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P03956

- MMP1_HUMAN

UniProt

P03956 - MMP1_HUMAN

Protein

Interstitial collagenase

Gene

MMP1

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 176 (01 Oct 2014)
      Sequence version 3 (01 Dec 1992)
      Previous versions | rss
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    Functioni

    Cleaves collagens of types I, II, and III at one site in the helical domain. Also cleaves collagens of types VII and X. In case of HIV infection, interacts and cleaves the secreted viral Tat protein, leading to a decrease in neuronal Tat's mediated neurotoxicity.1 Publication

    Catalytic activityi

    Cleavage of the triple helix of collagen at about three-quarters of the length of the molecule from the N-terminus, at 775-Gly-|-Ile-776 in the alpha-1(I) chain. Cleaves synthetic substrates and alpha-macroglobulins at bonds where P1' is a hydrophobic residue.

    Cofactori

    Binds 4 calcium ions per subunit.
    Binds 2 zinc ions per subunit.

    Enzyme regulationi

    Can be activated without removal of the activation peptide.

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Metal bindingi92 – 921Zinc 2; in inhibited form
    Metal bindingi124 – 1241Calcium 1
    Sitei143 – 1431Not glycosylated (PubMed:10092871)1 Publication
    Metal bindingi158 – 1581Calcium 2
    Metal bindingi168 – 1681Zinc 1
    Metal bindingi170 – 1701Zinc 1
    Metal bindingi175 – 1751Calcium 3
    Metal bindingi176 – 1761Calcium 3; via carbonyl oxygen
    Metal bindingi178 – 1781Calcium 3; via carbonyl oxygen
    Metal bindingi180 – 1801Calcium 3; via carbonyl oxygen
    Metal bindingi183 – 1831Zinc 1
    Metal bindingi190 – 1901Calcium 2; via carbonyl oxygen
    Metal bindingi192 – 1921Calcium 2; via carbonyl oxygen
    Metal bindingi194 – 1941Calcium 2
    Metal bindingi196 – 1961Zinc 1
    Metal bindingi198 – 1981Calcium 3
    Metal bindingi199 – 1991Calcium 1
    Metal bindingi201 – 2011Calcium 3
    Metal bindingi218 – 2181Zinc 2; catalytic
    Active sitei219 – 2191
    Metal bindingi222 – 2221Zinc 2; catalytic
    Metal bindingi228 – 2281Zinc 2; catalytic
    Sitei269 – 2702Cleavage; by autolysis
    Metal bindingi285 – 2851Calcium 4; via carbonyl oxygenBy similarity
    Metal bindingi329 – 3291Calcium 4; via carbonyl oxygenBy similarity
    Metal bindingi378 – 3781Calcium 4; via carbonyl oxygenBy similarity
    Metal bindingi427 – 4271Calcium 4; via carbonyl oxygenBy similarity

    GO - Molecular functioni

    1. calcium ion binding Source: InterPro
    2. metalloendopeptidase activity Source: BHF-UCL
    3. zinc ion binding Source: ProtInc

    GO - Biological processi

    1. blood coagulation Source: Reactome
    2. cellular protein metabolic process Source: Reactome
    3. collagen catabolic process Source: Reactome
    4. extracellular matrix disassembly Source: Reactome
    5. extracellular matrix organization Source: Reactome
    6. leukocyte migration Source: Reactome
    7. proteolysis Source: ProtInc
    8. viral process Source: UniProtKB-KW

    Keywords - Molecular functioni

    Hydrolase, Metalloprotease, Protease

    Keywords - Biological processi

    Collagen degradation, Host-virus interaction

    Keywords - Ligandi

    Calcium, Metal-binding, Zinc

    Enzyme and pathway databases

    ReactomeiREACT_118572. Degradation of the extracellular matrix.
    REACT_118682. Activation of Matrix Metalloproteinases.
    REACT_12560. Basigin interactions.
    REACT_150401. Collagen degradation.
    REACT_15428. Regulation of Insulin-like Growth Factor (IGF) transport and uptake by Insulin-like Growth Factor Binding Proteins (IGFBPs).
    REACT_197191. Collagen degradation.
    REACT_222620. Collagen degradation.

    Protein family/group databases

    MEROPSiM10.001.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Interstitial collagenase (EC:3.4.24.7)
    Alternative name(s):
    Fibroblast collagenase
    Matrix metalloproteinase-1
    Short name:
    MMP-1
    Cleaved into the following 2 chains:
    Gene namesi
    Name:MMP1
    Synonyms:CLG
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 11

    Organism-specific databases

    HGNCiHGNC:7155. MMP1.

    Subcellular locationi

    Secretedextracellular spaceextracellular matrix 1 Publication

    GO - Cellular componenti

    1. extracellular region Source: Reactome
    2. proteinaceous extracellular matrix Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Extracellular matrix, Secreted

    Pathology & Biotechi

    Organism-specific databases

    Orphaneti79408. Severe generalized recessive dystrophic epidermolysis bullosa.
    PharmGKBiPA30867.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 1919Add
    BLAST
    Propeptidei20 – 9980Activation peptide1 PublicationPRO_0000028703Add
    BLAST
    Chaini100 – 469370Interstitial collagenasePRO_0000028704Add
    BLAST
    Chaini100 – 26917022 kDa interstitial collagenasePRO_0000028705Add
    BLAST
    Chaini270 – 46920027 kDa interstitial collagenasePRO_0000028706Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Glycosylationi120 – 1201N-linked (GlcNAc...)1 PublicationCAR_000105
    Disulfide bondi278 ↔ 466By similarity

    Post-translational modificationi

    Undergoes autolytic cleavage to two major forms (22 kDa and 27 kDa). A minor form (25 kDa) is the glycosylated form of the 22 kDa form. The 27 kDa form has no activity while the 22/25 kDa form can act as activator for collagenase.1 Publication

    Keywords - PTMi

    Autocatalytic cleavage, Disulfide bond, Glycoprotein, Zymogen

    Proteomic databases

    PaxDbiP03956.
    PeptideAtlasiP03956.
    PRIDEiP03956.

    PTM databases

    PhosphoSiteiP03956.
    UniCarbKBiP03956.

    Miscellaneous databases

    PMAP-CutDBP03956.

    Expressioni

    Gene expression databases

    ArrayExpressiP03956.
    BgeeiP03956.
    CleanExiHS_MMP1.
    GenevestigatoriP03956.

    Interactioni

    Subunit structurei

    Interacts with HIV-1 Tat.1 Publication

    Protein-protein interaction databases

    BioGridi110456. 6 interactions.
    DIPiDIP-529N.
    IntActiP03956. 2 interactions.
    MINTiMINT-198818.
    STRINGi9606.ENSP00000322788.

    Structurei

    Secondary structure

    1
    469
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi33 – 419
    Helixi59 – 7012
    Helixi81 – 877
    Beta strandi103 – 1064
    Beta strandi112 – 1187
    Beta strandi123 – 1253
    Helixi127 – 14216
    Beta strandi144 – 1463
    Beta strandi148 – 1514
    Beta strandi153 – 1553
    Beta strandi158 – 1647
    Beta strandi169 – 1713
    Beta strandi176 – 1794
    Beta strandi182 – 1843
    Beta strandi187 – 1893
    Turni190 – 1934
    Beta strandi195 – 1984
    Beta strandi204 – 2096
    Helixi212 – 22312
    Beta strandi237 – 2393
    Helixi250 – 26011
    Beta strandi285 – 2906
    Beta strandi293 – 2986
    Beta strandi301 – 3044
    Beta strandi309 – 3113
    Beta strandi313 – 3164
    Helixi317 – 3193
    Beta strandi330 – 3345
    Helixi335 – 3373
    Beta strandi339 – 3446
    Beta strandi347 – 3526
    Beta strandi361 – 3633
    Helixi364 – 3685
    Beta strandi379 – 3824
    Turni384 – 3863
    Beta strandi388 – 3936
    Beta strandi396 – 4016
    Turni402 – 4054
    Beta strandi412 – 4143
    Helixi415 – 4184
    Beta strandi427 – 4326
    Beta strandi435 – 4406
    Beta strandi443 – 4486
    Turni449 – 4524
    Beta strandi453 – 4597
    Turni460 – 4634

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1AYKNMR-A101-269[»]
    1CGEX-ray1.90A102-269[»]
    1CGFX-ray2.10A/B102-263[»]
    1CGLX-ray2.40A/B101-269[»]
    1HFCX-ray1.50A101-269[»]
    1SU3X-ray2.20A/B20-469[»]
    2AYKNMR-A101-269[»]
    2CLTX-ray2.67A/B100-466[»]
    2J0TX-ray2.54A/B/C101-269[»]
    2TCLX-ray2.20A101-269[»]
    3AYKNMR-A101-269[»]
    3SHIX-ray2.20A/G/M106-261[»]
    4AUOX-ray3.00A/B100-466[»]
    4AYKNMR-A101-269[»]
    966CX-ray1.90A108-264[»]
    ProteinModelPortaliP03956.
    SMRiP03956. Positions 32-466.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP03956.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Repeati275 – 32450Hemopexin 1Add
    BLAST
    Repeati325 – 37147Hemopexin 2Add
    BLAST
    Repeati374 – 42249Hemopexin 3Add
    BLAST
    Repeati423 – 46644Hemopexin 4Add
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni98 – 276179MetalloproteaseAdd
    BLAST

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi90 – 978Cysteine switchBy similarity

    Domaini

    There are two distinct domains in this protein; the catalytic N-terminal, and the C-terminal which is involved in substrate specificity and in binding TIMP (tissue inhibitor of metalloproteinases).
    The conserved cysteine present in the cysteine-switch motif binds the catalytic zinc ion, thus inhibiting the enzyme. The dissociation of the cysteine from the zinc ion upon the activation-peptide release activates the enzyme.

    Sequence similaritiesi

    Belongs to the peptidase M10A family.Curated
    Contains 4 hemopexin repeats.Curated

    Keywords - Domaini

    Repeat, Signal

    Phylogenomic databases

    eggNOGiNOG258253.
    HOGENOMiHOG000217927.
    HOVERGENiHBG052484.
    InParanoidiP03956.
    KOiK01388.
    OMAiMRTNPFY.
    OrthoDBiEOG7XPZ57.
    PhylomeDBiP03956.
    TreeFamiTF315428.

    Family and domain databases

    Gene3Di2.110.10.10. 1 hit.
    3.40.390.10. 1 hit.
    InterProiIPR000585. Hemopexin-like_dom.
    IPR018487. Hemopexin-like_repeat.
    IPR018486. Hemopexin_CS.
    IPR024079. MetalloPept_cat_dom.
    IPR001818. Pept_M10_metallopeptidase.
    IPR021190. Pept_M10A.
    IPR016293. Pept_M10A_stromelysin-type.
    IPR021158. Pept_M10A_Zn_BS.
    IPR006026. Peptidase_Metallo.
    IPR002477. Peptidoglycan-bd-like.
    [Graphical view]
    PfamiPF00045. Hemopexin. 4 hits.
    PF00413. Peptidase_M10. 1 hit.
    PF01471. PG_binding_1. 1 hit.
    [Graphical view]
    PIRSFiPIRSF001191. Peptidase_M10A_matrix. 1 hit.
    PRINTSiPR00138. MATRIXIN.
    SMARTiSM00120. HX. 4 hits.
    SM00235. ZnMc. 1 hit.
    [Graphical view]
    SUPFAMiSSF47090. SSF47090. 1 hit.
    SSF50923. SSF50923. 1 hit.
    PROSITEiPS00546. CYSTEINE_SWITCH. 1 hit.
    PS00024. HEMOPEXIN. 1 hit.
    PS51642. HEMOPEXIN_2. 4 hits.
    PS00142. ZINC_PROTEASE. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

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

    P03956-1 [UniParc]FASTAAdd to Basket

    « Hide

    MHSFPPLLLL LFWGVVSHSF PATLETQEQD VDLVQKYLEK YYNLKNDGRQ    50
    VEKRRNSGPV VEKLKQMQEF FGLKVTGKPD AETLKVMKQP RCGVPDVAQF 100
    VLTEGNPRWE QTHLTYRIEN YTPDLPRADV DHAIEKAFQL WSNVTPLTFT 150
    KVSEGQADIM ISFVRGDHRD NSPFDGPGGN LAHAFQPGPG IGGDAHFDED 200
    ERWTNNFREY NLHRVAAHEL GHSLGLSHST DIGALMYPSY TFSGDVQLAQ 250
    DDIDGIQAIY GRSQNPVQPI GPQTPKACDS KLTFDAITTI RGEVMFFKDR 300
    FYMRTNPFYP EVELNFISVF WPQLPNGLEA AYEFADRDEV RFFKGNKYWA 350
    VQGQNVLHGY PKDIYSSFGF PRTVKHIDAA LSEENTGKTY FFVANKYWRY 400
    DEYKRSMDPG YPKMIAHDFP GIGHKVDAVF MKDGFFYFFH GTRQYKFDPK 450
    TKRILTLQKA NSWFNCRKN 469
    Length:469
    Mass (Da):54,007
    Last modified:December 1, 1992 - v3
    Checksum:i4B1361DCF4C54B20
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti43 – 431N → K in AAA35700. (PubMed:3027129)Curated
    Sequence conflicti64 – 641Missing in AAA35700. (PubMed:3027129)Curated
    Sequence conflicti115 – 1151T → R in AAA35699. (PubMed:3009463)Curated
    Sequence conflicti200 – 2001D → H in CAA28858. (PubMed:3030290)Curated
    Sequence conflicti208 – 2081R → T in CAA28858. (PubMed:3030290)Curated
    Sequence conflicti317 – 3171I → T in CAA28858. (PubMed:3030290)Curated
    Sequence conflicti410 – 4101G → S in AAA35699. (PubMed:3009463)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti29 – 291Q → P.
    Corresponds to variant rs554499 [ dbSNP | Ensembl ].
    VAR_011969
    Natural varianti191 – 1911I → V.1 Publication
    Corresponds to variant rs17879973 [ dbSNP | Ensembl ].
    VAR_021024
    Natural varianti252 – 2521D → G.
    Corresponds to variant rs513964 [ dbSNP | Ensembl ].
    VAR_011970
    Natural varianti262 – 2621R → S.
    Corresponds to variant rs12282811 [ dbSNP | Ensembl ].
    VAR_054005
    Natural varianti405 – 4051R → Q.1 Publication
    Corresponds to variant rs17879165 [ dbSNP | Ensembl ].
    VAR_021025
    Natural varianti406 – 4061S → T.1 Publication
    Corresponds to variant rs17884120 [ dbSNP | Ensembl ].
    VAR_021026

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X54925 mRNA. Translation: CAA38691.1.
    X05231 mRNA. Translation: CAA28858.1.
    M13509 mRNA. Translation: AAA35699.1.
    U78045 Genomic DNA. Translation: AAB36941.1.
    BT006874 mRNA. Translation: AAP35520.1.
    AY769434 Genomic DNA. Translation: AAV28732.1.
    BC013875 mRNA. Translation: AAH13875.1.
    M16567 Genomic DNA. Translation: AAA52033.1.
    M15996 mRNA. Translation: AAA35700.1.
    CCDSiCCDS8322.1.
    PIRiA37308. KCHUI.
    RefSeqiNP_002412.1. NM_002421.3.
    UniGeneiHs.83169.

    Genome annotation databases

    EnsembliENST00000315274; ENSP00000322788; ENSG00000196611.
    GeneIDi4312.
    KEGGihsa:4312.
    UCSCiuc001phi.2. human.

    Polymorphism databases

    DMDMi116852.

    Keywords - Coding sequence diversityi

    Polymorphism

    Cross-referencesi

    Web resourcesi

    NIEHS-SNPs
    Wikipedia

    Collagenase entry

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X54925 mRNA. Translation: CAA38691.1 .
    X05231 mRNA. Translation: CAA28858.1 .
    M13509 mRNA. Translation: AAA35699.1 .
    U78045 Genomic DNA. Translation: AAB36941.1 .
    BT006874 mRNA. Translation: AAP35520.1 .
    AY769434 Genomic DNA. Translation: AAV28732.1 .
    BC013875 mRNA. Translation: AAH13875.1 .
    M16567 Genomic DNA. Translation: AAA52033.1 .
    M15996 mRNA. Translation: AAA35700.1 .
    CCDSi CCDS8322.1.
    PIRi A37308. KCHUI.
    RefSeqi NP_002412.1. NM_002421.3.
    UniGenei Hs.83169.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1AYK NMR - A 101-269 [» ]
    1CGE X-ray 1.90 A 102-269 [» ]
    1CGF X-ray 2.10 A/B 102-263 [» ]
    1CGL X-ray 2.40 A/B 101-269 [» ]
    1HFC X-ray 1.50 A 101-269 [» ]
    1SU3 X-ray 2.20 A/B 20-469 [» ]
    2AYK NMR - A 101-269 [» ]
    2CLT X-ray 2.67 A/B 100-466 [» ]
    2J0T X-ray 2.54 A/B/C 101-269 [» ]
    2TCL X-ray 2.20 A 101-269 [» ]
    3AYK NMR - A 101-269 [» ]
    3SHI X-ray 2.20 A/G/M 106-261 [» ]
    4AUO X-ray 3.00 A/B 100-466 [» ]
    4AYK NMR - A 101-269 [» ]
    966C X-ray 1.90 A 108-264 [» ]
    ProteinModelPortali P03956.
    SMRi P03956. Positions 32-466.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 110456. 6 interactions.
    DIPi DIP-529N.
    IntActi P03956. 2 interactions.
    MINTi MINT-198818.
    STRINGi 9606.ENSP00000322788.

    Chemistry

    BindingDBi P03956.
    ChEMBLi CHEMBL2095216.
    GuidetoPHARMACOLOGYi 1628.

    Protein family/group databases

    MEROPSi M10.001.

    PTM databases

    PhosphoSitei P03956.
    UniCarbKBi P03956.

    Polymorphism databases

    DMDMi 116852.

    Proteomic databases

    PaxDbi P03956.
    PeptideAtlasi P03956.
    PRIDEi P03956.

    Protocols and materials databases

    DNASUi 4312.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000315274 ; ENSP00000322788 ; ENSG00000196611 .
    GeneIDi 4312.
    KEGGi hsa:4312.
    UCSCi uc001phi.2. human.

    Organism-specific databases

    CTDi 4312.
    GeneCardsi GC11M102660.
    H-InvDB HIX0201751.
    HGNCi HGNC:7155. MMP1.
    MIMi 120353. gene.
    neXtProti NX_P03956.
    Orphaneti 79408. Severe generalized recessive dystrophic epidermolysis bullosa.
    PharmGKBi PA30867.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG258253.
    HOGENOMi HOG000217927.
    HOVERGENi HBG052484.
    InParanoidi P03956.
    KOi K01388.
    OMAi MRTNPFY.
    OrthoDBi EOG7XPZ57.
    PhylomeDBi P03956.
    TreeFami TF315428.

    Enzyme and pathway databases

    Reactomei REACT_118572. Degradation of the extracellular matrix.
    REACT_118682. Activation of Matrix Metalloproteinases.
    REACT_12560. Basigin interactions.
    REACT_150401. Collagen degradation.
    REACT_15428. Regulation of Insulin-like Growth Factor (IGF) transport and uptake by Insulin-like Growth Factor Binding Proteins (IGFBPs).
    REACT_197191. Collagen degradation.
    REACT_222620. Collagen degradation.

    Miscellaneous databases

    EvolutionaryTracei P03956.
    GeneWikii MMP1.
    GenomeRNAii 4312.
    NextBioi 16969.
    PMAP-CutDB P03956.
    PROi P03956.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P03956.
    Bgeei P03956.
    CleanExi HS_MMP1.
    Genevestigatori P03956.

    Family and domain databases

    Gene3Di 2.110.10.10. 1 hit.
    3.40.390.10. 1 hit.
    InterProi IPR000585. Hemopexin-like_dom.
    IPR018487. Hemopexin-like_repeat.
    IPR018486. Hemopexin_CS.
    IPR024079. MetalloPept_cat_dom.
    IPR001818. Pept_M10_metallopeptidase.
    IPR021190. Pept_M10A.
    IPR016293. Pept_M10A_stromelysin-type.
    IPR021158. Pept_M10A_Zn_BS.
    IPR006026. Peptidase_Metallo.
    IPR002477. Peptidoglycan-bd-like.
    [Graphical view ]
    Pfami PF00045. Hemopexin. 4 hits.
    PF00413. Peptidase_M10. 1 hit.
    PF01471. PG_binding_1. 1 hit.
    [Graphical view ]
    PIRSFi PIRSF001191. Peptidase_M10A_matrix. 1 hit.
    PRINTSi PR00138. MATRIXIN.
    SMARTi SM00120. HX. 4 hits.
    SM00235. ZnMc. 1 hit.
    [Graphical view ]
    SUPFAMi SSF47090. SSF47090. 1 hit.
    SSF50923. SSF50923. 1 hit.
    PROSITEi PS00546. CYSTEINE_SWITCH. 1 hit.
    PS00024. HEMOPEXIN. 1 hit.
    PS51642. HEMOPEXIN_2. 4 hits.
    PS00142. ZINC_PROTEASE. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Cloning and characterization of human tumor cell interstitial collagenase."
      Templeton N.S., Brown P.D., Levy A.T., Margulies I.M.K., Liotta L.A., Stetler-Stevenson W.G.
      Cancer Res. 50:5431-5437(1990) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], SUBCELLULAR LOCATION.
    2. "Comparison of human stromelysin and collagenase by cloning and sequence analysis."
      Whitham S.E., Murphy G., Angel P., Rahmsdorf H.J., Smith B., Lyons A., Harris T.J.R., Reynolds J.J., Herrlich P., Docherty A.J.P.
      Biochem. J. 240:913-916(1986) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    3. "Human fibroblast collagenase. Complete primary structure and homology to an oncogene transformation-induced rat protein."
      Goldberg G.I., Wilhelm S.M., Kronberger A., Bauer E.A., Grant G.A., Eisen A.Z.
      J. Biol. Chem. 261:6600-6605(1986) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    4. "Three matrix metalloproteinases on 81kb of P1 insert."
      Lin D., Duncan M., Allen E., Araujo R., Aparicio A., Chai A., Chung E., Davis K., Federspiel N., Hyman R., Kalman S., Komp C., Kurdi O., Lashkari D., Lew H., Namath A., Oefner P., Roberts D., Heller R., Davis R.W.
      Submitted (DEC-1996) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    5. "Cloning of human full-length CDSs in BD Creator(TM) system donor vector."
      Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., Phelan M., Farmer A.
      Submitted (OCT-2004) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    6. NIEHS SNPs program
      Submitted (SEP-2004) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANTS VAL-191; GLN-405 AND THR-406.
    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: Ovary.
    8. "12-O-tetradecanoyl-phorbol-13-acetate induction of the human collagenase gene is mediated by an inducible enhancer element located in the 5'-flanking region."
      Angel P., Baumann I., Stein B., Delius H., Rahmsdorf H.J., Herrlich P.
      Mol. Cell. Biol. 7:2256-2266(1987) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-35.
    9. "Molecular cloning of human synovial cell collagenase and selection of a single gene from genomic DNA."
      Brinckerhoff C.E., Ruby P.L., Austin S.D., Fini M.E., White H.D.
      J. Clin. Invest. 79:542-546(1987) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1-70.
      Tissue: Synovial cell.
    10. "Fragments of human fibroblast collagenase. Purification and characterization."
      Clark I.M., Cawston T.E.
      Biochem. J. 263:201-206(1989) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 100-112 AND 270-287.
      Tissue: Fibroblast.
    11. "Human fibroblast collagenase contains an amino acid sequence homologous to the zinc-binding site of Serratia protease."
      McKerrow J.H.
      J. Biol. Chem. 262:5943-5943(1987) [PubMed] [Europe PMC] [Abstract]
      Cited for: SIMILARITY TO THERMOLYSIN TYPE PROTEASES.
    12. "Interstitial collagenase (matrix metalloproteinase-1) expresses serpinase activity."
      Desrochers P.E., Jeffrey J.J., Weiss S.J.
      J. Clin. Invest. 87:2258-2265(1991) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    13. "N-glycan structures of matrix metalloproteinase-1 derived from human fibroblasts and from HT-1080 fibrosarcoma cells."
      Saarinen J., Welgus H.G., Flizar C.A., Kalkkinen N., Helin J.
      Eur. J. Biochem. 259:829-840(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: GLYCOSYLATION AT ASN-120.
    14. "Interaction of HIV Tat and matrix metalloproteinase in HIV neuropathogenesis: a new host defense mechanism."
      Rumbaugh J., Turchan-Cholewo J., Galey D., St Hillaire C., Anderson C., Conant K., Nath A.
      FASEB J. 20:1736-1738(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH HIV-1 TAT.
    15. "Structure of the catalytic domain of human fibroblast collagenase complexed with an inhibitor."
      Borkakoti N., Winkler F.K., Williams D.H., D'Arcy A., Broadhurst M.J., Brown P.A., Johnson W.H., Murray E.J.
      Nat. Struct. Biol. 1:106-110(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF 100-269.
    16. "Crystal structures of recombinant 19-kDa human fibroblast collagenase complexed to itself."
      Lovejoy B., Hassell A.M., Luther M.A., Weigl D., Jordan S.R.
      Biochemistry 33:8207-8217(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 102-269.
    17. "Structure of the catalytic domain of fibroblast collagenase complexed with an inhibitor."
      Lovejoy B., Cleasby A., Hassell A.M., Longley K., Luther M.A., Weigl D., McGeehan G., McElroy A.B., Drewry D., Lambert M.H., Jordan S.R.
      Science 263:375-377(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF 102-269.
    18. Cited for: X-RAY CRYSTALLOGRAPHY (1.56 ANGSTROMS) OF 101-269.
    19. "High-resolution solution structure of the inhibitor-free catalytic fragment of human fibroblast collagenase determined by multidimensional NMR."
      Moy F.J., Chanda P.K., Cosmi S., Pisano M.R., Urbano C., Wilhelm J., Powers R.
      Biochemistry 37:1495-1504(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: STRUCTURE BY NMR OF 101-269.

    Entry informationi

    Entry nameiMMP1_HUMAN
    AccessioniPrimary (citable) accession number: P03956
    Secondary accession number(s): P08156
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: October 23, 1986
    Last sequence update: December 1, 1992
    Last modified: October 1, 2014
    This is version 176 of the entry and version 3 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 11
      Human chromosome 11: entries, gene names and cross-references to MIM
    2. Human entries with polymorphisms or disease mutations
      List of human entries with polymorphisms or disease mutations
    3. Human polymorphisms and disease mutations
      Index of human polymorphisms and disease mutations
    4. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    5. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    6. Peptidase families
      Classification of peptidase families and list of entries
    7. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3