Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Basket 0
(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

P41245

- MMP9_MOUSE

UniProt

P41245 - MMP9_MOUSE

Protein

Matrix metalloproteinase-9

Gene

Mmp9

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at transcript leveli
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 151 (01 Oct 2014)
      Sequence version 2 (27 Jul 2011)
      Previous versions | rss
    • Help video
    • Feedback
    • Comment

    Functioni

    Could play a role in bone osteoclastic resorption. Cleaves type IV and type V collagen into large C-terminal three quarter fragments and shorter N-terminal one quarter fragments By similarity.By similarity

    Catalytic activityi

    Cleavage of gelatin types I and V and collagen types IV and V.

    Cofactori

    Binds 2 zinc ions per subunit.By similarity
    Binds 3 calcium ions per subunit.By similarity

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Metal bindingi100 – 1001Zinc 2; in inhibited formBy similarity
    Metal bindingi131 – 1311Calcium 1By similarity
    Metal bindingi165 – 1651Calcium 2; via carbonyl oxygenBy similarity
    Metal bindingi175 – 1751Zinc 1; structuralBy similarity
    Metal bindingi177 – 1771Zinc 1; structuralBy similarity
    Metal bindingi182 – 1821Calcium 3By similarity
    Metal bindingi183 – 1831Calcium 3; via carbonyl oxygenBy similarity
    Metal bindingi185 – 1851Calcium 3; via carbonyl oxygenBy similarity
    Metal bindingi187 – 1871Calcium 3; via carbonyl oxygenBy similarity
    Metal bindingi190 – 1901Zinc 1; structuralBy similarity
    Metal bindingi197 – 1971Calcium 2; via carbonyl oxygenBy similarity
    Metal bindingi199 – 1991Calcium 2; via carbonyl oxygenBy similarity
    Metal bindingi201 – 2011Calcium 2By similarity
    Metal bindingi203 – 2031Zinc 1; structuralBy similarity
    Metal bindingi205 – 2051Calcium 3By similarity
    Metal bindingi206 – 2061Calcium 1By similarity
    Metal bindingi208 – 2081Calcium 1By similarity
    Metal bindingi208 – 2081Calcium 3By similarity
    Metal bindingi401 – 4011Zinc 2; catalyticBy similarity
    Active sitei402 – 4021PROSITE-ProRule annotation
    Metal bindingi405 – 4051Zinc 2; catalyticBy similarity
    Metal bindingi411 – 4111Zinc 2; catalyticBy similarity

    GO - Molecular functioni

    1. metalloendopeptidase activity Source: UniProtKB
    2. peptidase activity Source: MGI
    3. zinc ion binding Source: InterPro

    GO - Biological processi

    1. collagen catabolic process Source: MGI
    2. embryo implantation Source: MGI
    3. extracellular matrix organization Source: MGI
    4. leukocyte migration Source: InterPro
    5. ossification Source: InterPro
    6. positive regulation of apoptotic process Source: MGI
    7. positive regulation of keratinocyte migration Source: Ensembl
    8. proteolysis Source: UniProtKB
    9. skeletal system development Source: MGI

    Keywords - Molecular functioni

    Hydrolase, Metalloprotease, Protease

    Keywords - Biological processi

    Collagen degradation

    Keywords - Ligandi

    Calcium, Metal-binding, Zinc

    Enzyme and pathway databases

    ReactomeiREACT_188578. Signaling by SCF-KIT.
    REACT_199000. Activation of Matrix Metalloproteinases.
    REACT_199052. Degradation of the extracellular matrix.
    REACT_199055. Collagen degradation.

    Protein family/group databases

    MEROPSiM10.004.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Matrix metalloproteinase-9 (EC:3.4.24.35)
    Short name:
    MMP-9
    Alternative name(s):
    92 kDa gelatinase
    92 kDa type IV collagenase
    Gelatinase B
    Short name:
    GELB
    Gene namesi
    Name:Mmp9
    Synonyms:Clg4b
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome 2

    Organism-specific databases

    MGIiMGI:97011. Mmp9.

    Subcellular locationi

    GO - Cellular componenti

    1. extracellular space Source: UniProtKB
    2. proteinaceous extracellular matrix Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Extracellular matrix, Secreted

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 1919By similarityAdd
    BLAST
    Propeptidei20 – 10788Activation peptideBy similarityPRO_0000028758Add
    BLAST
    Chaini108 – 730623Matrix metalloproteinase-9PRO_0000028759Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Glycosylationi39 – 391N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi120 – 1201N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi127 – 1271N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi230 ↔ 256PROSITE-ProRule annotation
    Disulfide bondi244 ↔ 271PROSITE-ProRule annotation
    Disulfide bondi288 ↔ 314PROSITE-ProRule annotation
    Disulfide bondi302 ↔ 329PROSITE-ProRule annotation
    Disulfide bondi347 ↔ 373PROSITE-ProRule annotation
    Disulfide bondi361 ↔ 388PROSITE-ProRule annotation
    Disulfide bondi534 ↔ 729PROSITE-ProRule annotation

    Post-translational modificationi

    N- and O-glycosylated.By similarity

    Keywords - PTMi

    Disulfide bond, Glycoprotein, Zymogen

    Proteomic databases

    MaxQBiP41245.
    PaxDbiP41245.
    PRIDEiP41245.

    PTM databases

    PhosphoSiteiP41245.

    Expressioni

    Inductioni

    Up-regulated by ARHGEF4, SPATA13 and APC via the JNK signaling pathway in colorectal tumor cells.1 Publication

    Gene expression databases

    ArrayExpressiP41245.
    BgeeiP41245.
    CleanExiMM_MMP9.
    GenevestigatoriP41245.

    Interactioni

    Subunit structurei

    Exists as monomer or homodimer; disulfide-linked. Exists also as heterodimer with a 25 kDa protein. Interacts with ECM1.By similarity

    Protein-protein interaction databases

    BioGridi201454. 1 interaction.

    Structurei

    3D structure databases

    ProteinModelPortaliP41245.
    SMRiP41245. Positions 29-730.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini225 – 27349Fibronectin type-II 1PROSITE-ProRule annotationAdd
    BLAST
    Domaini283 – 33149Fibronectin type-II 2PROSITE-ProRule annotationAdd
    BLAST
    Domaini342 – 39049Fibronectin type-II 3PROSITE-ProRule annotationAdd
    BLAST
    Repeati536 – 58146Hemopexin 1Add
    BLAST
    Repeati582 – 62645Hemopexin 2Add
    BLAST
    Repeati628 – 67548Hemopexin 3Add
    BLAST
    Repeati676 – 72954Hemopexin 4Add
    BLAST

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi98 – 1058Cysteine 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 3 fibronectin type-II domains.PROSITE-ProRule annotation
    Contains 4 hemopexin repeats.Curated

    Keywords - Domaini

    Repeat, Signal

    Phylogenomic databases

    eggNOGiNOG328372.
    GeneTreeiENSGT00730000110410.
    HOGENOMiHOG000217926.
    HOVERGENiHBG052484.
    InParanoidiQ80XI8.
    KOiK01403.
    OMAiEGDLKWH.
    OrthoDBiEOG70KGNX.
    TreeFamiTF315428.

    Family and domain databases

    Gene3Di2.10.10.10. 3 hits.
    2.110.10.10. 1 hit.
    3.40.390.10. 2 hits.
    InterProiIPR000562. FN_type2_col-bd.
    IPR000585. Hemopexin-like_dom.
    IPR018487. Hemopexin-like_repeat.
    IPR018486. Hemopexin_CS.
    IPR013806. Kringle-like.
    IPR024079. MetalloPept_cat_dom.
    IPR028688. MMP9.
    IPR001818. Pept_M10_metallopeptidase.
    IPR021190. Pept_M10A.
    IPR021158. Pept_M10A_Zn_BS.
    IPR006026. Peptidase_Metallo.
    IPR002477. Peptidoglycan-bd-like.
    IPR006970. PT.
    [Graphical view]
    PANTHERiPTHR10201:SF30. PTHR10201:SF30. 1 hit.
    PfamiPF00040. fn2. 3 hits.
    PF00045. Hemopexin. 2 hits.
    PF00413. Peptidase_M10. 1 hit.
    PF01471. PG_binding_1. 1 hit.
    PF04886. PT. 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]

    Sequencei

    Sequence statusi: Complete.

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

    P41245-1 [UniParc]FASTAAdd to Basket

    « Hide

    MSPWQPLLLA LLAFGCSSAA PYQRQPTFVV FPKDLKTSNL TDTQLAEAYL    50
    YRYGYTRAAQ MMGEKQSLRP ALLMLQKQLS LPQTGELDSQ TLKAIRTPRC 100
    GVPDVGRFQT FKGLKWDHHN ITYWIQNYSE DLPRDMIDDA FARAFAVWGE 150
    VAPLTFTRVY GPEADIVIQF GVAEHGDGYP FDGKDGLLAH AFPPGAGVQG 200
    DAHFDDDELW SLGKGVVIPT YYGNSNGAPC HFPFTFEGRS YSACTTDGRN 250
    DGTPWCSTTA DYDKDGKFGF CPSERLYTEH GNGEGKPCVF PFIFEGRSYS 300
    ACTTKGRSDG YRWCATTANY DQDKLYGFCP TRVDATVVGG NSAGELCVFP 350
    FVFLGKQYSS CTSDGRRDGR LWCATTSNFD TDKKWGFCPD QGYSLFLVAA 400
    HEFGHALGLD HSSVPEALMY PLYSYLEGFP LNKDDIDGIQ YLYGRGSKPD 450
    PRPPATTTTE PQPTAPPTMC PTIPPTAYPT VGPTVGPTGA PSPGPTSSPS 500
    PGPTGAPSPG PTAPPTAGSS EASTESLSPA DNPCNVDVFD AIAEIQGALH 550
    FFKDGWYWKF LNHRGSPLQG PFLTARTWPA LPATLDSAFE DPQTKRVFFF 600
    SGRQMWVYTG KTVLGPRSLD KLGLGPEVTH VSGLLPRRLG KALLFSKGRV 650
    WRFDLKSQKV DPQSVIRVDK EFSGVPWNSH DIFQYQDKAY FCHGKFFWRV 700
    SFQNEVNKVD HEVNQVDDVG YVTYDLLQCP 730
    Length:730
    Mass (Da):80,535
    Last modified:July 27, 2011 - v2
    Checksum:iE16F45C24D4D1024
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti20 – 201A → C in AAB28942. (PubMed:8219207)Curated
    Sequence conflicti25 – 262QP → HA in AAB28942. (PubMed:8219207)Curated
    Sequence conflicti466 – 4661P → T in BAB23442. (PubMed:16141072)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti514 – 5141P → A.1 Publication
    Natural varianti639 – 6391L → P.1 Publication
    Natural varianti711 – 7111H → P.1 Publication

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    D12712 mRNA. Translation: BAA02208.1.
    S67830 mRNA. Translation: AAB28942.1.
    X72794 Genomic DNA. Translation: CAA51314.1.
    X72795 mRNA. Translation: CAA51315.1.
    Z27231 mRNA. Translation: CAA81745.1.
    AK004651 mRNA. Translation: BAB23442.1.
    AK159292 mRNA. Translation: BAE34968.1.
    AL591495 Genomic DNA. Translation: CAM26465.1.
    BC046991 mRNA. Translation: AAH46991.1.
    CCDSiCCDS17066.1.
    PIRiI52580.
    JC1456.
    RefSeqiNP_038627.1. NM_013599.3.
    UniGeneiMm.4406.

    Genome annotation databases

    EnsembliENSMUST00000017881; ENSMUSP00000017881; ENSMUSG00000017737.
    GeneIDi17395.
    KEGGimmu:17395.
    UCSCiuc008nwt.1. mouse.

    Keywords - Coding sequence diversityi

    Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    D12712 mRNA. Translation: BAA02208.1 .
    S67830 mRNA. Translation: AAB28942.1 .
    X72794 Genomic DNA. Translation: CAA51314.1 .
    X72795 mRNA. Translation: CAA51315.1 .
    Z27231 mRNA. Translation: CAA81745.1 .
    AK004651 mRNA. Translation: BAB23442.1 .
    AK159292 mRNA. Translation: BAE34968.1 .
    AL591495 Genomic DNA. Translation: CAM26465.1 .
    BC046991 mRNA. Translation: AAH46991.1 .
    CCDSi CCDS17066.1.
    PIRi I52580.
    JC1456.
    RefSeqi NP_038627.1. NM_013599.3.
    UniGenei Mm.4406.

    3D structure databases

    ProteinModelPortali P41245.
    SMRi P41245. Positions 29-730.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 201454. 1 interaction.

    Chemistry

    BindingDBi P41245.
    ChEMBLi CHEMBL2214.

    Protein family/group databases

    MEROPSi M10.004.

    PTM databases

    PhosphoSitei P41245.

    Proteomic databases

    MaxQBi P41245.
    PaxDbi P41245.
    PRIDEi P41245.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000017881 ; ENSMUSP00000017881 ; ENSMUSG00000017737 .
    GeneIDi 17395.
    KEGGi mmu:17395.
    UCSCi uc008nwt.1. mouse.

    Organism-specific databases

    CTDi 4318.
    MGIi MGI:97011. Mmp9.

    Phylogenomic databases

    eggNOGi NOG328372.
    GeneTreei ENSGT00730000110410.
    HOGENOMi HOG000217926.
    HOVERGENi HBG052484.
    InParanoidi Q80XI8.
    KOi K01403.
    OMAi EGDLKWH.
    OrthoDBi EOG70KGNX.
    TreeFami TF315428.

    Enzyme and pathway databases

    Reactomei REACT_188578. Signaling by SCF-KIT.
    REACT_199000. Activation of Matrix Metalloproteinases.
    REACT_199052. Degradation of the extracellular matrix.
    REACT_199055. Collagen degradation.

    Miscellaneous databases

    NextBioi 292032.
    PROi P41245.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P41245.
    Bgeei P41245.
    CleanExi MM_MMP9.
    Genevestigatori P41245.

    Family and domain databases

    Gene3Di 2.10.10.10. 3 hits.
    2.110.10.10. 1 hit.
    3.40.390.10. 2 hits.
    InterProi IPR000562. FN_type2_col-bd.
    IPR000585. Hemopexin-like_dom.
    IPR018487. Hemopexin-like_repeat.
    IPR018486. Hemopexin_CS.
    IPR013806. Kringle-like.
    IPR024079. MetalloPept_cat_dom.
    IPR028688. MMP9.
    IPR001818. Pept_M10_metallopeptidase.
    IPR021190. Pept_M10A.
    IPR021158. Pept_M10A_Zn_BS.
    IPR006026. Peptidase_Metallo.
    IPR002477. Peptidoglycan-bd-like.
    IPR006970. PT.
    [Graphical view ]
    PANTHERi PTHR10201:SF30. PTHR10201:SF30. 1 hit.
    Pfami PF00040. fn2. 3 hits.
    PF00045. Hemopexin. 2 hits.
    PF00413. Peptidase_M10. 1 hit.
    PF01471. PG_binding_1. 1 hit.
    PF04886. PT. 1 hit.
    [Graphical view ]
    PRINTSi PR00138. MATRIXIN.
    SMARTi SM00059. FN2. 3 hits.
    SM00120. HX. 4 hits.
    SM00235. ZnMc. 1 hit.
    [Graphical view ]
    SUPFAMi SSF47090. SSF47090. 1 hit.
    SSF50923. SSF50923. 1 hit.
    SSF57440. SSF57440. 3 hits.
    PROSITEi PS00546. 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 ]
    ProtoNeti Search...

    Publicationsi

    1. "Molecular cloning and expression of the mouse 105-kDa gelatinase cDNA."
      Tanaka H., Hojo K., Yoshida H., Yoshioka T., Sugita K.
      Biochem. Biophys. Res. Commun. 190:732-740(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    2. "Cloning and expression of the cDNA encoding mouse neutrophil gelatinase: demonstration of coordinate secondary granule protein gene expression during terminal neutrophil maturation."
      Graubert T., Johnston J., Berliner N.
      Blood 82:3192-3197(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], VARIANTS ALA-514; PRO-639 AND PRO-711.
    3. "Mouse gelatinase B. cDNA cloning, regulation of expression and glycosylation in WEHI-3 macrophages and gene organisation."
      Masure S., Nys G., Fiten P., van Damme J., Opdenakker G.
      Eur. J. Biochem. 218:129-141(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
      Strain: C57BL/6.
      Tissue: Liver.
    4. "High expression of 92-kD type IV collagenase (gelatinase B) in the osteoclast lineage during mouse development."
      Reponen P., Sahlberg C., Munaut C., Thesleff I., Tryggvason K.
      J. Cell Biol. 124:1091-1102(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Tissue: Bone.
    5. "The transcriptional landscape of the mammalian genome."
      Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
      , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
      Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Strain: C57BL/6J.
      Tissue: Lung.
    6. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: C57BL/6J.
    7. "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: Olfactory epithelium.
    8. "The adenomatous polyposis coli-associated exchange factors Asef and Asef2 are required for adenoma formation in Apc(Min/+)mice."
      Kawasaki Y., Tsuji S., Muroya K., Furukawa S., Shibata Y., Okuno M., Ohwada S., Akiyama T.
      EMBO Rep. 10:1355-1362(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: INDUCTION.

    Entry informationi

    Entry nameiMMP9_MOUSE
    AccessioniPrimary (citable) accession number: P41245
    Secondary accession number(s): Q06788, Q80XI8, Q9DC02
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: February 1, 1995
    Last sequence update: July 27, 2011
    Last modified: October 1, 2014
    This is version 151 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. MGD cross-references
      Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
    2. Peptidase families
      Classification of peptidase families and list of entries
    3. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3