Details for: AKAP8

Gene ID: 10270

Symbol: AKAP8

Ensembl ID: ENSG00000105127

Description: A-kinase anchoring protein 8

Associated with

Other Information

Genular Protein ID: 1669677098

Symbol: AKAP8_HUMAN

Name: A-kinase anchor protein 8

UniProtKB Accession Codes:

Database IDs:

Citations:

PubMed ID: 9473338

Title: Molecular cloning, chromosomal localization, and cell cycle-dependent subcellular distribution of the A-kinase anchoring protein, AKAP95.

PubMed ID: 9473338

DOI: 10.1006/excr.1997.3855

PubMed ID: 15057824

Title: The DNA sequence and biology of human chromosome 19.

PubMed ID: 15057824

DOI: 10.1038/nature02399

PubMed ID: 10601332

Title: The A-kinase-anchoring protein AKAP95 is a multivalent protein with a key role in chromatin condensation at mitosis.

PubMed ID: 10601332

DOI: 10.1083/jcb.147.6.1167

PubMed ID: 10791967

Title: A kinase-anchoring protein (AKAP)95 recruits human chromosome-associated protein (hCAP)-D2/Eg7 for chromosome condensation in mitotic extract.

PubMed ID: 10791967

DOI: 10.1083/jcb.149.3.531

PubMed ID: 10764601

Title: Analysis of A-kinase anchoring protein (AKAP) interaction with protein kinase A (PKA) regulatory subunits: PKA isoform specificity in AKAP binding.

PubMed ID: 10764601

DOI: 10.1006/jmbi.2000.3662

PubMed ID: 11591814

Title: Regulation of anchoring of the RIIalpha regulatory subunit of PKA to AKAP95 by threonine phosphorylation of RIIalpha: implications for chromosome dynamics at mitosis.

PubMed ID: 11591814

DOI: 10.1242/jcs.114.18.3255

PubMed ID: 11964380

Title: Distinct but overlapping domains of AKAP95 are implicated in chromosome condensation and condensin targeting.

PubMed ID: 11964380

DOI: 10.1093/embo-reports/kvf089

PubMed ID: 12740381

Title: Protein kinase A-anchoring protein AKAP95 interacts with MCM2, a regulator of DNA replication.

PubMed ID: 12740381

DOI: 10.1074/jbc.m300765200

PubMed ID: 14641107

Title: A novel partner for D-type cyclins: protein kinase A-anchoring protein AKAP95.

PubMed ID: 14641107

DOI: 10.1042/bj20031765

PubMed ID: 15470020

Title: A-kinase anchoring proteins interact with phosphodiesterases in T lymphocyte cell lines.

PubMed ID: 15470020

DOI: 10.4049/jimmunol.173.8.4806

PubMed ID: 16227597

Title: A-kinase-anchoring protein 95 functions as a potential carrier for the nuclear translocation of active caspase 3 through an enzyme-substrate-like association.

PubMed ID: 16227597

DOI: 10.1128/mcb.25.21.9469-9477.2005

PubMed ID: 17081983

Title: Global, in vivo, and site-specific phosphorylation dynamics in signaling networks.

PubMed ID: 17081983

DOI: 10.1016/j.cell.2006.09.026

PubMed ID: 16980585

Title: A novel histone deacetylase pathway regulates mitosis by modulating Aurora B kinase activity.

PubMed ID: 16980585

DOI: 10.1101/gad.1455006

PubMed ID: 18691976

Title: Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle.

PubMed ID: 18691976

DOI: 10.1016/j.molcel.2008.07.007

PubMed ID: 18669648

Title: A quantitative atlas of mitotic phosphorylation.

PubMed ID: 18669648

DOI: 10.1073/pnas.0805139105

PubMed ID: 19413330

Title: Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach.

PubMed ID: 19413330

DOI: 10.1021/ac9004309

PubMed ID: 19277197

Title: A-kinase anchoring in dendritic cells is required for antigen presentation.

PubMed ID: 19277197

DOI: 10.1371/journal.pone.0004807

PubMed ID: 19690332

Title: Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions.

PubMed ID: 19690332

DOI: 10.1126/scisignal.2000007

PubMed ID: 20068231

Title: Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis.

PubMed ID: 20068231

DOI: 10.1126/scisignal.2000475

PubMed ID: 21269460

Title: Initial characterization of the human central proteome.

PubMed ID: 21269460

DOI: 10.1186/1752-0509-5-17

PubMed ID: 21406692

Title: System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation.

PubMed ID: 21406692

DOI: 10.1126/scisignal.2001570

PubMed ID: 22130794

Title: Localization and retention of p90 ribosomal S6 kinase 1 in the nucleus: implications for its function.

PubMed ID: 22130794

DOI: 10.1091/mbc.e11-07-0658

PubMed ID: 23186163

Title: Toward a comprehensive characterization of a human cancer cell phosphoproteome.

PubMed ID: 23186163

DOI: 10.1021/pr300630k

PubMed ID: 23995757

Title: Regulation of transcription by the MLL2 complex and MLL complex-associated AKAP95.

PubMed ID: 23995757

DOI: 10.1038/nsmb.2656

PubMed ID: 24275569

Title: An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome.

PubMed ID: 24275569

DOI: 10.1016/j.jprot.2013.11.014

PubMed ID: 24129315

Title: Immunoaffinity enrichment and mass spectrometry analysis of protein methylation.

PubMed ID: 24129315

DOI: 10.1074/mcp.o113.027870

PubMed ID: 25770215

Title: Role for tyrosine phosphorylation of a-kinase anchoring protein 8 (AKAP8) in its dissociation from chromatin and the nuclear matrix.

PubMed ID: 25770215

DOI: 10.1074/jbc.m115.643882

PubMed ID: 26683827

Title: A-kinase anchoring protein AKAP95 is a novel regulator of ribosomal RNA synthesis.

PubMed ID: 26683827

DOI: 10.1111/febs.13630

PubMed ID: 26880274

Title: Dynamic changes in protein interaction between AKAP95 and Cx43 during cell cycle progression of A549 cells.

PubMed ID: 26880274

DOI: 10.1038/srep21224

PubMed ID: 28112733

Title: Site-specific mapping of the human SUMO proteome reveals co-modification with phosphorylation.

PubMed ID: 28112733

DOI: 10.1038/nsmb.3366

PubMed ID: 16959974

Title: The consensus coding sequences of human breast and colorectal cancers.

PubMed ID: 16959974

DOI: 10.1126/science.1133427

Sequence Information:

  • Length: 692
  • Mass: 76108
  • Checksum: CBCD5F014FD94B66
  • Sequence:
  • 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

Database document:

This is a preview of the gene's schema. Only a few entries are kept for 'singleCellExpressions,' 'mRNAExpressions,' and other large data arrays for visualization purposes. You can zoom in with the mouse wheel for a closer view, and the text will adjust automatically if necessary. For the full schema, download it here.