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Q9NSD9

- SYFB_HUMAN

UniProt

Q9NSD9 - SYFB_HUMAN

Protein

Phenylalanine--tRNA ligase beta subunit

Gene

FARSB

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 135 (01 Oct 2014)
      Sequence version 3 (18 May 2010)
      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. magnesium ion binding Source: InterPro
    3. phenylalanine-tRNA ligase activity Source: ProtInc
    4. RNA binding Source: InterPro

    GO - Biological processi

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

    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_15306. Cytosolic tRNA aminoacylation.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Phenylalanine--tRNA ligase beta subunit (EC:6.1.1.20)
    Alternative name(s):
    Phenylalanyl-tRNA synthetase beta subunit
    Short name:
    PheRS
    Gene namesi
    Name:FARSB
    Synonyms:FARSLB, FRSB
    ORF Names:HSPC173
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 2

    Organism-specific databases

    HGNCiHGNC:17800. FARSB.

    Subcellular locationi

    Cytoplasm By similarity

    GO - Cellular componenti

    1. cytoplasm Source: ProtInc
    2. cytosol Source: Reactome
    3. membrane Source: UniProtKB

    Keywords - Cellular componenti

    Cytoplasm

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA162388068.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 589589Phenylalanine--tRNA ligase beta subunitPRO_0000127016Add
    BLAST

    Proteomic databases

    MaxQBiQ9NSD9.
    PaxDbiQ9NSD9.
    PRIDEiQ9NSD9.

    PTM databases

    PhosphoSiteiQ9NSD9.

    Expressioni

    Gene expression databases

    ArrayExpressiQ9NSD9.
    BgeeiQ9NSD9.
    CleanExiHS_FARSB.
    GenevestigatoriQ9NSD9.

    Organism-specific databases

    HPAiHPA036678.

    Interactioni

    Subunit structurei

    Tetramer of two alpha and two beta subunits.By similarity

    Protein-protein interaction databases

    BioGridi115367. 31 interactions.
    DIPiDIP-32869N.
    IntActiQ9NSD9. 7 interactions.
    MINTiMINT-3073662.
    STRINGi9606.ENSP00000281828.

    Structurei

    Secondary structure

    1
    589
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi3 – 75
    Helixi8 – 158
    Helixi23 – 308
    Beta strandi34 – 407
    Helixi41 – 455
    Beta strandi48 – 503
    Beta strandi56 – 6611
    Helixi77 – 8711
    Beta strandi97 – 993
    Beta strandi107 – 1104
    Turni112 – 1176
    Beta strandi120 – 1267
    Helixi133 – 14513
    Turni146 – 15510
    Beta strandi156 – 1638
    Helixi164 – 1663
    Beta strandi171 – 1766
    Beta strandi178 – 1803
    Helixi194 – 2007
    Turni205 – 21410
    Beta strandi220 – 2245
    Turni234 – 2363
    Beta strandi237 – 2404
    Beta strandi251 – 2588
    Helixi260 – 27415
    Helixi275 – 2773
    Beta strandi281 – 2855
    Beta strandi287 – 2904
    Beta strandi296 – 2994
    Beta strandi305 – 3106
    Helixi311 – 3188
    Helixi324 – 33310
    Beta strandi337 – 3404
    Beta strandi342 – 35110
    Helixi361 – 37212
    Helixi374 – 3763
    Helixi392 – 40615
    Beta strandi416 – 4183
    Helixi420 – 4234
    Helixi425 – 4273
    Beta strandi438 – 4414
    Helixi445 – 4473
    Beta strandi448 – 4503
    Helixi455 – 46410
    Turni465 – 4673
    Beta strandi472 – 48312
    Beta strandi490 – 50516
    Helixi508 – 52114
    Turni528 – 5314
    Beta strandi532 – 5376
    Beta strandi543 – 55311
    Beta strandi556 – 5649
    Helixi566 – 5716
    Beta strandi578 – 5847
    Helixi586 – 5883

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    3L4GX-ray3.30B/D/F/H/J/L/N/P1-589[»]
    ProteinModelPortaliQ9NSD9.
    SMRiQ9NSD9. Positions 1-589.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini302 – 37978B5PROSITE-ProRule annotationAdd
    BLAST

    Sequence similaritiesi

    Contains 1 B5 domain.PROSITE-ProRule annotation

    Phylogenomic databases

    eggNOGiCOG0072.
    HOGENOMiHOG000105095.
    HOVERGENiHBG009523.
    InParanoidiQ9NSD9.
    KOiK01890.
    OMAiEVMPLIL.
    OrthoDBiEOG7R2BJ6.
    PhylomeDBiQ9NSD9.
    TreeFamiTF105681.

    Family and domain databases

    Gene3Di3.30.56.20. 1 hit.
    InterProiIPR005146. B3/B4_tRNA-bd.
    IPR009061. DNA-bd_dom_put.
    IPR004531. Phe-tRNA-synth_IIc_bsu_arc.
    IPR020825. Phe-tRNA_synthase_B3/B4.
    IPR005147. tRNA_synthase_B5-dom.
    [Graphical view]
    PfamiPF03483. B3_4. 1 hit.
    PF03484. B5. 1 hit.
    [Graphical view]
    SMARTiSM00873. B3_4. 1 hit.
    SM00874. B5. 1 hit.
    [Graphical view]
    SUPFAMiSSF46955. SSF46955. 2 hits.
    SSF56037. SSF56037. 1 hit.
    TIGRFAMsiTIGR00471. pheT_arch. 1 hit.
    PROSITEiPS51483. B5. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Q9NSD9-1 [UniParc]FASTAAdd to Basket

    « Hide

    MPTVSVKRDL LFQALGRTYT DEEFDELCFE FGLELDEITS EKEIISKEQG    50
    NVKAAGASDV VLYKIDVPAN RYDLLCLEGL VRGLQVFKER IKAPVYKRVM 100
    PDGKIQKLII TEETAKIRPF AVAAVLRNIK FTKDRYDSFI ELQEKLHQNI 150
    CRKRALVAIG THDLDTLSGP FTYTAKRPSD IKFKPLNKTK EYTACELMNI 200
    YKTDNHLKHY LHIIENKPLY PVIYDSNGVV LSMPPIINGD HSRITVNTRN 250
    IFIECTGTDF TKAKIVLDII VTMFSEYCEN QFTVEAAEVV FPNGKSHTFP 300
    ELAYRKEMVR ADLINKKVGI RETPENLAKL LTRMYLKSEV IGDGNQIEIE 350
    IPPTRADIIH ACDIVEDAAI AYGYNNIQMT LPKTYTIANQ FPLNKLTELL 400
    RHDMAAAGFT EALTFALCSQ EDIADKLGVD ISATKAVHIS NPKTAEFQVA 450
    RTTLLPGLLK TIAANRKMPL PLKLFEISDI VIKDSNTDVG AKNYRHLCAV 500
    YYNKNPGFEI IHGLLDRIMQ LLDVPPGEDK GGYVIKASEG PAFFPGRCAE 550
    IFARGQSVGK LGVLHPDVIT KFELTMPCSS LEINVGPFL 589
    Length:589
    Mass (Da):66,116
    Last modified:May 18, 2010 - v3
    Checksum:i6425BA46D124BC08
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti281 – 2811Q → R in AAF29136. (PubMed:11042152)Curated
    Sequence conflicti555 – 5551G → V in BAA95608. 1 PublicationCurated
    Sequence conflicti585 – 5851V → I in BAA95608. 1 PublicationCurated
    Sequence conflicti585 – 5851V → I in AAD02220. (PubMed:10049785)Curated
    Sequence conflicti585 – 5851V → I in AAF29136. (PubMed:11042152)Curated
    Sequence conflicti585 – 5851V → I in AAH17783. (PubMed:15489334)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    D84430 mRNA. Translation: BAA95608.1.
    AF042346 mRNA. Translation: AAD02220.1.
    AF161521 mRNA. Translation: AAF29136.1.
    AC097461 Genomic DNA. Translation: AAX88958.1.
    AC104772 Genomic DNA. Translation: AAX81986.1.
    BC017783 mRNA. Translation: AAH17783.1.
    CCDSiCCDS2454.1.
    RefSeqiNP_005678.3. NM_005687.3.
    UniGeneiHs.471452.

    Genome annotation databases

    EnsembliENST00000281828; ENSP00000281828; ENSG00000116120.
    GeneIDi10056.
    KEGGihsa:10056.
    UCSCiuc002vne.1. human.

    Polymorphism databases

    DMDMi296452943.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    D84430 mRNA. Translation: BAA95608.1 .
    AF042346 mRNA. Translation: AAD02220.1 .
    AF161521 mRNA. Translation: AAF29136.1 .
    AC097461 Genomic DNA. Translation: AAX88958.1 .
    AC104772 Genomic DNA. Translation: AAX81986.1 .
    BC017783 mRNA. Translation: AAH17783.1 .
    CCDSi CCDS2454.1.
    RefSeqi NP_005678.3. NM_005687.3.
    UniGenei Hs.471452.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    3L4G X-ray 3.30 B/D/F/H/J/L/N/P 1-589 [» ]
    ProteinModelPortali Q9NSD9.
    SMRi Q9NSD9. Positions 1-589.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 115367. 31 interactions.
    DIPi DIP-32869N.
    IntActi Q9NSD9. 7 interactions.
    MINTi MINT-3073662.
    STRINGi 9606.ENSP00000281828.

    Chemistry

    DrugBanki DB00120. L-Phenylalanine.

    PTM databases

    PhosphoSitei Q9NSD9.

    Polymorphism databases

    DMDMi 296452943.

    Proteomic databases

    MaxQBi Q9NSD9.
    PaxDbi Q9NSD9.
    PRIDEi Q9NSD9.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000281828 ; ENSP00000281828 ; ENSG00000116120 .
    GeneIDi 10056.
    KEGGi hsa:10056.
    UCSCi uc002vne.1. human.

    Organism-specific databases

    CTDi 10056.
    GeneCardsi GC02M223435.
    H-InvDB HIX0002878.
    HGNCi HGNC:17800. FARSB.
    HPAi HPA036678.
    MIMi 609690. gene.
    neXtProti NX_Q9NSD9.
    PharmGKBi PA162388068.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG0072.
    HOGENOMi HOG000105095.
    HOVERGENi HBG009523.
    InParanoidi Q9NSD9.
    KOi K01890.
    OMAi EVMPLIL.
    OrthoDBi EOG7R2BJ6.
    PhylomeDBi Q9NSD9.
    TreeFami TF105681.

    Enzyme and pathway databases

    BRENDAi 6.1.1.20. 2681.
    Reactomei REACT_15306. Cytosolic tRNA aminoacylation.

    Miscellaneous databases

    ChiTaRSi FARSB. human.
    GeneWikii FARSB.
    GenomeRNAii 10056.
    NextBioi 37993.
    PROi Q9NSD9.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q9NSD9.
    Bgeei Q9NSD9.
    CleanExi HS_FARSB.
    Genevestigatori Q9NSD9.

    Family and domain databases

    Gene3Di 3.30.56.20. 1 hit.
    InterProi IPR005146. B3/B4_tRNA-bd.
    IPR009061. DNA-bd_dom_put.
    IPR004531. Phe-tRNA-synth_IIc_bsu_arc.
    IPR020825. Phe-tRNA_synthase_B3/B4.
    IPR005147. tRNA_synthase_B5-dom.
    [Graphical view ]
    Pfami PF03483. B3_4. 1 hit.
    PF03484. B5. 1 hit.
    [Graphical view ]
    SMARTi SM00873. B3_4. 1 hit.
    SM00874. B5. 1 hit.
    [Graphical view ]
    SUPFAMi SSF46955. SSF46955. 2 hits.
    SSF56037. SSF56037. 1 hit.
    TIGRFAMsi TIGR00471. pheT_arch. 1 hit.
    PROSITEi PS51483. B5. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. Motegi H., Noda T., Shiba K.
      Submitted (APR-1996) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    2. "Human phenylalanyl-tRNA synthetase: cloning, characterization of the deduced amino acid sequences in terms of the structural domains and coordinately regulated expression of the alpha and beta subunits in chronic myeloid leukemia cells."
      Rodova M., Ankilova V., Safro M.G.
      Biochem. Biophys. Res. Commun. 255:765-773(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    3. "Cloning and functional analysis of cDNAs with open reading frames for 300 previously undefined genes expressed in CD34+ hematopoietic stem/progenitor cells."
      Zhang Q.-H., Ye M., Wu X.-Y., Ren S.-X., Zhao M., Zhao C.-J., Fu G., Shen Y., Fan H.-Y., Lu G., Zhong M., Xu X.-R., Han Z.-G., Zhang J.-W., Tao J., Huang Q.-H., Zhou J., Hu G.-X.
      , Gu J., Chen S.-J., Chen Z.
      Genome Res. 10:1546-1560(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Tissue: Umbilical cord blood.
    4. "Generation and annotation of the DNA sequences of human chromosomes 2 and 4."
      Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L., Du H.
      , Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K., McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C., Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S., Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H., Wilson R.K.
      Nature 434:724-731(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    5. "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: Testis.
    6. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    7. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

    Entry informationi

    Entry nameiSYFB_HUMAN
    AccessioniPrimary (citable) accession number: Q9NSD9
    Secondary accession number(s): O95708
    , Q4ZFX1, Q57ZJ5, Q9NZZ6
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: December 8, 2000
    Last sequence update: May 18, 2010
    Last modified: October 1, 2014
    This is version 135 of the entry and version 3 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 2
      Human chromosome 2: entries, gene names and cross-references to MIM
    3. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    4. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    5. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3