AKP8L_MOUSE
ID AKP8L_MOUSE Reviewed; 642 AA.
AC Q9R0L7;
DT 27-APR-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 25-MAY-2022, entry version 129.
DE RecName: Full=A-kinase anchor protein 8-like;
DE Short=AKAP8-like protein;
DE AltName: Full=Neighbor of A-kinase-anchoring protein 95;
DE Short=Neighbor of AKAP95;
GN Name=Akap8l; Synonyms=Nakap, Nakap95;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Hattori A., Seki N., Hayashi A., Kozuma S., Muramatsu M.-A., Miyajima N.,
RA Saito T.;
RT "Mouse NAKAP95.";
RL Submitted (JUN-1999) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP PROTEIN SEQUENCE OF 511-520, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC STRAIN=OF1; TISSUE=Hippocampus;
RA Lubec G., Sunyer B., Chen W.-Q.;
RL Submitted (JAN-2009) to UniProtKB.
RN [3]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
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. Proposed to target PRKACA to
CC the nucleus but does not seem to be implicated in the binding of
CC regulatory subunit II of PKA. 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. May regulate the initiation phase of DNA
CC replication when associated with TMPO isoform Beta. Required for cell
CC cycle G2/M transition and histone deacetylation during mitosis. In
CC mitotic cells recruits HDAC3 to the vicinity of chromatin leading to
CC deacetylation and subsequent phosphorylation at 'Ser-10' of histone H3;
CC in this function seems to act redundantly with AKAP8. May be involved
CC in regulation of pre-mRNA splicing (By similarity).
CC {ECO:0000250|UniProtKB:Q9ULX6}.
CC -!- SUBUNIT: Interacts (via N-terminus) with DHX9 (via RGG region).
CC Interacts with TMPO isoform Beta, PRPF40A, RNF43, lamin-B. Interacts
CC with HDAC3; increased during mitosis (By similarity).
CC {ECO:0000250|UniProtKB:Q9ULX6}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q9ULX6}. Nucleus
CC matrix {ECO:0000250|UniProtKB:Q9ULX6}. Nucleus speckle
CC {ECO:0000250|UniProtKB:Q9ULX6}. Nucleus, PML body
CC {ECO:0000250|UniProtKB:Q9ULX6}. Cytoplasm
CC {ECO:0000250|UniProtKB:Q9ULX6}. Note=Colocalizes with PRPF40A in the
CC nuclear matrix. Nuclear at steady state but shuttles between the
CC nucleus and cytoplasm. The shuttling property has been questioned.
CC Colocalizes with EBNA-LP in PML bodies. {ECO:0000250|UniProtKB:Q9ULX6}.
CC -!- PTM: Phosphorylated on serine or threonine residues possibly by PKA.
CC {ECO:0000250|UniProtKB:Q9ULX6}.
CC -!- SIMILARITY: Belongs to the AKAP95 family. {ECO:0000255|PROSITE-
CC ProRule:PRU01140}.
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DR EMBL; AB028921; BAA84711.1; -; mRNA.
DR AlphaFoldDB; Q9R0L7; -.
DR IntAct; Q9R0L7; 3.
DR MINT; Q9R0L7; -.
DR STRING; 10090.ENSMUSP00000051389; -.
DR iPTMnet; Q9R0L7; -.
DR PhosphoSitePlus; Q9R0L7; -.
DR EPD; Q9R0L7; -.
DR MaxQB; Q9R0L7; -.
DR PaxDb; Q9R0L7; -.
DR PeptideAtlas; Q9R0L7; -.
DR PRIDE; Q9R0L7; -.
DR ProteomicsDB; 285802; -.
DR MGI; MGI:1860606; Akap8l.
DR eggNOG; ENOG502QSFC; Eukaryota.
DR InParanoid; Q9R0L7; -.
DR PhylomeDB; Q9R0L7; -.
DR ChiTaRS; Akap8l; mouse.
DR PRO; PR:Q9R0L7; -.
DR Proteomes; UP000000589; Unplaced.
DR RNAct; Q9R0L7; protein.
DR GO; GO:0000785; C:chromatin; ISO:MGI.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0016363; C:nuclear matrix; IDA:UniProtKB.
DR GO; GO:0016607; C:nuclear speck; ISO:MGI.
DR GO; GO:0005634; C:nucleus; ISO:MGI.
DR GO; GO:0016605; C:PML body; IEA:UniProtKB-SubCell.
DR GO; GO:1990904; C:ribonucleoprotein complex; ISS:UniProtKB.
DR GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR GO; GO:0042826; F:histone deacetylase binding; ISO:MGI.
DR GO; GO:0005521; F:lamin binding; ISO:MGI.
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:0044839; P:cell cycle G2/M phase transition; ISO:MGI.
DR GO; GO:0007076; P:mitotic chromosome condensation; ISO:MGI.
DR GO; GO:0006397; P:mRNA processing; ISO:MGI.
DR GO; GO:0051081; P:nuclear membrane disassembly; ISO:MGI.
DR GO; GO:0031065; P:positive regulation of histone deacetylation; ISO:MGI.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; ISO:MGI.
DR GO; GO:0033127; P:regulation of histone phosphorylation; ISO:MGI.
DR GO; GO:0010793; P:regulation of mRNA export from nucleus; ISS:UniProtKB.
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; Cytoplasm; Direct protein sequencing; Metal-binding;
KW Methylation; Nucleus; Phosphoprotein; Reference proteome; Repeat;
KW Transcription; Transcription regulation; Zinc; Zinc-finger.
FT CHAIN 1..642
FT /note="A-kinase anchor protein 8-like"
FT /id="PRO_0000075385"
FT ZN_FING 392..414
FT /note="C2H2 AKAP95-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01140"
FT ZN_FING 485..508
FT /note="C2H2 AKAP95-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01140"
FT REGION 1..269
FT /note="Sufficient for activation of CTE-mediated
FT expression"
FT /evidence="ECO:0000250|UniProtKB:Q9ULX6"
FT REGION 265..382
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 546..642
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 275..280
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000255"
FT MOTIF 281..297
FT /note="Nuclear export signal (NES)"
FT /evidence="ECO:0000250|UniProtKB:Q9ULX6"
FT MOTIF 363..365
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000255"
FT COMPBIAS 280..301
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 318..335
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 363..382
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 554..568
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 586..611
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 209
FT /note="Asymmetric dimethylarginine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q9ULX6"
FT MOD_RES 209
FT /note="Omega-N-methylarginine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q9ULX6"
FT MOD_RES 218
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0000250|UniProtKB:Q9ULX6"
FT MOD_RES 238
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0000250|UniProtKB:Q9ULX6"
FT MOD_RES 248
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0000250|UniProtKB:Q9ULX6"
FT MOD_RES 258
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q9ULX6"
FT MOD_RES 268
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q9ULX6"
FT MOD_RES 284
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9ULX6"
FT MOD_RES 293
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q9ULX6"
FT MOD_RES 298
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9ULX6"
SQ SEQUENCE 642 AA; 71454 MW; 4CE8DFE66810A0FC CRC64;
MSYTGFVQGS ETTLQSTYCD TSAQPTCDYG YGTWNSGTNR GYENYGYGYG YGQDNTTNYG
YGMATSHSWE MASSDTNANP SASGSASADS VLSRINQRLD MMPHLETDMI QGGVYGSGGG
ERYDSYEACD SRAILSERDL YRSSYDYGEL DPEMEMAYEG QYDAYRDQFR MRGGDTFGPR
AQGWARDARS GRPMASGYGR MWEDPMGARG QCMPGASRLP SLFSQNIIPE YGMFQGMRGG
GAFSGGSRFG FGFGNGMKQM RRTWKTWTTA DFRTKKKKRK QGGSPDEPDS KATRTDCSDN
SDSDNDEGTE GEAAEGTESA EAMEKGSRVD GEDEEGKEDG REEGKEDPEK GALTAQDESS
QAKRKLQASK KSQDKQKKRQ RDRMVERIQF VCSLCKYRTF YEDEMGSHLD SKFHKEHFKY
VGTKLPKQTA DFLQEYVTNK TKKTEELRKT VEDLDGLIQQ IYRDQDLTQE IAMEHFVKKV
EAAHCAACDL FIPMQFGIIQ KHLKTMDHNR NRRLMMEQSK KSSLMVARSI LNNKLISKKL
ERYLKGENPF TDNPEEEKEQ DEVEAGALDE GAPSEATELT EGVPAQPPVP LEPAPGTTTP
PPPPPPEEEE SPVPLLGGAL QCQIRGIPGL DMEDDEEGGG GP
