ADAM9_HUMAN - dbPTM
ADAM9_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID ADAM9_HUMAN
UniProt AC Q13443
Protein Name Disintegrin and metalloproteinase domain-containing protein 9
Gene Name ADAM9
Organism Homo sapiens (Human).
Sequence Length 819
Subcellular Localization Isoform 1: Cell membrane
Single-pass type I membrane protein .
Isoform 2: Secreted .
Protein Description Cleaves and releases a number of molecules with important roles in tumorigenesis and angiogenesis, such as TEK, KDR, EPHB4, CD40, VCAM1 and CDH5. May mediate cell-cell, cell-matrix interactions and regulate the motility of cells via interactions with integrins.; Isoform 2: May act as alpha-secretase for amyloid precursor protein (APP)..
Protein Sequence MGSGARFPSGTLRVRWLLLLGLVGPVLGAARPGFQQTSHLSSYEIITPWRLTRERREAPRPYSKQVSYVIQAEGKEHIIHLERNKDLLPEDFVVYTYNKEGTLITDHPNIQNHCHYRGYVEGVHNSSIALSDCFGLRGLLHLENASYGIEPLQNSSHFEHIIYRMDDVYKEPLKCGVSNKDIEKETAKDEEEEPPSMTQLLRRRRAVLPQTRYVELFIVVDKERYDMMGRNQTAVREEMILLANYLDSMYIMLNIRIVLVGLEIWTNGNLINIVGGAGDVLGNFVQWREKFLITRRRHDSAQLVLKKGFGGTAGMAFVGTVCSRSHAGGINVFGQITVETFASIVAHELGHNLGMNHDDGRDCSCGAKSCIMNSGASGSRNFSSCSAEDFEKLTLNKGGNCLLNIPKPDEAYSAPSCGNKLVDAGEECDCGTPKECELDPCCEGSTCKLKSFAECAYGDCCKDCRFLPGGTLCRGKTSECDVPEYCNGSSQFCQPDVFIQNGYPCQNNKAYCYNGMCQYYDAQCQVIFGSKAKAAPKDCFIEVNSKGDRFGNCGFSGNEYKKCATGNALCGKLQCENVQEIPVFGIVPAIIQTPSRGTKCWGVDFQLGSDVPDPGMVNEGTKCGAGKICRNFQCVDASVLNYDCDVQKKCHGHGVCNSNKNCHCENGWAPPNCETKGYGGSVDSGPTYNEMNTALRDGLLVFFFLIVPLIVCAIFIFIKRDQLWRSYFRKKRSQTYESDGKNQANPSRQPGSVPRHVSPVTPPREVPIYANRFAVPTYAAKQPQQFPSRPPPPQPKVSSQGNLIPARPAPAPPLYSSLT
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
3Phosphorylation-----MGSGARFPSG
-----CCCCCCCCCH		28.1629759185
11PhosphorylationGARFPSGTLRVRWLL
CCCCCCHHHHHHHHH		18.7429759185
85UbiquitinationIIHLERNKDLLPEDF
EEEEECCCCCCCCCE		56.8529967540
125N-linked_GlycosylationGYVEGVHNSSIALSD
CCCCCCCCCCEEHHH		34.74UniProtKB CARBOHYD
144N-linked_GlycosylationRGLLHLENASYGIEP
HHHEEECCCCCCCCC		40.31UniProtKB CARBOHYD
154N-linked_GlycosylationYGIEPLQNSSHFEHI
CCCCCCCCCCCHHHE		53.84UniProtKB CARBOHYD
184AcetylationVSNKDIEKETAKDEE
CCHHHHHHHHCCCCC		61.787664399
186PhosphorylationNKDIEKETAKDEEEE
HHHHHHHHCCCCCCC		50.5029083192
188AcetylationDIEKETAKDEEEEPP
HHHHHHCCCCCCCCC		73.437664409
196PhosphorylationDEEEEPPSMTQLLRR
CCCCCCCCHHHHHHH		45.2229083192
198PhosphorylationEEEPPSMTQLLRRRR
CCCCCCHHHHHHHHH		22.0229083192
213PhosphorylationAVLPQTRYVELFIVV
CCCCCCCEEEEEEEE		11.1519664994
231N-linked_GlycosylationRYDMMGRNQTAVREE
HHHCCCCCHHHHHHH		37.51UniProtKB CARBOHYD
250PhosphorylationANYLDSMYIMLNIRI
HHHHHHHHHHHHCHH		6.27108417707
272UbiquitinationWTNGNLINIVGGAGD
ECCCCEEEECCCHHH		26.5127667366
290UbiquitinationNFVQWREKFLITRRR
HHHHHHHHHEEEECC		36.5827667366
292UbiquitinationVQWREKFLITRRRHD
HHHHHHHEEEECCCC		6.0627667366
3062-HydroxyisobutyrylationDSAQLVLKKGFGGTA
CCCEEEECCCCCCCC		43.29-
350UbiquitinationSIVAHELGHNLGMNH
HHHHHHHHHHCCCCC		12.4921963094
364PhosphorylationHDDGRDCSCGAKSCI
CCCCCCCCCCCCEEE		21.6368727765
368UbiquitinationRDCSCGAKSCIMNSG
CCCCCCCCEEECCCC		31.0121963094
370UbiquitinationCSCGAKSCIMNSGAS
CCCCCCEEECCCCCC		3.1821963094
377PhosphorylationCIMNSGASGSRNFSS
EECCCCCCCCCCCCC		40.6168727771
379PhosphorylationMNSGASGSRNFSSCS
CCCCCCCCCCCCCCC		22.8968727777
381N-linked_GlycosylationSGASGSRNFSSCSAE
CCCCCCCCCCCCCHH		42.73UniProtKB CARBOHYD
392UbiquitinationCSAEDFEKLTLNKGG
CCHHHHHHCEECCCC		46.9229967540
397UbiquitinationFEKLTLNKGGNCLLN
HHHCEECCCCCEEEC		71.9029967540
450UbiquitinationEGSTCKLKSFAECAY
CCCCCCCCCHHHHHC		29.0829967540
451PhosphorylationGSTCKLKSFAECAYG
CCCCCCCCHHHHHCC		39.8868701621
457PhosphorylationKSFAECAYGDCCKDC
CCHHHHHCCCCCCCC		25.7568701627
487N-linked_GlycosylationCDVPEYCNGSSQFCQ
CCCCHHCCCCCCCCC		53.10UniProtKB CARBOHYD
533AcetylationVIFGSKAKAAPKDCF
EEECCCCCCCCCCCE		49.1430586751
545PhosphorylationDCFIEVNSKGDRFGN
CCEEEECCCCCCCCC		43.1023879269
546UbiquitinationCFIEVNSKGDRFGNC
CEEEECCCCCCCCCC		60.6829967540
561UbiquitinationGFSGNEYKKCATGNA
CCCCCHHCCCCCCCC		34.8929967540
723UbiquitinationIFIKRDQLWRSYFRK
HHHHHHHHHHHHHHH		4.8727667366
733PhosphorylationSYFRKKRSQTYESDG
HHHHHHCCCCCCCCC		35.4428985074
735PhosphorylationFRKKRSQTYESDGKN
HHHHCCCCCCCCCCC		30.4228796482
736PhosphorylationRKKRSQTYESDGKNQ
HHHCCCCCCCCCCCC		13.0521712546
738PhosphorylationKRSQTYESDGKNQAN
HCCCCCCCCCCCCCC		41.0528796482
741 (in isoform 1)Ubiquitination-51.3721906983
741UbiquitinationQTYESDGKNQANPSR
CCCCCCCCCCCCCCC		51.3721906983
743UbiquitinationYESDGKNQANPSRQP
CCCCCCCCCCCCCCC		46.1027667366
747PhosphorylationGKNQANPSRQPGSVP
CCCCCCCCCCCCCCC		43.2730576142
752PhosphorylationNPSRQPGSVPRHVSP
CCCCCCCCCCCCCCC		35.3130266825
758O-linked_GlycosylationGSVPRHVSPVTPPRE
CCCCCCCCCCCCCCC		13.9220068231
758PhosphorylationGSVPRHVSPVTPPRE
CCCCCCCCCCCCCCC		13.9229255136
761PhosphorylationPRHVSPVTPPREVPI
CCCCCCCCCCCCCCE		30.8429255136
761O-linked_GlycosylationPRHVSPVTPPREVPI
CCCCCCCCCCCCCCE		30.8420068231
763UbiquitinationHVSPVTPPREVPIYA
CCCCCCCCCCCCEEC		35.3823000965
769PhosphorylationPPREVPIYANRFAVP
CCCCCCEECCCCCCC		7.5523927012
772MethylationEVPIYANRFAVPTYA
CCCEECCCCCCCCCC		16.84-
777PhosphorylationANRFAVPTYAAKQPQ
CCCCCCCCCCCCCCC		21.1321945579
777O-linked_GlycosylationANRFAVPTYAAKQPQ
CCCCCCCCCCCCCCC		21.1330814659
778PhosphorylationNRFAVPTYAAKQPQQ
CCCCCCCCCCCCCCC		9.8621945579
781UbiquitinationAVPTYAAKQPQQFPS
CCCCCCCCCCCCCCC		55.1023000965
781 (in isoform 1)Ubiquitination-55.1021906983
783UbiquitinationPTYAAKQPQQFPSRP
CCCCCCCCCCCCCCC		29.2723000965
796UbiquitinationRPPPPQPKVSSQGNL
CCCCCCCCCCCCCCE		49.8829967540
798PhosphorylationPPPQPKVSSQGNLIP
CCCCCCCCCCCCEEC		24.0721945579
799PhosphorylationPPQPKVSSQGNLIPA
CCCCCCCCCCCEECC		45.1321945579
815PhosphorylationPAPAPPLYSSLT---
CCCCCCCCCCCC---		11.2921945579
816PhosphorylationAPAPPLYSSLT----
CCCCCCCCCCC----		26.9321945579
817PhosphorylationPAPPLYSSLT-----
CCCCCCCCCC-----		23.5921945579
819PhosphorylationPPLYSSLT-------
CCCCCCCC-------		38.2121945579
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 ADAM9_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of ADAM9_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 ADAM9_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
MD2L2_HUMANMAD2L2physical
10527948
SNX9_HUMANSNX9physical
10531379
SH3G2_HUMANSH3GL2physical
10531379
KPCD_HUMANPRKCDphysical
9857183
Drug and Disease Associations
Kegg Disease
H00481 Cone-rod dystrophy and cone dystrophy, including: Cone-rod dystrophy (CORD); Cone dystrophy (COD); R
OMIM Disease
612775Cone-rod dystrophy 9 (CORD9)
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of ADAM9_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"A quantitative atlas of mitotic phosphorylation.";
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,Elledge S.J., Gygi S.P.;
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-758 AND THR-761, ANDMASS SPECTROMETRY.
"Global, in vivo, and site-specific phosphorylation dynamics insignaling networks.";
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,Mann M.;
Cell 127:635-648(2006).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-758 AND THR-761, ANDMASS SPECTROMETRY.
"An extensive survey of tyrosine phosphorylation revealing new sitesin human mammary epithelial cells.";
Heibeck T.H., Ding S.-J., Opresko L.K., Zhao R., Schepmoes A.A.,Yang F., Tolmachev A.V., Monroe M.E., Camp D.G. II, Smith R.D.,Wiley H.S., Qian W.-J.;
J. Proteome Res. 8:3852-3861(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-815, AND MASSSPECTROMETRY.
"Global survey of phosphotyrosine signaling identifies oncogenickinases in lung cancer.";
Rikova K., Guo A., Zeng Q., Possemato A., Yu J., Haack H., Nardone J.,Lee K., Reeves C., Li Y., Hu Y., Tan Z., Stokes M., Sullivan L.,Mitchell J., Wetzel R., Macneill J., Ren J.M., Yuan J.,Bakalarski C.E., Villen J., Kornhauser J.M., Smith B., Li D., Zhou X.,Gygi S.P., Gu T.-L., Polakiewicz R.D., Rush J., Comb M.J.;
Cell 131:1190-1203(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-815, AND MASSSPECTROMETRY.

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