AKAP1_HUMAN - dbPTM
AKAP1_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID AKAP1_HUMAN
UniProt AC Q92667
Protein Name A-kinase anchor protein 1, mitochondrial
Gene Name AKAP1
Organism Homo sapiens (Human).
Sequence Length 903
Subcellular Localization Mitochondrion outer membrane .
Protein Description Binds to type I and II regulatory subunits of protein kinase A and anchors them to the cytoplasmic face of the mitochondrial outer membrane..
Protein Sequence MAIQFRSLFPLALPGMLALLGWWWFFSRKKGHVSSHDEQQVEAGAVQLRADPAIKEPLPVEDVCPKVVSTPPSVTEPPEKELSTVSKLPAEPPALLQTHPPCRRSESSGILPNTTDMRLRPGTRRDDSTKLELALTGGEAKSIPLECPLSSPKGVLFSSKSAEVCKQDSPFSRVPRKVQPGYPVVPAEKRSSGERARETGGAEGTGDAVLGEKVLEEALLSREHVLELENSKGPSLASLEGEEDKGKSSSSQVVGPVQEEEYVAEKLPSRFIESAHTELAKDDAAPAPPVADAKAQDRGVEGELGNEESLDRNEEGLDRNEEGLDRNEESLDRNEEGLDRNEEIKRAAFQIISQVISEATEQVLATTVGKVAGRVCQASQLQGQKEESCVPVHQKTVLGPDTAEPATAEAAVAPPDAGLPLPGLPAEGSPPPKTYVSCLKSLLSSPTKDSKPNISAHHISLASCLALTTPSEELPDRAGILVEDATCVTCMSDSSQSVPLVASPGHCSDSFSTSGLEDSCTETSSSPRDKAITPPLPESTVPFSNGVLKGELSDLGAEDGWTMDAEADHSGGSDRNSMDSVDSCCSLKKTESFQNAQAGSNPKKVDLIIWEIEVPKHLVGRLIGKQGRYVSFLKQTSGAKIYISTLPYTQSVQICHIEGSQHHVDKALNLIGKKFKELNLTNIYAPPLPSLALPSLPMTSWLMLPDGITVEVIVVNQVNAGHLFVQQHTHPTFHALRSLDQQMYLCYSQPGIPTLPTPVEITVICAAPGADGAWWRAQVVASYEETNEVEIRYVDYGGYKRVKVDVLRQIRSDFVTLPFQGAEVLLDSVMPLSDDDQFSPEADAAMSEMTGNTALLAQVTSYSPTGLPLIQLWSVVGDEVVLINRSLVERGLAQWVDSYYTSL
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
34PhosphorylationSRKKGHVSSHDEQQV
HCCCCCCCCCCHHHH
19.1126471730
35PhosphorylationRKKGHVSSHDEQQVE
CCCCCCCCCCHHHHH
33.5926471730
55UbiquitinationLRADPAIKEPLPVED
EECCCHHCCCCCHHH
56.22-
55AcetylationLRADPAIKEPLPVED
EECCCHHCCCCCHHH
56.2226051181
64GlutathionylationPLPVEDVCPKVVSTP
CCCHHHCCCCCCCCC
4.1122555962
64S-palmitoylationPLPVEDVCPKVVSTP
CCCHHHCCCCCCCCC
4.1121044946
66AcetylationPVEDVCPKVVSTPPS
CHHHCCCCCCCCCCC
50.5826051181
69PhosphorylationDVCPKVVSTPPSVTE
HCCCCCCCCCCCCCC
37.8823401153
70PhosphorylationVCPKVVSTPPSVTEP
CCCCCCCCCCCCCCC
27.8430266825
70 (in isoform 2)Phosphorylation-27.84-
73PhosphorylationKVVSTPPSVTEPPEK
CCCCCCCCCCCCCHH
42.7630266825
75PhosphorylationVSTPPSVTEPPEKEL
CCCCCCCCCCCHHHC
47.3030266825
83PhosphorylationEPPEKELSTVSKLPA
CCCHHHCCCCCCCCC
28.0523186163
84PhosphorylationPPEKELSTVSKLPAE
CCHHHCCCCCCCCCC
41.2323186163
98PhosphorylationEPPALLQTHPPCRRS
CCCHHHCCCCCCCCC
36.0024043423
105PhosphorylationTHPPCRRSESSGILP
CCCCCCCCCCCCCCC
23.6023401153
105 (in isoform 2)Phosphorylation-23.60-
107PhosphorylationPPCRRSESSGILPNT
CCCCCCCCCCCCCCC
34.8029255136
107 (in isoform 2)Phosphorylation-34.80-
108PhosphorylationPCRRSESSGILPNTT
CCCCCCCCCCCCCCC
26.2930266825
108 (in isoform 2)Phosphorylation-26.29-
114PhosphorylationSSGILPNTTDMRLRP
CCCCCCCCCCCCCCC
23.4129396449
115PhosphorylationSGILPNTTDMRLRPG
CCCCCCCCCCCCCCC
34.1429396449
117SulfoxidationILPNTTDMRLRPGTR
CCCCCCCCCCCCCCC
4.0021406390
128PhosphorylationPGTRRDDSTKLELAL
CCCCCCCCCEEEEEE
31.5624400703
129PhosphorylationGTRRDDSTKLELALT
CCCCCCCCEEEEEEE
46.7928857561
136PhosphorylationTKLELALTGGEAKSI
CEEEEEEECCCCCCC
37.2228674419
142PhosphorylationLTGGEAKSIPLECPL
EECCCCCCCEEECCC
36.1625159151
150PhosphorylationIPLECPLSSPKGVLF
CEEECCCCCCCEEEE
29.7225159151
151PhosphorylationPLECPLSSPKGVLFS
EEECCCCCCCEEEEE
38.0125159151
151 (in isoform 2)Phosphorylation-38.01-
158PhosphorylationSPKGVLFSSKSAEVC
CCCEEEEECCCHHHH
32.4720806193
159PhosphorylationPKGVLFSSKSAEVCK
CCEEEEECCCHHHHC
24.2429116813
161PhosphorylationGVLFSSKSAEVCKQD
EEEEECCCHHHHCCC
31.4524732914
169PhosphorylationAEVCKQDSPFSRVPR
HHHHCCCCCCCCCCC
25.9225159151
169 (in isoform 2)Phosphorylation-25.92-
172PhosphorylationCKQDSPFSRVPRKVQ
HCCCCCCCCCCCCCC
35.4324732914
1892-HydroxyisobutyrylationYPVVPAEKRSSGERA
CCCCCHHHCCCCHHH
60.74-
213UbiquitinationGDAVLGEKVLEEALL
CCHHHCHHHHHHHHH
50.77-
231PhosphorylationHVLELENSKGPSLAS
HHHHHHCCCCCCCHH
29.6125849741
235PhosphorylationLENSKGPSLASLEGE
HHCCCCCCCHHCCCC
45.2829214152
238PhosphorylationSKGPSLASLEGEEDK
CCCCCCHHCCCCCCC
32.0426657352
248PhosphorylationGEEDKGKSSSSQVVG
CCCCCCCCCCCCEEC
44.0928348404
249PhosphorylationEEDKGKSSSSQVVGP
CCCCCCCCCCCEECC
37.1828348404
250PhosphorylationEDKGKSSSSQVVGPV
CCCCCCCCCCEECCC
31.7028348404
251PhosphorylationDKGKSSSSQVVGPVQ
CCCCCCCCCEECCCC
29.0128348404
262PhosphorylationGPVQEEEYVAEKLPS
CCCCHHHHHHHHCCH
14.2928796482
266UbiquitinationEEEYVAEKLPSRFIE
HHHHHHHHCCHHHHH
56.83-
266AcetylationEEEYVAEKLPSRFIE
HHHHHHHHCCHHHHH
56.8326051181
269PhosphorylationYVAEKLPSRFIESAH
HHHHHCCHHHHHHHH
50.7029978859
274PhosphorylationLPSRFIESAHTELAK
CCHHHHHHHHHHHHH
22.1223312004
309PhosphorylationGELGNEESLDRNEEG
CCCCCHHHCCCCHHC
29.4125849741
330PhosphorylationGLDRNEESLDRNEEG
HCCCCHHHHHHCHHC
29.4172272759
353PhosphorylationRAAFQIISQVISEAT
HHHHHHHHHHHHHHH
21.7422817900
353 (in isoform 2)Phosphorylation-21.74-
357PhosphorylationQIISQVISEATEQVL
HHHHHHHHHHHHHHH
23.4822817900
357 (in isoform 2)Phosphorylation-23.48-
360PhosphorylationSQVISEATEQVLATT
HHHHHHHHHHHHHHC
23.932499759
360 (in isoform 2)Phosphorylation-23.93-
366PhosphorylationATEQVLATTVGKVAG
HHHHHHHHCHHHHHH
20.1811113651
366 (in isoform 2)Phosphorylation-20.18-
385AcetylationASQLQGQKEESCVPV
HHHHCCCCCCCCCCC
70.9826051181
396PhosphorylationCVPVHQKTVLGPDTA
CCCCCCCEECCCCCC
17.8826552605
402PhosphorylationKTVLGPDTAEPATAE
CEECCCCCCCCCCCH
35.7326552605
407PhosphorylationPDTAEPATAEAAVAP
CCCCCCCCCHHHCCC
35.4326552605
429PhosphorylationPGLPAEGSPPPKTYV
CCCCCCCCCCCHHHH
26.2429255136
434PhosphorylationEGSPPPKTYVSCLKS
CCCCCCHHHHHHHHH
34.6226552605
435PhosphorylationGSPPPKTYVSCLKSL
CCCCCHHHHHHHHHH
9.1122210691
437PhosphorylationPPPKTYVSCLKSLLS
CCCHHHHHHHHHHHC
11.8826552605
440MethylationKTYVSCLKSLLSSPT
HHHHHHHHHHHCCCC
43.30-
441PhosphorylationTYVSCLKSLLSSPTK
HHHHHHHHHHCCCCC
22.9230266825
441 (in isoform 2)Phosphorylation-22.92-
444PhosphorylationSCLKSLLSSPTKDSK
HHHHHHHCCCCCCCC
39.2930266825
445PhosphorylationCLKSLLSSPTKDSKP
HHHHHHCCCCCCCCC
36.2429255136
445 (in isoform 2)Phosphorylation-36.24-
447PhosphorylationKSLLSSPTKDSKPNI
HHHHCCCCCCCCCCC
49.8130266825
447 (in isoform 2)Phosphorylation-49.81-
455PhosphorylationKDSKPNISAHHISLA
CCCCCCCCHHHHHHH
28.3428464451
468PhosphorylationLASCLALTTPSEELP
HHHHHHHCCCCHHCC
30.9327251275
469PhosphorylationASCLALTTPSEELPD
HHHHHHCCCCHHCCC
26.1827251275
503PhosphorylationQSVPLVASPGHCSDS
CCCCEEECCCCCCCC
24.7626074081
508PhosphorylationVASPGHCSDSFSTSG
EECCCCCCCCCCCCC
30.5226074081
523PhosphorylationLEDSCTETSSSPRDK
CCCCCCCCCCCCCCC
18.7626074081
524PhosphorylationEDSCTETSSSPRDKA
CCCCCCCCCCCCCCC
23.6826074081
525PhosphorylationDSCTETSSSPRDKAI
CCCCCCCCCCCCCCC
52.3526074081
526PhosphorylationSCTETSSSPRDKAIT
CCCCCCCCCCCCCCC
24.5826074081
533PhosphorylationSPRDKAITPPLPEST
CCCCCCCCCCCCCCC
24.5829255136
533 (in isoform 2)Phosphorylation-24.58-
539PhosphorylationITPPLPESTVPFSNG
CCCCCCCCCCCCCCC
32.5323927012
540PhosphorylationTPPLPESTVPFSNGV
CCCCCCCCCCCCCCE
30.4523927012
544PhosphorylationPESTVPFSNGVLKGE
CCCCCCCCCCEEEEE
26.9726074081
553PhosphorylationGVLKGELSDLGAEDG
CEEEEEHHHCCCCCC
26.8726074081
562PhosphorylationLGAEDGWTMDAEADH
CCCCCCCEECCCCCC
15.6528985074
570PhosphorylationMDAEADHSGGSDRNS
ECCCCCCCCCCCCCC
45.4524275569
573PhosphorylationEADHSGGSDRNSMDS
CCCCCCCCCCCCCCH
36.6028985074
577PhosphorylationSGGSDRNSMDSVDSC
CCCCCCCCCCHHHHH
25.5146161171
580PhosphorylationSDRNSMDSVDSCCSL
CCCCCCCHHHHHHCC
21.1221815630
583PhosphorylationNSMDSVDSCCSLKKT
CCCCHHHHHHCCCCC
18.1825159151
586PhosphorylationDSVDSCCSLKKTESF
CHHHHHHCCCCCHHH
47.7746161189
588AcetylationVDSCCSLKKTESFQN
HHHHHCCCCCHHHHC
41.1626051181
589UbiquitinationDSCCSLKKTESFQNA
HHHHCCCCCHHHHCC
63.92-
590PhosphorylationSCCSLKKTESFQNAQ
HHHCCCCCHHHHCCC
34.9630266825
592PhosphorylationCSLKKTESFQNAQAG
HCCCCCHHHHCCCCC
37.0523401153
600PhosphorylationFQNAQAGSNPKKVDL
HHCCCCCCCCCCCCE
53.6425159151
603UbiquitinationAQAGSNPKKVDLIIW
CCCCCCCCCCCEEEE
70.45-
6032-HydroxyisobutyrylationAQAGSNPKKVDLIIW
CCCCCCCCCCCEEEE
70.45-
631PhosphorylationGKQGRYVSFLKQTSG
CCCCCEEEEEEECCC
18.8724719451
634UbiquitinationGRYVSFLKQTSGAKI
CCEEEEEEECCCCEE
49.9021890473
634 (in isoform 1)Ubiquitination-49.9021890473
666UbiquitinationGSQHHVDKALNLIGK
CCHHHHHHHHHHHHH
54.40-
673UbiquitinationKALNLIGKKFKELNL
HHHHHHHHHHHHCCC
48.30-
676UbiquitinationNLIGKKFKELNLTNI
HHHHHHHHHCCCCCE
70.89-
783PhosphorylationRAQVVASYEETNEVE
EEEEEEEECCCCCEE
14.1930576142
799PhosphorylationRYVDYGGYKRVKVDV
EEEECCCCEEEEEEH
7.4030576142
800UbiquitinationYVDYGGYKRVKVDVL
EEECCCCEEEEEEHH
54.732189047
800 (in isoform 1)Ubiquitination-54.7321890473
803UbiquitinationYGGYKRVKVDVLRQI
CCCCEEEEEEHHHHH
36.43-
900PhosphorylationAQWVDSYYTSL----
HHHHHHHHHCC----
8.1930455815
901PhosphorylationQWVDSYYTSL-----
HHHHHHHHCC-----
18.4728348404
902PhosphorylationWVDSYYTSL------
HHHHHHHCC------
18.8928192239

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 ligaseSIAH2O43255
PMID:18323779

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of AKAP1_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 AKAP1_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
KAP1_HUMANPRKAR1Bphysical
12634056
AMY1_HUMANAMY1Aphysical
12414807
KAP0_HUMANPRKAR1Aphysical
10764601
KAP2_HUMANPRKAR2Aphysical
10764601
KAP2_HUMANPRKAR2Aphysical
10413680
CFA91_HUMANMAATS1physical
12223483
MYCBP_HUMANMYCBPphysical
12223483
MYCBP_HUMANMYCBPphysical
11483602
A4_HUMANAPPphysical
21832049
PHB_HUMANPHBphysical
26496610
KAP2_HUMANPRKAR2Aphysical
26496610
RL12_HUMANRPL12physical
26496610
TNNI3_HUMANTNNI3physical
26496610
CKAP5_HUMANCKAP5physical
26496610
FARP1_HUMANFARP1physical
26496610
PHB2_HUMANPHB2physical
26496610
PYM1_HUMANWIBGphysical
26496610
LARP4_HUMANLARP4physical
26496610
KAPCA_HUMANPRKACAphysical
26496610

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 AKAP1_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Quantitative phosphoproteomic analysis of T cell receptor signalingreveals system-wide modulation of protein-protein interactions.";
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,Rodionov V., Han D.K.;
Sci. Signal. 2:RA46-RA46(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-429 AND THR-533, ANDMASS SPECTROMETRY.
"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 THR-70; SER-151 AND THR-533,AND MASS SPECTROMETRY.
"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-169, AND MASSSPECTROMETRY.
"Evaluation of the low-specificity protease elastase for large-scalephosphoproteome analysis.";
Wang B., Malik R., Nigg E.A., Korner R.;
Anal. Chem. 80:9526-9533(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-70, AND MASSSPECTROMETRY.
"Large-scale characterization of HeLa cell nuclear phosphoproteins.";
Beausoleil S.A., Jedrychowski M., Schwartz D., Elias J.E., Villen J.,Li J., Cohn M.A., Cantley L.C., Gygi S.P.;
Proc. Natl. Acad. Sci. U.S.A. 101:12130-12135(2004).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-533, AND MASSSPECTROMETRY.

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