MMP17_HUMAN - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: MMP17_HUMAN
• UniProt AC: Q9ULZ9
• Protein Name: Matrix metalloproteinase-17
• Gene Name: MMP17
• Organism: Homo sapiens (Human).
• Sequence Length: 603
• Subcellular Localization: Isoform Long: Cell membrane; Lipid-anchor, GPI-anchor; Extracellular side. Secreted, extracellular space, extracellular matrix.
• Protein Description: Endopeptidase that degrades various components of the extracellular matrix, such as fibrin. May be involved in the activation of membrane-bound precursors of growth factors or inflammatory mediators, such as tumor necrosis factor-alpha. May also be involved in tumoral process. Cleaves pro-TNF-alpha at the '74-Ala-|-Gln-75' site. Not obvious if able to proteolytically activate progelatinase A. Does not hydrolyze collagen types I, II, III, IV and V, gelatin, fibronectin, laminin, decorin nor alpha1-antitrypsin..
• Protein Sequence: MRRRAARGPGPPPPGPGLSRLPLPLLLLLALGTRGGCAAPAPAPRAEDLSLGVEWLSRFGYLPPADPTTGQLQTQEELSKAITAMQQFGGLEATGILDEATLALMKTPRCSLPDLPVLTQARRRRQAPAPTKWNKRNLSWRVRTFPRDSPLGHDTVRALMYYALKVWSDIAPLNFHEVAGSAADIQIDFSKADHNDGYPFDGPGGTVAHAFFPGHHHTAGDTHFDDDEAWTFRSSDAHGMDLFAVAVHEFGHAIGLSHVAAAHSIMRPYYQGPVGDPLRYGLPYEDKVRVWQLYGVRESVSPTAQPEEPPLLPEPPDNRSSAPPRKDVPHRCSTHFDAVAQIRGEAFFFKGKYFWRLTRDRHLVSLQPAQMHRFWRGLPLHLDSVDAVYERTSDHKIVFFKGDRYWVFKDNNVEEGYPRPVSDFSLPPGGIDAAFSWAHNDRTYFFKDQLYWRYDDHTRHMDPGYPAQSPLWRGVPSTLDDAMRWSDGASYFFRGQEYWKVLDGELEVAPGYPQSTARDWLVCGDSQADGSVAAGVDAAEGPRAPPGQHDQSRSEDGYEVCSCTSGASSPPGAPGPLVAATMLLLLPPLSPGALWTAAQALTL

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
33	Phosphorylation	LLLLALGTRGGCAAP HHHHHHCCCCCCCCC	27.30	28787133
137	N-linked_Glycosylation	PTKWNKRNLSWRVRT CCCCCCCCCEEEEEE	39.78	UniProtKB CARBOHYD
139	Phosphorylation	KWNKRNLSWRVRTFP CCCCCCCEEEEEEEC	19.18	24719451
144	Phosphorylation	NLSWRVRTFPRDSPL CCEEEEEEECCCCCC	34.82	-
149	Phosphorylation	VRTFPRDSPLGHDTV EEEECCCCCCCHHHH	24.25	18452278
155	Phosphorylation	DSPLGHDTVRALMYY CCCCCHHHHHHHHHH	13.25	18452278
270	Phosphorylation	HSIMRPYYQGPVGDP HHHHCCCCCCCCCCC	15.07	22817900
318	N-linked_Glycosylation	LLPEPPDNRSSAPPR CCCCCCCCCCCCCCC	52.05	UniProtKB CARBOHYD
465	Phosphorylation	TRHMDPGYPAQSPLW CCCCCCCCCCCCCCC	10.77	28634298
469	Phosphorylation	DPGYPAQSPLWRGVP CCCCCCCCCCCCCCC	24.86	28634298
477	Phosphorylation	PLWRGVPSTLDDAMR CCCCCCCCCHHHHHH	38.91	24275569
490	Phosphorylation	MRWSDGASYFFRGQE HHCCCCCCEEECCCE	28.18	24275569
498	Phosphorylation	YFFRGQEYWKVLDGE EEECCCEEEEEECCE	11.57	24275569
565	GPI-anchor	YEVCSCTSGASSPPG EEECEECCCCCCCCC	36.37	-

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

Oops, there are no upstream regulatory protein records of MMP17_HUMAN !!

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of MMP17_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 MMP17_HUMAN !!

Protein-Protein Interaction

Oops, there are no PPI records of MMP17_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.