AKAP2_HUMAN
ID AKAP2_HUMAN Reviewed; 859 AA.
AC Q9Y2D5; B1ALX9; B2RTU4; B3KQ00; B4DTZ2; B7ZW07; B9EJB5; Q9UG26;
DT 21-FEB-2001, integrated into UniProtKB/Swiss-Prot.
DT 28-JUL-2009, sequence version 3.
DT 03-AUG-2022, entry version 177.
DE RecName: Full=A-kinase anchor protein 2;
DE Short=AKAP-2;
DE AltName: Full=AKAP-KL;
DE AltName: Full=Protein kinase A-anchoring protein 2;
DE Short=PRKA2;
GN Name=AKAP2; Synonyms=KIAA0920, PRKA2;
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 2).
RA Schuetze N., Reichel S., Ruecker N., Lechner A., Eulert J., Jakob F.;
RT "Homo sapiens AKAP-2 complete cDNA sequence.";
RL Submitted (DEC-2000) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Brain;
RX PubMed=10231032; DOI=10.1093/dnares/6.1.63;
RA Nagase T., Ishikawa K., Suyama M., Kikuno R., Hirosawa M., Miyajima N.,
RA Tanaka A., Kotani H., Nomura N., Ohara O.;
RT "Prediction of the coding sequences of unidentified human genes. XIII. The
RT complete sequences of 100 new cDNA clones from brain which code for large
RT proteins in vitro.";
RL DNA Res. 6:63-70(1999).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2), AND VARIANT
RP SER-561.
RC TISSUE=Placenta, and Small intestine;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15164053; DOI=10.1038/nature02465;
RA Humphray S.J., Oliver K., Hunt A.R., Plumb R.W., Loveland J.E., Howe K.L.,
RA Andrews T.D., Searle S., Hunt S.E., Scott C.E., Jones M.C., Ainscough R.,
RA Almeida J.P., Ambrose K.D., Ashwell R.I.S., Babbage A.K., Babbage S.,
RA Bagguley C.L., Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K.,
RA Beasley H., Beasley O., Bird C.P., Bray-Allen S., Brown A.J., Brown J.Y.,
RA Burford D., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C.,
RA Chen Y., Clarke G., Clark S.Y., Clee C.M., Clegg S., Collier R.E.,
RA Corby N., Crosier M., Cummings A.T., Davies J., Dhami P., Dunn M.,
RA Dutta I., Dyer L.W., Earthrowl M.E., Faulkner L., Fleming C.J.,
RA Frankish A., Frankland J.A., French L., Fricker D.G., Garner P.,
RA Garnett J., Ghori J., Gilbert J.G.R., Glison C., Grafham D.V., Gribble S.,
RA Griffiths C., Griffiths-Jones S., Grocock R., Guy J., Hall R.E.,
RA Hammond S., Harley J.L., Harrison E.S.I., Hart E.A., Heath P.D.,
RA Henderson C.D., Hopkins B.L., Howard P.J., Howden P.J., Huckle E.,
RA Johnson C., Johnson D., Joy A.A., Kay M., Keenan S., Kershaw J.K.,
RA Kimberley A.M., King A., Knights A., Laird G.K., Langford C., Lawlor S.,
RA Leongamornlert D.A., Leversha M., Lloyd C., Lloyd D.M., Lovell J.,
RA Martin S., Mashreghi-Mohammadi M., Matthews L., McLaren S., McLay K.E.,
RA McMurray A., Milne S., Nickerson T., Nisbett J., Nordsiek G., Pearce A.V.,
RA Peck A.I., Porter K.M., Pandian R., Pelan S., Phillimore B., Povey S.,
RA Ramsey Y., Rand V., Scharfe M., Sehra H.K., Shownkeen R., Sims S.K.,
RA Skuce C.D., Smith M., Steward C.A., Swarbreck D., Sycamore N., Tester J.,
RA Thorpe A., Tracey A., Tromans A., Thomas D.W., Wall M., Wallis J.M.,
RA West A.P., Whitehead S.L., Willey D.L., Williams S.A., Wilming L.,
RA Wray P.W., Young L., Ashurst J.L., Coulson A., Blocker H., Durbin R.M.,
RA Sulston J.E., Hubbard T., Jackson M.J., Bentley D.R., Beck S., Rogers J.,
RA Dunham I.;
RT "DNA sequence and analysis of human chromosome 9.";
RL Nature 429:369-374(2004).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2; 4 AND 5), AND VARIANT
RP SER-561.
RC TISSUE=Brain;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 539-859 (ISOFORMS 1/2/4).
RC TISSUE=Brain;
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 [8]
RP ALTERNATIVE SPLICING (ISOFORM 2).
RC TISSUE=Muscle;
RX PubMed=11478809; DOI=10.1006/bbrc.2001.5329;
RA Hu B., Copeland N.G., Gilbert D.J., Jenkins N.A., Kilimann M.W.;
RT "The paralemmin protein family: identification of paralemmin-2, an isoform
RT differentially spliced to AKAP2/AKAP-KL, and of palmdelphin, a more distant
RT cytosolic relative.";
RL Biochem. Biophys. Res. Commun. 285:1369-1376(2001).
RN [9]
RP IDENTIFICATION BY 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-393, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18220336; DOI=10.1021/pr0705441;
RA Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D., Yates J.R. III;
RT "Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient
RT phosphoproteomic analysis.";
RL J. Proteome Res. 7:1346-1351(2008).
RN [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-121; SER-152; SER-393;
RP SER-631; SER-720 AND SER-748, AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [12]
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 [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-152; SER-393; SER-461 AND
RP SER-720, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Leukemic T-cell;
RX PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA Rodionov V., Han D.K.;
RT "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT reveals system-wide modulation of protein-protein interactions.";
RL Sci. Signal. 2:RA46-RA46(2009).
RN [14]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-152; SER-393 AND SER-748, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [15]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-152; SER-393 AND SER-748, AND
RP 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-91; SER-152; SER-393;
RP SER-517; THR-526; SER-631; SER-778 AND SER-785, AND IDENTIFICATION BY MASS
RP 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 [17]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-174, 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 [18]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25944712; DOI=10.1002/pmic.201400617;
RA Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., Ayoub D.,
RA Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
RT "N-terminome analysis of the human mitochondrial proteome.";
RL Proteomics 15:2519-2524(2015).
RN [19]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-174, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=28112733; DOI=10.1038/nsmb.3366;
RA Hendriks I.A., Lyon D., Young C., Jensen L.J., Vertegaal A.C.,
RA Nielsen M.L.;
RT "Site-specific mapping of the human SUMO proteome reveals co-modification
RT with phosphorylation.";
RL Nat. Struct. Mol. Biol. 24:325-336(2017).
CC -!- FUNCTION: Binds to regulatory subunit (RII) of protein kinase A. May be
CC involved in establishing polarity in signaling systems or in
CC integrating PKA-RII isoforms with downstream effectors to capture,
CC amplify and focus diffuse, trans-cellular signals carried by cAMP (By
CC similarity). {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=5;
CC Name=1;
CC IsoId=Q9Y2D5-3; Sequence=Displayed;
CC Name=3; Synonyms=PALM2-AKAP2;
CC IsoId=Q9Y2D5-4; Sequence=VSP_037769, VSP_037771;
CC Name=2;
CC IsoId=Q9Y2D5-5; Sequence=VSP_037770;
CC Name=4;
CC IsoId=Q9Y2D5-6; Sequence=VSP_037769;
CC Name=5;
CC IsoId=Q9Y2D5-7; Sequence=VSP_037770, VSP_037771;
CC -!- DOMAIN: The RII-alpha binding site, predicted to form an amphipathic
CC helix, could participate in protein-protein interactions with a
CC complementary surface on the R-subunit dimer.
CC -!- MISCELLANEOUS: [Isoform 3]: Based on a naturally occurring readthrough
CC transcript which produces a PALM2-AKAP2 fusion protein. {ECO:0000305}.
CC -!- MISCELLANEOUS: [Isoform 4]: Based on a naturally occurring readthrough
CC transcript which produces a PALM2-AKAP2 fusion protein. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAA76764.2; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AJ303079; CAC38839.1; -; mRNA.
DR EMBL; AB023137; BAA76764.2; ALT_INIT; mRNA.
DR EMBL; AK057098; BAG51862.1; -; mRNA.
DR EMBL; AK300427; BAG62154.1; -; mRNA.
DR EMBL; AL158823; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL158829; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL353598; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL353806; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL627225; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471105; EAW59057.1; -; Genomic_DNA.
DR EMBL; BC140818; AAI40819.1; -; mRNA.
DR EMBL; BC146863; AAI46864.1; -; mRNA.
DR EMBL; BC171800; AAI71800.1; -; mRNA.
DR EMBL; AL110268; CAB53707.1; -; mRNA.
DR CCDS; CCDS35100.1; -. [Q9Y2D5-4]
DR CCDS; CCDS35101.1; -. [Q9Y2D5-6]
DR CCDS; CCDS43861.1; -. [Q9Y2D5-5]
DR CCDS; CCDS48003.1; -. [Q9Y2D5-3]
DR CCDS; CCDS56581.1; -. [Q9Y2D5-7]
DR PIR; T14787; T14787.
DR RefSeq; NP_001004065.2; NM_001004065.4. [Q9Y2D5-5]
DR RefSeq; NP_001130034.1; NM_001136562.2. [Q9Y2D5-3]
DR RefSeq; NP_001185585.1; NM_001198656.1. [Q9Y2D5-7]
DR RefSeq; NP_009134.1; NM_007203.4. [Q9Y2D5-4]
DR RefSeq; NP_671492.1; NM_147150.2. [Q9Y2D5-6]
DR AlphaFoldDB; Q9Y2D5; -.
DR SMR; Q9Y2D5; -.
DR BioGRID; 116386; 58.
DR BioGRID; 138657; 28.
DR IntAct; Q9Y2D5; 47.
DR MINT; Q9Y2D5; -.
DR STRING; 9606.ENSP00000363654; -.
DR iPTMnet; Q9Y2D5; -.
DR MetOSite; Q9Y2D5; -.
DR PhosphoSitePlus; Q9Y2D5; -.
DR SwissPalm; Q9Y2D5; -.
DR BioMuta; AKAP2; -.
DR DMDM; 254763433; -.
DR EPD; Q9Y2D5; -.
DR jPOST; Q9Y2D5; -.
DR MassIVE; Q9Y2D5; -.
DR MaxQB; Q9Y2D5; -.
DR PaxDb; Q9Y2D5; -.
DR PeptideAtlas; Q9Y2D5; -.
DR PRIDE; Q9Y2D5; -.
DR ProteomicsDB; 85738; -. [Q9Y2D5-3]
DR ProteomicsDB; 85739; -. [Q9Y2D5-4]
DR ProteomicsDB; 85740; -. [Q9Y2D5-5]
DR ProteomicsDB; 85741; -. [Q9Y2D5-6]
DR ProteomicsDB; 85742; -. [Q9Y2D5-7]
DR Antibodypedia; 56405; 50 antibodies from 16 providers.
DR DNASU; 445815; -.
DR GeneID; 445815; -.
DR MANE-Select; ENST00000374530.8; ENSP00000363654.3; NM_007203.5; NP_009134.1. [Q9Y2D5-4]
DR UCSC; uc004bem.4; human. [Q9Y2D5-3]
DR CTD; 445815; -.
DR DisGeNET; 445815; -.
DR GeneCards; AKAP2; -.
DR HGNC; HGNC:372; AKAP2.
DR HPA; ENSG00000157654; Low tissue specificity.
DR MIM; 604582; gene.
DR neXtProt; NX_Q9Y2D5; -.
DR OpenTargets; ENSG00000157654; -.
DR VEuPathDB; HostDB:ENSG00000157654; -.
DR eggNOG; ENOG502QR7I; Eukaryota.
DR GeneTree; ENSGT00930000151059; -.
DR HOGENOM; CLU_007780_0_0_1; -.
DR InParanoid; Q9Y2D5; -.
DR OMA; RDNCSAN; -.
DR OrthoDB; 604893at2759; -.
DR PhylomeDB; Q9Y2D5; -.
DR TreeFam; TF105402; -.
DR PathwayCommons; Q9Y2D5; -.
DR SignaLink; Q9Y2D5; -.
DR BioGRID-ORCS; 11217; 11 hits in 1029 CRISPR screens.
DR BioGRID-ORCS; 445815; 110 hits in 1000 CRISPR screens.
DR ChiTaRS; AKAP2; human.
DR GeneWiki; AKAP2; -.
DR Pharos; Q9Y2D5; Tbio.
DR PRO; PR:Q9Y2D5; -.
DR Proteomes; UP000005640; Unplaced.
DR RNAct; Q9Y2D5; protein.
DR ExpressionAtlas; Q9Y2D5; baseline and differential.
DR Genevisible; Q9Y2D5; HS.
DR InterPro; IPR029304; AKAP2_C.
DR Pfam; PF15304; AKAP2_C; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Coiled coil; Isopeptide bond; Phosphoprotein;
KW Reference proteome; Ubl conjugation.
FT CHAIN 1..859
FT /note="A-kinase anchor protein 2"
FT /id="PRO_0000064524"
FT REGION 73..165
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 252..313
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 335..431
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 514..563
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 566..579
FT /note="PKA-RII subunit binding domain"
FT REGION 586..676
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 731..804
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 213..290
FT /evidence="ECO:0000255"
FT COILED 710..748
FT /evidence="ECO:0000255"
FT COMPBIAS 101..117
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 131..165
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 252..276
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 277..301
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 398..416
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 514..538
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 640..654
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 741..760
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 91
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 121
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 152
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:24275569"
FT MOD_RES 336
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q5U301"
FT MOD_RES 393
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18220336,
FT ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:19690332,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
FT ECO:0007744|PubMed:24275569"
FT MOD_RES 461
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19690332"
FT MOD_RES 465
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q5U301"
FT MOD_RES 517
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 526
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 631
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:24275569"
FT MOD_RES 720
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:19690332"
FT MOD_RES 748
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692"
FT MOD_RES 778
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 785
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT CROSSLNK 174
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO1); alternate"
FT /evidence="ECO:0007744|PubMed:25114211"
FT CROSSLNK 174
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2); alternate"
FT /evidence="ECO:0007744|PubMed:28112733"
FT VAR_SEQ 1
FT /note="M -> MRWPQPGAAARLPPESPGPPESPGPPEREAAAARRWTGAEPQDCAPG
FT SGRPEKPPQLSEDDIWLKSEGDNYSATLLEPAASSLSPDHKNM (in isoform 2
FT and isoform 5)"
FT /evidence="ECO:0000303|PubMed:14702039,
FT ECO:0000303|PubMed:15489334"
FT /id="VSP_037770"
FT VAR_SEQ 1
FT /note="M -> MAEAELHKERLQAIAEKRKRQTEIEGKRQQLDEQILLLQHSKSKVLR
FT EKWLLQGIPAGTAEEEEARRRQSEEDEFRVKQLEDNIQRLEQEIQTLESEESQISAKEQ
FT IILEKLKETEKSFKDFQKGFSSTDGDAVNYISSQLPDLPILCSRTAEPSPGQDGTSRAA
FT GVGWENVLLKEGESASNATETSGPDMTIKKPPQLSEDDIWLKSEGDNYSATLLEPAASS
FT LSPDHKNM (in isoform 3 and isoform 4)"
FT /evidence="ECO:0000303|PubMed:10231032,
FT ECO:0000303|PubMed:15489334, ECO:0000303|Ref.1"
FT /id="VSP_037769"
FT VAR_SEQ 827
FT /note="S -> SYTSKLLSCKVTSE (in isoform 3 and isoform 5)"
FT /evidence="ECO:0000303|PubMed:10231032,
FT ECO:0000303|PubMed:15489334, ECO:0000303|Ref.1"
FT /id="VSP_037771"
FT VARIANT 561
FT /note="L -> S (in dbSNP:rs914358)"
FT /evidence="ECO:0000269|PubMed:14702039,
FT ECO:0000269|PubMed:15489334"
FT /id="VAR_024248"
FT CONFLICT 282
FT /note="K -> Q (in Ref. 3; BAG51862/BAG62154 and 6;
FT AAI46864/AAI71800)"
FT /evidence="ECO:0000305"
FT CONFLICT 647
FT /note="E -> G (in Ref. 7; CAB53707)"
FT /evidence="ECO:0000305"
FT CONFLICT 651
FT /note="L -> P (in Ref. 3; BAG51862)"
FT /evidence="ECO:0000305"
FT CONFLICT 719
FT /note="L -> S (in Ref. 3; BAG51862)"
FT /evidence="ECO:0000305"
FT CONFLICT Q9Y2D5-5:20
FT /note="P -> L (in Ref. 6; AAI46864)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 859 AA; 94661 MW; 6DCE563596DFBA4B CRC64;
MEIEVSVAEC KSVPGITSTP HPMDHPSAFY SPPHNGLLTD HHESLDNDVA REIRYLDEVL
EANCCDSAVD GTYNGTSSPE PGAVVLVGGL SPPVHEATQP EPTERTASRQ APPHIELSNS
SPDPMAEAER TNGHSPSQPR DALGDSLQVP VSPSSTTSSR CSSRDGEFTL TTLKKEAKFE
LRAFHEDKKP SKLFEDDEHE KEQYCIRKVR PSEEMLELEK ERRELIRSQA VKKNPGIAAK
WWNPPQEKTI EEQLDEEHLE SHKKYKERKE RRAQQEQLLL QKQLQQQQQQ PPSQLCTAPA
SSHERASMID KAKEDIVTEQ IDFSAARKQF QLMENSRQAV AKGQSTPRLF SIKPFYRPLG
SVNSDKPLTN PRPPSVGGPP EDSGASAAKG QKSPGALETP SAAGSQGNTA SQGKEGPYSE
PSKRGPLSKL WAEDGEFTSA RAVLTVVKDD DHGILDQFSR SVNVSLTQEE LDSGLDELSV
RSQDTTVLET LSNDFSMDNI SDSGASNETT NALQENSLAD FSLPQTPQTD NPSEGRGEGV
SKSFSDHGFY SPSSTLGDSP LVDDPLEYQA GLLVQNAIQQ AIAEQVDKAV SKTSRDGAEQ
QGPEATVEEA EAAAFGSEKP QSMFEPPQVS SPVQEKRDVL PKILPAEDRA LRERGPPQPL
PAVQPSGPIN MEETRPEGSY FSKYSEAAEL RSTASLLATQ ESDVMVGPFK LRSRKQRTLS
MIEEEIRAAQ EREEELKRQR QVLQSTQSPR TKNAPSLPSR TCYKTAPGKI EKVKPPPSPT
TEGPSLQPDL APEEAAGTQR PKNLMQTLME DYETHKSKRR ERMDDSSVLE ATRVNRRKSA
LALRWEAGIY ANQEEEDNE
