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Q16819

- MEP1A_HUMAN

UniProt

Q16819 - MEP1A_HUMAN

Protein

Meprin A subunit alpha

Gene

MEP1A

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 144 (01 Oct 2014)
      Sequence version 2 (22 Jul 2008)
      Previous versions | rss
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    Functioni

    Catalytic activityi

    Hydrolysis of protein and peptide substrates preferentially on carboxyl side of hydrophobic residues.

    Cofactori

    Binds 1 zinc ion per subunit.By similarity

    Enzyme regulationi

    Inhibited by several hydroxamate compounds, the most potent inhibitor is actinonin.1 Publication

    Kineticsi

    1. KM=110 µM for GRP1 Publication
    2. KM=18.0 µM for PTH 12-341 Publication
    3. KM=33.9 µM for secretin1 Publication
    4. KM=41.3 µM for substance P1 Publication
    5. KM=56.5 µM for LHRH1 Publication
    6. KM=73.2 µM for orcokinin1 Publication
    7. KM=292 µM for alpha-MSH1 Publication
    8. KM=125 µM for bradykinin1 Publication
    9. KM=200 µM for gastrin1 Publication

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Metal bindingi58 – 581Zinc; catalyticPROSITE-ProRule annotation
    Metal bindingi155 – 1551Zinc; via tele nitrogen; catalyticBy similarity
    Active sitei156 – 1561PROSITE-ProRule annotation
    Metal bindingi159 – 1591Zinc; via tele nitrogen; catalyticBy similarity
    Metal bindingi165 – 1651Zinc; via tele nitrogen; catalyticBy similarity

    GO - Molecular functioni

    1. metalloendopeptidase activity Source: ProtInc
    2. protein binding Source: IntAct
    3. zinc ion binding Source: InterPro

    GO - Biological processi

    1. digestion Source: ProtInc

    Keywords - Molecular functioni

    Hydrolase, Metalloprotease, Protease

    Keywords - Ligandi

    Metal-binding, Zinc

    Enzyme and pathway databases

    SignaLinkiQ16819.

    Protein family/group databases

    MEROPSiM12.002.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Meprin A subunit alpha (EC:3.4.24.18)
    Alternative name(s):
    Endopeptidase-2
    N-benzoyl-L-tyrosyl-P-amino-benzoic acid hydrolase subunit alpha
    PABA peptide hydrolase
    PPH alpha
    Gene namesi
    Name:MEP1A
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 6

    Organism-specific databases

    HGNCiHGNC:7015. MEP1A.

    Subcellular locationi

    GO - Cellular componenti

    1. extracellular space Source: ProtInc
    2. extracellular vesicular exosome Source: UniProt
    3. integral component of plasma membrane Source: ProtInc
    4. meprin A complex Source: Ensembl

    Keywords - Cellular componenti

    Membrane

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA30749.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 2121By similarityAdd
    BLAST
    Propeptidei22 – 6544By similarityPRO_0000028877Add
    BLAST
    Chaini66 – 746681Meprin A subunit alphaPRO_0000028878Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Disulfide bondi107 ↔ 259PROSITE-ProRule annotation
    Disulfide bondi128 ↔ 147PROSITE-ProRule annotation
    Glycosylationi140 – 1401N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi222 – 2221N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi258 – 2581N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi269 ↔ 431PROSITE-ProRule annotation
    Disulfide bondi277 – 277InterchainPROSITE-ProRule annotation
    Disulfide bondi308 – 308InterchainPROSITE-ProRule annotation
    Glycosylationi414 – 4141N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi440 – 4401N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi447 – 4471N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi539 – 5391N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi674 ↔ 685PROSITE-ProRule annotation
    Disulfide bondi679 ↔ 694PROSITE-ProRule annotation
    Disulfide bondi696 ↔ 709PROSITE-ProRule annotation

    Post-translational modificationi

    N-glycosylated; contains GlcNAc, galactose, mannose and a small amount of fucose.By similarity

    Keywords - PTMi

    Disulfide bond, Glycoprotein, Zymogen

    Proteomic databases

    PaxDbiQ16819.
    PRIDEiQ16819.

    PTM databases

    PhosphoSiteiQ16819.

    Expressioni

    Gene expression databases

    BgeeiQ16819.
    CleanExiHS_MEP1A.
    GenevestigatoriQ16819.

    Organism-specific databases

    HPAiHPA029416.

    Interactioni

    Subunit structurei

    Homotetramer consisting of disulfide-linked alpha subunits, homooligomer consisting of disulfide-linked alpha subunit homodimers, or heterotetramer of two alpha and two beta subunits formed by non-covalent association of two disulfide-linked heterodimers By similarity. Interacts with MBL2 through its carbohydrate moiety. This interaction may inhibit its catalytic activity By similarity.By similarity

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    MMP9P147802EBI-8153734,EBI-1382326

    Protein-protein interaction databases

    BioGridi110387. 11 interactions.
    IntActiQ16819. 1 interaction.
    STRINGi9606.ENSP00000230588.

    Structurei

    3D structure databases

    ProteinModelPortaliQ16819.
    SMRiQ16819. Positions 62-259, 435-589.
    ModBaseiSearch...
    MobiDBiSearch...

    Topological domain

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Topological domaini66 – 712647ExtracellularSequence AnalysisAdd
    BLAST
    Topological domaini741 – 7466CytoplasmicSequence Analysis

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei713 – 74028HelicalSequence AnalysisAdd
    BLAST

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini264 – 433170MAMPROSITE-ProRule annotationAdd
    BLAST
    Domaini434 – 593160MATHPROSITE-ProRule annotationAdd
    BLAST
    Domaini670 – 71041EGF-likePROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni66 – 263198MetalloproteaseAdd
    BLAST

    Sequence similaritiesi

    Belongs to the peptidase M12A family.Curated
    Contains 1 EGF-like domain.PROSITE-ProRule annotation
    Contains 1 MAM domain.PROSITE-ProRule annotation
    Contains 1 MATH domain.PROSITE-ProRule annotation

    Keywords - Domaini

    EGF-like domain, Signal, Transmembrane, Transmembrane helix

    Phylogenomic databases

    eggNOGiNOG322115.
    HOVERGENiHBG052457.
    InParanoidiQ16819.
    KOiK01395.
    OMAiMIQGTRD.
    OrthoDBiEOG73V6MT.
    PhylomeDBiQ16819.
    TreeFamiTF315280.

    Family and domain databases

    Gene3Di3.40.390.10. 1 hit.
    InterProiIPR008985. ConA-like_lec_gl_sf.
    IPR000742. EG-like_dom.
    IPR000998. MAM_dom.
    IPR002083. MATH.
    IPR008294. Meprin.
    IPR024079. MetalloPept_cat_dom.
    IPR001506. Peptidase_M12A.
    IPR006026. Peptidase_Metallo.
    IPR008974. TRAF-like.
    [Graphical view]
    PfamiPF01400. Astacin. 1 hit.
    PF00008. EGF. 1 hit.
    PF00629. MAM. 1 hit.
    PF00917. MATH. 1 hit.
    [Graphical view]
    PIRSFiPIRSF001196. Meprin. 1 hit.
    PRINTSiPR00480. ASTACIN.
    PR00020. MAMDOMAIN.
    SMARTiSM00181. EGF. 1 hit.
    SM00137. MAM. 1 hit.
    SM00061. MATH. 1 hit.
    SM00235. ZnMc. 1 hit.
    [Graphical view]
    SUPFAMiSSF49599. SSF49599. 1 hit.
    SSF49899. SSF49899. 1 hit.
    PROSITEiPS50026. EGF_3. 1 hit.
    PS00740. MAM_1. 1 hit.
    PS50060. MAM_2. 1 hit.
    PS50144. MATH. 1 hit.
    PS00142. ZINC_PROTEASE. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

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

    Q16819-1 [UniParc]FASTAAdd to Basket

    « Hide

    MAWIRSTCIL FFTLLFAHIA AVPIKYLPEE NVHDADFGEQ KDISEINLAA    50
    GLDLFQGDIL LQKSRNGLRD PNTRWTFPIP YILADNLGLN AKGAILYAFE 100
    MFRLKSCVDF KPYEGESSYI IFQQFDGCWS EVGDQHVGQN ISIGQGCAYK 150
    AIIEHEILHA LGFYHEQSRT DRDDYVNIWW DQILSGYQHN FDTYDDSLIT 200
    DLNTPYDYES LMHYQPFSFN KNASVPTITA KIPEFNSIIG QRLDFSAIDL 250
    ERLNRMYNCT TTHTLLDHCT FEKANICGMI QGTRDDTDWA HQDSAQAGEV 300
    DHTLLGQCTG AGYFMQFSTS SGSAEEAALL ESRILYPKRK QQCLQFFYKM 350
    TGSPSDRLVV WVRRDDSTGN VRKLVKVQTF QGDDDHNWKI AHVVLKEEQK 400
    FRYLFQGTKG DPQNSTGGIY LDDITLTETP CPTGVWTVRN FSQVLENTSK 450
    GDKLQSPRFY NSEGYGFGVT LYPNSRESSG YLRLAFHVCS GENDAILEWP 500
    VENRQVIITI LDQEPDVRNR MSSSMVFTTS KSHTSPAIND TVIWDRPSRV 550
    GTYHTDCNCF RSIDLGWSGF ISHQMLKRRS FLKNDDLIIF VDFEDITHLS 600
    QTEVPTKGKR LSPQGLILQG QEQQVSEEGS GKAMLEEALP VSLSQGQPSR 650
    QKRSVENTGP LEDHNWPQYF RDPCDPNPCQ NDGICVNVKG MASCRCISGH 700
    AFFYTGERCQ AVQVHGSVLG MVIGGTAGVI FLTFSIIAIL SQRPRK 746
    Length:746
    Mass (Da):84,419
    Last modified:July 22, 2008 - v2
    Checksum:iB5F0812F2850F958
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti26 – 261Y → H in AAA21338. 1 PublicationCurated
    Sequence conflicti162 – 1621G → V in AAL85339. 1 PublicationCurated
    Sequence conflicti306 – 3061G → E in BAF98731. (PubMed:14702039)Curated
    Sequence conflicti426 – 4261L → P in BAF98731. (PubMed:14702039)Curated
    Sequence conflicti518 – 5181R → Q in BAG37669. (PubMed:14702039)Curated
    Sequence conflicti546 – 5461R → S in BAF98731. (PubMed:14702039)Curated
    Sequence conflicti638 – 6381A → V in BAF98731. (PubMed:14702039)Curated
    Sequence conflicti711 – 7133AVQ → SAE in AAA21338. 1 PublicationCurated
    Sequence conflicti711 – 7133AVQ → SAE no nucleotide entry (PubMed:8262185)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti469 – 4691V → L.2 Publications
    Corresponds to variant rs2274658 [ dbSNP | Ensembl ].
    VAR_020056
    Natural varianti476 – 4761R → G.1 Publication
    Corresponds to variant rs12197930 [ dbSNP | Ensembl ].
    VAR_033492
    Natural varianti606 – 6061T → S.2 Publications
    Corresponds to variant rs2297020 [ dbSNP | Ensembl ].
    VAR_051583
    Natural varianti634 – 6341M → V.
    Corresponds to variant rs2297019 [ dbSNP | Ensembl ].
    VAR_021846
    Natural varianti726 – 7261T → M.1 Publication
    Corresponds to variant rs1804211 [ dbSNP | Ensembl ].
    VAR_033493

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M82962 mRNA. Translation: AAA21338.1.
    AF478685 mRNA. Translation: AAL85339.1.
    AK290282 mRNA. Translation: BAF82971.1.
    AK315246 mRNA. Translation: BAG37669.1.
    AK315840 mRNA. Translation: BAF98731.1.
    AL161618 Genomic DNA. Translation: CAC21508.1.
    CH471081 Genomic DNA. Translation: EAX04306.1.
    BC131714 mRNA. Translation: AAI31715.1.
    CCDSiCCDS4918.1.
    PIRiS60193. HYHUMA.
    RefSeqiNP_005579.2. NM_005588.2.
    UniGeneiHs.179704.

    Genome annotation databases

    EnsembliENST00000230588; ENSP00000230588; ENSG00000112818.
    GeneIDi4224.
    KEGGihsa:4224.
    UCSCiuc010jzh.1. human.

    Polymorphism databases

    DMDMi205830902.

    Keywords - Coding sequence diversityi

    Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M82962 mRNA. Translation: AAA21338.1 .
    AF478685 mRNA. Translation: AAL85339.1 .
    AK290282 mRNA. Translation: BAF82971.1 .
    AK315246 mRNA. Translation: BAG37669.1 .
    AK315840 mRNA. Translation: BAF98731.1 .
    AL161618 Genomic DNA. Translation: CAC21508.1 .
    CH471081 Genomic DNA. Translation: EAX04306.1 .
    BC131714 mRNA. Translation: AAI31715.1 .
    CCDSi CCDS4918.1.
    PIRi S60193. HYHUMA.
    RefSeqi NP_005579.2. NM_005588.2.
    UniGenei Hs.179704.

    3D structure databases

    ProteinModelPortali Q16819.
    SMRi Q16819. Positions 62-259, 435-589.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 110387. 11 interactions.
    IntActi Q16819. 1 interaction.
    STRINGi 9606.ENSP00000230588.

    Protein family/group databases

    MEROPSi M12.002.

    PTM databases

    PhosphoSitei Q16819.

    Polymorphism databases

    DMDMi 205830902.

    Proteomic databases

    PaxDbi Q16819.
    PRIDEi Q16819.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000230588 ; ENSP00000230588 ; ENSG00000112818 .
    GeneIDi 4224.
    KEGGi hsa:4224.
    UCSCi uc010jzh.1. human.

    Organism-specific databases

    CTDi 4224.
    GeneCardsi GC06P046807.
    H-InvDB HIX0032798.
    HGNCi HGNC:7015. MEP1A.
    HPAi HPA029416.
    MIMi 600388. gene.
    neXtProti NX_Q16819.
    PharmGKBi PA30749.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG322115.
    HOVERGENi HBG052457.
    InParanoidi Q16819.
    KOi K01395.
    OMAi MIQGTRD.
    OrthoDBi EOG73V6MT.
    PhylomeDBi Q16819.
    TreeFami TF315280.

    Enzyme and pathway databases

    SignaLinki Q16819.

    Miscellaneous databases

    GeneWikii MEP1A.
    GenomeRNAii 4224.
    NextBioi 16671.
    PROi Q16819.
    SOURCEi Search...

    Gene expression databases

    Bgeei Q16819.
    CleanExi HS_MEP1A.
    Genevestigatori Q16819.

    Family and domain databases

    Gene3Di 3.40.390.10. 1 hit.
    InterProi IPR008985. ConA-like_lec_gl_sf.
    IPR000742. EG-like_dom.
    IPR000998. MAM_dom.
    IPR002083. MATH.
    IPR008294. Meprin.
    IPR024079. MetalloPept_cat_dom.
    IPR001506. Peptidase_M12A.
    IPR006026. Peptidase_Metallo.
    IPR008974. TRAF-like.
    [Graphical view ]
    Pfami PF01400. Astacin. 1 hit.
    PF00008. EGF. 1 hit.
    PF00629. MAM. 1 hit.
    PF00917. MATH. 1 hit.
    [Graphical view ]
    PIRSFi PIRSF001196. Meprin. 1 hit.
    PRINTSi PR00480. ASTACIN.
    PR00020. MAMDOMAIN.
    SMARTi SM00181. EGF. 1 hit.
    SM00137. MAM. 1 hit.
    SM00061. MATH. 1 hit.
    SM00235. ZnMc. 1 hit.
    [Graphical view ]
    SUPFAMi SSF49599. SSF49599. 1 hit.
    SSF49899. SSF49899. 1 hit.
    PROSITEi PS50026. EGF_3. 1 hit.
    PS00740. MAM_1. 1 hit.
    PS50060. MAM_2. 1 hit.
    PS50144. MATH. 1 hit.
    PS00142. ZINC_PROTEASE. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. Sterchi E.E.
      Submitted (AUG-1994) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], VARIANT SER-606.
      Tissue: Jejunum.
    2. "Expression of human meprin alpha."
      Haun R.S.
      Submitted (JAN-2002) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Tissue: Small intestine.
    3. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
      Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
      , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
      Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], VARIANTS LEU-469 AND MET-726.
      Tissue: Colon and Small intestine.
    4. "The DNA sequence and analysis of human chromosome 6."
      Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L., Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., Gilbert J.G.R., Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D., Andrews T.D.
      , Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H., Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J., Brown J.Y., Burford D.C., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V., Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J., Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., Ellington A.E., Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J., French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J., Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C., Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A., Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R., Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M., Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A., Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L., Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I., Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y., Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E., Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A., Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W., Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M., West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J., Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M., Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I., Rogers J., Beck S.
      Nature 425:805-811(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    5. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    6. "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], VARIANTS LEU-469 AND GLY-476.
    7. "Cloning of the PABA peptide hydrolase alpha subunit (PPH alpha) from human small intestine and its expression in COS-1 cells."
      Dumermuth E., Eldering J.A., Gruenberg J., Jiang W., Sterchi E.E.
      FEBS Lett. 335:367-375(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 32-746, VARIANT SER-606.
      Tissue: Jejunum.
    8. "Human and mouse homo-oligomeric meprin A metalloendopeptidase: substrate and inhibitor specificities."
      Bylander J.E., Bertenshaw G.P., Matters G.L., Hubbard S.J., Bond J.S.
      Biol. Chem. 388:1163-1172(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: ENZYME REGULATION, BIOPHYSICOCHEMICAL PROPERTIES.

    Entry informationi

    Entry nameiMEP1A_HUMAN
    AccessioniPrimary (citable) accession number: Q16819
    Secondary accession number(s): A2RRM4
    , B0AZP9, B2RCS2, Q8TDC9, Q9H1R1
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 1, 1997
    Last sequence update: July 22, 2008
    Last modified: October 1, 2014
    This is version 144 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

    Complete proteome, Reference proteome

    Documents

    1. Human chromosome 6
      Human chromosome 6: 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. Peptidase families
      Classification of peptidase families and list of entries
    6. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3