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P41245

- MMP9_MOUSE

UniProt

P41245 - MMP9_MOUSE

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Protein

Matrix metalloproteinase-9

Gene

Mmp9

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at transcript leveli

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

Protein has several cofactor binding sites:
  • Zn2+By similarityNote: Binds 2 Zn(2+) ions per subunit.By similarity
  • Ca2+By similarityNote: Binds 3 Ca(2+) 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. negative regulation of cation channel activity Source: Ensembl
  6. ossification Source: InterPro
  7. positive regulation of apoptotic process Source: MGI
  8. positive regulation of keratinocyte migration Source: Ensembl
  9. positive regulation of receptor binding Source: Ensembl
  10. proteolysis Source: UniProtKB
  11. skeletal system development Source: MGI
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_188578. Signaling by SCF-KIT.
REACT_199000. Activation of Matrix Metalloproteinases.
REACT_199046. Assembly of collagen fibrils and other multimeric structures.
REACT_199052. Degradation of the extracellular matrix.
REACT_199055. Collagen degradation.
REACT_243590. EPH-ephrin mediated repulsion of cells.

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. extracellular vesicular exosome Source: Ensembl
  3. proteinaceous extracellular matrix Source: UniProtKB-KW
Complete GO annotation...

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

BgeeiP41245.
CleanExiMM_MMP9.
ExpressionAtlasiP41245. baseline and differential.
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.
GeneTreeiENSGT00760000119132.
HOGENOMiHOG000217926.
HOVERGENiHBG052484.
InParanoidiP41245.
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

        10         20         30         40         50
MSPWQPLLLA LLAFGCSSAA PYQRQPTFVV FPKDLKTSNL TDTQLAEAYL
60 70 80 90 100
YRYGYTRAAQ MMGEKQSLRP ALLMLQKQLS LPQTGELDSQ TLKAIRTPRC
110 120 130 140 150
GVPDVGRFQT FKGLKWDHHN ITYWIQNYSE DLPRDMIDDA FARAFAVWGE
160 170 180 190 200
VAPLTFTRVY GPEADIVIQF GVAEHGDGYP FDGKDGLLAH AFPPGAGVQG
210 220 230 240 250
DAHFDDDELW SLGKGVVIPT YYGNSNGAPC HFPFTFEGRS YSACTTDGRN
260 270 280 290 300
DGTPWCSTTA DYDKDGKFGF CPSERLYTEH GNGEGKPCVF PFIFEGRSYS
310 320 330 340 350
ACTTKGRSDG YRWCATTANY DQDKLYGFCP TRVDATVVGG NSAGELCVFP
360 370 380 390 400
FVFLGKQYSS CTSDGRRDGR LWCATTSNFD TDKKWGFCPD QGYSLFLVAA
410 420 430 440 450
HEFGHALGLD HSSVPEALMY PLYSYLEGFP LNKDDIDGIQ YLYGRGSKPD
460 470 480 490 500
PRPPATTTTE PQPTAPPTMC PTIPPTAYPT VGPTVGPTGA PSPGPTSSPS
510 520 530 540 550
PGPTGAPSPG PTAPPTAGSS EASTESLSPA DNPCNVDVFD AIAEIQGALH
560 570 580 590 600
FFKDGWYWKF LNHRGSPLQG PFLTARTWPA LPATLDSAFE DPQTKRVFFF
610 620 630 640 650
SGRQMWVYTG KTVLGPRSLD KLGLGPEVTH VSGLLPRRLG KALLFSKGRV
660 670 680 690 700
WRFDLKSQKV DPQSVIRVDK EFSGVPWNSH DIFQYQDKAY FCHGKFFWRV
710 720 730
SFQNEVNKVD HEVNQVDDVG YVTYDLLQCP
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:
EMBLi
GenBanki
DDBJi
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:
EMBLi
GenBanki
DDBJi
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 ENSGT00760000119132.
HOGENOMi HOG000217926.
HOVERGENi HBG052484.
InParanoidi P41245.
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_199046. Assembly of collagen fibrils and other multimeric structures.
REACT_199052. Degradation of the extracellular matrix.
REACT_199055. Collagen degradation.
REACT_243590. EPH-ephrin mediated repulsion of cells.

Miscellaneous databases

NextBioi 292032.
PROi P41245.
SOURCEi Search...

Gene expression databases

Bgeei P41245.
CleanExi MM_MMP9.
ExpressionAtlasi P41245. baseline and differential.
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

« Hide 'large scale' publications
  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: November 26, 2014
This is version 153 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