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 27-MAR-2024, entry version 169. DE RecName: Full=FAST kinase domain-containing protein 2, mitochondrial; DE Flags: Precursor; GN Name=FASTKD2 {ECO:0000303|PubMed:27667664, GN ECO:0000312|HGNC:HGNC:29160}; 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; P13569: CFTR; NbExp=5; IntAct=EBI-1055752, EBI-349854; 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}; 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; 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 SMR; Q9NYY8; -. DR BioGRID; 116535; 287. DR CORUM; Q9NYY8; -. DR IntAct; Q9NYY8; 35. DR MINT; Q9NYY8; -. DR STRING; 9606.ENSP00000385990; -. DR iPTMnet; Q9NYY8; -. DR MetOSite; Q9NYY8; -. DR PhosphoSitePlus; Q9NYY8; -. DR SwissPalm; Q9NYY8; -. DR BioMuta; FASTKD2; -. DR DMDM; 74734717; -. DR EPD; Q9NYY8; -. DR jPOST; Q9NYY8; -. DR MassIVE; Q9NYY8; -. DR MaxQB; Q9NYY8; -. DR PaxDb; 9606-ENSP00000236980; -. DR PeptideAtlas; Q9NYY8; -. DR ProteomicsDB; 83300; -. [Q9NYY8-1] DR ProteomicsDB; 83301; -. [Q9NYY8-2] DR Pumba; Q9NYY8; -. DR Antibodypedia; 34183; 260 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 AGR; HGNC:29160; -. 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; FEIRMDS; -. DR OrthoDB; 5257459at2759; -. DR PhylomeDB; Q9NYY8; -. DR TreeFam; TF352875; -. DR PathwayCommons; Q9NYY8; -. DR Reactome; R-HSA-9837092; FASTK family proteins regulate processing and stability of mitochondrial RNAs. DR SignaLink; Q9NYY8; -. DR SIGNOR; Q9NYY8; -. DR BioGRID-ORCS; 22868; 20 hits in 1162 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 188 other cell types or tissues. DR ExpressionAtlas; Q9NYY8; baseline and differential. 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:HPA. 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 PANTHER; PTHR21228:SF1; FAST KINASE DOMAIN-CONTAINING PROTEIN 2, MITOCHONDRIAL; 1. DR PANTHER; PTHR21228; FAST LEU-RICH DOMAIN-CONTAINING; 1. 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. DR Genevisible; Q9NYY8; HS. 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; uncertain 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 //