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Protein

72 kDa type IV collagenase

Gene

MMP2

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

Functioni

Ubiquitinous metalloproteinase that is involved in diverse functions such as remodeling of the vasculature, angiogenesis, tissue repair, tumor invasion, inflammation, and atherosclerotic plaque rupture. As well as degrading extracellular matrix proteins, can also act on several nonmatrix proteins such as big endothelial 1 and beta-type CGRP promoting vasoconstriction. Also cleaves KISS at a Gly-|-Leu bond. Appears to have a role in myocardial cell death pathways. Contributes to myocardial oxidative stress by regulating the activity of GSK3beta. Cleaves GSK3beta in vitro. Involved in the formation of the fibrovascular tissues in association with MMP14.
PEX, the C-terminal non-catalytic fragment of MMP2, posseses anti-angiogenic and anti-tumor properties and inhibits cell migration and cell adhesion to FGF2 and vitronectin. Ligand for integrinv/beta3 on the surface of blood vessels.
Isoform 2: Mediates the proteolysis of CHUK/IKKA and initiates a primary innate immune response by inducing mitochondrial-nuclear stress signaling with activation of the pro-inflammatory NF-kappaB, NFAT and IRF transcriptional pathways.

Catalytic activityi

Cleavage of gelatin type I and collagen types IV, V, VII, X. Cleaves the collagen-like sequence Pro-Gln-Gly-|-Ile-Ala-Gly-Gln.

Cofactori

Protein has several cofactor binding sites:
  • Ca2+Note: Binds 4 Ca2+ ions per subunit.
  • Zn2+Note: Binds 2 Zn2+ ions per subunit.

Enzyme regulationi

Inhibited by histatin-3 1/24 (histatin-5).1 Publication

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Metal bindingi102Zinc 2; in inhibited formBy similarity1
Metal bindingi134Calcium 1By similarity1
Metal bindingi168Calcium 2By similarity1
Metal bindingi178Zinc 1By similarity1
Metal bindingi180Zinc 1By similarity1
Metal bindingi185Calcium 3By similarity1
Metal bindingi186Calcium 3; via carbonyl oxygenBy similarity1
Metal bindingi193Zinc 1By similarity1
Metal bindingi200Calcium 2; via carbonyl oxygenBy similarity1
Metal bindingi202Calcium 2; via carbonyl oxygenBy similarity1
Metal bindingi204Calcium 2By similarity1
Metal bindingi206Zinc 1By similarity1
Metal bindingi208Calcium 3By similarity1
Metal bindingi209Calcium 1By similarity1
Metal bindingi211Calcium 3By similarity1
Metal bindingi403Zinc 2; catalyticBy similarity1
Active sitei404PROSITE-ProRule annotation1
Metal bindingi407Zinc 2; catalyticBy similarity1
Metal bindingi413Zinc 2; catalyticBy similarity1
Metal bindingi476Calcium 4; via carbonyl oxygen1
Metal bindingi521Calcium 4; via carbonyl oxygen1
Metal bindingi569Calcium 4; via carbonyl oxygen1
Metal bindingi618Calcium 4; via carbonyl oxygen1

GO - Molecular functioni

  • metalloendopeptidase activity Source: Reactome
  • metallopeptidase activity Source: UniProtKB
  • serine-type endopeptidase activity Source: Reactome
  • zinc ion binding Source: ProtInc

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Metalloprotease, Protease

Keywords - Biological processi

Angiogenesis, Collagen degradation

Keywords - Ligandi

Calcium, Metal-binding, Zinc

Enzyme and pathway databases

BioCyciMetaCyc:HS01565-MONOMER.
ZFISH:HS01565-MONOMER.
BRENDAi3.4.24.24. 2681.
ReactomeiR-HSA-1442490. Collagen degradation.
R-HSA-1474228. Degradation of the extracellular matrix.
R-HSA-1592389. Activation of Matrix Metalloproteinases.
R-HSA-381426. Regulation of Insulin-like Growth Factor (IGF) transport and uptake by Insulin-like Growth Factor Binding Proteins (IGFBPs).
R-HSA-3928665. EPH-ephrin mediated repulsion of cells.
SIGNORiP08253.

Protein family/group databases

MEROPSiM10.003.

Names & Taxonomyi

Protein namesi
Recommended name:
72 kDa type IV collagenase (EC:3.4.24.24)
Alternative name(s):
72 kDa gelatinase
Gelatinase A
Matrix metalloproteinase-2
Short name:
MMP-2
TBE-1
Cleaved into the following chain:
Gene namesi
Name:MMP2
Synonyms:CLG4A
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 16

Organism-specific databases

HGNCiHGNC:7166. MMP2.

Subcellular locationi

Isoform 1 :

GO - Cellular componenti

  • extracellular matrix Source: BHF-UCL
  • extracellular region Source: Reactome
  • extracellular space Source: UniProtKB
  • mitochondrion Source: UniProtKB-SubCell
  • nucleus Source: UniProtKB-SubCell
  • plasma membrane Source: Ensembl
  • proteinaceous extracellular matrix Source: UniProtKB-SubCell
  • sarcomere Source: Ensembl
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Extracellular matrix, Membrane, Mitochondrion, Nucleus, Secreted

Pathology & Biotechi

Involvement in diseasei

Multicentric osteolysis, nodulosis, and arthropathy (MONA)3 Publications
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionAn autosomal recessive syndrome characterized by severe multicentric osteolysis with predominant involvement of the hands and feet. Additional features include coarse face, corneal opacities, patches of thickened, hyperpigmented skin, hypertrichosis and gum hypertrophy.
See also OMIM:259600
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_032423101R → H in MONA. 1 PublicationCorresponds to variant rs121912953dbSNPEnsembl.1
Natural variantiVAR_054996400Missing in MONA. 1 Publication1
Natural variantiVAR_032425404E → K in MONA. 1 PublicationCorresponds to variant rs121912955dbSNPEnsembl.1

Keywords - Diseasei

Disease mutation

Organism-specific databases

DisGeNETi4313.
MalaCardsiMMP2.
MIMi259600. phenotype.
OpenTargetsiENSG00000087245.
Orphaneti85196. Nodulosis-arthropathy-osteolysis syndrome.
3460. Torg-Winchester syndrome.
PharmGKBiPA30877.

Chemistry databases

ChEMBLiCHEMBL333.
DrugBankiDB01197. Captopril.
DB00786. Marimastat.
GuidetoPHARMACOLOGYi1629.

Polymorphism and mutation databases

BioMutaiMMP2.
DMDMi116856.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 29By similarityAdd BLAST29
PropeptideiPRO_000002871430 – 109Activation peptideAdd BLAST80
ChainiPRO_0000028715110 – 66072 kDa type IV collagenaseAdd BLAST551
ChainiPRO_0000391626445 – 660PEXAdd BLAST216

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Disulfide bondi233 ↔ 259PROSITE-ProRule annotation
Disulfide bondi247 ↔ 274PROSITE-ProRule annotation
Disulfide bondi291 ↔ 317PROSITE-ProRule annotation
Disulfide bondi305 ↔ 332PROSITE-ProRule annotation
Disulfide bondi349 ↔ 375PROSITE-ProRule annotation
Disulfide bondi363 ↔ 390PROSITE-ProRule annotation
Disulfide bondi469 ↔ 660PROSITE-ProRule annotation1 Publication
Glycosylationi573N-linked (GlcNAc...)Sequence analysis1
Glycosylationi642N-linked (GlcNAc...)Sequence analysis1

Post-translational modificationi

Phosphorylation on multiple sites modulates enzymatic activity. Phosphorylated by PKC in vitro.1 Publication
The propeptide is processed by MMP14 (MT-MMP1) and MMP16 (MT-MMP3). Autocatalytic cleavage in the C-terminal produces the anti-angiogenic peptide, PEX. This processing appears to be facilitated by binding integrinv/beta3.2 Publications

Keywords - PTMi

Autocatalytic cleavage, Disulfide bond, Glycoprotein, Phosphoprotein, Zymogen

Proteomic databases

EPDiP08253.
MaxQBiP08253.
PaxDbiP08253.
PeptideAtlasiP08253.
PRIDEiP08253.

PTM databases

iPTMnetiP08253.
PhosphoSitePlusiP08253.

Miscellaneous databases

PMAP-CutDBP08253.

Expressioni

Tissue specificityi

Produced by normal skin fibroblasts. PEX is expressed in a number of tumors including gliomas, breast and prostate.1 Publication

Inductioni

Aspirin appears to inhibit expression.1 Publication

Gene expression databases

BgeeiENSG00000087245.
CleanExiHS_MMP2.
ExpressionAtlasiP08253. baseline and differential.
GenevisibleiP08253. HS.

Organism-specific databases

HPAiCAB002788.
HPA001939.

Interactioni

Subunit structurei

Interacts (via the C-terminal hemopexin-like domains-containing region) with the integrin alpha-V/beta-3; the interaction promotes vascular invasion in angiogenic vessels and melamoma cells. Interacts (via the C-terminal PEX domain) with TIMP2 (via the C-terminal); the interaction inhibits the degradation activity. Interacts with GSK3B.8 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
PCSK9Q8NBP74EBI-1033518,EBI-7539251
SCUBE3Q8IX302EBI-1033518,EBI-4479975

Protein-protein interaction databases

BioGridi110457. 34 interactors.
IntActiP08253. 17 interactors.
STRINGi9606.ENSP00000219070.

Chemistry databases

BindingDBiP08253.

Structurei

Secondary structure

1660
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi46 – 56Combined sources11
Turni62 – 64Combined sources3
Helixi67 – 80Combined sources14
Beta strandi86 – 88Combined sources3
Helixi91 – 97Combined sources7
Beta strandi111 – 113Combined sources3
Beta strandi120 – 128Combined sources9
Beta strandi133 – 135Combined sources3
Helixi137 – 152Combined sources16
Beta strandi154 – 156Combined sources3
Beta strandi158 – 161Combined sources4
Beta strandi163 – 165Combined sources3
Beta strandi168 – 174Combined sources7
Beta strandi179 – 181Combined sources3
Beta strandi186 – 189Combined sources4
Beta strandi192 – 195Combined sources4
Beta strandi197 – 199Combined sources3
Turni200 – 203Combined sources4
Beta strandi205 – 208Combined sources4
Beta strandi209 – 211Combined sources3
Beta strandi213 – 216Combined sources4
Helixi226 – 228Combined sources3
Beta strandi235 – 239Combined sources5
Beta strandi242 – 246Combined sources5
Beta strandi258 – 264Combined sources7
Turni265 – 267Combined sources3
Beta strandi271 – 273Combined sources3
Turni277 – 279Combined sources3
Turni284 – 288Combined sources5
Beta strandi293 – 297Combined sources5
Beta strandi300 – 304Combined sources5
Beta strandi316 – 321Combined sources6
Turni323 – 325Combined sources3
Beta strandi329 – 331Combined sources3
Beta strandi338 – 341Combined sources4
Turni342 – 346Combined sources5
Beta strandi351 – 355Combined sources5
Beta strandi358 – 362Combined sources5
Beta strandi369 – 371Combined sources3
Beta strandi374 – 379Combined sources6
Helixi381 – 384Combined sources4
Beta strandi387 – 389Combined sources3
Beta strandi394 – 396Combined sources3
Helixi397 – 408Combined sources12
Beta strandi422 – 424Combined sources3
Helixi435 – 445Combined sources11
Turni468 – 470Combined sources3
Beta strandi476 – 481Combined sources6
Beta strandi484 – 489Combined sources6
Beta strandi492 – 498Combined sources7
Beta strandi504 – 508Combined sources5
Helixi509 – 511Combined sources3
Beta strandi514 – 516Combined sources3
Beta strandi521 – 526Combined sources6
Turni527 – 530Combined sources4
Beta strandi531 – 536Combined sources6
Beta strandi539 – 544Combined sources6
Beta strandi553 – 555Combined sources3
Helixi556 – 559Combined sources4
Turni563 – 566Combined sources4
Beta strandi569 – 573Combined sources5
Turni575 – 577Combined sources3
Beta strandi580 – 584Combined sources5
Beta strandi587 – 592Combined sources6
Turni593 – 596Combined sources4
Helixi606 – 609Combined sources4
Beta strandi610 – 612Combined sources3
Beta strandi618 – 622Combined sources5
Turni624 – 626Combined sources3
Beta strandi628 – 633Combined sources6
Beta strandi636 – 641Combined sources6
Beta strandi644 – 652Combined sources9
Helixi653 – 656Combined sources4

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1CK7X-ray2.80A30-660[»]
1CXWNMR-A278-336[»]
1EAKX-ray2.66A/B/C/D32-452[»]
1GENX-ray2.15A443-660[»]
1GXDX-ray3.10A/B30-660[»]
1HOVNMR-A110-431[»]
1J7MNMR-A337-394[»]
1KS0NMR-A223-282[»]
1QIBX-ray2.80A115-217[»]
A394-449[»]
1RTGX-ray2.60A451-660[»]
3AYUX-ray2.00A110-450[»]
ProteinModelPortaliP08253.
SMRiP08253.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP08253.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini228 – 276Fibronectin type-II 1PROSITE-ProRule annotationAdd BLAST49
Domaini286 – 334Fibronectin type-II 2PROSITE-ProRule annotationAdd BLAST49
Domaini344 – 392Fibronectin type-II 3PROSITE-ProRule annotationAdd BLAST49
Repeati472 – 516Hemopexin 1Add BLAST45
Repeati517 – 563Hemopexin 2Add BLAST47
Repeati565 – 613Hemopexin 3Add BLAST49
Repeati614 – 660Hemopexin 4Add BLAST47

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni110 – 221Collagenase-like 1Add BLAST112
Regioni222 – 396Collagen-bindingAdd BLAST175
Regioni397 – 465Collagenase-like 2Add BLAST69
Regioni414 – 660Required for inhibitor TIMP2 bindingAdd BLAST247

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Motifi100 – 107Cysteine switchBy similarity8

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 3 fibronectin type-II domains.PROSITE-ProRule annotation
Contains 4 hemopexin repeats.Curated

Keywords - Domaini

Repeat, Signal

Phylogenomic databases

eggNOGiKOG1565. Eukaryota.
ENOG410XQ5D. LUCA.
GeneTreeiENSGT00760000118870.
HOGENOMiHOG000217926.
HOVERGENiHBG052484.
InParanoidiP08253.
KOiK01398.
OMAiKHESCTS.
OrthoDBiEOG091G03DP.
PhylomeDBiP08253.
TreeFamiTF315428.

Family and domain databases

CDDicd00062. FN2. 3 hits.
cd00094. HX. 1 hit.
cd04278. ZnMc_MMP. 1 hit.
Gene3Di1.10.101.10. 1 hit.
2.10.10.10. 3 hits.
2.110.10.10. 1 hit.
3.40.390.10. 2 hits.
InterProiIPR028708. 72kDa_collagenase.
IPR000562. FN_type2_col-bd.
IPR000585. Hemopexin-like_dom.
IPR018487. Hemopexin-like_repeat.
IPR018486. Hemopexin_CS.
IPR013806. Kringle-like.
IPR033739. M10A_MMP.
IPR024079. MetalloPept_cat_dom.
IPR001818. Pept_M10_metallopeptidase.
IPR021190. Pept_M10A.
IPR021158. Pept_M10A_Zn_BS.
IPR006026. Peptidase_Metallo.
IPR002477. Peptidoglycan-bd-like.
[Graphical view]
PANTHERiPTHR10201:SF29. PTHR10201:SF29. 2 hits.
PfamiPF00040. fn2. 3 hits.
PF00045. Hemopexin. 4 hits.
PF00413. Peptidase_M10. 1 hit.
PF01471. PG_binding_1. 1 hit.
[Graphical view]
PRINTSiPR00138. MATRIXIN.
SMARTiSM00059. FN2. 3 hits.
SM00120. HX. 4 hits.
SM00235. ZnMc. 1 hit.
[Graphical view]
SUPFAMiSSF47090. SSF47090. 1 hit.
SSF50923. SSF50923. 1 hit.
SSF57440. SSF57440. 3 hits.
PROSITEiPS00546. CYSTEINE_SWITCH. 1 hit.
PS00023. FN2_1. 3 hits.
PS51092. FN2_2. 3 hits.
PS00024. HEMOPEXIN. 1 hit.
PS51642. HEMOPEXIN_2. 4 hits.
PS00142. ZINC_PROTEASE. 1 hit.
[Graphical view]

Sequences (3)i

Sequence statusi: Complete.

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

This entry describes 3 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: P08253-1) [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
MEALMARGAL TGPLRALCLL GCLLSHAAAA PSPIIKFPGD VAPKTDKELA
60 70 80 90 100
VQYLNTFYGC PKESCNLFVL KDTLKKMQKF FGLPQTGDLD QNTIETMRKP
110 120 130 140 150
RCGNPDVANY NFFPRKPKWD KNQITYRIIG YTPDLDPETV DDAFARAFQV
160 170 180 190 200
WSDVTPLRFS RIHDGEADIM INFGRWEHGD GYPFDGKDGL LAHAFAPGTG
210 220 230 240 250
VGGDSHFDDD ELWTLGEGQV VRVKYGNADG EYCKFPFLFN GKEYNSCTDT
260 270 280 290 300
GRSDGFLWCS TTYNFEKDGK YGFCPHEALF TMGGNAEGQP CKFPFRFQGT
310 320 330 340 350
SYDSCTTEGR TDGYRWCGTT EDYDRDKKYG FCPETAMSTV GGNSEGAPCV
360 370 380 390 400
FPFTFLGNKY ESCTSAGRSD GKMWCATTAN YDDDRKWGFC PDQGYSLFLV
410 420 430 440 450
AAHEFGHAMG LEHSQDPGAL MAPIYTYTKN FRLSQDDIKG IQELYGASPD
460 470 480 490 500
IDLGTGPTPT LGPVTPEICK QDIVFDGIAQ IRGEIFFFKD RFIWRTVTPR
510 520 530 540 550
DKPMGPLLVA TFWPELPEKI DAVYEAPQEE KAVFFAGNEY WIYSASTLER
560 570 580 590 600
GYPKPLTSLG LPPDVQRVDA AFNWSKNKKT YIFAGDKFWR YNEVKKKMDP
610 620 630 640 650
GFPKLIADAW NAIPDNLDAV VDLQGGGHSY FFKGAYYLKL ENQSLKSVKF
660
GSIKSDWLGC
Length:660
Mass (Da):73,882
Last modified:February 1, 1991 - v2
Checksum:iBC7147DC8B49F289
GO
Isoform 2 (identifier: P08253-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-76: Missing.

Note: Induced by oxidative stress.
Show »
Length:584
Mass (Da):65,765
Checksum:iEC1C16C91ECBC26C
GO
Isoform 3 (identifier: P08253-3) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-51: MEALMARGALTGPLRALCLLGCLLSHAAAAPSPIIKFPGDVAPKTDKELAV → M

Note: No experimental confirmation available.
Show »
Length:610
Mass (Da):68,831
Checksum:iFB214CA4334DC5FC
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti235F → S in AK310314 (PubMed:14702039).Curated1
Sequence conflicti546S → G in BAG35588 (PubMed:14702039).Curated1
Sequence conflicti618D → G in BAG35588 (PubMed:14702039).Curated1

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_032423101R → H in MONA. 1 PublicationCorresponds to variant rs121912953dbSNPEnsembl.1
Natural variantiVAR_032424210D → Y.1 Publication1
Natural variantiVAR_036136228A → T in a colorectal cancer sample; somatic mutation. 1 PublicationCorresponds to variant rs759302357dbSNPEnsembl.1
Natural variantiVAR_054996400Missing in MONA. 1 Publication1
Natural variantiVAR_032425404E → K in MONA. 1 PublicationCorresponds to variant rs121912955dbSNPEnsembl.1
Natural variantiVAR_020616447A → V.1 PublicationCorresponds to variant rs17859943dbSNPEnsembl.1
Natural variantiVAR_036137498T → M in a colorectal cancer sample; somatic mutation. 1 PublicationCorresponds to variant rs764961297dbSNPEnsembl.1
Natural variantiVAR_020617621V → L.1 PublicationCorresponds to variant rs16955280dbSNPEnsembl.1
Natural variantiVAR_036138644S → I in a colorectal cancer sample; somatic mutation. 1 Publication1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_0446311 – 76Missing in isoform 2. 1 PublicationAdd BLAST76
Alternative sequenceiVSP_0457041 – 51MEALM…KELAV → M in isoform 3. 1 PublicationAdd BLAST51

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M55593
, M58552, M55582, M55583, M55584, M55585, M55586, M55587, M55588, M55589, M55590, M55591, M55592 Genomic DNA. Translation: AAA52028.1.
AK301536 mRNA. Translation: BAG63035.1.
AK310314 mRNA. No translation available.
AK312711 mRNA. Translation: BAG35588.1.
AY738117 Genomic DNA. Translation: AAU10089.1.
AC007336 Genomic DNA. No translation available.
AC092722 Genomic DNA. No translation available.
BC002576 mRNA. Translation: AAH02576.1.
M33789 Genomic DNA. Translation: AAA52027.1.
J03210 mRNA. Translation: AAA35701.1.
CCDSiCCDS10752.1. [P08253-1]
CCDS45487.1. [P08253-3]
CCDS76869.1. [P08253-2]
PIRiA28153.
RefSeqiNP_001121363.1. NM_001127891.2. [P08253-3]
NP_001289437.1. NM_001302508.1. [P08253-2]
NP_001289438.1. NM_001302509.1. [P08253-2]
NP_001289439.1. NM_001302510.1. [P08253-2]
NP_004521.1. NM_004530.5. [P08253-1]
UniGeneiHs.513617.

Genome annotation databases

EnsembliENST00000219070; ENSP00000219070; ENSG00000087245. [P08253-1]
ENST00000437642; ENSP00000394237; ENSG00000087245. [P08253-3]
ENST00000543485; ENSP00000444143; ENSG00000087245. [P08253-2]
ENST00000570308; ENSP00000461421; ENSG00000087245. [P08253-2]
GeneIDi4313.
KEGGihsa:4313.
UCSCiuc002ehz.5. human. [P08253-1]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Web resourcesi

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

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M55593
, M58552, M55582, M55583, M55584, M55585, M55586, M55587, M55588, M55589, M55590, M55591, M55592 Genomic DNA. Translation: AAA52028.1.
AK301536 mRNA. Translation: BAG63035.1.
AK310314 mRNA. No translation available.
AK312711 mRNA. Translation: BAG35588.1.
AY738117 Genomic DNA. Translation: AAU10089.1.
AC007336 Genomic DNA. No translation available.
AC092722 Genomic DNA. No translation available.
BC002576 mRNA. Translation: AAH02576.1.
M33789 Genomic DNA. Translation: AAA52027.1.
J03210 mRNA. Translation: AAA35701.1.
CCDSiCCDS10752.1. [P08253-1]
CCDS45487.1. [P08253-3]
CCDS76869.1. [P08253-2]
PIRiA28153.
RefSeqiNP_001121363.1. NM_001127891.2. [P08253-3]
NP_001289437.1. NM_001302508.1. [P08253-2]
NP_001289438.1. NM_001302509.1. [P08253-2]
NP_001289439.1. NM_001302510.1. [P08253-2]
NP_004521.1. NM_004530.5. [P08253-1]
UniGeneiHs.513617.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1CK7X-ray2.80A30-660[»]
1CXWNMR-A278-336[»]
1EAKX-ray2.66A/B/C/D32-452[»]
1GENX-ray2.15A443-660[»]
1GXDX-ray3.10A/B30-660[»]
1HOVNMR-A110-431[»]
1J7MNMR-A337-394[»]
1KS0NMR-A223-282[»]
1QIBX-ray2.80A115-217[»]
A394-449[»]
1RTGX-ray2.60A451-660[»]
3AYUX-ray2.00A110-450[»]
ProteinModelPortaliP08253.
SMRiP08253.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi110457. 34 interactors.
IntActiP08253. 17 interactors.
STRINGi9606.ENSP00000219070.

Chemistry databases

BindingDBiP08253.
ChEMBLiCHEMBL333.
DrugBankiDB01197. Captopril.
DB00786. Marimastat.
GuidetoPHARMACOLOGYi1629.

Protein family/group databases

MEROPSiM10.003.

PTM databases

iPTMnetiP08253.
PhosphoSitePlusiP08253.

Polymorphism and mutation databases

BioMutaiMMP2.
DMDMi116856.

Proteomic databases

EPDiP08253.
MaxQBiP08253.
PaxDbiP08253.
PeptideAtlasiP08253.
PRIDEiP08253.

Protocols and materials databases

DNASUi4313.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000219070; ENSP00000219070; ENSG00000087245. [P08253-1]
ENST00000437642; ENSP00000394237; ENSG00000087245. [P08253-3]
ENST00000543485; ENSP00000444143; ENSG00000087245. [P08253-2]
ENST00000570308; ENSP00000461421; ENSG00000087245. [P08253-2]
GeneIDi4313.
KEGGihsa:4313.
UCSCiuc002ehz.5. human. [P08253-1]

Organism-specific databases

CTDi4313.
DisGeNETi4313.
GeneCardsiMMP2.
HGNCiHGNC:7166. MMP2.
HPAiCAB002788.
HPA001939.
MalaCardsiMMP2.
MIMi120360. gene.
259600. phenotype.
neXtProtiNX_P08253.
OpenTargetsiENSG00000087245.
Orphaneti85196. Nodulosis-arthropathy-osteolysis syndrome.
3460. Torg-Winchester syndrome.
PharmGKBiPA30877.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG1565. Eukaryota.
ENOG410XQ5D. LUCA.
GeneTreeiENSGT00760000118870.
HOGENOMiHOG000217926.
HOVERGENiHBG052484.
InParanoidiP08253.
KOiK01398.
OMAiKHESCTS.
OrthoDBiEOG091G03DP.
PhylomeDBiP08253.
TreeFamiTF315428.

Enzyme and pathway databases

BioCyciMetaCyc:HS01565-MONOMER.
ZFISH:HS01565-MONOMER.
BRENDAi3.4.24.24. 2681.
ReactomeiR-HSA-1442490. Collagen degradation.
R-HSA-1474228. Degradation of the extracellular matrix.
R-HSA-1592389. Activation of Matrix Metalloproteinases.
R-HSA-381426. Regulation of Insulin-like Growth Factor (IGF) transport and uptake by Insulin-like Growth Factor Binding Proteins (IGFBPs).
R-HSA-3928665. EPH-ephrin mediated repulsion of cells.
SIGNORiP08253.

Miscellaneous databases

ChiTaRSiMMP2. human.
EvolutionaryTraceiP08253.
GeneWikiiMMP2.
GenomeRNAii4313.
PMAP-CutDBP08253.
PROiP08253.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000087245.
CleanExiHS_MMP2.
ExpressionAtlasiP08253. baseline and differential.
GenevisibleiP08253. HS.

Family and domain databases

CDDicd00062. FN2. 3 hits.
cd00094. HX. 1 hit.
cd04278. ZnMc_MMP. 1 hit.
Gene3Di1.10.101.10. 1 hit.
2.10.10.10. 3 hits.
2.110.10.10. 1 hit.
3.40.390.10. 2 hits.
InterProiIPR028708. 72kDa_collagenase.
IPR000562. FN_type2_col-bd.
IPR000585. Hemopexin-like_dom.
IPR018487. Hemopexin-like_repeat.
IPR018486. Hemopexin_CS.
IPR013806. Kringle-like.
IPR033739. M10A_MMP.
IPR024079. MetalloPept_cat_dom.
IPR001818. Pept_M10_metallopeptidase.
IPR021190. Pept_M10A.
IPR021158. Pept_M10A_Zn_BS.
IPR006026. Peptidase_Metallo.
IPR002477. Peptidoglycan-bd-like.
[Graphical view]
PANTHERiPTHR10201:SF29. PTHR10201:SF29. 2 hits.
PfamiPF00040. fn2. 3 hits.
PF00045. Hemopexin. 4 hits.
PF00413. Peptidase_M10. 1 hit.
PF01471. PG_binding_1. 1 hit.
[Graphical view]
PRINTSiPR00138. MATRIXIN.
SMARTiSM00059. FN2. 3 hits.
SM00120. HX. 4 hits.
SM00235. ZnMc. 1 hit.
[Graphical view]
SUPFAMiSSF47090. SSF47090. 1 hit.
SSF50923. SSF50923. 1 hit.
SSF57440. SSF57440. 3 hits.
PROSITEiPS00546. CYSTEINE_SWITCH. 1 hit.
PS00023. FN2_1. 3 hits.
PS51092. FN2_2. 3 hits.
PS00024. HEMOPEXIN. 1 hit.
PS51642. HEMOPEXIN_2. 4 hits.
PS00142. ZINC_PROTEASE. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiMMP2_HUMAN
AccessioniPrimary (citable) accession number: P08253
Secondary accession number(s): B2R6U1
, B4DWH3, E9PE45, Q9UCJ8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 1, 1988
Last sequence update: February 1, 1991
Last modified: November 30, 2016
This is version 210 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, Direct protein sequencing, 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. 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.