Lipid Modification Database
Tag Content
LipidDB ID
LipidDB-9606-00265
Entry Name
UniProt Accession
Theoretical PI
4.87
Molecular Weight
47088.3
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
A-kinase anchor protein 5
Protein Synonyms/Alias
AKAP-5; A-kinase anchor protein 79 kDa; AKAP 79; H21; cAMP-dependent protein kinase regulatory subunit II high affinity-binding protein;
Gene Name
AKAP5
Gene Synonyms/Alias
AKAP79;
Created Date
01-MAR-1992
 Lipid Modification Sites 
 Position   Sequence Form   Peptide   References   Modification Type 
36
Canonical
KEKASMLCFKRRKKA
[1]
S-Palmitoylation
129
Canonical
KSRLKIPCIKFPRGP
[1]
S-Palmitoylation
Organism
Homo sapiens (Human)
NCBI Taxa ID
9606
Reference
[1] Delint-Ramirez I, Willoughby D, Hammond GV, Ayling LJ, Cooper DM.Palmitoylation targets AKAP79 protein to lipid rafts and promotes its regulation of calcium-sensitive adenylyl cyclase type 8. J Biol Chem. 2011 Sep23;286(38):32962-75. doi: 10.1074/jbc.M111.243899. Epub 2011 Jul 19.[PMID:21771783]
Functional Description
May anchor the PKA protein to cytoskeletal and/or organelle-associated proteins, targeting the signal carried by cAMP to specific intracellular effectors. Association with to the beta2-adrenergic receptor (beta2-AR) not only regulates beta2-AR signaling pathway, but also the activation by PKA by switching off the beta2-AR signaling cascade.
Sequence Annotation
Domain: 73 103 AKAP.
Region: 1 170 Essential to the intracellular anchoringfunction.
Region: 392 405 PKA-RII subunit binding domain.
Protein Length
427 AA.
Protein Sequence
(Canonical)
METTISEIHV ENKDEKRSAE GSPGAERQKE KASMLCFKRR KKAAKALKPK AGSEAADVAR  60
KCPQEAGASD QPEPTRGAWA SLKRLVTRRK RSESSKQQKP LEGEMQPAIN AEDADLSKKK  120
AKSRLKIPCI KFPRGPKRSN HSKIIEDSDC SIKVQEEAEI LDIQTQTPLN DQATKAKSTQ  180
DLSEGISRKD GDEVCESNVS NSTTSGEKVI SVELGLDNGH SAIQTGTLIL EEIETIKEKQ  240
DVQPQQASPL ETSETDHQQP VLSDVPPLPA IPDQQIVEEA SNSTLESAPN GKDYESTEIV  300
AEETKPKDTE LSQESDFKEN GITEEKSKSE ESKRMEPIAI IITDTEISEF DVTKSKNVPK  360
QFLISAENEQ VGVFANDNGF EDRTSEQYET LLIETASSLV KNAIQLSIEQ LVNEMASDDN  420
KINNLLQ                                                            427
FASTA
(Canonical)
>LipidDB-9606-00265|P24588
METTISEIHVENKDEKRSAEGSPGAERQKEKASMLCFKRRKKAAKALKPKAGSEAADVAR
KCPQEAGASDQPEPTRGAWASLKRLVTRRKRSESSKQQKPLEGEMQPAINAEDADLSKKK
AKSRLKIPCIKFPRGPKRSNHSKIIEDSDCSIKVQEEAEILDIQTQTPLNDQATKAKSTQ
DLSEGISRKDGDEVCESNVSNSTTSGEKVISVELGLDNGHSAIQTGTLILEEIETIKEKQ
DVQPQQASPLETSETDHQQPVLSDVPPLPAIPDQQIVEEASNSTLESAPNGKDYESTEIV
AEETKPKDTELSQESDFKENGITEEKSKSEESKRMEPIAIIITDTEISEFDVTKSKNVPK
QFLISAENEQVGVFANDNGFEDRTSEQYETLLIETASSLVKNAIQLSIEQLVNEMASDDN
KINNLLQ
Gene Ontology
GO:0005829; C:cytosol; TAS:Reactome
GO:0005886; C:plasma membrane; TAS:Reactome
GO:0008179; F:adenylate cyclase binding; IPI:UniProtKB
GO:0051018; F:protein kinase A binding; TAS:ProtInc
GO:0006112; P:energy reserve metabolic process; TAS:Reactome
GO:0030819; P:positive regulation of cAMP biosynthetic process; IMP:UniProtKB
GO:0010739; P:positive regulation of protein kinase A signaling; IMP:UniProtKB
GO:0006605; P:protein targeting; IEA:InterPro
GO:0050796; P:regulation of insulin secretion; TAS:Reactome
GO:0007165; P:signal transduction; NAS:ProtInc
GO:0044281; P:small molecule metabolic process; TAS:Reactome
GO:0007268; P:synaptic transmission; TAS:Reactome
Interpro
InterPro; IPR001573; Pkinase-A_anch_WSK-motif
Pfam
Pfam; PF03832; WSK;
SMART
PROSITE
PRINTS