AKA10_HUMAN - dbPTM
AKA10_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID AKA10_HUMAN
UniProt AC O43572
Protein Name A-kinase anchor protein 10, mitochondrial
Gene Name AKAP10
Organism Homo sapiens (Human).
Sequence Length 662
Subcellular Localization Mitochondrion . Membrane . Cytoplasm . Predominantly mitochondrial but also membrane associated and cytoplasmic.
Protein Description Differentially targeted protein that binds to type I and II regulatory subunits of protein kinase A and anchors them to the mitochondria or the plasma membrane. Although the physiological relevance between PKA and AKAPS with mitochondria is not fully understood, one idea is that BAD, a proapoptotic member, is phosphorylated and inactivated by mitochondria-anchored PKA. It cannot be excluded too that it may facilitate PKA as well as G protein signal transduction, by acting as an adapter for assembling multiprotein complexes. With its RGS domain, it could lead to the interaction to G-alpha proteins, providing a link between the signaling machinery and the downstream kinase (By similarity)..
Protein Sequence MRGAGPSPRQSPRTLRPDPGPAMSFFRRKVKGKEQEKTSDVKSIKASISVHSPQKSTKNHALLEAAGPSHVAINAISANMDSFSSSRTATLKKQPSHMEAAHFGDLGRSCLDYQTQETKSSLSKTLEQVLHDTIVLPYFIQFMELRRMEHLVKFWLEAESFHSTTWSRIRAHSLNTVKQSSLAEPVSPSKKHETTASFLTDSLDKRLEDSGSAQLFMTHSEGIDLNNRTNSTQNHLLLSQECDSAHSLRLEMARAGTHQVSMETQESSSTLTVASRNSPASPLKELSGKLMKSIEQDAVNTFTKYISPDAAKPIPITEAMRNDIIARICGEDGQVDPNCFVLAQSIVFSAMEQEHFSEFLRSHHFCKYQIEVLTSGTVYLADILFCESALFYFSEYMEKEDAVNILQFWLAADNFQSQLAAKKGQYDGQEAQNDAMILYDKYFSLQATHPLGFDDVVRLEIESNICREGGPLPNCFTTPLRQAWTTMEKVFLPGFLSSNLYYKYLNDLIHSVRGDEFLGGNVSLTAPGSVGPPDESHPGSSDSSASQSSVKKASIKILKNFDEAIIVDAASLDPESLYQRTYAGKMTFGRVSDLGQFIRESEPEPDVRKSKGSMFSQAMKKWVQGNTDEAQEELAWKIAKMIVSDIMQQAQYDQPLEKSTKL
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
2Methylation------MRGAGPSPR
------CCCCCCCCC
43.60-
7Phosphorylation-MRGAGPSPRQSPRT
-CCCCCCCCCCCCCC
31.6225849741
9MethylationRGAGPSPRQSPRTLR
CCCCCCCCCCCCCCC
54.68-
11PhosphorylationAGPSPRQSPRTLRPD
CCCCCCCCCCCCCCC
20.0325849741
24PhosphorylationPDPGPAMSFFRRKVK
CCCCHHHHHHHHHHC
24.2846161205
38PhosphorylationKGKEQEKTSDVKSIK
CCCCCCCCCCCHHHH
29.4323403867
39PhosphorylationGKEQEKTSDVKSIKA
CCCCCCCCCCHHHHH
52.0224719451
47PhosphorylationDVKSIKASISVHSPQ
CCHHHHHEEEECCCC
15.4722152101
49PhosphorylationKSIKASISVHSPQKS
HHHHHEEEECCCCCC
15.9825849741
52PhosphorylationKASISVHSPQKSTKN
HHEEEECCCCCCCCC
27.2028731282
55MethylationISVHSPQKSTKNHAL
EEECCCCCCCCCCHH
64.57-
56PhosphorylationSVHSPQKSTKNHALL
EECCCCCCCCCCHHH
39.0910014611
57PhosphorylationVHSPQKSTKNHALLE
ECCCCCCCCCCHHHH
42.7923312004
90PhosphorylationFSSSRTATLKKQPSH
CCCCCCCCCCCCCCC
38.2030814895
93UbiquitinationSRTATLKKQPSHMEA
CCCCCCCCCCCCHHH
71.23-
96PhosphorylationATLKKQPSHMEAAHF
CCCCCCCCCHHHHHC
32.7322617229
113PhosphorylationLGRSCLDYQTQETKS
HHHHHHHHHHHHHHH
10.66141191
119UbiquitinationDYQTQETKSSLSKTL
HHHHHHHHHHHHHHH
36.98-
160PhosphorylationKFWLEAESFHSTTWS
HHHHHHHHCCCCHHH
34.9930387612
173PhosphorylationWSRIRAHSLNTVKQS
HHHHHHHCCCCCCCC
23.4881018103
180PhosphorylationSLNTVKQSSLAEPVS
CCCCCCCCCCCCCCC
22.9223403867
181PhosphorylationLNTVKQSSLAEPVSP
CCCCCCCCCCCCCCC
29.1623403867
187PhosphorylationSSLAEPVSPSKKHET
CCCCCCCCCCCCCHH
33.8823401153
189PhosphorylationLAEPVSPSKKHETTA
CCCCCCCCCCCHHHH
46.9930266825
194PhosphorylationSPSKKHETTASFLTD
CCCCCCHHHHHHHHH
27.6423186163
195PhosphorylationPSKKHETTASFLTDS
CCCCCHHHHHHHHHH
19.8123186163
197PhosphorylationKKHETTASFLTDSLD
CCCHHHHHHHHHHHH
20.7829255136
200PhosphorylationETTASFLTDSLDKRL
HHHHHHHHHHHHHHH
22.8729255136
202PhosphorylationTASFLTDSLDKRLED
HHHHHHHHHHHHHHC
32.9829255136
210PhosphorylationLDKRLEDSGSAQLFM
HHHHHHCCCCCEEEE
25.8524719451
229PhosphorylationGIDLNNRTNSTQNHL
CCCCCCCCCCCCCEE
35.3350564329
231PhosphorylationDLNNRTNSTQNHLLL
CCCCCCCCCCCEEEE
30.6623312004
232PhosphorylationLNNRTNSTQNHLLLS
CCCCCCCCCCEEEEC
35.1523312004
239PhosphorylationTQNHLLLSQECDSAH
CCCEEEECCCCCCHH
24.7323312004
244PhosphorylationLLSQECDSAHSLRLE
EECCCCCCHHHHHHH
39.2723312004
257PhosphorylationLEMARAGTHQVSMET
HHHHHHCCCEEEEEE
14.2422912867
261PhosphorylationRAGTHQVSMETQESS
HHCCCEEEEEEECCC
12.34101545607
264PhosphorylationTHQVSMETQESSSTL
CCEEEEEEECCCCEE
29.0623312004
267PhosphorylationVSMETQESSSTLTVA
EEEEEECCCCEEEEH
21.5524364847
268PhosphorylationSMETQESSSTLTVAS
EEEEECCCCEEEEHH
26.9623312004
269PhosphorylationMETQESSSTLTVASR
EEEECCCCEEEEHHC
36.3924364853
270PhosphorylationETQESSSTLTVASRN
EEECCCCEEEEHHCC
28.5323312004
272PhosphorylationQESSSTLTVASRNSP
ECCCCEEEEHHCCCC
17.7024364861
275PhosphorylationSSTLTVASRNSPASP
CCEEEEHHCCCCCCH
27.8828985074
278PhosphorylationLTVASRNSPASPLKE
EEEHHCCCCCCHHHH
22.2630266825
281PhosphorylationASRNSPASPLKELSG
HHCCCCCCHHHHHCH
33.8623401153
287PhosphorylationASPLKELSGKLMKSI
CCHHHHHCHHHHHHH
34.6723927012
289UbiquitinationPLKELSGKLMKSIEQ
HHHHHCHHHHHHHHH
41.87-
292UbiquitinationELSGKLMKSIEQDAV
HHCHHHHHHHHHHHH
59.73-
293PhosphorylationLSGKLMKSIEQDAVN
HCHHHHHHHHHHHHH
19.86113301101
312UbiquitinationYISPDAAKPIPITEA
CCCCCCCCCCCCCHH
45.24-
423UbiquitinationQSQLAAKKGQYDGQE
HHHHHHHCCCCCCCH
46.66-
442PhosphorylationAMILYDKYFSLQATH
CEEEEECCCCCEECC
8.7646161217
448PhosphorylationKYFSLQATHPLGFDD
CCCCCEECCCCCCCC
15.8646161211
549PhosphorylationDSSASQSSVKKASIK
CCCCCHHHHHHHHHH
30.2525627689
559UbiquitinationKASIKILKNFDEAII
HHHHHHHHCCCEEEE
60.07-
578PhosphorylationSLDPESLYQRTYAGK
HCCHHHHHHHHHCCC
12.7727642862
585UbiquitinationYQRTYAGKMTFGRVS
HHHHHCCCCEEEEHH
26.96-
610PhosphorylationPEPDVRKSKGSMFSQ
CCCCCCCCCCCHHHH
31.5222210691
611UbiquitinationEPDVRKSKGSMFSQA
CCCCCCCCCCHHHHH
59.02-
613PhosphorylationDVRKSKGSMFSQAMK
CCCCCCCCHHHHHHH
22.0122210691
621UbiquitinationMFSQAMKKWVQGNTD
HHHHHHHHHHCCCCH
39.24-
637UbiquitinationAQEELAWKIAKMIVS
HHHHHHHHHHHHHHH
27.46-
652PhosphorylationDIMQQAQYDQPLEKS
HHHHHHCCCCCCHHH
21.4027642862
658UbiquitinationQYDQPLEKSTKL---
CCCCCCHHHCCC---
71.72-

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 AKA10_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of AKA10_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 AKA10_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
COG3_HUMANCOG3physical
22863883
DCTN4_HUMANDCTN4physical
22863883
MYH9_HUMANMYH9physical
22863883

Drug and Disease Associations
Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
115080Sudden cardiac death (SCD)
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of AKA10_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"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-52 AND SER-187, AND MASSSPECTROMETRY.

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