MMP2;3;7;10;11MMP3; CTSK; CTSL2MMP1;3;8;13; PRSS2MMP2;3;4;9;10;12MMP1;2;3MMP3;13MMP3,13MMP1;2;3;9Endostatin-releasing proteasesMMP1-3; 7-9; 12; 13Elastin-degrading extracellular proteinasesMMP1; 3; 7; 12; 13; 19; CTSSLaminin gamma-2 degrading extracellular proteinasesMMP3; MMP7MMP1;2;3;7;9;12;13MMP1; 2; 3; 7;8;10;13;19MMP3; plasmin; (MMP12)MMP2; MMP3; MMP7MMP3; MMP7; PlasminMMP1; 3; 13; (2; 7-12; 19)STAT3-upregulated extracellular proteinsInitial activation of proMMP3Autocatalytic activation of MMP3Activated PKC-alpha activate MMP3Active MMP3 can cleave pro-HBEGF to form active HBEGF
P527
P688
The complete primary structure of human matrix metalloproteinase-3. Identity with stromelysinProteolytic cleavage of extracellular secreted {alpha}-synuclein via matrix metalloproteinasesDJ-1 cleavage by matrix metalloproteinase 3 mediates oxidative stress-induced dopaminergic cell deathCleavage of the matricellular protein SPARC by matrix metalloproteinase 3 produces polypeptides that influence angiogenesisIncreased alpha-synuclein aggregation following limited cleavage by certain matrix metalloproteinasesCloning of three Caenorhabditis elegans genes potentially encoding novel matrix metalloproteinasesMatrix metalloproteinase-8 plays a pivotal role in neuroinflammation by modulating TNF-α activation.Key Aging-Associated Alterations in Primary Microglia Response to Beta-Amyloid Stimulation.Characterization of opticin digestion by proteases involved in osteoarthritis development.
P921
Q50257637-4A193161-CFE8-4EBF-B390-596A98C04D12Q50257648-3E5701AC-FDBF-46F8-97A3-AAC56613CB41Q50257667-31D5E037-45DE-4D0A-8D5F-5FAD3C8D4E87Q50257671-EA838D3D-BD7E-4214-A869-7B9BB3EF16FCQ50257674-D6D0A2ED-4703-4DAA-A5EB-89003639A040Q50257679-913295CD-E2D2-4F9C-943E-6F0CE11DB782Q50257683-EA1A6078-CF1D-48CF-9632-B4F9FA8D627CQ50257684-50E65E8F-3CF7-4657-974A-AC71E714AE97Q50257694-EC879031-BB24-4282-9954-FF9C33FF04E9Q50257718-CD433F49-923B-4B13-B07F-2072CB344B5CQ50257720-7FCED928-ECE4-4623-A478-76C6A63186BCQ50257723-46FAA4E8-65FF-43EF-A033-8A221C67F65CQ50257727-087DC69C-EFD4-47E0-AD44-90DEDB529024Q50257730-867F6425-6883-4115-BA33-C15BFF36D198Q50257737-C3E7064A-F5EB-40A9-8133-8C1259E75760Q50257746-3D25BDCF-FC63-4A73-89AC-212202BF2583Q50257747-57629439-14B1-4DFF-B92D-CAFBEAAACDAEQ50257750-60A4CC98-7526-4991-999C-7185F9C93FABQ50257754-D554A9BA-1A86-4F2F-9D38-4035EFDA8EF8Q50257765-3CC0ABBA-B492-4DF6-B6E3-9D76E0D2475AQ50263039-CC77F198-FB44-4081-AE15-D5AC87377185Q50289906-2AAB1F56-E768-499F-940E-7811D5C99A47Q50289906-34151C9C-6C25-4FAA-8E4A-20FC571285DBQ50289907-4283E687-721A-4B19-AEEB-20915393F342Q50289907-7EF02503-C8EF-4D3C-BB36-EAD4E1AD9D2DQ50289907-9B261217-51DB-43C3-B356-277B8ED58159Q50298514-7FDF24AA-FAE7-42CC-BEDF-C3F1C47A818FQ50298514-C35C32B8-77B2-436C-84BB-D8C115828A9DQ50298515-E5A03055-C3A1-4485-877B-F00B93D8CE23
P527
Q24298260-720C8B07-9F37-4158-90E3-649874847BCCQ24301116-70608D96-0AFB-4A94-8594-0BE976B6C526Q24304197-94F85843-2016-4219-A0D6-7AEAFE62DE5DQ24309124-AB2C0A18-E977-4024-AEB8-7E1697F01735Q24316244-6563C1C2-41E2-487C-BE83-C0625A43CF3FQ28116117-1061DA1D-2BA3-4AE6-83E5-9279E0EB4882Q38435937-13982F73-C773-4DC4-B51A-B46301BA94D1Q41605528-0919A182-419D-4C1A-B938-5000C09F698CQ45185653-9A69FA1E-76DA-4DFA-88FC-AAE08890D2D2
P921
description
Protein in Homo sapiens
@de
mammalian protein found in Homo sapiens
@en
protein
@id
protein
@sv
proteinë
@sq
proteïne in Matrix metallopeptidase 3
@nl
protèin
@ace
protéine
@fr
بروتين في الإنسان العاقل
@ar
name
Matrix metallopeptidase 3
@en
Matrix metallopeptidase 3
@nl
type
label
Matrix metallopeptidase 3
@en
Matrix metallopeptidase 3
@nl
altLabel
MMP-3
@en
MMP3
@en
Matrix metalloproteinase-3
@en
matrix metalloproteinase 3 (stromelysin 1, progelatinase)
@en
proteoglycanase
@en
stromelysin-1
@en
transin-1
@en
prefLabel
Matrix metallopeptidase 3
@en
Matrix metallopeptidase 3
@nl
P361
P527
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P680
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P682
P705
P352
P6366
P637
P31
P352
P361
P527
P591
P6366
2778767966
2779295440
P637
P638
P680
P682
P702
P703
P705
ENSP00000299855
ENSP00000398346
ENSP00000435255