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Q8C0C7

- SYFA_MOUSE

UniProt

Q8C0C7 - SYFA_MOUSE

Protein

Phenylalanine--tRNA ligase alpha subunit

Gene

Farsa

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 3 out of 5- Experimental evidence at transcript leveli
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    • History
      Entry version 96 (01 Oct 2014)
      Sequence version 1 (01 Mar 2003)
      Previous versions | rss
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    Functioni

    Catalytic activityi

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

    GO - Molecular functioni

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

    GO - Biological processi

    1. phenylalanyl-tRNA aminoacylation Source: InterPro

    Keywords - Molecular functioni

    Aminoacyl-tRNA synthetase, Ligase

    Keywords - Biological processi

    Protein biosynthesis

    Keywords - Ligandi

    ATP-binding, Nucleotide-binding

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Phenylalanine--tRNA ligase alpha subunit (EC:6.1.1.20)
    Alternative name(s):
    Phenylalanyl-tRNA synthetase alpha subunit
    Short name:
    PheRS
    Gene namesi
    Name:Farsa
    Synonyms:Farsla
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome 8

    Organism-specific databases

    MGIiMGI:1913840. Farsa.

    Subcellular locationi

    Cytoplasm By similarity

    GO - Cellular componenti

    1. cytoplasm Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Cytoplasm

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11RemovedBy similarity
    Chaini2 – 508507Phenylalanine--tRNA ligase alpha subunitPRO_0000280447Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei2 – 21N-acetylalanineBy similarity
    Modified residuei193 – 1931PhosphoserineBy similarity
    Modified residuei311 – 3111N6-acetyllysineBy similarity

    Keywords - PTMi

    Acetylation, Phosphoprotein

    Proteomic databases

    MaxQBiQ8C0C7.
    PaxDbiQ8C0C7.
    PRIDEiQ8C0C7.

    PTM databases

    PhosphoSiteiQ8C0C7.

    Expressioni

    Gene expression databases

    ArrayExpressiQ8C0C7.
    BgeeiQ8C0C7.
    CleanExiMM_FARSA.
    GenevestigatoriQ8C0C7.

    Interactioni

    Subunit structurei

    Tetramer of two alpha and two beta subunits.By similarity

    Protein-protein interaction databases

    BioGridi211576. 4 interactions.
    IntActiQ8C0C7. 4 interactions.
    MINTiMINT-4113807.

    Structurei

    3D structure databases

    ProteinModelPortaliQ8C0C7.
    SMRiQ8C0C7. Positions 1-508.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Phylogenomic databases

    eggNOGiCOG0016.
    GeneTreeiENSGT00390000006387.
    HOGENOMiHOG000230294.
    HOVERGENiHBG068046.
    InParanoidiQ8C0C7.
    KOiK01889.
    OMAiGYKYDWK.
    OrthoDBiEOG789CB8.
    PhylomeDBiQ8C0C7.
    TreeFamiTF300647.

    Family and domain databases

    Gene3Di1.10.10.10. 1 hit.
    InterProiIPR006195. aa-tRNA-synth_II.
    IPR004529. Phe-tRNA-synth_IIc_asu.
    IPR002319. Phenylalanyl-tRNA_Synthase.
    IPR011991. WHTH_DNA-bd_dom.
    [Graphical view]
    PfamiPF01409. tRNA-synt_2d. 1 hit.
    [Graphical view]
    TIGRFAMsiTIGR00468. pheS. 1 hit.
    PROSITEiPS50862. AA_TRNA_LIGASE_II. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

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

    Q8C0C7-1 [UniParc]FASTAAdd to Basket

    « Hide

    MADNPVLELL LRRLEVADGG LDSAELATQL GVEHQAVVGA VKSLQALGEV    50
    IEAELRSTKC WELTTEGEEI AREGSHEARV FRSIPLEGLV QSELMHLPSG 100
    KVGFSKAMSN KWIRVDKSAA DGPRVFRVVD SIEDEVQKRL QLVQAGQAEK 150
    LAEKERNELR KRKLLTEVIL KTYWVSKGKA FSTSVSKQEA ELSPEMISSG 200
    SWRDRPFKPY NFSARGVLPD SGHLHPLLKV RSQFRQIFLE MGFTEMPTDN 250
    FIESSFWNFD ALFQPQQHPA RDQHDTFFLR DPAEALQLPM GYVQRVKRTH 300
    SQGGYGSQGY KYTWKLEEAR KNLLRTHTTA ASARALYQLA QKKPFTPAKY 350
    FSIDRVFRNE TLDATHLAEF HQIEGVIADH GLTLGHLMGV LREFFTKLGI 400
    TQLRFKPAYN PYTEPSMEVF SYHQGLKKWV EVGNSGVFRP EMLLPMGLPE 450
    NVSVIAWGLS LERPTMIKYG INNIRELVGH KVNLQMVYDS PVCRLDIEPR 500
    SSKTQEAA 508
    Length:508
    Mass (Da):57,599
    Last modified:March 1, 2003 - v1
    Checksum:i9C125BC4D4A26DAA
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti291 – 2911G → D in AAH06862. (PubMed:15489334)Curated
    Sequence conflicti291 – 2911G → D in AAH13533. (PubMed:15489334)Curated
    Sequence conflicti343 – 3431Missing in AAH13533. (PubMed:15489334)Curated
    Sequence conflicti455 – 4551I → T in AAH06862. (PubMed:15489334)Curated
    Sequence conflicti455 – 4551I → V in BAE32726. (PubMed:16141072)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AK031697 mRNA. Translation: BAC27519.1.
    AK154629 mRNA. Translation: BAE32726.1.
    BC006862 mRNA. Translation: AAH06862.1.
    BC013533 mRNA. Translation: AAH13533.1.
    CCDSiCCDS22480.2.
    RefSeqiNP_079924.2. NM_025648.3.
    UniGeneiMm.292517.

    Genome annotation databases

    EnsembliENSMUST00000003906; ENSMUSP00000003906; ENSMUSG00000003808.
    GeneIDi66590.
    KEGGimmu:66590.
    UCSCiuc009mnt.2. mouse.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AK031697 mRNA. Translation: BAC27519.1 .
    AK154629 mRNA. Translation: BAE32726.1 .
    BC006862 mRNA. Translation: AAH06862.1 .
    BC013533 mRNA. Translation: AAH13533.1 .
    CCDSi CCDS22480.2.
    RefSeqi NP_079924.2. NM_025648.3.
    UniGenei Mm.292517.

    3D structure databases

    ProteinModelPortali Q8C0C7.
    SMRi Q8C0C7. Positions 1-508.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 211576. 4 interactions.
    IntActi Q8C0C7. 4 interactions.
    MINTi MINT-4113807.

    PTM databases

    PhosphoSitei Q8C0C7.

    Proteomic databases

    MaxQBi Q8C0C7.
    PaxDbi Q8C0C7.
    PRIDEi Q8C0C7.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000003906 ; ENSMUSP00000003906 ; ENSMUSG00000003808 .
    GeneIDi 66590.
    KEGGi mmu:66590.
    UCSCi uc009mnt.2. mouse.

    Organism-specific databases

    CTDi 2193.
    MGIi MGI:1913840. Farsa.

    Phylogenomic databases

    eggNOGi COG0016.
    GeneTreei ENSGT00390000006387.
    HOGENOMi HOG000230294.
    HOVERGENi HBG068046.
    InParanoidi Q8C0C7.
    KOi K01889.
    OMAi GYKYDWK.
    OrthoDBi EOG789CB8.
    PhylomeDBi Q8C0C7.
    TreeFami TF300647.

    Miscellaneous databases

    ChiTaRSi FARSA. mouse.
    NextBioi 322092.
    PROi Q8C0C7.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q8C0C7.
    Bgeei Q8C0C7.
    CleanExi MM_FARSA.
    Genevestigatori Q8C0C7.

    Family and domain databases

    Gene3Di 1.10.10.10. 1 hit.
    InterProi IPR006195. aa-tRNA-synth_II.
    IPR004529. Phe-tRNA-synth_IIc_asu.
    IPR002319. Phenylalanyl-tRNA_Synthase.
    IPR011991. WHTH_DNA-bd_dom.
    [Graphical view ]
    Pfami PF01409. tRNA-synt_2d. 1 hit.
    [Graphical view ]
    TIGRFAMsi TIGR00468. pheS. 1 hit.
    PROSITEi PS50862. AA_TRNA_LIGASE_II. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "The transcriptional landscape of the mammalian genome."
      Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
      , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
      Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Strain: C57BL/6J and NOD.
      Tissue: Testis.
    2. "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].
      Strain: FVB/N.
      Tissue: Kidney and Mammary tumor.

    Entry informationi

    Entry nameiSYFA_MOUSE
    AccessioniPrimary (citable) accession number: Q8C0C7
    Secondary accession number(s): Q3U3Q9, Q91WR4, Q922S1
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: March 20, 2007
    Last sequence update: March 1, 2003
    Last modified: October 1, 2014
    This is version 96 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. Aminoacyl-tRNA synthetases
      List of aminoacyl-tRNA synthetase entries
    2. MGD cross-references
      Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
    3. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3