ADA23_HUMAN - dbPTM
ADA23_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID ADA23_HUMAN
UniProt AC O75077
Protein Name Disintegrin and metalloproteinase domain-containing protein 23
Gene Name ADAM23
Organism Homo sapiens (Human).
Sequence Length 832
Subcellular Localization Cell membrane
Single-pass type I membrane protein .
Isoform Gamma: Secreted.
Protein Description May play a role in cell-cell and cell-matrix interactions. This is a non-catalytic metalloprotease-like protein..
Protein Sequence MKPPGSSSRQPPLAGCSLAGASCGPQRGPAGSVPASAPARTPPCRLLLVLLLLPPLAASSRPRAWGAAAPSAPHWNETAEKNLGVLADEDNTLQQNSSSNISYSNAMQKEITLPSRLIYYINQDSESPYHVLDTKARHQQKHNKAVHLAQASFQIEAFGSKFILDLILNNGLLSSDYVEIHYENGKPQYSKGGEHCYYHGSIRGVKDSKVALSTCNGLHGMFEDDTFVYMIEPLELVHDEKSTGRPHIIQKTLAGQYSKQMKNLTMERGDQWPFLSELQWLKRRKRAVNPSRGIFEEMKYLELMIVNDHKTYKKHRSSHAHTNNFAKSVVNLVDSIYKEQLNTRVVLVAVETWTEKDQIDITTNPVQMLHEFSKYRQRIKQHADAVHLISRVTFHYKRSSLSYFGGVCSRTRGVGVNEYGLPMAVAQVLSQSLAQNLGIQWEPSSRKPKCDCTESWGGCIMEETGVSHSRKFSKCSILEYRDFLQRGGGACLFNRPTKLFEPTECGNGYVEAGEECDCGFHVECYGLCCKKCSLSNGAHCSDGPCCNNTSCLFQPRGYECRDAVNECDITEYCTGDSGQCPPNLHKQDGYACNQNQGRCYNGECKTRDNQCQYIWGTKAAGSDKFCYEKLNTEGTEKGNCGKDGDRWIQCSKHDVFCGFLLCTNLTRAPRIGQLQGEIIPTSFYHQGRVIDCSGAHVVLDDDTDVGYVEDGTPCGPSMMCLDRKCLQIQALNMSSCPLDSKGKVCSGHGVCSNEATCICDFTWAGTDCSIRDPVRNLHPPKDEGPKGPSATNLIIGSIAGAILVAAIVLGGTGWGFKNVKKRRFDPTQQGPI
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
76N-linked_GlycosylationAPSAPHWNETAEKNL
CCCCCCCHHHHHHHH		33.44UniProtKB CARBOHYD
96N-linked_GlycosylationEDNTLQQNSSSNISY
CCCCCCCCCCCCCCC		30.79UniProtKB CARBOHYD
100N-linked_GlycosylationLQQNSSSNISYSNAM
CCCCCCCCCCCCHHH		29.22UniProtKB CARBOHYD
119PhosphorylationTLPSRLIYYINQDSE
CCCCEEEEEECCCCC		11.6850563433
127PhosphorylationYINQDSESPYHVLDT
EECCCCCCCEECCCH		34.4150563439
129PhosphorylationNQDSESPYHVLDTKA
CCCCCCCEECCCHHH		17.5350563445
263N-linked_GlycosylationQYSKQMKNLTMERGD
HHHHHHHCCCCCCCC		35.09UniProtKB CARBOHYD
265PhosphorylationSKQMKNLTMERGDQW
HHHHHCCCCCCCCCC		26.7850563427
352PhosphorylationVVLVAVETWTEKDQI
EEEEEEECCCHHHCC		30.9672840355
354PhosphorylationLVAVETWTEKDQIDI
EEEEECCCHHHCCCC		40.3472840361
362PhosphorylationEKDQIDITTNPVQML
HHHCCCCCCCHHHHH		19.4426074081
363PhosphorylationKDQIDITTNPVQMLH
HHCCCCCCCHHHHHH		37.5526074081
373PhosphorylationVQMLHEFSKYRQRIK
HHHHHHHHHHHHHHH		26.2826074081
375PhosphorylationMLHEFSKYRQRIKQH
HHHHHHHHHHHHHHH		15.6926074081
393PhosphorylationVHLISRVTFHYKRSS
HHHHHHHHCEECCCC		12.0024719451
396PhosphorylationISRVTFHYKRSSLSY
HHHHHCEECCCCCCE		12.1411255591
399PhosphorylationVTFHYKRSSLSYFGG
HHCEECCCCCCEECC		31.3229449344
400PhosphorylationTFHYKRSSLSYFGGV
HCEECCCCCCEECCC		25.9329449344
402PhosphorylationHYKRSSLSYFGGVCS
EECCCCCCEECCCCC		21.9929449344
403PhosphorylationYKRSSLSYFGGVCSR
ECCCCCCEECCCCCC		16.1311255601
409PhosphorylationSYFGGVCSRTRGVGV
CEECCCCCCCCCCCC		33.9929449344
453PhosphorylationRKPKCDCTESWGGCI
CCCCCCCCCCCCCEE		21.5820836899
473PhosphorylationVSHSRKFSKCSILEY
CCCCCCCCCCCCHHH		35.4720836907
547N-linked_GlycosylationCSDGPCCNNTSCLFQ
CCCCCCCCCCCCCCC		62.62UniProtKB CARBOHYD
548N-linked_GlycosylationSDGPCCNNTSCLFQP
CCCCCCCCCCCCCCC		21.32UniProtKB CARBOHYD
664N-linked_GlycosylationCGFLLCTNLTRAPRI
HHHEEECCCCCCCCH		38.12UniProtKB CARBOHYD
707PhosphorylationDDDTDVGYVEDGTPC
CCCCCCEEECCCCCC		10.6616094384
732N-linked_GlycosylationCLQIQALNMSSCPLD
HEEEEECCCCCCCCC		31.16UniProtKB CARBOHYD
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

Oops, there are no upstream regulatory protein records of ADA23_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of ADA23_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 ADA23_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions

Oops, there are no PPI records of ADA23_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.
Regulatory Network of ADA23_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Quantitative phosphoproteome analysis using a dendrimer conjugationchemistry and tandem mass spectrometry.";
Tao W.A., Wollscheid B., O'Brien R., Eng J.K., Li X.-J.,Bodenmiller B., Watts J.D., Hood L., Aebersold R.;
Nat. Methods 2:591-598(2005).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-707, AND MASSSPECTROMETRY.

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