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Q16820

- MEP1B_HUMAN

UniProt

Q16820 - MEP1B_HUMAN

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Protein

Meprin A subunit beta

Gene

MEP1B

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

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

Zn2+1 PublicationNote: 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. zinc ion binding Source: ProtInc

GO - Biological processi

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

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.

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini23 – 652630ExtracellularSequence AnalysisAdd
BLAST
Transmembranei653 – 67321HelicalSequence AnalysisAdd
BLAST
Topological domaini674 – 70128CytoplasmicSequence AnalysisAdd
BLAST

GO - Cellular componenti

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

Keywords - Cellular componenti

Cell membrane, Membrane, Secreted

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi248 – 2481K → Y: Decreased activity toward gastrin. 1 Publication
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.
ExpressionAtlasiQ16820. baseline.
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 – 324Combined sources
Helixi37 – 437Combined sources
Turni50 – 523Combined sources
Beta strandi63 – 653Combined sources
Helixi67 – 693Combined sources
Beta strandi73 – 797Combined sources
Helixi85 – 10117Combined sources
Beta strandi105 – 1084Combined sources
Beta strandi113 – 1197Combined sources
Beta strandi122 – 1265Combined sources
Beta strandi133 – 1408Combined sources
Helixi147 – 15812Combined sources
Helixi163 – 1653Combined sources
Helixi169 – 1713Combined sources
Beta strandi173 – 1753Combined sources
Helixi177 – 1793Combined sources
Helixi185 – 1884Combined sources
Turni193 – 1953Combined sources
Turni213 – 2164Combined sources
Beta strandi217 – 2215Combined sources
Beta strandi223 – 2286Combined sources
Helixi229 – 2313Combined sources
Turni232 – 2365Combined sources
Helixi243 – 25210Combined sources
Beta strandi259 – 2657Combined sources
Helixi272 – 2743Combined sources
Beta strandi276 – 2783Combined sources
Beta strandi280 – 2823Combined sources
Beta strandi285 – 2895Combined sources
Beta strandi292 – 2943Combined sources
Beta strandi299 – 3046Combined sources
Beta strandi311 – 3155Combined sources
Beta strandi317 – 3193Combined sources
Beta strandi324 – 3285Combined sources
Beta strandi335 – 3373Combined sources
Beta strandi339 – 3479Combined sources
Beta strandi354 – 36310Combined sources
Beta strandi366 – 37914Combined sources
Beta strandi382 – 3843Combined sources
Beta strandi386 – 3927Combined sources
Beta strandi398 – 4058Combined sources
Beta strandi412 – 42514Combined sources
Beta strandi429 – 4346Combined sources
Helixi438 – 4403Combined sources
Beta strandi447 – 4493Combined sources
Beta strandi460 – 4667Combined sources
Beta strandi469 – 48012Combined sources
Helixi485 – 4873Combined sources
Beta strandi494 – 5018Combined sources
Helixi508 – 5103Combined sources
Beta strandi514 – 5196Combined sources
Beta strandi527 – 5315Combined sources
Helixi536 – 5394Combined sources
Beta strandi541 – 5444Combined sources
Beta strandi550 – 56415Combined sources
Helixi565 – 5684Combined sources
Beta strandi573 – 5753Combined sources
Beta strandi578 – 58710Combined sources
Helixi589 – 5913Combined sources

3D structure databases

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

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.
GeneTreeiENSGT00760000119227.
HOGENOMiHOG000043106.
HOVERGENiHBG052457.
InParanoidiQ16820.
KOiK08606.
OMAiDYVSIIW.
OrthoDBiEOG73V6MT.
PhylomeDBiQ16820.
TreeFamiTF315280.

Family and domain databases

Gene3Di3.40.390.10. 1 hit.
InterProiIPR013320. ConA-like_dom.
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]
PANTHERiPTHR10127:SF312. PTHR10127:SF312. 1 hit.
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

        10         20         30         40         50
MDLWNLSWFL FLDALLVISG LATPENFDVD GGMDQDIFDI NEGLGLDLFE
60 70 80 90 100
GDIRLDRAQI RNSIIGEKYR WPHTIPYVLE DSLEMNAKGV ILNAFERYRL
110 120 130 140 150
KTCIDFKPWA GETNYISVFK GSGCWSSVGN RRVGKQELSI GANCDRIATV
160 170 180 190 200
QHEFLHALGF WHEQSRSDRD DYVRIMWDRI LSGREHNFNT YSDDISDSLN
210 220 230 240 250
VPYDYTSVMH YSKTAFQNGT EPTIVTRISD FEDVIGQRMD FSDSDLLKLN
260 270 280 290 300
QLYNCSSSLS FMDSCSFELE NVCGMIQSSG DNADWQRVSQ VPRGPESDHS
310 320 330 340 350
NMGQCQGSGF FMHFDSSSVN VGATAVLESR TLYPKRGFQC LQFYLYNSGS
360 370 380 390 400
ESDQLNIYIR EYSADNVDGN LTLVEEIKEI PTGSWQLYHV TLKVTKKFRV
410 420 430 440 450
VFEGRKGSGA SLGGLSIDDI NLSETRCPHH IWHIRNFTQF IGSPNGTLYS
460 470 480 490 500
PPFYSSKGYA FQIYLNLAHV TNAGIYFHLI SGANDDQLQW PCPWQQATMT
510 520 530 540 550
LLDQNPDIRQ RMSNQRSITT DPFMTTDNGN YFWDRPSKVG TVALFSNGTQ
560 570 580 590 600
FRRGGGYGTS AFITHERLKS RDFIKGDDVY ILLTVEDISH LNSTQIQLTP
610 620 630 640 650
APSVQDLCSK TTCKNDGVCT VRDGKAECRC QSGEDWWYMG ERCEKRGSTR
660 670 680 690 700
DTIVIAVSST VAVFALMLII TLVSVYCTRK KYRERMSSNR PNLTPQNQHA

F
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:
EMBLi
GenBanki
DDBJi
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:
EMBLi
GenBanki
DDBJi
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:
PDBei
RCSB PDBi
PDBji
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.
GeneTreei ENSGT00760000119227.
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.
ExpressionAtlasi Q16820. baseline.
Genevestigatori Q16820.

Family and domain databases

Gene3Di 3.40.390.10. 1 hit.
InterProi IPR013320. ConA-like_dom.
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 ]
PANTHERi PTHR10127:SF312. PTHR10127:SF312. 1 hit.
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

« Hide 'large scale' publications
  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: November 26, 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
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