ADA22_HUMAN - dbPTM
ADA22_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID ADA22_HUMAN
UniProt AC Q9P0K1
Protein Name Disintegrin and metalloproteinase domain-containing protein 22
Gene Name ADAM22
Organism Homo sapiens (Human).
Sequence Length 906
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. [PubMed: 19692335 Involved in regulation of cell adhesion and spreading and in inhibition of cell proliferation. Neuronal receptor for LGI1.]
Protein Sequence MQAAVAVSVPFLLLCVLGTCPPARCGQAGDASLMELEKRKENRFVERQSIVPLRLIYRSGGEDESRHDALDTRVRGDLGGPQLTHVDQASFQVDAFGTSFILDVVLNHDLLSSEYIERHIEHGGKTVEVKGGEHCYYQGHIRGNPDSFVALSTCHGLHGMFYDGNHTYLIEPEENDTTQEDFHFHSVYKSRLFEFSLDDLPSEFQQVNITPSKFILKPRPKRSKRQLRRYPRNVEEETKYIELMIVNDHLMFKKHRLSVVHTNTYAKSVVNMADLIYKDQLKTRIVLVAMETWATDNKFAISENPLITLREFMKYRRDFIKEKSDAVHLFSGSQFESSRSGAAYIGGICSLLKGGGVNEFGKTDLMAVTLAQSLAHNIGIISDKRKLASGECKCEDTWSGCIMGDTGYYLPKKFTQCNIEEYHDFLNSGGGACLFNKPSKLLDPPECGNGFIETGEECDCGTPAECVLEGAECCKKCTLTQDSQCSDGLCCKKCKFQPMGTVCREAVNDCDIRETCSGNSSQCAPNIHKMDGYSCDGVQGICFGGRCKTRDRQCKYIWGQKVTASDKYCYEKLNIEGTEKGNCGKDKDTWIQCNKRDVLCGYLLCTNIGNIPRLGELDGEITSTLVVQQGRTLNCSGGHVKLEEDVDLGYVEDGTPCGPQMMCLEHRCLPVASFNFSTCLSSKEGTICSGNGVCSNELKCVCNRHWIGSDCNTYFPHNDDAKTGITLSGNGVAGTNIIIGIIAGTILVLALILGITAWGYKNYREQRQLPQGDYVKKPGDGDSFYSDIPPGVSTNSASSSKKRSNGLSHSWSERIPDTKHISDICENGRPRSNSWQGNLGGNKKKIRGKRFRPRSNSTETLSPAKSPSSSTGSIASSRKYPYPMPPLPDEDKKVNRQSARLWETSI
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
32PhosphorylationCGQAGDASLMELEKR
CCCCCCHHHHHHHHH		32.7550559019
57PhosphorylationIVPLRLIYRSGGEDE
CCEEEEEECCCCCCH		11.88-
175N-linked_GlycosylationYLIEPEENDTTQEDF
EEECCCCCCCCCCCC		50.71UniProtKB CARBOHYD
262PhosphorylationHRLSVVHTNTYAKSV
CCEEEEECHHHHHHH		20.0446501629
264PhosphorylationLSVVHTNTYAKSVVN
EEEEECHHHHHHHCC		26.4746501631
283PhosphorylationIYKDQLKTRIVLVAM
HCHHHHCCCEEEEEE		33.9325954137
292PhosphorylationIVLVAMETWATDNKF
EEEEEEEECCCCCCC		13.8125954137
295PhosphorylationVAMETWATDNKFAIS
EEEEECCCCCCCCCC		31.5025954137
302PhosphorylationTDNKFAISENPLITL
CCCCCCCCCCCCCHH		28.0850559013
308PhosphorylationISENPLITLREFMKY
CCCCCCCHHHHHHHH		27.6950559025
324PhosphorylationRDFIKEKSDAVHLFS
HHHHHHCCCEEEECC		31.7125022875
331PhosphorylationSDAVHLFSGSQFESS
CCEEEECCCCCCCCC		43.8425022875
333PhosphorylationAVHLFSGSQFESSRS
EEEECCCCCCCCCCC		30.4225022875
337PhosphorylationFSGSQFESSRSGAAY
CCCCCCCCCCCCCHH		32.1325022875
338PhosphorylationSGSQFESSRSGAAYI
CCCCCCCCCCCCHHH		24.2225022875
340PhosphorylationSQFESSRSGAAYIGG
CCCCCCCCCCHHHHH		34.4325022875
344PhosphorylationSSRSGAAYIGGICSL
CCCCCCHHHHHHHHH		10.2825022875
350PhosphorylationAYIGGICSLLKGGGV
HHHHHHHHHHCCCCC		34.5124719451
519N-linked_GlycosylationIRETCSGNSSQCAPN
CCHHHCCCCCCCCCC		23.3819692335
556PhosphorylationTRDRQCKYIWGQKVT
CCCCCCCCCCCCCCC		14.9959304967
565PhosphorylationWGQKVTASDKYCYEK
CCCCCCCCCCCCHHH		25.8522461510
634N-linked_GlycosylationVQQGRTLNCSGGHVK
EECCCEEECCCCEEE		19.8019692335
675N-linked_GlycosylationCLPVASFNFSTCLSS
EEEEEEEECCHHCCC		27.7119692335
689PhosphorylationSKEGTICSGNGVCSN
CCCCEEECCCCCCCC		31.2928985074
695PhosphorylationCSGNGVCSNELKCVC
ECCCCCCCCCEEEEE		30.8228985074
798 (in isoform 4)Phosphorylation-34.66-
798 (in isoform 5)Phosphorylation-34.66-
798PhosphorylationGVSTNSASSSKKRSN
CCCCCCCCCCCCCCC		34.6619664994
804PhosphorylationASSSKKRSNGLSHSW
CCCCCCCCCCCCCCH		44.0923312004
808PhosphorylationKKRSNGLSHSWSERI
CCCCCCCCCCHHHCC		19.5123312004
810PhosphorylationRSNGLSHSWSERIPD
CCCCCCCCHHHCCCC		28.9923312004
812PhosphorylationNGLSHSWSERIPDTK
CCCCCCHHHCCCCCC		21.7321712546
818PhosphorylationWSERIPDTKHISDIC
HHHCCCCCCCHHHHH		21.1123312004
819 (in isoform 2)Phosphorylation-46.4525884760
821 (in isoform 2)Phosphorylation-4.1628102081
822 (in isoform 2)Phosphorylation-22.2024117733
822PhosphorylationIPDTKHISDICENGR
CCCCCCHHHHHHCCC		22.2046501633
824 (in isoform 2)Phosphorylation-2.2429978859
832PhosphorylationCENGRPRSNSWQGNL
HHCCCCCCCCCCCCC		37.5922167270
833 (in isoform 5)Phosphorylation-48.85-
833 (in isoform 2)Phosphorylation-48.8525884760
834PhosphorylationNGRPRSNSWQGNLGG
CCCCCCCCCCCCCCC		23.2519664994
834 (in isoform 3)Phosphorylation-23.25-
834 (in isoform 5)Phosphorylation-23.25-
846 (in isoform 2)Phosphorylation-10.8925332170
850 (in isoform 2)Phosphorylation-35.3125884760
855PhosphorylationGKRFRPRSNSTETLS
CCCCCCCCCCCCCCC		37.5022115753
855 (in isoform 2)Phosphorylation-37.5025307156
857PhosphorylationRFRPRSNSTETLSPA
CCCCCCCCCCCCCCC		28.9427273156
858PhosphorylationFRPRSNSTETLSPAK
CCCCCCCCCCCCCCC		36.9229255136
859 (in isoform 2)Phosphorylation-47.8025307156
860PhosphorylationPRSNSTETLSPAKSP
CCCCCCCCCCCCCCC		32.4022115753
862PhosphorylationSNSTETLSPAKSPSS
CCCCCCCCCCCCCCC		30.1729396449
862 (in isoform 2)Phosphorylation-30.1725627689
863 (in isoform 2)Phosphorylation-46.9825159151
864 (in isoform 2)Phosphorylation-22.9125159151
866 (in isoform 2)Phosphorylation-31.9225159151
866PhosphorylationETLSPAKSPSSSTGS
CCCCCCCCCCCCCCC		31.9220363803
868PhosphorylationLSPAKSPSSSTGSIA
CCCCCCCCCCCCCCC		43.9727732954
869PhosphorylationSPAKSPSSSTGSIAS
CCCCCCCCCCCCCCC		34.9920363803
870PhosphorylationPAKSPSSSTGSIASS
CCCCCCCCCCCCCCC		40.9220363803
871PhosphorylationAKSPSSSTGSIASSR
CCCCCCCCCCCCCCC		36.5825159151
873PhosphorylationSPSSSTGSIASSRKY
CCCCCCCCCCCCCCC		18.3128985074
876PhosphorylationSSTGSIASSRKYPYP
CCCCCCCCCCCCCCC		29.0728985074
877PhosphorylationSTGSIASSRKYPYPM
CCCCCCCCCCCCCCC		24.6224114839
880PhosphorylationSIASSRKYPYPMPPL
CCCCCCCCCCCCCCC		13.5972491
882PhosphorylationASSRKYPYPMPPLPD
CCCCCCCCCCCCCCC		14.7472493
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_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of ADA22_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 ADA22_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
DLG4_HUMANDLG4physical
16990550
LGI1_HUMANLGI1physical
16990550
EPS8_HUMANEPS8physical
21988832
RAC2_HUMANRAC2physical
21988832
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 ADA22_HUMAN

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Related Literatures of Post-Translational Modification
N-linked Glycosylation
ReferencePubMed
"Structural characterization of the ectodomain of a disintegrin andmetalloproteinase-22 (ADAM22), a neural adhesion receptor instead ofmetalloproteinase: insights on ADAM function.";
Liu H., Shim A.H., He X.;
J. Biol. Chem. 284:29077-29086(2009).
Cited for: X-RAY CRYSTALLOGRAPHY (2.36 ANGSTROMS) OF 233-736, GLYCOSYLATION ATASN-519; ASN-634 AND ASN-675, AND DISULFIDE BONDS.
Phosphorylation
ReferencePubMed
"Lys-N and trypsin cover complementary parts of the phosphoproteome ina refined SCX-based approach.";
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,Mohammed S.;
Anal. Chem. 81:4493-4501(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-834; SER-869 ANDSER-870, AND MASS SPECTROMETRY.

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