Lipid Modification Database
Tag Content
LipidDB ID
LipidDB-9606-00992
Entry Name
UniProt Accession
Theoretical PI
4.37
Molecular Weight
191481.78
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
A-kinase anchor protein 12
Protein Synonyms/Alias
AKAP-12; A-kinase anchor protein 250 kDa; AKAP 250; Gravin; Myasthenia gravis autoantigen;
Gene Name
AKAP12
Gene Synonyms/Alias
AKAP250;
Created Date
01-FEB-1994
 Lipid Modification Sites 
 Position   Sequence Form   Peptide   References   Modification Type 
2
Canonical
******MGAGSSTEQ
[1]
N-Myristoylation
Organism
Homo sapiens (Human)
NCBI Taxa ID
9606
Reference
[1] Suzuki T, Moriya K, Nagatoshi K, Ota Y, Ezure T, Ando E, Tsunasawa S, UtsumiT. Strategy for comprehensive identification of human N-myristoylated proteinsusing an insect cell-free protein synthesis system. Proteomics. 2010May;10(9):1780-93. doi: 10.1002/pmic.200900783.[PMID:20213681]
Functional Description
Anchoring protein that mediates the subcellular compartmentation of protein kinase A (PKA) and protein kinase C (PKC).
Sequence Annotation
Domain: 604 634 AKAP 1.
Domain: 753 783 AKAP 2.
Domain: 798 828 AKAP 3.
Region: 266 557 Involved in PKC-binding.
Region: 1541 1554 RII-binding.
Modified residue: 75 75 Phosphoserine.
Modified residue: 96 96 Phosphoserine.
Modified residue: 219 219 Phosphoserine.
Modified residue: 371 371 Phosphoserine.
Modified residue: 374 374 Phosphotyrosine.
Modified residue: 381 381 Phosphoserine.
Modified residue: 483 483 Phosphoserine.
Modified residue: 505 505 Phosphoserine.
Modified residue: 557 557 Phosphoserine.
Modified residue: 598 598 Phosphoserine.
Modified residue: 612 612 Phosphoserine.
Modified residue: 627 627 Phosphoserine.
Modified residue: 645 645 Phosphoserine.
Modified residue: 696 696 Phosphoserine.
Modified residue: 697 697 Phosphoserine.
Modified residue: 698 698 Phosphoserine.
Modified residue: 1331 1331 Phosphoserine.
Modified residue: 1395 1395 Phosphoserine.
Modified residue: 1587 1587 Phosphoserine.
Protein Length
1782 AA.
Protein Sequence
(Canonical)
MGAGSSTEQR SPEQPPEGSS TPAEPEPSGG GPSAEAAPDT TADPAIAASD PATKLLQKNG  60
QLSTINGVAE QDELSLQEGD LNGQKGALNG QGALNSQEEE EVIVTEVGQR DSEDVSKRDS  120
DKEMATKSAV VHDITDDGQE ETPEIIEQIP SSESNLEELT QPTESQANDI GFKKVFKFVG  180
FKFTVKKDKT EKPDTVQLLT VKKDEGEGAA GAGDHKDPSL GAGEAASKES EPKQSTEKPE  240
ETLKREQSHA EISPPAESGQ AVEECKEEGE EKQEKEPSKS AESPTSPVTS ETGSTFKKFF  300
TQGWAGWRKK TSFRKPKEDE VEASEKKKEQ EPEKVDTEED GKAEVASEKL TASEQAHPQE  360
PAESAHEPRL SAEYEKVELP SEEQVSGSQG PSEEKPAPLA TEVFDEKIEV HQEEVVAEVH  420
VSTVEERTEE QKTEVEETAG SVPAEELVEM DAEPQEAEPA KELVKLKETC VSGEDPTQGA  480
DLSPDEKVLS KPPEGVVSEV EMLSSQERMK VQGSPLKKLF TSTGLKKLSG KKQKGKRGGG  540
DEESGEHTQV PADSPDSQEE QKGESSASSP EEPEEITCLE KGLAEVQQDG EAEEGATSDG  600
EKKREGVTPW ASFKKMVTPK KRVRRPSESD KEDELDKVKS ATLSSTESTA SEMQEEMKGS  660
VEEPKPEEPK RKVDTSVSWE ALICVGSSKK RARRGSSSDE EGGPKAMGGD HQKADEAGKD  720
KETGTDGILA GSQEHDPGQG SSSPEQAGSP TEGEGVSTWE SFKRLVTPRK KSKSKLEEKS  780
EDSIAGSGVE HSTPDTEPGK EESWVSIKKF IPGRRKKRPD GKQEQAPVED AGPTGANEDD  840
SDVPAVVPLS EYDAVEREKM EAQQAQKSAE QPEQKAATEV SKELSESQVH MMAAAVADGT  900
RAATIIEERS PSWISASVTE PLEQVEAEAA LLTEEVLERE VIAEEEPPTV TEPLPENREA  960
RGDTVVSEAE LTPEAVTAAE TAGPLGAEEG TEASAAEETT EMVSAVSQLT DSPDTTEEAT  1020
PVQEVEGGVP DIEEQERRTQ EVLQAVAEKV KEESQLPGTG GPEDVLQPVQ RAEAERPEEQ  1080
AEASGLKKET DVVLKVDAQE AKTEPFTQGK VVGQTTPESF EKAPQVTESI ESSELVTTCQ  1140
AETLAGVKSQ EMVMEQAIPP DSVETPTDSE TDGSTPVADF DAPGTTQKDE IVEIHEENEV  1200
ASGTQSGGTE AEAVPAQKER PPAPSSFVFQ EETKEQSKME DTLEHTDKEV SVETVSILSK  1260
TEGTQEADQY ADEKTKDVPF FEGLEGSIDT GITVSREKVT EVALKGEGTE EAECKKDDAL  1320
ELQSHAKSPP SPVEREMVVQ VEREKTEAEP THVNEEKLEH ETAVTVSEEV SKQLLQTVNV  1380
PIIDGAKEVS SLEGSPPPCL GQEEAVCTKI QVQSSEASFT LTAAAEEEKV LGETANILET  1440
GETLEPAGAH LVLEEKSSEK NEDFAAHPGE DAVPTGPDCQ AKSTPVIVSA TTKKGLSSDL  1500
EGEKTTSLKW KSDEVDEQVA CQEVKVSVAI EDLEPENGIL ELETKSSKLV QNIIQTAVDQ  1560
FVRTEETATE MLTSELQTQA HVIKADSQDA GQETEKEGEE PQASAQDETP ITSAKEESES  1620
TAVGQAHSDI SKDMSEASEK TMTVEVEGST VNDQQLEEVV LPSEEEGGGA GTKSVPEDDG  1680
HALLAERIEK SLVEPKEDEK GDDVDDPENQ NSALADTDAS GGLTKESPDT NGPKQKEKED  1740
AQEVELQEGK VHSESDKAIT PQAQEELQKQ ERESAKSELT ES                     1782
FASTA
(Canonical)
>LipidDB-9606-00992|Q02952
MGAGSSTEQRSPEQPPEGSSTPAEPEPSGGGPSAEAAPDTTADPAIAASDPATKLLQKNG
QLSTINGVAEQDELSLQEGDLNGQKGALNGQGALNSQEEEEVIVTEVGQRDSEDVSKRDS
DKEMATKSAVVHDITDDGQEETPEIIEQIPSSESNLEELTQPTESQANDIGFKKVFKFVG
FKFTVKKDKTEKPDTVQLLTVKKDEGEGAAGAGDHKDPSLGAGEAASKESEPKQSTEKPE
ETLKREQSHAEISPPAESGQAVEECKEEGEEKQEKEPSKSAESPTSPVTSETGSTFKKFF
TQGWAGWRKKTSFRKPKEDEVEASEKKKEQEPEKVDTEEDGKAEVASEKLTASEQAHPQE
PAESAHEPRLSAEYEKVELPSEEQVSGSQGPSEEKPAPLATEVFDEKIEVHQEEVVAEVH
VSTVEERTEEQKTEVEETAGSVPAEELVEMDAEPQEAEPAKELVKLKETCVSGEDPTQGA
DLSPDEKVLSKPPEGVVSEVEMLSSQERMKVQGSPLKKLFTSTGLKKLSGKKQKGKRGGG
DEESGEHTQVPADSPDSQEEQKGESSASSPEEPEEITCLEKGLAEVQQDGEAEEGATSDG
EKKREGVTPWASFKKMVTPKKRVRRPSESDKEDELDKVKSATLSSTESTASEMQEEMKGS
VEEPKPEEPKRKVDTSVSWEALICVGSSKKRARRGSSSDEEGGPKAMGGDHQKADEAGKD
KETGTDGILAGSQEHDPGQGSSSPEQAGSPTEGEGVSTWESFKRLVTPRKKSKSKLEEKS
EDSIAGSGVEHSTPDTEPGKEESWVSIKKFIPGRRKKRPDGKQEQAPVEDAGPTGANEDD
SDVPAVVPLSEYDAVEREKMEAQQAQKSAEQPEQKAATEVSKELSESQVHMMAAAVADGT
RAATIIEERSPSWISASVTEPLEQVEAEAALLTEEVLEREVIAEEEPPTVTEPLPENREA
RGDTVVSEAELTPEAVTAAETAGPLGAEEGTEASAAEETTEMVSAVSQLTDSPDTTEEAT
PVQEVEGGVPDIEEQERRTQEVLQAVAEKVKEESQLPGTGGPEDVLQPVQRAEAERPEEQ
AEASGLKKETDVVLKVDAQEAKTEPFTQGKVVGQTTPESFEKAPQVTESIESSELVTTCQ
AETLAGVKSQEMVMEQAIPPDSVETPTDSETDGSTPVADFDAPGTTQKDEIVEIHEENEV
ASGTQSGGTEAEAVPAQKERPPAPSSFVFQEETKEQSKMEDTLEHTDKEVSVETVSILSK
TEGTQEADQYADEKTKDVPFFEGLEGSIDTGITVSREKVTEVALKGEGTEEAECKKDDAL
ELQSHAKSPPSPVEREMVVQVEREKTEAEPTHVNEEKLEHETAVTVSEEVSKQLLQTVNV
PIIDGAKEVSSLEGSPPPCLGQEEAVCTKIQVQSSEASFTLTAAAEEEKVLGETANILET
GETLEPAGAHLVLEEKSSEKNEDFAAHPGEDAVPTGPDCQAKSTPVIVSATTKKGLSSDL
EGEKTTSLKWKSDEVDEQVACQEVKVSVAIEDLEPENGILELETKSSKLVQNIIQTAVDQ
FVRTEETATEMLTSELQTQAHVIKADSQDAGQETEKEGEEPQASAQDETPITSAKEESES
TAVGQAHSDISKDMSEASEKTMTVEVEGSTVNDQQLEEVVLPSEEEGGGAGTKSVPEDDG
HALLAERIEKSLVEPKEDEKGDDVDDPENQNSALADTDASGGLTKESPDTNGPKQKEKED
AQEVELQEGKVHSESDKAITPQAQEELQKQERESAKSELTES
Gene Ontology
GO:0005737; C:cytoplasm; TAS:ProtInc
GO:0005856; C:cytoskeleton; IEA:UniProtKB-KW
GO:0005925; C:focal adhesion; IDA:UniProtKB
GO:0008179; F:adenylate cyclase binding; IPI:UniProtKB
GO:0051018; F:protein kinase A binding; TAS:ProtInc
GO:0007186; P:G-protein coupled receptor signaling pathway; TAS:ProtInc
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:0090036; P:regulation of protein kinase C signaling; IEA:InterPro
Interpro
InterPro; IPR028540; AKAP12
InterPro; IPR001573; Pkinase-A_anch_WSK-motif
InterPro; IPR018459; RII_binding_1
Pfam
Pfam; PF10522; RII_binding_1;
Pfam; PF03832; WSK;
SMART
PROSITE
PRINTS