ATS10_HUMAN - dbPTM
ATS10_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID ATS10_HUMAN
UniProt AC Q9H324
Protein Name A disintegrin and metalloproteinase with thrombospondin motifs 10
Gene Name ADAMTS10
Organism Homo sapiens (Human).
Sequence Length 1103
Subcellular Localization Secreted, extracellular space, extracellular matrix .
Protein Description Metalloprotease that participate in microfibrils assembly. Microfibrils are extracellular matrix components occurring independently or along with elastin in the formation of elastic tissues..
Protein Sequence MAPACQILRWALALGLGLMFEVTHAFRSQDEFLSSLESYEIAFPTRVDHNGALLAFSPPPPRRQRRGTGATAESRLFYKVASPSTHFLLNLTRSSRLLAGHVSVEYWTREGLAWQRAARPHCLYAGHLQGQASTSHVAISTCGGLHGLIVADEEEYLIEPLHGGPKGSRSPEESGPHVVYKRSSLRHPHLDTACGVRDEKPWKGRPWWLRTLKPPPARPLGNETERGQPGLKRSVSRERYVETLVVADKMMVAYHGRRDVEQYVLAIMNIVAKLFQDSSLGSTVNILVTRLILLTEDQPTLEITHHAGKSLDSFCKWQKSIVNHSGHGNAIPENGVANHDTAVLITRYDICIYKNKPCGTLGLAPVGGMCERERSCSVNEDIGLATAFTIAHEIGHTFGMNHDGVGNSCGARGQDPAKLMAAHITMKTNPFVWSSCSRDYITSFLDSGLGLCLNNRPPRQDFVYPTVAPGQAYDADEQCRFQHGVKSRQCKYGEVCSELWCLSKSNRCITNSIPAAEGTLCQTHTIDKGWCYKRVCVPFGSRPEGVDGAWGPWTPWGDCSRTCGGGVSSSSRHCDSPRPTIGGKYCLGERRRHRSCNTDDCPPGSQDFREVQCSEFDSIPFRGKFYKWKTYRGGGVKACSLTCLAEGFNFYTERAAAVVDGTPCRPDTVDICVSGECKHVGCDRVLGSDLREDKCRVCGGDGSACETIEGVFSPASPGAGYEDVVWIPKGSVHIFIQDLNLSLSHLALKGDQESLLLEGLPGTPQPHRLPLAGTTFQLRQGPDQVQSLEALGPINASLIVMVLARTELPALRYRFNAPIARDSLPPYSWHYAPWTKCSAQCAGGSQVQAVECRNQLDSSAVAPHYCSAHSKLPKRQRACNTEPCPPDWVVGNWSLCSRSCDAGVRSRSVVCQRRVSAAEEKALDDSACPQPRPPVLEACHGPTCPPEWAALDWSECTPSCGPGLRHRVVLCKSADHRATLPPAHCSPAAKPPATMRCNLRRCPPARWVAGEWGECSAQCGVGQRQRSVRCTSHTGQASHECTEALRPPTTQQCEAKCDSPTPGDGPEECKDVNKVAYCPLVLKFQFCSRAYFRQMCCKTCHGH
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
4 (in isoform 2)Phosphorylation-12.6127135362
5 (in isoform 2)Phosphorylation-2.2327135362
38 (in isoform 2)Phosphorylation-33.1022210691
57PhosphorylationNGALLAFSPPPPRRQ
CCEEEEECCCCCCCC		30.7823186163
66 (in isoform 2)Phosphorylation-38.3922210691
68PhosphorylationPRRQRRGTGATAESR
CCCCCCCCCCCHHHH		23.1046159177
71PhosphorylationQRRGTGATAESRLFY
CCCCCCCCHHHHHEE		32.1046159183
74PhosphorylationGTGATAESRLFYKVA
CCCCCHHHHHEEEEC		31.6414894181
75 (in isoform 2)Phosphorylation-21.9622210691
90N-linked_GlycosylationPSTHFLLNLTRSSRL
CCHHHHHHCCHHHHH		41.32UniProtKB CARBOHYD
222N-linked_GlycosylationPPARPLGNETERGQP
CCCCCCCCCCCCCCC		61.78UniProtKB CARBOHYD
234PhosphorylationGQPGLKRSVSRERYV
CCCCCCCCCCHHHHH		23.9028348404
240PhosphorylationRSVSRERYVETLVVA
CCCCHHHHHHHHHHH		9.6311232757
254PhosphorylationADKMMVAYHGRRDVE
HCEEEHHHCCCCCHH		8.0611232767
278PhosphorylationVAKLFQDSSLGSTVN
HHHHHCCCCCHHHHH		19.3846159147
279PhosphorylationAKLFQDSSLGSTVNI
HHHHCCCCCHHHHHH		45.0746159153
282PhosphorylationFQDSSLGSTVNILVT
HCCCCCHHHHHHHHH		34.1846159159
283PhosphorylationQDSSLGSTVNILVTR
CCCCCHHHHHHHHHH		18.7746159171
320PhosphorylationSFCKWQKSIVNHSGH
HHHHHHHHHHCCCCC		19.3719369195
323N-linked_GlycosylationKWQKSIVNHSGHGNA
HHHHHHHCCCCCCCC		23.18UniProtKB CARBOHYD
510PhosphorylationSKSNRCITNSIPAAE
ECCCCEECCCCCCCC		26.9222210691
519PhosphorylationSIPAAEGTLCQTHTI
CCCCCCCCEEEEEEE		18.8322210691
541PhosphorylationRVCVPFGSRPEGVDG
EEEEECCCCCCCCCC		45.0726074081
554PhosphorylationDGAWGPWTPWGDCSR
CCCCCCCCCCCCCCC		16.5826074081
560PhosphorylationWTPWGDCSRTCGGGV
CCCCCCCCCCCCCCC		35.0526074081
595PhosphorylationGERRRHRSCNTDDCP
CCCCCCCCCCCCCCC		12.9522210691
605PhosphorylationTDDCPPGSQDFREVQ
CCCCCCCCCCCCEEE		32.1422210691
740N-linked_GlycosylationHIFIQDLNLSLSHLA
EEEEEECCCCHHHHH		35.55UniProtKB CARBOHYD
795N-linked_GlycosylationLEALGPINASLIVMV
HHHHCCCCHHHHHHH		26.98UniProtKB CARBOHYD
892N-linked_GlycosylationPPDWVVGNWSLCSRS
CCCCEEECHHHCCCC		17.35UniProtKB CARBOHYD
908PhosphorylationDAGVRSRSVVCQRRV
CCCCCCHHHHHHHCC		21.8322210691
1050PhosphorylationEALRPPTTQQCEAKC
HHCCCCCCCCCHHCC		23.5546159165
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 ATS10_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of ATS10_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 ATS10_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions

Oops, there are no PPI records of ATS10_HUMAN !!
Drug and Disease Associations
Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
277600Weill-Marchesani syndrome 1 (WMS1)
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of ATS10_HUMAN

loading...

Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Large-scale proteomics analysis of the human kinome.";
Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G.,Mann M., Daub H.;
Mol. Cell. Proteomics 8:1751-1764(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-74, AND MASSSPECTROMETRY.

TOP
© 2024 Institute of Bioinformatics and Systems Biology, NYCU | Designed by : BiOmics Laboratory