MMP14_HUMAN - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: MMP14_HUMAN
• UniProt AC: P50281
• Protein Name: Matrix metalloproteinase-14
• Gene Name: MMP14
• Organism: Homo sapiens (Human).
• Sequence Length: 582
• Subcellular Localization: Membrane ; Single-pass type I membrane protein . Melanosome. Cytoplasm. Identified by mass spectrometry in melanosome fractions from stage I to stage IV. Forms a complex with BST2 and localizes to the cytoplasm.
• Protein Description: Endopeptidase that degrades various components of the extracellular matrix such as collagen. Activates progelatinase A. Essential for pericellular collagenolysis and modeling of skeletal and extraskeletal connective tissues during development (By similarity). May be involved in actin cytoskeleton reorganization by cleaving PTK7. [PubMed: 20837484 Acts as a positive regulator of cell growth and migration via activation of MMP15. Involved in the formation of the fibrovascular tissues in association with pro-MMP2]
• Protein Sequence: MSPAPRPPRCLLLPLLTLGTALASLGSAQSSSFSPEAWLQQYGYLPPGDLRTHTQRSPQSLSAAIAAMQKFYGLQVTGKADADTMKAMRRPRCGVPDKFGAEIKANVRRKRYAIQGLKWQHNEITFCIQNYTPKVGEYATYEAIRKAFRVWESATPLRFREVPYAYIREGHEKQADIMIFFAEGFHGDSTPFDGEGGFLAHAYFPGPNIGGDTHFDSAEPWTVRNEDLNGNDIFLVAVHELGHALGLEHSSDPSAIMAPFYQWMDTENFVLPDDDRRGIQQLYGGESGFPTKMPPQPRTTSRPSVPDKPKNPTYGPNICDGNFDTVAMLRGEMFVFKERWFWRVRNNQVMDGYPMPIGQFWRGLPASINTAYERKDGKFVFFKGDKHWVFDEASLEPGYPKHIKELGRGLPTDKIDAALFWMPNGKTYFFRGNKYYRFNEELRAVDSEYPKNIKVWEGIPESPRGSFMGSDEVFTYFYKGNKYWKFNNQKLKVEPGYPKSALRDWMGCPSGGRPDEGTEEETEVIIIEVDEEGGGAVSAAAVVLPVLLLLLVLAVGLAVFFFRRHGTPRRLLYCQRSLLDKV

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
2	Phosphorylation	------MSPAPRPPR ------CCCCCCCCC	29.75	30266825
72	Phosphorylation	IAAMQKFYGLQVTGK HHHHHHHHCCCCCCC	24.78	21406692
77	Phosphorylation	KFYGLQVTGKADADT HHHCCCCCCCCCHHH	21.72	21406692
77	O-linked_Glycosylation	KFYGLQVTGKADADT HHHCCCCCCCCCHHH	21.72	37823573
138	Phosphorylation	YTPKVGEYATYEAIR CCCCCCHHHHHHHHH	9.79	-
140	Phosphorylation	PKVGEYATYEAIRKA CCCCHHHHHHHHHHH	22.46	-
141	Phosphorylation	KVGEYATYEAIRKAF CCCHHHHHHHHHHHH	8.66	-
291	O-linked_Glycosylation	GGESGFPTKMPPQPR CCCCCCCCCCCCCCC	37.40	55826281
299	O-linked_Glycosylation	KMPPQPRTTSRPSVP CCCCCCCCCCCCCCC	35.49	55830371
299	Phosphorylation	KMPPQPRTTSRPSVP CCCCCCCCCCCCCCC	35.49	22210691
300	O-linked_Glycosylation	MPPQPRTTSRPSVPD CCCCCCCCCCCCCCC	24.82	55830377
301	O-linked_Glycosylation	PPQPRTTSRPSVPDK CCCCCCCCCCCCCCC	41.40	55830383
304	O-linked_Glycosylation	PRTTSRPSVPDKPKN CCCCCCCCCCCCCCC	45.21	55830389
399	Phosphorylation	EASLEPGYPKHIKEL HHHCCCCCCHHHHHH	21.59	7721107
462	Phosphorylation	VWEGIPESPRGSFMG EEECCCCCCCCCCCC	17.97	24961811
470	Phosphorylation	PRGSFMGSDEVFTYF CCCCCCCCCCEEEEE	20.86	28348404
510	Phosphorylation	RDWMGCPSGGRPDEG HHHCCCCCCCCCCCC	58.94	30631047
567	Phosphorylation	FFFRRHGTPRRLLYC HHHHHHCCHHHHHHH	13.90	22002060
573	Phosphorylation	GTPRRLLYCQRSLLD CCHHHHHHHHHHHHH	7.36	26356563
574	S-palmitoylation	TPRRLLYCQRSLLDK CHHHHHHHHHHHHHC	2.46	15946988
577	Phosphorylation	RLLYCQRSLLDKV-- HHHHHHHHHHHCC--	13.86	22199227
581	Ubiquitination	CQRSLLDKV------ HHHHHHHCC------	50.22	-

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
399	Y	Phosphorylation	Kinase	PKDCC	Q504Y2	Uniprot
567	T	Phosphorylation	Kinase	PRKCG	P05129	GPS
573	Y	Phosphorylation	Kinase	SRC	P12931	PSP

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of MMP14_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 MMP14_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
LUM_HUMAN	LUM	physical	15466200
C1QBP_HUMAN	C1QBP	physical	12220632
RAD_HUMAN	RRAD	physical	21988832
PLLP_HUMAN	PLLP	physical	21988832
KASH5_HUMAN	CCDC155	physical	25416956
TICN3_HUMAN	SPOCK3	physical	11751414
TIMP2_HUMAN	TIMP2	physical	8804434
MMP3_HUMAN	MMP3	physical	8804434
TIMP1_HUMAN	TIMP1	physical	8804434

Drug and Disease Associations

• Kegg Disease
• There are no disease associations of PTM sites.
• OMIM Disease
• 277950: Winchester syndrome (WNCHRS)
• Kegg Drug
• D03797: Prinomastat (USAN/INN)
• DrugBank
• There are no disease associations of PTM sites.