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P51511

- MMP15_HUMAN

UniProt

P51511 - MMP15_HUMAN

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Protein

Matrix metalloproteinase-15

Gene
MMP15
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. May activate progelatinase A.1 Publication

Cofactori

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

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi111 – 1111Zinc; in inhibited form By similarity
Metal bindingi259 – 2591Zinc; catalytic By similarity
Active sitei260 – 2601 By similarity
Metal bindingi263 – 2631Zinc; catalytic By similarity
Metal bindingi269 – 2691Zinc; catalytic By similarity

GO - Molecular functioni

  1. calcium ion binding Source: InterPro
  2. enzyme activator activity Source: ProtInc
  3. metalloendopeptidase activity Source: ProtInc
  4. protein binding Source: IntAct
  5. zinc ion binding Source: ProtInc

GO - Biological processi

  1. cellular protein modification process Source: ProtInc
  2. collagen catabolic process Source: Reactome
  3. extracellular matrix disassembly Source: Reactome
  4. extracellular matrix organization Source: Reactome
  5. positive regulation of catalytic activity Source: GOC
  6. response to estradiol Source: Ensembl
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Metalloprotease, Protease

Keywords - Ligandi

Calcium, Metal-binding, Zinc

Enzyme and pathway databases

ReactomeiREACT_118572. Degradation of the extracellular matrix.
REACT_118682. Activation of Matrix Metalloproteinases.
REACT_150401. Collagen degradation.

Protein family/group databases

MEROPSiM10.015.

Names & Taxonomyi

Protein namesi
Recommended name:
Matrix metalloproteinase-15 (EC:3.4.24.-)
Short name:
MMP-15
Alternative name(s):
Membrane-type matrix metalloproteinase 2
Short name:
MT-MMP 2
Short name:
MTMMP2
Membrane-type-2 matrix metalloproteinase
Short name:
MT2-MMP
Short name:
MT2MMP
SMCP-2
Gene namesi
Name:MMP15
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 16

Organism-specific databases

HGNCiHGNC:7161. MMP15.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini132 – 625494Extracellular Reviewed predictionAdd
BLAST
Transmembranei626 – 64621Helical; Reviewed predictionAdd
BLAST
Topological domaini647 – 66923Cytoplasmic Reviewed predictionAdd
BLAST

GO - Cellular componenti

  1. extracellular matrix Source: InterPro
  2. integral component of plasma membrane Source: ProtInc
  3. plasma membrane Source: Reactome
Complete GO annotation...

Keywords - Cellular componenti

Membrane

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA30873.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 4141Or 45 Reviewed predictionAdd
BLAST
Propeptidei42 – 13190 By similarityPRO_0000028808Add
BLAST
Chaini132 – 669538Matrix metalloproteinase-15PRO_0000028809Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi150 – 1501N-linked (GlcNAc...) Reviewed prediction
Disulfide bondi370 ↔ 559 By similarity
Modified residuei589 – 5891Phosphoserine1 Publication

Post-translational modificationi

The precursor is cleaved by a furin endopeptidase By similarity.

Keywords - PTMi

Cleavage on pair of basic residues, Disulfide bond, Glycoprotein, Phosphoprotein, Zymogen

Proteomic databases

MaxQBiP51511.
PaxDbiP51511.
PRIDEiP51511.

PTM databases

PhosphoSiteiP51511.

Expressioni

Tissue specificityi

Appeared to be synthesized preferentially in liver, placenta, testis, colon and intestine. Substantial amounts are also detected in pancreas, kidney, lung, heart and skeletal muscle.

Gene expression databases

BgeeiP51511.
CleanExiHS_MMP15.
GenevestigatoriP51511.

Organism-specific databases

HPAiCAB002611.
HPA040390.

Interactioni

Binary interactionsi

WithEntry#Exp.IntActNotes
PROCP040702EBI-1383043,EBI-1383018

Protein-protein interaction databases

BioGridi110467. 1 interaction.
IntActiP51511. 2 interactions.
MINTiMINT-7897770.
STRINGi9606.ENSP00000219271.

Structurei

3D structure databases

ProteinModelPortaliP51511.
SMRiP51511. Positions 83-559.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Repeati367 – 41549Hemopexin 1Add
BLAST
Repeati416 – 46146Hemopexin 2Add
BLAST
Repeati463 – 51149Hemopexin 3Add
BLAST
Repeati512 – 55948Hemopexin 4Add
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi109 – 1168Cysteine switch By similarity

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi331 – 34010Poly-Pro

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.
Contains 4 hemopexin repeats.

Keywords - Domaini

Repeat, Signal, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiNOG295915.
HOGENOMiHOG000217928.
HOVERGENiHBG052484.
InParanoidiP51511.
KOiK07995.
OMAiVQMQRKG.
OrthoDBiEOG7XPZ57.
PhylomeDBiP51511.
TreeFamiTF352396.

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.
IPR028729. MMP15.
IPR001818. Pept_M10_metallopeptidase.
IPR021190. Pept_M10A.
IPR021805. Pept_M10A_metallopeptidase_C.
IPR016293. Pept_M10A_stromelysin-type.
IPR021158. Pept_M10A_Zn_BS.
IPR006026. Peptidase_Metallo.
IPR002477. Peptidoglycan-bd-like.
[Graphical view]
PANTHERiPTHR10201:SF25. PTHR10201:SF25. 1 hit.
PfamiPF11857. DUF3377. 1 hit.
PF00045. 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.

P51511-1 [UniParc]FASTAAdd to Basket

« Hide

MGSDPSAPGR PGWTGSLLGD REEAARPRLL PLLLVLLGCL GLGVAAEDAE    50
VHAENWLRLY GYLPQPSRHM STMRSAQILA SALAEMQRFY GIPVTGVLDE 100
ETKEWMKRPR CGVPDQFGVR VKANLRRRRK RYALTGRKWN NHHLTFSIQN 150
YTEKLGWYHS MEAVRRAFRV WEQATPLVFQ EVPYEDIRLR RQKEADIMVL 200
FASGFHGDSS PFDGTGGFLA HAYFPGPGLG GDTHFDADEP WTFSSTDLHG 250
NNLFLVAVHE LGHALGLEHS SNPNAIMAPF YQWKDVDNFK LPEDDLRGIQ 300
QLYGTPDGQP QPTQPLPTVT PRRPGRPDHR PPRPPQPPPP GGKPERPPKP 350
GPPVQPRATE RPDQYGPNIC DGDFDTVAML RGEMFVFKGR WFWRVRHNRV 400
LDNYPMPIGH FWRGLPGDIS AAYERQDGRF VFFKGDRYWL FREANLEPGY 450
PQPLTSYGLG IPYDRIDTAI WWEPTGHTFF FQEDRYWRFN EETQRGDPGY 500
PKPISVWQGI PASPKGAFLS NDAAYTYFYK GTKYWKFDNE RLRMEPGYPK 550
SILRDFMGCQ EHVEPGPRWP DVARPPFNPH GGAEPGADSA EGDVGDGDGD 600
FGAGVNKDGG SRVVVQMEEV ARTVNVVMVL VPLLLLLCVL GLTYALVQMQ 650
RKGAPRVLLY CKRSLQEWV 669
Length:669
Mass (Da):75,807
Last modified:October 1, 1996 - v1
Checksum:iFE875EC0674B297F
GO

Sequence cautioni

The sequence BAA13071.1 differs from that shown. Reason: Erroneous initiation.

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti200 – 2001L → P.1 Publication
Corresponds to variant rs41340745 [ dbSNP | Ensembl ].
VAR_030523
Natural varianti350 – 3501P → L.1 Publication
Corresponds to variant rs41335851 [ dbSNP | Ensembl ].
VAR_030524
Natural varianti596 – 5961D → G.2 Publications
Corresponds to variant rs41504346 [ dbSNP | Ensembl ].
VAR_030525
Natural varianti609 – 6091G → R.2 Publications
Corresponds to variant rs3743563 [ dbSNP | Ensembl ].
VAR_020055
Natural varianti622 – 6221R → W.1 Publication
Corresponds to variant rs41434246 [ dbSNP | Ensembl ].
VAR_030526

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
Z48482 mRNA. Translation: CAA88373.1.
EF032329 Genomic DNA. Translation: ABJ53423.1.
BC036495 mRNA. Translation: AAH36495.1.
BC055428 mRNA. Translation: AAH55428.1.
D86331 mRNA. Translation: BAA13071.1. Different initiation.
D85510 mRNA. Translation: BAA22225.1.
CCDSiCCDS10792.1.
PIRiI38029.
RefSeqiNP_002419.1. NM_002428.2.
UniGeneiHs.80343.

Genome annotation databases

EnsembliENST00000219271; ENSP00000219271; ENSG00000102996.
GeneIDi4324.
KEGGihsa:4324.
UCSCiuc002ena.3. human.

Polymorphism databases

DMDMi1705988.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Web resourcesi

NIEHS-SNPs
Atlas of Genetics and Cytogenetics in Oncology and Haematology

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
Z48482 mRNA. Translation: CAA88373.1 .
EF032329 Genomic DNA. Translation: ABJ53423.1 .
BC036495 mRNA. Translation: AAH36495.1 .
BC055428 mRNA. Translation: AAH55428.1 .
D86331 mRNA. Translation: BAA13071.1 . Different initiation.
D85510 mRNA. Translation: BAA22225.1 .
CCDSi CCDS10792.1.
PIRi I38029.
RefSeqi NP_002419.1. NM_002428.2.
UniGenei Hs.80343.

3D structure databases

ProteinModelPortali P51511.
SMRi P51511. Positions 83-559.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 110467. 1 interaction.
IntActi P51511. 2 interactions.
MINTi MINT-7897770.
STRINGi 9606.ENSP00000219271.

Chemistry

BindingDBi P51511.
ChEMBLi CHEMBL2963.

Protein family/group databases

MEROPSi M10.015.

PTM databases

PhosphoSitei P51511.

Polymorphism databases

DMDMi 1705988.

Proteomic databases

MaxQBi P51511.
PaxDbi P51511.
PRIDEi P51511.

Protocols and materials databases

DNASUi 4324.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000219271 ; ENSP00000219271 ; ENSG00000102996 .
GeneIDi 4324.
KEGGi hsa:4324.
UCSCi uc002ena.3. human.

Organism-specific databases

CTDi 4324.
GeneCardsi GC16P058060.
HGNCi HGNC:7161. MMP15.
HPAi CAB002611.
HPA040390.
MIMi 602261. gene.
neXtProti NX_P51511.
PharmGKBi PA30873.
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG295915.
HOGENOMi HOG000217928.
HOVERGENi HBG052484.
InParanoidi P51511.
KOi K07995.
OMAi VQMQRKG.
OrthoDBi EOG7XPZ57.
PhylomeDBi P51511.
TreeFami TF352396.

Enzyme and pathway databases

Reactomei REACT_118572. Degradation of the extracellular matrix.
REACT_118682. Activation of Matrix Metalloproteinases.
REACT_150401. Collagen degradation.

Miscellaneous databases

GeneWikii MMP15.
GenomeRNAii 4324.
NextBioi 17013.
PROi P51511.
SOURCEi Search...

Gene expression databases

Bgeei P51511.
CleanExi HS_MMP15.
Genevestigatori P51511.

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.
IPR028729. MMP15.
IPR001818. Pept_M10_metallopeptidase.
IPR021190. Pept_M10A.
IPR021805. Pept_M10A_metallopeptidase_C.
IPR016293. Pept_M10A_stromelysin-type.
IPR021158. Pept_M10A_Zn_BS.
IPR006026. Peptidase_Metallo.
IPR002477. Peptidoglycan-bd-like.
[Graphical view ]
PANTHERi PTHR10201:SF25. PTHR10201:SF25. 1 hit.
Pfami PF11857. DUF3377. 1 hit.
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. "cDNA sequence and mRNA tissue distribution of a novel human matrix metalloproteinase with a potential transmembrane segment."
    Will H., Hinzmann B.
    Eur. J. Biochem. 231:602-608(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Tissue: Lung.
  2. NIEHS SNPs program
    Submitted (SEP-2006) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANTS PRO-200; LEU-350; GLY-596; ARG-609 AND TRP-622.
  3. "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: Brain.
  4. "Assignment of the human genes for membrane-type-1, -2, and -3 matrix metalloproteinases (MMP14, MMP15, and MMP16) to 14q12.2, 16q12.2-q21, and 8q21, respectively, by in situ hybridization."
    Sato H., Tanaka M., Takino T., Inoue M., Seiki M.
    Genomics 39:412-413(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 94-669, VARIANT ARG-609.
  5. Shofuda K., Yasumitsu H., Nishihashi A., Miki K., Miyazaki K.
    Submitted (MAY-1996) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 163-669.
    Tissue: Placenta.
  6. "Membrane-type matrix metalloproteinases 1 and 2 exhibit broad-spectrum proteolytic capacities comparable to many matrix metalloproteinases."
    d'Ortho M.P., Will H., Atkinson S., Butler G., Messent A., Gavrilovic J., Smith B., Timpl R., Zardi L., Murphy G.
    Eur. J. Biochem. 250:751-757(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  7. "Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle."
    Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., Greff Z., Keri G., Stemmann O., Mann M.
    Mol. Cell 31:438-448(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-589, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  8. Cited for: VARIANT [LARGE SCALE ANALYSIS] GLY-596.

Entry informationi

Entry nameiMMP15_HUMAN
AccessioniPrimary (citable) accession number: P51511
Secondary accession number(s): A0A2U6, Q14111
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: October 1, 1996
Last modified: September 3, 2014
This is version 149 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, Reference proteome

Documents

  1. Human chromosome 16
    Human chromosome 16: 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

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