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Protein

Phenylalanine--tRNA ligase, mitochondrial

Gene

FARS2

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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.2 Publications

Catalytic activityi

ATP + L-phenylalanine + tRNA(Phe) = AMP + diphosphate + L-phenylalanyl-tRNA(Phe).2 Publications

Kineticsi

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).1 Publication

  1. KM=2.2 µM for L-phenylalanine2 Publications
  2. KM=1900 µM for L-tyrosine2 Publications
  3. KM=11.7 µM for DL-m-tyrosine2 Publications
  4. KM=7.3 µM for L-phenylalanine2 Publications
  5. KM=2.9 mM for ATP2 Publications
  6. KM=1.2 µM for tRNA(Phe)2 Publications

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei179 – 1791Substrate2 Publications
    Binding sitei287 – 2871Substrate; via carbonyl oxygen2 Publications
    Binding sitei312 – 3121Substrate; via carbonyl oxygen2 Publications

    GO - Molecular functioni

    • ATP binding Source: UniProtKB-KW
    • magnesium ion binding Source: InterPro
    • phenylalanine-tRNA ligase activity Source: UniProtKB
    • tRNA binding Source: UniProtKB

    GO - Biological processi

    • gene expression Source: Reactome
    • phenylalanyl-tRNA aminoacylation Source: UniProtKB
    • tRNA aminoacylation for protein translation Source: Reactome
    • tRNA processing Source: UniProtKB
    Complete GO annotation...

    Keywords - Molecular functioni

    Aminoacyl-tRNA synthetase, Ligase

    Keywords - Biological processi

    Protein biosynthesis

    Keywords - Ligandi

    ATP-binding, Nucleotide-binding

    Enzyme and pathway databases

    BRENDAi6.1.1.20. 2681.
    ReactomeiREACT_15302. Mitochondrial tRNA aminoacylation.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Phenylalanine--tRNA ligase, mitochondrial (EC:6.1.1.20)
    Alternative name(s):
    Phenylalanyl-tRNA synthetase
    Short name:
    PheRS
    Gene namesi
    Name:FARS2
    Synonyms:FARS1
    ORF Names:HSPC320
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640 Componenti: Chromosome 6

    Organism-specific databases

    HGNCiHGNC:21062. FARS2.

    Subcellular locationi

    GO - Cellular componenti

    Complete GO annotation...

    Keywords - Cellular componenti

    Mitochondrion

    Pathology & Biotechi

    Involvement in diseasei

    Combined oxidative phosphorylation deficiency 14 (COXPD14)2 Publications

    The disease is caused by mutations affecting the gene represented in this entry.

    Disease descriptionA 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.

    See also OMIM:614946
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti144 – 1441Y → 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. 2 Publications
    VAR_069487
    Natural varianti329 – 3291I → 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. 1 Publication
    VAR_069488
    Natural varianti391 – 3911D → 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. 1 Publication
    VAR_069489

    Keywords - Diseasei

    Disease mutation

    Organism-specific databases

    MIMi614946. phenotype.
    Orphaneti319519. Combined oxidative phosphorylation defect type 14.
    PharmGKBiPA134954893.

    Chemistry

    DrugBankiDB00120. L-Phenylalanine.

    Polymorphism and mutation databases

    BioMutaiFARS2.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini? – 451Phenylalanine--tRNA ligase, mitochondrialPRO_0000035813
    Transit peptidei1 – ?MitochondrionSequence Analysis

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei202 – 2021N6-acetyllysine1 Publication

    Keywords - PTMi

    Acetylation

    Proteomic databases

    MaxQBiO95363.
    PaxDbiO95363.
    PeptideAtlasiO95363.
    PRIDEiO95363.

    PTM databases

    PhosphoSiteiO95363.

    Expressioni

    Gene expression databases

    BgeeiO95363.
    CleanExiHS_FARS2.
    ExpressionAtlasiO95363. baseline and differential.
    GenevestigatoriO95363.

    Organism-specific databases

    HPAiHPA018148.
    HPA028836.

    Interactioni

    Subunit structurei

    Monomer.3 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    ADAMTSL4Q6UY14-33EBI-2513774,EBI-10173507
    AGTRAPQ6RW133EBI-2513774,EBI-741181
    APPL1Q9UKG13EBI-2513774,EBI-741243
    CALCOCO2Q131373EBI-2513774,EBI-739580
    CMTM5Q96DZ93EBI-2513774,EBI-2548702
    HMBOX1Q6NT763EBI-2513774,EBI-2549423
    IKZF3Q9UKT93EBI-2513774,EBI-747204
    KRT13A1A4E93EBI-2513774,EBI-10171552
    KRT31Q153233EBI-2513774,EBI-948001
    KRT40Q6A1623EBI-2513774,EBI-10171697
    KRTAP10-5P603703EBI-2513774,EBI-10172150
    KRTAP10-7P604093EBI-2513774,EBI-10172290
    KRTAP10-9P604113EBI-2513774,EBI-10172052
    MID2Q9UJV3-23EBI-2513774,EBI-10172526
    MKRN3Q130643EBI-2513774,EBI-2340269
    NOTCH2NLQ7Z3S93EBI-2513774,EBI-945833
    RCBTB2O951993EBI-2513774,EBI-742404
    STX11O755583EBI-2513774,EBI-714135
    TADA2AO754783EBI-2513774,EBI-742268
    TFCP2Q128003EBI-2513774,EBI-717422
    TRIM27P143733EBI-2513774,EBI-719493
    TRIM54Q9BYV23EBI-2513774,EBI-2130429

    Protein-protein interaction databases

    BioGridi115909. 42 interactions.
    IntActiO95363. 26 interactions.
    MINTiMINT-3077661.
    STRINGi9606.ENSP00000274680.

    Structurei

    Secondary structure

    1
    451
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi49 – 535Combined sources
    Beta strandi56 – 594Combined sources
    Helixi68 – 714Combined sources
    Turni72 – 754Combined sources
    Helixi78 – 803Combined sources
    Beta strandi81 – 844Combined sources
    Helixi85 – 10319Combined sources
    Beta strandi105 – 1073Combined sources
    Beta strandi111 – 1133Combined sources
    Beta strandi118 – 1214Combined sources
    Helixi122 – 1254Combined sources
    Helixi127 – 1293Combined sources
    Helixi136 – 1383Combined sources
    Helixi140 – 1423Combined sources
    Beta strandi145 – 1528Combined sources
    Helixi156 – 1594Combined sources
    Helixi160 – 1656Combined sources
    Beta strandi169 – 17810Combined sources
    Beta strandi184 – 1863Combined sources
    Beta strandi189 – 20113Combined sources
    Helixi202 – 2054Combined sources
    Turni206 – 2083Combined sources
    Helixi212 – 2143Combined sources
    Helixi233 – 25523Combined sources
    Helixi256 – 2583Combined sources
    Beta strandi261 – 2688Combined sources
    Beta strandi271 – 28111Combined sources
    Beta strandi284 – 29411Combined sources
    Helixi296 – 3016Combined sources
    Beta strandi307 – 3159Combined sources
    Helixi316 – 3238Combined sources
    Helixi329 – 3335Combined sources
    Helixi337 – 3404Combined sources
    Helixi341 – 3433Combined sources
    Beta strandi363 – 3708Combined sources
    Helixi378 – 38912Combined sources
    Helixi390 – 3923Combined sources
    Beta strandi393 – 40311Combined sources
    Turni405 – 4073Combined sources
    Beta strandi410 – 4189Combined sources
    Beta strandi421 – 4233Combined sources
    Helixi427 – 44418Combined sources
    Beta strandi448 – 4514Combined sources

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    3CMQX-ray2.20A38-451[»]
    3HFVX-ray2.60A38-451[»]
    3TEGX-ray2.20A38-451[»]
    3TUPX-ray3.05A38-451[»]
    ProteinModelPortaliO95363.
    SMRiO95363. Positions 47-451.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiO95363.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini358 – 45093FDX-ACBPROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni157 – 1604Substrate binding
    Regioni186 – 1883Substrate binding
    Regioni193 – 1953Substrate binding

    Sequence similaritiesi

    Contains 1 FDX-ACB domain.PROSITE-ProRule annotation

    Keywords - Domaini

    Transit peptide

    Phylogenomic databases

    eggNOGiCOG0016.
    GeneTreeiENSGT00530000063467.
    HOGENOMiHOG000165163.
    HOVERGENiHBG082540.
    InParanoidiO95363.
    KOiK01889.
    OMAiEFTHPKT.
    OrthoDBiEOG7CG6ZS.
    PhylomeDBiO95363.
    TreeFamiTF105798.

    Family and domain databases

    Gene3Di3.30.70.380. 1 hit.
    InterProiIPR006195. aa-tRNA-synth_II.
    IPR004530. Phe-tRNA-synth_IIc_mito.
    IPR002319. Phenylalanyl-tRNA_Synthase.
    IPR005121. PheS_beta_Fdx_antiC-bd.
    [Graphical view]
    PfamiPF03147. FDX-ACB. 1 hit.
    PF01409. tRNA-synt_2d. 2 hits.
    [Graphical view]
    SMARTiSM00896. FDX-ACB. 1 hit.
    [Graphical view]
    SUPFAMiSSF54991. SSF54991. 1 hit.
    TIGRFAMsiTIGR00469. pheS_mito. 1 hit.
    PROSITEiPS50862. AA_TRNA_LIGASE_II. 1 hit.
    PS51447. FDX_ACB. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    O95363-1 [UniParc]FASTAAdd to basket

    « Hide

            10         20         30         40         50
    MVGSALRRGA HAYVYLVSKA SHISRGHQHQ AWGSRPPAAE CATQRAPGSV
    60 70 80 90 100
    VELLGKSYPQ DDHSNLTRKV LTRVGRNLHN QQHHPLWLIK ERVKEHFYKQ
    110 120 130 140 150
    YVGRFGTPLF SVYDNLSPVV TTWQNFDSLL IPADHPSRKK GDNYYLNRTH
    160 170 180 190 200
    MLRAHTSAHQ WDLLHAGLDA FLVVGDVYRR DQIDSQHYPI FHQLEAVRLF
    210 220 230 240 250
    SKHELFAGIK DGESLQLFEQ SSRSAHKQET HTMEAVKLVE FDLKQTLTRL
    260 270 280 290 300
    MAHLFGDELE IRWVDCYFPF THPSFEMEIN FHGEWLEVLG CGVMEQQLVN
    310 320 330 340 350
    SAGAQDRIGW AFGLGLERLA MILYDIPDIR LFWCEDERFL KQFCVSNINQ
    360 370 380 390 400
    KVKFQPLSKY PAVINDISFW LPSENYAEND FYDLVRTIGG DLVEKVDLID
    410 420 430 440 450
    KFVHPKTHKT SHCYRITYRH MERTLSQREV RHIHQALQEA AVQLLGVEGR

    F
    Length:451
    Mass (Da):52,357
    Last modified:May 1, 1999 - v1
    Checksum:i1E5CC647A4A7193B
    GO

    Sequence cautioni

    The sequence AAF28998.1 differs from that shown. Reason: Frameshift at position 414. Curated

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti158 – 1581A → T in BAD97143 (Ref. 4) Curated
    Sequence conflicti361 – 3611P → T in AAF28998 (Ref. 7) Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti57 – 571S → C.
    Corresponds to variant rs34382405 [ dbSNP | Ensembl ].
    VAR_052642
    Natural varianti144 – 1441Y → 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. 2 Publications
    VAR_069487
    Natural varianti280 – 2801N → S.3 Publications
    Corresponds to variant rs11243011 [ dbSNP | Ensembl ].
    VAR_052643
    Natural varianti329 – 3291I → 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. 1 Publication
    VAR_069488
    Natural varianti391 – 3911D → 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. 1 Publication
    VAR_069489

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    AF097441 mRNA. Translation: AAC83802.1.
    AK312454 mRNA. Translation: BAG35361.1.
    CR542279 mRNA. Translation: CAG47075.1.
    AK223423 mRNA. Translation: BAD97143.1.
    AL133473
    , AL022097, AL590868, AL121978, AL392184 Genomic DNA. Translation: CAI19901.1.
    AL022097
    , AL121978, AL392184, AL590868, AL133473 Genomic DNA. Translation: CAI19950.1.
    AL392184
    , AL121978, AL590868, AL133473, AL022097 Genomic DNA. Translation: CAI20375.1.
    AL121978
    , AL133473, AL022097, AL392184, AL590868 Genomic DNA. Translation: CAI21657.1.
    AL590868
    , AL392184, AL133473, AL121978, AL022097 Genomic DNA. Translation: CAI39442.1.
    BC020239 mRNA. Translation: AAH20239.1.
    BC021112 mRNA. Translation: AAH21112.1.
    AF161438 mRNA. Translation: AAF28998.1. Frameshift.
    CCDSiCCDS4494.1.
    RefSeqiNP_006558.1. NM_006567.3.
    XP_005248868.1. XM_005248811.1.
    XP_005248869.1. XM_005248812.2.
    UniGeneiHs.484547.

    Genome annotation databases

    EnsembliENST00000274680; ENSP00000274680; ENSG00000145982.
    ENST00000324331; ENSP00000316335; ENSG00000145982.
    GeneIDi10667.
    KEGGihsa:10667.
    UCSCiuc003mwr.2. human.

    Keywords - Coding sequence diversityi

    Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    AF097441 mRNA. Translation: AAC83802.1.
    AK312454 mRNA. Translation: BAG35361.1.
    CR542279 mRNA. Translation: CAG47075.1.
    AK223423 mRNA. Translation: BAD97143.1.
    AL133473
    , AL022097, AL590868, AL121978, AL392184 Genomic DNA. Translation: CAI19901.1.
    AL022097
    , AL121978, AL392184, AL590868, AL133473 Genomic DNA. Translation: CAI19950.1.
    AL392184
    , AL121978, AL590868, AL133473, AL022097 Genomic DNA. Translation: CAI20375.1.
    AL121978
    , AL133473, AL022097, AL392184, AL590868 Genomic DNA. Translation: CAI21657.1.
    AL590868
    , AL392184, AL133473, AL121978, AL022097 Genomic DNA. Translation: CAI39442.1.
    BC020239 mRNA. Translation: AAH20239.1.
    BC021112 mRNA. Translation: AAH21112.1.
    AF161438 mRNA. Translation: AAF28998.1. Frameshift.
    CCDSiCCDS4494.1.
    RefSeqiNP_006558.1. NM_006567.3.
    XP_005248868.1. XM_005248811.1.
    XP_005248869.1. XM_005248812.2.
    UniGeneiHs.484547.

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    3CMQX-ray2.20A38-451[»]
    3HFVX-ray2.60A38-451[»]
    3TEGX-ray2.20A38-451[»]
    3TUPX-ray3.05A38-451[»]
    ProteinModelPortaliO95363.
    SMRiO95363. Positions 47-451.
    ModBaseiSearch...
    MobiDBiSearch...

    Protein-protein interaction databases

    BioGridi115909. 42 interactions.
    IntActiO95363. 26 interactions.
    MINTiMINT-3077661.
    STRINGi9606.ENSP00000274680.

    Chemistry

    BindingDBiO95363.
    ChEMBLiCHEMBL2511.
    DrugBankiDB00120. L-Phenylalanine.

    PTM databases

    PhosphoSiteiO95363.

    Polymorphism and mutation databases

    BioMutaiFARS2.

    Proteomic databases

    MaxQBiO95363.
    PaxDbiO95363.
    PeptideAtlasiO95363.
    PRIDEiO95363.

    Protocols and materials databases

    DNASUi10667.
    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

    EnsembliENST00000274680; ENSP00000274680; ENSG00000145982.
    ENST00000324331; ENSP00000316335; ENSG00000145982.
    GeneIDi10667.
    KEGGihsa:10667.
    UCSCiuc003mwr.2. human.

    Organism-specific databases

    CTDi10667.
    GeneCardsiGC06P005207.
    HGNCiHGNC:21062. FARS2.
    HPAiHPA018148.
    HPA028836.
    MIMi611592. gene.
    614946. phenotype.
    neXtProtiNX_O95363.
    Orphaneti319519. Combined oxidative phosphorylation defect type 14.
    PharmGKBiPA134954893.
    GenAtlasiSearch...

    Phylogenomic databases

    eggNOGiCOG0016.
    GeneTreeiENSGT00530000063467.
    HOGENOMiHOG000165163.
    HOVERGENiHBG082540.
    InParanoidiO95363.
    KOiK01889.
    OMAiEFTHPKT.
    OrthoDBiEOG7CG6ZS.
    PhylomeDBiO95363.
    TreeFamiTF105798.

    Enzyme and pathway databases

    BRENDAi6.1.1.20. 2681.
    ReactomeiREACT_15302. Mitochondrial tRNA aminoacylation.

    Miscellaneous databases

    ChiTaRSiFARS2. human.
    EvolutionaryTraceiO95363.
    GeneWikiiFARS2.
    GenomeRNAii10667.
    NextBioi40563.
    PROiO95363.
    SOURCEiSearch...

    Gene expression databases

    BgeeiO95363.
    CleanExiHS_FARS2.
    ExpressionAtlasiO95363. baseline and differential.
    GenevestigatoriO95363.

    Family and domain databases

    Gene3Di3.30.70.380. 1 hit.
    InterProiIPR006195. aa-tRNA-synth_II.
    IPR004530. Phe-tRNA-synth_IIc_mito.
    IPR002319. Phenylalanyl-tRNA_Synthase.
    IPR005121. PheS_beta_Fdx_antiC-bd.
    [Graphical view]
    PfamiPF03147. FDX-ACB. 1 hit.
    PF01409. tRNA-synt_2d. 2 hits.
    [Graphical view]
    SMARTiSM00896. FDX-ACB. 1 hit.
    [Graphical view]
    SUPFAMiSSF54991. SSF54991. 1 hit.
    TIGRFAMsiTIGR00469. pheS_mito. 1 hit.
    PROSITEiPS50862. AA_TRNA_LIGASE_II. 1 hit.
    PS51447. FDX_ACB. 1 hit.
    [Graphical view]
    ProtoNetiSearch...

    Publicationsi

    « Hide 'large scale' publications
    1. "Expression and characterization of a human mitochondrial phenylalanyl-tRNA synthetase."
      Bullard J.M., Cai Y.-C., Demeler B., Spremulli L.L.
      J. Mol. Biol. 288:567-577(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], SUBUNIT.
    2. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
      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.
      Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], VARIANT SER-280.
      Tissue: Caudate nucleus.
    3. "Cloning of human full open reading frames in Gateway(TM) system entry vector (pDONR201)."
      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.
      Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], VARIANT SER-280.
    4. Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S.
      Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Tissue: Kidney epithelium.
    5. "The DNA sequence and analysis of human chromosome 6."
      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.
      Nature 425:805-811(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    6. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
      The MGC Project Team
      Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Tissue: Pancreas.
    7. "Human partial CDS from CD34+ stem cells."
      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.
      Submitted (MAY-1999) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 108-451, VARIANT SER-280.
      Tissue: Umbilical cord blood.
    8. "Lysine acetylation targets protein complexes and co-regulates major cellular functions."
      Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M.
      Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-202, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    9. "The tRNA-induced conformational activation of human mitochondrial phenylalanyl-tRNA synthetase."
      Klipcan L., Levin I., Kessler N., Moor N., Finarov I., Safro M.
      Structure 16:1095-1104(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.20 ANGSTROMS) OF 38-451 IN COMPLEX WITH SUBSTRATE, SUBUNIT.
    10. "Eukaryotic cytosolic and mitochondrial phenylalanyl-tRNA synthetases catalyze the charging of tRNA with the meta-tyrosine."
      Klipcan L., Moor N., Kessler N., Safro M.G.
      Proc. Natl. Acad. Sci. U.S.A. 106:11045-11048(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.60 ANGSTROMS) OF 38-451 IN COMPLEX WITH SUBSTRATE, FUNCTION, CATALYTIC ACTIVITY, SUBSTRATE SPECIFICITY, KINETIC PARAMETERS.
    11. Cited for: VARIANTS COXPD14 THR-329 AND VAL-391, CHARACTERIZATION OF VARIANTS COXPD14 CYS-144; THR-329 AND VAL-391, FUNCTION, CATALYTIC ACTIVITY, KINETIC PARAMETERS.
    12. "Genomic analysis of mitochondrial diseases in a consanguineous population reveals novel candidate disease genes."
      Shamseldin H.E., Alshammari M., Al-Sheddi T., Salih M.A., Alkhalidi H., Kentab A., Repetto G.M., Hashem M., Alkuraya F.S.
      J. Med. Genet. 49:234-241(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT COXPD14 CYS-144.

    Entry informationi

    Entry nameiSYFM_HUMAN
    AccessioniPrimary (citable) accession number: O95363
    Secondary accession number(s): B2R664
    , Q53F66, Q5TCS3, Q6FG29, Q9NPY7, Q9P062
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 23, 2004
    Last sequence update: May 1, 1999
    Last modified: May 27, 2015
    This is version 135 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program
    DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. Aminoacyl-tRNA synthetases
      List of aminoacyl-tRNA synthetase entries
    2. Human chromosome 6
      Human chromosome 6: entries, gene names and cross-references to MIM
    3. Human entries with polymorphisms or disease mutations
      List of human entries with polymorphisms or disease mutations
    4. Human polymorphisms and disease mutations
      Index of human polymorphisms and disease mutations
    5. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    6. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    7. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3

    Similar proteinsi

    Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
    100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
    90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
    50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.