ADA10_HUMAN - dbPTM
ADA10_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID ADA10_HUMAN
UniProt AC O14672
Protein Name Disintegrin and metalloproteinase domain-containing protein 10
Gene Name ADAM10
Organism Homo sapiens (Human).
Sequence Length 748
Subcellular Localization Cell membrane
Single-pass type I membrane protein . Golgi apparatus membrane
Single-pass type I membrane protein . Is localized in the plasma membrane but is predominantly expressed in the Golgi apparatus and in released membrane vesicles derived
Protein Description Cleaves the membrane-bound precursor of TNF-alpha at '76-Ala-|-Val-77' to its mature soluble form. Responsible for the proteolytical release of soluble JAM3 from endothelial cells surface. [PubMed: 20592283 Responsible for the proteolytic release of several other cell-surface proteins, including heparin-binding epidermal growth-like factor, ephrin-A2, CD44, CDH2 and for constitutive and regulated alpha-secretase cleavage of amyloid precursor protein (APP)]
Protein Sequence MVLLRVLILLLSWAAGMGGQYGNPLNKYIRHYEGLSYNVDSLHQKHQRAKRAVSHEDQFLRLDFHAHGRHFNLRMKRDTSLFSDEFKVETSNKVLDYDTSHIYTGHIYGEEGSFSHGSVIDGRFEGFIQTRGGTFYVEPAERYIKDRTLPFHSVIYHEDDINYPHKYGPQGGCADHSVFERMRKYQMTGVEEVTQIPQEEHAANGPELLRKKRTTSAEKNTCQLYIQTDHLFFKYYGTREAVIAQISSHVKAIDTIYQTTDFSGIRNISFMVKRIRINTTADEKDPTNPFRFPNIGVEKFLELNSEQNHDDYCLAYVFTDRDFDDGVLGLAWVGAPSGSSGGICEKSKLYSDGKKKSLNTGIITVQNYGSHVPPKVSHITFAHEVGHNFGSPHDSGTECTPGESKNLGQKENGNYIMYARATSGDKLNNNKFSLCSIRNISQVLEKKRNNCFVESGQPICGNGMVEQGEECDCGYSDQCKDECCFDANQPEGRKCKLKPGKQCSPSQGPCCTAQCAFKSKSEKCRDDSDCAREGICNGFTALCPASDPKPNFTDCNRHTQVCINGQCAGSICEKYGLEECTCASSDGKDDKELCHVCCMKKMDPSTCASTGSVQWSRHFSGRTITLQPGSPCNDFRGYCDVFMRCRLVDADGPLARLKKAIFSPELYENIAEWIVAHWWAVLLMGIALIMLMAGFIKICSVHTPSSNPKLPPPKPLPGTLKRRRPPQPIQQPQRQRPRESYQMGHMRR
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
36O-linked_GlycosylationIRHYEGLSYNVDSLH
HHHHCCCCCCHHHHH		26.0555834733
41PhosphorylationGLSYNVDSLHQKHQR
CCCCCHHHHHHHHHH		24.3827080861
45UbiquitinationNVDSLHQKHQRAKRA
CHHHHHHHHHHHHHH		30.84-
93UbiquitinationFKVETSNKVLDYDTS
EEEEECCCEEECCCC		43.89-
109UbiquitinationIYTGHIYGEEGSFSH
EEECEEECCCCCCCC		26.35-
130O-linked_GlycosylationRFEGFIQTRGGTFYV
EEEEEEEECCCEEEE		26.8555831919
166UbiquitinationDDINYPHKYGPQGGC
CCCCCCHHCCCCCCC		47.61-
177PhosphorylationQGGCADHSVFERMRK
CCCCCCHHHHHHHHH		29.1124719451
184UbiquitinationSVFERMRKYQMTGVE
HHHHHHHHHHCCCCE		30.41-
185PhosphorylationVFERMRKYQMTGVEE
HHHHHHHHHCCCCEE		7.9826503514
188PhosphorylationRMRKYQMTGVEEVTQ
HHHHHHCCCCEEHHC		23.6626503514
194O-linked_GlycosylationMTGVEEVTQIPQEEH
CCCCEEHHCCCHHHH		24.86OGP
194PhosphorylationMTGVEEVTQIPQEEH
CCCCEEHHCCCHHHH		24.8626503514
214PhosphorylationELLRKKRTTSAEKNT
HHHHHHCCCCCCCCE		33.7046158995
257PhosphorylationVKAIDTIYQTTDFSG
HHHHCEEECCCCCCC		11.25110735949
263PhosphorylationIYQTTDFSGIRNISF
EECCCCCCCCCEEEE		35.8024719451
267N-linked_GlycosylationTDFSGIRNISFMVKR
CCCCCCCEEEEEEEE		32.1319349973
267N-linked_GlycosylationTDFSGIRNISFMVKR
CCCCCCCEEEEEEEE		32.13UniProtKB CARBOHYD
2732-HydroxyisobutyrylationRNISFMVKRIRINTT
CEEEEEEEEEEECCC		30.25-
278N-linked_GlycosylationMVKRIRINTTADEKD
EEEEEEECCCCCCCC		22.8729224781
278N-linked_GlycosylationMVKRIRINTTADEKD
EEEEEEECCCCCCCC		22.8729224781
284UbiquitinationINTTADEKDPTNPFR
ECCCCCCCCCCCCCC		70.3421906983
300UbiquitinationPNIGVEKFLELNSEQ
CCCCHHHHHHCCCCC		3.97-
3542-HydroxyisobutyrylationSKLYSDGKKKSLNTG
CCCCCCCCCCCCCCC		63.12-
357PhosphorylationYSDGKKKSLNTGIIT
CCCCCCCCCCCCEEE		35.41113299685
410UbiquitinationESKNLGQKENGNYIM
CCCCCCCCCCCCEEE		51.88-
420UbiquitinationGNYIMYARATSGDKL
CCEEEEEEECCCCCC		22.40-
436PhosphorylationNNKFSLCSIRNISQV
CCEEEEHHHHCHHHH		29.859394371
439N-linked_GlycosylationFSLCSIRNISQVLEK
EEEHHHHCHHHHHHH		36.2719349973
439N-linked_GlycosylationFSLCSIRNISQVLEK
EEEHHHHCHHHHHHH		36.2717660510
551N-linked_GlycosylationPASDPKPNFTDCNRH
CCCCCCCCCCCCCCC		59.58UniProtKB CARBOHYD
6002-HydroxyisobutyrylationLCHVCCMKKMDPSTC
HEEEEEEECCCHHHH		30.91-
601UbiquitinationCHVCCMKKMDPSTCA
EEEEEEECCCHHHHC		22.96-
605PhosphorylationCMKKMDPSTCASTGS
EEECCCHHHHCCCCC		31.6746158989
610O-linked_GlycosylationDPSTCASTGSVQWSR
CHHHHCCCCCEEEEE		18.23OGP
705PhosphorylationICSVHTPSSNPKLPP
HHCCCCCCCCCCCCC		43.8550563413
709UbiquitinationHTPSSNPKLPPPKPL
CCCCCCCCCCCCCCC		77.27-
709SumoylationHTPSSNPKLPPPKPL
CCCCCCCCCCCCCCC		77.27-
714UbiquitinationNPKLPPPKPLPGTLK
CCCCCCCCCCCCCCC		66.03-
719PhosphorylationPPKPLPGTLKRRRPP
CCCCCCCCCCCCCCC		27.4529255136
721UbiquitinationKPLPGTLKRRRPPQP
CCCCCCCCCCCCCCC		43.63-
740PhosphorylationQRQRPRESYQMGHMR
CCCCCCHHHHCCCCC		23.1930803981
741PhosphorylationRQRPRESYQMGHMRR
CCCCCHHHHCCCCCC		9.5828796482
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
719TPhosphorylationKinaseFAM20CQ8IXL6
Uniprot
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of ADA10_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 ADA10_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
MD2L1_HUMANMAD2L1physical
11741929
GRB2_HUMANGRB2physical
11741929
LCK_HUMANLCKphysical
11741929
OR4S2_HUMANOR4S2physical
22939629
MSRB2_HUMANMSRB2physical
22939629
DLG1_HUMANDLG1physical
17301176
TSN5_HUMANTSPAN5physical
23091066
Drug and Disease Associations
Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
615537Reticulate acropigmentation of Kitamura (RAK)
615590Alzheimer disease 18 (AD18)
Kegg Drug
D09320 Aderbasib (USAN/INN)
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of ADA10_HUMAN

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Related Literatures of Post-Translational Modification
N-linked Glycosylation
ReferencePubMed
"Mass-spectrometric identification and relative quantification of N-linked cell surface glycoproteins.";
Wollscheid B., Bausch-Fluck D., Henderson C., O'Brien R., Bibel M.,Schiess R., Aebersold R., Watts J.D.;
Nat. Biotechnol. 27:378-386(2009).
Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-278, AND MASSSPECTROMETRY.
"Glycoproteomics analysis of human liver tissue by combination ofmultiple enzyme digestion and hydrazide chemistry.";
Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.;
J. Proteome Res. 8:651-661(2009).
Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-278, AND MASSSPECTROMETRY.
"Elucidation of N-glycosylation sites on human platelet proteins: aglycoproteomic approach.";
Lewandrowski U., Moebius J., Walter U., Sickmann A.;
Mol. Cell. Proteomics 5:226-233(2006).
Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-278, AND MASSSPECTROMETRY.

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