AKP8L_HUMAN
ID AKP8L_HUMAN Reviewed; 646 AA.
AC Q9ULX6; B4DJ74; B5BU90; O94792; Q96J58; Q9NRQ0; Q9UGM0;
DT 27-APR-2001, integrated into UniProtKB/Swiss-Prot.
DT 12-SEP-2018, sequence version 4.
DT 03-AUG-2022, entry version 199.
DE RecName: Full=A-kinase anchor protein 8-like;
DE Short=AKAP8-like protein;
DE AltName: Full=Helicase A-binding protein 95;
DE Short=HAP95;
DE AltName: Full=Homologous to AKAP95 protein;
DE Short=HA95;
DE AltName: Full=Neighbor of A-kinase-anchoring protein 95;
DE Short=Neighbor of AKAP95;
GN Name=AKAP8L; Synonyms=NAKAP, NAKAP95; ORFNames=HRIHFB2018;
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 1), TISSUE SPECIFICITY, AND VARIANT
RP HIS-458.
RC TISSUE=Fetal brain;
RX PubMed=10697960; DOI=10.1007/s100380070040;
RA Seki N., Ueki N., Yano K., Saito T., Masuho Y., Muramatsu M.-A.;
RT "cDNA cloning of a novel human gene NAKAP95, neighbor of A-kinase anchoring
RT protein 95 (AKAP95) on chromosome 19p13.11-p13.12 region.";
RL J. Hum. Genet. 45:31-37(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=10761695; DOI=10.1016/s0248-4900(00)88761-4;
RA Orstavik S., Eide T., Collas P., Han I.O., Tasken K., Kieff E., Jahnsen T.,
RA Skalhegg B.S.;
RT "Identification, cloning and characterization of a novel nuclear protein,
RT HA95, homologous to A-kinase anchoring protein 95.";
RL Biol. Cell 92:27-37(2000).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, SUBCELLULAR LOCATION, AND
RP INTERACTION WITH DHX9.
RC TISSUE=Placenta, and T-cell lymphoma;
RX PubMed=10748171; DOI=10.1074/jbc.m909887199;
RA Westberg C., Yang J.-P., Tang H., Reddy T.R., Wong-Staal F.;
RT "A novel shuttle protein binds to RNA helicase A and activates the
RT retroviral constitutive transport element.";
RL J. Biol. Chem. 275:21396-21401(2000).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Substantia nigra;
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RX PubMed=19054851; DOI=10.1038/nmeth.1273;
RA Goshima N., Kawamura Y., Fukumoto A., Miura A., Honma R., Satoh R.,
RA Wakamatsu A., Yamamoto J., Kimura K., Nishikawa T., Andoh T., Iida Y.,
RA Ishikawa K., Ito E., Kagawa N., Kaminaga C., Kanehori K., Kawakami B.,
RA Kenmochi K., Kimura R., Kobayashi M., Kuroita T., Kuwayama H., Maruyama Y.,
RA Matsuo K., Minami K., Mitsubori M., Mori M., Morishita R., Murase A.,
RA Nishikawa A., Nishikawa S., Okamoto T., Sakagami N., Sakamoto Y.,
RA Sasaki Y., Seki T., Sono S., Sugiyama A., Sumiya T., Takayama T.,
RA Takayama Y., Takeda H., Togashi T., Yahata K., Yamada H., Yanagisawa Y.,
RA Endo Y., Imamoto F., Kisu Y., Tanaka S., Isogai T., Imai J., Watanabe S.,
RA Nomura N.;
RT "Human protein factory for converting the transcriptome into an in vitro-
RT expressed proteome.";
RL Nat. Methods 5:1011-1017(2008).
RN [6]
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., Lamerdin J.E.,
RA Hellsten U., Goodstein D., Couronne O., Tran-Gyamfi M., Aerts A.,
RA Altherr M., Ashworth L., Bajorek E., Black S., Branscomb E., Caenepeel S.,
RA Carrano A.V., Caoile C., Chan Y.M., Christensen M., Cleland C.A.,
RA Copeland A., Dalin E., Dehal P., Denys M., Detter J.C., Escobar J.,
RA Flowers D., Fotopulos D., Garcia C., Georgescu A.M., Glavina T., Gomez M.,
RA Gonzales E., Groza M., Hammon N., Hawkins T., Haydu L., Ho I., Huang W.,
RA Israni S., Jett J., Kadner K., Kimball H., Kobayashi A., Larionov V.,
RA Leem S.-H., Lopez F., Lou Y., Lowry S., Malfatti S., Martinez D.,
RA McCready P.M., Medina C., Morgan J., Nelson K., Nolan M., Ovcharenko I.,
RA Pitluck S., Pollard M., Popkie A.P., Predki P., Quan G., Ramirez L.,
RA Rash S., Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A.,
RA She X., Smith D., Slezak T., Solovyev V., Thayer N., Tice H., Tsai M.,
RA Ustaszewska A., Vo N., Wagner M., Wheeler J., Wu K., Xie G., Yang J.,
RA Dubchak I., 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 [7]
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 [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Placenta;
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 [9]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-358 (ISOFORM 1), AND
RP SUBCELLULAR LOCATION.
RC TISSUE=Fetal brain;
RX PubMed=9853615; DOI=10.1038/4315;
RA Ueki N., Oda T., Kondo M., Yano K., Noguchi T., Muramatsu M.-A.;
RT "Selection system for genes encoding nuclear-targeted proteins.";
RL Nat. Biotechnol. 16:1338-1342(1998).
RN [10]
RP FUNCTION, INTERACTION WITH LAMIN-B, AND SUBCELLULAR LOCATION.
RX PubMed=11034899; DOI=10.1242/jcs.113.21.3703;
RA Martins S.B., Eide T., Steen R.L., Jahnsen T., Skaalhegg B.S., Collas P.;
RT "HA95 is a protein of the chromatin and nuclear matrix regulating nuclear
RT envelope dynamics.";
RL J. Cell Sci. 113:3703-3713(2000).
RN [11]
RP FUNCTION, FUNCTION (MICROBIAL INFECTION), INTERACTION WITH DHX9, AND
RP NUCLEAR EXPORT SIGNAL.
RX PubMed=11402034; DOI=10.1074/jbc.m102809200;
RA Yang J.P., Tang H., Reddy T.R., Wong-Staal F.;
RT "Mapping the functional domains of HAP95, a protein that binds RNA helicase
RT A and activates the constitutive transport element of type D
RT retroviruses.";
RL J. Biol. Chem. 276:30694-30700(2001).
RN [12]
RP INTERACTION WITH EBNA-LP.
RX PubMed=11160753; DOI=10.1128/jvi.75.5.2475-2481.2001;
RA Han I., Harada S., Weaver D., Xue Y., Lane W., Orstavik S., Skalhegg B.,
RA Kieff E.;
RT "EBNA-LP associates with cellular proteins including DNA-PK and HA95.";
RL J. Virol. 75:2475-2481(2001).
RN [13]
RP INTERACTION WITH PRKACA, FUNCTION (MICROBIAL INFECTION), AND SUBCELLULAR
RP LOCATION.
RX PubMed=11884601; DOI=10.1128/mcb.22.7.2136-2146.2002;
RA Han I., Xue Y., Harada S., Orstavik S., Skalhegg B., Kieff E.;
RT "Protein kinase A associates with HA95 and affects transcriptional
RT coactivation by Epstein-Barr virus nuclear proteins.";
RL Mol. Cell. Biol. 22:2136-2146(2002).
RN [14]
RP INTERACTION WITH TMPO-BETA, AND FUNCTION.
RX PubMed=12538639; DOI=10.1083/jcb.200210026;
RA Martins S., Eikvar S., Furukawa K., Collas P.;
RT "HA95 and LAP2 beta mediate a novel chromatin-nuclear envelope interaction
RT implicated in initiation of DNA replication.";
RL J. Cell Biol. 160:177-188(2003).
RN [15]
RP PHOSPHORYLATION.
RX PubMed=12950172; DOI=10.1021/bi0350699;
RA Martins S.B., Marstad A., Collas P.;
RT "In vitro modulation of the interaction between HA95 and LAP2beta by cAMP
RT signaling.";
RL Biochemistry 42:10456-10461(2003).
RN [16]
RP INTERACTION WITH PRPF40A, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=16391387; DOI=10.1385/nmm:7:4:297;
RA Sayer J.A., Manczak M., Akileswaran L., Reddy P.H., Coghlan V.M.;
RT "Interaction of the nuclear matrix protein NAKAP with HypA and huntingtin:
RT implications for nuclear toxicity in Huntington's disease pathogenesis.";
RL NeuroMolecular Med. 7:297-310(2005).
RN [17]
RP FUNCTION, AND INTERACTION WITH HDAC3.
RX PubMed=16980585; DOI=10.1101/gad.1455006;
RA Li Y., Kao G.D., Garcia B.A., Shabanowitz J., Hunt D.F., Qin J., Phelan C.,
RA Lazar M.A.;
RT "A novel histone deacetylase pathway regulates mitosis by modulating Aurora
RT B kinase activity.";
RL Genes Dev. 20:2566-2579(2006).
RN [18]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=17594903; DOI=10.1016/j.yexcr.2007.05.014;
RA Kvissel A.K., Oerstavik S., Eikvar S., Brede G., Jahnsen T., Collas P.,
RA Akusjaervi G., Skaalhegg B.S.;
RT "Involvement of the catalytic subunit of protein kinase A and of HA95 in
RT pre-mRNA splicing.";
RL Exp. Cell Res. 313:2795-2809(2007).
RN [19]
RP INTERACTION WITH RNF43.
RX PubMed=18313049; DOI=10.1016/j.yexcr.2008.01.013;
RA Sugiura T., Yamaguchi A., Miyamoto K.;
RT "A cancer-associated RING finger protein, RNF43, is a ubiquitin ligase that
RT interacts with a nuclear protein, HAP95.";
RL Exp. Cell Res. 314:1519-1528(2008).
RN [20]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-283, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
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 the
RT kinome across the cell cycle.";
RL Mol. Cell 31:438-448(2008).
RN [21]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-292 AND SER-297, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [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 [22]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-257, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19608861; DOI=10.1126/science.1175371;
RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C.,
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 [23]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-283, AND IDENTIFICATION BY
RP 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 [24]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-267 AND SER-552, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [25]
RP METHYLATION [LARGE SCALE ANALYSIS] AT ARG-208; ARG-217; ARG-237 AND
RP ARG-247, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Colon carcinoma;
RX PubMed=24129315; DOI=10.1074/mcp.o113.027870;
RA Guo A., Gu H., Zhou J., Mulhern D., Wang Y., Lee K.A., Yang V., Aguiar M.,
RA Kornhauser J., Jia X., Ren J., Beausoleil S.A., Silva J.C., Vemulapalli V.,
RA Bedford M.T., Comb M.J.;
RT "Immunoaffinity enrichment and mass spectrometry analysis of protein
RT methylation.";
RL Mol. Cell. Proteomics 13:372-387(2014).
RN [26]
RP FUNCTION (MICROBIAL INFECTION), AND INTERACTION WITH HIV-1 REVERSE
RP TRANSCRIPTASE/RIBONUCLEASE H.
RX PubMed=25034436; DOI=10.1186/1742-4690-11-58;
RA Xing L., Zhao X., Guo F., Kleiman L.;
RT "The role of A-kinase anchoring protein 95-like protein in annealing of
RT tRNALys3 to HIV-1 RNA.";
RL Retrovirology 11:58-58(2014).
RN [27]
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., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
CC -!- FUNCTION: Could play a role in constitutive transport element (CTE)-
CC mediated gene expression by association with DHX9. Increases CTE-
CC dependent nuclear unspliced mRNA export (PubMed:10748171,
CC PubMed:11402034). Proposed to target PRKACA to the nucleus but does not
CC seem to be implicated in the binding of regulatory subunit II of PKA
CC (PubMed:10761695, PubMed:11884601). May be involved in nuclear envelope
CC breakdown and chromatin condensation. May be involved in anchoring
CC nuclear membranes to chromatin in interphase and in releasing membranes
CC from chromating at mitosis (PubMed:11034899). May regulate the
CC initiation phase of DNA replication when associated with TMPO isoform
CC Beta (PubMed:12538639). Required for cell cycle G2/M transition and
CC histone deacetylation during mitosis. In mitotic cells recruits HDAC3
CC to the vicinity of chromatin leading to deacetylation and subsequent
CC phosphorylation at 'Ser-10' of histone H3; in this function seems to
CC act redundantly with AKAP8 (PubMed:16980585). May be involved in
CC regulation of pre-mRNA splicing (PubMed:17594903).
CC {ECO:0000269|PubMed:10748171, ECO:0000269|PubMed:11034899,
CC ECO:0000269|PubMed:11402034, ECO:0000269|PubMed:11884601,
CC ECO:0000269|PubMed:12538639, ECO:0000269|PubMed:16980585,
CC ECO:0000305|PubMed:10761695}.
CC -!- FUNCTION: (Microbial infection) In case of EBV infection, may target
CC PRKACA to EBNA-LP-containing nuclear sites to modulate transcription
CC from specific promoters. {ECO:0000269|PubMed:11884601}.
CC -!- FUNCTION: (Microbial infection) Can synergize with DHX9 to activate the
CC CTE-mediated gene expression of type D retroviruses.
CC {ECO:0000269|PubMed:11402034}.
CC -!- FUNCTION: (Microbial infection) In case of HIV-1 infection, involved in
CC the DHX9-promoted annealing of host tRNA(Lys3) to viral genomic RNA as
CC a primer in reverse transcription; in vitro negatively regulates DHX9
CC annealing activity. {ECO:0000269|PubMed:25034436}.
CC -!- SUBUNIT: Interacts (via N-terminus) with DHX9 (via RGG region)
CC (PubMed:10748171, PubMed:11402034). Interacts with TMPO isoform Beta,
CC PRPF40A, RNF43, lamin-B (PubMed:11034899, PubMed:12538639
CC PubMed:16391387, PubMed:18313049). Interacts with HDAC3; increased
CC during mitosis (PubMed:16980585). Interacts with EBV EBNA-LP
CC (PubMed:11160753). Interacts with HIV-1 reverse
CC transcriptase/ribonuclease H (PubMed:25034436).
CC {ECO:0000269|PubMed:10748171, ECO:0000269|PubMed:11160753,
CC ECO:0000269|PubMed:11402034, ECO:0000269|PubMed:12538639,
CC ECO:0000269|PubMed:16391387, ECO:0000269|PubMed:16980585,
CC ECO:0000269|PubMed:18313049, ECO:0000269|PubMed:25034436}.
CC -!- INTERACTION:
CC Q9ULX6; Q9NYB9-2: ABI2; NbExp=3; IntAct=EBI-357530, EBI-11096309;
CC Q9ULX6; Q8N5M1: ATPAF2; NbExp=3; IntAct=EBI-357530, EBI-1166928;
CC Q9ULX6; Q9Y2V2: CARHSP1; NbExp=3; IntAct=EBI-357530, EBI-718719;
CC Q9ULX6; Q8NEC5: CATSPER1; NbExp=3; IntAct=EBI-357530, EBI-744545;
CC Q9ULX6; Q96HB5: CCDC120; NbExp=3; IntAct=EBI-357530, EBI-744556;
CC Q9ULX6; Q8N4L8: CCDC24; NbExp=3; IntAct=EBI-357530, EBI-1104933;
CC Q9ULX6; Q8NE01: CNNM3; NbExp=3; IntAct=EBI-357530, EBI-741032;
CC Q9ULX6; Q02930-3: CREB5; NbExp=3; IntAct=EBI-357530, EBI-10192698;
CC Q9ULX6; P33240: CSTF2; NbExp=3; IntAct=EBI-357530, EBI-711360;
CC Q9ULX6; Q9H0L4: CSTF2T; NbExp=3; IntAct=EBI-357530, EBI-747012;
CC Q9ULX6; Q14129: DGCR6; NbExp=3; IntAct=EBI-357530, EBI-12206931;
CC Q9ULX6; Q9NQL9: DMRT3; NbExp=3; IntAct=EBI-357530, EBI-9679045;
CC Q9ULX6; Q9H0I2: ENKD1; NbExp=3; IntAct=EBI-357530, EBI-744099;
CC Q9ULX6; Q7L5A3: FAM214B; NbExp=3; IntAct=EBI-357530, EBI-745689;
CC Q9ULX6; Q8WU58: FAM222B; NbExp=3; IntAct=EBI-357530, EBI-2807642;
CC Q9ULX6; Q12950: FOXD4; NbExp=3; IntAct=EBI-357530, EBI-11317801;
CC Q9ULX6; O43559: FRS3; NbExp=3; IntAct=EBI-357530, EBI-725515;
CC Q9ULX6; O95872: GPANK1; NbExp=3; IntAct=EBI-357530, EBI-751540;
CC Q9ULX6; Q13227: GPS2; NbExp=3; IntAct=EBI-357530, EBI-713355;
CC Q9ULX6; O15379: HDAC3; NbExp=5; IntAct=EBI-357530, EBI-607682;
CC Q9ULX6; Q9Y5R4: HEMK1; NbExp=3; IntAct=EBI-357530, EBI-10329202;
CC Q9ULX6; O14964: HGS; NbExp=3; IntAct=EBI-357530, EBI-740220;
CC Q9ULX6; Q9ULV5-2: HSF4; NbExp=3; IntAct=EBI-357530, EBI-12056251;
CC Q9ULX6; Q0VD86: INCA1; NbExp=3; IntAct=EBI-357530, EBI-6509505;
CC Q9ULX6; Q5T749: KPRP; NbExp=3; IntAct=EBI-357530, EBI-10981970;
CC Q9ULX6; Q14657: LAGE3; NbExp=3; IntAct=EBI-357530, EBI-1052105;
CC Q9ULX6; Q8TAP9: MPLKIP; NbExp=3; IntAct=EBI-357530, EBI-11603426;
CC Q9ULX6; Q9NP98: MYOZ1; NbExp=3; IntAct=EBI-357530, EBI-744402;
CC Q9ULX6; Q86VE0: MYPOP; NbExp=3; IntAct=EBI-357530, EBI-2858213;
CC Q9ULX6; Q9HBE1-4: PATZ1; NbExp=3; IntAct=EBI-357530, EBI-11022007;
CC Q9ULX6; Q9Y5E9: PCDHB14; NbExp=3; IntAct=EBI-357530, EBI-10329013;
CC Q9ULX6; Q9UBV8: PEF1; NbExp=3; IntAct=EBI-357530, EBI-724639;
CC Q9ULX6; P78337: PITX1; NbExp=3; IntAct=EBI-357530, EBI-748265;
CC Q9ULX6; Q16512: PKN1; NbExp=3; IntAct=EBI-357530, EBI-602382;
CC Q9ULX6; Q494U1-3: PLEKHN1; NbExp=3; IntAct=EBI-357530, EBI-12014286;
CC Q9ULX6; Q7Z5V6-2: PPP1R32; NbExp=3; IntAct=EBI-357530, EBI-12000762;
CC Q9ULX6; P54646: PRKAA2; NbExp=3; IntAct=EBI-357530, EBI-1383852;
CC Q9ULX6; Q9BTL3: RAMAC; NbExp=3; IntAct=EBI-357530, EBI-744023;
CC Q9ULX6; Q68DV7: RNF43; NbExp=2; IntAct=EBI-357530, EBI-1647060;
CC Q9ULX6; Q14D33: RTP5; NbExp=3; IntAct=EBI-357530, EBI-10217913;
CC Q9ULX6; Q9BVN2: RUSC1; NbExp=3; IntAct=EBI-357530, EBI-6257312;
CC Q9ULX6; Q9UPU9-3: SAMD4A; NbExp=3; IntAct=EBI-357530, EBI-11986417;
CC Q9ULX6; Q8IYX7: SAXO1; NbExp=3; IntAct=EBI-357530, EBI-3957636;
CC Q9ULX6; Q8TEC5: SH3RF2; NbExp=3; IntAct=EBI-357530, EBI-2130111;
CC Q9ULX6; P09234: SNRPC; NbExp=3; IntAct=EBI-357530, EBI-766589;
CC Q9ULX6; Q8WW24: TEKT4; NbExp=3; IntAct=EBI-357530, EBI-750487;
CC Q9ULX6; Q96M29: TEKT5; NbExp=3; IntAct=EBI-357530, EBI-10239812;
CC Q9ULX6; Q96A09: TENT5B; NbExp=3; IntAct=EBI-357530, EBI-752030;
CC Q9ULX6; Q7Z6R9: TFAP2D; NbExp=3; IntAct=EBI-357530, EBI-11952651;
CC Q9ULX6; Q01085-2: TIAL1; NbExp=3; IntAct=EBI-357530, EBI-11064654;
CC Q9ULX6; Q08117-2: TLE5; NbExp=3; IntAct=EBI-357530, EBI-11741437;
CC Q9ULX6; P62328: TMSB4X; NbExp=3; IntAct=EBI-357530, EBI-712598;
CC Q9ULX6; Q96RU7: TRIB3; NbExp=3; IntAct=EBI-357530, EBI-492476;
CC Q9ULX6; Q3SY00: TSGA10IP; NbExp=3; IntAct=EBI-357530, EBI-10241197;
CC Q9ULX6; P29597: TYK2; NbExp=3; IntAct=EBI-357530, EBI-1383454;
CC Q9ULX6; Q64LD2-2: WDR25; NbExp=3; IntAct=EBI-357530, EBI-12032042;
CC Q9ULX6; Q15915: ZIC1; NbExp=3; IntAct=EBI-357530, EBI-11963196;
CC Q9ULX6; Q8N895: ZNF366; NbExp=3; IntAct=EBI-357530, EBI-2813661;
CC Q9ULX6; A8K8V0: ZNF785; NbExp=3; IntAct=EBI-357530, EBI-3925400;
CC Q9ULX6; Q9R1C7: Prpf40a; Xeno; NbExp=3; IntAct=EBI-357530, EBI-645554;
CC Q9ULX6; PRO_0000308465 [P29991]; Xeno; NbExp=3; IntAct=EBI-357530, EBI-8826747;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:10748171,
CC ECO:0000269|PubMed:10761695}. Nucleus matrix
CC {ECO:0000269|PubMed:11034899, ECO:0000269|PubMed:16391387}. Nucleus
CC speckle {ECO:0000269|PubMed:17594903}. Nucleus, PML body
CC {ECO:0000269|PubMed:11884601}. Cytoplasm {ECO:0000269|PubMed:10748171}.
CC Note=Colocalizes with PRPF40A in the nuclear matrix (PubMed:16391387).
CC Nuclear at steady state but shuttles between the nucleus and cytoplasm
CC (PubMed:10748171). The shuttling property has been questioned
CC (PubMed:11034899). Colocalizes with EBNA-LP in PML bodies
CC (PubMed:11884601). {ECO:0000269|PubMed:10748171,
CC ECO:0000269|PubMed:11034899, ECO:0000269|PubMed:11884601,
CC ECO:0000269|PubMed:16391387}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9ULX6-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9ULX6-2; Sequence=VSP_044426;
CC -!- TISSUE SPECIFICITY: Ubiquitously expressed. Expressed in the brain
CC cortex (at protein level). {ECO:0000269|PubMed:10697960,
CC ECO:0000269|PubMed:16391387}.
CC -!- PTM: Phosphorylated on serine or threonine residues possibly by PKA;
CC probably modulating the interaction with TMPO isoform Beta.
CC {ECO:0000269|PubMed:12950172}.
CC -!- SIMILARITY: Belongs to the AKAP95 family. {ECO:0000255|PROSITE-
CC ProRule:PRU01140}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAF86048.1; Type=Frameshift; Evidence={ECO:0000305};
CC Sequence=BAA34791.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AB025905; BAA85003.1; -; mRNA.
DR EMBL; AJ243467; CAB65092.1; -; mRNA.
DR EMBL; AF199414; AAF86048.1; ALT_FRAME; mRNA.
DR EMBL; AK295956; BAG58736.1; -; mRNA.
DR EMBL; AB451326; BAG70140.1; -; mRNA.
DR EMBL; AB451469; BAG70283.1; -; mRNA.
DR EMBL; AC005785; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC006128; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; KF456508; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; KF456511; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471106; EAW84475.1; -; Genomic_DNA.
DR EMBL; BC000713; AAH00713.1; -; mRNA.
DR EMBL; AB015332; BAA34791.1; ALT_INIT; mRNA.
DR CCDS; CCDS46005.1; -. [Q9ULX6-1]
DR CCDS; CCDS77249.1; -. [Q9ULX6-2]
DR RefSeq; NP_001278407.1; NM_001291478.1. [Q9ULX6-2]
DR RefSeq; NP_055186.3; NM_014371.3. [Q9ULX6-1]
DR AlphaFoldDB; Q9ULX6; -.
DR BioGRID; 117940; 171.
DR CORUM; Q9ULX6; -.
DR DIP; DIP-27541N; -.
DR IntAct; Q9ULX6; 175.
DR MINT; Q9ULX6; -.
DR STRING; 9606.ENSP00000380557; -.
DR GlyGen; Q9ULX6; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q9ULX6; -.
DR PhosphoSitePlus; Q9ULX6; -.
DR BioMuta; AKAP8L; -.
DR DMDM; 296439446; -.
DR EPD; Q9ULX6; -.
DR jPOST; Q9ULX6; -.
DR MassIVE; Q9ULX6; -.
DR MaxQB; Q9ULX6; -.
DR PaxDb; Q9ULX6; -.
DR PeptideAtlas; Q9ULX6; -.
DR PRIDE; Q9ULX6; -.
DR ProteomicsDB; 85148; -. [Q9ULX6-1]
DR Antibodypedia; 7497; 207 antibodies from 26 providers.
DR DNASU; 26993; -.
DR Ensembl; ENST00000397410.10; ENSP00000380557.3; ENSG00000011243.19. [Q9ULX6-1]
DR Ensembl; ENST00000595465.6; ENSP00000470952.1; ENSG00000011243.19. [Q9ULX6-2]
DR GeneID; 26993; -.
DR KEGG; hsa:26993; -.
DR MANE-Select; ENST00000397410.10; ENSP00000380557.3; NM_014371.4; NP_055186.3.
DR UCSC; uc002naw.2; human. [Q9ULX6-1]
DR CTD; 26993; -.
DR DisGeNET; 26993; -.
DR GeneCards; AKAP8L; -.
DR HGNC; HGNC:29857; AKAP8L.
DR HPA; ENSG00000011243; Low tissue specificity.
DR MIM; 609475; gene.
DR neXtProt; NX_Q9ULX6; -.
DR OpenTargets; ENSG00000011243; -.
DR PharmGKB; PA134867364; -.
DR VEuPathDB; HostDB:ENSG00000011243; -.
DR eggNOG; ENOG502QSFC; Eukaryota.
DR GeneTree; ENSGT00530000063777; -.
DR HOGENOM; CLU_024193_0_0_1; -.
DR InParanoid; Q9ULX6; -.
DR OMA; GFSGNMR; -.
DR OrthoDB; 902224at2759; -.
DR PhylomeDB; Q9ULX6; -.
DR TreeFam; TF105407; -.
DR PathwayCommons; Q9ULX6; -.
DR SignaLink; Q9ULX6; -.
DR SIGNOR; Q9ULX6; -.
DR BioGRID-ORCS; 26993; 20 hits in 1088 CRISPR screens.
DR ChiTaRS; AKAP8L; human.
DR GeneWiki; AKAP8L; -.
DR GenomeRNAi; 26993; -.
DR Pharos; Q9ULX6; Tbio.
DR PRO; PR:Q9ULX6; -.
DR Proteomes; UP000005640; Chromosome 19.
DR RNAct; Q9ULX6; protein.
DR Bgee; ENSG00000011243; Expressed in right hemisphere of cerebellum and 191 other tissues.
DR ExpressionAtlas; Q9ULX6; baseline and differential.
DR Genevisible; Q9ULX6; HS.
DR GO; GO:0000785; C:chromatin; IDA:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0016363; C:nuclear matrix; IDA:UniProtKB.
DR GO; GO:0016607; C:nuclear speck; IDA:UniProtKB.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0016605; C:PML body; IEA:UniProtKB-SubCell.
DR GO; GO:1990904; C:ribonucleoprotein complex; IDA:UniProtKB.
DR GO; GO:0017151; F:DEAD/H-box RNA helicase binding; TAS:UniProtKB.
DR GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR GO; GO:0042826; F:histone deacetylase binding; IDA:UniProtKB.
DR GO; GO:0005521; F:lamin binding; IDA:UniProtKB.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0034237; F:protein kinase A regulatory subunit binding; IBA:GO_Central.
DR GO; GO:0003723; F:RNA binding; HDA:UniProtKB.
DR GO; GO:0044839; P:cell cycle G2/M phase transition; IMP:UniProtKB.
DR GO; GO:0007076; P:mitotic chromosome condensation; IMP:UniProtKB.
DR GO; GO:0006397; P:mRNA processing; IDA:UniProtKB.
DR GO; GO:0051081; P:nuclear membrane disassembly; IMP:UniProtKB.
DR GO; GO:0031065; P:positive regulation of histone deacetylation; IMP:UniProtKB.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IDA:UniProtKB.
DR GO; GO:0010793; P:regulation of mRNA export from nucleus; IDA:UniProtKB.
DR GO; GO:0008380; P:RNA splicing; IEA:UniProtKB-KW.
DR InterPro; IPR007071; AKAP95.
DR InterPro; IPR034736; ZF_C2H2_AKAP95.
DR PANTHER; PTHR12190; PTHR12190; 1.
DR Pfam; PF04988; AKAP95; 1.
DR PROSITE; PS51799; ZF_C2H2_AKAP95; 2.
PE 1: Evidence at protein level;
KW Acetylation; Alternative splicing; Cytoplasm; Host-virus interaction;
KW Metal-binding; Methylation; mRNA processing; mRNA splicing; Nucleus;
KW Phosphoprotein; Reference proteome; Repeat; Transcription;
KW Transcription regulation; Zinc; Zinc-finger.
FT CHAIN 1..646
FT /note="A-kinase anchor protein 8-like"
FT /id="PRO_0000075384"
FT ZN_FING 391..413
FT /note="C2H2 AKAP95-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01140"
FT ZN_FING 484..507
FT /note="C2H2 AKAP95-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01140"
FT REGION 1..268
FT /note="Sufficient for activation of CTE-mediated
FT expression"
FT /evidence="ECO:0000269|PubMed:11402034"
FT REGION 264..381
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 545..646
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 274..279
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000255"
FT MOTIF 280..296
FT /note="Nuclear export signal (NES)"
FT /evidence="ECO:0000269|PubMed:11402034"
FT MOTIF 362..364
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000255"
FT COMPBIAS 279..300
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 317..334
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 362..381
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 553..567
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 586..612
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 208
FT /note="Asymmetric dimethylarginine; alternate"
FT /evidence="ECO:0007744|PubMed:24129315"
FT MOD_RES 208
FT /note="Omega-N-methylarginine; alternate"
FT /evidence="ECO:0007744|PubMed:24129315"
FT MOD_RES 217
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0007744|PubMed:24129315"
FT MOD_RES 237
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0007744|PubMed:24129315"
FT MOD_RES 247
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0007744|PubMed:24129315"
FT MOD_RES 257
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:19608861"
FT MOD_RES 267
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 283
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18691976,
FT ECO:0007744|PubMed:20068231"
FT MOD_RES 292
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 297
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 552
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT VAR_SEQ 61..121
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_044426"
FT VARIANT 458
FT /note="Q -> H (in dbSNP:rs2058322)"
FT /evidence="ECO:0000269|PubMed:10697960"
FT /id="VAR_068822"
FT CONFLICT 100
FT /note="D -> N (in Ref. 3; AAF86048)"
FT /evidence="ECO:0000305"
FT CONFLICT 189
FT /note="S -> N (in Ref. 3; AAF86048)"
FT /evidence="ECO:0000305"
FT CONFLICT 351..358
FT /note="ALTTQDEN -> EFSWGAWC (in Ref. 9; BAA34791)"
FT /evidence="ECO:0000305"
FT CONFLICT 599..616
FT /note="AVSPPPPPPPEEEEEGAV -> GRVAATAAAPRRRRRRAPW (in Ref.
FT 3; AAF86048)"
FT /evidence="ECO:0000305"
FT CONFLICT 641..646
FT /note="GGGGAP -> EGRRGRPV (in Ref. 3; AAF86048)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 646 AA; 71640 MW; CBC265BF25996BA2 CRC64;
MSYTGFVQGS ETTLQSTYSD TSAQPTCDYG YGTWNSGTNR GYEGYGYGYG YGQDNTTNYG
YGMATSHSWE MPSSDTNANT SASGSASADS VLSRINQRLD MVPHLETDMM QGGVYGSGGE
RYDSYESCDS RAVLSERDLY RSGYDYSELD PEMEMAYEGQ YDAYRDQFRM RGNDTFGPRA
QGWARDARSG RPMASGYGRM WEDPMGARGQ CMSGASRLPS LFSQNIIPEY GMFQGMRGGG
AFPGGSRFGF GFGNGMKQMR RTWKTWTTAD FRTKKKKRKQ GGSPDEPDSK ATRTDCSDNS
DSDNDEGTEG EATEGLEGTE AVEKGSRVDG EDEEGKEDGR EEGKEDPEKG ALTTQDENGQ
TKRKLQAGKK SQDKQKKRQR DRMVERIQFV CSLCKYRTFY EDEMASHLDS KFHKEHFKYV
GTKLPKQTAD FLQEYVTNKT KKTEELRKTV EDLDGLIQQI YRDQDLTQEI AMEHFVKKVE
AAHCAACDLF IPMQFGIIQK HLKTMDHNRN RRLMMEQSKK SSLMVARSIL NNKLISKKLE
RYLKGENPFT DSPEEEKEQE EAEGGALDEG AQGEAAGISE GAEGVPAQPP VPPEPAPGAV
SPPPPPPPEE EEEGAVPLLG GALQRQIRGI PGLDVEDDEE GGGGAP
