MMP15_HUMAN - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: MMP15_HUMAN
• UniProt AC: P51511
• Protein Name: Matrix metalloproteinase-15
• Gene Name: MMP15
• Organism: Homo sapiens (Human).
• Sequence Length: 669
• Subcellular Localization: Membrane ; Single-pass type I membrane protein ; Extracellular side .
• Protein Description: Endopeptidase that degrades various components of the extracellular matrix. May activate progelatinase A..
• Protein Sequence: MGSDPSAPGRPGWTGSLLGDREEAARPRLLPLLLVLLGCLGLGVAAEDAEVHAENWLRLYGYLPQPSRHMSTMRSAQILASALAEMQRFYGIPVTGVLDEETKEWMKRPRCGVPDQFGVRVKANLRRRRKRYALTGRKWNNHHLTFSIQNYTEKLGWYHSMEAVRRAFRVWEQATPLVFQEVPYEDIRLRRQKEADIMVLFASGFHGDSSPFDGTGGFLAHAYFPGPGLGGDTHFDADEPWTFSSTDLHGNNLFLVAVHELGHALGLEHSSNPNAIMAPFYQWKDVDNFKLPEDDLRGIQQLYGTPDGQPQPTQPLPTVTPRRPGRPDHRPPRPPQPPPPGGKPERPPKPGPPVQPRATERPDQYGPNICDGDFDTVAMLRGEMFVFKGRWFWRVRHNRVLDNYPMPIGHFWRGLPGDISAAYERQDGRFVFFKGDRYWLFREANLEPGYPQPLTSYGLGIPYDRIDTAIWWEPTGHTFFFQEDRYWRFNEETQRGDPGYPKPISVWQGIPASPKGAFLSNDAAYTYFYKGTKYWKFDNERLRMEPGYPKSILRDFMGCQEHVEPGPRWPDVARPPFNPHGGAEPGADSAEGDVGDGDGDFGAGVNKDGGSRVVVQMEEVARTVNVVMVLVPLLLLLCVLGLTYALVQMQRKGAPRVLLYCKRSLQEWV

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
14	Phosphorylation	APGRPGWTGSLLGDR CCCCCCCCCHHCCCH	23.86	24719451
67	Phosphorylation	YGYLPQPSRHMSTMR CCCCCCCCCCHHHHH	29.57	20058876
75	Phosphorylation	RHMSTMRSAQILASA CCHHHHHHHHHHHHH	17.44	30206219
81	Phosphorylation	RSAQILASALAEMQR HHHHHHHHHHHHHHH	21.99	24719451
90	Phosphorylation	LAEMQRFYGIPVTGV HHHHHHHHCCCCCCC	19.14	30206219
95	Phosphorylation	RFYGIPVTGVLDEET HHHCCCCCCCCCHHH	19.07	30206219
150	N-linked_Glycosylation	HLTFSIQNYTEKLGW EEEEEEECHHHHHCC	43.98	UniProtKB CARBOHYD
305	O-linked_Glycosylation	GIQQLYGTPDGQPQP HHHHHHCCCCCCCCC	12.49	55828305
313	O-linked_Glycosylation	PDGQPQPTQPLPTVT CCCCCCCCCCCCCCC	37.26	55828309
318	O-linked_Glycosylation	QPTQPLPTVTPRRPG CCCCCCCCCCCCCCC	44.70	55828315
320	O-linked_Glycosylation	TQPLPTVTPRRPGRP CCCCCCCCCCCCCCC	17.35	55828321
388	Ubiquitination	RGEMFVFKGRWFWRV CCEEEEEECEEEEEE	42.11	-
520	Phosphorylation	SPKGAFLSNDAAYTY CCCCCCCCCCCCEEE	26.64	29396449
525	Phosphorylation	FLSNDAAYTYFYKGT CCCCCCCEEEEECCC	12.05	29396449
526	Phosphorylation	LSNDAAYTYFYKGTK CCCCCCEEEEECCCE	11.48	29396449
527	Phosphorylation	SNDAAYTYFYKGTKY CCCCCEEEEECCCEE	7.70	29396449
551	Phosphorylation	MEPGYPKSILRDFMG CCCCCCHHHHHHHHC	23.50	24719451
589	Phosphorylation	GAEPGADSAEGDVGD CCCCCCCCCCCCCCC	27.90	28355574
660	Phosphorylation	GAPRVLLYCKRSLQE CCCEEEEEEHHHHHH	7.55	24719451
662	Ubiquitination	PRVLLYCKRSLQEWV CEEEEEEHHHHHHCC	31.31	-

Upstream regulatory proteins (kinases for phosphorylation sites, E3 ubiquitin ligases of ubiquitination sites, ...)

Oops, there are no upstream regulatory protein records of MMP15_HUMAN !!

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of MMP15_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 MMP15_HUMAN !!

Protein-Protein Interaction

Oops, there are no PPI records of MMP15_HUMAN !!

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.

Related Literatures of Post-Translational Modification

Phosphorylation

"Kinase-selective enrichment enables quantitative phosphoproteomics ofthe kinome across the cell cycle.";
Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,Greff Z., Keri G., Stemmann O., Mann M.;
Mol. Cell 31:438-448(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-589, AND MASSSPECTROMETRY.
PubMed: 18691976