Q9Y285 (SYFA_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

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 names

Name:	FARSA
Synonyms:	FARS, FARSL, FARSLA

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	508 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein 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 subunits By similarity.
Subcellular location	Cytoplasm By similarity.
Sequence similarities	Belongs to the class-II aminoacyl-tRNA synthetase family. Phe-tRNA synthetase alpha subunit type 2 subfamily.
Sequence caution	The sequence AAB51175.1 differs from that shown. Reason: Erroneous gene model prediction.

Ontologies

Keywords
Biological process	Protein biosynthesis
Cellular component	Cytoplasm
Coding sequence diversity	Polymorphism
Ligand	ATP-binding Nucleotide-binding
Molecular function	Aminoacyl-tRNA synthetase Ligase
PTM	Acetylation Phosphoprotein
Technical term	3D-structure Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	phenylalanyl-tRNA aminoacylation Inferred from electronic annotation. Source: InterPro tRNA aminoacylation for protein translation Traceable author statement. Source: Reactome
Cellular_component	cytosol Traceable author statement. Source: Reactome
Molecular_function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW phenylalanine-tRNA ligase activity Traceable author statement Ref.1. Source: ProtInc tRNA binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
ECSIT	Q9BQ95	2	EBI-725361,EBI-712452

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Initiator methionine

1

1

Removed Ref.7 Ref.8

Chain

2 – 508

507

Phenylalanine--tRNA ligase alpha subunit

PRO_0000126824

Amino acid modifications

Modified residue

2

1

N-acetylalanine Ref.8

Modified residue

193

1

Phosphoserine Ref.9

Modified residue

311

1

N6-acetyllysine Ref.10

Natural variations

Natural variant

341

1

Q → R.
Corresponds to variant rs35087277 [ dbSNP | Ensembl ].

VAR_052641

Experimental info

Sequence conflict

179

1

S → G in BAA95666. Ref.3

Sequence conflict

376

1

V → L in BAA95666. Ref.3

Secondary structure

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508

Helix Strand Turn

Details...

Turn

194 – 198

5

Turn

201 – 204

4

Beta strand

212 – 214

3

Helix

226 – 240

15

Beta strand

251 – 254

4

Helix

255 – 258

4

Helix

260 – 262

3

Beta strand

266 – 268

3

Turn

273 – 275

3

Beta strand

278 – 280

3

Helix

290 – 301

12

Helix

316 – 319

4

Beta strand

321 – 324

4

Helix

329 – 340

12

Beta strand

342 – 344

3

Beta strand

348 – 357

10

Beta strand

364 – 366

3

Beta strand

368 – 381

14

Helix

384 – 396

13

Turn

397 – 399

3

Beta strand

404 – 407

4

Beta strand

414 – 421

8

Beta strand

430 – 436

7

Helix

440 – 443

4

Helix

444 – 446

3

Beta strand

452 – 461

10

Helix

462 – 465

4

Turn

466 – 470

5

Helix

474 – 476

3

Helix

484 – 489

6

Turn

497 – 499

3

Sequences

	Sequence		Length	Mass (Da)
	Q9Y285 [UniParc]. Last modified January 23, 2007. Version 3. Checksum: 99BC12E1F3C5FCFD	FASTA	508	57,564
	10 20 30 40 50 60 MADGQVAELL LRRLEASDGG LDSAELAAEL GMEHQAVVGA VKSLQALGEV IEAELRSTKH 70 80 90 100 110 120 WELTAEGEEI AREGSHEARV FRSIPPEGLA QSELMRLPSG KVGFSKAMSN KWIRVDKSAA 130 140 150 160 170 180 DGPRVFRVVD SMEDEVQRRL QLVRGGQAEK LGEKERSELR KRKLLAEVTL KTYWVSKGSA 190 200 210 220 230 240 FSTSISKQET ELSPEMISSG SWRDRPFKPY NFLAHGVLPD SGHLHPLLKV RSQFRQIFLE 250 260 270 280 290 300 MGFTEMPTDN FIESSFWNFD ALFQPQQHPA RDQHDTFFLR DPAEALQLPM DYVQRVKRTH 310 320 330 340 350 360 SQGGYGSQGY KYNWKLDEAR KNLLRTHTTS ASARALYRLA QKKPFTPVKY FSIDRVFRNE 370 380 390 400 410 420 TLDATHLAEF HQIEGVVADH GLTLGHLMGV LREFFTKLGI TQLRFKPAYN PYTEPSMEVF 430 440 450 460 470 480 SYHQGLKKWV EVGNSGVFRP EMLLPMGLPE NVSVIAWGLS LERPTMIKYG INNIRELVGH 490 500 KVNLQMVYDS PLCRLDAEPR PPPTQEAA

References

	« Hide 'large scale' referencesShow 'large scale' references »
[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, 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, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[10]	"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, MASS SPECTROMETRY.
[11]	"Initial characterization of the human central proteome." Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J. BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

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.

IPI

IPI00031820.

PIR

T45074.

RefSeq

NP_004452.1. NM_004461.2.

UniGene

Hs.23111.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
3L4G	X-ray	3.30	A/C/E/G/I/K/M/O	1-508	[»]

ProteinModelPortal

Q9Y285.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-53610N.

IntAct

Q9Y285. 9 interactions.

MINT

MINT-1378519.

STRING

9606.ENSP00000320309.

PTM databases

PhosphoSite

Q9Y285.

Polymorphism databases

DMDM

12643946.

Proteomic databases

PaxDb

Q9Y285.

PeptideAtlas

Q9Y285.

PRIDE

Q9Y285.

Protocols and materials databases

DNASU

2193.

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000314606; ENSP00000320309; ENSG00000179115.

GeneID

2193.

KEGG

hsa:2193.

UCSC

uc002mvs.2. human.

Organism-specific databases

CTD

2193.

GeneCards

GC19M013033.

HGNC

HGNC:3592. FARSA.

HPA

HPA001911.

MIM

602918. gene.

neXtProt

NX_Q9Y285.

PharmGKB

PA28005.

GenAtlas

Search...

Phylogenomic databases

eggNOG

COG0016.

HOGENOM

HOG000230294.

HOVERGEN

HBG068046.

InParanoid

Q9Y285.

KO

K01889.

OMA

PLMKVRT.

OrthoDB

EOG4CZBFN.

PhylomeDB

Q9Y285.

Enzyme and pathway databases

BRENDA

6.1.1.20. 2681.

Reactome

REACT_71. Gene Expression.

Gene expression databases

ArrayExpress

Q9Y285.

Bgee

Q9Y285.

CleanEx

HS_FARSA.

Genevestigator

Q9Y285.

GermOnline

ENSG00000179115. Homo sapiens.

Family and domain databases

Gene3D

1.10.10.10. 1 hit.

InterPro

IPR006195. aa-tRNA-synth_II.
IPR004529. Phe-tRNA-synth_IIc_asu.
IPR002319. Phenylalanyl-tRNA_Synthase.
IPR011991. WHTH_DNA-bd_dom.
[Graphical view]

Pfam

PF01409. tRNA-synt_2d. 1 hit.
[Graphical view]

TIGRFAMs

TIGR00468. pheS. 1 hit.

PROSITE

PS50862. AA_TRNA_LIGASE_II. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

DrugBank

DB00120. L-Phenylalanine.

GenomeRNAi

2193.

NextBio

8865.

SOURCE

Search...

Entry information

Entry name

SYFA_HUMAN

Accession

Primary (citable) accession number: Q9Y285
Secondary accession number(s): Q9NSD8, Q9Y4W8

Entry history

Integrated into UniProtKB/Swiss-Prot:	December 8, 2000
Last sequence update:	January 23, 2007
Last modified:	May 1, 2013
This is version 132 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.