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Phenylalanine--tRNA ligase, mitochondrial (EC 6.1.1.20) (Phenylalanyl-tRNA synthetase) (PheRS)

 SYFM_HUMAN              Reviewed;         451 AA.
O95363; B2R664; Q53F66; Q5TCS3; Q6FG29; Q9NPY7; Q9P062;
23-NOV-2004, integrated into UniProtKB/Swiss-Prot.
01-MAY-1999, sequence version 1.
30-AUG-2017, entry version 158.
RecName: Full=Phenylalanine--tRNA ligase, mitochondrial;
EC=6.1.1.20 {ECO:0000269|PubMed:19549855, ECO:0000269|PubMed:22833457};
AltName: Full=Phenylalanyl-tRNA synthetase;
Short=PheRS;
Flags: Precursor;
Name=FARS2; Synonyms=FARS1; ORFNames=HSPC320;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA], AND SUBUNIT.
PubMed=10329163; DOI=10.1006/jmbi.1999.2708;
Bullard J.M., Cai Y.-C., Demeler B., Spremulli L.L.;
"Expression and characterization of a human mitochondrial
phenylalanyl-tRNA synthetase.";
J. Mol. Biol. 288:567-577(1999).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT SER-280.
TISSUE=Caudate nucleus;
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 MRNA], AND VARIANT SER-280.
Halleck A., Ebert L., Mkoundinya M., Schick M., Eisenstein S.,
Neubert P., Kstrang K., Schatten R., Shen B., Henze S., Mar W.,
Korn B., Zuo D., Hu Y., LaBaer J.;
"Cloning of human full open reading frames in Gateway(TM) system entry
vector (pDONR201).";
Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Kidney epithelium;
Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S.;
Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases.
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=14574404; DOI=10.1038/nature02055;
Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L.,
Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E.,
Gilbert J.G.R., Clamp M.E., Bethel G., Milne S., Ainscough R.,
Almeida J.P., Ambrose K.D., Andrews T.D., Ashwell R.I.S.,
Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Barker D.J.,
Barlow K.F., Bates K., Beare D.M., Beasley H., Beasley O., Bird C.P.,
Blakey S.E., Bray-Allen S., Brook J., Brown A.J., Brown J.Y.,
Burford D.C., Burrill W., Burton J., Carder C., Carter N.P.,
Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V.,
Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J.,
Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E.,
Ellington A.E., Evans K.A., Faulkner L., Francis M.D., Frankish A.,
Frankland J., French L., Garner P., Garnett J., Ghori M.J.,
Gilby L.M., Gillson C.J., Glithero R.J., Grafham D.V., Grant M.,
Gribble S., Griffiths C., Griffiths M.N.D., Hall R., Halls K.S.,
Hammond S., Harley J.L., Hart E.A., Heath P.D., Heathcott R.,
Holmes S.J., Howden P.J., Howe K.L., Howell G.R., Huckle E.,
Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., Joy A.A.,
Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., Langford C.,
Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., Lloyd D.M.,
Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M.,
Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K.,
McMurray A., Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T.,
Novik K.L., Oliver K., Overton-Larty E.K., Parker A., Patel R.,
Pearce A.V., Peck A.I., Phillimore B.J.C.T., Phillips S., Plumb R.W.,
Porter K.M., Ramsey Y., Ranby S.A., Rice C.M., Ross M.T., Searle S.M.,
Sehra H.K., Sheridan E., Skuce C.D., Smith S., Smith M., Spraggon L.,
Squares S.L., Steward C.A., Sycamore N., Tamlyn-Hall G., Tester J.,
Theaker A.J., Thomas D.W., Thorpe A., Tracey A., Tromans A., Tubby B.,
Wall M., Wallis J.M., West A.P., White S.S., Whitehead S.L.,
Whittaker H., Wild A., Willey D.J., Wilmer T.E., Wood J.M., Wray P.W.,
Wyatt J.C., Young L., Younger R.M., Bentley D.R., Coulson A.,
Durbin R.M., Hubbard T., Sulston J.E., Dunham I., Rogers J., Beck S.;
"The DNA sequence and analysis of human chromosome 6.";
Nature 425:805-811(2003).
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Pancreas;
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).
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 108-451, AND VARIANT
SER-280.
TISSUE=Umbilical cord blood;
Ye M., Zhang Q.-H., Zhou J., Shen Y., Wu X.-Y., Guan Z.Q., Wang L.,
Fan H.-Y., Mao Y.-F., Dai M., Huang Q.-H., Chen S.-J., Chen Z.;
"Human partial CDS from CD34+ stem cells.";
Submitted (MAY-1999) to the EMBL/GenBank/DDBJ databases.
[8]
ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-202, 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]
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).
[10]
X-RAY CRYSTALLOGRAPHY (2.20 ANGSTROMS) OF 38-451 IN COMPLEX WITH
SUBSTRATE, AND SUBUNIT.
PubMed=18611382; DOI=10.1016/j.str.2008.03.020;
Klipcan L., Levin I., Kessler N., Moor N., Finarov I., Safro M.;
"The tRNA-induced conformational activation of human mitochondrial
phenylalanyl-tRNA synthetase.";
Structure 16:1095-1104(2008).
[11]
X-RAY CRYSTALLOGRAPHY (2.60 ANGSTROMS) OF 38-451 IN COMPLEX WITH
SUBSTRATE, FUNCTION, CATALYTIC ACTIVITY, SUBSTRATE SPECIFICITY, AND
KINETIC PARAMETERS.
PubMed=19549855; DOI=10.1073/pnas.0905212106;
Klipcan L., Moor N., Kessler N., Safro M.G.;
"Eukaryotic cytosolic and mitochondrial phenylalanyl-tRNA synthetases
catalyze the charging of tRNA with the meta-tyrosine.";
Proc. Natl. Acad. Sci. U.S.A. 106:11045-11048(2009).
[12]
VARIANTS COXPD14 THR-329 AND VAL-391, CHARACTERIZATION OF VARIANTS
COXPD14 CYS-144; THR-329 AND VAL-391, FUNCTION, CATALYTIC ACTIVITY,
AND KINETIC PARAMETERS.
PubMed=22833457; DOI=10.1093/hmg/dds294;
Elo J.M., Yadavalli S.S., Euro L., Isohanni P., Gotz A., Carroll C.J.,
Valanne L., Alkuraya F.S., Uusimaa J., Paetau A., Caruso E.M.,
Pihko H., Ibba M., Tyynismaa H., Suomalainen A.;
"Mitochondrial phenylalanyl-tRNA synthetase mutations underlie fatal
infantile Alpers encephalopathy.";
Hum. Mol. Genet. 21:4521-4529(2012).
[13]
VARIANT COXPD14 CYS-144.
PubMed=22499341; DOI=10.1136/jmedgenet-2012-100836;
Shamseldin H.E., Alshammari M., Al-Sheddi T., Salih M.A.,
Alkhalidi H., Kentab A., Repetto G.M., Hashem M., Alkuraya F.S.;
"Genomic analysis of mitochondrial diseases in a consanguineous
population reveals novel candidate disease genes.";
J. Med. Genet. 49:234-241(2012).
[14]
VARIANT SPG77 TYR-142, AND CHARACTERIZATION OF VARIANT SPG77 TYR-142.
PubMed=26553276; DOI=10.1002/humu.22930;
Yang Y., Liu W., Fang Z., Shi J., Che F., He C., Yao L., Wang E.,
Wu Y.;
"A newly identified missense mutation in FARS2 causes autosomal-
recessive spastic paraplegia.";
Hum. Mutat. 37:165-169(2016).
-!- FUNCTION: Is responsible for the charging of tRNA(Phe) with
phenylalanine in mitochondrial translation. To a lesser extent,
also catalyzes direct attachment of m-Tyr (an oxidized version of
Phe) to tRNA(Phe), thereby opening the way for delivery of the
misacylated tRNA to the ribosome and incorporation of ROS-damaged
amino acid into proteins. {ECO:0000269|PubMed:19549855,
ECO:0000269|PubMed:22833457}.
-!- CATALYTIC ACTIVITY: ATP + L-phenylalanine + tRNA(Phe) = AMP +
diphosphate + L-phenylalanyl-tRNA(Phe).
{ECO:0000269|PubMed:19549855, ECO:0000269|PubMed:22833457}.
-!- BIOPHYSICOCHEMICAL PROPERTIES:
Kinetic parameters:
KM=2.2 uM for L-phenylalanine {ECO:0000269|PubMed:19549855,
ECO:0000269|PubMed:22833457};
KM=1900 uM for L-tyrosine {ECO:0000269|PubMed:19549855,
ECO:0000269|PubMed:22833457};
KM=11.7 uM for DL-m-tyrosine {ECO:0000269|PubMed:19549855,
ECO:0000269|PubMed:22833457};
KM=7.3 uM for L-phenylalanine {ECO:0000269|PubMed:19549855,
ECO:0000269|PubMed:22833457};
KM=2.9 mM for ATP {ECO:0000269|PubMed:19549855,
ECO:0000269|PubMed:22833457};
KM=1.2 uM for tRNA(Phe) {ECO:0000269|PubMed:19549855,
ECO:0000269|PubMed:22833457};
Note=kcat is 2.8 min(-1), 2.0 min(-1) and 3.1 min(-1) with L-
phenylalanine, L-tyrosine and m-tyrosine as substrate,
respectively. Thus, the catalytic efficiency of the m-Tyr
attachment is only 5-fold lower than that of the correct amino
acid, while that of Tyr attachment is 1000-fold lower
(PubMed:19549855). {ECO:0000269|PubMed:19549855};
-!- SUBUNIT: Monomer. {ECO:0000269|PubMed:10329163,
ECO:0000269|PubMed:18611382, ECO:0000269|PubMed:19549855}.
-!- INTERACTION:
Q6UY14-3:ADAMTSL4; NbExp=3; IntAct=EBI-2513774, EBI-10173507;
Q6RW13:AGTRAP; NbExp=3; IntAct=EBI-2513774, EBI-741181;
Q9UKG1:APPL1; NbExp=7; IntAct=EBI-2513774, EBI-741243;
O95429:BAG4; NbExp=4; IntAct=EBI-2513774, EBI-2949658;
Q13137:CALCOCO2; NbExp=5; IntAct=EBI-2513774, EBI-739580;
Q96DZ9:CMTM5; NbExp=3; IntAct=EBI-2513774, EBI-2548702;
Q6NT76:HMBOX1; NbExp=3; IntAct=EBI-2513774, EBI-2549423;
Q9UKT9:IKZF3; NbExp=5; IntAct=EBI-2513774, EBI-747204;
Q9H3M0:KCNF1; NbExp=4; IntAct=EBI-2513774, EBI-6918743;
A1A4E9:KRT13; NbExp=3; IntAct=EBI-2513774, EBI-10171552;
Q15323:KRT31; NbExp=3; IntAct=EBI-2513774, EBI-948001;
Q6A162:KRT40; NbExp=5; IntAct=EBI-2513774, EBI-10171697;
P60370:KRTAP10-5; NbExp=3; IntAct=EBI-2513774, EBI-10172150;
P60409:KRTAP10-7; NbExp=3; IntAct=EBI-2513774, EBI-10172290;
P60411:KRTAP10-9; NbExp=5; IntAct=EBI-2513774, EBI-10172052;
Q9BYR6:KRTAP3-3; NbExp=4; IntAct=EBI-2513774, EBI-3957694;
Q9UJV3-2:MID2; NbExp=5; IntAct=EBI-2513774, EBI-10172526;
Q13064:MKRN3; NbExp=3; IntAct=EBI-2513774, EBI-2340269;
Q7Z3S9:NOTCH2NL; NbExp=3; IntAct=EBI-2513774, EBI-945833;
O95199:RCBTB2; NbExp=7; IntAct=EBI-2513774, EBI-742404;
O75558:STX11; NbExp=3; IntAct=EBI-2513774, EBI-714135;
O75478:TADA2A; NbExp=3; IntAct=EBI-2513774, EBI-742268;
Q12800:TFCP2; NbExp=3; IntAct=EBI-2513774, EBI-717422;
P14373:TRIM27; NbExp=3; IntAct=EBI-2513774, EBI-719493;
Q9BYV2:TRIM54; NbExp=3; IntAct=EBI-2513774, EBI-2130429;
-!- SUBCELLULAR LOCATION: Mitochondrion matrix
{ECO:0000250|UniProtKB:Q6AYQ3}. Mitochondrion
{ECO:0000250|UniProtKB:Q6AYQ3}.
-!- DISEASE: Combined oxidative phosphorylation deficiency 14
(COXPD14) [MIM:614946]: A severe multisystemic autosomal recessive
disorder characterized by neonatal onset of global developmental
delay, refractory seizures, and lactic acidosis. Biochemical
studies show deficiencies of multiple mitochondrial respiratory
enzymes. {ECO:0000269|PubMed:22499341,
ECO:0000269|PubMed:22833457}. Note=The disease is caused by
mutations affecting the gene represented in this entry.
-!- DISEASE: Spastic paraplegia 77, autosomal recessive (SPG77)
[MIM:617046]: A form of spastic paraplegia, a neurodegenerative
disorder characterized by a slow, gradual, progressive weakness
and spasticity of the lower limbs. Rate of progression and the
severity of symptoms are quite variable. Initial symptoms may
include difficulty with balance, weakness and stiffness in the
legs, muscle spasms, and dragging the toes when walking. In some
forms of the disorder, bladder symptoms (such as incontinence) may
appear, or the weakness and stiffness may spread to other parts of
the body. {ECO:0000269|PubMed:26553276}. Note=The disease is
caused by mutations affecting the gene represented in this entry.
-!- SIMILARITY: Belongs to the class-II aminoacyl-tRNA synthetase
family. {ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=AAF28998.1; Type=Frameshift; Positions=414; Evidence={ECO:0000305};
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EMBL; AF097441; AAC83802.1; -; mRNA.
EMBL; AK312454; BAG35361.1; -; mRNA.
EMBL; CR542279; CAG47075.1; -; mRNA.
EMBL; AK223423; BAD97143.1; -; mRNA.
EMBL; AL133473; CAI19901.1; -; Genomic_DNA.
EMBL; AL022097; CAI19901.1; JOINED; Genomic_DNA.
EMBL; AL590868; CAI19901.1; JOINED; Genomic_DNA.
EMBL; AL121978; CAI19901.1; JOINED; Genomic_DNA.
EMBL; AL392184; CAI19901.1; JOINED; Genomic_DNA.
EMBL; AL022097; CAI19950.1; -; Genomic_DNA.
EMBL; AL121978; CAI19950.1; JOINED; Genomic_DNA.
EMBL; AL392184; CAI19950.1; JOINED; Genomic_DNA.
EMBL; AL590868; CAI19950.1; JOINED; Genomic_DNA.
EMBL; AL133473; CAI19950.1; JOINED; Genomic_DNA.
EMBL; AL392184; CAI20375.1; -; Genomic_DNA.
EMBL; AL121978; CAI20375.1; JOINED; Genomic_DNA.
EMBL; AL590868; CAI20375.1; JOINED; Genomic_DNA.
EMBL; AL133473; CAI20375.1; JOINED; Genomic_DNA.
EMBL; AL022097; CAI20375.1; JOINED; Genomic_DNA.
EMBL; AL121978; CAI21657.1; -; Genomic_DNA.
EMBL; AL133473; CAI21657.1; JOINED; Genomic_DNA.
EMBL; AL022097; CAI21657.1; JOINED; Genomic_DNA.
EMBL; AL392184; CAI21657.1; JOINED; Genomic_DNA.
EMBL; AL590868; CAI21657.1; JOINED; Genomic_DNA.
EMBL; AL590868; CAI39442.1; -; Genomic_DNA.
EMBL; AL392184; CAI39442.1; JOINED; Genomic_DNA.
EMBL; AL133473; CAI39442.1; JOINED; Genomic_DNA.
EMBL; AL121978; CAI39442.1; JOINED; Genomic_DNA.
EMBL; AL022097; CAI39442.1; JOINED; Genomic_DNA.
EMBL; BC020239; AAH20239.1; -; mRNA.
EMBL; BC021112; AAH21112.1; -; mRNA.
EMBL; AF161438; AAF28998.1; ALT_FRAME; mRNA.
CCDS; CCDS4494.1; -.
RefSeq; NP_001305801.1; NM_001318872.1.
RefSeq; NP_006558.1; NM_006567.4.
RefSeq; XP_005248869.1; XM_005248812.3.
RefSeq; XP_016865675.1; XM_017010186.1.
RefSeq; XP_016865676.1; XM_017010187.1.
UniGene; Hs.484547; -.
PDB; 3CMQ; X-ray; 2.20 A; A=38-451.
PDB; 3HFV; X-ray; 2.60 A; A=38-451.
PDB; 3TEG; X-ray; 2.20 A; A=38-451.
PDB; 3TUP; X-ray; 3.05 A; A=38-451.
PDB; 5MGH; X-ray; 1.87 A; A=47-451.
PDB; 5MGU; X-ray; 1.89 A; A=46-451.
PDB; 5MGV; X-ray; 2.05 A; A=47-451.
PDB; 5MGW; X-ray; 1.46 A; A=46-451.
PDBsum; 3CMQ; -.
PDBsum; 3HFV; -.
PDBsum; 3TEG; -.
PDBsum; 3TUP; -.
PDBsum; 5MGH; -.
PDBsum; 5MGU; -.
PDBsum; 5MGV; -.
PDBsum; 5MGW; -.
ProteinModelPortal; O95363; -.
SMR; O95363; -.
BioGrid; 115909; 52.
IntAct; O95363; 68.
MINT; MINT-3077661; -.
STRING; 9606.ENSP00000274680; -.
BindingDB; O95363; -.
ChEMBL; CHEMBL2511; -.
DrugBank; DB00120; L-Phenylalanine.
iPTMnet; O95363; -.
PhosphoSitePlus; O95363; -.
BioMuta; FARS2; -.
EPD; O95363; -.
MaxQB; O95363; -.
PaxDb; O95363; -.
PeptideAtlas; O95363; -.
PRIDE; O95363; -.
DNASU; 10667; -.
Ensembl; ENST00000274680; ENSP00000274680; ENSG00000145982.
Ensembl; ENST00000324331; ENSP00000316335; ENSG00000145982.
GeneID; 10667; -.
KEGG; hsa:10667; -.
UCSC; uc003mwr.3; human.
CTD; 10667; -.
DisGeNET; 10667; -.
GeneCards; FARS2; -.
HGNC; HGNC:21062; FARS2.
HPA; HPA018148; -.
HPA; HPA028836; -.
MalaCards; FARS2; -.
MIM; 611592; gene.
MIM; 614946; phenotype.
MIM; 617046; phenotype.
neXtProt; NX_O95363; -.
OpenTargets; ENSG00000145982; -.
Orphanet; 319519; Combined oxidative phosphorylation defect type 14.
PharmGKB; PA134954893; -.
eggNOG; KOG2783; Eukaryota.
eggNOG; COG0016; LUCA.
eggNOG; COG0072; LUCA.
GeneTree; ENSGT00530000063467; -.
HOGENOM; HOG000165163; -.
HOVERGEN; HBG082540; -.
InParanoid; O95363; -.
KO; K01889; -.
OMA; VKLMEHE; -.
OrthoDB; EOG091G07OD; -.
PhylomeDB; O95363; -.
TreeFam; TF105798; -.
BRENDA; 6.1.1.20; 2681.
Reactome; R-HSA-379726; Mitochondrial tRNA aminoacylation.
ChiTaRS; FARS2; human.
EvolutionaryTrace; O95363; -.
GeneWiki; FARS2; -.
GenomeRNAi; 10667; -.
PRO; PR:O95363; -.
Proteomes; UP000005640; Chromosome 6.
Bgee; ENSG00000145982; -.
CleanEx; HS_FARS2; -.
ExpressionAtlas; O95363; baseline and differential.
Genevisible; O95363; HS.
GO; GO:0005759; C:mitochondrial matrix; TAS:Reactome.
GO; GO:0005739; C:mitochondrion; ISS:UniProtKB.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0004826; F:phenylalanine-tRNA ligase activity; IDA:UniProtKB.
GO; GO:0000049; F:tRNA binding; IDA:UniProtKB.
GO; GO:0006432; P:phenylalanyl-tRNA aminoacylation; IDA:UniProtKB.
GO; GO:0006418; P:tRNA aminoacylation for protein translation; TAS:Reactome.
GO; GO:0008033; P:tRNA processing; IDA:UniProtKB.
Gene3D; 3.30.70.380; -; 1.
InterPro; IPR006195; aa-tRNA-synth_II.
InterPro; IPR005121; Fdx_antiC-bd.
InterPro; IPR004530; Phe-tRNA-synth_IIc_mito.
InterPro; IPR002319; Phenylalanyl-tRNA_Synthase.
PANTHER; PTHR11538:SF53; PTHR11538:SF53; 1.
Pfam; PF03147; FDX-ACB; 1.
Pfam; PF01409; tRNA-synt_2d; 2.
SMART; SM00896; FDX-ACB; 1.
SUPFAM; SSF54991; SSF54991; 1.
TIGRFAMs; TIGR00469; pheS_mito; 1.
PROSITE; PS50862; AA_TRNA_LIGASE_II; 1.
PROSITE; PS51447; FDX_ACB; 1.
1: Evidence at protein level;
3D-structure; Acetylation; Aminoacyl-tRNA synthetase; ATP-binding;
Complete proteome; Disease mutation; Hereditary spastic paraplegia;
Ligase; Mitochondrion; Neurodegeneration; Nucleotide-binding;
Polymorphism; Primary mitochondrial disease; Protein biosynthesis;
Reference proteome; Transit peptide.
TRANSIT 1 ? Mitochondrion. {ECO:0000255}.
CHAIN ? 451 Phenylalanine--tRNA ligase,
mitochondrial.
/FTId=PRO_0000035813.
DOMAIN 358 450 FDX-ACB. {ECO:0000255|PROSITE-
ProRule:PRU00778}.
REGION 157 160 Substrate binding.
REGION 186 188 Substrate binding.
REGION 193 195 Substrate binding.
BINDING 179 179 Substrate. {ECO:0000269|PubMed:18611382,
ECO:0000269|PubMed:19549855}.
BINDING 287 287 Substrate; via carbonyl oxygen.
{ECO:0000269|PubMed:18611382,
ECO:0000269|PubMed:19549855}.
BINDING 312 312 Substrate; via carbonyl oxygen.
{ECO:0000269|PubMed:18611382,
ECO:0000269|PubMed:19549855}.
MOD_RES 202 202 N6-acetyllysine.
{ECO:0000244|PubMed:19608861}.
VARIANT 57 57 S -> C (in dbSNP:rs34382405).
/FTId=VAR_052642.
VARIANT 142 142 D -> Y (in SPG77; resulted in severely
impaired phenylalanine-tRNA ligase
activity). {ECO:0000269|PubMed:26553276}.
/FTId=VAR_077044.
VARIANT 144 144 Y -> C (in COXPD14; results in decreased
affinity for tRNA causing a decrease in
the catalytic efficiency for tRNA
charging; does not affect ATP or Phe
binding; dbSNP:rs397514610).
{ECO:0000269|PubMed:22499341,
ECO:0000269|PubMed:22833457}.
/FTId=VAR_069487.
VARIANT 280 280 N -> S (in dbSNP:rs11243011).
{ECO:0000269|PubMed:14702039,
ECO:0000269|Ref.3, ECO:0000269|Ref.7}.
/FTId=VAR_052643.
VARIANT 329 329 I -> T (in COXPD14; results in a 4-fold
decrease in the catalytic efficiency of
amino acid activation mainly due to a
decreased affinity for ATP; does not
affect Phe binding; affects the stability
of the enzyme, leading to a significant
decrease in overall charging capacity;
dbSNP:rs397514611).
{ECO:0000269|PubMed:22833457}.
/FTId=VAR_069488.
VARIANT 391 391 D -> V (in COXPD14; results in a decrease
in affinity for Phe causing a decrease in
aminoacylation activity; affects the
stability of the enzyme, leading to a
significant decrease in overall charging
capacity; dbSNP:rs397514612).
{ECO:0000269|PubMed:22833457}.
/FTId=VAR_069489.
CONFLICT 158 158 A -> T (in Ref. 4; BAD97143).
{ECO:0000305}.
CONFLICT 361 361 P -> T (in Ref. 7; AAF28998).
{ECO:0000305}.
STRAND 49 53 {ECO:0000244|PDB:3CMQ}.
STRAND 56 59 {ECO:0000244|PDB:3CMQ}.
HELIX 68 71 {ECO:0000244|PDB:3CMQ}.
TURN 72 75 {ECO:0000244|PDB:3CMQ}.
HELIX 78 80 {ECO:0000244|PDB:3CMQ}.
STRAND 81 84 {ECO:0000244|PDB:3TUP}.
HELIX 85 103 {ECO:0000244|PDB:3CMQ}.
STRAND 105 107 {ECO:0000244|PDB:3CMQ}.
STRAND 111 113 {ECO:0000244|PDB:3CMQ}.
STRAND 118 121 {ECO:0000244|PDB:3CMQ}.
HELIX 122 125 {ECO:0000244|PDB:3CMQ}.
HELIX 127 129 {ECO:0000244|PDB:3CMQ}.
HELIX 136 138 {ECO:0000244|PDB:3CMQ}.
HELIX 140 142 {ECO:0000244|PDB:3CMQ}.
STRAND 145 152 {ECO:0000244|PDB:3CMQ}.
HELIX 156 159 {ECO:0000244|PDB:3CMQ}.
HELIX 160 165 {ECO:0000244|PDB:3CMQ}.
STRAND 169 178 {ECO:0000244|PDB:3CMQ}.
STRAND 184 186 {ECO:0000244|PDB:3TUP}.
STRAND 189 201 {ECO:0000244|PDB:3CMQ}.
HELIX 202 205 {ECO:0000244|PDB:3CMQ}.
TURN 206 208 {ECO:0000244|PDB:3CMQ}.
HELIX 212 214 {ECO:0000244|PDB:3CMQ}.
HELIX 233 255 {ECO:0000244|PDB:3CMQ}.
HELIX 256 258 {ECO:0000244|PDB:3HFV}.
STRAND 261 268 {ECO:0000244|PDB:3CMQ}.
STRAND 271 281 {ECO:0000244|PDB:3CMQ}.
STRAND 284 294 {ECO:0000244|PDB:3CMQ}.
HELIX 296 301 {ECO:0000244|PDB:3CMQ}.
STRAND 307 315 {ECO:0000244|PDB:3CMQ}.
HELIX 316 323 {ECO:0000244|PDB:3CMQ}.
HELIX 329 333 {ECO:0000244|PDB:3CMQ}.
HELIX 337 340 {ECO:0000244|PDB:3CMQ}.
HELIX 341 343 {ECO:0000244|PDB:3CMQ}.
STRAND 363 370 {ECO:0000244|PDB:3CMQ}.
HELIX 378 389 {ECO:0000244|PDB:3CMQ}.
HELIX 390 392 {ECO:0000244|PDB:3CMQ}.
STRAND 393 403 {ECO:0000244|PDB:3CMQ}.
TURN 405 407 {ECO:0000244|PDB:3CMQ}.
STRAND 410 418 {ECO:0000244|PDB:3CMQ}.
STRAND 421 423 {ECO:0000244|PDB:3CMQ}.
HELIX 427 444 {ECO:0000244|PDB:3CMQ}.
STRAND 448 451 {ECO:0000244|PDB:3HFV}.
SEQUENCE 451 AA; 52357 MW; 1E5CC647A4A7193B CRC64;
MVGSALRRGA HAYVYLVSKA SHISRGHQHQ AWGSRPPAAE CATQRAPGSV VELLGKSYPQ
DDHSNLTRKV LTRVGRNLHN QQHHPLWLIK ERVKEHFYKQ YVGRFGTPLF SVYDNLSPVV
TTWQNFDSLL IPADHPSRKK GDNYYLNRTH MLRAHTSAHQ WDLLHAGLDA FLVVGDVYRR
DQIDSQHYPI FHQLEAVRLF SKHELFAGIK DGESLQLFEQ SSRSAHKQET HTMEAVKLVE
FDLKQTLTRL MAHLFGDELE IRWVDCYFPF THPSFEMEIN FHGEWLEVLG CGVMEQQLVN
SAGAQDRIGW AFGLGLERLA MILYDIPDIR LFWCEDERFL KQFCVSNINQ KVKFQPLSKY
PAVINDISFW LPSENYAEND FYDLVRTIGG DLVEKVDLID KFVHPKTHKT SHCYRITYRH
MERTLSQREV RHIHQALQEA AVQLLGVEGR F


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