Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

A-kinase anchor protein 8

Gene

AKAP8

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Anchoring protein that mediates the subcellular compartmentation of cAMP-dependent protein kinase (PKA type II) (PubMed:9473338). Acts as an anchor for a PKA-signaling complex onto mitotic chromosomes, which is required for maintenance of chromosomes in a condensed form throughout mitosis. Recruits condensin complex subunit NCAPD2 to chromosomes required for chromatin condensation; the function appears to be independent from PKA-anchoring (PubMed:10601332, PubMed:10791967, PubMed:11964380). May help to deliver cyclin D/E to CDK4 to facilitate cell cycle progression (PubMed:14641107). Required for cell cycle G2/M transition and histone deacetylation during mitosis. In mitotic cells recruits HDAC3 to the vicinity of chromatin leading to deacetylation and subsequent phosphorylation at 'Ser-10' of histone H3; in this function may act redundantly with AKAP8L (PubMed:16980585). Involved in nuclear retention of RPS6KA1 upon ERK activation thus inducing cell proliferation (PubMed:22130794). May be involved in regulation of DNA replication by acting as scaffold for MCM2 (PubMed:12740381). Enhances HMT activity of the KMT2 family MLL4/WBP7 complex and is involved in transcriptional regulation. In a teratocarcinoma cell line is involved in retinoic acid-mediated induction of developmental genes implicating H3 'Lys-4' methylation (PubMed:23995757). May be involved in recruitment of active CASP3 to the nucleus in apoptotic cells (PubMed:16227597). May act as a carrier protein of GJA1 for its transport to the nucleus (PubMed:26880274). Seems to involved in modulation of rDNA transcription. Preferentially binds GC-rich DNA in vitro and associates to GC-rich ribosomal RNA promoters (PubMed:26683827). Involved in modulation of Toll-like receptor signaling. Required for the cAMP-dependent suppression of TNF-alpha in early stages of LPS-induced macrophage activation; the function probably implicates targeting of PKA to NFKB1 (By similarity).By similarity2 Publications7 Publications

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri390 – 41425C2H2 AKAP95-type 1Add
BLAST
Zinc fingeri479 – 50426C2H2 AKAP95-type 2Add
BLAST

GO - Molecular functioni

  • double-stranded DNA binding Source: Ensembl
  • histone deacetylase binding Source: UniProtKB
  • poly(A) RNA binding Source: UniProtKB
  • protein kinase A regulatory subunit binding Source: UniProtKB
  • zinc ion binding Source: Ensembl

GO - Biological processi

  • cell cycle G2/M phase transition Source: UniProtKB
  • innate immune response Source: UniProtKB-KW
  • mitotic chromosome condensation Source: Ensembl
  • mitotic nuclear division Source: ProtInc
  • positive regulation of histone deacetylation Source: UniProtKB
  • protein transport Source: UniProtKB-KW
  • regulation of histone phosphorylation Source: UniProtKB
  • regulation of transcription, DNA-templated Source: UniProtKB-KW
  • signal transduction Source: ProtInc
  • transcription, DNA-templated Source: UniProtKB-KW
Complete GO annotation...

Keywords - Biological processi

Immunity, Innate immunity, Protein transport, Transcription, Transcription regulation, Transport

Keywords - Ligandi

DNA-binding, Metal-binding, Zinc

Names & Taxonomyi

Protein namesi
Recommended name:
A-kinase anchor protein 8
Short name:
AKAP-8
Alternative name(s):
A-kinase anchor protein 95 kDa
Short name:
AKAP 95
Gene namesi
Name:AKAP8
Synonyms:AKAP95
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 19

Organism-specific databases

HGNCiHGNC:378. AKAP8.

Subcellular locationi

GO - Cellular componenti

  • condensed chromosome Source: Ensembl
  • female pronucleus Source: Ensembl
  • Golgi apparatus Source: Ensembl
  • membrane Source: UniProtKB
  • mitochondrion Source: Ensembl
  • nuclear matrix Source: UniProtKB
  • nucleolus Source: UniProtKB-SubCell
  • nucleoplasm Source: HPA
  • nucleus Source: ProtInc
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi290 – 2901R → S: No nuclear localization; when associated with 304-N-S-305. 1 Publication
Mutagenesisi304 – 3052KR → NS: No nuclear localization; when associated with S-290. 1 Publication
Mutagenesisi392 – 3921C → S: Abolishes chromosome-condensation activity; when associated with S-395. 1 Publication
Mutagenesisi395 – 3951C → S: Abolishes chromosome-condensation activity; when associated with S-392. 1 Publication
Mutagenesisi481 – 4811C → S: Abolishes chromosome-condensation activity and recruitment of condensin complex; when associated with S-484. 1 Publication
Mutagenesisi484 – 4841C → S: Abolishes chromosome-condensation activity and recruitment of condensin complex; when associated with S-481. 1 Publication
Mutagenesisi582 – 5821I → P: No effect on activity to regulate DNA replication and on condensin complex recruitment. 2 Publications

Organism-specific databases

PharmGKBiPA24672.

Polymorphism and mutation databases

BioMutaiAKAP8.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 692692A-kinase anchor protein 8PRO_0000075381Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei112 – 1121PhosphoserineCombined sources
Modified residuei323 – 3231PhosphoserineCombined sources
Modified residuei328 – 3281PhosphoserineCombined sources
Modified residuei339 – 3391PhosphoserineCombined sources
Modified residuei662 – 6621PhosphoserineBy similarity

Post-translational modificationi

Phosphorylated on tyrosine residues probably by SRC subfamily protein kinases; multiple phosphorylation is leading to dissociation from nuclear structures implicated in chromatin structural changes.1 Publication

Keywords - PTMi

Phosphoprotein

Proteomic databases

EPDiO43823.
MaxQBiO43823.
PaxDbiO43823.
PeptideAtlasiO43823.
PRIDEiO43823.

PTM databases

iPTMnetiO43823.
PhosphoSiteiO43823.
SwissPalmiO43823.

Expressioni

Tissue specificityi

Highly expressed in heart, liver, skeletal muscle, kidney and pancreas. Expressed in mature dendritic cells.1 Publication

Gene expression databases

BgeeiO43823.
CleanExiHS_AKAP8.
ExpressionAtlasiO43823. baseline and differential.
GenevisibleiO43823. HS.

Organism-specific databases

HPAiHPA004776.

Interactioni

Subunit structurei

Binds to the PKA RII-alpha regulatory subunit PRKAR2A (phosphorylated at 'Thr-54') during mitosis (PubMed:9473338, PubMed:10601332, PubMed:10764601, PubMed:11591814). Interacts (via C-terminus) with FIGN (By similarity). Interacts with NCAPD2, CCND1, MCM2, RPS6KA1, PDE4A (PubMed:10601332, PubMed:11964380, PubMed:11591814, PubMed:12740381, PubMed:14641107, PubMed:15470020, PubMed:22130794). Interacts with CCND3, CCNE1, DDX5, CASP3. Interacts with NFKB1; detetcted in the cytoplasm. Interacts with MYCBP; MYCBP is translocated to the nucleus and the interaction prevents the association of the PKA catalytic subunit leading to suppression of PKA activity (By similarity). Interacts with DPY30; mediating AKAP8 association with at least the MLL4/WBP7 HMT complex (PubMed:23995757). Interacts with HDAC3; increased during mitosis (PubMed:16980585). Interacts with GJA1; in the nucleus and in the nuclear membrane; the nuclear association increases with progress of cell cycle G1, S and G2 phase and decreases in M phase (PubMed:26880274).By similarity1 Publication12 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
CASP3P425745EBI-1237481,EBI-524064
MCM2P497367EBI-1237481,EBI-374819
PRKAR2AP138613EBI-1237481,EBI-2556122
RPS6KA1Q154185EBI-1237481,EBI-963034

GO - Molecular functioni

  • histone deacetylase binding Source: UniProtKB
  • protein kinase A regulatory subunit binding Source: UniProtKB

Protein-protein interaction databases

BioGridi115561. 48 interactions.
DIPiDIP-38194N.
IntActiO43823. 28 interactions.
MINTiMINT-2796393.
STRINGi9606.ENSP00000269701.

Structurei

3D structure databases

ProteinModelPortaliO43823.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni1 – 210210Interaction with DPY301 PublicationAdd
BLAST
Regioni1 – 195195Interaction with MCM21 PublicationAdd
BLAST
Regioni109 – 20193Interaction with DDX5By similarityAdd
BLAST
Regioni387 – 45064Involved in chromatin-binding1 PublicationAdd
BLAST
Regioni525 – 56945Involved in condensin complex recruitment1 PublicationAdd
BLAST
Regioni572 – 58918RII-bindingBy similarityAdd
BLAST
Regioni576 – 59318Required for interaction with MYCBPBy similarityAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi289 – 30618Bipartite nuclear localization signalBy similarity1 PublicationAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi107 – 11812Poly-GlyAdd
BLAST

Sequence similaritiesi

Belongs to the AKAP95 family.Curated
Contains 2 C2H2 AKAP95-type zinc fingers.Curated

Zinc finger

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri390 – 41425C2H2 AKAP95-type 1Add
BLAST
Zinc fingeri479 – 50426C2H2 AKAP95-type 2Add
BLAST

Keywords - Domaini

Repeat, Zinc-finger

Phylogenomic databases

eggNOGiENOG410IFNG. Eukaryota.
ENOG410YE5A. LUCA.
GeneTreeiENSGT00530000063777.
HOGENOMiHOG000033876.
HOVERGENiHBG053198.
InParanoidiO43823.
KOiK16525.
OMAiGCGRSQT.
OrthoDBiEOG741Z1X.
PhylomeDBiO43823.
TreeFamiTF105407.

Family and domain databases

InterProiIPR007071. AKAP95.
[Graphical view]
PANTHERiPTHR12190. PTHR12190. 1 hit.
PfamiPF04988. AKAP95. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

O43823-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MDQGYGGYGA WSAGPANTQG AYGTGVASWQ GYENYNYYGA QNTSVTTGAT
60 70 80 90 100
YSYGPASWEA AKANDGGLAA GAPAMHMASY GPEPCTDNSD SLIAKINQRL
110 120 130 140 150
DMMSKEGGRG GSGGGGEGIQ DRESSFRFQP FESYDSRPCL PEHNPYRPSY
160 170 180 190 200
SYDYEFDLGS DRNGSFGGQY SECRDPARER GSLDGFMRGR GQGRFQDRSN
210 220 230 240 250
PGTFMRSDPF VPPAASSEPL STPWNELNYV GGRGLGGPSP SRPPPSLFSQ
260 270 280 290 300
SMAPDYGVMG MQGAGGYDST MPYGCGRSQP RMRDRDRPKR RGFDRFGPDG
310 320 330 340 350
TGRKRKQFQL YEEPDTKLAR VDSEGDFSEN DDAAGDFRSG DEEFKGEDEL
360 370 380 390 400
CDSGRQRGEK EDEDEDVKKR REKQRRRDRT RDRAADRIQF ACSVCKFRSF
410 420 430 440 450
DDEEIQKHLQ SKFHKETLRF ISTKLPDKTV EFLQEYIVNR NKKIEKRRQE
460 470 480 490 500
LMEKETAKPK PDPFKGIGQE HFFKKIEAAH CLACDMLIPA QPQLLQRHLH
510 520 530 540 550
SVDHNHNRRL AAEQFKKTSL HVAKSVLNNR HIVKMLEKYL KGEDPFTSET
560 570 580 590 600
VDPEMEGDDN LGGEDKKETP EEVAADVLAE VITAAVRAVD GEGAPAPESS
610 620 630 640 650
GEPAEDEGPT DTAEAGSDPQ AEQLLEEQVP CGTAHEKGVP KARSEAAEAG
660 670 680 690
NGAETMAAEA ESAQTRVAPA PAAADAEVEQ TDAESKDAVP TE
Length:692
Mass (Da):76,108
Last modified:June 1, 1998 - v1
Checksum:iCBCD5F014FD94B66
GO

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti664 – 6641Q → H in a breast cancer sample; somatic mutation. 1 Publication
VAR_036534

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Y11997 mRNA. Translation: CAA72722.1.
AC005785 Genomic DNA. Translation: AAC62838.1.
CCDSiCCDS12329.1.
PIRiT13161.
RefSeqiNP_005849.1. NM_005858.3.
UniGeneiHs.594496.

Genome annotation databases

EnsembliENST00000269701; ENSP00000269701; ENSG00000105127.
GeneIDi10270.
KEGGihsa:10270.
UCSCiuc002nav.4. human.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Y11997 mRNA. Translation: CAA72722.1.
AC005785 Genomic DNA. Translation: AAC62838.1.
CCDSiCCDS12329.1.
PIRiT13161.
RefSeqiNP_005849.1. NM_005858.3.
UniGeneiHs.594496.

3D structure databases

ProteinModelPortaliO43823.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi115561. 48 interactions.
DIPiDIP-38194N.
IntActiO43823. 28 interactions.
MINTiMINT-2796393.
STRINGi9606.ENSP00000269701.

PTM databases

iPTMnetiO43823.
PhosphoSiteiO43823.
SwissPalmiO43823.

Polymorphism and mutation databases

BioMutaiAKAP8.

Proteomic databases

EPDiO43823.
MaxQBiO43823.
PaxDbiO43823.
PeptideAtlasiO43823.
PRIDEiO43823.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000269701; ENSP00000269701; ENSG00000105127.
GeneIDi10270.
KEGGihsa:10270.
UCSCiuc002nav.4. human.

Organism-specific databases

CTDi10270.
GeneCardsiAKAP8.
HGNCiHGNC:378. AKAP8.
HPAiHPA004776.
MIMi604692. gene.
neXtProtiNX_O43823.
PharmGKBiPA24672.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiENOG410IFNG. Eukaryota.
ENOG410YE5A. LUCA.
GeneTreeiENSGT00530000063777.
HOGENOMiHOG000033876.
HOVERGENiHBG053198.
InParanoidiO43823.
KOiK16525.
OMAiGCGRSQT.
OrthoDBiEOG741Z1X.
PhylomeDBiO43823.
TreeFamiTF105407.

Miscellaneous databases

ChiTaRSiAKAP8. human.
GeneWikiiAKAP8.
GenomeRNAii10270.
PROiO43823.
SOURCEiSearch...

Gene expression databases

BgeeiO43823.
CleanExiHS_AKAP8.
ExpressionAtlasiO43823. baseline and differential.
GenevisibleiO43823. HS.

Family and domain databases

InterProiIPR007071. AKAP95.
[Graphical view]
PANTHERiPTHR12190. PTHR12190. 1 hit.
PfamiPF04988. AKAP95. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Molecular cloning, chromosomal localization, and cell cycle-dependent subcellular distribution of the A-kinase anchoring protein, AKAP95."
    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.
    Exp. Cell Res. 238:305-316(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], INTERACTION WITH PRKAR2A, FUNCTION.
    Tissue: Cerebellum and Testis.
  2. "The DNA sequence and biology of human chromosome 19."
    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.
    Nature 428:529-535(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  3. "The A-kinase-anchoring protein AKAP95 is a multivalent protein with a key role in chromatin condensation at mitosis."
    Collas P., Le Guellec K., Tasken K.
    J. Cell Biol. 147:1167-1180(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH PRKAR2A AND NCAPD2.
  4. "A kinase-anchoring protein (AKAP)95 recruits human chromosome-associated protein (hCAP)-D2/Eg7 for chromosome condensation in mitotic extract."
    Steen R.L., Cubizolles F., Le Guellec K., Collas P.
    J. Cell Biol. 149:531-536(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  5. "Analysis of A-kinase anchoring protein (AKAP) interaction with protein kinase A (PKA) regulatory subunits: PKA isoform specificity in AKAP binding."
    Herberg F.W., Maleszka A., Eide T., Vossebein L., Tasken K.
    J. Mol. Biol. 298:329-339(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH PRKAR2A.
  6. "Regulation of anchoring of the RIIalpha regulatory subunit of PKA to AKAP95 by threonine phosphorylation of RIIalpha: implications for chromosome dynamics at mitosis."
    Landsverk H.B., Carlson C.R., Steen R.L., Vossebein L., Herberg F.W., Tasken K., Collas P.
    J. Cell Sci. 114:3255-3264(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH PRKAR2A.
  7. "Distinct but overlapping domains of AKAP95 are implicated in chromosome condensation and condensin targeting."
    Eide T., Carlson C., Tasken K.A., Hirano T., Tasken K., Collas P.
    EMBO Rep. 3:426-432(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH NCAPD2, MUTAGENESIS OF ILE-582.
  8. "Protein kinase A-anchoring protein AKAP95 interacts with MCM2, a regulator of DNA replication."
    Eide T., Tasken K.A., Carlson C., Williams G., Jahnsen T., Tasken K., Collas P.
    J. Biol. Chem. 278:26750-26756(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH MCM2, MUTAGENESIS OF ILE-582.
  9. "A novel partner for D-type cyclins: protein kinase A-anchoring protein AKAP95."
    Arsenijevic T., Degraef C., Dumont J.E., Roger P.P., Pirson I.
    Biochem. J. 378:673-679(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH CCND1.
  10. "A-kinase anchoring proteins interact with phosphodiesterases in T lymphocyte cell lines."
    Asirvatham A.L., Galligan S.G., Schillace R.V., Davey M.P., Vasta V., Beavo J.A., Carr D.W.
    J. Immunol. 173:4806-4814(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH PDE4A.
  11. "A-kinase-anchoring protein 95 functions as a potential carrier for the nuclear translocation of active caspase 3 through an enzyme-substrate-like association."
    Kamada S., Kikkawa U., Tsujimoto Y., Hunter T.
    Mol. Cell. Biol. 25:9469-9477(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, MUTAGENESIS OF ARG-290 AND 304-LYS-ARG-305, NUCLEAR LOCALIZATION SIGNAL.
  12. "Global, in vivo, and site-specific phosphorylation dynamics in signaling networks."
    Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.
    Cell 127:635-648(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-323; SER-328 AND SER-339, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  13. "A novel histone deacetylase pathway regulates mitosis by modulating Aurora B kinase activity."
    Li Y., Kao G.D., Garcia B.A., Shabanowitz J., Hunt D.F., Qin J., Phelan C., Lazar M.A.
    Genes Dev. 20:2566-2579(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH HDAC3.
  14. "Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle."
    Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., Greff Z., Keri G., Stemmann O., Mann M.
    Mol. Cell 31:438-448(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-328, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  15. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-323; SER-328 AND SER-339, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  16. "Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
    Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
    Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  17. "A-kinase anchoring in dendritic cells is required for antigen presentation."
    Schillace R.V., Miller C.L., Pisenti N., Grotzke J.E., Swarbrick G.M., Lewinsohn D.M., Carr D.W.
    PLoS ONE 4:E4807-E4807(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: TISSUE SPECIFICITY, SUBCELLULAR LOCATION.
  18. "Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
    Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
    Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-323 AND SER-328, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Leukemic T-cell.
  19. "Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
    Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
    Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-323 AND SER-328, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  20. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  21. "System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
    Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
    Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-112; SER-323; SER-328 AND SER-339, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  22. "Localization and retention of p90 ribosomal S6 kinase 1 in the nucleus: implications for its function."
    Gao X., Chaturvedi D., Patel T.B.
    Mol. Biol. Cell 23:503-515(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH RPS6KA1.
  23. "Regulation of transcription by the MLL2 complex and MLL complex-associated AKAP95."
    Jiang H., Lu X., Shimada M., Dou Y., Tang Z., Roeder R.G.
    Nat. Struct. Mol. Biol. 20:1156-1163(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH DPY30, SUBUNIT.
  24. "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome."
    Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., Ye M., Zou H.
    J. Proteomics 96:253-262(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-323 AND SER-328, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  25. "Role for tyrosine phosphorylation of a-kinase anchoring protein 8 (AKAP8) in its dissociation from chromatin and the nuclear matrix."
    Kubota S., Morii M., Yuki R., Yamaguchi N., Yamaguchi H., Aoyama K., Kuga T., Tomonaga T., Yamaguchi N.
    J. Biol. Chem. 290:10891-10904(2015) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION.
  26. "A-kinase anchoring protein AKAP95 is a novel regulator of ribosomal RNA synthesis."
    Marstad A., Landsverk O.J., Stroemme O., Otterlei M., Collas P., Sundan A., Brede G.
    FEBS J. 283:757-770(2016) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION.
  27. "Dynamic changes in protein interaction between AKAP95 and Cx43 during cell cycle progression of A549 cells."
    Chen X., Kong X., Zhuang W., Teng B., Yu X., Hua S., Wang S., Liang F., Ma D., Zhang S., Zou X., Dai Y., Yang W., Zhang Y.
    Sci. Rep. 6:21224-21224(2016) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH GJA1, FUNCTION, SUBCELLULAR LOCATION.
  28. Cited for: VARIANT [LARGE SCALE ANALYSIS] HIS-664.

Entry informationi

Entry nameiAKAP8_HUMAN
AccessioniPrimary (citable) accession number: O43823
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 15, 1999
Last sequence update: June 1, 1998
Last modified: June 8, 2016
This is version 147 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Human chromosome 19
    Human chromosome 19: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.