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FAST kinase domain-containing protein 5, mitochondrial

 FAKD5_HUMAN             Reviewed;         764 AA.
Q7L8L6; Q96JN3; Q9H5D1; Q9H8Y3;
01-MAY-2007, integrated into UniProtKB/Swiss-Prot.
05-JUL-2004, sequence version 1.
27-SEP-2017, entry version 116.
RecName: Full=FAST kinase domain-containing protein 5, mitochondrial;
Flags: Precursor;
Name=FASTKD5; Synonyms=KIAA1792;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Brain;
PubMed=11347906; DOI=10.1093/dnares/8.2.85;
Nagase T., Nakayama M., Nakajima D., Kikuno R., Ohara O.;
"Prediction of the coding sequences of unidentified human genes. XX.
The complete sequences of 100 new cDNA clones from brain which code
for large proteins in vitro.";
DNA Res. 8:85-95(2001).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Lung;
PubMed=14702039; DOI=10.1038/ng1285;
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=11780052; DOI=10.1038/414865a;
Deloukas P., Matthews L.H., Ashurst J.L., Burton J., Gilbert J.G.R.,
Jones M., Stavrides G., Almeida J.P., Babbage A.K., Bagguley C.L.,
Bailey J., Barlow K.F., Bates K.N., Beard L.M., Beare D.M.,
Beasley O.P., Bird C.P., Blakey S.E., Bridgeman A.M., Brown A.J.,
Buck D., Burrill W.D., Butler A.P., Carder C., Carter N.P.,
Chapman J.C., Clamp M., Clark G., Clark L.N., Clark S.Y., Clee C.M.,
Clegg S., Cobley V.E., Collier R.E., Connor R.E., Corby N.R.,
Coulson A., Coville G.J., Deadman R., Dhami P.D., Dunn M.,
Ellington A.G., Frankland J.A., Fraser A., French L., Garner P.,
Grafham D.V., Griffiths C., Griffiths M.N.D., Gwilliam R., Hall R.E.,
Hammond S., Harley J.L., Heath P.D., Ho S., Holden J.L., Howden P.J.,
Huckle E., Hunt A.R., Hunt S.E., Jekosch K., Johnson C.M., Johnson D.,
Kay M.P., Kimberley A.M., King A., Knights A., Laird G.K., Lawlor S.,
Lehvaeslaiho M.H., Leversha M.A., Lloyd C., Lloyd D.M., Lovell J.D.,
Marsh V.L., Martin S.L., McConnachie L.J., McLay K., McMurray A.A.,
Milne S.A., Mistry D., Moore M.J.F., Mullikin J.C., Nickerson T.,
Oliver K., Parker A., Patel R., Pearce T.A.V., Peck A.I.,
Phillimore B.J.C.T., Prathalingam S.R., Plumb R.W., Ramsay H.,
Rice C.M., Ross M.T., Scott C.E., Sehra H.K., Shownkeen R., Sims S.,
Skuce C.D., Smith M.L., Soderlund C., Steward C.A., Sulston J.E.,
Swann R.M., Sycamore N., Taylor R., Tee L., Thomas D.W., Thorpe A.,
Tracey A., Tromans A.C., Vaudin M., Wall M., Wallis J.M.,
Whitehead S.L., Whittaker P., Willey D.L., Williams L., Williams S.A.,
Wilming L., Wray P.W., Hubbard T., Durbin R.M., Bentley D.R., Beck S.,
Rogers J.;
"The DNA sequence and comparative analysis of human chromosome 20.";
Nature 414:865-871(2001).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Muscle, and Skin;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[5]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-95, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=16964243; DOI=10.1038/nbt1240;
Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.;
"A probability-based approach for high-throughput protein
phosphorylation analysis and site localization.";
Nat. Biotechnol. 24:1285-1292(2006).
[6]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-95, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007;
Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,
Greff Z., Keri G., Stemmann O., Mann M.;
"Kinase-selective enrichment enables quantitative phosphoproteomics of
the kinome across the cell cycle.";
Mol. Cell 31:438-448(2008).
[7]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-95, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18669648; DOI=10.1073/pnas.0805139105;
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
Elledge S.J., Gygi S.P.;
"A quantitative atlas of mitotic phosphorylation.";
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
[8]
ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-507, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19608861; DOI=10.1126/science.1175371;
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M.,
Walther T.C., Olsen J.V., Mann M.;
"Lysine acetylation targets protein complexes and co-regulates major
cellular functions.";
Science 325:834-840(2009).
[9]
SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
PubMed=20869947; DOI=10.1016/j.bbrc.2010.09.075;
Simarro M., Gimenez-Cassina A., Kedersha N., Lazaro J.B.,
Adelmant G.O., Marto J.A., Rhee K., Tisdale S., Danial N.,
Benarafa C., Orduna A., Anderson P.;
"Fast kinase domain-containing protein 3 is a mitochondrial protein
essential for cellular respiration.";
Biochem. Biophys. Res. Commun. 401:440-446(2010).
[10]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21269460; DOI=10.1186/1752-0509-5-17;
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
"Initial characterization of the human central proteome.";
BMC Syst. Biol. 5:17-17(2011).
[11]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-95, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma, and Erythroleukemia;
PubMed=23186163; DOI=10.1021/pr300630k;
Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
Mohammed S.;
"Toward a comprehensive characterization of a human cancer cell
phosphoproteome.";
J. Proteome Res. 12:260-271(2013).
[12]
FUNCTION, IDENTIFICATION IN A COMPLEX WITH GRSF1; DDX28; DHX30 AND
FASTKD2, SUBCELLULAR LOCATION, RNA-BINDING, AND IDENTIFICATION BY MASS
SPECTROMETRY.
PubMed=25683715; DOI=10.1016/j.celrep.2015.01.030;
Antonicka H., Shoubridge E.A.;
"Mitochondrial RNA granules are centers for posttranscriptional RNA
processing and ribosome biogenesis.";
Cell Rep. 0:0-0(2015).
[13]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=25944712; DOI=10.1002/pmic.201400617;
Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M.,
Ayoub D., Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
"N-terminome analysis of the human mitochondrial proteome.";
Proteomics 15:2519-2524(2015).
-!- FUNCTION: Plays an important role in the processing of non-
canonical mitochondrial mRNA precursors (PubMed:25683715).
{ECO:0000269|PubMed:25683715}.
-!- SUBUNIT: Found in a complex with GRSF1, DDX28, DHX30 and FASTKD2.
Associates with the 12S mitochondrial rRNA (12S mt-rRNA).
{ECO:0000269|PubMed:25683715}.
-!- INTERACTION:
O95259:KCNH1; NbExp=3; IntAct=EBI-747570, EBI-2909270;
-!- SUBCELLULAR LOCATION: Mitochondrion matrix, mitochondrion nucleoid
{ECO:0000269|PubMed:20869947, ECO:0000269|PubMed:25683715}.
Note=Localizes to mitochondrial RNA granules found in close
proximity to the mitochondrial nucleoids.
{ECO:0000269|PubMed:25683715}.
-!- TISSUE SPECIFICITY: Expression detected in spleen, thymus, testis,
ovary, colon, heart, smooth muscle, kidney, brain, lung, liver and
white adipose tissue with highest expression in heart, smooth
muscle, liver and thyroid. {ECO:0000269|PubMed:20869947}.
-!- SIMILARITY: Belongs to the FAST kinase family. {ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=BAB15696.1; Type=Frameshift; Positions=662; Evidence={ECO:0000305};
Sequence=BAB47421.1; Type=Erroneous initiation; Note=Translation N-terminally shortened.; Evidence={ECO:0000305};
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EMBL; AB058695; BAB47421.1; ALT_INIT; mRNA.
EMBL; AK023211; BAB14464.1; -; mRNA.
EMBL; AK027215; BAB15696.1; ALT_FRAME; mRNA.
EMBL; AL121891; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; BC011856; AAH11856.1; -; mRNA.
EMBL; BC007413; AAH07413.1; -; mRNA.
CCDS; CCDS13048.1; -.
RefSeq; NP_068598.1; NM_021826.4.
UniGene; Hs.741168; -.
ProteinModelPortal; Q7L8L6; -.
BioGrid; 121924; 22.
CORUM; Q7L8L6; -.
IntAct; Q7L8L6; 18.
MINT; MINT-1441258; -.
STRING; 9606.ENSP00000369618; -.
iPTMnet; Q7L8L6; -.
PhosphoSitePlus; Q7L8L6; -.
BioMuta; FASTKD5; -.
DMDM; 74749905; -.
EPD; Q7L8L6; -.
MaxQB; Q7L8L6; -.
PaxDb; Q7L8L6; -.
PeptideAtlas; Q7L8L6; -.
PRIDE; Q7L8L6; -.
DNASU; 60493; -.
Ensembl; ENST00000380266; ENSP00000369618; ENSG00000215251.
GeneID; 60493; -.
KEGG; hsa:60493; -.
UCSC; uc002whz.5; human.
CTD; 60493; -.
DisGeNET; 60493; -.
EuPathDB; HostDB:ENSG00000215251.3; -.
GeneCards; FASTKD5; -.
HGNC; HGNC:25790; FASTKD5.
HPA; HPA043833; -.
neXtProt; NX_Q7L8L6; -.
OpenTargets; ENSG00000215251; -.
PharmGKB; PA145148886; -.
eggNOG; ENOG410IF51; Eukaryota.
eggNOG; ENOG4111F08; LUCA.
GeneTree; ENSGT00510000049012; -.
HOGENOM; HOG000112492; -.
HOVERGEN; HBG103634; -.
InParanoid; Q7L8L6; -.
OMA; IKHHMIL; -.
OrthoDB; EOG091G0BFG; -.
PhylomeDB; Q7L8L6; -.
TreeFam; TF352874; -.
GenomeRNAi; 60493; -.
PRO; PR:Q7L8L6; -.
Proteomes; UP000005640; Chromosome 20.
Bgee; ENSG00000215251; -.
Genevisible; Q7L8L6; HS.
GO; GO:0042645; C:mitochondrial nucleoid; IDA:UniProtKB.
GO; GO:0005739; C:mitochondrion; IDA:UniProtKB.
GO; GO:0035770; C:ribonucleoprotein granule; IDA:UniProtKB.
GO; GO:0004672; F:protein kinase activity; IEA:InterPro.
GO; GO:0003723; F:RNA binding; IDA:UniProtKB.
GO; GO:0019843; F:rRNA binding; IDA:UniProtKB.
GO; GO:0045333; P:cellular respiration; ISS:UniProtKB.
GO; GO:0000963; P:mitochondrial RNA processing; IMP:UniProtKB.
GO; GO:0006397; P:mRNA processing; IEA:UniProtKB-KW.
InterPro; IPR013579; FAST_2.
InterPro; IPR010622; FAST_Leu-rich.
InterPro; IPR013584; RAP.
Pfam; PF06743; FAST_1; 1.
Pfam; PF08368; FAST_2; 1.
Pfam; PF08373; RAP; 1.
SMART; SM00952; RAP; 1.
PROSITE; PS51286; RAP; 1.
1: Evidence at protein level;
Acetylation; Complete proteome; Mitochondrion; Mitochondrion nucleoid;
mRNA processing; Phosphoprotein; Polymorphism; Reference proteome;
RNA-binding; rRNA-binding; Transit peptide.
TRANSIT 1 27 Mitochondrion. {ECO:0000255}.
CHAIN 28 764 FAST kinase domain-containing protein 5,
mitochondrial.
/FTId=PRO_0000284979.
DOMAIN 697 757 RAP. {ECO:0000255|PROSITE-
ProRule:PRU00619}.
MOD_RES 95 95 Phosphoserine.
{ECO:0000244|PubMed:16964243,
ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:18691976,
ECO:0000244|PubMed:23186163}.
MOD_RES 507 507 N6-acetyllysine.
{ECO:0000244|PubMed:19608861}.
VARIANT 256 256 R -> C (in dbSNP:rs3746700).
/FTId=VAR_053891.
VARIANT 288 288 I -> T (in dbSNP:rs2422857).
/FTId=VAR_053892.
VARIANT 377 377 I -> V (in dbSNP:rs3746699).
/FTId=VAR_053893.
SEQUENCE 764 AA; 86574 MW; 1064229F9B212405 CRC64;
MAATLKSLKL VRYRAFCSPS AFGAVRSVSY WNVSSTQHGG QDPPEHISLC HSAKKVKNIC
STFSSRRILT TSSAHPGLEF SKTSSSKAST LQLGSPRATG VDEEDVEVFD SFENMRVFLQ
LRPEYRVHSY NASETSQLLS VSEGELILHK VRVNQNNLQA QVIVDYLCKL SSLPAEQHPV
LLGSTSFALL CQLSVKKIQL FDTQDLINVL KAFVILGIPH SHSMLDVYET KCCHQVWEMN
MDQLLLVADL WRYLGRKVPR FLNIFSSYLN LHWKDLSLSQ LVHLIYVIGE NRQVSQDLMQ
KLESLILKYI DLINLEEVGT ICLGFFKSST NLSEFVMRKI GDLACANIQH LSSRSLVNIV
KMFRFTHVDH INFMKQIGEI APQRIPSLGV QGVMHLTLYC SALRFLNEGV MNAVAASLPP
RVAHCRSKDV AKILWSFGTL NYKPPNAEEF YSSLISEIHR KMPEFNQYPE HLPTCLLGLA
FLEYFPVELI DFALSPGFVR LAQERTKFDL LKELYTLDGT VGIECPDYRG NRLSTHLQQE
GSELLWYLAE KDMNSKPEFL ETVFLLETML GGPQYVKHHM ILPHTRSSDL EVQLDVNLKP
LPFNREATPA ENVAKLRLEH VGVSLTDDLM NKLLKGKARG HFQGKTESEP GQQPMELENK
AAVPLGGFLC NVADKSGAME MAGLCPAACM QTPRMKLAVQ FTNRNQYCYG SRDLLGLHNM
KRRQLARLGY RVVELSYWEW LPLLKRTRLE KLAFLHEKVF TSAL


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