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Q9Y285

- SYFA_HUMAN

UniProt

Q9Y285 - SYFA_HUMAN

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Protein

Phenylalanine--tRNA ligase alpha subunit

Gene
FARSA, FARS, FARSL, FARSLA
Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

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: ProtInc
  3. poly(A) RNA binding Source: UniProtKB
  4. protein binding Source: IntAct
  5. tRNA binding Source: InterPro

GO - Biological processi

  1. gene expression Source: Reactome
  2. phenylalanyl-tRNA aminoacylation Source: InterPro
  3. tRNA aminoacylation for protein translation Source: Reactome
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_15306. Cytosolic tRNA aminoacylation.

Names & Taxonomyi

Protein namesi
Recommended name:
Phenylalanine--tRNA ligase alpha subunit (EC:6.1.1.20)
Alternative name(s):
CML33
Phenylalanyl-tRNA synthetase alpha subunit
Short name:
PheRS
Gene namesi
Name:FARSA
Synonyms:FARS, FARSL, FARSLA
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 19

Organism-specific databases

HGNCiHGNC:3592. FARSA.

Subcellular locationi

Cytoplasm By similarity

GO - Cellular componenti

  1. cytoplasm Source: ProtInc
  2. cytosol Source: Reactome
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA28005.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed2 Publications
Chaini2 – 508507Phenylalanine--tRNA ligase alpha subunitPRO_0000126824Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylalanine4 Publications
Modified residuei193 – 1931Phosphoserine1 Publication
Modified residuei311 – 3111N6-acetyllysine1 Publication

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

MaxQBiQ9Y285.
PaxDbiQ9Y285.
PeptideAtlasiQ9Y285.
PRIDEiQ9Y285.

PTM databases

PhosphoSiteiQ9Y285.

Expressioni

Gene expression databases

ArrayExpressiQ9Y285.
BgeeiQ9Y285.
CleanExiHS_FARSA.
GenevestigatoriQ9Y285.

Organism-specific databases

HPAiHPA001911.

Interactioni

Subunit structurei

Tetramer of two alpha and two beta subunits By similarity.

Binary interactionsi

WithEntry#Exp.IntActNotes
ECSITQ9BQ952EBI-725361,EBI-712452

Protein-protein interaction databases

BioGridi108487. 27 interactions.
DIPiDIP-53610N.
IntActiQ9Y285. 10 interactions.
MINTiMINT-1378519.
STRINGi9606.ENSP00000320309.

Structurei

Secondary structure

1
508
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Turni194 – 1985
Turni201 – 2044
Beta strandi212 – 2143
Helixi226 – 24015
Beta strandi251 – 2544
Helixi255 – 2584
Helixi260 – 2623
Beta strandi266 – 2683
Turni273 – 2753
Beta strandi278 – 2803
Helixi290 – 30112
Helixi316 – 3194
Beta strandi321 – 3244
Helixi329 – 34012
Beta strandi342 – 3443
Beta strandi348 – 35710
Beta strandi364 – 3663
Beta strandi368 – 38114
Helixi384 – 39613
Turni397 – 3993
Beta strandi404 – 4074
Beta strandi414 – 4218
Beta strandi430 – 4367
Helixi440 – 4434
Helixi444 – 4463
Beta strandi452 – 46110
Helixi462 – 4654
Turni466 – 4705
Helixi474 – 4763
Helixi484 – 4896
Turni497 – 4993

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3L4GX-ray3.30A/C/E/G/I/K/M/O1-508[»]
ProteinModelPortaliQ9Y285.
SMRiQ9Y285. Positions 1-508.

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

eggNOGiCOG0016.
HOGENOMiHOG000230294.
HOVERGENiHBG068046.
InParanoidiQ9Y285.
KOiK01889.
PhylomeDBiQ9Y285.
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.

Q9Y285-1 [UniParc]FASTAAdd to Basket

« Hide

MADGQVAELL LRRLEASDGG LDSAELAAEL GMEHQAVVGA VKSLQALGEV    50
IEAELRSTKH WELTAEGEEI AREGSHEARV FRSIPPEGLA QSELMRLPSG 100
KVGFSKAMSN KWIRVDKSAA DGPRVFRVVD SMEDEVQRRL QLVRGGQAEK 150
LGEKERSELR KRKLLAEVTL KTYWVSKGSA FSTSISKQET ELSPEMISSG 200
SWRDRPFKPY NFLAHGVLPD SGHLHPLLKV RSQFRQIFLE MGFTEMPTDN 250
FIESSFWNFD ALFQPQQHPA RDQHDTFFLR DPAEALQLPM DYVQRVKRTH 300
SQGGYGSQGY KYNWKLDEAR KNLLRTHTTS ASARALYRLA QKKPFTPVKY 350
FSIDRVFRNE TLDATHLAEF HQIEGVVADH GLTLGHLMGV LREFFTKLGI 400
TQLRFKPAYN PYTEPSMEVF SYHQGLKKWV EVGNSGVFRP EMLLPMGLPE 450
NVSVIAWGLS LERPTMIKYG INNIRELVGH KVNLQMVYDS PLCRLDAEPR 500
PPPTQEAA 508
Length:508
Mass (Da):57,564
Last modified:January 23, 2007 - v3
Checksum:i99BC12E1F3C5FCFD
GO

Sequence cautioni

The sequence AAB51175.1 differs from that shown. Reason: Erroneous gene model prediction.

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti341 – 3411Q → R.
Corresponds to variant rs35087277 [ dbSNP | Ensembl ].
VAR_052641

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti179 – 1791S → G in BAA95666. 1 Publication
Sequence conflicti376 – 3761V → L in BAA95666. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
U07424 mRNA. Translation: AAB61694.1.
AF042347 mRNA. Translation: AAD02221.1.
D84471 mRNA. Translation: BAA95666.1.
BT007198 mRNA. Translation: AAP35862.1.
AD000092 Genomic DNA. Translation: AAB51175.1. Sequence problems.
BC006495 mRNA. Translation: AAH06495.1.
BC043565 mRNA. Translation: AAH43565.1.
CCDSiCCDS12287.1.
PIRiT45074.
RefSeqiNP_004452.1. NM_004461.2.
UniGeneiHs.23111.

Genome annotation databases

EnsembliENST00000314606; ENSP00000320309; ENSG00000179115.
GeneIDi2193.
KEGGihsa:2193.
UCSCiuc002mvs.2. human.

Polymorphism databases

DMDMi12643946.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
U07424 mRNA. Translation: AAB61694.1 .
AF042347 mRNA. Translation: AAD02221.1 .
D84471 mRNA. Translation: BAA95666.1 .
BT007198 mRNA. Translation: AAP35862.1 .
AD000092 Genomic DNA. Translation: AAB51175.1 . Sequence problems.
BC006495 mRNA. Translation: AAH06495.1 .
BC043565 mRNA. Translation: AAH43565.1 .
CCDSi CCDS12287.1.
PIRi T45074.
RefSeqi NP_004452.1. NM_004461.2.
UniGenei Hs.23111.

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 A/C/E/G/I/K/M/O 1-508 [» ]
ProteinModelPortali Q9Y285.
SMRi Q9Y285. Positions 1-508.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 108487. 27 interactions.
DIPi DIP-53610N.
IntActi Q9Y285. 10 interactions.
MINTi MINT-1378519.
STRINGi 9606.ENSP00000320309.

Chemistry

DrugBanki DB00120. L-Phenylalanine.

PTM databases

PhosphoSitei Q9Y285.

Polymorphism databases

DMDMi 12643946.

Proteomic databases

MaxQBi Q9Y285.
PaxDbi Q9Y285.
PeptideAtlasi Q9Y285.
PRIDEi Q9Y285.

Protocols and materials databases

DNASUi 2193.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000314606 ; ENSP00000320309 ; ENSG00000179115 .
GeneIDi 2193.
KEGGi hsa:2193.
UCSCi uc002mvs.2. human.

Organism-specific databases

CTDi 2193.
GeneCardsi GC19M013033.
HGNCi HGNC:3592. FARSA.
HPAi HPA001911.
MIMi 602918. gene.
neXtProti NX_Q9Y285.
PharmGKBi PA28005.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG0016.
HOGENOMi HOG000230294.
HOVERGENi HBG068046.
InParanoidi Q9Y285.
KOi K01889.
PhylomeDBi Q9Y285.
TreeFami TF300647.

Enzyme and pathway databases

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

Miscellaneous databases

GeneWikii FARSA_(gene).
GenomeRNAii 2193.
NextBioi 8865.
PROi Q9Y285.
SOURCEi Search...

Gene expression databases

ArrayExpressi Q9Y285.
Bgeei Q9Y285.
CleanExi HS_FARSA.
Genevestigatori Q9Y285.

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

« Hide 'large scale' publications
  1. "Expression of a gene encoding a tRNA synthetase-like protein is enhanced in tumorigenic human myeloid leukemia cells and is cell cycle stage- and differentiation-dependent."
    Sen S., Zhou H., Ripmaster T., Hittelman W.N., Schimmel P., White R.A.
    Proc. Natl. Acad. Sci. U.S.A. 94:6164-6169(1997) [PubMed] [Europe PMC] [Abstract]
    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. Motegi H., Noda T., Shiba K.
    Submitted (APR-1996) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Tissue: Testis.
  4. "Cloning of human full-length CDSs in BD Creator(TM) system donor vector."
    Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., Phelan M., Farmer A.
    Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
  5. "The DNA sequence and biology of human chromosome 19."
    Grimwood J., Gordon L.A., Olsen A.S., Terry A., Schmutz J., Lamerdin J.E., Hellsten U., Goodstein D., Couronne O., Tran-Gyamfi M., Aerts A., Altherr M., Ashworth L., Bajorek E., Black S., Branscomb E., Caenepeel S., Carrano A.V.
    , Caoile C., Chan Y.M., Christensen M., Cleland C.A., Copeland A., Dalin E., Dehal P., Denys M., Detter J.C., Escobar J., Flowers D., Fotopulos D., Garcia C., Georgescu A.M., Glavina T., Gomez M., Gonzales E., Groza M., Hammon N., Hawkins T., Haydu L., Ho I., Huang W., Israni S., Jett J., Kadner K., Kimball H., Kobayashi A., Larionov V., Leem S.-H., Lopez F., Lou Y., Lowry S., Malfatti S., Martinez D., McCready P.M., Medina C., Morgan J., Nelson K., Nolan M., Ovcharenko I., Pitluck S., Pollard M., Popkie A.P., Predki P., Quan G., Ramirez L., Rash S., Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A., She X., Smith D., Slezak T., Solovyev V., Thayer N., Tice H., Tsai M., Ustaszewska A., Vo N., Wagner M., Wheeler J., Wu K., Xie G., Yang J., Dubchak I., Furey T.S., DeJong P., Dickson M., Gordon D., Eichler E.E., Pennacchio L.A., Richardson P., Stubbs L., Rokhsar D.S., Myers R.M., Rubin E.M., Lucas S.M.
    Nature 428:529-535(2004) [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: Leukocyte and Lung.
  7. "Exploring proteomes and analyzing protein processing by mass spectrometric identification of sorted N-terminal peptides."
    Gevaert K., Goethals M., Martens L., Van Damme J., Staes A., Thomas G.R., Vandekerckhove J.
    Nat. Biotechnol. 21:566-569(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 2-12.
    Tissue: Platelet.
  8. Bienvenut W.V.
    Submitted (OCT-2004) to UniProtKB
    Cited for: PROTEIN SEQUENCE OF 2-12 AND 326-334, ACETYLATION AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY.
    Tissue: B-cell lymphoma.
  9. "Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle."
    Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., Greff Z., Keri G., Stemmann O., Mann M.
    Mol. Cell 31:438-448(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-193, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  10. "Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
    Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
    Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  11. "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-311, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  12. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  13. "Comparative large-scale characterisation of plant vs. mammal proteins reveals similar and idiosyncratic N-alpha acetylation features."
    Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T., Giglione C.
    Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  14. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiSYFA_HUMAN
AccessioniPrimary (citable) accession number: Q9Y285
Secondary accession number(s): Q9NSD8, Q9Y4W8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 8, 2000
Last sequence update: January 23, 2007
Last modified: September 3, 2014
This is version 144 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, Direct protein sequencing, Reference proteome

Documents

  1. Aminoacyl-tRNA synthetases
    List of aminoacyl-tRNA synthetase entries
  2. Human chromosome 19
    Human chromosome 19: 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

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