CAPON_HUMAN - dbPTM
CAPON_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID CAPON_HUMAN
UniProt AC O75052
Protein Name Carboxyl-terminal PDZ ligand of neuronal nitric oxide synthase protein
Gene Name NOS1AP
Organism Homo sapiens (Human).
Sequence Length 506
Subcellular Localization
Protein Description Adapter protein involved in neuronal nitric-oxide (NO) synthesis regulation via its association with nNOS/NOS1. The complex formed with NOS1 and synapsins is necessary for specific NO and synapsin functions at a presynaptic level. Mediates an indirect interaction between NOS1 and RASD1 leading to enhance the ability of NOS1 to activate RASD1. Competes with DLG4 for interaction with NOS1, possibly affecting NOS1 activity by regulating the interaction between NOS1 and DLG4 (By similarity)..
Protein Sequence MPSKTKYNLVDDGHDLRIPLHNEDAFQHGICFEAKYVGSLDVPRPNSRVEIVAAMRRIRYEFKAKNIKKKKVSIMVSVDGVKVILKKKKKLLLLQKKEWTWDESKMLVMQDPIYRIFYVSHDSQDLKIFSYIARDGASNIFRCNVFKSKKKSQAMRIVRTVGQAFEVCHKLSLQHTQQNADGQEDGESERNSNSSGDPGRQLTGAERASTATAEETDIDAVEVPLPGNDVLEFSRGVTDLDAVGKEGGSHTGSKVSHPQEPMLTASPRMLLPSSSSKPPGLGTETPLSTHHQMQLLQQLLQQQQQQTQVAVAQVHLLKDQLAAEAAARLEAQARVHQLLLQNKDMLQHISLLVKQVQELELKLSGQNAMGSQDSLLEITFRSGALPVLCDPTTPKPEDLHSPPLGAGLADFAHPAGSPLGRRDCLVKLECFRFLPPEDTPPPAQGEALLGGLELIKFRESGIASEYESNTDESEERDSWSQEELPRLLNVLQRQELGDGLDDEIAV
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
5Phosphorylation---MPSKTKYNLVDD
---CCCCCCEECCCC		43.00-
6Ubiquitination--MPSKTKYNLVDDG
--CCCCCCEECCCCC		35.5629967540
7Phosphorylation-MPSKTKYNLVDDGH
-CCCCCCEECCCCCC		20.9627642862
36PhosphorylationGICFEAKYVGSLDVP
CEEEEEEEEEECCCC		19.6630576142
73PhosphorylationNIKKKKVSIMVSVDG
CCCCCCEEEEEEECC		17.5326437602
91UbiquitinationILKKKKKLLLLQKKE
EEECCCEEEEEECCC		5.8229967540
92UbiquitinationLKKKKKLLLLQKKEW
EECCCEEEEEECCCC		6.5229967540
96AcetylationKKLLLLQKKEWTWDE
CEEEEEECCCCCCCH		53.2621466224
97AcetylationKLLLLQKKEWTWDES
EEEEEECCCCCCCHH		45.5921466224
97UbiquitinationKLLLLQKKEWTWDES
EEEEEECCCCCCCHH		45.59-
100PhosphorylationLLQKKEWTWDESKML
EEECCCCCCCHHHEE		24.9127251275
114PhosphorylationLVMQDPIYRIFYVSH
EEECCCEEEEEEEEC		11.75-
138PhosphorylationYIARDGASNIFRCNV
EEECCCCCCCEECCC		35.6729978859
172PhosphorylationFEVCHKLSLQHTQQN
HHHHHHHHCHHCCCC		30.6827251275
176PhosphorylationHKLSLQHTQQNADGQ
HHHHCHHCCCCCCCC		20.9120873877
188PhosphorylationDGQEDGESERNSNSS
CCCCCCCCCCCCCCC		47.5922617229
192PhosphorylationDGESERNSNSSGDPG
CCCCCCCCCCCCCCC		44.2922617229
194PhosphorylationESERNSNSSGDPGRQ
CCCCCCCCCCCCCHH		35.2022617229
195PhosphorylationSERNSNSSGDPGRQL
CCCCCCCCCCCCHHC		52.0123898821
203PhosphorylationGDPGRQLTGAERAST
CCCCHHCCHHHHCCC		26.4723312004
209PhosphorylationLTGAERASTATAEET
CCHHHHCCCCCCCCC		25.4625849741
210PhosphorylationTGAERASTATAEETD
CHHHHCCCCCCCCCC		27.3525849741
212PhosphorylationAERASTATAEETDID
HHHCCCCCCCCCCCC		34.3925849741
216PhosphorylationSTATAEETDIDAVEV
CCCCCCCCCCCEEEC		29.7530278072
238PhosphorylationLEFSRGVTDLDAVGK
EEECCCCCCHHHCCC		33.4023312004
249PhosphorylationAVGKEGGSHTGSKVS
HCCCCCCCCCCCCCC		28.8224719451
251PhosphorylationGKEGGSHTGSKVSHP
CCCCCCCCCCCCCCC		44.8630624053
253PhosphorylationEGGSHTGSKVSHPQE
CCCCCCCCCCCCCCC		30.9223312004
256PhosphorylationSHTGSKVSHPQEPML
CCCCCCCCCCCCCCC		32.9423403867
259PhosphorylationGSKVSHPQEPMLTAS
CCCCCCCCCCCCCCC		63.1032142685
264PhosphorylationHPQEPMLTASPRMLL
CCCCCCCCCCCCEEC		20.8830266825
266PhosphorylationQEPMLTASPRMLLPS
CCCCCCCCCCEECCC		14.0630266825
350PhosphorylationKDMLQHISLLVKQVQ
HHHHHHHHHHHHHHH		17.3320068231
364PhosphorylationQELELKLSGQNAMGS
HHHHHHHCCCCCCCC		36.4230278072
371PhosphorylationSGQNAMGSQDSLLEI
CCCCCCCCCCCCHHH		20.1030278072
374PhosphorylationNAMGSQDSLLEITFR
CCCCCCCCCHHHEEC		27.5030278072
379PhosphorylationQDSLLEITFRSGALP
CCCCHHHEECCCCCC		12.0129396449
401PhosphorylationPKPEDLHSPPLGAGL
CCCHHCCCCCCCCCH		35.19-
417PhosphorylationDFAHPAGSPLGRRDC
HHCCCCCCCCCCCHH		21.03-
439PhosphorylationRFLPPEDTPPPAQGE
ECCCCCCCCCCHHHC		35.7127732954
460PhosphorylationELIKFRESGIASEYE
EEEEEHHHCCCCCCC		31.1022210691
464PhosphorylationFRESGIASEYESNTD
EHHHCCCCCCCCCCC		38.5022210691
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 CAPON_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of CAPON_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 CAPON_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
LRP1_HUMANLRP1physical
10827173
LRP2_HUMANLRP2physical
10827173
RASD1_HUMANRASD1physical
11086993
SYN1_HUMANSYN1physical
11867766
SYN2_HUMANSYN2physical
11867766
SYN3_HUMANSYN3physical
11867766
NOS1_HUMANNOS1physical
9459447
A4_HUMANAPPphysical
21832049
F133A_HUMANFAM133Aphysical
25416956
AKND1_HUMANAKNAD1physical
25814554
NHP2_HUMANNHP2physical
25814554
NKAP_HUMANNKAPphysical
25814554
RYBP_HUMANRYBPphysical
25814554
KCRM_HUMANCKMphysical
25814554
FYN_HUMANFYNphysical
25814554
CH60_HUMANHSPD1physical
25814554
PLAL2_HUMANPLAGL2physical
25814554
PNPH_HUMANPNPphysical
25814554
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 CAPON_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-371 AND SER-374, ANDMASS SPECTROMETRY.
"Kinase-selective enrichment enables quantitative phosphoproteomics ofthe kinome across the cell cycle.";
Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,Greff Z., Keri G., Stemmann O., Mann M.;
Mol. Cell 31:438-448(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-266, AND MASSSPECTROMETRY.
"Combining protein-based IMAC, peptide-based IMAC, and MudPIT forefficient phosphoproteomic analysis.";
Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D.,Yates J.R. III;
J. Proteome Res. 7:1346-1351(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-266, AND MASSSPECTROMETRY.

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