AKA7A_HUMAN - dbPTM
AKA7A_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID AKA7A_HUMAN
UniProt AC O43687
Protein Name A-kinase anchor protein 7 isoforms alpha and beta
Gene Name AKAP7
Organism Homo sapiens (Human).
Sequence Length 104
Subcellular Localization Isoform Alpha: Lateral cell membrane
Lipid-anchor. Targeted predominantly to the lateral membrane.
Isoform Beta: Apical cell membrane
Lipid-anchor. Targeted predominantly to the apical membrane.
Protein Description Targets the cAMP-dependent protein kinase (PKA) to the plasma membrane, and permits functional coupling to the L-type calcium channel. The membrane-associated form reduces epithelial sodium channel (ENaC) activity, whereas the free cytoplasmic form may negatively regulate ENaC channel feedback inhibition by intracellular sodium..
Protein Sequence MGQLCCFPFSRDEGKISELESSSSAVLQRYSKDIPSWSSGEKNGGEPDDAELVRLSKRLVENAVLKAVQQYLEETQNKNKPGEGSSVKTEAADQNGNDNENNRK
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
2N-myristoyl glycine------MGQLCCFPF
------CCCCCCEEC
29.21-
2Myristoylation------MGQLCCFPF
------CCCCCCEEC
29.219545239
5S-palmitoylation---MGQLCCFPFSRD
---CCCCCCEECCCC
1.409545239
6S-palmitoylation--MGQLCCFPFSRDE
--CCCCCCEECCCCC
7.079545239
17PhosphorylationSRDEGKISELESSSS
CCCCCCHHHCHHCCH
39.3523312004
21PhosphorylationGKISELESSSSAVLQ
CCHHHCHHCCHHHHH
48.4126657352
22PhosphorylationKISELESSSSAVLQR
CHHHCHHCCHHHHHH
20.9546161483
23PhosphorylationISELESSSSAVLQRY
HHHCHHCCHHHHHHH
31.4323312004
24PhosphorylationSELESSSSAVLQRYS
HHCHHCCHHHHHHHC
25.0923532336
31PhosphorylationSAVLQRYSKDIPSWS
HHHHHHHCCCCCCCC
26.4923532336
36PhosphorylationRYSKDIPSWSSGEKN
HHCCCCCCCCCCCCC
39.6726657352

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 AKA7A_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of AKA7A_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 AKA7A_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
SP17_HUMANSPA17physical
25416956
ROP1A_HUMANROPN1physical
25416956
CEP76_HUMANCEP76physical
25416956

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 AKA7A_HUMAN

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Related Literatures of Post-Translational Modification
Myristoylation
ReferencePubMed
"A novel lipid-anchored A-kinase anchoring protein facilitates cAMP-responsive membrane events.";
Fraser I.D.C., Tavalin S.J., Lester L.B., Langeberg L.K.,Westphal A.M., Dean R.A., Marrion N.V., Scott J.D.;
EMBO J. 17:2261-2272(1998).
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM ALPHA), FUNCTION, SUBCELLULARLOCATION, TISSUE SPECIFICITY, MYRISTOYLATION AT GLY-2, ANDPALMITOYLATION AT CYS-5 AND CYS-6.
Palmitoylation
ReferencePubMed
"A novel lipid-anchored A-kinase anchoring protein facilitates cAMP-responsive membrane events.";
Fraser I.D.C., Tavalin S.J., Lester L.B., Langeberg L.K.,Westphal A.M., Dean R.A., Marrion N.V., Scott J.D.;
EMBO J. 17:2261-2272(1998).
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM ALPHA), FUNCTION, SUBCELLULARLOCATION, TISSUE SPECIFICITY, MYRISTOYLATION AT GLY-2, ANDPALMITOYLATION AT CYS-5 AND CYS-6.

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