ID   AKAP8_HUMAN             Reviewed;         692 AA.
AC   O43823;
DT   15-JUL-1999, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-1998, sequence version 1.
DT   25-JAN-2012, entry version 99.
DE   RecName: Full=A-kinase anchor protein 8;
DE            Short=AKAP-8;
DE   AltName: Full=A-kinase anchor protein 95 kDa;
DE            Short=AKAP 95;
GN   Name=AKAP8; Synonyms=AKAP95;
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC   Catarrhini; Hominidae; Homo.
OX   NCBI_TaxID=9606;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Cerebellum, and Testis;
RX   MEDLINE=98142017; PubMed=9473338; DOI=10.1006/excr.1997.3855;
RA   Eide T., Coghlan V., Oerstavik S., Holsve C., Solberg R.,
RA   Skaelhegg B.S., Lamb N.J.C., Langeberg L., Fernandez A., Scott J.D.,
RA   Jahnsen T., Tasken K.;
RT   "Molecular cloning, chromosomal localization, and cell cycle-dependent
RT   subcellular distribution of the A-kinase anchoring protein, AKAP95.";
RL   Exp. Cell Res. 238:305-316(1998).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=15057824; DOI=10.1038/nature02399;
RA   Grimwood J., Gordon L.A., Olsen A.S., Terry A., Schmutz J.,
RA   Lamerdin J.E., Hellsten U., Goodstein D., Couronne O., Tran-Gyamfi M.,
RA   Aerts A., Altherr M., Ashworth L., Bajorek E., Black S., Branscomb E.,
RA   Caenepeel S., Carrano A.V., Caoile C., Chan Y.M., Christensen M.,
RA   Cleland C.A., Copeland A., Dalin E., Dehal P., Denys M., Detter J.C.,
RA   Escobar J., Flowers D., Fotopulos D., Garcia C., Georgescu A.M.,
RA   Glavina T., Gomez M., Gonzales E., Groza M., Hammon N., Hawkins T.,
RA   Haydu L., Ho I., Huang W., Israni S., Jett J., Kadner K., Kimball H.,
RA   Kobayashi A., Larionov V., Leem S.-H., Lopez F., Lou Y., Lowry S.,
RA   Malfatti S., Martinez D., McCready P.M., Medina C., Morgan J.,
RA   Nelson K., Nolan M., Ovcharenko I., Pitluck S., Pollard M.,
RA   Popkie A.P., Predki P., Quan G., Ramirez L., Rash S., Retterer J.,
RA   Rodriguez A., Rogers S., Salamov A., Salazar A., She X., Smith D.,
RA   Slezak T., Solovyev V., Thayer N., Tice H., Tsai M., Ustaszewska A.,
RA   Vo N., Wagner M., Wheeler J., Wu K., Xie G., Yang J., Dubchak I.,
RA   Furey T.S., DeJong P., Dickson M., Gordon D., Eichler E.E.,
RA   Pennacchio L.A., Richardson P., Stubbs L., Rokhsar D.S., Myers R.M.,
RA   Rubin E.M., Lucas S.M.;
RT   "The DNA sequence and biology of human chromosome 19.";
RL   Nature 428:529-535(2004).
RN   [3]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-328, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Cervix carcinoma;
RX   PubMed=15302935; DOI=10.1073/pnas.0404720101;
RA   Beausoleil S.A., Jedrychowski M., Schwartz D., Elias J.E., Villen J.,
RA   Li J., Cohn M.A., Cantley L.C., Gygi S.P.;
RT   "Large-scale characterization of HeLa cell nuclear phosphoproteins.";
RL   Proc. Natl. Acad. Sci. U.S.A. 101:12130-12135(2004).
RN   [4]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-323; SER-328 AND
RP   SER-339, AND MASS SPECTROMETRY.
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.,
RA   Mann M.;
RT   "Global, in vivo, and site-specific phosphorylation dynamics in
RT   signaling networks.";
RL   Cell 127:635-648(2006).
RN   [5]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-112, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Cervix carcinoma;
RX   PubMed=16964243; DOI=10.1038/nbt1240;
RA   Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.;
RT   "A probability-based approach for high-throughput protein
RT   phosphorylation analysis and site localization.";
RL   Nat. Biotechnol. 24:1285-1292(2006).
RN   [6]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-328, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Cervix carcinoma;
RX   PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007;
RA   Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,
RA   Greff Z., Keri G., Stemmann O., Mann M.;
RT   "Kinase-selective enrichment enables quantitative phosphoproteomics of
RT   the kinome across the cell cycle.";
RL   Mol. Cell 31:438-448(2008).
RN   [7]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-323; SER-328 AND
RP   SER-339, AND MASS SPECTROMETRY.
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   [8]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-323 AND SER-328, AND
RP   MASS SPECTROMETRY.
RC   TISSUE=Embryonic kidney;
RX   PubMed=19413330; DOI=10.1021/ac9004309;
RA   Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,
RA   Mohammed S.;
RT   "Lys-N and trypsin cover complementary parts of the phosphoproteome in
RT   a refined SCX-based approach.";
RL   Anal. Chem. 81:4493-4501(2009).
RN   [9]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-323 AND SER-328, AND
RP   MASS SPECTROMETRY.
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   [10]
RP   ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-538, AND MASS SPECTROMETRY.
RX   PubMed=19608861; DOI=10.1126/science.1175371;
RA   Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.,
RA   Olsen J.V., Mann M.;
RT   "Lysine acetylation targets protein complexes and co-regulates major
RT   cellular functions.";
RL   Science 325:834-840(2009).
RN   [11]
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.,
RA   Buerckstuemmer T., 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   [12]
RP   VARIANT [LARGE SCALE ANALYSIS] HIS-664.
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.,
RA   Buckhaults P., Farrell C., Meeh P., Markowitz S.D., Willis J.,
RA   Dawson D., Willson J.K.V., Gazdar A.F., Hartigan J., Wu L., Liu C.,
RA   Parmigiani G., Park B.H., Bachman K.E., Papadopoulos N.,
RA   Vogelstein B., Kinzler K.W., Velculescu V.E.;
RT   "The consensus coding sequences of human breast and colorectal
RT   cancers.";
RL   Science 314:268-274(2006).
CC   -!- FUNCTION: Anchoring protein that mediates the subcellular
CC       compartmentation of cAMP-dependent protein kinase (PKA type II).
CC   -!- SUBUNIT: Binds to dimeric RII-alpha regulatory subunit of PKA
CC       during mitosis. Interacts (via C-terminus) with FIGN (By
CC       similarity).
CC   -!- SUBCELLULAR LOCATION: Nucleus matrix. Note=Associated with the
CC       nuclear matrix. Redistributed and detached from condensed
CC       chromatin during mitosis.
CC   -!- TISSUE SPECIFICITY: Highly expressed in heart, liver, skeletal
CC       muscle, kidney and pancreas.
CC   -!- SIMILARITY: Belongs to the AKAP95 family.
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DR   EMBL; Y11997; CAA72722.1; -; mRNA.
DR   EMBL; AC005785; AAC62838.1; -; Genomic_DNA.
DR   IPI; IPI00014474; -.
DR   PIR; T13161; T13161.
DR   RefSeq; NP_005849.1; NM_005858.3.
DR   UniGene; Hs.594496; -.
DR   ProteinModelPortal; O43823; -.
DR   IntAct; O43823; 6.
DR   STRING; O43823; -.
DR   PhosphoSite; O43823; -.
DR   PeptideAtlas; O43823; -.
DR   PRIDE; O43823; -.
DR   Ensembl; ENST00000269701; ENSP00000269701; ENSG00000105127.
DR   GeneID; 10270; -.
DR   KEGG; hsa:10270; -.
DR   UCSC; uc002nav.1; human.
DR   CTD; 10270; -.
DR   GeneCards; GC19M015464; -.
DR   H-InvDB; HIX0202796; -.
DR   HGNC; HGNC:378; AKAP8.
DR   HPA; HPA004776; -.
DR   MIM; 604692; gene.
DR   neXtProt; NX_O43823; -.
DR   PharmGKB; PA24672; -.
DR   eggNOG; prNOG17009; -.
DR   HOGENOM; HBG714294; -.
DR   HOVERGEN; HBG053198; -.
DR   InParanoid; O43823; -.
DR   OMA; QDRESSF; -.
DR   OrthoDB; EOG4BG8VN; -.
DR   NextBio; 38910; -.
DR   ArrayExpress; O43823; -.
DR   Bgee; O43823; -.
DR   CleanEx; HS_AKAP8; -.
DR   Genevestigator; O43823; -.
DR   GermOnline; ENSG00000105127; Homo sapiens.
DR   GO; GO:0016363; C:nuclear matrix; ISS:UniProtKB.
DR   GO; GO:0007165; P:signal transduction; TAS:ProtInc.
DR   InterPro; IPR007071; AKAP95.
DR   InterPro; IPR015880; Znf_C2H2-like.
DR   PANTHER; PTHR12190; AKAP95; 1.
DR   Pfam; PF04988; AKAP95; 1.
DR   SMART; SM00355; ZnF_C2H2; 1.
PE   1: Evidence at protein level;
KW   Acetylation; Complete proteome; DNA-binding; Metal-binding; Nucleus;
KW   Phosphoprotein; Polymorphism; Reference proteome; Repeat; Zinc;
KW   Zinc-finger.
FT   CHAIN         1    692       A-kinase anchor protein 8.
FT                                /FTId=PRO_0000075381.
FT   ZN_FING     390    414       C2H2 AKAP95-type 1.
FT   ZN_FING     479    504       C2H2 AKAP95-type 2.
FT   REGION      572    589       RII-binding (By similarity).
FT   MOTIF       368    377       Nuclear localization signal (Potential).
FT   COMPBIAS    107    118       Poly-Gly.
FT   MOD_RES     112    112       Phosphoserine.
FT   MOD_RES     323    323       Phosphoserine.
FT   MOD_RES     328    328       Phosphoserine.
FT   MOD_RES     339    339       Phosphoserine.
FT   MOD_RES     538    538       N6-acetyllysine.
FT   VARIANT     664    664       Q -> H (in a breast cancer sample;
FT                                somatic mutation).
FT                                /FTId=VAR_036534.
SQ   SEQUENCE   692 AA;  76108 MW;  CBCD5F014FD94B66 CRC64;
     MDQGYGGYGA WSAGPANTQG AYGTGVASWQ GYENYNYYGA QNTSVTTGAT YSYGPASWEA
     AKANDGGLAA GAPAMHMASY GPEPCTDNSD SLIAKINQRL DMMSKEGGRG GSGGGGEGIQ
     DRESSFRFQP FESYDSRPCL PEHNPYRPSY SYDYEFDLGS DRNGSFGGQY SECRDPARER
     GSLDGFMRGR GQGRFQDRSN PGTFMRSDPF VPPAASSEPL STPWNELNYV GGRGLGGPSP
     SRPPPSLFSQ SMAPDYGVMG MQGAGGYDST MPYGCGRSQP RMRDRDRPKR RGFDRFGPDG
     TGRKRKQFQL YEEPDTKLAR VDSEGDFSEN DDAAGDFRSG DEEFKGEDEL CDSGRQRGEK
     EDEDEDVKKR REKQRRRDRT RDRAADRIQF ACSVCKFRSF DDEEIQKHLQ SKFHKETLRF
     ISTKLPDKTV EFLQEYIVNR NKKIEKRRQE LMEKETAKPK PDPFKGIGQE HFFKKIEAAH
     CLACDMLIPA QPQLLQRHLH SVDHNHNRRL AAEQFKKTSL HVAKSVLNNR HIVKMLEKYL
     KGEDPFTSET VDPEMEGDDN LGGEDKKETP EEVAADVLAE VITAAVRAVD GEGAPAPESS
     GEPAEDEGPT DTAEAGSDPQ AEQLLEEQVP CGTAHEKGVP KARSEAAEAG NGAETMAAEA
     ESAQTRVAPA PAAADAEVEQ TDAESKDAVP TE
//