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P51512

- MMP16_HUMAN

UniProt

P51512 - MMP16_HUMAN

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Protein

Matrix metalloproteinase-16

Gene

MMP16

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 collagen type III and fibronectin. Activates progelatinase A. Involved in the matrix remodeling of blood vessels. Isoform short cleaves fibronectin and also collagen type III, but at lower rate. It has no effect on type I, II, IV and V collagen. However, upon interaction with CSPG4, it may be involved in degradation and invasion of type I collagen by melanoma cells.1 Publication

Cofactori

Protein has several cofactor binding sites:
  • Zn2+By similarityNote: Binds 1 zinc ion per subunit.By similarity
  • Ca2+By similarity

Enzyme regulationi

TIMP-2 shows little inhibitory activity compared to TIMP-1. TIMP-1 seems to have less binding affinity than TIMP-2 for the short isoform.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi101 – 1011Zinc 1; in inhibited formBy similarity
Metal bindingi183 – 1831Calcium 1; via carbonyl oxygen
Metal bindingi193 – 1931Zinc 1
Metal bindingi195 – 1951Zinc 1
Metal bindingi200 – 2001Calcium 2
Metal bindingi201 – 2011Calcium 2; via carbonyl oxygen
Metal bindingi203 – 2031Calcium 2; via carbonyl oxygen
Metal bindingi205 – 2051Calcium 2; via carbonyl oxygen
Metal bindingi215 – 2151Calcium 1; via carbonyl oxygen
Metal bindingi217 – 2171Calcium 1; via carbonyl oxygen
Metal bindingi219 – 2191Calcium 1
Metal bindingi223 – 2231Calcium 2
Metal bindingi226 – 2261Calcium 2
Metal bindingi246 – 2461Zinc 2; catalytic
Active sitei247 – 2471
Metal bindingi250 – 2501Zinc 2; catalytic
Metal bindingi256 – 2561Zinc 2; catalytic

GO - Molecular functioni

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

GO - Biological processi

  1. chondrocyte proliferation Source: Ensembl
  2. collagen catabolic process Source: UniProtKB-KW
  3. craniofacial suture morphogenesis Source: Ensembl
  4. embryonic cranial skeleton morphogenesis Source: Ensembl
  5. endochondral ossification Source: Ensembl
  6. extracellular matrix disassembly Source: Reactome
  7. extracellular matrix organization Source: Reactome
  8. positive regulation of catalytic activity Source: GOC
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Metalloprotease, Protease

Keywords - Biological processi

Collagen degradation

Keywords - Ligandi

Calcium, Metal-binding, Zinc

Enzyme and pathway databases

ReactomeiREACT_118682. Activation of Matrix Metalloproteinases.

Protein family/group databases

MEROPSiM10.016.

Names & Taxonomyi

Protein namesi
Recommended name:
Matrix metalloproteinase-16 (EC:3.4.24.-)
Short name:
MMP-16
Alternative name(s):
MMP-X2
Membrane-type matrix metalloproteinase 3
Short name:
MT-MMP 3
Short name:
MTMMP3
Membrane-type-3 matrix metalloproteinase
Short name:
MT3-MMP
Short name:
MT3MMP
Gene namesi
Name:MMP16
Synonyms:MMPX2
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 8

Organism-specific databases

HGNCiHGNC:7162. MMP16.

Subcellular locationi

Isoform Long : Cell membrane Curated; Single-pass type I membrane protein Curated; Extracellular side Curated
Note: Localized at the cell surface of melanoma cells.
Isoform Short : Secretedextracellular spaceextracellular matrix. Cell surface
Note: Localized at the cell surface of melanoma cells.

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini120 – 564445ExtracellularSequence AnalysisAdd
BLAST
Transmembranei565 – 58521HelicalSequence AnalysisAdd
BLAST
Topological domaini586 – 60722CytoplasmicSequence AnalysisAdd
BLAST

GO - Cellular componenti

  1. Golgi lumen Source: Reactome
  2. integral component of plasma membrane Source: ProtInc
  3. plasma membrane Source: Reactome
  4. proteinaceous extracellular matrix Source: UniProtKB-KW
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Extracellular matrix, Membrane, Secreted

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA30874.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 3131Sequence AnalysisAdd
BLAST
Propeptidei32 – 11988By similarityPRO_0000028812Add
BLAST
Chaini120 – 607488Matrix metalloproteinase-16PRO_0000028813Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi83 – 831N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi343 ↔ 532By similarity

Post-translational modificationi

The precursor is cleaved by a furin endopeptidase.By similarity

Keywords - PTMi

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

Proteomic databases

PaxDbiP51512.
PRIDEiP51512.

PTM databases

PhosphoSiteiP51512.

Miscellaneous databases

PMAP-CutDBP51512.

Expressioni

Tissue specificityi

Expressed in heart, brain, placenta, ovary and small intestine. Isoform Short is found in the ovary.

Developmental stagei

Expressed in tissues undergoing reconstruction. Present in fetal tissues, especially in brain. Expression seems to decline with advanced development.

Gene expression databases

BgeeiP51512.
CleanExiHS_MMP16.
ExpressionAtlasiP51512. baseline and differential.
GenevestigatoriP51512.

Organism-specific databases

HPAiHPA023693.

Interactioni

Subunit structurei

Interacts with CSPG4 through CSPG4 chondroitin sulfate glycosaminoglycan.2 Publications

Protein-protein interaction databases

IntActiP51512. 1 interaction.
MINTiMINT-4722491.
STRINGi9606.ENSP00000286614.

Structurei

Secondary structure

1
607
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi128 – 1369Combined sources
Turni141 – 1433Combined sources
Helixi145 – 16016Combined sources
Beta strandi166 – 1694Combined sources
Beta strandi177 – 1793Combined sources
Beta strandi183 – 1919Combined sources
Beta strandi194 – 1963Combined sources
Beta strandi201 – 2044Combined sources
Beta strandi207 – 2093Combined sources
Turni215 – 2184Combined sources
Beta strandi220 – 2234Combined sources
Beta strandi228 – 2314Combined sources
Beta strandi234 – 2396Combined sources
Helixi240 – 25112Combined sources
Beta strandi265 – 2673Combined sources
Helixi280 – 29011Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1RM8X-ray1.80A124-292[»]
ProteinModelPortaliP51512.
SMRiP51512. Positions 69-561.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP51512.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Repeati340 – 38849Hemopexin 1Add
BLAST
Repeati389 – 43446Hemopexin 2Add
BLAST
Repeati436 – 48449Hemopexin 3Add
BLAST
Repeati485 – 53248Hemopexin 4Add
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi99 – 1068Cysteine switchBy similarity

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, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiNOG295915.
GeneTreeiENSGT00760000118870.
HOGENOMiHOG000217928.
HOVERGENiHBG052484.
InParanoidiP51512.
KOiK07996.
OMAiVPPHRSV.
OrthoDBiEOG7XPZ57.
PhylomeDBiP51512.
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.
IPR028697. MMP16.
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:SF26. PTHR10201:SF26. 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]

Sequences (2)i

Sequence statusi: Complete.

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

This entry describes 2 isoformsi produced by alternative splicing. Align

Isoform Long (identifier: P51512-1) [UniParc]FASTAAdd to Basket

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
MILLTFSTGR RLDFVHHSGV FFLQTLLWIL CATVCGTEQY FNVEVWLQKY
60 70 80 90 100
GYLPPTDPRM SVLRSAETMQ SALAAMQQFY GINMTGKVDR NTIDWMKKPR
110 120 130 140 150
CGVPDQTRGS SKFHIRRKRY ALTGQKWQHK HITYSIKNVT PKVGDPETRK
160 170 180 190 200
AIRRAFDVWQ NVTPLTFEEV PYSELENGKR DVDITIIFAS GFHGDSSPFD
210 220 230 240 250
GEGGFLAHAY FPGPGIGGDT HFDSDEPWTL GNPNHDGNDL FLVAVHELGH
260 270 280 290 300
ALGLEHSNDP TAIMAPFYQY METDNFKLPN DDLQGIQKIY GPPDKIPPPT
310 320 330 340 350
RPLPTVPPHR SIPPADPRKN DRPKPPRPPT GRPSYPGAKP NICDGNFNTL
360 370 380 390 400
AILRREMFVF KDQWFWRVRN NRVMDGYPMQ ITYFWRGLPP SIDAVYENSD
410 420 430 440 450
GNFVFFKGNK YWVFKDTTLQ PGYPHDLITL GSGIPPHGID SAIWWEDVGK
460 470 480 490 500
TYFFKGDRYW RYSEEMKTMD PGYPKPITVW KGIPESPQGA FVHKENGFTY
510 520 530 540 550
FYKGKEYWKF NNQILKVEPG YPRSILKDFM GCDGPTDRVK EGHSPPDDVD
560 570 580 590 600
IVIKLDNTAS TVKAIAIVIP CILALCLLVL VYTVFQFKRK GTPRHILYCK

RSMQEWV
Length:607
Mass (Da):69,521
Last modified:July 15, 1998 - v2
Checksum:i30D6247D9CB21663
GO
Isoform Short (identifier: P51512-2) [UniParc]FASTAAdd to Basket

Also known as: SM3

The sequence of this isoform differs from the canonical sequence as follows:
     408-457: GNKYWVFKDT...VGKTYFFKGD → VKGDTLSVIQ...TYEELSSITY
     458-607: Missing.

Show »
Length:457
Mass (Da):52,515
Checksum:i94184CDA9F76C5EB
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti521 – 5211Y → H in BAA23742. (PubMed:7559440)Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei408 – 45750GNKYW…FFKGD → VKGDTLSVIQDGWLYKYHWK WILEQRQSVPVLSRQTEKHK TYEELSSITY in isoform Short. 1 PublicationVSP_005453Add
BLAST
Alternative sequencei458 – 607150Missing in isoform Short. 1 PublicationVSP_005454Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB009303 mRNA. Translation: BAA23742.1.
D83646 mRNA. Translation: BAA12022.1.
D83647 mRNA. Translation: BAA12023.1.
D85511 mRNA. Translation: BAA22226.1.
DQ003082 Genomic DNA. Translation: AAX84515.1.
AK314274 mRNA. Translation: BAG36934.1.
CH471060 Genomic DNA. Translation: EAW91651.1.
BC069500 mRNA. Translation: AAH69500.1.
BC075004 mRNA. Translation: AAH75004.1.
BC075005 mRNA. Translation: AAH75005.1.
CCDSiCCDS6246.1. [P51512-1]
RefSeqiNP_005932.2. NM_005941.4. [P51512-1]
UniGeneiHs.492187.
Hs.546267.

Genome annotation databases

EnsembliENST00000286614; ENSP00000286614; ENSG00000156103. [P51512-1]
GeneIDi4325.
KEGGihsa:4325.
UCSCiuc003yeb.4. human. [P51512-1]

Polymorphism databases

DMDMi3041669.

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Web resourcesi

NIEHS-SNPs

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB009303 mRNA. Translation: BAA23742.1 .
D83646 mRNA. Translation: BAA12022.1 .
D83647 mRNA. Translation: BAA12023.1 .
D85511 mRNA. Translation: BAA22226.1 .
DQ003082 Genomic DNA. Translation: AAX84515.1 .
AK314274 mRNA. Translation: BAG36934.1 .
CH471060 Genomic DNA. Translation: EAW91651.1 .
BC069500 mRNA. Translation: AAH69500.1 .
BC075004 mRNA. Translation: AAH75004.1 .
BC075005 mRNA. Translation: AAH75005.1 .
CCDSi CCDS6246.1. [P51512-1 ]
RefSeqi NP_005932.2. NM_005941.4. [P51512-1 ]
UniGenei Hs.492187.
Hs.546267.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1RM8 X-ray 1.80 A 124-292 [» ]
ProteinModelPortali P51512.
SMRi P51512. Positions 69-561.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

IntActi P51512. 1 interaction.
MINTi MINT-4722491.
STRINGi 9606.ENSP00000286614.

Chemistry

BindingDBi P51512.
ChEMBLi CHEMBL2200.
DrugBanki DB00786. Marimastat.

Protein family/group databases

MEROPSi M10.016.

PTM databases

PhosphoSitei P51512.

Polymorphism databases

DMDMi 3041669.

Proteomic databases

PaxDbi P51512.
PRIDEi P51512.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000286614 ; ENSP00000286614 ; ENSG00000156103 . [P51512-1 ]
GeneIDi 4325.
KEGGi hsa:4325.
UCSCi uc003yeb.4. human. [P51512-1 ]

Organism-specific databases

CTDi 4325.
GeneCardsi GC08M089044.
HGNCi HGNC:7162. MMP16.
HPAi HPA023693.
MIMi 602262. gene.
neXtProti NX_P51512.
PharmGKBi PA30874.
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG295915.
GeneTreei ENSGT00760000118870.
HOGENOMi HOG000217928.
HOVERGENi HBG052484.
InParanoidi P51512.
KOi K07996.
OMAi VPPHRSV.
OrthoDBi EOG7XPZ57.
PhylomeDBi P51512.
TreeFami TF352396.

Enzyme and pathway databases

Reactomei REACT_118682. Activation of Matrix Metalloproteinases.

Miscellaneous databases

EvolutionaryTracei P51512.
GeneWikii MMP16.
GenomeRNAii 4325.
NextBioi 17017.
PMAP-CutDB P51512.
PROi P51512.
SOURCEi Search...

Gene expression databases

Bgeei P51512.
CleanExi HS_MMP16.
ExpressionAtlasi P51512. baseline and differential.
Genevestigatori P51512.

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.
IPR028697. MMP16.
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:SF26. PTHR10201:SF26. 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. "Identification of the second membrane-type matrix metalloproteinase (MT-MMP-2) gene from a human placenta cDNA library. MT-MMPs form a unique membrane-type subclass in the MMP family."
    Takino T., Sato H., Shinagawa A., Seiki M.
    J. Biol. Chem. 270:23013-23020(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM LONG).
    Tissue: Placenta.
  2. Seiki M.
    Submitted (DEC-1997) to the EMBL/GenBank/DDBJ databases
    Cited for: SEQUENCE REVISION.
  3. "Identification of soluble type of membrane-type matrix metalloproteinase-3 formed by alternatively spliced mRNA."
    Matsumoto S., Katoh M., Saito S., Watanabe T., Masuho Y.
    Biochim. Biophys. Acta 1354:159-170(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS LONG AND SHORT).
    Tissue: Ovary.
  4. "Expression of three membrane-type matrix metalloproteinases (MT-MMPs) in rat vascular smooth muscle cells and characterization of MT3-MMPs with and without transmembrane domain."
    Shofuda K., Yasumitsu H., Nishihashi A., Miki K., Miyazaki K.
    J. Biol. Chem. 272:9749-9754(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM LONG).
    Tissue: Fetal brain.
  5. NIEHS SNPs program
    Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  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 LONG).
  7. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  8. "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 LONG).
    Tissue: Brain.
  9. "Melanoma chondroitin sulfate proteoglycan regulates matrix metalloproteinase-dependent human melanoma invasion into type I collagen."
    Iida J., Pei D., Kang T., Simpson M.A., Herlyn M., Furcht L.T., McCarthy J.B.
    J. Biol. Chem. 276:18786-18794(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH CSPG4, SUBCELLULAR LOCATION, FUNCTION.
  10. "Crystal structure of the catalytic domain of MMP-16/MT3-MMP: characterization of MT-MMP specific features."
    Lang R., Braun M., Sounni N.E., Noel A., Frankenne F., Foidart J.M., Bode W., Maskos K.
    J. Mol. Biol. 336:213-225(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 124-292 IN COMPLEX WITH INHIBITOR, ZINC-BINDING SITES, CALCIUM-BINDING SITES.

Entry informationi

Entry nameiMMP16_HUMAN
AccessioniPrimary (citable) accession number: P51512
Secondary accession number(s): B2RAN7, Q14824, Q52H48
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: July 15, 1998
Last modified: November 26, 2014
This is version 155 of the entry and version 2 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, Reference proteome

Documents

  1. Human chromosome 8
    Human chromosome 8: entries, gene names and cross-references to MIM
  2. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. Peptidase families
    Classification of peptidase families and list of entries
  5. SIMILARITY comments
    Index of protein domains and families

External Data

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