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P01033

- TIMP1_HUMAN

UniProt

P01033 - TIMP1_HUMAN

Protein

Metalloproteinase inhibitor 1

Gene

TIMP1

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 170 (01 Oct 2014)
      Sequence version 1 (21 Jul 1986)
      Previous versions | rss
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    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
    4. protein binding 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

    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: UniProt
    5. platelet alpha granule lumen Source: Reactome

    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. 2 Publications
    Mutagenesisi25 – 251T → V: Normal interaction with metalloproteinase. 2 Publications
    Mutagenesisi30 – 301H → A: Nearly abolishes metalloproteinase inhibition. 2 Publications
    Mutagenesisi32 – 321Q → A: Nearly abolishes metalloproteinase inhibition. 2 Publications
    Mutagenesisi121 – 1211T → L: Decreases protein flexibility and increases affinity for MMP14. 2 Publications

    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

    ArrayExpressiP01033.
    BgeeiP01033.
    CleanExiHS_TIMP1.
    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

    MAPFEPLASG ILLLLWLIAP SRACTCVPPH PQTAFCNSDL VIRAKFVGTP    50
    EVNQTTLYQR YEIKMTKMYK GFQALGDAAD IRFVYTPAME SVCGYFHRSH 100
    NRSEEFLIAG KLQDGLLHIT TCSFVAPWNS LSLAQRRGFT KTYTVGCEEC 150
    TVFPCLSIPC KLQSGTHCLW TDQLLQGSEK GFQSRHLACL PREPGLCTWQ 200
    SLRSQIA 207
    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

    ArrayExpressi P01033.
    Bgeei P01033.
    CleanExi HS_TIMP1.
    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

    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 1, 2014
    This is version 170 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