P08253 · MMP2_HUMAN
- Protein72 kDa type IV collagenase
- GeneMMP2
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids660 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Isoform 2
Catalytic activity
Cofactor
Activity regulation
Features
Showing features for binding site, active site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Binding site | 102 | Zn2+ 1 (UniProtKB | ChEBI); catalytic; in inhibited form | ||||
Sequence: C | ||||||
Binding site | 134 | Ca2+ 1 (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 168 | Ca2+ 2 (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 178 | Zn2+ 2 (UniProtKB | ChEBI) | ||||
Sequence: H | ||||||
Binding site | 180 | Zn2+ 2 (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 185 | Ca2+ 3 (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 186 | Ca2+ 3 (UniProtKB | ChEBI) | ||||
Sequence: G | ||||||
Binding site | 193 | Zn2+ 2 (UniProtKB | ChEBI) | ||||
Sequence: H | ||||||
Binding site | 200 | Ca2+ 2 (UniProtKB | ChEBI) | ||||
Sequence: G | ||||||
Binding site | 202 | Ca2+ 2 (UniProtKB | ChEBI) | ||||
Sequence: G | ||||||
Binding site | 204 | Ca2+ 2 (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 206 | Zn2+ 2 (UniProtKB | ChEBI) | ||||
Sequence: H | ||||||
Binding site | 208 | Ca2+ 3 (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 209 | Ca2+ 1 (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 211 | Ca2+ 1 (UniProtKB | ChEBI) | ||||
Sequence: E | ||||||
Binding site | 211 | Ca2+ 3 (UniProtKB | ChEBI) | ||||
Sequence: E | ||||||
Binding site | 403 | Zn2+ 1 (UniProtKB | ChEBI); catalytic | ||||
Sequence: H | ||||||
Active site | 404 | |||||
Sequence: E | ||||||
Binding site | 407 | Zn2+ 1 (UniProtKB | ChEBI); catalytic | ||||
Sequence: H | ||||||
Binding site | 413 | Zn2+ 1 (UniProtKB | ChEBI); catalytic | ||||
Sequence: H | ||||||
Binding site | 476 | Ca2+ 4 (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 521 | Ca2+ 4 (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 569 | Ca2+ 4 (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 618 | Ca2+ 4 (UniProtKB | ChEBI) | ||||
Sequence: D |
GO annotations
Keywords
- Molecular function
- Biological process
- Ligand
Enzyme and pathway databases
Protein family/group databases
Names & Taxonomy
Protein names
- Recommended name72 kDa type IV collagenase
- EC number
- Alternative names
- Cleaved into 1 chains
Gene names
Organism names
- Organism
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Primates > Haplorrhini > Catarrhini > Hominidae > Homo
Accessions
- Primary accessionP08253
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
Isoform 1
Isoform 2
Keywords
- Cellular component
Disease & Variants
Involvement in disease
Multicentric osteolysis, nodulosis, and arthropathy (MONA)
- Note
- 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 alsoMIM:259600
Natural variants in MONA
Variant ID | Position(s) | Change | Description | |
---|---|---|---|---|
VAR_032423 | 101 | R>H | in MONA; dbSNP:rs121912953 | |
VAR_054996 | 400 | missing | in MONA; dbSNP:rs2142358692 | |
VAR_032425 | 404 | E>K | in MONA; dbSNP:rs121912955 |
Features
Showing features for natural variant.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Natural variant | VAR_032423 | 101 | in MONA; dbSNP:rs121912953 | |||
Sequence: R → H | ||||||
Natural variant | VAR_032424 | 210 | in dbSNP:rs1230286710 | |||
Sequence: D → Y | ||||||
Natural variant | VAR_036136 | 228 | in a colorectal cancer sample; somatic mutation; dbSNP:rs759302357 | |||
Sequence: A → T | ||||||
Natural variant | VAR_054996 | 400 | in MONA; dbSNP:rs2142358692 | |||
Sequence: Missing | ||||||
Natural variant | VAR_032425 | 404 | in MONA; dbSNP:rs121912955 | |||
Sequence: E → K | ||||||
Natural variant | VAR_020616 | 447 | in dbSNP:rs17859943 | |||
Sequence: A → V | ||||||
Natural variant | VAR_036137 | 498 | in a colorectal cancer sample; somatic mutation; dbSNP:rs764961297 | |||
Sequence: T → M | ||||||
Natural variant | VAR_020617 | 621 | in dbSNP:rs16955280 | |||
Sequence: V → L | ||||||
Natural variant | VAR_036138 | 644 | in a colorectal cancer sample; somatic mutation | |||
Sequence: S → I |
Variants
We now provide the "Disease & Variants" viewer in its own tab.
The viewer provides 818 variants from UniProt as well as other sources including ClinVar and dbSNP.
Keywords
- Disease
Organism-specific databases
Miscellaneous
Chemistry
Genetic variation databases
PTM/Processing
Features
Showing features for signal, propeptide, chain, modified residue (large scale data), disulfide bond, glycosylation.
Type | ID | Position(s) | Source | Description | |||
---|---|---|---|---|---|---|---|
Signal | 1-29 | UniProt | |||||
Sequence: MEALMARGALTGPLRALCLLGCLLSHAAA | |||||||
Propeptide | PRO_0000028714 | 30-109 | UniProt | Activation peptide | |||
Sequence: APSPIIKFPGDVAPKTDKELAVQYLNTFYGCPKESCNLFVLKDTLKKMQKFFGLPQTGDLDQNTIETMRKPRCGNPDVAN | |||||||
Chain | PRO_0000028715 | 110-660 | UniProt | 72 kDa type IV collagenase | |||
Sequence: YNFFPRKPKWDKNQITYRIIGYTPDLDPETVDDAFARAFQVWSDVTPLRFSRIHDGEADIMINFGRWEHGDGYPFDGKDGLLAHAFAPGTGVGGDSHFDDDELWTLGEGQVVRVKYGNADGEYCKFPFLFNGKEYNSCTDTGRSDGFLWCSTTYNFEKDGKYGFCPHEALFTMGGNAEGQPCKFPFRFQGTSYDSCTTEGRTDGYRWCGTTEDYDRDKKYGFCPETAMSTVGGNSEGAPCVFPFTFLGNKYESCTSAGRSDGKMWCATTANYDDDRKWGFCPDQGYSLFLVAAHEFGHAMGLEHSQDPGALMAPIYTYTKNFRLSQDDIKGIQELYGASPDIDLGTGPTPTLGPVTPEICKQDIVFDGIAQIRGEIFFFKDRFIWRTVTPRDKPMGPLLVATFWPELPEKIDAVYEAPQEEKAVFFAGNEYWIYSASTLERGYPKPLTSLGLPPDVQRVDAAFNWSKNKKTYIFAGDKFWRYNEVKKKMDPGFPKLIADAWNAIPDNLDAVVDLQGGGHSYFFKGAYYLKLENQSLKSVKFGSIKSDWLGC | |||||||
Modified residue (large scale data) | 205 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Disulfide bond | 233↔259 | UniProt | |||||
Sequence: CKFPFLFNGKEYNSCTDTGRSDGFLWC | |||||||
Disulfide bond | 247↔274 | UniProt | |||||
Sequence: CTDTGRSDGFLWCSTTYNFEKDGKYGFC | |||||||
Disulfide bond | 291↔317 | UniProt | |||||
Sequence: CKFPFRFQGTSYDSCTTEGRTDGYRWC | |||||||
Disulfide bond | 305↔332 | UniProt | |||||
Sequence: CTTEGRTDGYRWCGTTEDYDRDKKYGFC | |||||||
Disulfide bond | 349↔375 | UniProt | |||||
Sequence: CVFPFTFLGNKYESCTSAGRSDGKMWC | |||||||
Disulfide bond | 363↔390 | UniProt | |||||
Sequence: CTSAGRSDGKMWCATTANYDDDRKWGFC | |||||||
Chain | PRO_0000391626 | 445-660 | UniProt | PEX | |||
Sequence: YGASPDIDLGTGPTPTLGPVTPEICKQDIVFDGIAQIRGEIFFFKDRFIWRTVTPRDKPMGPLLVATFWPELPEKIDAVYEAPQEEKAVFFAGNEYWIYSASTLERGYPKPLTSLGLPPDVQRVDAAFNWSKNKKTYIFAGDKFWRYNEVKKKMDPGFPKLIADAWNAIPDNLDAVVDLQGGGHSYFFKGAYYLKLENQSLKSVKFGSIKSDWLGC | |||||||
Disulfide bond | 469↔660 | UniProt | |||||
Sequence: CKQDIVFDGIAQIRGEIFFFKDRFIWRTVTPRDKPMGPLLVATFWPELPEKIDAVYEAPQEEKAVFFAGNEYWIYSASTLERGYPKPLTSLGLPPDVQRVDAAFNWSKNKKTYIFAGDKFWRYNEVKKKMDPGFPKLIADAWNAIPDNLDAVVDLQGGGHSYFFKGAYYLKLENQSLKSVKFGSIKSDWLGC | |||||||
Glycosylation | 573 | UniProt | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | |||||||
Glycosylation | 642 | UniProt | N-linked (GlcNAc...) asparagine | ||||
Sequence: N |
Post-translational modification
Keywords
- PTM
Proteomic databases
PTM databases
Expression
Tissue specificity
Induction
Gene expression databases
Organism-specific databases
Interaction
Subunit
Binary interactions
Type | Entry 1 | Entry 2 | Number of experiments | Intact | |
---|---|---|---|---|---|
BINARY | P08253 | APP P05067 | 3 | EBI-1033518, EBI-77613 | |
BINARY | P08253 | APP PRO_0000000092 P05067 | 4 | EBI-1033518, EBI-821758 | |
BINARY | P08253 | APP PRO_0000000093 P05067 | 2 | EBI-1033518, EBI-2431589 | |
BINARY | P08253 | COL5A1 P20908 | 4 | EBI-1033518, EBI-2464511 | |
BINARY | P08253 | PCSK9 Q8NBP7 | 4 | EBI-1033518, EBI-7539251 | |
BINARY | P08253 | REL Q04864-2 | 3 | EBI-1033518, EBI-10829018 | |
BINARY | P08253 | SCUBE3 Q8IX30 | 2 | EBI-1033518, EBI-4479975 | |
BINARY | P08253 | TIMP2 P16035 | 3 | EBI-1033518, EBI-1033507 |
Protein-protein interaction databases
Chemistry
Miscellaneous
Structure
Family & Domains
Features
Showing features for motif, region, domain, repeat.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Motif | 100-107 | Cysteine switch | ||||
Sequence: PRCGNPDV | ||||||
Region | 110-221 | Collagenase-like 1 | ||||
Sequence: YNFFPRKPKWDKNQITYRIIGYTPDLDPETVDDAFARAFQVWSDVTPLRFSRIHDGEADIMINFGRWEHGDGYPFDGKDGLLAHAFAPGTGVGGDSHFDDDELWTLGEGQVV | ||||||
Region | 222-396 | Collagen-binding | ||||
Sequence: RVKYGNADGEYCKFPFLFNGKEYNSCTDTGRSDGFLWCSTTYNFEKDGKYGFCPHEALFTMGGNAEGQPCKFPFRFQGTSYDSCTTEGRTDGYRWCGTTEDYDRDKKYGFCPETAMSTVGGNSEGAPCVFPFTFLGNKYESCTSAGRSDGKMWCATTANYDDDRKWGFCPDQGYS | ||||||
Domain | 228-276 | Fibronectin type-II 1 | ||||
Sequence: ADGEYCKFPFLFNGKEYNSCTDTGRSDGFLWCSTTYNFEKDGKYGFCPH | ||||||
Domain | 286-334 | Fibronectin type-II 2 | ||||
Sequence: AEGQPCKFPFRFQGTSYDSCTTEGRTDGYRWCGTTEDYDRDKKYGFCPE | ||||||
Domain | 344-392 | Fibronectin type-II 3 | ||||
Sequence: SEGAPCVFPFTFLGNKYESCTSAGRSDGKMWCATTANYDDDRKWGFCPD | ||||||
Region | 397-465 | Collagenase-like 2 | ||||
Sequence: LFLVAAHEFGHAMGLEHSQDPGALMAPIYTYTKNFRLSQDDIKGIQELYGASPDIDLGTGPTPTLGPVT | ||||||
Region | 414-660 | Required for inhibitor TIMP2 binding | ||||
Sequence: SQDPGALMAPIYTYTKNFRLSQDDIKGIQELYGASPDIDLGTGPTPTLGPVTPEICKQDIVFDGIAQIRGEIFFFKDRFIWRTVTPRDKPMGPLLVATFWPELPEKIDAVYEAPQEEKAVFFAGNEYWIYSASTLERGYPKPLTSLGLPPDVQRVDAAFNWSKNKKTYIFAGDKFWRYNEVKKKMDPGFPKLIADAWNAIPDNLDAVVDLQGGGHSYFFKGAYYLKLENQSLKSVKFGSIKSDWLGC | ||||||
Repeat | 472-516 | Hemopexin 1 | ||||
Sequence: DIVFDGIAQIRGEIFFFKDRFIWRTVTPRDKPMGPLLVATFWPEL | ||||||
Repeat | 517-563 | Hemopexin 2 | ||||
Sequence: PEKIDAVYEAPQEEKAVFFAGNEYWIYSASTLERGYPKPLTSLGLPP | ||||||
Repeat | 565-613 | Hemopexin 3 | ||||
Sequence: VQRVDAAFNWSKNKKTYIFAGDKFWRYNEVKKKMDPGFPKLIADAWNAI | ||||||
Repeat | 614-660 | Hemopexin 4 | ||||
Sequence: PDNLDAVVDLQGGGHSYFFKGAYYLKLENQSLKSVKFGSIKSDWLGC |
Domain
Sequence similarities
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence & Isoforms
- Sequence statusComplete
- Sequence processingThe displayed sequence is further processed into a mature form.
This entry describes 3 isoforms produced by Alternative splicing.
P08253-1
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.
- Name1
- Length660
- Mass (Da)73,882
- Last updated1991-02-01 v2
- ChecksumBC7147DC8B49F289
P08253-2
- Name2
- NoteInduced by oxidative stress.
- Differences from canonical
- 1-76: Missing
P08253-3
- Name3
- Differences from canonical
- 1-51: MEALMARGALTGPLRALCLLGCLLSHAAAAPSPIIKFPGDVAPKTDKELAV → M
Computationally mapped potential isoform sequences
There are 4 potential isoforms mapped to this entry
Features
Showing features for alternative sequence, sequence conflict.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Alternative sequence | VSP_045704 | 1-51 | in isoform 3 | |||
Sequence: MEALMARGALTGPLRALCLLGCLLSHAAAAPSPIIKFPGDVAPKTDKELAV → M | ||||||
Alternative sequence | VSP_044631 | 1-76 | in isoform 2 | |||
Sequence: Missing | ||||||
Sequence conflict | 235 | in Ref. 3; AK310314 | ||||
Sequence: F → S | ||||||
Sequence conflict | 546 | in Ref. 3; BAG35588 | ||||
Sequence: S → G | ||||||
Sequence conflict | 618 | in Ref. 3; BAG35588 | ||||
Sequence: D → G |
Keywords
- Coding sequence diversity
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
M55593 EMBL· GenBank· DDBJ | AAA52028.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
M58552 EMBL· GenBank· DDBJ | AAA52028.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
M55582 EMBL· GenBank· DDBJ | AAA52028.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
M55583 EMBL· GenBank· DDBJ | AAA52028.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
M55584 EMBL· GenBank· DDBJ | AAA52028.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
M55585 EMBL· GenBank· DDBJ | AAA52028.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
M55586 EMBL· GenBank· DDBJ | AAA52028.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
M55587 EMBL· GenBank· DDBJ | AAA52028.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
M55588 EMBL· GenBank· DDBJ | AAA52028.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
M55589 EMBL· GenBank· DDBJ | AAA52028.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
M55590 EMBL· GenBank· DDBJ | AAA52028.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
M55591 EMBL· GenBank· DDBJ | AAA52028.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
M55592 EMBL· GenBank· DDBJ | AAA52028.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AK301536 EMBL· GenBank· DDBJ | BAG63035.1 EMBL· GenBank· DDBJ | mRNA | ||
AK310314 EMBL· GenBank· DDBJ | - | mRNA | No translation available. | |
AK312711 EMBL· GenBank· DDBJ | BAG35588.1 EMBL· GenBank· DDBJ | mRNA | ||
AY738117 EMBL· GenBank· DDBJ | AAU10089.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AC007336 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. | |
AC092722 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. | |
BC002576 EMBL· GenBank· DDBJ | AAH02576.1 EMBL· GenBank· DDBJ | mRNA | ||
M33789 EMBL· GenBank· DDBJ | AAA52027.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
J03210 EMBL· GenBank· DDBJ | AAA35701.1 EMBL· GenBank· DDBJ | mRNA |