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Q8C0C7 (SYFA_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 77. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Phenylalanine--tRNA ligase alpha chain
EC=6.1.1.20
Alternative name(s):
Phenylalanyl-tRNA synthetase alpha chain
Short name=PheRS
Gene names
Name:Farsa
Synonyms:Farsla
OrganismMus musculus (Mouse)
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

Protein attributes

Sequence length508 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at transcript level

General annotation (Comments)

Catalytic activity

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

Subunit structure

Tetramer of two alpha and two beta chains By similarity.

Subcellular location

Cytoplasm By similarity.

Sequence similarities

Belongs to the class-II aminoacyl-tRNA synthetase family. Phe-tRNA synthetase alpha chain type 2 subfamily.

Ontologies

Keywords
   Biological processProtein biosynthesis
   Cellular componentCytoplasm
   LigandATP-binding
Nucleotide-binding
   Molecular functionAminoacyl-tRNA synthetase
Ligase
   PTMAcetylation
Phosphoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological processphenylalanyl-tRNA aminoacylation

Inferred from electronic annotation. Source: InterPro

   Cellular componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular functionATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

phenylalanine-tRNA ligase activity

Inferred from electronic annotation. Source: EC

tRNA binding

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed By similarity
Chain2 – 508507Phenylalanine--tRNA ligase alpha chain
PRO_0000280447

Amino acid modifications

Modified residue21N-acetylalanine By similarity
Modified residue1931Phosphoserine By similarity
Modified residue3111N6-acetyllysine By similarity

Experimental info

Sequence conflict2911G → D in AAH06862. Ref.2
Sequence conflict2911G → D in AAH13533. Ref.2
Sequence conflict3431Missing in AAH13533. Ref.2
Sequence conflict4551I → T in AAH06862. Ref.2
Sequence conflict4551I → V in BAE32726. Ref.1

Sequences

Sequence LengthMass (Da)Tools
Q8C0C7 [UniParc].

Last modified March 1, 2003. Version 1.
Checksum: 9C125BC4D4A26DAA

FASTA50857,599
        10         20         30         40         50         60 
MADNPVLELL LRRLEVADGG LDSAELATQL GVEHQAVVGA VKSLQALGEV IEAELRSTKC 

        70         80         90        100        110        120 
WELTTEGEEI AREGSHEARV FRSIPLEGLV QSELMHLPSG KVGFSKAMSN KWIRVDKSAA 

       130        140        150        160        170        180 
DGPRVFRVVD SIEDEVQKRL QLVQAGQAEK LAEKERNELR KRKLLTEVIL KTYWVSKGKA 

       190        200        210        220        230        240 
FSTSVSKQEA ELSPEMISSG SWRDRPFKPY NFSARGVLPD SGHLHPLLKV RSQFRQIFLE 

       250        260        270        280        290        300 
MGFTEMPTDN FIESSFWNFD ALFQPQQHPA RDQHDTFFLR DPAEALQLPM GYVQRVKRTH 

       310        320        330        340        350        360 
SQGGYGSQGY KYTWKLEEAR KNLLRTHTTA ASARALYQLA QKKPFTPAKY FSIDRVFRNE 

       370        380        390        400        410        420 
TLDATHLAEF HQIEGVIADH GLTLGHLMGV LREFFTKLGI TQLRFKPAYN PYTEPSMEVF 

       430        440        450        460        470        480 
SYHQGLKKWV EVGNSGVFRP EMLLPMGLPE NVSVIAWGLS LERPTMIKYG INNIRELVGH 

       490        500 
KVNLQMVYDS PVCRLDIEPR SSKTQEAA

« Hide

References

[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. expand/collapse author list , 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: 16141072] [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: 15489334] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: FVB/N.
Tissue: Kidney and Mammary tumor.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		AK031697 mRNA. Translation: BAC27519.1.
AK154629 mRNA. Translation: BAE32726.1.
BC006862 mRNA. Translation: AAH06862.1.
BC013533 mRNA. Translation: AAH13533.1.
IPIIPI00263874.
RefSeqNP_079924.2. NM_025648.3.
UniGeneMm.292517.

3D structure databases

HSSPHSSP built from PDB template 2ALY based on UniProtKB P27001.
ProteinModelPortalQ8C0C7.
SMRQ8C0C7. Positions 1-508.
ModBaseSearch...

Protein-protein interaction databases

IntActQ8C0C7. 1 interaction.
STRINGQ8C0C7.

PTM databases

PhosphoSiteQ8C0C7.

Proteomic databases

PRIDEQ8C0C7.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000003906; ENSMUSP00000003906; ENSMUSG00000003808.
GeneID66590.
KEGGmmu:66590.
NMPDRfig|10090.3.peg.18881.
UCSCuc009mns.2. mouse.

Organism-specific databases

CTD2193.
MGIMGI:1913840. Farsa.

Phylogenomic databases

HOGENOMHBG497668.
HOVERGENHBG068046.
InParanoidQ8C0C7.
OMAFKPYNFL.
OrthoDBEOG4CZBFN.
PhylomeDBQ8C0C7.

Gene expression databases

ArrayExpressQ8C0C7.
BgeeQ8C0C7.
CleanExMM_FARSA.
GenevestigatorQ8C0C7.

Family and domain databases

InterProIPR006195. aa-tRNA-synth_II.
IPR013196. HTH_11.
IPR004529. Phe-tRNA-synth_IIc_asu.
IPR002319. Phenylalanyl-tRNA_Synthase.
IPR011991. WHTH_trsnscrt_rep_DNA-bd.
[Graphical view]
Gene3DG3DSA:1.10.10.10. Wing_hlx_DNA_bd. 1 hit.
KOK01889.
PfamPF08279. HTH_11. 1 hit.
PF01409. tRNA-synt_2d. 1 hit.
[Graphical view]
TIGRFAMsTIGR00468. PheS. 1 hit.
PROSITEPS50862. AA_TRNA_LIGASE_II. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio322092.
SOURCESearch...

Entry information

Entry nameSYFA_MOUSE
AccessionPrimary (citable) accession number: Q8C0C7
Secondary accession number(s): Q3U3Q9, Q91WR4, Q922S1
Entry history
Integrated into UniProtKB/Swiss-Prot: March 20, 2007
Last sequence update: March 1, 2003
Last modified: January 25, 2012
This is version 77 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

Aminoacyl-tRNA synthetases

List of aminoacyl-tRNA synthetase entries

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot

SIMILARITY comments

Index of protein domains and families

to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents