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P03956

- MMP1_HUMAN

UniProt

P03956 - MMP1_HUMAN

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Protein
Interstitial collagenase
Gene
MMP1, CLG
Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

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)
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 oxygen By similarity
Metal bindingi329 – 3291Calcium 4; via carbonyl oxygen By similarity
Metal bindingi378 – 3781Calcium 4; via carbonyl oxygen By similarity
Metal bindingi427 – 4271Calcium 4; via carbonyl oxygen By 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
Complete GO annotation...

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 Inferred 1 Publication

GO - Cellular componenti

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

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 – 1919
Add
BLAST
Propeptidei20 – 9980Activation peptide
PRO_0000028703Add
BLAST
Chaini100 – 469370Interstitial collagenase
PRO_0000028704Add
BLAST
Chaini100 – 26917022 kDa interstitial collagenase
PRO_0000028705Add
BLAST
Chaini270 – 46920027 kDa interstitial collagenase
PRO_0000028706Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi120 – 1201N-linked (GlcNAc...)1 Publication
CAR_000105
Disulfide bondi278 ↔ 466 By 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. 1 interaction.
MINTiMINT-198818.
STRINGi9606.ENSP00000322788.

Structurei

Secondary structure

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.

Miscellaneous databases

EvolutionaryTraceiP03956.

Family & Domainsi

Domains and Repeats

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

Region

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

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi90 – 978Cysteine switch By 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.
Contains 4 hemopexin repeats.

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

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 conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti43 – 431N → K in AAA35700. 1 Publication
Sequence conflicti64 – 641Missing in AAA35700. 1 Publication
Sequence conflicti115 – 1151T → R in AAA35699. 1 Publication
Sequence conflicti200 – 2001D → H in CAA28858. 1 Publication
Sequence conflicti208 – 2081R → T in CAA28858. 1 Publication
Sequence conflicti317 – 3171I → T in CAA28858. 1 Publication
Sequence conflicti410 – 4101G → S in AAA35699. 1 Publication

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. 1 interaction.
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

« Hide 'large scale' publications
  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: September 3, 2014
This is version 175 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

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