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P01033

- TIMP1_HUMAN

UniProt

P01033 - TIMP1_HUMAN

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Protein

Metalloproteinase inhibitor 1

Gene

TIMP1

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

Functioni

Metalloproteinase inhibitor that functions by forming one to one complexes with target metalloproteinases, such as collagenases, and irreversibly inactivates them by binding to their catalytic zinc cofactor. Acts on MMP1, MMP2, MMP3, MMP7, MMP8, MMP9, MMP10, MMP11, MMP12, MMP13 and MMP16. Does not act on MMP14. Also functions as a growth factor that regulates cell differentiation, migration and cell death and activates cellular signaling cascades via CD63 and ITGB1. Plays a role in integrin signaling. Mediates erythropoiesis in vitro; but, unlike IL3, it is species-specific, stimulating the growth and differentiation of only human and murine erythroid progenitors.12 Publications

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi24 – 241Zinc; via amino nitrogen and carbonyl oxygen; shared with metalloproteinase partner

GO - Molecular functioni

  1. cytokine activity Source: UniProtKB
  2. metal ion binding Source: UniProtKB-KW
  3. metalloendopeptidase inhibitor activity Source: UniProtKB

GO - Biological processi

  1. aging Source: Ensembl
  2. blood coagulation Source: Reactome
  3. extracellular matrix disassembly Source: Reactome
  4. extracellular matrix organization Source: Reactome
  5. negative regulation of apoptotic process Source: Ensembl
  6. negative regulation of endopeptidase activity Source: UniProtKB
  7. negative regulation of membrane protein ectodomain proteolysis Source: UniProtKB
  8. negative regulation of metalloenzyme activity Source: UniProtKB
  9. negative regulation of trophoblast cell migration Source: BHF-UCL
  10. platelet activation Source: Reactome
  11. platelet degranulation Source: Reactome
  12. positive regulation of cell proliferation Source: UniProtKB
  13. regulation of integrin-mediated signaling pathway Source: UniProtKB
  14. response to cytokine Source: Ensembl
  15. response to peptide hormone Source: Ensembl
Complete GO annotation...

Keywords - Molecular functioni

Growth factor, Metalloenzyme inhibitor, Metalloprotease inhibitor, Protease inhibitor

Keywords - Ligandi

Metal-binding, Zinc

Enzyme and pathway databases

ReactomeiREACT_118682. Activation of Matrix Metalloproteinases.

Protein family/group databases

MEROPSiI35.001.

Names & Taxonomyi

Protein namesi
Recommended name:
Metalloproteinase inhibitor 1
Alternative name(s):
Erythroid-potentiating activity
Short name:
EPA
Fibroblast collagenase inhibitor
Short name:
Collagenase inhibitor
Tissue inhibitor of metalloproteinases 1
Short name:
TIMP-1
Gene namesi
Name:TIMP1
Synonyms:CLGI, TIMP
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome X

Organism-specific databases

HGNCiHGNC:11820. TIMP1.

Subcellular locationi

Secreted 6 Publications

GO - Cellular componenti

  1. basement membrane Source: Ensembl
  2. extracellular region Source: UniProtKB
  3. extracellular space Source: UniProtKB
  4. extracellular vesicular exosome Source: UniProtKB
  5. platelet alpha granule lumen Source: Reactome
Complete GO annotation...

Keywords - Cellular componenti

Secreted

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi25 – 251T → E, G, K, Q or R: Reduced interaction with metalloproteinase. 1 Publication
Mutagenesisi25 – 251T → V: Normal interaction with metalloproteinase. 1 Publication
Mutagenesisi30 – 301H → A: Nearly abolishes metalloproteinase inhibition. 1 Publication
Mutagenesisi32 – 321Q → A: Nearly abolishes metalloproteinase inhibition. 1 Publication
Mutagenesisi121 – 1211T → L: Decreases protein flexibility and increases affinity for MMP14. 1 Publication

Organism-specific databases

PharmGKBiPA36526.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 23236 PublicationsAdd
BLAST
Chaini24 – 207184Metalloproteinase inhibitor 1PRO_0000034323Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi24 ↔ 931 PublicationPROSITE-ProRule annotation
Disulfide bondi26 ↔ 122
Disulfide bondi36 ↔ 147
Glycosylationi53 – 531N-linked (GlcNAc...) (complex)4 PublicationsCAR_000002
Glycosylationi101 – 1011N-linked (GlcNAc...)1 PublicationCAR_000003
Disulfide bondi150 ↔ 197
Disulfide bondi155 ↔ 160
Disulfide bondi168 ↔ 189

Post-translational modificationi

The activity of TIMP1 is dependent on the presence of disulfide bonds.
N-glycosylated.7 Publications

Keywords - PTMi

Disulfide bond, Glycoprotein

Proteomic databases

MaxQBiP01033.
PaxDbiP01033.
PRIDEiP01033.

PTM databases

PhosphoSiteiP01033.
UniCarbKBiP01033.

Miscellaneous databases

PMAP-CutDBP01033.

Expressioni

Tissue specificityi

Detected in rheumatoid synovial fluid (at protein level).1 Publication

Gene expression databases

BgeeiP01033.
CleanExiHS_TIMP1.
ExpressionAtlasiP01033. baseline and differential.
GenevestigatoriP01033.

Organism-specific databases

HPAiCAB022360.

Interactioni

Subunit structurei

Interacts with MMP1, MMP3, MMP10 and MMP13, but has only very low affinity for MMP14. Interacts with CD63; identified in a complex with CD63 and ITGB1.10 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
CD63P089625EBI-712536,EBI-762053

Protein-protein interaction databases

BioGridi112932. 9 interactions.
DIPiDIP-1107N.
IntActiP01033. 5 interactions.
MINTiMINT-2981826.
STRINGi9606.ENSP00000218388.

Structurei

Secondary structure

1
207
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi31 – 377
Beta strandi39 – 468
Beta strandi57 – 7014
Helixi72 – 743
Turni77 – 793
Beta strandi83 – 897
Helixi90 – 923
Beta strandi105 – 1139
Beta strandi116 – 1183
Beta strandi125 – 1273
Helixi128 – 1303
Helixi133 – 1408
Helixi143 – 1453
Turni146 – 1494
Beta strandi151 – 1544
Beta strandi157 – 1593
Beta strandi167 – 1704
Helixi172 – 1765
Beta strandi177 – 1815
Helixi182 – 1865
Beta strandi188 – 1936
Beta strandi196 – 2005

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1D2BNMR-A24-149[»]
1LQNmodel-A1-207[»]
1OO9NMR-B24-149[»]
1UEAX-ray2.80B/D24-207[»]
2J0TX-ray2.54D/E/F24-149[»]
3MA2X-ray2.05B/C24-148[»]
3V96X-ray1.90A24-207[»]
ProteinModelPortaliP01033.
SMRiP01033. Positions 24-204.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP01033.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini24 – 147124NTRPROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni24 – 285Involved in metalloproteinase-binding
Regioni90 – 912Involved in metalloproteinase-binding

Sequence similaritiesi

Contains 1 NTR domain.PROSITE-ProRule annotation

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiNOG259409.
HOGENOMiHOG000285981.
HOVERGENiHBG068749.
InParanoidiP01033.
KOiK16451.
OMAiDKGFQSR.
OrthoDBiEOG79GT74.
PhylomeDBiP01033.
TreeFamiTF317409.

Family and domain databases

Gene3Di3.90.370.10. 1 hit.
InterProiIPR001134. Netrin_domain.
IPR001820. Prot_inh_TIMP.
IPR008993. TIMP-like_OB-fold.
IPR015611. TIMP1.
IPR027465. TIMP_C_dom.
[Graphical view]
PANTHERiPTHR11844. PTHR11844. 1 hit.
PTHR11844:SF20. PTHR11844:SF20. 1 hit.
PfamiPF00965. TIMP. 1 hit.
[Graphical view]
SMARTiSM00206. NTR. 1 hit.
[Graphical view]
SUPFAMiSSF50242. SSF50242. 1 hit.
PROSITEiPS50189. NTR. 1 hit.
PS00288. TIMP. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P01033-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MAPFEPLASG ILLLLWLIAP SRACTCVPPH PQTAFCNSDL VIRAKFVGTP
60 70 80 90 100
EVNQTTLYQR YEIKMTKMYK GFQALGDAAD IRFVYTPAME SVCGYFHRSH
110 120 130 140 150
NRSEEFLIAG KLQDGLLHIT TCSFVAPWNS LSLAQRRGFT KTYTVGCEEC
160 170 180 190 200
TVFPCLSIPC KLQSGTHCLW TDQLLQGSEK GFQSRHLACL PREPGLCTWQ

SLRSQIA
Length:207
Mass (Da):23,171
Last modified:July 21, 1986 - v1
Checksum:i5AE4F90FFAB2ECDC
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti23 – 231A → P in CAA26443. (PubMed:3839290)Curated
Sequence conflicti44 – 441A → P in BAA01913. 1 PublicationCurated

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
X03124 mRNA. Translation: CAA26902.1.
X02598 mRNA. Translation: CAA26443.1.
M12670 mRNA. Translation: AAA52436.1.
M59906 mRNA. Translation: AAA63234.1.
S68252 mRNA. Translation: AAD14009.1.
BC000866 mRNA. Translation: AAH00866.1.
L47361 Genomic DNA. Translation: AAA75558.1.
D11139 Genomic DNA. Translation: BAA01913.1.
CCDSiCCDS14281.1.
PIRiA93372. ZYHUEP.
RefSeqiNP_003245.1. NM_003254.2.
UniGeneiHs.522632.

Genome annotation databases

EnsembliENST00000218388; ENSP00000218388; ENSG00000102265.
GeneIDi7076.
KEGGihsa:7076.
UCSCiuc004dif.3. human.

Polymorphism databases

DMDMi135850.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
X03124 mRNA. Translation: CAA26902.1 .
X02598 mRNA. Translation: CAA26443.1 .
M12670 mRNA. Translation: AAA52436.1 .
M59906 mRNA. Translation: AAA63234.1 .
S68252 mRNA. Translation: AAD14009.1 .
BC000866 mRNA. Translation: AAH00866.1 .
L47361 Genomic DNA. Translation: AAA75558.1 .
D11139 Genomic DNA. Translation: BAA01913.1 .
CCDSi CCDS14281.1.
PIRi A93372. ZYHUEP.
RefSeqi NP_003245.1. NM_003254.2.
UniGenei Hs.522632.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1D2B NMR - A 24-149 [» ]
1LQN model - A 1-207 [» ]
1OO9 NMR - B 24-149 [» ]
1UEA X-ray 2.80 B/D 24-207 [» ]
2J0T X-ray 2.54 D/E/F 24-149 [» ]
3MA2 X-ray 2.05 B/C 24-148 [» ]
3V96 X-ray 1.90 A 24-207 [» ]
ProteinModelPortali P01033.
SMRi P01033. Positions 24-204.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 112932. 9 interactions.
DIPi DIP-1107N.
IntActi P01033. 5 interactions.
MINTi MINT-2981826.
STRINGi 9606.ENSP00000218388.

Protein family/group databases

MEROPSi I35.001.

PTM databases

PhosphoSitei P01033.
UniCarbKBi P01033.

Polymorphism databases

DMDMi 135850.

Proteomic databases

MaxQBi P01033.
PaxDbi P01033.
PRIDEi P01033.

Protocols and materials databases

DNASUi 7076.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000218388 ; ENSP00000218388 ; ENSG00000102265 .
GeneIDi 7076.
KEGGi hsa:7076.
UCSCi uc004dif.3. human.

Organism-specific databases

CTDi 7076.
GeneCardsi GC0XP047441.
HGNCi HGNC:11820. TIMP1.
HPAi CAB022360.
MIMi 305370. gene.
neXtProti NX_P01033.
PharmGKBi PA36526.
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG259409.
HOGENOMi HOG000285981.
HOVERGENi HBG068749.
InParanoidi P01033.
KOi K16451.
OMAi DKGFQSR.
OrthoDBi EOG79GT74.
PhylomeDBi P01033.
TreeFami TF317409.

Enzyme and pathway databases

Reactomei REACT_118682. Activation of Matrix Metalloproteinases.

Miscellaneous databases

EvolutionaryTracei P01033.
GeneWikii TIMP1.
GenomeRNAii 7076.
NextBioi 27675.
PMAP-CutDB P01033.
PROi P01033.
SOURCEi Search...

Gene expression databases

Bgeei P01033.
CleanExi HS_TIMP1.
ExpressionAtlasi P01033. baseline and differential.
Genevestigatori P01033.

Family and domain databases

Gene3Di 3.90.370.10. 1 hit.
InterProi IPR001134. Netrin_domain.
IPR001820. Prot_inh_TIMP.
IPR008993. TIMP-like_OB-fold.
IPR015611. TIMP1.
IPR027465. TIMP_C_dom.
[Graphical view ]
PANTHERi PTHR11844. PTHR11844. 1 hit.
PTHR11844:SF20. PTHR11844:SF20. 1 hit.
Pfami PF00965. TIMP. 1 hit.
[Graphical view ]
SMARTi SM00206. NTR. 1 hit.
[Graphical view ]
SUPFAMi SSF50242. SSF50242. 1 hit.
PROSITEi PS50189. NTR. 1 hit.
PS00288. TIMP. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Sequence of human tissue inhibitor of metalloproteinases and its identity to erythroid-potentiating activity."
    Docherty A.J.P., Lyons A., Smith B.J., Wright E.M., Stephens P.E., Harris T.J.R., Murphy G., Reynolds J.J.
    Nature 318:66-69(1985) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 24-51, FUNCTION, SUBCELLULAR LOCATION, GLYCOSYLATION.
  2. "Molecular characterization and expression of the gene encoding human erythroid-potentiating activity."
    Gasson J.C., Golde D.W., Kaufman S.E., Westbrook C.A., Hewick R.M., Kaufman R.J., Wong G.G., Temple P.A., Leary A.C., Brown E.L., Orr E.C., Clark S.C.
    Nature 315:768-771(1985) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 24-49, SUBCELLULAR LOCATION, GLYCOSYLATION, FUNCTION.
  3. Cited for: NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 24-207, DISULFIDE BOND, SUBCELLULAR LOCATION, GLYCOSYLATION.
  4. "Molecular cloning and synthesis of biologically active human tissue inhibitor of metalloproteinases in yeast."
    Kaczorek M., Honore N., Ribes V., Dehoux P., Cornet P., Cartwright T., Streeck R.E.
    Biotechnology (N.Y.) 5:595-598(1987)
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  5. "Characterization of three abundant mRNAs from human ovarian granulosa cells."
    Rapp G., Freudenstein J., Klaudiny J., Mucha J., Wempe F., Zimmer M., Scheit K.H.
    DNA Cell Biol. 9:479-485(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Tissue: Ovary.
  6. "Characterization of a human corneal metalloproteinase inhibitor (TIMP-1)."
    Opbroek A., Kenney M.C., Brown D.
    Curr. Eye Res. 12:877-883(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  7. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Cervix.
  8. "Genomic organization of the human TIMP-1 gene. Investigation of a causative role in the pathogenesis of X-linked retinitis pigmentosa 2."
    Hardcastle A.J., Thiselton D.L., Nayudu M., Hampson R.M., Bhattacharya S.S.
    Invest. Ophthalmol. Vis. Sci. 38:1893-1896(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-40.
  9. "Isolation and characterization of tissue inhibitors of metalloproteinases (TIMP-1 and TIMP-2) from human rheumatoid synovial fluid."
    Osthues A., Knaueper V., Oberhoff R., Reinke H., Tschesche H.
    FEBS Lett. 296:16-20(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 24-38, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, FUNCTION.
    Tissue: Synovial fluid.
  10. "The cytokine-protease connection: identification of a 96-kD THP-1 gelatinase and regulation by interleukin-1 and cytokine inducers."
    van Ranst M., Norga K., Masure S., Proost P., Vandekerckhove F., Auwerx J., van Damme J., Opdenakker G.
    Cytokine 3:231-239(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 24-52.
  11. "Signal peptide prediction based on analysis of experimentally verified cleavage sites."
    Zhang Z., Henzel W.J.
    Protein Sci. 13:2819-2824(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 24-38.
  12. Matsuda T., Kohno K., Kuwano M.
    Submitted (JUL-1992) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 42-207.
  13. "Disulphide bond assignment in human tissue inhibitor of metalloproteinases (TIMP)."
    Williamson R.A., Martson F.A.O., Angal S., Koklitis P., Panico M., Morris H.R., Carne A.F., Smith B.J., Harris T.J.R., Freedman R.B.
    Biochem. J. 268:267-274(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: DISULFIDE BONDS, PARTIAL PROTEIN SEQUENCE.
  14. "Site-directed mutations that alter the inhibitory activity of the tissue inhibitor of metalloproteinases-1: importance of the N-terminal region between cysteine 3 and cysteine 13."
    O'Shea M., Willenbrock F., Williamson R.A., Cockett M.I., Freedman R.B., Reynolds J.J., Docherty A.J.P., Murphy G.
    Biochemistry 31:10146-10152(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: MUTAGENESIS, FUNCTION.
  15. "Metalloproteinase inhibition and erythroid potentiation are independent activities of tissue inhibitor of metalloproteinases-1."
    Chesler L., Golde D.W., Bersch N., Johnson M.D.
    Blood 86:4506-4515(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION AS A GROWTH FACTOR AND PROTEASE INHIBITOR, INTERACTION WITH MMP3, SUBCELLULAR LOCATION, MUTAGENESIS OF HIS-30 AND GLN-32.
  16. Cited for: INTERACTION WITH MMP13, FUNCTION.
  17. "The role of the C-terminal domain of human collagenase-3 (MMP-13) in the activation of procollagenase-3, substrate specificity, and tissue inhibitor of metalloproteinase interaction."
    Knaeuper V., Cowell S., Smith B., Lopez-Otin C., O'Shea M., Morris H., Zardi L., Murphy G.
    J. Biol. Chem. 272:7608-7616(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH MMP13, FUNCTION.
  18. "Human plasma N-glycoproteome analysis by immunoaffinity subtraction, hydrazide chemistry, and mass spectrometry."
    Liu T., Qian W.-J., Gritsenko M.A., Camp D.G. II, Monroe M.E., Moore R.J., Smith R.D.
    J. Proteome Res. 4:2070-2080(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-53.
    Tissue: Plasma.
  19. "Identification of CD63 as a tissue inhibitor of metalloproteinase-1 interacting cell surface protein."
    Jung K.K., Liu X.W., Chirco R., Fridman R., Kim H.R.
    EMBO J. 25:3934-3942(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH CD63.
  20. "Identification of N-linked glycoproteins in human saliva by glycoprotein capture and mass spectrometry."
    Ramachandran P., Boontheung P., Xie Y., Sondej M., Wong D.T., Loo J.A.
    J. Proteome Res. 5:1493-1503(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-53 AND ASN-101.
    Tissue: Saliva.
  21. "Elucidation of N-glycosylation sites on human platelet proteins: a glycoproteomic approach."
    Lewandrowski U., Moebius J., Walter U., Sickmann A.
    Mol. Cell. Proteomics 5:226-233(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-53.
    Tissue: Platelet.
  22. Cited for: GLYCOSYLATION AT ASN-53.
  23. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  24. "Timp1 interacts with beta-1 integrin and CD63 along melanoma genesis and confers anoikis resistance by activating PI3-K signaling pathway independently of Akt phosphorylation."
    Toricelli M., Melo F.H., Peres G.B., Silva D.C., Jasiulionis M.G.
    Mol. Cancer 12:22-22(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION IN A COMPLEX WITH CD63 AND ITGB1.
  25. "TIMP-1 modulates chemotaxis of human neural stem cells through CD63 and integrin signalling."
    Lee S.Y., Kim J.M., Cho S.Y., Kim H.S., Shin H.S., Jeon J.Y., Kausar R., Jeong S.Y., Lee Y.S., Lee M.A.
    Biochem. J. 459:565-576(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION.
  26. Cited for: REVIEW.
  27. "Mechanism of inhibition of the human matrix metalloproteinase stromelysin-1 by TIMP-1."
    Gomis-Rueth F.-X., Maskos K., Betz M., Bergner A., Huber R., Suzuki K., Yoshida N., Nagase H., Brew K., Bourenkov G.P., Bartunik H., Bode W.
    Nature 389:77-81(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.80 ANGSTROMS) OF 24-207 IN COMPLEX WITH MMP3, INTERACTION WITH MMP3.
  28. "NMR structure of tissue inhibitor of metalloproteinases-1 implicates localized induced fit in recognition of matrix metalloproteinases."
    Wu B., Arumugam S., Gao G., Lee G.I., Semenchenko V., Huang W., Brew K., Van Doren S.R.
    J. Mol. Biol. 295:257-268(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: STRUCTURE BY NMR OF 24-149, DISULFIDE BOND.
  29. "Global orientation of bound MMP-3 and N-TIMP-1 in solution via residual dipolar couplings."
    Arumugam S., Van Doren S.R.
    Biochemistry 42:7950-7958(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: STRUCTURE BY NMR OF 24-149 IN COMPLEX WITH MMP3, INTERACTION WITH MMP3.
  30. "Crystal structure of the catalytic domain of matrix metalloproteinase-1 in complex with the inhibitory domain of tissue inhibitor of metalloproteinase-1."
    Iyer S., Wei S., Brew K., Acharya K.R.
    J. Biol. Chem. 282:364-371(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.54 ANGSTROMS) OF 24-149 IN COMPLEX WITH MMP1, FUNCTION, INTERACTION WITH MMP1 AND MMP3, DISULFIDE BOND, MUTAGENESIS OF THR-25.
  31. "The intrinsic protein flexibility of endogenous protease inhibitor TIMP-1 controls its binding interface and affects its function."
    Grossman M., Tworowski D., Dym O., Lee M.H., Levy Y., Murphy G., Sagi I.
    Biochemistry 49:6184-6192(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.05 ANGSTROMS) OF 24-148 OF MUTANT LEU-121 IN COMPLEX WITH MMP14, FUNCTION, INTERACTION WITH MMP14, DISULFIDE BOND, MUTAGENESIS OF THR-121.
  32. "Matrix metalloproteinase-10 (MMP10) interaction with tissue inhibitors of metalloproteinases TIMP-1 and TIMP-2: binding studies and crystal structure."
    Batra J., Robinson J., Soares A.S., Fields A.P., Radisky D.C., Radisky E.S.
    J. Biol. Chem. 287:15935-15946(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.90 ANGSTROMS) OF 24-207 IN COMPLEX WITH MMP10, FUNCTION, INTERACTION WITH MMP10, DISULFIDE BOND.

Entry informationi

Entry nameiTIMP1_HUMAN
AccessioniPrimary (citable) accession number: P01033
Secondary accession number(s): Q14252, Q9UCU1
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: July 21, 1986
Last modified: October 29, 2014
This is version 171 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome X
    Human chromosome X: entries, gene names and cross-references to MIM
  2. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3