Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Basket 0
(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

O95363

- SYFM_HUMAN

UniProt

O95363 - SYFM_HUMAN

Protein

Phenylalanine--tRNA ligase, mitochondrial

Gene

FARS2

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 127 (01 Oct 2014)
      Sequence version 1 (01 May 1999)
      Previous versions | rss
    • Help video
    • Feedback
    • Comment

    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

    1. ATP binding Source: UniProtKB-KW
    2. magnesium ion binding Source: InterPro
    3. phenylalanine-tRNA ligase activity Source: UniProtKB
    4. tRNA binding Source: UniProtKB

    GO - Biological processi

    1. gene expression Source: Reactome
    2. phenylalanyl-tRNA aminoacylation Source: UniProtKB
    3. tRNA aminoacylation for protein translation Source: Reactome
    4. tRNA processing Source: UniProtKB

    Keywords - Molecular functioni

    Aminoacyl-tRNA synthetase, Ligase

    Keywords - Biological processi

    Protein biosynthesis

    Keywords - Ligandi

    ATP-binding, Nucleotide-binding

    Enzyme and pathway databases

    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: Chromosome 6

    Organism-specific databases

    HGNCiHGNC:21062. FARS2.

    Subcellular locationi

    GO - Cellular componenti

    1. mitochondrial matrix Source: Reactome

    Keywords - Cellular componenti

    Mitochondrion

    Pathology & Biotechi

    Involvement in diseasei

    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.2 Publications
    Note: The disease is caused by mutations affecting the gene represented in this entry.
    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. 1 Publication
    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.

    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

    ArrayExpressiO95363.
    BgeeiO95363.
    CleanExiHS_FARS2.
    GenevestigatoriO95363.

    Organism-specific databases

    HPAiHPA018148.
    HPA028836.

    Interactioni

    Subunit structurei

    Monomer.3 Publications

    Protein-protein interaction databases

    BioGridi115909. 8 interactions.
    IntActiO95363. 4 interactions.
    MINTiMINT-3077661.
    STRINGi9606.ENSP00000274680.

    Structurei

    Secondary structure

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

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    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.
    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

    MVGSALRRGA HAYVYLVSKA SHISRGHQHQ AWGSRPPAAE CATQRAPGSV    50
    VELLGKSYPQ DDHSNLTRKV LTRVGRNLHN QQHHPLWLIK ERVKEHFYKQ 100
    YVGRFGTPLF SVYDNLSPVV TTWQNFDSLL IPADHPSRKK GDNYYLNRTH 150
    MLRAHTSAHQ WDLLHAGLDA FLVVGDVYRR DQIDSQHYPI FHQLEAVRLF 200
    SKHELFAGIK DGESLQLFEQ SSRSAHKQET HTMEAVKLVE FDLKQTLTRL 250
    MAHLFGDELE IRWVDCYFPF THPSFEMEIN FHGEWLEVLG CGVMEQQLVN 300
    SAGAQDRIGW AFGLGLERLA MILYDIPDIR LFWCEDERFL KQFCVSNINQ 350
    KVKFQPLSKY PAVINDISFW LPSENYAEND FYDLVRTIGG DLVEKVDLID 400
    KFVHPKTHKT SHCYRITYRH MERTLSQREV RHIHQALQEA AVQLLGVEGR 450
    F 451
    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.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti158 – 1581A → T in BAD97143. 1 PublicationCurated
    Sequence conflicti361 – 3611P → T in AAF28998. 1 PublicationCurated

    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. 1 Publication
    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:
    EMBL
    GenBank
    DDBJ
    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:
    EMBL
    GenBank
    DDBJ
    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.
    CCDSi CCDS4494.1.
    RefSeqi NP_006558.1. NM_006567.3.
    XP_005248868.1. XM_005248811.1.
    XP_005248869.1. XM_005248812.2.
    UniGenei Hs.484547.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    3CMQ X-ray 2.20 A 38-451 [» ]
    3HFV X-ray 2.60 A 38-451 [» ]
    3TEG X-ray 2.20 A 38-451 [» ]
    3TUP X-ray 3.05 A 38-451 [» ]
    ProteinModelPortali O95363.
    SMRi O95363. Positions 47-451.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 115909. 8 interactions.
    IntActi O95363. 4 interactions.
    MINTi MINT-3077661.
    STRINGi 9606.ENSP00000274680.

    Chemistry

    BindingDBi O95363.
    ChEMBLi CHEMBL2511.
    DrugBanki DB00120. L-Phenylalanine.

    PTM databases

    PhosphoSitei O95363.

    Proteomic databases

    MaxQBi O95363.
    PaxDbi O95363.
    PeptideAtlasi O95363.
    PRIDEi O95363.

    Protocols and materials databases

    DNASUi 10667.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000274680 ; ENSP00000274680 ; ENSG00000145982 .
    ENST00000324331 ; ENSP00000316335 ; ENSG00000145982 .
    GeneIDi 10667.
    KEGGi hsa:10667.
    UCSCi uc003mwr.2. human.

    Organism-specific databases

    CTDi 10667.
    GeneCardsi GC06P005207.
    HGNCi HGNC:21062. FARS2.
    HPAi HPA018148.
    HPA028836.
    MIMi 611592. gene.
    614946. phenotype.
    neXtProti NX_O95363.
    Orphaneti 319519. Combined oxidative phosphorylation defect type 14.
    PharmGKBi PA134954893.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG0016.
    HOGENOMi HOG000165163.
    HOVERGENi HBG082540.
    InParanoidi O95363.
    KOi K01889.
    OMAi EFTHPKT.
    OrthoDBi EOG7CG6ZS.
    PhylomeDBi O95363.
    TreeFami TF105798.

    Enzyme and pathway databases

    Reactomei REACT_15302. Mitochondrial tRNA aminoacylation.

    Miscellaneous databases

    EvolutionaryTracei O95363.
    GeneWikii FARS2.
    GenomeRNAii 10667.
    NextBioi 40563.
    PROi O95363.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi O95363.
    Bgeei O95363.
    CleanExi HS_FARS2.
    Genevestigatori O95363.

    Family and domain databases

    Gene3Di 3.30.70.380. 1 hit.
    InterProi IPR006195. aa-tRNA-synth_II.
    IPR004530. Phe-tRNA-synth_IIc_mito.
    IPR002319. Phenylalanyl-tRNA_Synthase.
    IPR005121. PheS_beta_Fdx_antiC-bd.
    [Graphical view ]
    Pfami PF03147. FDX-ACB. 1 hit.
    PF01409. tRNA-synt_2d. 2 hits.
    [Graphical view ]
    SMARTi SM00896. FDX-ACB. 1 hit.
    [Graphical view ]
    SUPFAMi SSF54991. SSF54991. 1 hit.
    TIGRFAMsi TIGR00469. pheS_mito. 1 hit.
    PROSITEi PS50862. AA_TRNA_LIGASE_II. 1 hit.
    PS51447. FDX_ACB. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    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: October 1, 2014
    This is version 127 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