MEP1B_RAT - dbPTM
MEP1B_RAT - PTM Information in dbPTM
Basic Information of Protein
UniProt ID MEP1B_RAT
UniProt AC P28826
Protein Name Meprin A subunit beta
Gene Name Mep1b
Organism Rattus norvegicus (Rat).
Sequence Length 704
Subcellular Localization Cell membrane
Single-pass type I membrane protein . Secreted . Homodimers are essentially membrane bound but may also be shed from the surface by ADAM-10 and ADAM-17.
Protein Description Membrane metallopeptidase that sheds many membrane-bound proteins. Exhibits a strong preference for acidic amino acids at the P1' position. 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..
Protein Sequence MDARHWPWFLVFATFLLVSGLPAPEKFVKDIDGGIDQDIFDINEDLGLDLFEGDIKLEASGRNSIIGDNYRWPHTIPYVLEDSLEMNAKGVILNAFERYRLKTCIDFKPWSGEENYISVFKGSGCWSSVGNIHAGKQELSIGTNCDRIATVQHEFLHALGFWHEQSRADRDDYITIVWDRILSGKEHNFNIYNDSVSDSLNVPYDYTSVMHYSKTAFQNGTESTIITKISDFEDVIGQRMDFSDYDLLKLNQLYSCTSSLSFMDSCDFELENICGMIQSSQDSADWQRLSQVLSGPENDHSNMGQCKDSGFFMHFNTSTGNGGVTAMLESRVLYPKRGFQCVEFYLYNSGSGNGQLNVYTREYTAGHQDGVLTLQREIRDIPTGSWQLYYVTLQVTEKFRVVFEGVGGPGASSGGLSIDDINLSETRCPHHIWHIQNFTQLLGGQTTVYSPPFYSSKGYAFQINLDLTSPTNVGLYFHLISGANDDQLQWPCPWQQATMTLLDQNPDIRQRMSNQRSITTDPKMTDDNGSYLWDRPSKVGVEAFFPNGTQFSRGRGYGTSVFITQERLKSREFLKGDDVYILLTVEDISHLNSTAAVPGPVPTTSTVHNACSEVECQNGGICTLQEGRAECKCPAGEDWWYMGKRCEKRGSTKDTIVIAVSSTVTVFAVMLIITLISVYCTRRKYRKKASAKTAAMNLENQHAF
Overview of Protein Modification Sites with Functional and Structural Information
Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations Modification Substrate Peptides
&
Secondary Structure
ASA (%) Reference Orthologous
Protein Cluster
193N-linked_GlycosylationEHNFNIYNDSVSDSL
CCCCCCCCCCCCCCC
31.14-
219N-linked_GlycosylationYSKTAFQNGTESTII
EEEEHHCCCCEEEEE
53.56-
316N-linked_GlycosylationSGFFMHFNTSTGNGG
CCEEEEEEECCCCCC
20.59-
422N-linked_GlycosylationGLSIDDINLSETRCP
CCCCCCCCCCCCCCC
44.50-
437N-linked_GlycosylationHHIWHIQNFTQLLGG
CHHEEECCHHHHHCC
41.13-
528N-linked_GlycosylationDPKMTDDNGSYLWDR
CCCCCCCCCCCCCCC
44.09-
547N-linked_GlycosylationGVEAFFPNGTQFSRG
CCEEECCCCCCCCCC
62.07-
592N-linked_GlycosylationVEDISHLNSTAAVPG
EHHHHCCCCCCCCCC
31.71-

Upstream regulatory proteins (kinases for phosphorylation sites, E3 ubiquitin ligases of ubiquitination sites, ...)
Modified Location Modified Residue Modification Type of Upstream Proteins Gene Name of Upstream Proteins UniProt AC of Upstream Proteins Sources

Oops, there are no upstream regulatory protein records of MEP1B_RAT !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of MEP1B_RAT !!

Disease-associated PTM Sites based on SAP

* Distance = the distance between SAP position and PTM sites.

Modified Location Modification Variant Position
(Distance <= 10)
Residue Change SAP Related Disease Reference

Oops, there are no SNP-PTM records of MEP1B_RAT !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
OS9_RATOs9physical
12093806
OS9_MOUSEOs9physical
12093806

Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of MEP1B_RAT

loading...

Related Literatures of Post-Translational Modification

TOP