICGQLQCQTGRTQPLLGSIRDLLWETIDVNGTELNCSWVHLDLGSDVAQPLLTLPGTACGPGLVCIDHRCQRVDLLGAQECRSKCHGHGVCDSNRHCYCEEGWAPPDCTTQLKATSSLTTGLLLSLLVLLVLVMLGASYWYRARLHQRLCQLKGPTCQYRAAQSGPSERPGPPQRALLARGTKQASALSFPAPPSRPLPPDPVSKRLQAELADRPNPPTRPLPADPVVRSPKSQGPAKPPPPRKPLPADPQGRCPSGDLPGPGAGIPPLVVPSRPAPPPPTVSSLYL
uniprot
proteins
ec_number
3.4.24.-
uniprot
proteins
function
FUNCTION: Active metalloproteinase with gelatinolytic and collagenolytic activity. Plays a role in the wound healing process. Mediates both heterotypic intraepithelial cell/T-cell interactions and homotypic T-cell aggregation. Inhibits beta-1 integrin-mediated cell adhesion and migration of airway smooth muscle cells. Suppresses cell motility on or towards fibronectin possibly by driving alpha-v/beta-1 integrin (ITAGV-ITGB1) cell surface expression via ERK1/2 inactivation. Cleaves E-cadherin in response to growth factor deprivation. Plays a role in glomerular cell migration. Plays a role in pathological neovascularization. May play a role in cartilage remodeling. May be proteolytically processed, during sperm epididymal maturation and the acrosome reaction. May play a role in sperm-egg binding through its disintegrin domain. {ECO:0000269|PubMed:12091380, ECO:0000269|PubMed:15358598, ECO:0000269|PubMed:15818704, ECO:0000269|PubMed:17416588, ECO:0000269|PubMed:17575078, ECO:0000269|PubMed:18387333, ECO:0000269|PubMed:18434311}.
uniprot
proteins
mass_dalton
92959
uniprot
proteins
mutagenesis
MUTAGEN 484..485; /note="RG->SV: Reduces ADAM15-mediated T-cell aggregation."; /evidence="ECO:0000269|PubMed:17416588
uniprot
proteins
post_translational_modification
PTM: The precursor is cleaved by a furin endopeptidase. {ECO:0000250}.; PTM: Phosphorylation increases association with PTKs. {ECO:0000269|PubMed:11741929}.
uniprot
proteins
pubmed
10531379
uniprot
proteins
pubmed
11741929
uniprot
proteins
pubmed
12091380
uniprot
proteins
pubmed
12243749
uniprot
proteins
pubmed
12615925
uniprot
proteins
pubmed
14702039
uniprot
proteins
pubmed
15358598
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
15818704
uniprot
proteins
pubmed
16303743
uniprot
proteins
pubmed
16710414
uniprot
proteins
pubmed
17416588
uniprot
proteins
pubmed
17575078
uniprot
proteins
pubmed
17937806
uniprot
proteins
pubmed
18296648
uniprot
proteins
pubmed
18387333
uniprot
proteins
pubmed
18434311
uniprot
proteins
pubmed
19207106
uniprot
proteins
pubmed
19718658
uniprot
proteins
pubmed
8617717
uniprot
proteins
pubmed
9016778
uniprot
proteins
pubmed
9039960
uniprot
proteins
pubmed
9516430
uniprot
proteins
pubmed
9914169
uniprot
proteins
sequence_length
863
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Endomembrane system {ECO:0000269|PubMed:12243749}; Single-pass type I membrane protein {ECO:0000269|PubMed:12243749}. Cell junction, adherens junction {ECO:0000269|PubMed:12243749}. Cell projection, cilium, flagellum {ECO:0000250}. Cytoplasmic vesicle, secretory vesicle, acrosome {ECO:0000250}. Note=The majority of the protein is localized in a perinuclear compartment which may correspond to the trans-Golgi network or the late endosome. The pro-protein is the major detectable form on the cell surface, whereas the majority of the protein in the cell is processed (By similarity). {ECO:0000250}.
uniprot
proteins
transmembrane_region
TRANSMEM 697..717; /note="Helical"; /evidence="ECO:0000255
uniprot
proteins