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Q16820

- MEP1B_HUMAN

UniProt

Q16820 - MEP1B_HUMAN

Protein

Meprin A subunit beta

Gene

MEP1B

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 139 (01 Oct 2014)
      Sequence version 3 (18 May 2010)
      Previous versions | rss
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    Functioni

    Membrane metallopeptidase that sheds many membrane-bound proteins. Known substrates include: FGF19, VGFA, IL1B, IL18, procollagen I and III, E-cadherin, KLK7, gastrin, ADAM10, tenascin-C. The presence of several pro-inflammatory cytokine among substrates implicate MEP1B in inflammation. It is also involved in tissue remodeling due to its capability to degrade extracellular matrix components.1 Publication

    Catalytic activityi

    Hydrolysis of proteins, including azocasein, and peptides. Hydrolysis of 5-His-|-Leu-6, 6-Leu-|-Cys-7, 14-Ala-|-Leu-15 and 19-Cys-|-Gly-20 bonds in insulin B chain. Exhibits a strong preference for acidic amino acids at the P1' position.1 Publication

    Cofactori

    Binds 1 zinc ion per subunit.1 Publication

    Enzyme regulationi

    Strongly inhibited by fetuin-A/AHSG.2 Publications

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Metal bindingi52 – 521Zinc; catalytic
    Metal bindingi152 – 1521Zinc; via tele nitrogen; catalytic
    Active sitei153 – 1531PROSITE-ProRule annotation
    Metal bindingi156 – 1561Zinc; via tele nitrogen; catalytic
    Metal bindingi162 – 1621Zinc; via tele nitrogen; catalytic
    Sitei238 – 2381Mediates preference for acidic residues at subsite P1'

    GO - Molecular functioni

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

    GO - Biological processi

    1. digestion Source: ProtInc
    2. inflammatory response Source: UniProtKB-KW

    Keywords - Molecular functioni

    Hydrolase, Metalloprotease, Protease

    Keywords - Biological processi

    Inflammatory response

    Keywords - Ligandi

    Metal-binding, Zinc

    Enzyme and pathway databases

    SignaLinkiQ16820.

    Protein family/group databases

    MEROPSiM12.004.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Meprin A subunit beta (EC:3.4.24.63)
    Alternative name(s):
    Endopeptidase-2
    Meprin B
    N-benzoyl-L-tyrosyl-P-amino-benzoic acid hydrolase subunit beta
    PABA peptide hydrolase
    PPH beta
    Gene namesi
    Name:MEP1B
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 18

    Organism-specific databases

    HGNCiHGNC:7020. MEP1B.

    Subcellular locationi

    Cell membrane; Single-pass type I membrane protein. Secreted
    Note: Homodimers are essentially membrane bound but may also be shed from the surface by ADAM-10 and ADAM-17.

    GO - Cellular componenti

    1. extracellular space Source: ProtInc
    2. integral component of plasma membrane Source: ProtInc
    3. plasma membrane Source: ProtInc

    Keywords - Cellular componenti

    Cell membrane, Membrane, Secreted

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi248 – 2481K → Y: Decreased activity toward gastrin. 2 Publications
    Mutagenesisi595 – 60713Missing: Abolishes secretion. 1 PublicationAdd
    BLAST

    Organism-specific databases

    PharmGKBiPA30754.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 2222Sequence AnalysisAdd
    BLAST
    Propeptidei23 – 61392 PublicationsPRO_0000028883Add
    BLAST
    Chaini62 – 701640Meprin A subunit betaPRO_0000028884Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Disulfide bondi103 ↔ 2551 PublicationPROSITE-ProRule annotation
    Disulfide bondi124 ↔ 1441 PublicationPROSITE-ProRule annotation
    Glycosylationi218 – 2181N-linked (GlcNAc...)1 Publication
    Glycosylationi254 – 2541N-linked (GlcNAc...)1 Publication
    Disulfide bondi265 ↔ 4271 PublicationPROSITE-ProRule annotation
    Disulfide bondi273 – 273InterchainPROSITE-ProRule annotation
    Disulfide bondi305 – 305Interchain1 PublicationPROSITE-ProRule annotation
    Glycosylationi370 – 3701N-linked (GlcNAc...)1 Publication
    Glycosylationi421 – 4211N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi436 – 4361N-linked (GlcNAc...)1 Publication
    Glycosylationi445 – 4451N-linked (GlcNAc...)1 Publication
    Disulfide bondi492 – 492InterchainPROSITE-ProRule annotation
    Glycosylationi547 – 5471N-linked (GlcNAc...)1 Publication
    Glycosylationi592 – 5921N-linked (GlcNAc...)1 Publication
    Glycosylationi593 – 5931O-linked (GalNAc...)Sequence Analysis
    Glycosylationi594 – 5941O-linked (GalNAc...)Sequence Analysis
    Glycosylationi599 – 5991O-linked (GalNAc...)Sequence Analysis
    Glycosylationi603 – 6031O-linked (GalNAc...)Sequence Analysis
    Disulfide bondi608 ↔ 619PROSITE-ProRule annotation
    Disulfide bondi613 ↔ 628PROSITE-ProRule annotation
    Disulfide bondi630 ↔ 643PROSITE-ProRule annotation

    Post-translational modificationi

    N-glycosylated; contains high mannose and/or complex biantennary structures.
    O-glycosylation protect the C-terminal region from proteolytic cleavage and diminish secretion, this seems to be specific to human.7 Publications
    Proteolytically activated by trypsin in the intestinal lumen and kallikrein-related peptidases in other tissues.

    Keywords - PTMi

    Disulfide bond, Glycoprotein, Zymogen

    Proteomic databases

    PaxDbiQ16820.
    PRIDEiQ16820.

    PTM databases

    PhosphoSiteiQ16820.

    Expressioni

    Tissue specificityi

    The major site of expression is the brush border membrane of small intestinal and kidney epithelial cells.1 Publication

    Gene expression databases

    BgeeiQ16820.
    CleanExiHS_MEP1B.
    GenevestigatoriQ16820.

    Organism-specific databases

    HPAiCAB025850.

    Interactioni

    Subunit structurei

    Homotetramer consisting of disulfide-linked beta subunits, 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-968418,EBI-1382326

    Protein-protein interaction databases

    BioGridi110388. 4 interactions.
    DIPiDIP-34900N.
    IntActiQ16820. 1 interaction.
    STRINGi9606.ENSP00000269202.

    Structurei

    Secondary structure

    1
    701
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Turni29 – 324
    Helixi37 – 437
    Turni50 – 523
    Beta strandi63 – 653
    Helixi67 – 693
    Beta strandi73 – 797
    Helixi85 – 10117
    Beta strandi105 – 1084
    Beta strandi113 – 1197
    Beta strandi122 – 1265
    Beta strandi133 – 1408
    Helixi147 – 15812
    Helixi163 – 1653
    Helixi169 – 1713
    Beta strandi173 – 1753
    Helixi177 – 1793
    Helixi185 – 1884
    Turni193 – 1953
    Turni213 – 2164
    Beta strandi217 – 2215
    Beta strandi223 – 2286
    Helixi229 – 2313
    Turni232 – 2365
    Helixi243 – 25210
    Beta strandi259 – 2657
    Helixi272 – 2743
    Beta strandi276 – 2783
    Beta strandi280 – 2823
    Beta strandi285 – 2895
    Beta strandi292 – 2943
    Beta strandi299 – 3046
    Beta strandi311 – 3155
    Beta strandi317 – 3193
    Beta strandi324 – 3285
    Beta strandi335 – 3373
    Beta strandi339 – 3479
    Beta strandi354 – 36310
    Beta strandi366 – 37914
    Beta strandi382 – 3843
    Beta strandi386 – 3927
    Beta strandi398 – 4058
    Beta strandi412 – 42514
    Beta strandi429 – 4346
    Helixi438 – 4403
    Beta strandi447 – 4493
    Beta strandi460 – 4667
    Beta strandi469 – 48012
    Helixi485 – 4873
    Beta strandi494 – 5018
    Helixi508 – 5103
    Beta strandi514 – 5196
    Beta strandi527 – 5315
    Helixi536 – 5394
    Beta strandi541 – 5444
    Beta strandi550 – 56415
    Helixi565 – 5684
    Beta strandi573 – 5753
    Beta strandi578 – 58710
    Helixi589 – 5913

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    4GWMX-ray1.85A/B23-614[»]
    4GWNX-ray3.00A62-614[»]
    ProteinModelPortaliQ16820.
    SMRiQ16820. Positions 25-597.
    ModBaseiSearch...
    MobiDBiSearch...

    Topological domain

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Topological domaini23 – 652630ExtracellularSequence AnalysisAdd
    BLAST
    Topological domaini674 – 70128CytoplasmicSequence AnalysisAdd
    BLAST

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei653 – 67321HelicalSequence AnalysisAdd
    BLAST

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini260 – 429170MAMPROSITE-ProRule annotationAdd
    BLAST
    Domaini430 – 585156MATHPROSITE-ProRule annotationAdd
    BLAST
    Domaini604 – 64441EGF-likePROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni64 – 259196MetalloproteaseAdd
    BLAST
    Regioni595 – 60713Required for proteolytic processingAdd
    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.
    HOGENOMiHOG000043106.
    HOVERGENiHBG052457.
    InParanoidiQ16820.
    KOiK08606.
    OMAiDYVSIIW.
    OrthoDBiEOG73V6MT.
    PhylomeDBiQ16820.
    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.
    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.

    Q16820-1 [UniParc]FASTAAdd to Basket

    « Hide

    MDLWNLSWFL FLDALLVISG LATPENFDVD GGMDQDIFDI NEGLGLDLFE    50
    GDIRLDRAQI RNSIIGEKYR WPHTIPYVLE DSLEMNAKGV ILNAFERYRL 100
    KTCIDFKPWA GETNYISVFK GSGCWSSVGN RRVGKQELSI GANCDRIATV 150
    QHEFLHALGF WHEQSRSDRD DYVRIMWDRI LSGREHNFNT YSDDISDSLN 200
    VPYDYTSVMH YSKTAFQNGT EPTIVTRISD FEDVIGQRMD FSDSDLLKLN 250
    QLYNCSSSLS FMDSCSFELE NVCGMIQSSG DNADWQRVSQ VPRGPESDHS 300
    NMGQCQGSGF FMHFDSSSVN VGATAVLESR TLYPKRGFQC LQFYLYNSGS 350
    ESDQLNIYIR EYSADNVDGN LTLVEEIKEI PTGSWQLYHV TLKVTKKFRV 400
    VFEGRKGSGA SLGGLSIDDI NLSETRCPHH IWHIRNFTQF IGSPNGTLYS 450
    PPFYSSKGYA FQIYLNLAHV TNAGIYFHLI SGANDDQLQW PCPWQQATMT 500
    LLDQNPDIRQ RMSNQRSITT DPFMTTDNGN YFWDRPSKVG TVALFSNGTQ 550
    FRRGGGYGTS AFITHERLKS RDFIKGDDVY ILLTVEDISH LNSTQIQLTP 600
    APSVQDLCSK TTCKNDGVCT VRDGKAECRC QSGEDWWYMG ERCEKRGSTR 650
    DTIVIAVSST VAVFALMLII TLVSVYCTRK KYRERMSSNR PNLTPQNQHA 700
    F 701
    Length:701
    Mass (Da):79,571
    Last modified:May 18, 2010 - v3
    Checksum:i4733DBF018A4F3CD
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti71 – 711W → S AA sequence (PubMed:8262185)Curated
    Sequence conflicti74 – 741T → P AA sequence (PubMed:8262185)Curated
    Sequence conflicti546 – 5461S → P in AAU05377. 1 PublicationCurated
    Sequence conflicti546 – 5461S → P in AAI36560. (PubMed:15489334)Curated
    Sequence conflicti546 – 5461S → P in AAI44245. (PubMed:15489334)Curated
    Sequence conflicti698 – 6981Missing in CAA57107. (PubMed:9288916)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti324 – 3241T → A.1 Publication
    VAR_069387
    Natural varianti326 – 3261V → M.
    Corresponds to variant rs9959396 [ dbSNP | Ensembl ].
    VAR_057064
    Natural varianti695 – 6951P → L.2 Publications
    Corresponds to variant rs616114 [ dbSNP | Ensembl ].
    VAR_057065

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X81333 mRNA. Translation: CAA57107.1.
    AY695931 mRNA. Translation: AAU05377.1.
    BC136559 mRNA. Translation: AAI36560.1.
    BC144244 mRNA. Translation: AAI44245.1.
    CCDSiCCDS45846.1.
    PIRiS49383. HYHUMB.
    RefSeqiNP_005916.2. NM_005925.2.
    UniGeneiHs.194777.

    Genome annotation databases

    EnsembliENST00000269202; ENSP00000269202; ENSG00000141434.
    GeneIDi4225.
    KEGGihsa:4225.
    UCSCiuc002kxj.4. human.

    Polymorphism databases

    DMDMi296439304.

    Keywords - Coding sequence diversityi

    Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X81333 mRNA. Translation: CAA57107.1 .
    AY695931 mRNA. Translation: AAU05377.1 .
    BC136559 mRNA. Translation: AAI36560.1 .
    BC144244 mRNA. Translation: AAI44245.1 .
    CCDSi CCDS45846.1.
    PIRi S49383. HYHUMB.
    RefSeqi NP_005916.2. NM_005925.2.
    UniGenei Hs.194777.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    4GWM X-ray 1.85 A/B 23-614 [» ]
    4GWN X-ray 3.00 A 62-614 [» ]
    ProteinModelPortali Q16820.
    SMRi Q16820. Positions 25-597.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 110388. 4 interactions.
    DIPi DIP-34900N.
    IntActi Q16820. 1 interaction.
    STRINGi 9606.ENSP00000269202.

    Protein family/group databases

    MEROPSi M12.004.

    PTM databases

    PhosphoSitei Q16820.

    Polymorphism databases

    DMDMi 296439304.

    Proteomic databases

    PaxDbi Q16820.
    PRIDEi Q16820.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000269202 ; ENSP00000269202 ; ENSG00000141434 .
    GeneIDi 4225.
    KEGGi hsa:4225.
    UCSCi uc002kxj.4. human.

    Organism-specific databases

    CTDi 4225.
    GeneCardsi GC18P029793.
    H-InvDB HIX0039722.
    HGNCi HGNC:7020. MEP1B.
    HPAi CAB025850.
    MIMi 600389. gene.
    neXtProti NX_Q16820.
    PharmGKBi PA30754.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG322115.
    HOGENOMi HOG000043106.
    HOVERGENi HBG052457.
    InParanoidi Q16820.
    KOi K08606.
    OMAi DYVSIIW.
    OrthoDBi EOG73V6MT.
    PhylomeDBi Q16820.
    TreeFami TF315280.

    Enzyme and pathway databases

    SignaLinki Q16820.

    Miscellaneous databases

    GeneWikii MEP1B.
    GenomeRNAii 4225.
    NextBioi 16675.
    PROi Q16820.
    SOURCEi Search...

    Gene expression databases

    Bgeei Q16820.
    CleanExi HS_MEP1B.
    Genevestigatori Q16820.

    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.
    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. "Polarised expression of human intestinal N-benzoyl-L-tyrosyl-p-aminobenzoic acid hydrolase (human meprin) alpha and beta subunits in Madin-Darby canine kidney cells."
      Eldering J.A., Gruenberg J., Hahn D., Croes H.J., Fransen J.A., Sterchi E.E.
      Eur. J. Biochem. 247:920-932(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 62-105, VARIANT LEU-695.
      Tissue: Intestine.
    2. "Expression of human meprin beta."
      Haun R.S.
      Submitted (JUL-2004) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Tissue: Small intestine.
    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], VARIANT LEU-695.
      Tissue: Testis.
    4. "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: PROTEIN SEQUENCE OF 62-79.
      Tissue: Small intestine mucosa.
    5. "N-Benzoyl-L-tyrosyl-p-aminobenzoic acid hydrolase beta (human meprinbeta). A 13-amino-acid sequence is required for proteolytic processing and subsequent secretion."
      Pischitzis A., Hahn D., Leuenberger B., Sterchi E.E.
      Eur. J. Biochem. 261:421-429(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBCELLULAR LOCATION, PROTEOLYTIC PROCESSING.
    6. "Human meprin beta: O-linked glycans in the intervening region of the type I membrane protein protect the C-terminal region from proteolytic cleavage and diminish its secretion."
      Leuenberger B., Hahn D., Pischitzis A., Hansen M.K., Sterchi E.E.
      Biochem. J. 369:659-665(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: GLYCOSYLATION AT SER-593; THR-594; THR-599 AND SER-603, TISSUE SPECIFICITY, MUTAGENESIS OF 595-GLN--LEU-607.
    7. "Critical amino acids in the active site of meprin metalloproteinases for substrate and peptide bond specificity."
      Villa J.P., Bertenshaw G.P., Bond J.S.
      J. Biol. Chem. 278:42545-42550(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: CLEAVAGE OF GASTRIN, SUBSTRATE SPECIFICITY, MUTAGENESIS OF LYS-248.
    8. "Prointerleukin-18 is activated by meprin beta in vitro and in vivo in intestinal inflammation."
      Banerjee S., Bond J.S.
      J. Biol. Chem. 283:31371-31377(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: CLEAVAGE OF IL18.
    9. "The metalloprotease meprinbeta processes E-cadherin and weakens intercellular adhesion."
      Huguenin M., Muller E.J., Trachsel-Rosmann S., Oneda B., Ambort D., Sterchi E.E., Lottaz D.
      PLoS ONE 3:E2153-E2153(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: CLEAVAGE OF E-CADHERIN.
    10. "Fetuin-A and cystatin C are endogenous inhibitors of human meprin metalloproteases."
      Hedrich J., Lottaz D., Meyer K., Yiallouros I., Jahnen-Dechent W., Stocker W., Becker-Pauly C.
      Biochemistry 49:8599-8607(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: ENZYME REGULATION.
    11. "Specific processing of tenascin-C by the metalloprotease meprinbeta neutralizes its inhibition of cell spreading."
      Ambort D., Brellier F., Becker-Pauly C., Stocker W., Andrejevic-Blant S., Chiquet M., Sterchi E.E.
      Matrix Biol. 29:31-42(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: CLEAVAGE OF TNC.
    12. "Proteomic analyses reveal an acidic prime side specificity for the astacin metalloprotease family reflected by physiological substrates."
      Becker-Pauly C., Barre O., Schilling O., Auf dem Keller U., Ohler A., Broder C., Schutte A., Kappelhoff R., Stocker W., Overall C.M.
      Mol. Cell. Proteomics 10:M111.009233.01-M111.009233.19(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, CATALYTIC ACTIVITY, SUBSTRATE SPECIFICITY, CLEAVAGE OF FGF19; KLK7 AND VGFA.
    13. Cited for: CLEAVAGE OF ADAM10, ENZYME REGULATION.
    14. "Structural basis for the sheddase function of human meprin beta metalloproteinase at the plasma membrane."
      Arolas J.L., Broder C., Jefferson T., Guevara T., Sterchi E.E., Bode W., Stocker W., Becker-Pauly C., Gomis-Ruth F.X.
      Proc. Natl. Acad. Sci. U.S.A. 109:16131-16136(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.85 ANGSTROMS) OF 25-614, GLYCOSYLATION AT ASN-218; ASN-254; ASN-370; ASN-436; ASN-445; ASN-547 AND ASN-592, DISULFIDE BONDS, COFACTOR, ZINC-BINDING SITES, SUBUNIT, SUBCELLULAR LOCATION.
    15. Cited for: VARIANT ALA-324.

    Entry informationi

    Entry nameiMEP1B_HUMAN
    AccessioniPrimary (citable) accession number: Q16820
    Secondary accession number(s): B7ZM35, B9EGL6, Q670J1
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 1, 1997
    Last sequence update: May 18, 2010
    Last modified: October 1, 2014
    This is version 139 of the entry and version 3 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

    3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

    Documents

    1. Human chromosome 18
      Human chromosome 18: 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. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    6. Peptidase families
      Classification of peptidase families and list of entries
    7. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3