AKA12_HUMAN
ID AKA12_HUMAN Reviewed; 1782 AA.
AC Q02952; O00310; O00498; Q4LE68; Q5SZ80; Q5TGN1; Q68D82; Q99970;
DT 01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT 11-JAN-2011, sequence version 4.
DT 03-AUG-2022, entry version 193.
DE RecName: Full=A-kinase anchor protein 12;
DE Short=AKAP-12;
DE AltName: Full=A-kinase anchor protein 250 kDa;
DE Short=AKAP 250;
DE AltName: Full=Gravin;
DE AltName: Full=Myasthenia gravis autoantigen;
GN Name=AKAP12; Synonyms=AKAP250;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND VARIANTS GLU-117; GLN-216 AND
RP SER-987.
RC TISSUE=Heart;
RX PubMed=9000000; DOI=10.1016/s0960-9822(06)00027-3;
RA Nauert J.B., Klauck T.M., Langeberg L.K., Scott J.D.;
RT "Gravin, an autoantigen recognized by serum from myasthenia gravis
RT patients, is a kinase scaffold protein.";
RL Curr. Biol. 7:52-62(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
RC TISSUE=Umbilical vein endothelial cell;
RX PubMed=9604001; DOI=10.1093/oxfordjournals.jbchem.a022051;
RA Sato N., Kokame K., Shimokado K., Kato H., Miyata T.;
RT "Changes of gene expression by lysophosphatidylcholine in vascular
RT endothelial cells: 12 up-regulated distinct genes including 5 cell growth-
RT related, 3 thrombosis-related, and 4 others.";
RL J. Biochem. 123:1119-1126(1998).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANTS GLU-117;
RP GLN-216 AND ASP-1600.
RC TISSUE=Brain;
RA Nakajima D., Saito K., Yamakawa H., Kikuno R.F., Nakayama M., Ohara R.,
RA Okazaki N., Koga H., Nagase T., Ohara O.;
RT "Preparation of a set of expression-ready clones of mammalian long cDNAs
RT encoding large proteins by the ORF trap cloning method.";
RL Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3), AND VARIANTS GLN-216;
RP GLY-920 AND LYS-1355.
RC TISSUE=Testis;
RX PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D.,
RA Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A.,
RA Wiemann S., Schupp I.;
RT "The full-ORF clone resource of the German cDNA consortium.";
RL BMC Genomics 8:399-399(2007).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=14574404; DOI=10.1038/nature02055;
RA Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L.,
RA Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., Gilbert J.G.R.,
RA Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D.,
RA Andrews T.D., Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J.,
RA Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H.,
RA Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J.,
RA Brown J.Y., Burford D.C., Burrill W., Burton J., Carder C., Carter N.P.,
RA Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V.,
RA Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J.,
RA Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., Ellington A.E.,
RA Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J.,
RA French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J.,
RA Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C.,
RA Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A.,
RA Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R.,
RA Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M.,
RA Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K.,
RA Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R.,
RA Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M.,
RA Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A.,
RA Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L.,
RA Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I.,
RA Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y.,
RA Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E.,
RA Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A.,
RA Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W.,
RA Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M.,
RA West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J.,
RA Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M.,
RA Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I.,
RA Rogers J., Beck S.;
RT "The DNA sequence and analysis of human chromosome 6.";
RL Nature 425:805-811(2003).
RN [6]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 43-1782, AND VARIANTS GLU-117 AND GLN-216.
RC TISSUE=Umbilical vein endothelial cell;
RA Bowditch R.D., Ginsberg M.H.;
RT "Sequence of gravin cDNA isolated from a human umbilical vein endothelial
RT cell library.";
RL Submitted (APR-1997) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 1478-1782.
RC TISSUE=Umbilical vein endothelial cell;
RX PubMed=1522245; DOI=10.1172/jci115976;
RA Gordon T., Grove B., Loftus J.C., O'Toole T., McMillan R., Lindstrom J.,
RA Ginsberg M.H.;
RT "Molecular cloning and preliminary characterization of a novel cytoplasmic
RT antigen recognized by myasthenia gravis sera.";
RL J. Clin. Invest. 90:992-999(1992).
RN [8]
RP ALTERNATIVE SPLICING.
RX PubMed=15496411; DOI=10.1074/jbc.m408828200;
RA Streb J.W., Kitchen C.M., Gelman I.H., Miano J.M.;
RT "Multiple promoters direct expression of three AKAP12 isoforms with
RT distinct subcellular and tissue distribution profiles.";
RL J. Biol. Chem. 279:56014-56023(2004).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-219, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
RA Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.;
RT "Global, in vivo, and site-specific phosphorylation dynamics in signaling
RT networks.";
RL Cell 127:635-648(2006).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-505, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic kidney;
RX PubMed=17525332; DOI=10.1126/science.1140321;
RA Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III, Hurov K.E.,
RA Luo J., Bakalarski C.E., Zhao Z., Solimini N., Lerenthal Y., Shiloh Y.,
RA Gygi S.P., Elledge S.J.;
RT "ATM and ATR substrate analysis reveals extensive protein networks
RT responsive to DNA damage.";
RL Science 316:1160-1166(2007).
RN [11]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a
RT refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1395, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19369195; DOI=10.1074/mcp.m800588-mcp200;
RA Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G.,
RA Mann M., Daub H.;
RT "Large-scale proteomics analysis of the human kinome.";
RL Mol. Cell. Proteomics 8:1751-1764(2009).
RN [13]
RP MYRISTOYLATION AT GLY-2.
RX PubMed=20213681; DOI=10.1002/pmic.200900783;
RA Suzuki T., Moriya K., Nagatoshi K., Ota Y., Ezure T., Ando E.,
RA Tsunasawa S., Utsumi T.;
RT "Strategy for comprehensive identification of human N-myristoylated
RT proteins using an insect cell-free protein synthesis system.";
RL Proteomics 10:1780-1793(2010).
RN [14]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [15]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-75; SER-96; SER-371; SER-381;
RP SER-483; SER-557; SER-598; SER-612; SER-627; SER-645; SER-1331 AND
RP SER-1587, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T.,
RA Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.;
RT "System-wide temporal characterization of the proteome and phosphoproteome
RT of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [16]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-612; SER-627 AND SER-629, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma, and Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [17]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-154; SER-483; SER-598;
RP SER-612; SER-627; SER-696; SER-697; SER-698; SER-761; SER-1328; SER-1395
RP AND SER-1587, VARIANT [LARGE SCALE ANALYSIS] GLU-117, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [18]
RP MYRISTOYLATION AT GLY-2, CLEAVAGE OF INITIATOR METHIONINE, AND
RP IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=25255805; DOI=10.1038/ncomms5919;
RA Thinon E., Serwa R.A., Broncel M., Brannigan J.A., Brassat U., Wright M.H.,
RA Heal W.P., Wilkinson A.J., Mann D.J., Tate E.W.;
RT "Global profiling of co- and post-translationally N-myristoylated proteomes
RT in human cells.";
RL Nat. Commun. 5:4919-4919(2014).
RN [19]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-1051, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25114211; DOI=10.1073/pnas.1413825111;
RA Impens F., Radoshevich L., Cossart P., Ribet D.;
RT "Mapping of SUMO sites and analysis of SUMOylation changes induced by
RT external stimuli.";
RL Proc. Natl. Acad. Sci. U.S.A. 111:12432-12437(2014).
RN [20]
RP MYRISTOYLATION AT GLY-2, CLEAVAGE OF INITIATOR METHIONINE, AND
RP IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=25807930; DOI=10.1002/anie.201500342;
RA Broncel M., Serwa R.A., Ciepla P., Krause E., Dallman M.J., Magee A.I.,
RA Tate E.W.;
RT "Multifunctional reagents for quantitative proteome-wide analysis of
RT protein modification in human cells and dynamic profiling of protein
RT lipidation during vertebrate development.";
RL Angew. Chem. Int. Ed. 54:5948-5951(2015).
RN [21]
RP VARIANT [LARGE SCALE ANALYSIS] LYS-240.
RX PubMed=16959974; DOI=10.1126/science.1133427;
RA Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D.,
RA Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., Buckhaults P.,
RA Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V.,
RA Gazdar A.F., Hartigan J., Wu L., Liu C., Parmigiani G., Park B.H.,
RA Bachman K.E., Papadopoulos N., Vogelstein B., Kinzler K.W.,
RA Velculescu V.E.;
RT "The consensus coding sequences of human breast and colorectal cancers.";
RL Science 314:268-274(2006).
CC -!- FUNCTION: Anchoring protein that mediates the subcellular
CC compartmentation of protein kinase A (PKA) and protein kinase C (PKC).
CC -!- SUBUNIT: Binds to dimeric RII-alpha regulatory subunit of PKC.
CC -!- INTERACTION:
CC Q02952; P00533: EGFR; NbExp=3; IntAct=EBI-2562430, EBI-297353;
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cell cortex {ECO:0000305}. Cytoplasm,
CC cytoskeleton {ECO:0000305}. Membrane {ECO:0000305}; Lipid-anchor
CC {ECO:0000305}. Note=May be part of the cortical cytoskeleton.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1; Synonyms=Alpha;
CC IsoId=Q02952-1; Sequence=Displayed;
CC Name=2; Synonyms=Beta;
CC IsoId=Q02952-2; Sequence=VSP_004110, VSP_004111;
CC Name=3; Synonyms=Gamma;
CC IsoId=Q02952-3; Sequence=VSP_028133, VSP_028134;
CC -!- TISSUE SPECIFICITY: Expressed in endothelial cells, cultured
CC fibroblasts and osteosarcoma, but not in platelets, leukocytes,
CC monocytic cell lines or peripherical blood cells.
CC -!- INDUCTION: Activated by lysophosphatidylcholine (lysoPC).
CC -!- DOMAIN: Polybasic regions located between residues 266 and 557 are
CC involved in binding PKC.
CC -!- MISCELLANEOUS: Antibodies against the C-terminal of gravin can be
CC produced by patients with myasthenia gravis (MG).
CC -!- SEQUENCE CAUTION:
CC Sequence=BAE06085.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC -!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology and
CC Haematology;
CC URL="http://atlasgeneticsoncology.org/Genes/AKAP12ID607ch6q25.html";
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DR EMBL; U81607; AAC51366.1; -; mRNA.
DR EMBL; AB003476; BAA19927.1; -; mRNA.
DR EMBL; AB210003; BAE06085.1; ALT_INIT; mRNA.
DR EMBL; CR749527; CAH18338.1; -; mRNA.
DR EMBL; AL590413; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL356535; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL033392; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AF001504; AAB58938.1; -; mRNA.
DR EMBL; M96322; AAA35931.1; -; mRNA.
DR CCDS; CCDS5229.1; -. [Q02952-1]
DR CCDS; CCDS5230.1; -. [Q02952-2]
DR PIR; A43922; A43922.
DR PIR; JW0057; JW0057.
DR RefSeq; NP_005091.2; NM_005100.3. [Q02952-1]
DR RefSeq; NP_653080.1; NM_144497.2. [Q02952-2]
DR RefSeq; XP_005267292.1; XM_005267235.2.
DR RefSeq; XP_016867006.1; XM_017011517.1. [Q02952-1]
DR AlphaFoldDB; Q02952; -.
DR SMR; Q02952; -.
DR BioGRID; 114958; 119.
DR CORUM; Q02952; -.
DR IntAct; Q02952; 60.
DR MINT; Q02952; -.
DR STRING; 9606.ENSP00000384537; -.
DR ChEMBL; CHEMBL4295800; -.
DR GlyGen; Q02952; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q02952; -.
DR MetOSite; Q02952; -.
DR PhosphoSitePlus; Q02952; -.
DR SwissPalm; Q02952; -.
DR BioMuta; AKAP12; -.
DR DMDM; 317373554; -.
DR EPD; Q02952; -.
DR jPOST; Q02952; -.
DR MassIVE; Q02952; -.
DR MaxQB; Q02952; -.
DR PaxDb; Q02952; -.
DR PeptideAtlas; Q02952; -.
DR PRIDE; Q02952; -.
DR ProteomicsDB; 58141; -. [Q02952-1]
DR ProteomicsDB; 58142; -. [Q02952-2]
DR ProteomicsDB; 58143; -. [Q02952-3]
DR Antibodypedia; 1199; 236 antibodies from 38 providers.
DR DNASU; 9590; -.
DR Ensembl; ENST00000253332.5; ENSP00000253332.1; ENSG00000131016.17. [Q02952-1]
DR Ensembl; ENST00000354675.10; ENSP00000346702.6; ENSG00000131016.17. [Q02952-2]
DR Ensembl; ENST00000359755.5; ENSP00000352794.5; ENSG00000131016.17. [Q02952-3]
DR Ensembl; ENST00000402676.7; ENSP00000384537.2; ENSG00000131016.17. [Q02952-1]
DR GeneID; 9590; -.
DR KEGG; hsa:9590; -.
DR MANE-Select; ENST00000402676.7; ENSP00000384537.2; NM_005100.4; NP_005091.2.
DR UCSC; uc003qoe.5; human. [Q02952-1]
DR CTD; 9590; -.
DR DisGeNET; 9590; -.
DR GeneCards; AKAP12; -.
DR HGNC; HGNC:370; AKAP12.
DR HPA; ENSG00000131016; Low tissue specificity.
DR MIM; 604698; gene.
DR neXtProt; NX_Q02952; -.
DR OpenTargets; ENSG00000131016; -.
DR PharmGKB; PA24664; -.
DR VEuPathDB; HostDB:ENSG00000131016; -.
DR eggNOG; ENOG502RDV6; Eukaryota.
DR GeneTree; ENSGT00730000111244; -.
DR HOGENOM; CLU_002691_0_0_1; -.
DR InParanoid; Q02952; -.
DR OMA; AWEPVEL; -.
DR OrthoDB; 158752at2759; -.
DR PhylomeDB; Q02952; -.
DR TreeFam; TF105411; -.
DR PathwayCommons; Q02952; -.
DR Reactome; R-HSA-9013405; RHOD GTPase cycle.
DR Reactome; R-HSA-9035034; RHOF GTPase cycle.
DR SignaLink; Q02952; -.
DR BioGRID-ORCS; 9590; 17 hits in 1078 CRISPR screens.
DR ChiTaRS; AKAP12; human.
DR GeneWiki; AKAP12; -.
DR GenomeRNAi; 9590; -.
DR Pharos; Q02952; Tbio.
DR PRO; PR:Q02952; -.
DR Proteomes; UP000005640; Chromosome 6.
DR RNAct; Q02952; protein.
DR Bgee; ENSG00000131016; Expressed in pons and 205 other tissues.
DR Genevisible; Q02952; HS.
DR GO; GO:0005938; C:cell cortex; IEA:UniProtKB-SubCell.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell.
DR GO; GO:0005829; C:cytosol; IDA:HPA.
DR GO; GO:0005925; C:focal adhesion; HDA:UniProtKB.
DR GO; GO:0043025; C:neuronal cell body; IEA:Ensembl.
DR GO; GO:0005886; C:plasma membrane; IDA:HPA.
DR GO; GO:0098685; C:Schaffer collateral - CA1 synapse; IEA:Ensembl.
DR GO; GO:0008179; F:adenylate cyclase binding; IPI:UniProtKB.
DR GO; GO:0005516; F:calmodulin binding; IEA:UniProtKB-KW.
DR GO; GO:0051018; F:protein kinase A binding; TAS:ProtInc.
DR GO; GO:0007193; P:adenylate cyclase-inhibiting G protein-coupled receptor signaling pathway; IMP:UniProtKB.
DR GO; GO:0071347; P:cellular response to interleukin-1; IEA:Ensembl.
DR GO; GO:0071356; P:cellular response to tumor necrosis factor; IEA:Ensembl.
DR GO; GO:0007186; P:G protein-coupled receptor signaling pathway; TAS:ProtInc.
DR GO; GO:0035733; P:hepatic stellate cell activation; IEA:Ensembl.
DR GO; GO:0050804; P:modulation of chemical synaptic transmission; IEA:Ensembl.
DR GO; GO:0043116; P:negative regulation of vascular permeability; IEA:Ensembl.
DR GO; GO:0070374; P:positive regulation of ERK1 and ERK2 cascade; IEA:Ensembl.
DR GO; GO:0061870; P:positive regulation of hepatic stellate cell migration; IEA:Ensembl.
DR GO; GO:0051770; P:positive regulation of nitric-oxide synthase biosynthetic process; IEA:Ensembl.
DR GO; GO:1900143; P:positive regulation of oligodendrocyte apoptotic process; IEA:Ensembl.
DR GO; GO:0010739; P:positive regulation of protein kinase A signaling; IEA:InterPro.
DR GO; GO:0032760; P:positive regulation of tumor necrosis factor production; IEA:Ensembl.
DR GO; GO:0010738; P:regulation of protein kinase A signaling; IMP:UniProtKB.
DR GO; GO:0090036; P:regulation of protein kinase C signaling; IEA:InterPro.
DR GO; GO:0051602; P:response to electrical stimulus; IEA:Ensembl.
DR GO; GO:0032496; P:response to lipopolysaccharide; IEA:Ensembl.
DR GO; GO:0007165; P:signal transduction; IBA:GO_Central.
DR InterPro; IPR028540; AKAP12.
DR InterPro; IPR001573; AKAP_WSK.
DR InterPro; IPR018459; RII-bd_1.
DR PANTHER; PTHR23209; PTHR23209; 1.
DR Pfam; PF10522; RII_binding_1; 1.
DR Pfam; PF03832; WSK; 3.
DR PROSITE; PS51893; AKAP_CAM_BD; 3.
PE 1: Evidence at protein level;
KW Alternative splicing; Calmodulin-binding; Cytoplasm; Cytoskeleton;
KW Isopeptide bond; Lipoprotein; Membrane; Myristate; Phosphoprotein;
KW Reference proteome; Repeat; Ubl conjugation.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:25255805,
FT ECO:0000269|PubMed:25807930"
FT CHAIN 2..1782
FT /note="A-kinase anchor protein 12"
FT /id="PRO_0000064519"
FT REGION 1..53
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 71..169
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 189..400
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 266..557
FT /note="Involved in PKC-binding"
FT /evidence="ECO:0000305"
FT REGION 421..886
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 938..1089
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1105..1134
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1157..1274
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1305..1355
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1541..1554
FT /note="RII-binding"
FT /evidence="ECO:0000305"
FT REGION 1584..1782
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 607..627
FT /note="AKAP CaM-binding 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01241"
FT MOTIF 756..776
FT /note="AKAP CaM-binding 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01241"
FT MOTIF 801..821
FT /note="AKAP CaM-binding 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01241"
FT COMPBIAS 1..17
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 82..98
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 103..139
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 145..168
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 189..212
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 230..251
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 261..279
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 280..299
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 311..347
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 360..380
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 421..436
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 454..469
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 505..519
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 534..549
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 557..579
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 595..609
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 622..640
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 641..655
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 656..675
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 692..723
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 735..756
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 764..785
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 794..809
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 997..1019
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1030..1048
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1069..1089
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1108..1134
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1233..1251
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1305..1323
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1337..1355
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1588..1603
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1605..1628
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1642..1657
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1679..1698
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1710..1729
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1730..1755
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1766..1782
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 11
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q5QD51"
FT MOD_RES 19
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9WTQ5"
FT MOD_RES 28
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9WTQ5"
FT MOD_RES 75
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21406692"
FT MOD_RES 96
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21406692"
FT MOD_RES 154
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 219
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17081983"
FT MOD_RES 248
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9WTQ5"
FT MOD_RES 258
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q5QD51"
FT MOD_RES 280
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q5QD51"
FT MOD_RES 283
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9WTQ5"
FT MOD_RES 286
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9WTQ5"
FT MOD_RES 347
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q5QD51"
FT MOD_RES 371
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21406692"
FT MOD_RES 374
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:Q9WTQ5"
FT MOD_RES 381
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21406692"
FT MOD_RES 392
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9WTQ5"
FT MOD_RES 483
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21406692,
FT ECO:0007744|PubMed:24275569"
FT MOD_RES 505
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17525332"
FT MOD_RES 554
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q5QD51"
FT MOD_RES 557
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21406692"
FT MOD_RES 598
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21406692,
FT ECO:0007744|PubMed:24275569"
FT MOD_RES 612
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21406692,
FT ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569"
FT MOD_RES 627
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21406692,
FT ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569"
FT MOD_RES 629
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 642
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q5QD51"
FT MOD_RES 644
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q5QD51"
FT MOD_RES 645
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21406692"
FT MOD_RES 648
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9WTQ5"
FT MOD_RES 651
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9WTQ5"
FT MOD_RES 696
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 697
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 698
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 749
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9WTQ5"
FT MOD_RES 761
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 787
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9WTQ5"
FT MOD_RES 806
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9WTQ5"
FT MOD_RES 1328
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 1331
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21406692"
FT MOD_RES 1391
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9WTQ5"
FT MOD_RES 1395
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19369195,
FT ECO:0007744|PubMed:24275569"
FT MOD_RES 1587
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21406692,
FT ECO:0007744|PubMed:24275569"
FT MOD_RES 1727
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9WTQ5"
FT LIPID 2
FT /note="N-myristoyl glycine"
FT /evidence="ECO:0000269|PubMed:20213681,
FT ECO:0000269|PubMed:25255805, ECO:0000269|PubMed:25807930"
FT CROSSLNK 1051
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO1)"
FT /evidence="ECO:0007744|PubMed:25114211"
FT VAR_SEQ 1..105
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:17974005"
FT /id="VSP_028133"
FT VAR_SEQ 1..98
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:9604001"
FT /id="VSP_004110"
FT VAR_SEQ 99..106
FT /note="EEEVIVTE -> MLGTITIT (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:9604001"
FT /id="VSP_004111"
FT VAR_SEQ 106
FT /note="E -> M (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:17974005"
FT /id="VSP_028134"
FT VARIANT 117
FT /note="K -> E (in dbSNP:rs10872670)"
FT /evidence="ECO:0000269|PubMed:9000000, ECO:0000269|Ref.3,
FT ECO:0000269|Ref.6, ECO:0007744|PubMed:24275569"
FT /id="VAR_035115"
FT VARIANT 216
FT /note="K -> Q (in dbSNP:rs3734799)"
FT /evidence="ECO:0000269|PubMed:17974005,
FT ECO:0000269|PubMed:9000000, ECO:0000269|Ref.3,
FT ECO:0000269|Ref.6"
FT /id="VAR_035116"
FT VARIANT 240
FT /note="E -> K (in a colorectal cancer sample; somatic
FT mutation; dbSNP:rs552053449)"
FT /evidence="ECO:0000269|PubMed:16959974"
FT /id="VAR_035780"
FT VARIANT 920
FT /note="E -> G (in dbSNP:rs13212161)"
FT /evidence="ECO:0000269|PubMed:17974005"
FT /id="VAR_035117"
FT VARIANT 987
FT /note="A -> S (in dbSNP:rs1042069)"
FT /evidence="ECO:0000269|PubMed:9000000"
FT /id="VAR_056731"
FT VARIANT 1096
FT /note="V -> I (in dbSNP:rs3734797)"
FT /id="VAR_035118"
FT VARIANT 1296
FT /note="R -> L (in dbSNP:rs9478198)"
FT /id="VAR_035119"
FT VARIANT 1355
FT /note="E -> K (in dbSNP:rs12201388)"
FT /evidence="ECO:0000269|PubMed:17974005"
FT /id="VAR_035120"
FT VARIANT 1600
FT /note="E -> D (in dbSNP:rs3823310)"
FT /evidence="ECO:0000269|Ref.3"
FT /id="VAR_035121"
FT VARIANT 1689
FT /note="E -> D (in dbSNP:rs3734795)"
FT /id="VAR_035122"
FT CONFLICT 142..145
FT /note="TPEI -> NRN (in Ref. 1; AAC51366)"
FT /evidence="ECO:0000305"
FT CONFLICT 423
FT /note="T -> I (in Ref. 3; BAE06085)"
FT /evidence="ECO:0000305"
FT CONFLICT 449
FT /note="E -> G (in Ref. 1; AAC51366)"
FT /evidence="ECO:0000305"
FT CONFLICT 695
FT /note="G -> R (in Ref. 1; AAC51366)"
FT /evidence="ECO:0000305"
FT CONFLICT 868
FT /note="S -> G (in Ref. 1; AAC51366)"
FT /evidence="ECO:0000305"
FT CONFLICT 946
FT /note="E -> G (in Ref. 4; CAH18338)"
FT /evidence="ECO:0000305"
FT CONFLICT 1182
FT /note="A -> T (in Ref. 4; CAH18338)"
FT /evidence="ECO:0000305"
FT CONFLICT 1531
FT /note="E -> EE (in Ref. 4; CAH18338, 3; BAE06085, 6;
FT AAB58938 and 7; AAA35931)"
FT /evidence="ECO:0000305"
FT CONFLICT 1582
FT /note="V -> M (in Ref. 4; CAH18338 and 7; AAA35931)"
FT /evidence="ECO:0000305"
FT CONFLICT 1602
FT /note="Q -> L (in Ref. 2; BAA19927)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1782 AA; 191482 MW; DB9DBA4647E6DDD5 CRC64;
MGAGSSTEQR SPEQPPEGSS TPAEPEPSGG GPSAEAAPDT TADPAIAASD PATKLLQKNG
QLSTINGVAE QDELSLQEGD LNGQKGALNG QGALNSQEEE EVIVTEVGQR DSEDVSKRDS
DKEMATKSAV VHDITDDGQE ETPEIIEQIP SSESNLEELT QPTESQANDI GFKKVFKFVG
FKFTVKKDKT EKPDTVQLLT VKKDEGEGAA GAGDHKDPSL GAGEAASKES EPKQSTEKPE
ETLKREQSHA EISPPAESGQ AVEECKEEGE EKQEKEPSKS AESPTSPVTS ETGSTFKKFF
TQGWAGWRKK TSFRKPKEDE VEASEKKKEQ EPEKVDTEED GKAEVASEKL TASEQAHPQE
PAESAHEPRL SAEYEKVELP SEEQVSGSQG PSEEKPAPLA TEVFDEKIEV HQEEVVAEVH
VSTVEERTEE QKTEVEETAG SVPAEELVEM DAEPQEAEPA KELVKLKETC VSGEDPTQGA
DLSPDEKVLS KPPEGVVSEV EMLSSQERMK VQGSPLKKLF TSTGLKKLSG KKQKGKRGGG
DEESGEHTQV PADSPDSQEE QKGESSASSP EEPEEITCLE KGLAEVQQDG EAEEGATSDG
EKKREGVTPW ASFKKMVTPK KRVRRPSESD KEDELDKVKS ATLSSTESTA SEMQEEMKGS
VEEPKPEEPK RKVDTSVSWE ALICVGSSKK RARRGSSSDE EGGPKAMGGD HQKADEAGKD
KETGTDGILA GSQEHDPGQG SSSPEQAGSP TEGEGVSTWE SFKRLVTPRK KSKSKLEEKS
EDSIAGSGVE HSTPDTEPGK EESWVSIKKF IPGRRKKRPD GKQEQAPVED AGPTGANEDD
SDVPAVVPLS EYDAVEREKM EAQQAQKSAE QPEQKAATEV SKELSESQVH MMAAAVADGT
RAATIIEERS PSWISASVTE PLEQVEAEAA LLTEEVLERE VIAEEEPPTV TEPLPENREA
RGDTVVSEAE LTPEAVTAAE TAGPLGAEEG TEASAAEETT EMVSAVSQLT DSPDTTEEAT
PVQEVEGGVP DIEEQERRTQ EVLQAVAEKV KEESQLPGTG GPEDVLQPVQ RAEAERPEEQ
AEASGLKKET DVVLKVDAQE AKTEPFTQGK VVGQTTPESF EKAPQVTESI ESSELVTTCQ
AETLAGVKSQ EMVMEQAIPP DSVETPTDSE TDGSTPVADF DAPGTTQKDE IVEIHEENEV
ASGTQSGGTE AEAVPAQKER PPAPSSFVFQ EETKEQSKME DTLEHTDKEV SVETVSILSK
TEGTQEADQY ADEKTKDVPF FEGLEGSIDT GITVSREKVT EVALKGEGTE EAECKKDDAL
ELQSHAKSPP SPVEREMVVQ VEREKTEAEP THVNEEKLEH ETAVTVSEEV SKQLLQTVNV
PIIDGAKEVS SLEGSPPPCL GQEEAVCTKI QVQSSEASFT LTAAAEEEKV LGETANILET
GETLEPAGAH LVLEEKSSEK NEDFAAHPGE DAVPTGPDCQ AKSTPVIVSA TTKKGLSSDL
EGEKTTSLKW KSDEVDEQVA CQEVKVSVAI EDLEPENGIL ELETKSSKLV QNIIQTAVDQ
FVRTEETATE MLTSELQTQA HVIKADSQDA GQETEKEGEE PQASAQDETP ITSAKEESES
TAVGQAHSDI SKDMSEASEK TMTVEVEGST VNDQQLEEVV LPSEEEGGGA GTKSVPEDDG
HALLAERIEK SLVEPKEDEK GDDVDDPENQ NSALADTDAS GGLTKESPDT NGPKQKEKED
AQEVELQEGK VHSESDKAIT PQAQEELQKQ ERESAKSELT ES
