AKAP1_MOUSE - dbPTM
AKAP1_MOUSE - PTM Information in dbPTM
Basic Information of Protein
UniProt ID AKAP1_MOUSE
UniProt AC O08715
Protein Name A-kinase anchor protein 1, mitochondrial
Gene Name Akap1
Organism Mus musculus (Mouse).
Sequence Length 857
Subcellular Localization Mitochondrion outer membrane .
Isoform 2: Endoplasmic reticulum.
Isoform 4: Endoplasmic reticulum.
Isoform 1: Mitochondrion outer membrane.
Isoform 3: Mitochondrion outer membrane.
Isoform 5: Mitochondrion outer membrane.
Isoform 6: Mitochondrion ou
Protein Description Differentially targeted protein that binds to type I and II regulatory subunits of protein kinase A. Anchors them to the cytoplasmic face of the mitochondrial outer membrane or allows them to reside in the endoplasmic reticulum. Does not contain the classic KDEL endoplasmic reticulum-targeting sequence. This explains how it is able to switch its localization, either being in the endoplasmic reticulum or in the mitochondria depending on which N-terminal part begins the isoform. The longest N-terminal part only present in isoform 2 and isoform 4 acts as a suppressor of mitochondrial targeting and as an activator of recessive endoplasmic reticulum targeting motif..
Protein Sequence MAIQLRSLFPLALPGMLALLGWWWFFSRKKDRLSSSDKQVETLKVGPAIKDRRLSEEACPGVLSVAPTVTQPPGREEQRCVDKPSTEPLALPRTRQVRRRSESSGNLPSVADTRSQPGPCRDEIAKVELSLMGDKAKSIPLGCPLLPKDASFPYEAVERCKQESALGKTPGRGWPSPYAASGEKARETGGTEGTGDAVLGENVSEEGLLSQECVSEVEKSEFPILAPGGGEGEEVSHGPPQVAELLKKEEYIVGKLPSSFVEPVHSEPVKDEDALEPQVKGSSNTSDRDLAGELDKDETVPENDQIKQAAFQLISQVILEATEEFRATTVGKTVAQVHPTSATQPKGKEESCVPASQETSLGQDTSDPASTRTGATASPSAEALPPKTYVSCLSSPLSGPTKDQKPKNSAHHISLAPCPPPVTPQRQSLEGASNPRGDDNFVACMANNSQSVLSVSSLGQCSDPVSTSGLEDSCTETISSSGDKAMTPPLPVSTQPFSNGVLKEELSDLGTEDGWTMDTEADHSGGSDGNSMDSVDSCCGLTKPDSPQSVQAGSNPKKVDLIIWEIEVPKHLVGRLIGKQGRYVSFLKQTSGAKIYISTLPYTQNIQICHIEGSQHHVDKALNLIGKKFKELNLTNIYAPPLPSLALPSLPMTSWLMLPDGITVEVIVVNQVNAGHLFVQQHTHPTFHALRSLDQQMYLCYSQPGIPTLPTPVEITVICAAPGADGAWWRAQVVASYEETNEVEIRYVDYGGYKRVKVDVLRQIRSDFVTLPFQGAEVLLDSVVPLSDDDHFSPEADAAMSEMTGNTALLAQVTSYSATGLPLIQLWSVVGDEVVLINRSLVERGLAQWVDSYYASL
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
25 (in isoform 3)Phosphorylation-2.2127149854
25 (in isoform 4)Phosphorylation-2.2127149854
26 (in isoform 3)Phosphorylation-4.3027149854
26 (in isoform 4)Phosphorylation-4.3027149854
28 (in isoform 3)Phosphorylation-44.9027149854
28 (in isoform 4)Phosphorylation-44.9027149854
29 (in isoform 3)Phosphorylation-58.8027149854
29 (in isoform 4)Phosphorylation-58.8027149854
30 (in isoform 3)Phosphorylation-47.1527149854
30 (in isoform 4)Phosphorylation-47.1527149854
32 (in isoform 3)Phosphorylation-45.4027149854
32 (in isoform 4)Phosphorylation-45.4027149854
55PhosphorylationAIKDRRLSEEACPGV
HHHCCCCCCCCCCCE		31.4227087446
64PhosphorylationEACPGVLSVAPTVTQ
CCCCCEEEECCEECC		17.5225619855
68PhosphorylationGVLSVAPTVTQPPGR
CEEEECCEECCCCCC		26.8425619855
70PhosphorylationLSVAPTVTQPPGREE
EEECCEECCCCCCCH		37.5225619855
101PhosphorylationTRQVRRRSESSGNLP
CHHHHHHHCCCCCCC		39.7627087446
103PhosphorylationQVRRRSESSGNLPSV
HHHHHHCCCCCCCCH		44.8027087446
104PhosphorylationVRRRSESSGNLPSVA
HHHHHCCCCCCCCHH		27.8727742792
109PhosphorylationESSGNLPSVADTRSQ
CCCCCCCCHHCCCCC		32.8622802335
113PhosphorylationNLPSVADTRSQPGPC
CCCCHHCCCCCCCCC		23.6025619855
115PhosphorylationPSVADTRSQPGPCRD
CCHHCCCCCCCCCHH		42.7051454205
135UbiquitinationELSLMGDKAKSIPLG
EHHHHCCCCCCCCCC		52.5722790023
135 (in isoform 4)Ubiquitination-52.5722790023
138PhosphorylationLMGDKAKSIPLGCPL
HHCCCCCCCCCCCCC		34.0172261009
143S-palmitoylationAKSIPLGCPLLPKDA
CCCCCCCCCCCCCCC		2.5728526873
151PhosphorylationPLLPKDASFPYEAVE
CCCCCCCCCCHHHHH		36.5725521595
154PhosphorylationPKDASFPYEAVERCK
CCCCCCCHHHHHHHH		17.9529899451
164PhosphorylationVERCKQESALGKTPG
HHHHHHHHHCCCCCC		26.71-
168 (in isoform 4)Ubiquitination-53.01-
176PhosphorylationTPGRGWPSPYAASGE
CCCCCCCCCCCCCCC		24.8426643407
259PhosphorylationIVGKLPSSFVEPVHS
EEECCCHHHCCCCCC		31.2230352176
282PhosphorylationLEPQVKGSSNTSDRD
CCCCCCCCCCCCCHH		18.0722871156
283PhosphorylationEPQVKGSSNTSDRDL
CCCCCCCCCCCCHHH		53.4425338131
285PhosphorylationQVKGSSNTSDRDLAG
CCCCCCCCCCHHHCC		33.6725338131
333PhosphorylationRATTVGKTVAQVHPT
HHHCCCCCEEECCCC		18.3651459033
352S-nitrosocysteinePKGKEESCVPASQET
CCCCCCCCCCCCCCC		4.87-
352S-nitrosylationPKGKEESCVPASQET
CCCCCCCCCCCCCCC		4.8721278135
366PhosphorylationTSLGQDTSDPASTRT
CCCCCCCCCCCCCCC		50.3026643407
370PhosphorylationQDTSDPASTRTGATA
CCCCCCCCCCCCCCC		24.6626643407
371PhosphorylationDTSDPASTRTGATAS
CCCCCCCCCCCCCCC		34.0626643407
373PhosphorylationSDPASTRTGATASPS
CCCCCCCCCCCCCCC		31.1226643407
376PhosphorylationASTRTGATASPSAEA
CCCCCCCCCCCCCCC		29.0725619855
378PhosphorylationTRTGATASPSAEALP
CCCCCCCCCCCCCCC		18.2926824392
380PhosphorylationTGATASPSAEALPPK
CCCCCCCCCCCCCCC		35.9225619855
388PhosphorylationAEALPPKTYVSCLSS
CCCCCCCCEEEECCC		34.6225777480
389PhosphorylationEALPPKTYVSCLSSP
CCCCCCCEEEECCCC		9.1125777480
391PhosphorylationLPPKTYVSCLSSPLS
CCCCCEEEECCCCCC		10.0323984901
392S-palmitoylationPPKTYVSCLSSPLSG
CCCCEEEECCCCCCC		2.8128526873
394PhosphorylationKTYVSCLSSPLSGPT
CCEEEECCCCCCCCC		33.9525159016
395PhosphorylationTYVSCLSSPLSGPTK
CEEEECCCCCCCCCC		19.5325521595
398PhosphorylationSCLSSPLSGPTKDQK
EECCCCCCCCCCCCC		46.2225159016
401PhosphorylationSSPLSGPTKDQKPKN
CCCCCCCCCCCCCCC		51.2628066266
423PhosphorylationAPCPPPVTPQRQSLE
CCCCCCCCCCCCCCC		21.3425619855
428PhosphorylationPVTPQRQSLEGASNP
CCCCCCCCCCCCCCC		30.49108494509
433PhosphorylationRQSLEGASNPRGDDN
CCCCCCCCCCCCCCC		59.2227742792
487PhosphorylationSSGDKAMTPPLPVST
CCCCCCCCCCCCCCC		26.9825521595
493PhosphorylationMTPPLPVSTQPFSNG
CCCCCCCCCCCCCCC		21.2725159016
494PhosphorylationTPPLPVSTQPFSNGV
CCCCCCCCCCCCCCC		40.2623140645
498PhosphorylationPVSTQPFSNGVLKEE
CCCCCCCCCCCCHHH		39.0823140645
519PhosphorylationEDGWTMDTEADHSGG
CCCCEECCCCCCCCC		23.4251459025
524PhosphorylationMDTEADHSGGSDGNS
ECCCCCCCCCCCCCC		45.4551459017
527PhosphorylationEADHSGGSDGNSMDS
CCCCCCCCCCCCCCC		45.9651459041
531PhosphorylationSGGSDGNSMDSVDSC
CCCCCCCCCCCCHHC		29.5146161173
546PhosphorylationCGLTKPDSPQSVQAG
CCCCCCCCCCCCCCC		33.1129472430
549PhosphorylationTKPDSPQSVQAGSNP
CCCCCCCCCCCCCCC		21.4129472430
588UbiquitinationGRYVSFLKQTSGAKI
CCEEEEEEECCCCEE		49.9022790023
588 (in isoform 4)Ubiquitination-49.9022790023
621 (in isoform 4)Ubiquitination-9.38-
627UbiquitinationKALNLIGKKFKELNL
HHHHHHHHHHHHCCC		48.3022790023
627 (in isoform 4)Ubiquitination-48.3022790023
660 (in isoform 4)Ubiquitination-58.11-
856PhosphorylationWVDSYYASL------
HHHHHHHCC------		20.6326643407
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
-KUbiquitinationE3 ubiquitin ligaseSiah2Q06986
PMID:22199232
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of AKAP1_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 AKAP1_MOUSE !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
DNM1L_MOUSEDnm1lphysical
22099302
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of AKAP1_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-55, AND MASSSPECTROMETRY.
"Specific phosphopeptide enrichment with immobilized titanium ionaffinity chromatography adsorbent for phosphoproteome analysis.";
Zhou H., Ye M., Dong J., Han G., Jiang X., Wu R., Zou H.;
J. Proteome Res. 7:3957-3967(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-55, AND MASSSPECTROMETRY.
"Large-scale phosphorylation analysis of mouse liver.";
Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-55; SER-101 AND SER-103,AND MASS SPECTROMETRY.

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