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UniProtKB/Swiss-Prot entry O43823


[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

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Entry information
Entry name AKAP8_HUMAN
Primary accession number O43823
Secondary accession numbers None
Integrated into Swiss-Prot on July 15, 1999
Sequence was last modified on June 1, 1998 (Sequence version 1)
Annotations were last modified on    June 16, 2009 (Entry version 72)
Name and origin of the protein
Protein name A-kinase anchor protein 8
Synonyms A-kinase anchor protein 95 kDa
AKAP 95
Gene name
Name: AKAP8
Synonyms: AKAP95
From
Homo sapiens (Human) [TaxID: 9606] 
Taxonomy Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; Homo.
Protein existence 1: Evidence at protein level;
References
[1]
NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Cerebellum, and Testis;
DOI=10.1006/excr.1997.3855; PubMed=9473338 [NCBI, ExPASy, EBI, Israel, Japan]
Eide T., Coghlan V., Oerstavik S., Holsve C., Solberg R., Skaelhegg B.S., Lamb N.J.C., Langeberg L., Fernandez A., Scott J.D., Jahnsen T., Tasken K.;
"Molecular cloning, chromosomal localization, and cell cycle-dependent subcellular distribution of the A-kinase anchoring protein, AKAP95.";
Exp. Cell Res. 238:305-316(1998).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
DOI=10.1038/nature02399; PubMed=15057824 [NCBI, ExPASy, EBI, Israel, Japan]
Grimwood J., Gordon L.A., Olsen A.S., Terry A., Schmutz J., Lamerdin J.E., Hellsten U., Goodstein D., Couronne O., Tran-Gyamfi M., Aerts A., Altherr M., Ashworth L., Bajorek E., Black S., Branscomb E., Caenepeel S., Carrano A.V., Caoile C., Chan Y.M., Christensen M., Cleland C.A., Copeland A., Dalin E., Dehal P., Denys M., Detter J.C., Escobar J., Flowers D., Fotopulos D., Garcia C., Georgescu A.M., Glavina T., Gomez M., Gonzales E., Groza M., Hammon N., Hawkins T., Haydu L., Ho I., Huang W., Israni S., Jett J., Kadner K., Kimball H., Kobayashi A., Larionov V., Leem S.-H., Lopez F., Lou Y., Lowry S., Malfatti S., Martinez D., McCready P.M., Medina C., Morgan J., Nelson K., Nolan M., Ovcharenko I., Pitluck S., Pollard M., Popkie A.P., Predki P., Quan G., Ramirez L., Rash S., Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A., She X., Smith D., Slezak T., Solovyev V., Thayer N., Tice H., Tsai M., Ustaszewska A., Vo N., Wagner M., Wheeler J., Wu K., Xie G., Yang J., Dubchak I., Furey T.S., DeJong P., Dickson M., Gordon D., Eichler E.E., Pennacchio L.A., Richardson P., Stubbs L., Rokhsar D.S., Myers R.M., Rubin E.M., Lucas S.M.;
"The DNA sequence and biology of human chromosome 19.";
Nature 428:529-535(2004).
[3]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-328, AND MASS SPECTROMETRY.
TISSUE=Epithelium;
DOI=10.1073/pnas.0404720101; PubMed=15302935 [NCBI, ExPASy, EBI, Israel, Japan]
Beausoleil S.A., Jedrychowski M., Schwartz D., Elias J.E., Villen J., Li J., Cohn M.A., Cantley L.C., Gygi S.P.;
"Large-scale characterization of HeLa cell nuclear phosphoproteins.";
Proc. Natl. Acad. Sci. U.S.A. 101:12130-12135(2004).
[4]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-323; SER-328 AND SER-339, AND MASS SPECTROMETRY.
TISSUE=Epithelium;
DOI=10.1016/j.cell.2006.09.026; PubMed=17081983 [NCBI, ExPASy, EBI, Israel, Japan]
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.;
"Global, in vivo, and site-specific phosphorylation dynamics in signaling networks.";
Cell 127:635-648(2006).
[5]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-112, AND MASS SPECTROMETRY.
TISSUE=Epithelium;
DOI=10.1038/nbt1240; PubMed=16964243 [NCBI, ExPASy, EBI, Israel, Japan]
Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.;
"A probability-based approach for high-throughput protein phosphorylation analysis and site localization.";
Nat. Biotechnol. 24:1285-1292(2006).
[6]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-328, AND MASS SPECTROMETRY.
DOI=10.1016/j.molcel.2008.07.007; PubMed=18691976 [NCBI, ExPASy, EBI, Israel, Japan]
Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., Greff Z., Keri G., Stemmann O., Mann M.;
"Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle.";
Mol. Cell 31:438-448(2008).
[7]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-323; SER-328 AND SER-339, AND MASS SPECTROMETRY.
DOI=10.1073/pnas.0805139105; PubMed=18669648 [NCBI, ExPASy, EBI, Israel, Japan]
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P.;
"A quantitative atlas of mitotic phosphorylation.";
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
[8]
IDENTIFICATION [LARGE SCALE ANALYSIS], AND MASS SPECTROMETRY.
Colinge J., Superti-Furga G., Bennett K.L.;
Submitted (OCT-2008) to UniProtKB.
[9]
VARIANT [LARGE SCALE ANALYSIS] HIS-664.
DOI=10.1126/science.1133427; PubMed=16959974 [NCBI, ExPASy, EBI, Israel, Japan]
Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D., Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., Buckhaults P., Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V., Gazdar A.F., Hartigan J., Wu L., Liu C., Parmigiani G., Park B.H., Bachman K.E., Papadopoulos N., Vogelstein B., Kinzler K.W., Velculescu V.E.;
"The consensus coding sequences of human breast and colorectal cancers.";
Science 314:268-274(2006).
Comments
  • FUNCTION: Anchoring protein that mediates the subcellular compartmentation of cAMP-dependent protein kinase (PKA type II).
  • SUBUNIT: Binds to dimeric RII-alpha regulatory subunit of PKA during mitosis.
  • SUBCELLULAR LOCATION: Nucleus matrix. Note=Associated with the nuclear matrix. Redistributed and detached from condensed chromatin during mitosis.
  • TISSUE SPECIFICITY: Highly expressed in heart, liver, skeletal muscle, kidney and pancreas.
  • SIMILARITY: Belongs to the AKAP95 family.
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
Y11997; CAA72722.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AC005785; AAC62838.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
IPI IPI00014474; -.
PIR T13161; T13161.
RefSeq NP_005849.1; -.
UniGene Hs.631640
3D structure databases
ModBase O43823.
PTM databases
PhosphoSite O43823; -.
Organism-specific databases
GeneCards GC19M015325; -.
H-InvDB HIX0014839; -.
HGNC HGNC:378; AKAP8.
GenAtlas AKAP8.
HPA HPA004776; -.
MIM 604692; gene. [NCBI / EBI]
PharmGKB PA24672; -.
Gene expression databases
ArrayExpress O43823; -.
Bgee O43823; -.
CleanEx HS_AKAP8; -.
GermOnline ENSG00000105127; Homo sapiens.
Ontologies
GO
GO:0016363; Cellular component: nuclear matrix (inferred from electronic annotation from UniProtKB-SubCell).
GO:0003677; Molecular function: DNA binding (inferred from electronic annotation from UniProtKB-KW).
GO:0008270; Molecular function: zinc ion binding (inferred from electronic annotation from UniProtKB-KW).
GO:0007165; Biological process: signal transduction (traceable author statement from ProtInc).
QuickGo view.
Family and domain databases
InterPro IPR007071; AKAP95.
IPR018459; RII_binding_1.
IPR015880; Znf_C2H2-like.
Graphical view of domain structure.
PANTHER PTHR12190; AKAP95; 1.
Pfam PF04988; AKAP95; 1.
PF10522; RII_binding_1; 1.
Pfam graphical view of domain structure.
SMART SM00355; ZnF_C2H2; 1.
SMART graphical view of domain structure.
Proteomic databases
PeptideAtlas O43823; -.
PRIDE O43823; -.
Genome annotation databases
Ensembl ENSG00000105127; Homo sapiens. [Contig view]
GeneID 10270; -.
KEGG hsa:10270; -.
Phylogenomic databases
HOGENOM O43823; -.
HOVERGEN O43823; -.
OMA O43823; KETLRFI.
Other
NextBio 38910; -.
SOURCE AKAP8; Homo sapiens.
ProtoNet O43823.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
DNA-binding; Metal-binding; Nucleus; Phosphoprotein; Polymorphism; Repeat; Zinc; Zinc-finger.
Features
SEVIEWER logo Feature table viewer FT aligner logo Feature aligner
KeyFrom   To Length Description FTId
CHAIN   1   692  692     A-kinase anchor protein 8. PRO_0000075381
ZN_FING   390   414  25     C2H2 AKAP95-type 1. 
ZN_FING   479   504  26     C2H2 AKAP95-type 2. 
REGION   572   589  18     RII-binding (By similarity). 
MOTIF   368   377  10     Nuclear localization signal (Potential). 
COMPBIAS   107   118  12     Poly-Gly. 
MOD_RES   112   112        Phosphoserine. 
MOD_RES   323   323        Phosphoserine. 
MOD_RES   328   328        Phosphoserine. 
MOD_RES   339   339        Phosphoserine. 
VARIANT   664   664  1     Q -> H (in a breast cancer sample; somatic mutation). VAR_036534 
Sequence information
Length: 692 AA [This is the length of the unprocessed precursor] Molecular weight: 76108 Da [This is the MW of the unprocessed precursor] CRC64: CBCD5F014FD94B66 [This is a checksum on the sequence]
        10         20         30         40         50         60 
MDQGYGGYGA WSAGPANTQG AYGTGVASWQ GYENYNYYGA QNTSVTTGAT YSYGPASWEA 

        70         80         90        100        110        120 
AKANDGGLAA GAPAMHMASY GPEPCTDNSD SLIAKINQRL DMMSKEGGRG GSGGGGEGIQ 

       130        140        150        160        170        180 
DRESSFRFQP FESYDSRPCL PEHNPYRPSY SYDYEFDLGS DRNGSFGGQY SECRDPARER 

       190        200        210        220        230        240 
GSLDGFMRGR GQGRFQDRSN PGTFMRSDPF VPPAASSEPL STPWNELNYV GGRGLGGPSP 

       250        260        270        280        290        300 
SRPPPSLFSQ SMAPDYGVMG MQGAGGYDST MPYGCGRSQP RMRDRDRPKR RGFDRFGPDG 

       310        320        330        340        350        360 
TGRKRKQFQL YEEPDTKLAR VDSEGDFSEN DDAAGDFRSG DEEFKGEDEL CDSGRQRGEK 

       370        380        390        400        410        420 
EDEDEDVKKR REKQRRRDRT RDRAADRIQF ACSVCKFRSF DDEEIQKHLQ SKFHKETLRF 

       430        440        450        460        470        480 
ISTKLPDKTV EFLQEYIVNR NKKIEKRRQE LMEKETAKPK PDPFKGIGQE HFFKKIEAAH 

       490        500        510        520        530        540 
CLACDMLIPA QPQLLQRHLH SVDHNHNRRL AAEQFKKTSL HVAKSVLNNR HIVKMLEKYL 

       550        560        570        580        590        600 
KGEDPFTSET VDPEMEGDDN LGGEDKKETP EEVAADVLAE VITAAVRAVD GEGAPAPESS 

       610        620        630        640        650        660 
GEPAEDEGPT DTAEAGSDPQ AEQLLEEQVP CGTAHEKGVP KARSEAAEAG NGAETMAAEA 

       670        680        690 
ESAQTRVAPA PAAADAEVEQ TDAESKDAVP TE 

O43823 in FASTA format

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