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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

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 – 1531 By similarity
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
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-17.2 Publications

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini23 – 652630Extracellular Reviewed predictionAdd
BLAST
Transmembranei653 – 67321Helical; Reviewed predictionAdd
BLAST
Topological domaini674 – 70128Cytoplasmic Reviewed predictionAdd
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 – 2222 Reviewed predictionAdd
BLAST
Propeptidei23 – 6139PRO_0000028883Add
BLAST
Chaini62 – 701640Meprin A subunit betaPRO_0000028884Add
BLAST

Amino acid modifications

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

Post-translational modificationi

N-glycosylated; contains high mannose and/or complex biantennary structures.2 Publications
O-glycosylation protect the C-terminal region from proteolytic cleavage and diminish secretion, this seems to be specific to human.
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.1 Publication

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.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini260 – 429170MAMAdd
BLAST
Domaini430 – 585156MATHAdd
BLAST
Domaini604 – 64441EGF-likeAdd
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.
Contains 1 EGF-like domain.
Contains 1 MAM domain.
Contains 1 MATH domain.

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

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 conflict

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

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

« 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: July 9, 2014
This is version 138 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

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