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Q99542

- MMP19_HUMAN

UniProt

Q99542 - MMP19_HUMAN

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Protein

Matrix metalloproteinase-19

Gene

MMP19

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

Functioni

Endopeptidase that degrades various components of the extracellular matrix, such as aggrecan and cartilage oligomeric matrix protein (comp), during development, haemostasis and pathological conditions (arthritic disease). May also play a role in neovascularization or angiogenesis. Hydrolyzes collagen type IV, laminin, nidogen, nascin-C isoform, fibronectin, and type I gelatin.2 Publications

Catalytic activityi

Cleaves aggrecan at the 360-Ser-|-Phe-361 site.

Cofactori

Binds 1 zinc ion per subunit.By similarity
Calcium.By similarity

Enzyme regulationi

Strongly inhibited by TIMP-2, TIMP-3 and TIMP-4, while TIMP-1 is less efficient.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi85 – 851Zinc; in inhibited formBy similarity
Metal bindingi212 – 2121Zinc; catalyticPROSITE-ProRule annotation
Active sitei213 – 2131PROSITE-ProRule annotation
Metal bindingi216 – 2161Zinc; catalyticPROSITE-ProRule annotation
Metal bindingi222 – 2221Zinc; catalyticPROSITE-ProRule annotation

GO - Molecular functioni

  1. calcium ion binding Source: InterPro
  2. metalloendopeptidase activity Source: InterPro
  3. zinc ion binding Source: InterPro

GO - Biological processi

  1. angiogenesis Source: UniProtKB-KW
  2. cell differentiation Source: UniProtKB-KW
  3. collagen catabolic process Source: Reactome
  4. extracellular matrix disassembly Source: Reactome
  5. extracellular matrix organization Source: Reactome
  6. luteolysis Source: Ensembl
  7. ovarian follicle development Source: Ensembl
  8. ovulation from ovarian follicle Source: Ensembl
  9. proteolysis Source: UniProtKB
  10. response to cAMP Source: Ensembl
  11. response to hormone Source: Ensembl
Complete GO annotation...

Keywords - Molecular functioni

Developmental protein, Hydrolase, Metalloprotease, Protease

Keywords - Biological processi

Angiogenesis, Collagen degradation, Differentiation

Keywords - Ligandi

Calcium, Metal-binding, Zinc

Enzyme and pathway databases

ReactomeiREACT_118572. Degradation of the extracellular matrix.
REACT_150401. Collagen degradation.

Protein family/group databases

MEROPSiM10.021.

Names & Taxonomyi

Protein namesi
Recommended name:
Matrix metalloproteinase-19 (EC:3.4.24.-)
Short name:
MMP-19
Alternative name(s):
Matrix metalloproteinase RASI
Matrix metalloproteinase-18
Short name:
MMP-18
Gene namesi
Name:MMP19
Synonyms:MMP18, RASI
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 12

Organism-specific databases

HGNCiHGNC:7165. MMP19.

Subcellular locationi

GO - Cellular componenti

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

Keywords - Cellular componenti

Extracellular matrix, Secreted

Pathology & Biotechi

Involvement in diseasei

May play a role in pathological processes participating in rheumatoid arthritis (RA)-associated joint tissue destruction. Autoantigen anti-MMP19 are frequent in RA patients.

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi88 – 881E → P: Reduced autolysis rate. 1 Publication
Mutagenesisi90 – 901P → V: Reduced autolysis rate. 1 Publication

Organism-specific databases

PharmGKBiPA30876.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 1818Sequence AnalysisAdd
BLAST
Propeptidei19 – 97791 PublicationPRO_0000028826Add
BLAST
Chaini98 – 508411Matrix metalloproteinase-19PRO_0000028827Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi289 ↔ 472By similarity
Glycosylationi464 – 4641N-linked (GlcNAc...)Sequence Analysis

Post-translational modificationi

Activated by autolytic cleavage after Lys-97.
Tyrosine phosphorylated by PKDCC/VLK.1 Publication

Keywords - PTMi

Disulfide bond, Glycoprotein, Phosphoprotein, Zymogen

Proteomic databases

PaxDbiQ99542.
PRIDEiQ99542.

PTM databases

PhosphoSiteiQ99542.

Expressioni

Tissue specificityi

Expressed in mammary gland, placenta, lung, pancreas, ovary, small intestine, spleen, thymus, prostate, testis colon, heart and blood vessel walls. Not detected in brain and peripheral blood leukocytes. Also expressed in the synovial fluid of normal and rheumatoid patients.

Gene expression databases

BgeeiQ99542.
CleanExiHS_MMP19.
ExpressionAtlasiQ99542. baseline and differential.
GenevestigatoriQ99542.

Organism-specific databases

HPAiHPA012845.

Interactioni

Protein-protein interaction databases

IntActiQ99542. 1 interaction.
STRINGi9606.ENSP00000313437.

Structurei

3D structure databases

ProteinModelPortaliQ99542.
SMRiQ99542. Positions 38-456.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Repeati286 – 33348Hemopexin 1Add
BLAST
Repeati334 – 38047Hemopexin 2Add
BLAST
Repeati381 – 42545Hemopexin 3Add
BLAST
Repeati426 – 47247Hemopexin 4Add
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi83 – 908Cysteine switchBy similarity

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi265 – 2717Poly-Glu

Domaini

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

eggNOGiNOG295915.
GeneTreeiENSGT00760000119132.
HOGENOMiHOG000217927.
HOVERGENiHBG052484.
InParanoidiQ99542.
KOiK07998.
OMAiWMHCHPQ.
PhylomeDBiQ99542.
TreeFamiTF315428.

Family and domain databases

Gene3Di1.10.101.10. 1 hit.
2.110.10.10. 1 hit.
3.40.390.10. 1 hit.
InterProiIPR000585. Hemopexin-like_dom.
IPR018487. Hemopexin-like_repeat.
IPR024079. MetalloPept_cat_dom.
IPR028724. MMP19.
IPR001818. Pept_M10_metallopeptidase.
IPR021190. Pept_M10A.
IPR016293. Pept_M10A_stromelysin-type.
IPR006026. Peptidase_Metallo.
IPR002477. Peptidoglycan-bd-like.
[Graphical view]
PANTHERiPTHR10201:SF117. PTHR10201:SF117. 1 hit.
PfamiPF00045. Hemopexin. 3 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.
PROSITEiPS51642. HEMOPEXIN_2. 4 hits.
PS00142. ZINC_PROTEASE. 1 hit.
[Graphical view]

Sequences (4)i

Sequence statusi: Complete.

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

This entry describes 4 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: Q99542) [UniParc]FASTAAdd to Basket

Also known as: RASI-1, RASI-11

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MNCQQLWLGF LLPMTVSGRV LGLAEVAPVD YLSQYGYLQK PLEGSNNFKP
60 70 80 90 100
EDITEALRAF QEASELPVSG QLDDATRARM RQPRCGLEDP FNQKTLKYLL
110 120 130 140 150
LGRWRKKHLT FRILNLPSTL PPHTARAALR QAFQDWSNVA PLTFQEVQAG
160 170 180 190 200
AADIRLSFHG RQSSYCSNTF DGPGRVLAHA DIPELGSVHF DEDEFWTEGT
210 220 230 240 250
YRGVNLRIIA AHEVGHALGL GHSRYSQALM APVYEGYRPH FKLHPDDVAG
260 270 280 290 300
IQALYGKKSP VIRDEEEEET ELPTVPPVPT EPSPMPDPCS SELDAMMLGP
310 320 330 340 350
RGKTYAFKGD YVWTVSDSGP GPLFRVSALW EGLPGNLDAA VYSPRTQWIH
360 370 380 390 400
FFKGDKVWRY INFKMSPGFP KKLNRVEPNL DAALYWPLNQ KVFLFKGSGY
410 420 430 440 450
WQWDELARTD FSSYPKPIKG LFTGVPNQPS AAMSWQDGRV YFFKGKVYWR
460 470 480 490 500
LNQQLRVEKG YPRNISHNWM HCRPRTIDTT PSGGNTTPSG TGITLDTTLS

ATETTFEY
Length:508
Mass (Da):57,357
Last modified:May 1, 1997 - v1
Checksum:iBA480549AA9A8972
GO
Isoform 2 (identifier: Q99542-3) [UniParc]FASTAAdd to Basket

Also known as: RASI-9

The sequence of this isoform differs from the canonical sequence as follows:
     1-286: Missing.
     287-298: DPCSSELDAMML → MGVTWDFSMSNG

Show »
Length:222
Mass (Da):25,350
Checksum:i594DBE2F520DC0FE
GO
Isoform 3 (identifier: Q99542-4) [UniParc]FASTAAdd to Basket

Also known as: RASI-6

The sequence of this isoform differs from the canonical sequence as follows:
     58-63: RAFQEA → SLRSAG
     64-508: Missing.

Note: May be produced at very low levels due to a premature stop codon in the mRNA, leading to nonsense-mediated mRNA decay.

Show »
Length:63
Mass (Da):6,931
Checksum:iC134E217099633E8
GO
Isoform 4 (identifier: Q99542-5) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     174-255: Missing.
     300-387: PRGKTYAFKG...PNLDAALYWP → EAPPLQAVGR...LASNTMDSLL
     388-508: Missing.

Note: No experimental confirmation available.

Show »
Length:305
Mass (Da):33,793
Checksum:i70E8A1C240863A8E
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti376 – 3761V → S in CAA69913. (PubMed:8920941)Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti103 – 1031R → C.1 Publication
Corresponds to variant rs17844794 [ dbSNP | Ensembl ].
VAR_021036
Natural varianti245 – 2451P → S.
Corresponds to variant rs1056784 [ dbSNP | Ensembl ].
VAR_054006
Natural varianti488 – 4881P → T.1 Publication
Corresponds to variant rs17118042 [ dbSNP | Ensembl ].
VAR_021037
Natural varianti491 – 4911T → M.1 Publication
Corresponds to variant rs17844806 [ dbSNP | Ensembl ].
VAR_021038

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 286286Missing in isoform 2. 1 PublicationVSP_005457Add
BLAST
Alternative sequencei58 – 636RAFQEA → SLRSAG in isoform 3. 1 PublicationVSP_041893
Alternative sequencei64 – 508445Missing in isoform 3. 1 PublicationVSP_041894Add
BLAST
Alternative sequencei174 – 25582Missing in isoform 4. 1 PublicationVSP_054573Add
BLAST
Alternative sequencei287 – 29812DPCSS…DAMML → MGVTWDFSMSNG in isoform 2. 1 PublicationVSP_005458Add
BLAST
Alternative sequencei300 – 38788PRGKT…ALYWP → EAPPLQAVGRRWGQPADPEA WTNGSDMGLQHEQWRAPWED LCFQGGLCVDCIRFRTGPLV PSVCPLGGAPRKPGCCCLLA SNTMDSLL in isoform 4. 1 PublicationVSP_054574Add
BLAST
Alternative sequencei388 – 508121Missing in isoform 4. 1 PublicationVSP_054575Add
BLAST

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
Y08622 mRNA. Translation: CAA69913.1.
X92521 mRNA. Translation: CAA63299.1.
U37791 mRNA. Translation: AAC51521.1.
U38321 mRNA. Translation: AAB63008.1.
U38431 mRNA. Translation: AAC99995.1. Sequence problems.
U38322 mRNA. Translation: AAB63009.1.
AK303202 mRNA. Translation: BAG64292.1.
AY706993 Genomic DNA. Translation: AAT97983.1.
AC023055 Genomic DNA. No translation available.
BC050368 mRNA. Translation: AAH50368.1.
CCDSiCCDS61146.1. [Q99542-5]
CCDS8895.1. [Q99542-1]
PIRiJC5082.
RefSeqiNP_001259030.1. NM_001272101.1. [Q99542-5]
NP_002420.1. NM_002429.5. [Q99542-1]
UniGeneiHs.591033.

Genome annotation databases

EnsembliENST00000322569; ENSP00000313437; ENSG00000123342. [Q99542-1]
ENST00000409200; ENSP00000386625; ENSG00000123342. [Q99542-5]
ENST00000552872; ENSP00000446776; ENSG00000123342. [Q99542-4]
GeneIDi4327.
KEGGihsa:4327.
UCSCiuc001sia.3. human. [Q99542-3]
uc001sib.4. human. [Q99542-1]
uc010spw.3. human.

Polymorphism databases

DMDMi12643345.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Web resourcesi

NIEHS-SNPs

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
Y08622 mRNA. Translation: CAA69913.1 .
X92521 mRNA. Translation: CAA63299.1 .
U37791 mRNA. Translation: AAC51521.1 .
U38321 mRNA. Translation: AAB63008.1 .
U38431 mRNA. Translation: AAC99995.1 . Sequence problems.
U38322 mRNA. Translation: AAB63009.1 .
AK303202 mRNA. Translation: BAG64292.1 .
AY706993 Genomic DNA. Translation: AAT97983.1 .
AC023055 Genomic DNA. No translation available.
BC050368 mRNA. Translation: AAH50368.1 .
CCDSi CCDS61146.1. [Q99542-5 ]
CCDS8895.1. [Q99542-1 ]
PIRi JC5082.
RefSeqi NP_001259030.1. NM_001272101.1. [Q99542-5 ]
NP_002420.1. NM_002429.5. [Q99542-1 ]
UniGenei Hs.591033.

3D structure databases

ProteinModelPortali Q99542.
SMRi Q99542. Positions 38-456.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

IntActi Q99542. 1 interaction.
STRINGi 9606.ENSP00000313437.

Chemistry

BindingDBi Q99542.
ChEMBLi CHEMBL1938214.
DrugBanki DB00786. Marimastat.

Protein family/group databases

MEROPSi M10.021.

PTM databases

PhosphoSitei Q99542.

Polymorphism databases

DMDMi 12643345.

Proteomic databases

PaxDbi Q99542.
PRIDEi Q99542.

Protocols and materials databases

DNASUi 4327.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000322569 ; ENSP00000313437 ; ENSG00000123342 . [Q99542-1 ]
ENST00000409200 ; ENSP00000386625 ; ENSG00000123342 . [Q99542-5 ]
ENST00000552872 ; ENSP00000446776 ; ENSG00000123342 . [Q99542-4 ]
GeneIDi 4327.
KEGGi hsa:4327.
UCSCi uc001sia.3. human. [Q99542-3 ]
uc001sib.4. human. [Q99542-1 ]
uc010spw.3. human.

Organism-specific databases

CTDi 4327.
GeneCardsi GC12M056230.
HGNCi HGNC:7165. MMP19.
HPAi HPA012845.
MIMi 601807. gene.
neXtProti NX_Q99542.
PharmGKBi PA30876.
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG295915.
GeneTreei ENSGT00760000119132.
HOGENOMi HOG000217927.
HOVERGENi HBG052484.
InParanoidi Q99542.
KOi K07998.
OMAi WMHCHPQ.
PhylomeDBi Q99542.
TreeFami TF315428.

Enzyme and pathway databases

Reactomei REACT_118572. Degradation of the extracellular matrix.
REACT_150401. Collagen degradation.

Miscellaneous databases

GeneWikii MMP19.
GenomeRNAii 4327.
NextBioi 17029.
PROi Q99542.
SOURCEi Search...

Gene expression databases

Bgeei Q99542.
CleanExi HS_MMP19.
ExpressionAtlasi Q99542. baseline and differential.
Genevestigatori Q99542.

Family and domain databases

Gene3Di 1.10.101.10. 1 hit.
2.110.10.10. 1 hit.
3.40.390.10. 1 hit.
InterProi IPR000585. Hemopexin-like_dom.
IPR018487. Hemopexin-like_repeat.
IPR024079. MetalloPept_cat_dom.
IPR028724. MMP19.
IPR001818. Pept_M10_metallopeptidase.
IPR021190. Pept_M10A.
IPR016293. Pept_M10A_stromelysin-type.
IPR006026. Peptidase_Metallo.
IPR002477. Peptidoglycan-bd-like.
[Graphical view ]
PANTHERi PTHR10201:SF117. PTHR10201:SF117. 1 hit.
Pfami PF00045. Hemopexin. 3 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 PS51642. HEMOPEXIN_2. 4 hits.
PS00142. ZINC_PROTEASE. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Identification of MMP-18, a putative novel human matrix metalloproteinase."
    Cossins J., Dudgeon T.J., Catlin G., Gearing A.J.H., Clements J.M.
    Biochem. Biophys. Res. Commun. 228:494-498(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    Tissue: Mammary gland.
  2. "Identification and characterization of a novel human matrix metalloproteinase with unique structural characteristics, chromosomal location and tissue distribution."
    Pendas A.M., Knaeuper V.V., Puente X.S., Llano E., Mattei M.-G., Apte S., Murphy G., Lopez-Otin C.
    J. Biol. Chem. 272:4281-4286(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    Tissue: Liver.
  3. "The matrix metalloproteinase RASI-1 is expressed in synovial blood vessels of a rheumatoid arthritis patient."
    Kolb C., Mauch S., Peter H.-H., Krawinkel U., Sedlacek R.
    Immunol. Lett. 57:83-88(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    Tissue: Rheumatoid arthritic synovial fluid.
  4. "Matrix metalloproteinase MMP-19 (RASI-1) is expressed on the surface of activated peripheral blood mononuclear cells and is detected as an autoantigen in rheumatoid arthritis."
    Sedlacek R., Mauch S., Kolb B., Schaetzlein C., Eibel H., Peter H.-H., Schmitt J., Krawinkel U.
    Immunobiology 198:408-423(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    Tissue: Rheumatoid arthritic synovial fluid.
  5. Mauch S., Sedlacek R., Krawinkel U., Schaetzlein C.
    Submitted (OCT-1995) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1; 2 AND 3).
  6. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
    Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
    , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
    Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 4).
    Tissue: Thymus.
  7. NIEHS SNPs program
    Submitted (AUG-2004) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANTS CYS-103; THR-488 AND MET-491.
  8. "The finished DNA sequence of human chromosome 12."
    Scherer S.E., Muzny D.M., Buhay C.J., Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V., Hume J., Jackson A., Khan Z.M., Kovar-Smith C., Lewis L.R.
    , Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R., Montgomery K.T., Morgan M.B., Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D., Lovering R.C., Wheeler D.A., Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z., Clerc-Blankenburg K.P., Davis C., Delgado O., Dinh H.H., Draper H., Gonzalez-Garay M.L., Havlak P., Jackson L.R., Jacob L.S., Kelly S.H., Li L., Li Z., Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O., Pasternak S., Perez L.M., Plopper F.J.H., Santibanez J., Shen H., Tabor P.E., Verduzco D., Waldron L., Wang Q., Williams G.A., Zhang J., Zhou J., Allen C.C., Amin A.G., Anyalebechi V., Bailey M., Barbaria J.A., Bimage K.E., Bryant N.P., Burch P.E., Burkett C.E., Burrell K.L., Calderon E., Cardenas V., Carter K., Casias K., Cavazos I., Cavazos S.R., Ceasar H., Chacko J., Chan S.N., Chavez D., Christopoulos C., Chu J., Cockrell R., Cox C.D., Dang M., Dathorne S.R., David R., Davis C.M., Davy-Carroll L., Deshazo D.R., Donlin J.E., D'Souza L., Eaves K.A., Egan A., Emery-Cohen A.J., Escotto M., Flagg N., Forbes L.D., Gabisi A.M., Garza M., Hamilton C., Henderson N., Hernandez O., Hines S., Hogues M.E., Huang M., Idlebird D.G., Johnson R., Jolivet A., Jones S., Kagan R., King L.M., Leal B., Lebow H., Lee S., LeVan J.M., Lewis L.C., London P., Lorensuhewa L.M., Loulseged H., Lovett D.A., Lucier A., Lucier R.L., Ma J., Madu R.C., Mapua P., Martindale A.D., Martinez E., Massey E., Mawhiney S., Meador M.G., Mendez S., Mercado C., Mercado I.C., Merritt C.E., Miner Z.L., Minja E., Mitchell T., Mohabbat F., Mohabbat K., Montgomery B., Moore N., Morris S., Munidasa M., Ngo R.N., Nguyen N.B., Nickerson E., Nwaokelemeh O.O., Nwokenkwo S., Obregon M., Oguh M., Oragunye N., Oviedo R.J., Parish B.J., Parker D.N., Parrish J., Parks K.L., Paul H.A., Payton B.A., Perez A., Perrin W., Pickens A., Primus E.L., Pu L.-L., Puazo M., Quiles M.M., Quiroz J.B., Rabata D., Reeves K., Ruiz S.J., Shao H., Sisson I., Sonaike T., Sorelle R.P., Sutton A.E., Svatek A.F., Svetz L.A., Tamerisa K.S., Taylor T.R., Teague B., Thomas N., Thorn R.D., Trejos Z.Y., Trevino B.K., Ukegbu O.N., Urban J.B., Vasquez L.I., Vera V.A., Villasana D.M., Wang L., Ward-Moore S., Warren J.T., Wei X., White F., Williamson A.L., Wleczyk R., Wooden H.S., Wooden S.H., Yen J., Yoon L., Yoon V., Zorrilla S.E., Nelson D., Kucherlapati R., Weinstock G., Gibbs R.A.
    Nature 440:346-351(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  9. "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] (ISOFORM 1).
  10. "Biochemical characterization of the catalytic domain of human matrix metalloproteinase 19. Evidence for a role as a potent basement membrane degrading enzyme."
    Stracke J.O., Hutton M., Stewart M., Pendas A.M., Smith B., Lopez-Otin C., Murphy G., Knaeuper V.
    J. Biol. Chem. 275:14809-14816(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF N-TERMINUS, FUNCTION, MUTAGENESIS.
  11. "Matrix metalloproteinases 19 and 20 cleave aggrecan and cartilage oligomeric matrix protein (COMP)."
    Stracke J.O., Fosang A.J., Last K., Mercuri F.A., Pendas A.M., Llano E., Perris R., Di Cesare P.E., Murphy G., Knaeuper V.
    FEBS Lett. 478:52-56(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  12. Cited for: PHOSPHORYLATION.

Entry informationi

Entry nameiMMP19_HUMAN
AccessioniPrimary (citable) accession number: Q99542
Secondary accession number(s): B4E030
, O15278, O95606, Q99580
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 24, 2001
Last sequence update: May 1, 1997
Last modified: October 29, 2014
This is version 155 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

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 12
    Human chromosome 12: 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. Peptidase families
    Classification of peptidase families and list of entries
  6. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3