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9SOP

Tissue inhibitor of metalloproteinase-1 (TIMP-1)

Functional Information from GO Data
ChainGOidnamespacecontents
A0002020molecular_functionprotease binding
A0004857molecular_functionenzyme inhibitor activity
A0005125molecular_functioncytokine activity
A0005515molecular_functionprotein binding
A0005576cellular_componentextracellular region
A0005604cellular_componentbasement membrane
A0005615cellular_componentextracellular space
A0005788cellular_componentendoplasmic reticulum lumen
A0007165biological_processsignal transduction
A0008083molecular_functiongrowth factor activity
A0008191molecular_functionmetalloendopeptidase inhibitor activity
A0008270molecular_functionzinc ion binding
A0008284biological_processpositive regulation of cell population proliferation
A0009725biological_processresponse to hormone
A0010951biological_processnegative regulation of endopeptidase activity
A0030414molecular_functionpeptidase inhibitor activity
A0031012cellular_componentextracellular matrix
A0031093cellular_componentplatelet alpha granule lumen
A0034097biological_processresponse to cytokine
A0034774cellular_componentsecretory granule lumen
A0043066biological_processnegative regulation of apoptotic process
A0043086biological_processnegative regulation of catalytic activity
A0043434biological_processresponse to peptide hormone
A0045861biological_processnegative regulation of proteolysis
A0046872molecular_functionmetal ion binding
A0051045biological_processnegative regulation of membrane protein ectodomain proteolysis
A0051216biological_processcartilage development
A0070062cellular_componentextracellular exosome
A0071492biological_processcellular response to UV-A
A1901164biological_processnegative regulation of trophoblast cell migration
A1901653biological_processcellular response to peptide
A1905049biological_processnegative regulation of metallopeptidase activity
A1905641biological_processcellular response to acetaldehyde
A2001044biological_processregulation of integrin-mediated signaling pathway
B0002020molecular_functionprotease binding
B0004857molecular_functionenzyme inhibitor activity
B0005125molecular_functioncytokine activity
B0005515molecular_functionprotein binding
B0005576cellular_componentextracellular region
B0005604cellular_componentbasement membrane
B0005615cellular_componentextracellular space
B0005788cellular_componentendoplasmic reticulum lumen
B0007165biological_processsignal transduction
B0008083molecular_functiongrowth factor activity
B0008191molecular_functionmetalloendopeptidase inhibitor activity
B0008270molecular_functionzinc ion binding
B0008284biological_processpositive regulation of cell population proliferation
B0009725biological_processresponse to hormone
B0010951biological_processnegative regulation of endopeptidase activity
B0030414molecular_functionpeptidase inhibitor activity
B0031012cellular_componentextracellular matrix
B0031093cellular_componentplatelet alpha granule lumen
B0034097biological_processresponse to cytokine
B0034774cellular_componentsecretory granule lumen
B0043066biological_processnegative regulation of apoptotic process
B0043086biological_processnegative regulation of catalytic activity
B0043434biological_processresponse to peptide hormone
B0045861biological_processnegative regulation of proteolysis
B0046872molecular_functionmetal ion binding
B0051045biological_processnegative regulation of membrane protein ectodomain proteolysis
B0051216biological_processcartilage development
B0070062cellular_componentextracellular exosome
B0071492biological_processcellular response to UV-A
B1901164biological_processnegative regulation of trophoblast cell migration
B1901653biological_processcellular response to peptide
B1905049biological_processnegative regulation of metallopeptidase activity
B1905641biological_processcellular response to acetaldehyde
B2001044biological_processregulation of integrin-mediated signaling pathway
Functional Information from PROSITE/UniProt
site_idPS00288
Number of Residues13
DetailsTIMP Tissue inhibitors of metalloproteinases signature. CtCvPpHPQtaFC
ChainResidueDetails
ACYS1-CYS13

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues10
DetailsRegion: {"description":"Involved in metalloproteinase-binding","evidences":[{"source":"PubMed","id":"22427646","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"3V96","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues2
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"22427646","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues4
DetailsSite: {"description":"Involved in metalloproteinase-binding","evidences":[{"source":"PubMed","id":"22427646","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"3V96","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues2
DetailsModified residue: {"description":"Phosphoserine; by FAM20C","evidences":[{"source":"PubMed","id":"26091039","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI5
Number of Residues2
DetailsGlycosylation: {"description":"N-linked (GlcNAc...) (complex) asparagine","featureId":"CAR_000002","evidences":[{"source":"PubMed","id":"16263699","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"16335952","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"16740002","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"19139490","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI6
Number of Residues123
DetailsDomain: {"description":"NTR","evidences":[{"source":"PROSITE-ProRule","id":"PRU00295","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI7
Number of Residues1
DetailsGlycosylation: {"description":"N-linked (GlcNAc...) asparagine","featureId":"CAR_000003","evidences":[{"source":"PubMed","id":"16740002","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

247536

PDB entries from 2026-01-14

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