CAP1_MOUSE - dbPTM
CAP1_MOUSE - PTM Information in dbPTM
Basic Information of Protein
UniProt ID CAP1_MOUSE
UniProt AC P40124
Protein Name Adenylyl cyclase-associated protein 1
Gene Name Cap1
Organism Mus musculus (Mouse).
Sequence Length 474
Subcellular Localization Cell membrane
Peripheral membrane protein.
Protein Description Directly regulates filament dynamics and has been implicated in a number of complex developmental and morphological processes, including mRNA localization and the establishment of cell polarity..
Protein Sequence MADMQNLVERLERAVGRLEAVSHTSDMHCGYGDSPSKGAVPYVQAFDSLLANPVAEYLKMSKEIGGDVQKHAEMVHTGLKLERALLATASQCQQPAGNKLSDLLAPISEQIQEVITFREKNRGSKFFNHLSAVSESIQALGWVALAAKPGPFVKEMNDAAMFYTNRVLKEYRDVDKKHVDWVRAYLSIWTELQAYIKEFHTTGLAWSKTGPVAKELSGLPSGPSVGSGPPPPPPGPPPPPISTSSGSDDSASRSALFAQINQGESITHALKHVSDDMKTHKNPALKAQSGPVRSGPKPFSAPKPQTSPSPKPATKKEPALLELEGKKWRVENQENVSNLVIDDTELKQVAYIYKCVNTTLQIKGKINSITVDNCKKLGLVFDDVVGIVEIINSRDVKVQVMGKVPTISINKTDGCHAYLSKNSLDCEIVSAKSSEMNVLIPTEGGDFNEFPVPEQFKTLWNGQKLVTTVTEIAG
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
2Acetylation------MADMQNLVE
------CHHHHHHHH		22.45-
22PhosphorylationVGRLEAVSHTSDMHC
HHHHHHHEECCCCCC		28.2625619855
24PhosphorylationRLEAVSHTSDMHCGY
HHHHHEECCCCCCCC		20.9325619855
25PhosphorylationLEAVSHTSDMHCGYG
HHHHEECCCCCCCCC		27.7525619855
29S-nitrosylationSHTSDMHCGYGDSPS
EECCCCCCCCCCCCC		3.4521278135
29GlutathionylationSHTSDMHCGYGDSPS
EECCCCCCCCCCCCC		3.4524333276
29S-nitrosocysteineSHTSDMHCGYGDSPS
EECCCCCCCCCCCCC		3.45-
31PhosphorylationTSDMHCGYGDSPSKG
CCCCCCCCCCCCCCC		24.1324925903
34PhosphorylationMHCGYGDSPSKGAVP
CCCCCCCCCCCCCCC		27.0624925903
36PhosphorylationCGYGDSPSKGAVPYV
CCCCCCCCCCCCCHH		47.9024925903
42PhosphorylationPSKGAVPYVQAFDSL
CCCCCCCHHHHHHHH		9.9021183079
62AcetylationAEYLKMSKEIGGDVQ
HHHHHHHHHHCCCHH		50.2622826441
62MalonylationAEYLKMSKEIGGDVQ
HHHHHHHHHHCCCHH		50.2626320211
62UbiquitinationAEYLKMSKEIGGDVQ
HHHHHHHHHHCCCHH		50.26-
70AcetylationEIGGDVQKHAEMVHT
HHCCCHHHHHHHHHH		44.6323236377
77PhosphorylationKHAEMVHTGLKLERA
HHHHHHHHCHHHHHH		32.5724759943
80AcetylationEMVHTGLKLERALLA
HHHHHCHHHHHHHHH		50.0422826441
90PhosphorylationRALLATASQCQQPAG
HHHHHHHHHCCCCCC		27.4328285833
92S-nitrosocysteineLLATASQCQQPAGNK
HHHHHHHCCCCCCCH		3.62-
92GlutathionylationLLATASQCQQPAGNK
HHHHHHHCCCCCCCH		3.6224333276
92S-nitrosylationLLATASQCQQPAGNK
HHHHHHHCCCCCCCH		3.6221278135
92S-palmitoylationLLATASQCQQPAGNK
HHHHHHHCCCCCCCH		3.6228526873
154AcetylationAKPGPFVKEMNDAAM
CCCCCHHHHHHHHHH		52.1822826441
163PhosphorylationMNDAAMFYTNRVLKE
HHHHHHHHHHHHHHH		7.0422817900
164PhosphorylationNDAAMFYTNRVLKEY
HHHHHHHHHHHHHHH		12.7925367039
177AcetylationEYRDVDKKHVDWVRA
HHHCCCHHHHHHHHH		44.3822826441
208AcetylationTTGLAWSKTGPVAKE
HCCCCCCCCCCCHHH		46.9622826441
224PhosphorylationSGLPSGPSVGSGPPP
CCCCCCCCCCCCCCC		42.5126026062
227PhosphorylationPSGPSVGSGPPPPPP
CCCCCCCCCCCCCCC		46.0728285833
242PhosphorylationGPPPPPISTSSGSDD
CCCCCCCCCCCCCCC		28.1929899451
243PhosphorylationPPPPPISTSSGSDDS
CCCCCCCCCCCCCCH		27.8626026062
245PhosphorylationPPPISTSSGSDDSAS
CCCCCCCCCCCCHHH		42.2626026062
254PhosphorylationSDDSASRSALFAQIN
CCCHHHHHHHHHHHH		27.1629472430
265PhosphorylationAQINQGESITHALKH
HHHHHCCCHHHHHHH		39.3425521595
267PhosphorylationINQGESITHALKHVS
HHHCCCHHHHHHHCC		15.4625521595
286UbiquitinationTHKNPALKAQSGPVR
HCCCCCHHCCCCCCC		46.62-
286MethylationTHKNPALKAQSGPVR
HCCCCCHHCCCCCCC		46.62-
286MalonylationTHKNPALKAQSGPVR
HCCCCCHHCCCCCCC		46.6226320211
289PhosphorylationNPALKAQSGPVRSGP
CCCHHCCCCCCCCCC		50.34-
294PhosphorylationAQSGPVRSGPKPFSA
CCCCCCCCCCCCCCC		60.7328609623
297UbiquitinationGPVRSGPKPFSAPKP
CCCCCCCCCCCCCCC		63.3227667366
297MalonylationGPVRSGPKPFSAPKP
CCCCCCCCCCCCCCC		63.3226320211
300PhosphorylationRSGPKPFSAPKPQTS
CCCCCCCCCCCCCCC		52.7928609623
306PhosphorylationFSAPKPQTSPSPKPA
CCCCCCCCCCCCCCC		51.6526824392
307PhosphorylationSAPKPQTSPSPKPAT
CCCCCCCCCCCCCCC		20.3826824392
309PhosphorylationPKPQTSPSPKPATKK
CCCCCCCCCCCCCCC		45.3726824392
311MalonylationPQTSPSPKPATKKEP
CCCCCCCCCCCCCCC		52.1826320211
314PhosphorylationSPSPKPATKKEPALL
CCCCCCCCCCCCCEE		51.6925159016
326AcetylationALLELEGKKWRVENQ
CEEEECCCEEEECCC		39.5223236377
337PhosphorylationVENQENVSNLVIDDT
ECCCCCCCCEECCHH		35.7130635358
347UbiquitinationVIDDTELKQVAYIYK
ECCHHHHHHHHHHHH		36.1722790023
351PhosphorylationTELKQVAYIYKCVNT
HHHHHHHHHHHHHCC		13.1125367039
353PhosphorylationLKQVAYIYKCVNTTL
HHHHHHHHHHHCCCE		5.9022817900
355GlutathionylationQVAYIYKCVNTTLQI
HHHHHHHHHCCCEEE		1.2824333276
365MalonylationTTLQIKGKINSITVD
CCEEECCEEEEEEEC		33.4426320211
375MalonylationSITVDNCKKLGLVFD
EEEECCHHHHCCEEC		58.2326320211
375AcetylationSITVDNCKKLGLVFD
EEEECCHHHHCCEEC		58.2390413
403UbiquitinationVKVQVMGKVPTISIN
CEEEEEEECCEEEEE		27.2627667366
411AcetylationVPTISINKTDGCHAY
CCEEEEECCCCCEEE		46.4523806337
415S-nitrosocysteineSINKTDGCHAYLSKN
EEECCCCCEEEECCC		1.52-
415S-nitrosylationSINKTDGCHAYLSKN
EEECCCCCEEEECCC		1.5221278135
415GlutathionylationSINKTDGCHAYLSKN
EEECCCCCEEEECCC		1.5224333276
418PhosphorylationKTDGCHAYLSKNSLD
CCCCCEEEECCCCCC		6.4525367039
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
309SPhosphorylationKinaseGSK3BP49841
PSP
309SPhosphorylationKinaseGSK3BQ9WV60
PSP
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of CAP1_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 CAP1_MOUSE !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions

Oops, there are no PPI records of CAP1_MOUSE !!
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of CAP1_MOUSE

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Solid tumor proteome and phosphoproteome analysis by high resolutionmass spectrometry.";
Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J.,Faessler R., Mann M.;
J. Proteome Res. 7:5314-5326(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-309, AND MASSSPECTROMETRY.

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