PMAP: SubstrateDB :

Homo sapiens

MGKNKLLHPSLVLLLLVLLPTDASVSGKPQYMVLVPSLLHTETTEKGCVLLSYLNETVTV
SASLESVRGNRSLFTDLEAENDVLHCVAFAVPKSSSNEEVMFLTVQVKGPTQEFKKRTTV
MVKNEDSLVFVQTDKSIYKPGQTVKFRVVSMDENFHPLNELIPLVYIQDPKGNRIAQWQS
FQLEGGLKQFSFPLSSEPFQGSYKVVVQKKSGGRTEHPFTVEEFVLPKFEVQVTVPKIIT
ILEEEMNVSVCGLYTYGKPVPGHVTVSICRKYSDASDCHGEDSQAFCEKFSGQLNSHGCF
YQQVKTKVFQLKRKEYEMKLHTEAQIQEEGTVVELTGRQSSEITRTITKLSFVKVDSHFR
QGIPFFGQVRLVDGKGVPIPNKVIFIRGNEANYYSNATTDEHGLVQFSINTTNVMGTSLT
VRVNYKDRSPCYGYQWVSEEHEEAHHTAYLVFSPSKSFVHLEPMSHELPCGHTQTVQAHY
ILNGGTLLGLKKLSFYYLIMAKGGIVRTGTHGLLVKQEDMKGHFSISIPVKSDIAPVARL
LIYAVLPTGDVIGDSAKYDVENCLANKVDLSFSPSQSLPASHAHLRVTAAPQSVCALRAV
DQSVLLMKPDAELSASSVYNLLPEKDLTGFPGPLNDQDDEDCINRHNVYINGITYTPVSS
TNEKDMYSFLEDMGLKAFTNSKIRKPKMCPQLQQYEMHGPEGLRVGFYESDVMGRGHARL
VHVEEPHTETVRKYFPETWIWDLVVVNSAGVAEVGVTVPDTITEWKAGAFCLSEDAGLGI
SSTASLRAFQPFFVELTMPYSVIRGEAFTLKATVLNYLPKCIRVSVQLEASPAFLAVPVE
KEQAPHCICANGRQTVSWAVTPKSLGNVNFTVSAEALESQELCGTEVPSVPEHGRKDTVI
KPLLVEPEGLEKETTFNSLLCPSGGEVSEELSLKLPPNVVEESARASVSVLGDILGSAMQ
NTQNLLQMPYGCGEQNMVLFAPNIYVLDYLNETQQLTPEIKSKAIGYLNTGYQRQLNYKH
YDGSYSTFGERYGRNQGNTWLTAFVLKTFAQARAYIFIDEAHITQALIWLSQRQKDNGCF
RSSGSLLNNAIKGGVEDEVTLSAYITIALLEIPLTVTHPVVRNALFCLESAWKTAQEGDH
GSHVYTKALLAYAFALAGNQDKRKEVLKSLNEEAVKKDNSVHWERPQKPKAPVGHFYEPQ
APSAEVEMTSYVLLAYLTAQPAPTSEDLTSATNIVKWITKQQNAQGGFSSTQDTVVALHA
LSKYGAATFTRTGKAAQVTIQSSGTFSSKFQVDNNNRLLLQQVSLPELPGEYSMKVTGEG
CVYLQTSLKYNILPEKEEFPFALGVQTLPQTCDEPKAHTSFQISLSVSYTGSRSASNMAI
VDVKMVSGFIPLKPTVKMLERSNHVSRTEVSSNHVLIYLDKVSNQTLSLFFTVLQDVPVR
DLKPAIVKVYDYYETDEFAIAEYNAPCSKDLGNA

The graphic displays domains and Protease cut sites on the protein sequence. Drag your mouse right/left over the graphic. Use the selection boxes on the right to select which annotations to view simultaneously. Combine annotation with multiple checkmarks.

InterPro Domain:
CutDB Proteolytic Event:
Protease:
MEROPS family:
Seq range:	-
Cleavage position:
Cleavage residues:

is proteolytically cut by ADAMTS4 peptidase (M12.221) cleavage. SDVM-GRGH.

is proteolytically cut by matrix metallopeptidase-2 (M10.003) cleavage. GHAR-LVHV.

is proteolytically cut by matrix metallopeptidase-2 (M10.003) cleavage. GPEG-LRVG.

is proteolytically cut by cathepsin E (A01.010) cleavage. SPAF-LAVP.

is proteolytically cut by lebetase (M12.164) cleavage. GRGH-ARLV.

is proteolytically cut by lebetase (M12.164) cleavage. GPEG-LRVG.

is proteolytically cut by lebetase (M12.164) cleavage. GHAR-LVHV.

is proteolytically cut by atrolysin E (M12.145) cleavage. ESDV-MGRG.

is proteolytically cut by atrolysin E (M12.145) cleavage. MGRG-HARL.

is proteolytically cut by atrolysin C (M12.144) cleavage. GHAR-LVHV.

is proteolytically cut by atrolysin A (M12.142) cleavage. GRGH-ARLV.

is proteolytically cut by atrolysin A (M12.142) cleavage. GHAR-LVHV.

is proteolytically cut by matrix metallopeptidase-3 (M10.005) cleavage. RVGF-YESD.

is proteolytically cut by matrix metallopeptidase-3 (M10.005) cleavage. GPEG-LRVG.

is proteolytically cut by matrix metallopeptidase-1 (M10.001) cleavage. GPEG-LRVG.

is proteolytically cut by membrane-type matrix metallopeptidase-1 (M10.014) cleavage..

is proteolytically cut by chymase (S01.140) cleavage. RVGF-YESD.

is proteolytically cut by chymase (S01.140) cleavage. VGFY-ESDV.

is proteolytically cut by ADAMTS12 peptidase (M12.237) cleavage..

is proteolytically cut by adamalysin-19 (M12.214) cleavage..