CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-011011
UniProt Accession
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
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
54AASDPATKLLQKNGQubiquitination[1]
122VSKRDSDKEMATKSAubiquitination[1]
173QANDIGFKKVFKFVGubiquitination[2]
177IGFKKVFKFVGFKFTubiquitination[1, 2, 3, 4]
182VFKFVGFKFTVKKDKubiquitination[1, 2, 3, 4]
189KFTVKKDKTEKPDTVubiquitination[1, 2]
192VKKDKTEKPDTVQLLubiquitination[1]
203VQLLTVKKDEGEGAAubiquitination[1]
228GAGEAASKESEPKQSubiquitination[1]
279KQEKEPSKSAESPTSubiquitination[1]
297SETGSTFKKFFTQGWubiquitination[1, 2]
298ETGSTFKKFFTQGWAubiquitination[3]
315RKKTSFRKPKEDEVEubiquitination[1]
317KTSFRKPKEDEVEASubiquitination[1, 2]
342VDTEEDGKAEVASEKubiquitination[1]
376RLSAEYEKVELPSEEubiquitination[1, 2]
395SQGPSEEKPAPLATEubiquitination[1, 2]
432EERTEEQKTEVEETAubiquitination[1, 2]
461PQEAEPAKELVKLKEubiquitination[1, 2]
467AKELVKLKETCVSGEubiquitination[1]
491PDEKVLSKPPEGVVSubiquitination[1, 2]
602GATSDGEKKREGVTPubiquitination[1]
614VTPWASFKKMVTPKKacetylation[5]
639EDELDKVKSATLSSTubiquitination[1]
670EPKPEEPKRKVDTSVubiquitination[1]
672KPEEPKRKVDTSVSWubiquitination[1, 2]
689LICVGSSKKRARRGSubiquitination[1, 2]
763VSTWESFKRLVTPRKubiquitination[1, 2]
800TPDTEPGKEESWVSIubiquitination[1, 2]
808EESWVSIKKFIPGRRubiquitination[1, 2]
859YDAVEREKMEAQQAQubiquitination[1]
867MEAQQAQKSAEQPEQubiquitination[1, 2]
875SAEQPEQKAATEVSKubiquitination[1, 2]
882KAATEVSKELSESQVubiquitination[1]
1049VLQAVAEKVKEESQLubiquitination[1, 2]
1051QAVAEKVKEESQLPGubiquitination[1, 2]
1087QAEASGLKKETDVVLubiquitination[1, 2]
1102KVDAQEAKTEPFTQGubiquitination[1, 2]
1110TEPFTQGKVVGQTTPubiquitination[1, 2]
1234FVFQEETKEQSKMEDubiquitination[1]
1260ETVSILSKTEGTQEAubiquitination[1]
1274ADQYADEKTKDVPFFubiquitination[1, 2]
1316TEEAECKKDDALELQubiquitination[1]
1456AHLVLEEKSSEKNEDubiquitination[1]
1493VIVSATTKKGLSSDLubiquitination[1]
1548ELETKSSKLVQNIIQubiquitination[2]
1584QTQAHVIKADSQDAGubiquitination[1]
1690LLAERIEKSLVEPKEubiquitination[1]
1700VEPKEDEKGDDVDDPubiquitination[1, 2]
1725DASGGLTKESPDTNGubiquitination[1, 2]
1750EVELQEGKVHSESDKubiquitination[1]
1776KQERESAKSELTES*ubiquitination[1, 2]
Reference
 [1] Systematic and quantitative assessment of the ubiquitin-modified proteome.
 Kim W, Bennett EJ, Huttlin EL, Guo A, Li J, Possemato A, Sowa ME, Rad R, Rush J, Comb MJ, Harper JW, Gygi SP.
 Mol Cell. 2011 Oct 21;44(2):325-40. [PMID: 21906983]
 [2] Landscape of the PARKIN-dependent ubiquitylome in response to mitochondrial depolarization.
 Sarraf SA, Raman M, Guarani-Pereira V, Sowa ME, Huttlin EL, Gygi SP, Harper JW.
 Nature. 2013 Apr 18;496(7445):372-6. [PMID: 23503661]
 [3] A proteome-wide, quantitative survey of in vivo ubiquitylation sites reveals widespread regulatory roles.
 Wagner SA, Beli P, Weinert BT, Nielsen ML, Cox J, Mann M, Choudhary C.
 Mol Cell Proteomics. 2011 Oct;10(10):M111.013284. [PMID: 21890473]
 [4] Systems-wide analysis of ubiquitylation dynamics reveals a key role for PAF15 ubiquitylation in DNA-damage bypass.
 Povlsen LK, Beli P, Wagner SA, Poulsen SL, Sylvestersen KB, Poulsen JW, Nielsen ML, Bekker-Jensen S, Mailand N, Choudhary C.
 Nat Cell Biol. 2012 Oct;14(10):1089-98. [PMID: 23000965]
 [5] Spermidine and resveratrol induce autophagy by distinct pathways converging on the acetylproteome.
 Morselli E, Mariño G, Bennetzen MV, Eisenberg T, Megalou E, Schroeder S, Cabrera S, Bénit P, Rustin P, Criollo A, Kepp O, Galluzzi L, Shen S, Malik SA, Maiuri MC, Horio Y, López-Otín C, Andersen JS, Tavernarakis N, Madeo F, Kroemer G.
 J Cell Biol. 2011 Feb 21;192(4):615-29. [PMID: 21339330] 
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 (Probable).
 REGION 1541 1554 RII-binding (Probable).
 MOD_RES 19 19 Phosphoserine (By similarity).
 MOD_RES 75 75 Phosphoserine.
 MOD_RES 96 96 Phosphoserine.
 MOD_RES 219 219 Phosphoserine.
 MOD_RES 371 371 Phosphoserine.
 MOD_RES 374 374 Phosphotyrosine (By similarity).
 MOD_RES 381 381 Phosphoserine.
 MOD_RES 483 483 Phosphoserine.
 MOD_RES 505 505 Phosphoserine.
 MOD_RES 557 557 Phosphoserine.
 MOD_RES 598 598 Phosphoserine.
 MOD_RES 612 612 Phosphoserine.
 MOD_RES 627 627 Phosphoserine.
 MOD_RES 629 629 Phosphoserine (By similarity).
 MOD_RES 645 645 Phosphoserine.
 MOD_RES 646 646 Phosphothreonine (By similarity).
 MOD_RES 648 648 Phosphoserine (By similarity).
 MOD_RES 696 696 Phosphoserine (By similarity).
 MOD_RES 697 697 Phosphoserine (By similarity).
 MOD_RES 698 698 Phosphoserine (By similarity).
 MOD_RES 1331 1331 Phosphoserine.
 MOD_RES 1395 1395 Phosphoserine.
 MOD_RES 1587 1587 Phosphoserine.
 LIPID 2 2 N-myristoyl glycine.  
Keyword
 Alternative splicing; Complete proteome; Cytoplasm; Cytoskeleton; Lipoprotein; Myristate; Phosphoprotein; Polymorphism; Reference proteome; Repeat. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 1782 AA 
Protein Sequence
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 
Gene Ontology
 GO:0005938; C:cell cortex; IEA:UniProtKB-SubCell.
 GO:0005737; C:cytoplasm; IDA:HPA.
 GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell.
 GO:0005886; C:plasma membrane; IDA:HPA.
 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 cascade; IMP:UniProtKB.
 GO:0006605; P:protein targeting; IEA:InterPro. 
Interpro
 IPR001573; Pkinase-A_anch_WSK-motif.
 IPR018459; RII_binding_1. 
Pfam
 PF10522; RII_binding_1
 PF03832; WSK 
SMART
  
PROSITE
  
PRINTS