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P34960

- MMP12_MOUSE

UniProt

P34960 - MMP12_MOUSE

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Protein
Macrophage metalloelastase
Gene
Mmp12, Mme, Mmel
Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

May be involved in tissue injury and remodeling. Has significant elastolytic activity. Can accept large and small amino acids at the P1' site, but has a preference for leucine. Aromatic or hydrophobic residues are preferred at the P1 site, with small hydrophobic residues (preferably alanine) occupying P3 By similarity.

Catalytic activityi

Hydrolysis of soluble and insoluble elastin. Specific cleavages are also produced at 14-Ala-|-Leu-15 and 16-Tyr-|-Leu-17 in the B chain of insulin.

Cofactori

Binds 4 calcium ions per subunit By similarity.
Binds 2 zinc ions per subunit By similarity.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi96 – 961Zinc 2; in inhibited form By similarity
Metal bindingi128 – 1281Calcium 1 By similarity
Metal bindingi162 – 1621Calcium 2 By similarity
Metal bindingi172 – 1721Zinc 1 By similarity
Metal bindingi174 – 1741Zinc 1 By similarity
Metal bindingi179 – 1791Calcium 3 By similarity
Metal bindingi180 – 1801Calcium 3; via carbonyl oxygen By similarity
Metal bindingi182 – 1821Calcium 3; via carbonyl oxygen By similarity
Metal bindingi184 – 1841Calcium 3; via carbonyl oxygen By similarity
Metal bindingi187 – 1871Zinc 1 By similarity
Metal bindingi194 – 1941Calcium 2; via carbonyl oxygen By similarity
Metal bindingi198 – 1981Calcium 2 By similarity
Metal bindingi200 – 2001Zinc 1 By similarity
Metal bindingi202 – 2021Calcium 3 By similarity
Metal bindingi203 – 2031Calcium 1 By similarity
Metal bindingi205 – 2051Calcium 1 By similarity
Metal bindingi205 – 2051Calcium 3 By similarity
Metal bindingi222 – 2221Zinc 2; catalytic By similarity
Active sitei223 – 2231 By similarity
Metal bindingi226 – 2261Zinc 2; catalytic By similarity
Metal bindingi232 – 2321Zinc 2; catalytic By similarity
Metal bindingi293 – 2931Calcium 4; via carbonyl oxygen By similarity
Metal bindingi385 – 3851Calcium 4; via carbonyl oxygen By similarity
Metal bindingi434 – 4341Calcium 4; via carbonyl oxygen By similarity

GO - Molecular functioni

  1. calcium ion binding Source: InterPro
  2. metalloendopeptidase activity Source: InterPro
  3. zinc ion binding Source: InterPro

GO - Biological processi

  1. wound healing Source: InterPro
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Metalloprotease, Protease

Keywords - Ligandi

Calcium, Metal-binding, Zinc

Enzyme and pathway databases

ReactomeiREACT_199052. Degradation of the extracellular matrix.

Protein family/group databases

MEROPSiM10.009.

Names & Taxonomyi

Protein namesi
Recommended name:
Macrophage metalloelastase (EC:3.4.24.65)
Short name:
MME
Alternative name(s):
Matrix metalloproteinase-12
Short name:
MMP-12
Gene namesi
Name:Mmp12
Synonyms:Mme, Mmel
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Chromosome 9

Organism-specific databases

MGIiMGI:97005. Mmp12.

Subcellular locationi

GO - Cellular componenti

  1. extracellular region Source: Reactome
  2. proteinaceous extracellular matrix Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Extracellular matrix, Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2828 Inferred
Add
BLAST
Propeptidei29 – 10981Activation peptide
PRO_0000028778Add
BLAST
Chaini110 – 473364Macrophage metalloelastase
PRO_0000028779Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi32 – 321N-linked (GlcNAc...) Reviewed prediction
Glycosylationi85 – 851N-linked (GlcNAc...) Reviewed prediction
Disulfide bondi286 ↔ 473 By similarity
Glycosylationi321 – 3211N-linked (GlcNAc...) Reviewed prediction

Keywords - PTMi

Disulfide bond, Glycoprotein, Zymogen

Proteomic databases

PRIDEiP34960.

PTM databases

PhosphoSiteiP34960.

Expressioni

Gene expression databases

ArrayExpressiP34960.
BgeeiP34960.
CleanExiMM_MME.
MM_MMP12.
GenevestigatoriP34960.

Interactioni

Structurei

3D structure databases

ProteinModelPortaliP34960.
SMRiP34960. Positions 40-473.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Repeati289 – 33244Hemopexin 1
Add
BLAST
Repeati333 – 37947Hemopexin 2
Add
BLAST
Repeati381 – 42949Hemopexin 3
Add
BLAST
Repeati430 – 47344Hemopexin 4
Add
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi94 – 1018Cysteine switch By 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.
Contains 4 hemopexin repeats.

Keywords - Domaini

Repeat, Signal

Phylogenomic databases

eggNOGiNOG323958.
GeneTreeiENSGT00750000117336.
HOVERGENiHBG052484.
InParanoidiP34960.
KOiK01413.
OMAiPKLISTH.
PhylomeDBiP34960.
TreeFamiTF315428.

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.
IPR028718. MMP12.
IPR001818. Pept_M10_metallopeptidase.
IPR021190. Pept_M10A.
IPR016293. Pept_M10A_stromelysin-type.
IPR021158. Pept_M10A_Zn_BS.
IPR006026. Peptidase_Metallo.
IPR002477. Peptidoglycan-bd-like.
[Graphical view]
PANTHERiPTHR10201:SF32. PTHR10201:SF32. 1 hit.
PfamiPF00045. 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]

Sequencei

Sequence statusi: Complete.

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

P34960-1 [UniParc]FASTAAdd to Basket

« Hide

MSCTLLKGVC TMKFLMMIVF LQVSACGAAP MNDSEFAEWY LSRFYDYGKD    50
RIPMTKTKTN RNFLKEKLQE MQQFFGLEAT GQLDNSTLAI MHIPRCGVPD 100
VQHLRAVPQR SRWMKRYLTY RIYNYTPDMK REDVDYIFQK AFQVWSDVTP 150
LRFRKLHKDE ADIMILFAFG AHGDFNYFDG KGGTLAHAFY PGPGIQGDAH 200
FDEAETWTKS FQGTNLFLVA VHELGHSLGL QHSNNPKSIM YPTYRYLNPS 250
TFRLSADDIR NIQSLYGAPV KPPSLTKPSS PPSTFCHQSL SFDAVTTVGE 300
KIFFFKDWFF WWKLPGSPAT NITSISSIWP SIPSGIQAAY EIESRNQLFL 350
FKDEKYWLIN NLVPEPHYPR SIYSLGFSAS VKKVDAAVFD PLRQKVYFFV 400
DKHYWRYDVR QELMDPAYPK LISTHFPGIK PKIDAVLYFK RHYYIFQGAY 450
QLEYDPLFRR VTKTLKSTSW FGC 473
Length:473
Mass (Da):54,971
Last modified:July 10, 2007 - v3
Checksum:iD377250610BA249E
GO

Sequence cautioni

The sequence AAA39526.1 differs from that shown. Reason: Erroneous initiation.
The sequence BAC40889.1 differs from that shown. Reason: Erroneous initiation.

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti65 – 651K → E in AAH19135. 1 Publication
Sequence conflicti65 – 651K → E in CAJ18584. 1 Publication
Sequence conflicti78 – 781E → V in BAE30809. 1 Publication
Sequence conflicti78 – 781E → V in BAE30260. 1 Publication
Sequence conflicti78 – 781E → V in BAE30039. 1 Publication
Sequence conflicti78 – 781E → V in BAE29689. 1 Publication
Sequence conflicti80 – 801T → N in BAE33415. 1 Publication
Sequence conflicti87 – 871T → A in BAE42486. 1 Publication
Sequence conflicti172 – 1721H → N in BAE42198. 1 Publication
Sequence conflicti188 – 1881A → V in AAA39526. 1 Publication
Sequence conflicti199 – 1991A → T in BAC40836. 1 Publication
Sequence conflicti241 – 2411Y → D in AAH19135. 1 Publication
Sequence conflicti241 – 2411Y → D in CAJ18584. 1 Publication
Sequence conflicti247 – 2471L → F in BAE33072. 1 Publication
Sequence conflicti250 – 2501S → N in AAH19135. 1 Publication
Sequence conflicti250 – 2501S → N in CAJ18584. 1 Publication
Sequence conflicti268 – 2681A → P in BAC40846. 1 Publication
Sequence conflicti272 – 2721P → T in AAH19135. 1 Publication
Sequence conflicti272 – 2721P → T in CAJ18584. 1 Publication
Sequence conflicti303 – 3031F → L in AAA39526. 1 Publication
Sequence conflicti303 – 3031F → Y in BAC40889. 1 Publication
Sequence conflicti303 – 3031F → Y in BAC40913. 1 Publication
Sequence conflicti319 – 3191A → D in BAE33415. 1 Publication
Sequence conflicti323 – 3231T → I in AAH19135. 1 Publication
Sequence conflicti323 – 3231T → I in CAJ18584. 1 Publication
Sequence conflicti328 – 3281I → T in BAE41743. 1 Publication
Sequence conflicti335 – 3351G → A in AAA39526. 1 Publication
Sequence conflicti403 – 4031H → Q in AAH19135. 1 Publication
Sequence conflicti403 – 4031H → Q in CAJ18584. 1 Publication
Sequence conflicti432 – 4321K → R in BAC40836. 1 Publication
Sequence conflicti467 – 4671S → G in BAE42201. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
M82831 mRNA. Translation: AAA39526.1. Different initiation.
AK089309 mRNA. Translation: BAC40836.1.
AK089335 mRNA. Translation: BAC40846.1.
AK089452 mRNA. Translation: BAC40889.1. Different initiation.
AK089523 mRNA. Translation: BAC40913.1.
AK090051 mRNA. Translation: BAC41067.1.
AK150596 mRNA. Translation: BAE29689.1.
AK151021 mRNA. Translation: BAE30039.1.
AK151273 mRNA. Translation: BAE30260.1.
AK151933 mRNA. Translation: BAE30809.1.
AK155139 mRNA. Translation: BAE33072.1.
AK155743 mRNA. Translation: BAE33411.1.
AK155747 mRNA. Translation: BAE33414.1.
AK155748 mRNA. Translation: BAE33415.1.
AK155865 mRNA. Translation: BAE33469.1.
AK170360 mRNA. Translation: BAE41743.1.
AK170364 mRNA. Translation: BAE41746.1.
AK170798 mRNA. Translation: BAE42035.1.
AK170804 mRNA. Translation: BAE42039.1.
AK170976 mRNA. Translation: BAE42154.1.
AK171006 mRNA. Translation: BAE42177.1.
AK171032 mRNA. Translation: BAE42198.1.
AK171036 mRNA. Translation: BAE42201.1.
AK171176 mRNA. Translation: BAE42294.1.
AK171428 mRNA. Translation: BAE42446.1.
AK171447 mRNA. Translation: BAE42457.1.
AK171448 mRNA. Translation: BAE42458.1.
AK171449 mRNA. Translation: BAE42459.1.
AK171450 mRNA. Translation: BAE42460.1.
AK171466 mRNA. Translation: BAE42472.1.
AK171468 mRNA. Translation: BAE42474.1.
AK171470 mRNA. Translation: BAE42476.1.
AK171472 mRNA. Translation: BAE42478.1.
AK171485 mRNA. Translation: BAE42486.1.
AK171518 mRNA. Translation: BAE42502.1.
AK171542 mRNA. Translation: BAE42516.1.
AK171570 mRNA. Translation: BAE42531.1.
BC019135 mRNA. Translation: AAH19135.2.
CT010377 mRNA. Translation: CAJ18584.1.
CCDSiCCDS22804.1.
PIRiA42401.
RefSeqiNP_032631.3. NM_008605.3.
UniGeneiMm.2055.

Genome annotation databases

EnsembliENSMUST00000005950; ENSMUSP00000005950; ENSMUSG00000049723.
GeneIDi17381.
KEGGimmu:17381.
UCSCiuc009och.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
M82831 mRNA. Translation: AAA39526.1 . Different initiation.
AK089309 mRNA. Translation: BAC40836.1 .
AK089335 mRNA. Translation: BAC40846.1 .
AK089452 mRNA. Translation: BAC40889.1 . Different initiation.
AK089523 mRNA. Translation: BAC40913.1 .
AK090051 mRNA. Translation: BAC41067.1 .
AK150596 mRNA. Translation: BAE29689.1 .
AK151021 mRNA. Translation: BAE30039.1 .
AK151273 mRNA. Translation: BAE30260.1 .
AK151933 mRNA. Translation: BAE30809.1 .
AK155139 mRNA. Translation: BAE33072.1 .
AK155743 mRNA. Translation: BAE33411.1 .
AK155747 mRNA. Translation: BAE33414.1 .
AK155748 mRNA. Translation: BAE33415.1 .
AK155865 mRNA. Translation: BAE33469.1 .
AK170360 mRNA. Translation: BAE41743.1 .
AK170364 mRNA. Translation: BAE41746.1 .
AK170798 mRNA. Translation: BAE42035.1 .
AK170804 mRNA. Translation: BAE42039.1 .
AK170976 mRNA. Translation: BAE42154.1 .
AK171006 mRNA. Translation: BAE42177.1 .
AK171032 mRNA. Translation: BAE42198.1 .
AK171036 mRNA. Translation: BAE42201.1 .
AK171176 mRNA. Translation: BAE42294.1 .
AK171428 mRNA. Translation: BAE42446.1 .
AK171447 mRNA. Translation: BAE42457.1 .
AK171448 mRNA. Translation: BAE42458.1 .
AK171449 mRNA. Translation: BAE42459.1 .
AK171450 mRNA. Translation: BAE42460.1 .
AK171466 mRNA. Translation: BAE42472.1 .
AK171468 mRNA. Translation: BAE42474.1 .
AK171470 mRNA. Translation: BAE42476.1 .
AK171472 mRNA. Translation: BAE42478.1 .
AK171485 mRNA. Translation: BAE42486.1 .
AK171518 mRNA. Translation: BAE42502.1 .
AK171542 mRNA. Translation: BAE42516.1 .
AK171570 mRNA. Translation: BAE42531.1 .
BC019135 mRNA. Translation: AAH19135.2 .
CT010377 mRNA. Translation: CAJ18584.1 .
CCDSi CCDS22804.1.
PIRi A42401.
RefSeqi NP_032631.3. NM_008605.3.
UniGenei Mm.2055.

3D structure databases

ProteinModelPortali P34960.
SMRi P34960. Positions 40-473.
ModBasei Search...
MobiDBi Search...

Chemistry

BindingDBi P34960.
ChEMBLi CHEMBL2594.

Protein family/group databases

MEROPSi M10.009.

PTM databases

PhosphoSitei P34960.

Proteomic databases

PRIDEi P34960.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSMUST00000005950 ; ENSMUSP00000005950 ; ENSMUSG00000049723 .
GeneIDi 17381.
KEGGi mmu:17381.
UCSCi uc009och.1. mouse.

Organism-specific databases

CTDi 4321.
MGIi MGI:97005. Mmp12.

Phylogenomic databases

eggNOGi NOG323958.
GeneTreei ENSGT00750000117336.
HOVERGENi HBG052484.
InParanoidi P34960.
KOi K01413.
OMAi PKLISTH.
PhylomeDBi P34960.
TreeFami TF315428.

Enzyme and pathway databases

Reactomei REACT_199052. Degradation of the extracellular matrix.

Miscellaneous databases

NextBioi 291984.
PROi P34960.
SOURCEi Search...

Gene expression databases

ArrayExpressi P34960.
Bgeei P34960.
CleanExi MM_MME.
MM_MMP12.
Genevestigatori P34960.

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.
IPR028718. MMP12.
IPR001818. Pept_M10_metallopeptidase.
IPR021190. Pept_M10A.
IPR016293. Pept_M10A_stromelysin-type.
IPR021158. Pept_M10A_Zn_BS.
IPR006026. Peptidase_Metallo.
IPR002477. Peptidoglycan-bd-like.
[Graphical view ]
PANTHERi PTHR10201:SF32. PTHR10201:SF32. 1 hit.
Pfami 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. "Molecular cloning, chromosomal localization, and bacterial expression of a murine macrophage metalloelastase."
    Shapiro S.D., Griffin G.L., Gilbert D.J., Jenkins N.A., Copeland N.G., Welgus H.G., Senior R.M., Ley T.J.
    J. Biol. Chem. 267:4664-4671(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 110-136.
    Tissue: Macrophage.
  2. "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: BALB/c, C57BL/6J and NOD.
    Tissue: B-cell, Dendritic cell and Macrophage.
  3. "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].
    Strain: Czech II.
    Tissue: Mammary gland.
  4. "Cloning of mouse full open reading frames in Gateway(R) system entry vector (pDONR201)."
    Ebert L., Muenstermann E., Schatten R., Henze S., Bohn E., Mollenhauer J., Wiemann S., Schick M., Korn B.
    Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 11-473.

Entry informationi

Entry nameiMMP12_MOUSE
AccessioniPrimary (citable) accession number: P34960
Secondary accession number(s): Q3TB28
, Q3TBV6, Q3TBV9, Q3TD61, Q3U1S8, Q3U1S9, Q3U2R8, Q3UBC5, Q4FJM7, Q8BJ92, Q8BJB3, Q8BJB6, Q8BJB8, Q8BJB9, Q8VED6
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 1994
Last sequence update: July 10, 2007
Last modified: September 3, 2014
This is version 141 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Direct protein sequencing, 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

Similar proteinsi