ADA15_HUMAN - dbPTM
ADA15_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID ADA15_HUMAN
UniProt AC Q13444
Protein Name Disintegrin and metalloproteinase domain-containing protein 15
Gene Name ADAM15
Organism Homo sapiens (Human).
Sequence Length 863
Subcellular Localization Endomembrane system
Single-pass type I membrane protein . Cell junction, adherens junction . Cell projection, cilium, flagellum. Cytoplasmic vesicle, secretory vesicle, acrosome. The majority of the protein is localized in a perinuclear compartment
Protein Description Active metalloproteinase with gelatinolytic and collagenolytic activity. Plays a role in the wound healing process. Mediates both heterotypic intraepithelial cell/T-cell interactions and homotypic T-cell aggregation. Inhibits beta-1 integrin-mediated cell adhesion and migration of airway smooth muscle cells. Suppresses cell motility on or towards fibronectin possibly by driving alpha-v/beta-1 integrin (ITAGV-ITGB1) cell surface expression via ERK1/2 inactivation. Cleaves E-cadherin in response to growth factor deprivation. Plays a role in glomerular cell migration. Plays a role in pathological neovascularization. May play a role in cartilage remodeling. May be proteolytically processed, during sperm epididymal maturation and the acrosome reaction. May play a role in sperm-egg binding through its disintegrin domain..
Protein Sequence MRLALLWALGLLGAGSPLPSWPLPNIGGTEEQQAESEKAPREPLEPQVLQDDLPISLKKVLQTSLPEPLRIKLELDGDSHILELLQNRELVPGRPTLVWYQPDGTRVVSEGHTLENCCYQGRVRGYAGSWVSICTCSGLRGLVVLTPERSYTLEQGPGDLQGPPIISRIQDLHLPGHTCALSWRESVHTQKPPEHPLGQRHIRRRRDVVTETKTVELVIVADHSEAQKYRDFQHLLNRTLEVALLLDTFFRPLNVRVALVGLEAWTQRDLVEISPNPAVTLENFLHWRRAHLLPRLPHDSAQLVTGTSFSGPTVGMAIQNSICSPDFSGGVNMDHSTSILGVASSIAHELGHSLGLDHDLPGNSCPCPGPAPAKTCIMEASTDFLPGLNFSNCSRRALEKALLDGMGSCLFERLPSLPPMAAFCGNMFVEPGEQCDCGFLDDCVDPCCDSLTCQLRPGAQCASDGPCCQNCQLRPSGWQCRPTRGDCDLPEFCPGDSSQCPPDVSLGDGEPCAGGQAVCMHGRCASYAQQCQSLWGPGAQPAAPLCLQTANTRGNAFGSCGRNPSGSYVSCTPRDAICGQLQCQTGRTQPLLGSIRDLLWETIDVNGTELNCSWVHLDLGSDVAQPLLTLPGTACGPGLVCIDHRCQRVDLLGAQECRSKCHGHGVCDSNRHCYCEEGWAPPDCTTQLKATSSLTTGLLLSLLVLLVLVMLGASYWYRARLHQRLCQLKGPTCQYRAAQSGPSERPGPPQRALLARGTKQASALSFPAPPSRPLPPDPVSKRLQAELADRPNPPTRPLPADPVVRSPKSQGPAKPPPPRKPLPADPQGRCPSGDLPGPGAGIPPLVVPSRPAPPPPTVSSLYL
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 Orthologous
Protein Cluster
52 (in isoform 13)Phosphorylation-41.1925072903
55 (in isoform 13)Phosphorylation-11.0825072903
56PhosphorylationLQDDLPISLKKVLQT
HCCCCCCCHHHHHHH		32.0025159151
58UbiquitinationDDLPISLKKVLQTSL
CCCCCCHHHHHHHCC		33.7621906983
58 (in isoform 10)Ubiquitination-33.76-
59UbiquitinationDLPISLKKVLQTSLP
CCCCCHHHHHHHCCC		54.1721906983
68UbiquitinationLQTSLPEPLRIKLEL
HHHCCCCCEEEEEEE		25.6221963094
69UbiquitinationQTSLPEPLRIKLELD
HHCCCCCEEEEEEEC		9.3622817900
72UbiquitinationLPEPLRIKLELDGDS
CCCCEEEEEEECCCH		29.4921906983
82UbiquitinationLDGDSHILELLQNRE
ECCCHHHHHHHHCCC		2.9621963094
167PhosphorylationLQGPPIISRIQDLHL
CCCCCCEEEEECCCC		24.8522210691
182PhosphorylationPGHTCALSWRESVHT
CCCEEEEEHHHHHHC		12.9324719451
189O-linked_GlycosylationSWRESVHTQKPPEHP
EHHHHHHCCCCCCCC		35.81OGP
237N-linked_GlycosylationRDFQHLLNRTLEVAL
HHHHHHHHHHHHHHH		41.05UniProtKB CARBOHYD
375PhosphorylationPGPAPAKTCIMEAST
CCCCCCCEEEEEECC		14.9029083192
381PhosphorylationKTCIMEASTDFLPGL
CEEEEEECCCCCCCC		18.4029083192
382PhosphorylationTCIMEASTDFLPGLN
EEEEEECCCCCCCCC		37.5129083192
389N-linked_GlycosylationTDFLPGLNFSNCSRR
CCCCCCCCCCHHHHH		44.19UniProtKB CARBOHYD
391PhosphorylationFLPGLNFSNCSRRAL
CCCCCCCCHHHHHHH		35.5329083192
392N-linked_GlycosylationLPGLNFSNCSRRALE
CCCCCCCHHHHHHHH		24.52UniProtKB CARBOHYD
394PhosphorylationGLNFSNCSRRALEKA
CCCCCHHHHHHHHHH		29.1129083192
400UbiquitinationCSRRALEKALLDGMG
HHHHHHHHHHHHHHH		45.22-
606N-linked_GlycosylationLWETIDVNGTELNCS
HHHEECCCCCEEEEE		48.17UniProtKB CARBOHYD
611N-linked_GlycosylationDVNGTELNCSWVHLD
CCCCCEEEEEEEEEE		16.14UniProtKB CARBOHYD
660UbiquitinationGAQECRSKCHGHGVC
CHHHHHHHCCCCCCC		15.7622817900
670UbiquitinationGHGVCDSNRHCYCEE
CCCCCCCCCEEEECC		25.1922817900
715PhosphorylationLVMLGASYWYRARLH
HHHHCHHHHHHHHHH		13.1111741929
729UbiquitinationHQRLCQLKGPTCQYR
HHHHHHCCCCCCHHH		36.6423000965
735PhosphorylationLKGPTCQYRAAQSGP
CCCCCCHHHHHHHCC		12.3614702039
735 (in isoform 10)Phosphorylation-12.3627282143
736PhosphorylationKGPTCQYRAAQSGPS
CCCCCHHHHHHHCCC		9.5127251275
736 (in isoform 10)Phosphorylation-9.5129743597
739UbiquitinationTCQYRAAQSGPSERP
CCHHHHHHHCCCCCC		48.1923000965
740PhosphorylationCQYRAAQSGPSERPG
CHHHHHHHCCCCCCC		48.2028555341
742 (in isoform 10)Phosphorylation-37.9625849741
759UbiquitinationALLARGTKQASALSF
HHHHCCCCCCHHHCC		46.8427667366
762PhosphorylationARGTKQASALSFPAP
HCCCCCCHHHCCCCC		27.5228348404
765PhosphorylationTKQASALSFPAPPSR
CCCCHHHCCCCCCCC		28.9727251275
765UbiquitinationTKQASALSFPAPPSR
CCCCHHHCCCCCCCC		28.9727667366
766PhosphorylationKQASALSFPAPPSRP
CCCHHHCCCCCCCCC		6.6027251275
766 (in isoform 9)Phosphorylation-6.6027251275
769UbiquitinationSALSFPAPPSRPLPP
HHHCCCCCCCCCCCC		27.8627667366
771UbiquitinationLSFPAPPSRPLPPDP
HCCCCCCCCCCCCCH		45.5329967540
775UbiquitinationAPPSRPLPPDPVSKR
CCCCCCCCCCHHHHH		33.6527667366
781UbiquitinationLPPDPVSKRLQAELA
CCCCHHHHHHHHHHC		58.3129967540
781PhosphorylationLPPDPVSKRLQAELA
CCCCHHHHHHHHHHC		58.3124719451
789UbiquitinationRLQAELADRPNPPTR
HHHHHHCCCCCCCCC		78.2627667366
806PhosphorylationPADPVVRSPKSQGPA
CCCCCCCCCCCCCCC		25.6827251275
809PhosphorylationPVVRSPKSQGPAKPP
CCCCCCCCCCCCCCC		43.6928555341
813UbiquitinationSPKSQGPAKPPPPRK
CCCCCCCCCCCCCCC		43.7627667366
814UbiquitinationPKSQGPAKPPPPRKP
CCCCCCCCCCCCCCC		62.2827667366
820UbiquitinationAKPPPPRKPLPADPQ
CCCCCCCCCCCCCCC		57.59-
832PhosphorylationDPQGRCPSGDLPGPG
CCCCCCCCCCCCCCC		48.8726657352
857PhosphorylationRPAPPPPTVSSLYL-
CCCCCCCCCCCCCC-		38.5022468782
862PhosphorylationPPTVSSLYL------
CCCCCCCCC------		16.5922468782
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
715YPhosphorylationKinaseHCKP08631
Uniprot
715YPhosphorylationKinaseLCKP06239
Uniprot
715YPhosphorylationKinaseSRCP12931
GPS
715YPhosphorylationKinaseSRC-FAMILY-GPS
715YPhosphorylationKinaseSRC_GROUP-PhosphoELM
715YPhosphorylationKinaseSRC64-PhosphoELM
735YPhosphorylationKinaseHCKP08631
Uniprot
735YPhosphorylationKinaseLCKP06239
Uniprot
735YPhosphorylationKinaseSRCP12931
GPS
735YPhosphorylationKinaseSRC-FAMILY-GPS
735YPhosphorylationKinaseSRC_GROUP-PhosphoELM
735YPhosphorylationKinaseSRC64-PhosphoELM
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of ADA15_HUMAN !!
Disease-associated PTM Sites based on SAP

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

Modified Location Modification Variant Position
(Distance <= 10) 		Residue Change SAP Related Disease Reference

Oops, there are no SNP-PTM records of ADA15_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
PCH2_HUMANTRIP13physical
16189514
SNX9_HUMANSNX9physical
10531379
SH3G2_HUMANSH3GL2physical
10531379
LCK_HUMANLCKphysical
11741929
GRB2_HUMANGRB2physical
11741929
MD2L1_HUMANMAD2L1physical
11741929
HCK_HUMANHCKphysical
11741929
HCK_HUMANHCKphysical
16374509
LCK_HUMANLCKphysical
16374509
SRC_HUMANSRCphysical
16374509
SNX30_HUMANSNX30physical
16374509
NPHP1_HUMANNPHP1physical
16374509
ARHG7_HUMANARHGEF7physical
16374509
LYN_HUMANLYNphysical
16374509
YES_HUMANYES1physical
16374509
FYN_HUMANFYNphysical
16374509
SNX9_HUMANSNX9physical
16374509
SPD2A_HUMANSH3PXD2Aphysical
16374509
PACN3_HUMANPACSIN3physical
16374509
SHLB1_HUMANSH3GLB1physical
16374509
GRB2_HUMANGRB2physical
16374509
ARHG6_HUMANARHGEF6physical
16374509
NCK1_HUMANNCK1physical
16374509
SRBS2_HUMANSORBS2physical
16374509
SH3R3_HUMANSH3RF3physical
16374509
GRB2_HUMANGRB2physical
18296648
SPD2A_HUMANSH3PXD2Aphysical
18296648
MK03_HUMANMAPK3physical
18296648
MK01_HUMANMAPK1physical
18296648
NCK1_HUMANNCK1physical
18296648
SRC_HUMANSRCphysical
18296648
PTK6_HUMANPTK6physical
18296648
RBPMS_HUMANRBPMSphysical
25416956
NUP62_HUMANNUP62physical
25416956
BANP_HUMANBANPphysical
25416956
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.
Regulatory Network of ADA15_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Phosphorylation-dependent interactions between ADAM15 cytoplasmicdomain and Src family protein-tyrosine kinases.";
Poghosyan Z., Robbins S.M., Houslay M.D., Webster A., Murphy G.,Edwards D.R.;
J. Biol. Chem. 277:4999-5007(2002).
Cited for: PHOSPHORYLATION AT TYR-715 AND TYR-735, AND INTERACTION WITH GRB2; LCKAND HCK.

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