ID   AKA28_HUMAN             Reviewed;         197 AA.
AC   Q86UN6; A6NNZ0; Q86UN4; Q86UN5;
DT   13-APR-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2003, sequence version 1.
DT   24-JAN-2024, entry version 143.
DE   RecName: Full=A-kinase anchor protein 14;
DE            Short=AKAP-14;
DE   AltName: Full=A-kinase anchor protein 28 kDa;
DE            Short=AKAP 28;
DE   AltName: Full=Protein kinase A-anchoring protein 14;
DE            Short=PRKA14;
GN   Name=AKAP14; Synonyms=AKAP28;
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] (ISOFORMS 1; 2 AND 3), SUBUNIT, TISSUE
RP   SPECIFICITY, AND MUTAGENESIS OF LEU-43 AND VAL-47.
RC   TISSUE=Lung epithelium;
RX   PubMed=12475942; DOI=10.1091/mbc.e02-07-0391;
RA   Kultgen P.L., Byrd S.K., Ostrowski L.E., Milgram S.L.;
RT   "Characterization of an A-kinase anchoring protein in human ciliary
RT   axonemes.";
RL   Mol. Biol. Cell 13:4156-4166(2002).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=15772651; DOI=10.1038/nature03440;
RA   Ross M.T., Grafham D.V., Coffey A.J., Scherer S., McLay K., Muzny D.,
RA   Platzer M., Howell G.R., Burrows C., Bird C.P., Frankish A., Lovell F.L.,
RA   Howe K.L., Ashurst J.L., Fulton R.S., Sudbrak R., Wen G., Jones M.C.,
RA   Hurles M.E., Andrews T.D., Scott C.E., Searle S., Ramser J., Whittaker A.,
RA   Deadman R., Carter N.P., Hunt S.E., Chen R., Cree A., Gunaratne P.,
RA   Havlak P., Hodgson A., Metzker M.L., Richards S., Scott G., Steffen D.,
RA   Sodergren E., Wheeler D.A., Worley K.C., Ainscough R., Ambrose K.D.,
RA   Ansari-Lari M.A., Aradhya S., Ashwell R.I., Babbage A.K., Bagguley C.L.,
RA   Ballabio A., Banerjee R., Barker G.E., Barlow K.F., Barrett I.P.,
RA   Bates K.N., Beare D.M., Beasley H., Beasley O., Beck A., Bethel G.,
RA   Blechschmidt K., Brady N., Bray-Allen S., Bridgeman A.M., Brown A.J.,
RA   Brown M.J., Bonnin D., Bruford E.A., Buhay C., Burch P., Burford D.,
RA   Burgess J., Burrill W., Burton J., Bye J.M., Carder C., Carrel L.,
RA   Chako J., Chapman J.C., Chavez D., Chen E., Chen G., Chen Y., Chen Z.,
RA   Chinault C., Ciccodicola A., Clark S.Y., Clarke G., Clee C.M., Clegg S.,
RA   Clerc-Blankenburg K., Clifford K., Cobley V., Cole C.G., Conquer J.S.,
RA   Corby N., Connor R.E., David R., Davies J., Davis C., Davis J., Delgado O.,
RA   Deshazo D., Dhami P., Ding Y., Dinh H., Dodsworth S., Draper H.,
RA   Dugan-Rocha S., Dunham A., Dunn M., Durbin K.J., Dutta I., Eades T.,
RA   Ellwood M., Emery-Cohen A., Errington H., Evans K.L., Faulkner L.,
RA   Francis F., Frankland J., Fraser A.E., Galgoczy P., Gilbert J., Gill R.,
RA   Gloeckner G., Gregory S.G., Gribble S., Griffiths C., Grocock R., Gu Y.,
RA   Gwilliam R., Hamilton C., Hart E.A., Hawes A., Heath P.D., Heitmann K.,
RA   Hennig S., Hernandez J., Hinzmann B., Ho S., Hoffs M., Howden P.J.,
RA   Huckle E.J., Hume J., Hunt P.J., Hunt A.R., Isherwood J., Jacob L.,
RA   Johnson D., Jones S., de Jong P.J., Joseph S.S., Keenan S., Kelly S.,
RA   Kershaw J.K., Khan Z., Kioschis P., Klages S., Knights A.J., Kosiura A.,
RA   Kovar-Smith C., Laird G.K., Langford C., Lawlor S., Leversha M., Lewis L.,
RA   Liu W., Lloyd C., Lloyd D.M., Loulseged H., Loveland J.E., Lovell J.D.,
RA   Lozado R., Lu J., Lyne R., Ma J., Maheshwari M., Matthews L.H.,
RA   McDowall J., McLaren S., McMurray A., Meidl P., Meitinger T., Milne S.,
RA   Miner G., Mistry S.L., Morgan M., Morris S., Mueller I., Mullikin J.C.,
RA   Nguyen N., Nordsiek G., Nyakatura G., O'dell C.N., Okwuonu G., Palmer S.,
RA   Pandian R., Parker D., Parrish J., Pasternak S., Patel D., Pearce A.V.,
RA   Pearson D.M., Pelan S.E., Perez L., Porter K.M., Ramsey Y., Reichwald K.,
RA   Rhodes S., Ridler K.A., Schlessinger D., Schueler M.G., Sehra H.K.,
RA   Shaw-Smith C., Shen H., Sheridan E.M., Shownkeen R., Skuce C.D.,
RA   Smith M.L., Sotheran E.C., Steingruber H.E., Steward C.A., Storey R.,
RA   Swann R.M., Swarbreck D., Tabor P.E., Taudien S., Taylor T., Teague B.,
RA   Thomas K., Thorpe A., Timms K., Tracey A., Trevanion S., Tromans A.C.,
RA   d'Urso M., Verduzco D., Villasana D., Waldron L., Wall M., Wang Q.,
RA   Warren J., Warry G.L., Wei X., West A., Whitehead S.L., Whiteley M.N.,
RA   Wilkinson J.E., Willey D.L., Williams G., Williams L., Williamson A.,
RA   Williamson H., Wilming L., Woodmansey R.L., Wray P.W., Yen J., Zhang J.,
RA   Zhou J., Zoghbi H., Zorilla S., Buck D., Reinhardt R., Poustka A.,
RA   Rosenthal A., Lehrach H., Meindl A., Minx P.J., Hillier L.W., Willard H.F.,
RA   Wilson R.K., Waterston R.H., Rice C.M., Vaudin M., Coulson A., Nelson D.L.,
RA   Weinstock G., Sulston J.E., Durbin R.M., Hubbard T., Gibbs R.A., Beck S.,
RA   Rogers J., Bentley D.R.;
RT   "The DNA sequence of the human X chromosome.";
RL   Nature 434:325-337(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   TISSUE=Testis;
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).
CC   -!- FUNCTION: Binds to type II regulatory subunits of protein kinase A and
CC       anchors/targets them.
CC   -!- SUBUNIT: Binds to type II regulatory subunits (RII).
CC       {ECO:0000269|PubMed:12475942}.
CC   -!- INTERACTION:
CC       Q86UN6; Q9C005: DPY30; NbExp=3; IntAct=EBI-2119626, EBI-744973;
CC       Q86UN6; P31321: PRKAR1B; NbExp=3; IntAct=EBI-2119626, EBI-2805516;
CC       Q86UN6; P13861-2: PRKAR2A; NbExp=3; IntAct=EBI-2119626, EBI-11752137;
CC       Q86UN6; P31323: PRKAR2B; NbExp=7; IntAct=EBI-2119626, EBI-2930670;
CC       Q86UN6; Q9HAT0: ROPN1; NbExp=3; IntAct=EBI-2119626, EBI-1378139;
CC       Q86UN6; Q96C74: ROPN1L; NbExp=3; IntAct=EBI-2119626, EBI-9033237;
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=3;
CC       Name=1; Synonyms=Isoform A;
CC         IsoId=Q86UN6-1; Sequence=Displayed;
CC       Name=2; Synonyms=Isoform B;
CC         IsoId=Q86UN6-2; Sequence=VSP_009909;
CC       Name=3; Synonyms=Isoform C;
CC         IsoId=Q86UN6-3; Sequence=VSP_009910, VSP_009911;
CC   -!- TISSUE SPECIFICITY: Present in cilia (at protein level). Expressed in
CC       tissues containing axoneme-based organelles (cilia and/or flagella):
CC       trachea and testis. Highly expressed in airway cilia.
CC       {ECO:0000269|PubMed:12475942}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AF514780; AAP20825.1; -; mRNA.
DR   EMBL; AF514781; AAP20826.1; -; mRNA.
DR   EMBL; AF514782; AAP20827.1; -; mRNA.
DR   EMBL; AC002477; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; BC066357; AAH66357.1; -; mRNA.
DR   CCDS; CCDS14591.1; -. [Q86UN6-1]
DR   CCDS; CCDS35376.1; -. [Q86UN6-2]
DR   CCDS; CCDS35377.1; -. [Q86UN6-3]
DR   RefSeq; NP_001008534.1; NM_001008534.1. [Q86UN6-2]
DR   RefSeq; NP_001008535.1; NM_001008535.1. [Q86UN6-3]
DR   RefSeq; NP_848928.1; NM_178813.5. [Q86UN6-1]
DR   AlphaFoldDB; Q86UN6; -.
DR   SMR; Q86UN6; -.
DR   BioGRID; 127707; 18.
DR   IntAct; Q86UN6; 15.
DR   STRING; 9606.ENSP00000360485; -.
DR   iPTMnet; Q86UN6; -.
DR   PhosphoSitePlus; Q86UN6; -.
DR   BioMuta; AKAP14; -.
DR   DMDM; 46395790; -.
DR   MassIVE; Q86UN6; -.
DR   PaxDb; 9606-ENSP00000360485; -.
DR   PeptideAtlas; Q86UN6; -.
DR   ProteomicsDB; 1648; -.
DR   ProteomicsDB; 69835; -. [Q86UN6-1]
DR   ProteomicsDB; 69836; -. [Q86UN6-2]
DR   ProteomicsDB; 69837; -. [Q86UN6-3]
DR   Antibodypedia; 44608; 120 antibodies from 27 providers.
DR   DNASU; 158798; -.
DR   Ensembl; ENST00000334356.2; ENSP00000334680.2; ENSG00000186471.13. [Q86UN6-2]
DR   Ensembl; ENST00000371422.5; ENSP00000360476.1; ENSG00000186471.13. [Q86UN6-3]
DR   Ensembl; ENST00000371425.8; ENSP00000360479.4; ENSG00000186471.13. [Q86UN6-2]
DR   Ensembl; ENST00000371431.8; ENSP00000360485.3; ENSG00000186471.13. [Q86UN6-1]
DR   GeneID; 158798; -.
DR   KEGG; hsa:158798; -.
DR   MANE-Select; ENST00000371431.8; ENSP00000360485.3; NM_178813.6; NP_848928.1.
DR   UCSC; uc004ese.4; human. [Q86UN6-1]
DR   AGR; HGNC:24061; -.
DR   CTD; 158798; -.
DR   GeneCards; AKAP14; -.
DR   HGNC; HGNC:24061; AKAP14.
DR   HPA; ENSG00000186471; Group enriched (choroid plexus, fallopian tube, testis).
DR   MIM; 300462; gene.
DR   neXtProt; NX_Q86UN6; -.
DR   OpenTargets; ENSG00000186471; -.
DR   PharmGKB; PA134914893; -.
DR   VEuPathDB; HostDB:ENSG00000186471; -.
DR   eggNOG; ENOG502S0CR; Eukaryota.
DR   GeneTree; ENSGT00390000003444; -.
DR   HOGENOM; CLU_116552_0_0_1; -.
DR   InParanoid; Q86UN6; -.
DR   OMA; TWELPSC; -.
DR   OrthoDB; 5382799at2759; -.
DR   PhylomeDB; Q86UN6; -.
DR   TreeFam; TF329057; -.
DR   PathwayCommons; Q86UN6; -.
DR   SignaLink; Q86UN6; -.
DR   BioGRID-ORCS; 158798; 9 hits in 772 CRISPR screens.
DR   ChiTaRS; AKAP14; human.
DR   GenomeRNAi; 158798; -.
DR   Pharos; Q86UN6; Tbio.
DR   PRO; PR:Q86UN6; -.
DR   Proteomes; UP000005640; Chromosome X.
DR   RNAct; Q86UN6; Protein.
DR   Bgee; ENSG00000186471; Expressed in bronchial epithelial cell and 116 other cell types or tissues.
DR   GO; GO:0005930; C:axoneme; IDA:UniProtKB.
DR   GO; GO:0005952; C:cAMP-dependent protein kinase complex; IMP:UniProtKB.
DR   GO; GO:0034237; F:protein kinase A regulatory subunit binding; IPI:UniProtKB.
DR   InterPro; IPR025663; AKAP_28.
DR   PANTHER; PTHR35075; A-KINASE ANCHOR PROTEIN 14; 1.
DR   PANTHER; PTHR35075:SF1; A-KINASE ANCHOR PROTEIN 14; 1.
DR   Pfam; PF14469; AKAP28; 1.
DR   Genevisible; Q86UN6; HS.
PE   1: Evidence at protein level;
KW   Alternative splicing; Cytoplasm; Reference proteome.
FT   CHAIN           1..197
FT                   /note="A-kinase anchor protein 14"
FT                   /id="PRO_0000064521"
FT   REGION          1..29
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          35..52
FT                   /note="RII-binding"
FT   VAR_SEQ         88..147
FT                   /note="Missing (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:12475942"
FT                   /id="VSP_009909"
FT   VAR_SEQ         88..89
FT                   /note="KC -> VS (in isoform 3)"
FT                   /evidence="ECO:0000303|PubMed:12475942"
FT                   /id="VSP_009910"
FT   VAR_SEQ         90..197
FT                   /note="Missing (in isoform 3)"
FT                   /evidence="ECO:0000303|PubMed:12475942"
FT                   /id="VSP_009911"
FT   MUTAGEN         43
FT                   /note="L->P: Abolishes RII-binding; when associated with
FT                   P-47."
FT                   /evidence="ECO:0000269|PubMed:12475942"
FT   MUTAGEN         47
FT                   /note="V->P: Abolishes RII-binding; when associated with
FT                   P-43."
FT                   /evidence="ECO:0000269|PubMed:12475942"
FT   CONFLICT        Q86UN6-2:87
FT                   /note="S -> SP (in Ref. 1; AAP20826)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   197 AA;  22815 MW;  3A76B9C3036EAEB9 CRC64;
     MSETQNSTSQ KAMDEDNKAA SQTMPNTQDK NYEDELTQVA LALVEDVINY AVKIVEEERN
     PLKNIKWMTH GEFTVEKGLK QIDEYFSKCV SKKCWAHGVE FVERKDLIHS FLYIYYVHWS
     ISTADLPVAR ISAGTYFTMK VSKTKPPDAP IVVSYVGDHQ ALVHRPGMVR FRENWQKNLT
     DAKYSFMESF PFLFNRV
//