MEP1B_HUMAN - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: MEP1B_HUMAN
• UniProt AC: Q16820
• Protein Name: Meprin A subunit beta
• Gene Name: MEP1B
• Organism: Homo sapiens (Human).
• Sequence Length: 701
• 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: MDLWNLSWFLFLDALLVISGLATPENFDVDGGMDQDIFDINEGLGLDLFEGDIRLDRAQIRNSIIGEKYRWPHTIPYVLEDSLEMNAKGVILNAFERYRLKTCIDFKPWAGETNYISVFKGSGCWSSVGNRRVGKQELSIGANCDRIATVQHEFLHALGFWHEQSRSDRDDYVRIMWDRILSGREHNFNTYSDDISDSLNVPYDYTSVMHYSKTAFQNGTEPTIVTRISDFEDVIGQRMDFSDSDLLKLNQLYNCSSSLSFMDSCSFELENVCGMIQSSGDNADWQRVSQVPRGPESDHSNMGQCQGSGFFMHFDSSSVNVGATAVLESRTLYPKRGFQCLQFYLYNSGSESDQLNIYIREYSADNVDGNLTLVEEIKEIPTGSWQLYHVTLKVTKKFRVVFEGRKGSGASLGGLSIDDINLSETRCPHHIWHIRNFTQFIGSPNGTLYSPPFYSSKGYAFQIYLNLAHVTNAGIYFHLISGANDDQLQWPCPWQQATMTLLDQNPDIRQRMSNQRSITTDPFMTTDNGNYFWDRPSKVGTVALFSNGTQFRRGGGYGTSAFITHERLKSRDFIKGDDVYILLTVEDISHLNSTQIQLTPAPSVQDLCSKTTCKNDGVCTVRDGKAECRCQSGEDWWYMGERCEKRGSTRDTIVIAVSSTVAVFALMLIITLVSVYCTRKKYRERMSSNRPNLTPQNQHAF

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
120	Ubiquitination	TNYISVFKGSGCWSS CCEEEEEECCCCCCC	50.43	-
192	Phosphorylation	EHNFNTYSDDISDSL CCCCCCCCCCCHHHC	27.11	-
196	Phosphorylation	NTYSDDISDSLNVPY CCCCCCCHHHCCCCC	28.30	-
198	Phosphorylation	YSDDISDSLNVPYDY CCCCCHHHCCCCCCC	18.30	-
218	N-linked_Glycosylation	YSKTAFQNGTEPTIV EEECHHCCCCCCEEE	53.56	22988105
242	Phosphorylation	IGQRMDFSDSDLLKL HCCCCCCCHHHHHHH	31.76	-
244	Phosphorylation	QRMDFSDSDLLKLNQ CCCCCCHHHHHHHHH	29.03	-
254	N-linked_Glycosylation	LKLNQLYNCSSSLSF HHHHHHCCCCCCCCC	27.99	22988105
289	Phosphorylation	NADWQRVSQVPRGPE CCCHHHHHCCCCCCC	27.87	22210691
297	Phosphorylation	QVPRGPESDHSNMGQ CCCCCCCCCCCCCCC	43.70	22210691
300	Phosphorylation	RGPESDHSNMGQCQG CCCCCCCCCCCCCCC	33.24	22210691
308	Phosphorylation	NMGQCQGSGFFMHFD CCCCCCCCCEEEEEC	13.42	22210691
318	Phosphorylation	FMHFDSSSVNVGATA EEEECCCCCEECCEE	22.97	22210691
370	N-linked_Glycosylation	SADNVDGNLTLVEEI CCCCCCCCEEEEEEE	25.95	22988105
421	N-linked_Glycosylation	GLSIDDINLSETRCP CEEHHCCCCCCCCCC	44.50	UniProtKB CARBOHYD
436	N-linked_Glycosylation	HHIWHIRNFTQFIGS CCEEEECCHHHHCCC	43.65	22988105
445	N-linked_Glycosylation	TQFIGSPNGTLYSPP HHHCCCCCCCEECCC	58.75	22988105
513	Phosphorylation	PDIRQRMSNQRSITT HHHHHHHHCCCCCCC	31.81	25072903
517	Phosphorylation	QRMSNQRSITTDPFM HHHHCCCCCCCCCCE	17.96	25072903
519	Phosphorylation	MSNQRSITTDPFMTT HHCCCCCCCCCCEEC	26.79	25072903
520	Phosphorylation	SNQRSITTDPFMTTD HCCCCCCCCCCEECC	39.75	25072903
525	Phosphorylation	ITTDPFMTTDNGNYF CCCCCCEECCCCCEE	31.23	25072903
526	Phosphorylation	TTDPFMTTDNGNYFW CCCCCEECCCCCEEE	18.71	25072903
531	Phosphorylation	MTTDNGNYFWDRPSK EECCCCCEEECCCCC	13.88	25072903
547	N-linked_Glycosylation	GTVALFSNGTQFRRG EEEEEEECCCEEECC	50.63	22988105
592	N-linked_Glycosylation	VEDISHLNSTQIQLT EEHHHCCCCCEEEEE	37.27	22988105
593	O-linked_Glycosylation	EDISHLNSTQIQLTP EHHHCCCCCEEEEEC	28.22	UniProtKB CARBOHYD
594	O-linked_Glycosylation	DISHLNSTQIQLTPA HHHCCCCCEEEEECC	28.72	UniProtKB CARBOHYD
599	O-linked_Glycosylation	NSTQIQLTPAPSVQD CCCEEEEECCCCHHH	10.88	12387727
599	O-linked_Glycosylation	NSTQIQLTPAPSVQD CCCEEEEECCCCHHH	10.88	UniProtKB CARBOHYD
603	O-linked_Glycosylation	IQLTPAPSVQDLCSK EEEECCCCHHHHHCC	34.22	12387727
603	O-linked_Glycosylation	IQLTPAPSVQDLCSK EEEECCCCHHHHHCC	34.22	UniProtKB CARBOHYD
611	Phosphorylation	VQDLCSKTTCKNDGV HHHHHCCCCCCCCCE	22.57	-
612	Phosphorylation	QDLCSKTTCKNDGVC HHHHCCCCCCCCCEE	25.81	-
620	Phosphorylation	CKNDGVCTVRDGKAE CCCCCEEEEECCCEE	19.03	-
687	Phosphorylation	KKYRERMSSNRPNLT HHHHHHHHCCCCCCC	30.59	12941954

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
687	S	Phosphorylation	Kinase	PKC-FAMILY	-	GPS
687	S	Phosphorylation	Kinase	PKC_GROUP	-	PhosphoELM

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of MEP1B_HUMAN !!

Disease-associated PTM Sites based on SAP

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

Oops, there are no SNP-PTM records of MEP1B_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
PYY_HUMAN	PYY	physical	11278902
GAST_HUMAN	GAST	physical	11278902
FINC_HUMAN	FN1	physical	8063866

Drug and Disease Associations

• Kegg Disease
• There are no disease associations of PTM sites.
• OMIM Disease
• There are no disease associations of PTM sites.
• Kegg Drug
• There are no disease associations of PTM sites.
• DrugBank
• There are no disease associations of PTM sites.