ADA22_MOUSE - dbPTM
ADA22_MOUSE - PTM Information in dbPTM
Basic Information of Protein
UniProt ID ADA22_MOUSE
UniProt AC Q9R1V6
Protein Name Disintegrin and metalloproteinase domain-containing protein 22
Gene Name Adam22
Organism Mus musculus (Mouse).
Sequence Length 904
Subcellular Localization Membrane
Single-pass type I membrane protein . Cell projection, axon .
Protein Description Probable ligand for integrin in the brain. This is a non catalytic metalloprotease-like protein. Involved in regulation of cell adhesion and spreading and in inhibition of cell proliferation (By similarity). Neuronal receptor for LGI1..
Protein Sequence MQAAAAASFWLLCVLGTCPLARCGRAGVASLKGLERGKENRFLERQSIIPLRLIYRLGGEDETQHNQLDTRVRGDPGGPQLTHVDKASFRVDAFGTSFVLDVLLNHELLSSGYVERQIEHGGKVVENKGGEHCYYQGQIRGNPVSFVALSTCHGLHGMFYDGNHTYLIEPEENEKSQESSHCHSVYKSRQFEFPLDDLPSEFQRVNITPPQFILKPRLKRRKRQLLRFPRNVEEETKYIELMIVNDHLMFKKHRLSVVYTNTYAKSVVNMADVIYKDQLKTRIVLVAMETWAADNKFAISENPLITLREFMKYRRDFIKEKADAVHLFSGSQFESSRSGAAYIGGICSLLRGGGVNEFGKTDLMAVTLAQSLAHNVGIISDKRKLASGECKCEDTWSGCIMGDTGYYLPKKFTQCNVEEYHDFLNSGGGACLFNKPSKLLDPPECGNGFIETGEECDCGTPAECALEGAECCKKCTLTQDSQCSDGLCCKKCKFQPLGTVCREAVNDCDIREICSGNSSQCAPNVHKMDGYSCDGTQGICFGGRCKTRDRQCKYIWGQKVTASDRYCYEKLNIEGTEKGNCGKDKDTWTQCNKRDVLCGYLLCTNIGNIPRLGELDGEITSTLVVQQGRTLNCSGAHVKLEEDVDLGYVEDGTPCGPQMMCLEHRCLPVASFNFSTCSSSKAGTVCSGNGVCSNELKCVCNRHWTGADCGTHFPHNDDAKTGITLSGNGVAGTNIIIGIIAGTILVLALILGITAWGYKNYREQRQLPQGDYVKKPGDGDSFYSDFPPGGSTNSASSSKKRSNGLSHSWSERIPDTKHISDICENGRPRSNSWQGNMGGNKKKIRGKRFRPRSNSTETLSPAKSPSSSTGSIASSRKYPYPMPPLPDEGKTAGRQSARLWETSI
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
23S-nitrosylationGTCPLARCGRAGVAS
CCCCHHHCCCCHHHH
3.4421278135
23S-nitrosocysteineGTCPLARCGRAGVAS
CCCCHHHCCCCHHHH
3.44-
163N-linked_GlycosylationHGMFYDGNHTYLIEP
EEEEECCCEEEEECC
22.79-
367PhosphorylationKTDLMAVTLAQSLAH
CCHHHHHHHHHHHHH
13.5620047950
387PhosphorylationSDKRKLASGECKCED
CCCCHHHCCCCCCCC
45.6320415495
517N-linked_GlycosylationIREICSGNSSQCAPN
HHHHCCCCCCCCCCC
23.38-
632N-linked_GlycosylationVQQGRTLNCSGAHVK
EECCCEEECCCCEEE
19.80-
673N-linked_GlycosylationCLPVASFNFSTCSSS
EEEEEEEECCCCCCC
27.71-
772PhosphorylationRQLPQGDYVKKPGDG
HCCCCCCCCCCCCCC
22.4629514104
781PhosphorylationKKPGDGDSFYSDFPP
CCCCCCCCCCCCCCC
31.4525521595
783PhosphorylationPGDGDSFYSDFPPGG
CCCCCCCCCCCCCCC
15.9825521595
784PhosphorylationGDGDSFYSDFPPGGS
CCCCCCCCCCCCCCC
30.6622807455
798PhosphorylationSTNSASSSKKRSNGL
CCCCCCCCCCCCCCC
39.4451458265
802PhosphorylationASSSKKRSNGLSHSW
CCCCCCCCCCCCCCH
44.0921183079
806PhosphorylationKKRSNGLSHSWSERI
CCCCCCCCCCHHHCC
19.5122324799
808PhosphorylationRSNGLSHSWSERIPD
CCCCCCCCHHHCCCC
28.9922324799
810PhosphorylationNGLSHSWSERIPDTK
CCCCCCHHHCCCCCC
21.7322324799
814 (in isoform 6)Phosphorylation-49.8220047950
816PhosphorylationWSERIPDTKHISDIC
HHHCCCCCCCHHHHH
21.1122324799
817 (in isoform 10)Phosphorylation-46.4525521595
817 (in isoform 17)Phosphorylation-46.4529899451
817 (in isoform 11)Ubiquitination-46.4522790023
817UbiquitinationSERIPDTKHISDICE
HHCCCCCCCHHHHHH
46.4522790023
819 (in isoform 17)Phosphorylation-4.1629899451
819 (in isoform 10)Phosphorylation-4.1625521595
820 (in isoform 17)Phosphorylation-22.2029899451
820 (in isoform 7)Phosphorylation-22.2020047950
820 (in isoform 10)Phosphorylation-22.2025521595
820PhosphorylationIPDTKHISDICENGR
CCCCCCHHHHHHCCC
22.2022324799
822 (in isoform 10)Phosphorylation-2.2420415495
830PhosphorylationCENGRPRSNSWQGNM
HHCCCCCCCCCCCCC
37.5925521595
832PhosphorylationNGRPRSNSWQGNMGG
CCCCCCCCCCCCCCC
23.2525521595
853PhosphorylationGKRFRPRSNSTETLS
CCCCCCCCCCCCCCC
37.5022324799
855PhosphorylationRFRPRSNSTETLSPA
CCCCCCCCCCCCCCC
28.9425521595
856PhosphorylationFRPRSNSTETLSPAK
CCCCCCCCCCCCCCC
36.9225521595
856 (in isoform 8)Phosphorylation-36.9220047950
858PhosphorylationPRSNSTETLSPAKSP
CCCCCCCCCCCCCCC
32.4022324799
860PhosphorylationSNSTETLSPAKSPSS
CCCCCCCCCCCCCCC
30.1725521595
864PhosphorylationETLSPAKSPSSSTGS
CCCCCCCCCCCCCCC
31.9225521595
866PhosphorylationLSPAKSPSSSTGSIA
CCCCCCCCCCCCCCC
43.9725521595
867PhosphorylationSPAKSPSSSTGSIAS
CCCCCCCCCCCCCCC
34.9922324799
868PhosphorylationPAKSPSSSTGSIASS
CCCCCCCCCCCCCCC
40.9225521595
869PhosphorylationAKSPSSSTGSIASSR
CCCCCCCCCCCCCCC
36.5822324799
871PhosphorylationSPSSSTGSIASSRKY
CCCCCCCCCCCCCCC
18.3125521595
874PhosphorylationSSTGSIASSRKYPYP
CCCCCCCCCCCCCCC
29.0722324799
875PhosphorylationSTGSIASSRKYPYPM
CCCCCCCCCCCCCCC
24.6222324799
882 (in isoform 14)Phosphorylation-4.3825521595
884 (in isoform 14)Phosphorylation-50.7225521595
885 (in isoform 14)Phosphorylation-7.4225521595
887 (in isoform 14)Phosphorylation-82.2120415495
918 (in isoform 14)Phosphorylation-21183079
926 (in isoform 11)Phosphorylation-21183079

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 ADA22_MOUSE !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of ADA22_MOUSE !!

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 ADA22_MOUSE !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions

Oops, there are no PPI records of ADA22_MOUSE !!

Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of ADA22_MOUSE

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Qualitative and quantitative analyses of protein phosphorylation innaive and stimulated mouse synaptosomal preparations.";
Munton R.P., Tweedie-Cullen R., Livingstone-Zatchej M., Weinandy F.,Waidelich M., Longo D., Gehrig P., Potthast F., Rutishauser D.,Gerrits B., Panse C., Schlapbach R., Mansuy I.M.;
Mol. Cell. Proteomics 6:283-293(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-832; SER-864 ANDSER-866, AND MASS SPECTROMETRY.

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