AKA10_HUMAN
ID AKA10_HUMAN Reviewed; 662 AA.
AC O43572; B2R650; Q96AJ7;
DT 21-FEB-2001, integrated into UniProtKB/Swiss-Prot.
DT 19-JUL-2005, sequence version 2.
DT 03-AUG-2022, entry version 170.
DE RecName: Full=A-kinase anchor protein 10, mitochondrial;
DE Short=AKAP-10;
DE AltName: Full=Dual specificity A kinase-anchoring protein 2;
DE Short=D-AKAP-2;
DE AltName: Full=Protein kinase A-anchoring protein 10;
DE Short=PRKA10;
DE Flags: Precursor;
GN Name=AKAP10;
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], AND SUBCELLULAR LOCATION.
RC TISSUE=Brain;
RX PubMed=11248059; DOI=10.1073/pnas.051633398;
RA Wang L., Sunahara R.K., Krumins A., Perkins G., Crochiere M.L., Mackey M.,
RA Bell S., Ellisman M.H., Taylor S.S.;
RT "Cloning and mitochondrial localization of full-length D-AKAP2, a protein
RT kinase A anchoring protein.";
RL Proc. Natl. Acad. Sci. U.S.A. 98:3220-3225(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Chatterjee T.K., Fisher R.A.;
RT "Homo sapiens protein kinase A anchoring protein with an RGS domain.";
RL Submitted (DEC-1997) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain;
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 [4]
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Lung;
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 [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-52, 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 [7]
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 [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-189 AND SER-281, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma, and 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 [9]
RP VARIANT VAL-646.
RX PubMed=17485678; DOI=10.1073/pnas.0610393104;
RA Tingley W.G., Pawlikowska L., Zaroff J.G., Kim T., Nguyen T., Young S.G.,
RA Vranizan K., Kwok P.Y., Whooley M.A., Conklin B.R.;
RT "Gene-trapped mouse embryonic stem cell-derived cardiac myocytes and human
RT genetics implicate AKAP10 in heart rhythm regulation.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:8461-8466(2007).
CC -!- FUNCTION: Differentially targeted protein that binds to type I and II
CC regulatory subunits of protein kinase A and anchors them to the
CC mitochondria or the plasma membrane. Although the physiological
CC relevance between PKA and AKAPS with mitochondria is not fully
CC understood, one idea is that BAD, a proapoptotic member, is
CC phosphorylated and inactivated by mitochondria-anchored PKA. It cannot
CC be excluded too that it may facilitate PKA as well as G protein signal
CC transduction, by acting as an adapter for assembling multiprotein
CC complexes. With its RGS domain, it could lead to the interaction to G-
CC alpha proteins, providing a link between the signaling machinery and
CC the downstream kinase (By similarity). {ECO:0000250}.
CC -!- INTERACTION:
CC O43572; P00514: PRKAR1A; Xeno; NbExp=2; IntAct=EBI-752153, EBI-1041635;
CC -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000269|PubMed:11248059}.
CC Membrane {ECO:0000269|PubMed:11248059}. Cytoplasm
CC {ECO:0000269|PubMed:11248059}. Note=Predominantly mitochondrial but
CC also membrane associated and cytoplasmic.
CC -!- DOMAIN: RII-alpha binding site, predicted to form an amphipathic helix,
CC could participate in protein-protein interactions with a complementary
CC surface on the R-subunit dimer.
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DR EMBL; AF037439; AAB92260.1; -; mRNA.
DR EMBL; AK312438; BAG35347.1; -; mRNA.
DR EMBL; CH471212; EAW50913.1; -; Genomic_DNA.
DR EMBL; BC017055; AAH17055.1; -; mRNA.
DR CCDS; CCDS11214.1; -.
DR RefSeq; NP_009133.2; NM_007202.3.
DR PDB; 3IM4; X-ray; 2.28 A; C=623-662.
DR PDB; 3TMH; X-ray; 3.80 A; D/H/L=623-662.
DR PDBsum; 3IM4; -.
DR PDBsum; 3TMH; -.
DR AlphaFoldDB; O43572; -.
DR SMR; O43572; -.
DR BioGRID; 116385; 28.
DR DIP; DIP-48753N; -.
DR IntAct; O43572; 73.
DR MINT; O43572; -.
DR STRING; 9606.ENSP00000225737; -.
DR iPTMnet; O43572; -.
DR PhosphoSitePlus; O43572; -.
DR SwissPalm; O43572; -.
DR BioMuta; AKAP10; -.
DR EPD; O43572; -.
DR jPOST; O43572; -.
DR MassIVE; O43572; -.
DR MaxQB; O43572; -.
DR PaxDb; O43572; -.
DR PeptideAtlas; O43572; -.
DR PRIDE; O43572; -.
DR ProteomicsDB; 49061; -.
DR Antibodypedia; 26069; 266 antibodies from 35 providers.
DR DNASU; 11216; -.
DR Ensembl; ENST00000225737.11; ENSP00000225737.6; ENSG00000108599.15.
DR GeneID; 11216; -.
DR KEGG; hsa:11216; -.
DR MANE-Select; ENST00000225737.11; ENSP00000225737.6; NM_007202.4; NP_009133.2.
DR UCSC; uc002gwo.5; human.
DR CTD; 11216; -.
DR DisGeNET; 11216; -.
DR GeneCards; AKAP10; -.
DR HGNC; HGNC:368; AKAP10.
DR HPA; ENSG00000108599; Low tissue specificity.
DR MalaCards; AKAP10; -.
DR MIM; 604694; gene.
DR neXtProt; NX_O43572; -.
DR OpenTargets; ENSG00000108599; -.
DR PharmGKB; PA24662; -.
DR VEuPathDB; HostDB:ENSG00000108599; -.
DR eggNOG; KOG3590; Eukaryota.
DR GeneTree; ENSGT00390000015077; -.
DR InParanoid; O43572; -.
DR OMA; QWQAFDL; -.
DR OrthoDB; 644347at2759; -.
DR PhylomeDB; O43572; -.
DR TreeFam; TF105409; -.
DR PathwayCommons; O43572; -.
DR Reactome; R-HSA-983231; Factors involved in megakaryocyte development and platelet production.
DR SignaLink; O43572; -.
DR BioGRID-ORCS; 11216; 11 hits in 1081 CRISPR screens.
DR ChiTaRS; AKAP10; human.
DR EvolutionaryTrace; O43572; -.
DR GeneWiki; AKAP10; -.
DR GenomeRNAi; 11216; -.
DR Pharos; O43572; Tbio.
DR PRO; PR:O43572; -.
DR Proteomes; UP000005640; Chromosome 17.
DR RNAct; O43572; protein.
DR Bgee; ENSG00000108599; Expressed in buccal mucosa cell and 194 other tissues.
DR ExpressionAtlas; O43572; baseline and differential.
DR Genevisible; O43572; HS.
DR GO; GO:0005829; C:cytosol; IDA:HPA.
DR GO; GO:0005739; C:mitochondrion; IBA:GO_Central.
DR GO; GO:0005886; C:plasma membrane; IDA:HPA.
DR GO; GO:0032991; C:protein-containing complex; IDA:UniProtKB.
DR GO; GO:0051018; F:protein kinase A binding; IPI:UniProtKB.
DR GO; GO:0008104; P:protein localization; IBA:GO_Central.
DR GO; GO:0007165; P:signal transduction; TAS:ProtInc.
DR CDD; cd12804; AKAP10_AKB; 1.
DR Gene3D; 1.10.167.10; -; 3.
DR InterPro; IPR037719; AKAP10_AKB_dom.
DR InterPro; IPR016137; RGS.
DR InterPro; IPR036305; RGS_sf.
DR InterPro; IPR044926; RGS_subdomain_2.
DR Pfam; PF00615; RGS; 2.
DR SMART; SM00315; RGS; 2.
DR SUPFAM; SSF48097; SSF48097; 2.
DR PROSITE; PS50132; RGS; 2.
PE 1: Evidence at protein level;
KW 3D-structure; Cytoplasm; Membrane; Mitochondrion; Phosphoprotein;
KW Reference proteome; Repeat; Transit peptide.
FT TRANSIT 1..28
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN 29..662
FT /note="A-kinase anchor protein 10, mitochondrial"
FT /id="PRO_0000030404"
FT DOMAIN 125..369
FT /note="RGS 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00171"
FT DOMAIN 379..505
FT /note="RGS 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00171"
FT REGION 1..55
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 261..282
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 524..548
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 634..647
FT /note="PKA-RII subunit binding"
FT COMPBIAS 27..41
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 52
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18691976"
FT MOD_RES 189
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 281
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT VARIANT 249
FT /note="R -> H (in dbSNP:rs2108978)"
FT /id="VAR_024607"
FT VARIANT 646
FT /note="I -> V (associated with increased basal heart rate
FT and decreased heart rate variability; dbSNP:rs203462)"
FT /evidence="ECO:0000269|PubMed:17485678"
FT /id="VAR_024608"
FT CONFLICT 177
FT /note="V -> M (in Ref. 2; AAB92260)"
FT /evidence="ECO:0000305"
FT CONFLICT 524
FT /note="L -> P (in Ref. 2; AAB92260)"
FT /evidence="ECO:0000305"
FT HELIX 629..653
FT /evidence="ECO:0007829|PDB:3IM4"
SQ SEQUENCE 662 AA; 73818 MW; B7A6D92CA2D3D794 CRC64;
MRGAGPSPRQ SPRTLRPDPG PAMSFFRRKV KGKEQEKTSD VKSIKASISV HSPQKSTKNH
ALLEAAGPSH VAINAISANM DSFSSSRTAT LKKQPSHMEA AHFGDLGRSC LDYQTQETKS
SLSKTLEQVL HDTIVLPYFI QFMELRRMEH LVKFWLEAES FHSTTWSRIR AHSLNTVKQS
SLAEPVSPSK KHETTASFLT DSLDKRLEDS GSAQLFMTHS EGIDLNNRTN STQNHLLLSQ
ECDSAHSLRL EMARAGTHQV SMETQESSST LTVASRNSPA SPLKELSGKL MKSIEQDAVN
TFTKYISPDA AKPIPITEAM RNDIIARICG EDGQVDPNCF VLAQSIVFSA MEQEHFSEFL
RSHHFCKYQI EVLTSGTVYL ADILFCESAL FYFSEYMEKE DAVNILQFWL AADNFQSQLA
AKKGQYDGQE AQNDAMILYD KYFSLQATHP LGFDDVVRLE IESNICREGG PLPNCFTTPL
RQAWTTMEKV FLPGFLSSNL YYKYLNDLIH SVRGDEFLGG NVSLTAPGSV GPPDESHPGS
SDSSASQSSV KKASIKILKN FDEAIIVDAA SLDPESLYQR TYAGKMTFGR VSDLGQFIRE
SEPEPDVRKS KGSMFSQAMK KWVQGNTDEA QEELAWKIAK MIVSDIMQQA QYDQPLEKST
KL
