FAKD2_HUMAN
ID FAKD2_HUMAN Reviewed; 710 AA.
AC Q9NYY8; Q9NVX6; Q9Y2H7;
DT 07-FEB-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 160.
DE RecName: Full=FAST kinase domain-containing protein 2, mitochondrial;
DE Flags: Precursor;
GN Name=FASTKD2 {ECO:0000303|PubMed:27667664, ECO:0000312|HGNC:HGNC:29160};
GN Synonyms=KIAA0971;
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 [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Brain;
RX PubMed=10231032; DOI=10.1093/dnares/6.1.63;
RA Nagase T., Ishikawa K., Suyama M., Kikuno R., Hirosawa M., Miyajima N.,
RA Tanaka A., Kotani H., Nomura N., Ohara O.;
RT "Prediction of the coding sequences of unidentified human genes. XIII. The
RT complete sequences of 100 new cDNA clones from brain which code for large
RT proteins in vitro.";
RL DNA Res. 6:63-70(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Adrenal gland;
RX PubMed=10931946; DOI=10.1073/pnas.160270997;
RA Hu R.-M., Han Z.-G., Song H.-D., Peng Y.-D., Huang Q.-H., Ren S.-X.,
RA Gu Y.-J., Huang C.-H., Li Y.-B., Jiang C.-L., Fu G., Zhang Q.-H., Gu B.-W.,
RA Dai M., Mao Y.-F., Gao G.-F., Rong R., Ye M., Zhou J., Xu S.-H., Gu J.,
RA Shi J.-X., Jin W.-R., Zhang C.-K., Wu T.-M., Huang G.-Y., Chen Z.,
RA Chen M.-D., Chen J.-L.;
RT "Gene expression profiling in the human hypothalamus-pituitary-adrenal axis
RT and full-length cDNA cloning.";
RL Proc. Natl. Acad. Sci. U.S.A. 97:9543-9548(2000).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Melanoma;
RX PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D.,
RA Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A.,
RA Wiemann S., Schupp I.;
RT "The full-ORF clone resource of the German cDNA consortium.";
RL BMC Genomics 8:399-399(2007).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15815621; DOI=10.1038/nature03466;
RA Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P.,
RA Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C.,
RA Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L.,
RA Du H., Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A.,
RA Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J.,
RA Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M.,
RA Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T.,
RA Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S.,
RA Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K.,
RA McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C.,
RA Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S.,
RA Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C.,
RA Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M.,
RA Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C.,
RA Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J.,
RA Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E.,
RA Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X.,
RA Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M.,
RA Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C.,
RA Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S.,
RA Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H.,
RA Wilson R.K.;
RT "Generation and annotation of the DNA sequences of human chromosomes 2 and
RT 4.";
RL Nature 434:724-731(2005).
RN [5]
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 [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 442-710 (ISOFORM 1).
RC TISSUE=Teratocarcinoma;
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 [7]
RP FUNCTION, SUBCELLULAR LOCATION, INVOLVEMENT IN COXPD44, AND VARIANT COXPD44
RP 432-ARG--GLN-710 DEL.
RX PubMed=18771761; DOI=10.1016/j.ajhg.2008.08.009;
RA Ghezzi D., Saada A., D'Adamo P., Fernandez-Vizarra E., Gasparini P.,
RA Tiranti V., Elpeleg O., Zeviani M.;
RT "FASTKD2 nonsense mutation in an infantile mitochondrial encephalomyopathy
RT associated with cytochrome c oxidase deficiency.";
RL Am. J. Hum. Genet. 83:415-423(2008).
RN [8]
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 [9]
RP SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=20869947; DOI=10.1016/j.bbrc.2010.09.075;
RA Simarro M., Gimenez-Cassina A., Kedersha N., Lazaro J.B., Adelmant G.O.,
RA Marto J.A., Rhee K., Tisdale S., Danial N., Benarafa C., Orduna A.,
RA Anderson P.;
RT "Fast kinase domain-containing protein 3 is a mitochondrial protein
RT essential for cellular respiration.";
RL Biochem. Biophys. Res. Commun. 401:440-446(2010).
RN [10]
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).
RN [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-126 AND SER-140, 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 [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-708, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [13]
RP FUNCTION, IDENTIFICATION IN A COMPLEX WITH GRSF1; DDX28; DHX30 AND FASTKD5,
RP SUBCELLULAR LOCATION, RNA-BINDING, AND IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=25683715; DOI=10.1016/j.celrep.2015.01.030;
RA Antonicka H., Shoubridge E.A.;
RT "Mitochondrial RNA granules are centers for post-transcriptional RNA
RT processing and ribosome biogenesis.";
RL Cell Rep. 10:920-932(2015).
RN [14]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25944712; DOI=10.1002/pmic.201400617;
RA Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., Ayoub D.,
RA Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
RT "N-terminome analysis of the human mitochondrial proteome.";
RL Proteomics 15:2519-2524(2015).
RN [15]
RP FUNCTION.
RX PubMed=26370583; DOI=10.1261/rna.052365.115;
RA Popow J., Alleaume A.-M., Curk T., Schwarzl T., Sauer S., Hentze M.W.;
RT "FASTKD2 is an RNA-binding protein required for mitochondrial RNA
RT processing and translation.";
RL RNA 21:1873-1884(2015).
RN [16]
RP SUBUNIT, AND FUNCTION.
RX PubMed=27667664; DOI=10.1016/j.cmet.2016.08.017;
RA Arroyo J.D., Jourdain A.A., Calvo S.E., Ballarano C.A., Doench J.G.,
RA Root D.E., Mootha V.K.;
RT "A Genome-wide CRISPR Death Screen Identifies Genes Essential for Oxidative
RT Phosphorylation.";
RL Cell Metab. 24:875-885(2016).
RN [17]
RP VARIANTS COXPD44 205-ARG--GLN-710 DEL AND PRO-255.
RX PubMed=28499982; DOI=10.1016/j.mito.2017.05.005;
RA Yoo D.H., Choi Y.C., Nam D.E., Choi S.S., Kim J.W., Choi B.O., Chung K.W.;
RT "Identification of FASTKD2 compound heterozygous mutations as the
RT underlying cause of autosomal recessive MELAS-like syndrome.";
RL Mitochondrion 35:54-58(2017).
RN [18]
RP VARIANT COXPD44 290-ARG--GLN-710 DEL, AND CHARACTERIZATION OF VARIANT
RP COXPD44 290-ARG--GLN-710 DEL.
RX PubMed=31944455; DOI=10.1002/humu.23985;
RA Wei X., Du M., Li D., Wen S., Xie J., Li Y., Chen A., Zhang K., Xu P.,
RA Jia M., Wen C., Zhou H., Lyu J., Yang Y., Fang H.;
RT "Mutations in FASTKD2 are associated with mitochondrial disease with multi-
RT OXPHOS deficiency.";
RL Hum. Mutat. 41:961-972(2020).
CC -!- FUNCTION: Plays an important role in assembly of the mitochondrial
CC large ribosomal subunit (PubMed:25683715). As a component of a
CC functional protein-RNA module, consisting of RCC1L, NGRN, RPUSD3,
CC RPUSD4, TRUB2, FASTKD2 and 16S mitochondrial ribosomal RNA (16S mt-
CC rRNA), controls 16S mt-rRNA abundance and is required for intra-
CC mitochondrial translation (PubMed:27667664, PubMed:25683715,
CC PubMed:26370583). May play a role in mitochondrial apoptosis.
CC {ECO:0000269|PubMed:18771761, ECO:0000269|PubMed:25683715,
CC ECO:0000269|PubMed:26370583, ECO:0000269|PubMed:27667664}.
CC -!- SUBUNIT: Monomer. Found in a complex with GRSF1, DDX28, DHX30 and
CC FASTKD5. Associates with the 16S mitochondrial rRNA (16S mt-rRNA)
CC (PubMed:25683715). Forms a regulatory protein-RNA complex, consisting
CC of RCC1L, NGRN, RPUSD3, RPUSD4, TRUB2, FASTKD2 and 16S mt-rRNA
CC (PubMed:27667664). {ECO:0000269|PubMed:25683715,
CC ECO:0000269|PubMed:27667664}.
CC -!- INTERACTION:
CC Q9NYY8; P13473-2: LAMP2; NbExp=3; IntAct=EBI-1055752, EBI-21591415;
CC Q9NYY8; Q9Y371: SH3GLB1; NbExp=3; IntAct=EBI-1055752, EBI-2623095;
CC -!- SUBCELLULAR LOCATION: Mitochondrion matrix, mitochondrion nucleoid
CC {ECO:0000269|PubMed:20869947, ECO:0000269|PubMed:25683715}.
CC Mitochondrion matrix {ECO:0000305|PubMed:18771761}. Note=Localizes to
CC mitochondrial RNA granules found in close proximity to the
CC mitochondrial nucleoids. {ECO:0000269|PubMed:25683715}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9NYY8-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9NYY8-2; Sequence=VSP_017186, VSP_017187;
CC -!- TISSUE SPECIFICITY: Expression detected in spleen, thymus, testis,
CC ovary, colon, heart, smooth muscle, kidney, brain, lung, liver and
CC white adipose tissue with highest expression in heart, smooth muscle
CC and thyroid. {ECO:0000269|PubMed:20869947}.
CC -!- DISEASE: Combined oxidative phosphorylation deficiency 44 (COXPD44)
CC [MIM:618855]: An autosomal recessive mitochondrial disorder
CC characterized by onset in infancy or early childhood of global
CC developmental delay, hypotonia, and abnormal movements. Combined
CC oxidative phosphorylation deficiency is present in skeletal muscle.
CC Most patients have seizures associated with status epilepticus.
CC Additional variable features include optic atrophy, hypertrophic
CC cardiomyopathy, stroke-like episodes, and increased lactate levels in
CC serum and cerebrospinal fluid. {ECO:0000269|PubMed:18771761,
CC ECO:0000269|PubMed:28499982, ECO:0000269|PubMed:31944455}. Note=The
CC disease is caused by variants affecting the gene represented in this
CC entry.
CC -!- SIMILARITY: Belongs to the FAST kinase family. {ECO:0000305}.
CC -!- CAUTION: It is uncertain whether Met-1 or Met-17 is the initiator.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAA76815.2; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC Sequence=BAA91617.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AB023188; BAA76815.2; ALT_INIT; mRNA.
DR EMBL; AF223470; AAF64145.1; -; mRNA.
DR EMBL; AL833877; CAD38734.1; -; mRNA.
DR EMBL; AC008269; AAX93275.1; -; Genomic_DNA.
DR EMBL; BC001544; AAH01544.1; -; mRNA.
DR EMBL; AK001315; BAA91617.1; ALT_INIT; mRNA.
DR CCDS; CCDS2371.1; -. [Q9NYY8-1]
DR RefSeq; NP_001129665.1; NM_001136193.1. [Q9NYY8-1]
DR RefSeq; NP_001129666.1; NM_001136194.1. [Q9NYY8-1]
DR RefSeq; NP_055744.2; NM_014929.3. [Q9NYY8-1]
DR AlphaFoldDB; Q9NYY8; -.
DR BioGRID; 116535; 271.
DR CORUM; Q9NYY8; -.
DR IntAct; Q9NYY8; 32.
DR MINT; Q9NYY8; -.
DR STRING; 9606.ENSP00000236980; -.
DR iPTMnet; Q9NYY8; -.
DR MetOSite; Q9NYY8; -.
DR PhosphoSitePlus; Q9NYY8; -.
DR BioMuta; FASTKD2; -.
DR DMDM; 74734717; -.
DR EPD; Q9NYY8; -.
DR jPOST; Q9NYY8; -.
DR MassIVE; Q9NYY8; -.
DR MaxQB; Q9NYY8; -.
DR PaxDb; Q9NYY8; -.
DR PeptideAtlas; Q9NYY8; -.
DR PRIDE; Q9NYY8; -.
DR ProteomicsDB; 83300; -. [Q9NYY8-1]
DR ProteomicsDB; 83301; -. [Q9NYY8-2]
DR Antibodypedia; 34183; 239 antibodies from 25 providers.
DR DNASU; 22868; -.
DR Ensembl; ENST00000236980.10; ENSP00000236980.6; ENSG00000118246.14. [Q9NYY8-1]
DR Ensembl; ENST00000402774.8; ENSP00000385990.3; ENSG00000118246.14. [Q9NYY8-1]
DR Ensembl; ENST00000403094.3; ENSP00000384929.3; ENSG00000118246.14. [Q9NYY8-1]
DR GeneID; 22868; -.
DR KEGG; hsa:22868; -.
DR MANE-Select; ENST00000402774.8; ENSP00000385990.3; NM_001136193.2; NP_001129665.1.
DR UCSC; uc002vbu.4; human. [Q9NYY8-1]
DR CTD; 22868; -.
DR DisGeNET; 22868; -.
DR GeneCards; FASTKD2; -.
DR HGNC; HGNC:29160; FASTKD2.
DR HPA; ENSG00000118246; Low tissue specificity.
DR MalaCards; FASTKD2; -.
DR MIM; 612322; gene.
DR MIM; 618855; phenotype.
DR neXtProt; NX_Q9NYY8; -.
DR OpenTargets; ENSG00000118246; -.
DR Orphanet; 166105; FASTKD2-related infantile mitochondrial encephalomyopathy.
DR PharmGKB; PA134974924; -.
DR VEuPathDB; HostDB:ENSG00000118246; -.
DR eggNOG; ENOG502QVSD; Eukaryota.
DR GeneTree; ENSGT01030000234607; -.
DR HOGENOM; CLU_025270_0_0_1; -.
DR InParanoid; Q9NYY8; -.
DR OMA; FDIWKLK; -.
DR PhylomeDB; Q9NYY8; -.
DR TreeFam; TF352875; -.
DR PathwayCommons; Q9NYY8; -.
DR SignaLink; Q9NYY8; -.
DR SIGNOR; Q9NYY8; -.
DR BioGRID-ORCS; 22868; 18 hits in 1082 CRISPR screens.
DR ChiTaRS; FASTKD2; human.
DR GenomeRNAi; 22868; -.
DR Pharos; Q9NYY8; Tbio.
DR PRO; PR:Q9NYY8; -.
DR Proteomes; UP000005640; Chromosome 2.
DR RNAct; Q9NYY8; protein.
DR Bgee; ENSG00000118246; Expressed in adrenal tissue and 187 other tissues.
DR ExpressionAtlas; Q9NYY8; baseline and differential.
DR Genevisible; Q9NYY8; HS.
DR GO; GO:0005759; C:mitochondrial matrix; IBA:GO_Central.
DR GO; GO:0042645; C:mitochondrial nucleoid; IDA:UniProtKB.
DR GO; GO:0005739; C:mitochondrion; IDA:UniProtKB.
DR GO; GO:0035770; C:ribonucleoprotein granule; IDA:UniProtKB.
DR GO; GO:0003723; F:RNA binding; HDA:UniProtKB.
DR GO; GO:0019843; F:rRNA binding; IDA:UniProtKB.
DR GO; GO:0006915; P:apoptotic process; IMP:UniProtKB.
DR GO; GO:1902775; P:mitochondrial large ribosomal subunit assembly; IMP:UniProtKB.
DR GO; GO:0000963; P:mitochondrial RNA processing; IBA:GO_Central.
DR GO; GO:0032543; P:mitochondrial translation; IDA:UniProtKB.
DR GO; GO:0070131; P:positive regulation of mitochondrial translation; IMP:UniProtKB.
DR GO; GO:0044528; P:regulation of mitochondrial mRNA stability; IBA:GO_Central.
DR GO; GO:0006396; P:RNA processing; IDA:UniProtKB.
DR InterPro; IPR013579; FAST_2.
DR InterPro; IPR010622; FAST_Leu-rich.
DR InterPro; IPR013584; RAP.
DR Pfam; PF06743; FAST_1; 1.
DR Pfam; PF08368; FAST_2; 1.
DR Pfam; PF08373; RAP; 1.
DR SMART; SM00952; RAP; 1.
DR PROSITE; PS51286; RAP; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Disease variant; Mitochondrion;
KW Mitochondrion nucleoid; Phosphoprotein; Primary mitochondrial disease;
KW Reference proteome; Ribosome biogenesis; RNA-binding; rRNA-binding;
KW Transit peptide.
FT TRANSIT 1..?
FT /note="Mitochondrion"
FT /evidence="ECO:0000305"
FT CHAIN ?..710
FT /note="FAST kinase domain-containing protein 2,
FT mitochondrial"
FT /id="PRO_0000050783"
FT DOMAIN 634..691
FT /note="RAP"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00619"
FT MOD_RES 126
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 140
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 708
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT VAR_SEQ 634..648
FT /note="VAVLCVSRSAYCLGS -> LLTYISFAGLSELKS (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:10231032"
FT /id="VSP_017186"
FT VAR_SEQ 649..710
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:10231032"
FT /id="VSP_017187"
FT VARIANT 15
FT /note="S -> N (in dbSNP:rs3762568)"
FT /id="VAR_053889"
FT VARIANT 205..710
FT /note="Missing (in COXPD44)"
FT /evidence="ECO:0000269|PubMed:28499982"
FT /id="VAR_084340"
FT VARIANT 255
FT /note="L -> P (in COXPD44; unknown pathological
FT significance)"
FT /evidence="ECO:0000269|PubMed:28499982"
FT /id="VAR_084341"
FT VARIANT 290..710
FT /note="Missing (in COXPD44; decreased mitochondrial large
FT ribosomal subunit assembly)"
FT /evidence="ECO:0000269|PubMed:31944455"
FT /id="VAR_084342"
FT VARIANT 432..710
FT /note="Missing (in COXPD44)"
FT /evidence="ECO:0000269|PubMed:18771761"
FT /id="VAR_084343"
FT VARIANT 445
FT /note="V -> E (in dbSNP:rs13003768)"
FT /id="VAR_053890"
SQ SEQUENCE 710 AA; 81463 MW; 11BF1D5A0CF1DA15 CRC64;
MLTTLKPFGS VSVESKMNNK AGSFFWNLRQ FSTLVSTSRT MRLCCLGLCK PKIVHSNWNI
LNNFHNRMQS TDIIRYLFQD AFIFKSDVGF QTKGISTLTA LRIERLLYAK RLFFDSKQSL
VPVDKSDDEL KKVNLNHEVS NEDVLTKETK PNRISSRKLS EECNSLSDVL DAFSKAPTFP
SSNYFTAMWT IAKRLSDDQK RFEKRLMFSH PAFNQLCEHM MREAKIMQYK YLLFSLHAIV
KLGIPQNTIL VQTLLRVTQE RINECDEICL SVLSTVLEAM EPCKNVHVLR TGFRILVDQQ
VWKIEDVFTL QVVMKCIGKD APIALKRKLE MKALRELDRF SVLNSQHMFE VLAAMNHRSL
ILLDECSKVV LDNIHGCPLR IMINILQSCK DLQYHNLDLF KGLADYVAAT FDIWKFRKVL
FILILFENLG FRPVGLMDLF MKRIVEDPES LNMKNILSIL HTYSSLNHVY KCQNKEQFVE
VMASALTGYL HTISSENLLD AVYSFCLMNY FPLAPFNQLL QKDIISELLT SDDMKNAYKL
HTLDTCLKLD DTVYLRDIAL SLPQLPRELP SSHTNAKVAE VLSSLLGGEG HFSKDVHLPH
NYHIDFEIRM DTNRNQVLPL SDVDTTSATD IQRVAVLCVS RSAYCLGSSH PRGFLAMKMR
HLNAMGFHVI LVNNWEMDKL EMEDAVTFLK TKIYSVEALP VAAVNVQSTQ
