Full text data of FARSA
FARSA
(FARS, FARSL, FARSLA)
[Confidence: medium (present in either hRBCD or BSc_CH or PM22954596)]
Phenylalanine--tRNA ligase alpha subunit; 6.1.1.20 (CML33; Phenylalanyl-tRNA synthetase alpha subunit; PheRS)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
Phenylalanine--tRNA ligase alpha subunit; 6.1.1.20 (CML33; Phenylalanyl-tRNA synthetase alpha subunit; PheRS)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
UniProt
Q9Y285
ID SYFA_HUMAN Reviewed; 508 AA.
AC Q9Y285; Q9NSD8; Q9Y4W8;
DT 08-DEC-2000, integrated into UniProtKB/Swiss-Prot.
read moreDT 23-JAN-2007, sequence version 3.
DT 22-JAN-2014, entry version 137.
DE RecName: Full=Phenylalanine--tRNA ligase alpha subunit;
DE EC=6.1.1.20;
DE AltName: Full=CML33;
DE AltName: Full=Phenylalanyl-tRNA synthetase alpha subunit;
DE Short=PheRS;
GN Name=FARSA; Synonyms=FARS, FARSL, FARSLA;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=9177188; DOI=10.1073/pnas.94.12.6164;
RA Sen S., Zhou H., Ripmaster T., Hittelman W.N., Schimmel P.,
RA White R.A.;
RT "Expression of a gene encoding a tRNA synthetase-like protein is
RT enhanced in tumorigenic human myeloid leukemia cells and is cell cycle
RT stage- and differentiation-dependent.";
RL Proc. Natl. Acad. Sci. U.S.A. 94:6164-6169(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=10049785; DOI=10.1006/bbrc.1999.0141;
RA Rodova M., Ankilova V., Safro M.G.;
RT "Human phenylalanyl-tRNA synthetase: cloning, characterization of the
RT deduced amino acid sequences in terms of the structural domains and
RT coordinately regulated expression of the alpha and beta subunits in
RT chronic myeloid leukemia cells.";
RL Biochem. Biophys. Res. Commun. 255:765-773(1999).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Testis;
RA Motegi H., Noda T., Shiba K.;
RL Submitted (APR-1996) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S.,
RA Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y.,
RA Phelan M., Farmer A.;
RT "Cloning of human full-length CDSs in BD Creator(TM) system donor
RT vector.";
RL Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15057824; DOI=10.1038/nature02399;
RA Grimwood J., Gordon L.A., Olsen A.S., Terry A., Schmutz J.,
RA Lamerdin J.E., Hellsten U., Goodstein D., Couronne O., Tran-Gyamfi M.,
RA Aerts A., Altherr M., Ashworth L., Bajorek E., Black S., Branscomb E.,
RA Caenepeel S., Carrano A.V., Caoile C., Chan Y.M., Christensen M.,
RA Cleland C.A., Copeland A., Dalin E., Dehal P., Denys M., Detter J.C.,
RA Escobar J., Flowers D., Fotopulos D., Garcia C., Georgescu A.M.,
RA Glavina T., Gomez M., Gonzales E., Groza M., Hammon N., Hawkins T.,
RA Haydu L., Ho I., Huang W., Israni S., Jett J., Kadner K., Kimball H.,
RA Kobayashi A., Larionov V., Leem S.-H., Lopez F., Lou Y., Lowry S.,
RA Malfatti S., Martinez D., McCready P.M., Medina C., Morgan J.,
RA Nelson K., Nolan M., Ovcharenko I., Pitluck S., Pollard M.,
RA Popkie A.P., Predki P., Quan G., Ramirez L., Rash S., Retterer J.,
RA Rodriguez A., Rogers S., Salamov A., Salazar A., She X., Smith D.,
RA Slezak T., Solovyev V., Thayer N., Tice H., Tsai M., Ustaszewska A.,
RA Vo N., Wagner M., Wheeler J., Wu K., Xie G., Yang J., Dubchak I.,
RA Furey T.S., DeJong P., Dickson M., Gordon D., Eichler E.E.,
RA Pennacchio L.A., Richardson P., Stubbs L., Rokhsar D.S., Myers R.M.,
RA Rubin E.M., Lucas S.M.;
RT "The DNA sequence and biology of human chromosome 19.";
RL Nature 428:529-535(2004).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Leukocyte, and Lung;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [7]
RP PROTEIN SEQUENCE OF 2-12.
RC TISSUE=Platelet;
RX PubMed=12665801; DOI=10.1038/nbt810;
RA Gevaert K., Goethals M., Martens L., Van Damme J., Staes A.,
RA Thomas G.R., Vandekerckhove J.;
RT "Exploring proteomes and analyzing protein processing by mass
RT spectrometric identification of sorted N-terminal peptides.";
RL Nat. Biotechnol. 21:566-569(2003).
RN [8]
RP PROTEIN SEQUENCE OF 2-12 AND 326-334, ACETYLATION AT ALA-2, AND MASS
RP SPECTROMETRY.
RC TISSUE=B-cell lymphoma;
RA Bienvenut W.V.;
RL Submitted (OCT-2004) to UniProtKB.
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-193, AND MASS
RP SPECTROMETRY.
RC TISSUE=Cervix carcinoma;
RX PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007;
RA Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,
RA Greff Z., Keri G., Stemmann O., Mann M.;
RT "Kinase-selective enrichment enables quantitative phosphoproteomics of
RT the kinome across the cell cycle.";
RL Mol. Cell 31:438-448(2008).
RN [10]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, AND MASS SPECTROMETRY.
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,
RA Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in
RT a refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [11]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-311, AND MASS SPECTROMETRY.
RX PubMed=19608861; DOI=10.1126/science.1175371;
RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M.,
RA Walther T.C., Olsen J.V., Mann M.;
RT "Lysine acetylation targets protein complexes and co-regulates major
RT cellular functions.";
RL Science 325:834-840(2009).
RN [12]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
RA Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [13]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, AND MASS SPECTROMETRY.
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E.,
RA Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K.,
RA Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-
RT terminal acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
CC -!- CATALYTIC ACTIVITY: ATP + L-phenylalanine + tRNA(Phe) = AMP +
CC diphosphate + L-phenylalanyl-tRNA(Phe).
CC -!- SUBUNIT: Tetramer of two alpha and two beta subunits (By
CC similarity).
CC -!- INTERACTION:
CC Q9BQ95:ECSIT; NbExp=2; IntAct=EBI-725361, EBI-712452;
CC -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity).
CC -!- SIMILARITY: Belongs to the class-II aminoacyl-tRNA synthetase
CC family. Phe-tRNA synthetase alpha subunit type 2 subfamily.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAB51175.1; Type=Erroneous gene model prediction;
CC -----------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution-NoDerivs License
CC -----------------------------------------------------------------------
DR EMBL; U07424; AAB61694.1; -; mRNA.
DR EMBL; AF042347; AAD02221.1; -; mRNA.
DR EMBL; D84471; BAA95666.1; -; mRNA.
DR EMBL; BT007198; AAP35862.1; -; mRNA.
DR EMBL; AD000092; AAB51175.1; ALT_SEQ; Genomic_DNA.
DR EMBL; BC006495; AAH06495.1; -; mRNA.
DR EMBL; BC043565; AAH43565.1; -; mRNA.
DR PIR; T45074; T45074.
DR RefSeq; NP_004452.1; NM_004461.2.
DR UniGene; Hs.23111; -.
DR PDB; 3L4G; X-ray; 3.30 A; A/C/E/G/I/K/M/O=1-508.
DR PDBsum; 3L4G; -.
DR ProteinModelPortal; Q9Y285; -.
DR SMR; Q9Y285; 1-508.
DR DIP; DIP-53610N; -.
DR IntAct; Q9Y285; 9.
DR MINT; MINT-1378519; -.
DR STRING; 9606.ENSP00000320309; -.
DR DrugBank; DB00120; L-Phenylalanine.
DR PhosphoSite; Q9Y285; -.
DR DMDM; 12643946; -.
DR PaxDb; Q9Y285; -.
DR PeptideAtlas; Q9Y285; -.
DR PRIDE; Q9Y285; -.
DR DNASU; 2193; -.
DR Ensembl; ENST00000314606; ENSP00000320309; ENSG00000179115.
DR GeneID; 2193; -.
DR KEGG; hsa:2193; -.
DR UCSC; uc002mvs.2; human.
DR CTD; 2193; -.
DR GeneCards; GC19M013033; -.
DR HGNC; HGNC:3592; FARSA.
DR HPA; HPA001911; -.
DR MIM; 602918; gene.
DR neXtProt; NX_Q9Y285; -.
DR PharmGKB; PA28005; -.
DR eggNOG; COG0016; -.
DR HOGENOM; HOG000230294; -.
DR HOVERGEN; HBG068046; -.
DR InParanoid; Q9Y285; -.
DR KO; K01889; -.
DR PhylomeDB; Q9Y285; -.
DR BRENDA; 6.1.1.20; 2681.
DR Reactome; REACT_71; Gene Expression.
DR GeneWiki; FARSA_(gene); -.
DR GenomeRNAi; 2193; -.
DR NextBio; 8865; -.
DR PRO; PR:Q9Y285; -.
DR ArrayExpress; Q9Y285; -.
DR Bgee; Q9Y285; -.
DR CleanEx; HS_FARSA; -.
DR Genevestigator; Q9Y285; -.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004826; F:phenylalanine-tRNA ligase activity; TAS:ProtInc.
DR GO; GO:0000049; F:tRNA binding; IEA:InterPro.
DR GO; GO:0006432; P:phenylalanyl-tRNA aminoacylation; IEA:InterPro.
DR GO; GO:0006418; P:tRNA aminoacylation for protein translation; TAS:Reactome.
DR Gene3D; 1.10.10.10; -; 1.
DR InterPro; IPR006195; aa-tRNA-synth_II.
DR InterPro; IPR004529; Phe-tRNA-synth_IIc_asu.
DR InterPro; IPR002319; Phenylalanyl-tRNA_Synthase.
DR InterPro; IPR011991; WHTH_DNA-bd_dom.
DR Pfam; PF01409; tRNA-synt_2d; 1.
DR TIGRFAMs; TIGR00468; pheS; 1.
DR PROSITE; PS50862; AA_TRNA_LIGASE_II; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Aminoacyl-tRNA synthetase; ATP-binding;
KW Complete proteome; Cytoplasm; Direct protein sequencing; Ligase;
KW Nucleotide-binding; Phosphoprotein; Polymorphism;
KW Protein biosynthesis; Reference proteome.
FT INIT_MET 1 1 Removed.
FT CHAIN 2 508 Phenylalanine--tRNA ligase alpha subunit.
FT /FTId=PRO_0000126824.
FT MOD_RES 2 2 N-acetylalanine.
FT MOD_RES 193 193 Phosphoserine.
FT MOD_RES 311 311 N6-acetyllysine.
FT VARIANT 341 341 Q -> R (in dbSNP:rs35087277).
FT /FTId=VAR_052641.
FT CONFLICT 179 179 S -> G (in Ref. 3; BAA95666).
FT CONFLICT 376 376 V -> L (in Ref. 3; BAA95666).
FT TURN 194 198
FT TURN 201 204
FT STRAND 212 214
FT HELIX 226 240
FT STRAND 251 254
FT HELIX 255 258
FT HELIX 260 262
FT STRAND 266 268
FT TURN 273 275
FT STRAND 278 280
FT HELIX 290 301
FT HELIX 316 319
FT STRAND 321 324
FT HELIX 329 340
FT STRAND 342 344
FT STRAND 348 357
FT STRAND 364 366
FT STRAND 368 381
FT HELIX 384 396
FT TURN 397 399
FT STRAND 404 407
FT STRAND 414 421
FT STRAND 430 436
FT HELIX 440 443
FT HELIX 444 446
FT STRAND 452 461
FT HELIX 462 465
FT TURN 466 470
FT HELIX 474 476
FT HELIX 484 489
FT TURN 497 499
SQ SEQUENCE 508 AA; 57564 MW; 99BC12E1F3C5FCFD CRC64;
MADGQVAELL LRRLEASDGG LDSAELAAEL GMEHQAVVGA VKSLQALGEV IEAELRSTKH
WELTAEGEEI AREGSHEARV FRSIPPEGLA QSELMRLPSG KVGFSKAMSN KWIRVDKSAA
DGPRVFRVVD SMEDEVQRRL QLVRGGQAEK LGEKERSELR KRKLLAEVTL KTYWVSKGSA
FSTSISKQET ELSPEMISSG SWRDRPFKPY NFLAHGVLPD SGHLHPLLKV RSQFRQIFLE
MGFTEMPTDN FIESSFWNFD ALFQPQQHPA RDQHDTFFLR DPAEALQLPM DYVQRVKRTH
SQGGYGSQGY KYNWKLDEAR KNLLRTHTTS ASARALYRLA QKKPFTPVKY FSIDRVFRNE
TLDATHLAEF HQIEGVVADH GLTLGHLMGV LREFFTKLGI TQLRFKPAYN PYTEPSMEVF
SYHQGLKKWV EVGNSGVFRP EMLLPMGLPE NVSVIAWGLS LERPTMIKYG INNIRELVGH
KVNLQMVYDS PLCRLDAEPR PPPTQEAA
//
ID SYFA_HUMAN Reviewed; 508 AA.
AC Q9Y285; Q9NSD8; Q9Y4W8;
DT 08-DEC-2000, integrated into UniProtKB/Swiss-Prot.
read moreDT 23-JAN-2007, sequence version 3.
DT 22-JAN-2014, entry version 137.
DE RecName: Full=Phenylalanine--tRNA ligase alpha subunit;
DE EC=6.1.1.20;
DE AltName: Full=CML33;
DE AltName: Full=Phenylalanyl-tRNA synthetase alpha subunit;
DE Short=PheRS;
GN Name=FARSA; Synonyms=FARS, FARSL, FARSLA;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=9177188; DOI=10.1073/pnas.94.12.6164;
RA Sen S., Zhou H., Ripmaster T., Hittelman W.N., Schimmel P.,
RA White R.A.;
RT "Expression of a gene encoding a tRNA synthetase-like protein is
RT enhanced in tumorigenic human myeloid leukemia cells and is cell cycle
RT stage- and differentiation-dependent.";
RL Proc. Natl. Acad. Sci. U.S.A. 94:6164-6169(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=10049785; DOI=10.1006/bbrc.1999.0141;
RA Rodova M., Ankilova V., Safro M.G.;
RT "Human phenylalanyl-tRNA synthetase: cloning, characterization of the
RT deduced amino acid sequences in terms of the structural domains and
RT coordinately regulated expression of the alpha and beta subunits in
RT chronic myeloid leukemia cells.";
RL Biochem. Biophys. Res. Commun. 255:765-773(1999).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Testis;
RA Motegi H., Noda T., Shiba K.;
RL Submitted (APR-1996) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S.,
RA Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y.,
RA Phelan M., Farmer A.;
RT "Cloning of human full-length CDSs in BD Creator(TM) system donor
RT vector.";
RL Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15057824; DOI=10.1038/nature02399;
RA Grimwood J., Gordon L.A., Olsen A.S., Terry A., Schmutz J.,
RA Lamerdin J.E., Hellsten U., Goodstein D., Couronne O., Tran-Gyamfi M.,
RA Aerts A., Altherr M., Ashworth L., Bajorek E., Black S., Branscomb E.,
RA Caenepeel S., Carrano A.V., Caoile C., Chan Y.M., Christensen M.,
RA Cleland C.A., Copeland A., Dalin E., Dehal P., Denys M., Detter J.C.,
RA Escobar J., Flowers D., Fotopulos D., Garcia C., Georgescu A.M.,
RA Glavina T., Gomez M., Gonzales E., Groza M., Hammon N., Hawkins T.,
RA Haydu L., Ho I., Huang W., Israni S., Jett J., Kadner K., Kimball H.,
RA Kobayashi A., Larionov V., Leem S.-H., Lopez F., Lou Y., Lowry S.,
RA Malfatti S., Martinez D., McCready P.M., Medina C., Morgan J.,
RA Nelson K., Nolan M., Ovcharenko I., Pitluck S., Pollard M.,
RA Popkie A.P., Predki P., Quan G., Ramirez L., Rash S., Retterer J.,
RA Rodriguez A., Rogers S., Salamov A., Salazar A., She X., Smith D.,
RA Slezak T., Solovyev V., Thayer N., Tice H., Tsai M., Ustaszewska A.,
RA Vo N., Wagner M., Wheeler J., Wu K., Xie G., Yang J., Dubchak I.,
RA Furey T.S., DeJong P., Dickson M., Gordon D., Eichler E.E.,
RA Pennacchio L.A., Richardson P., Stubbs L., Rokhsar D.S., Myers R.M.,
RA Rubin E.M., Lucas S.M.;
RT "The DNA sequence and biology of human chromosome 19.";
RL Nature 428:529-535(2004).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Leukocyte, and Lung;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [7]
RP PROTEIN SEQUENCE OF 2-12.
RC TISSUE=Platelet;
RX PubMed=12665801; DOI=10.1038/nbt810;
RA Gevaert K., Goethals M., Martens L., Van Damme J., Staes A.,
RA Thomas G.R., Vandekerckhove J.;
RT "Exploring proteomes and analyzing protein processing by mass
RT spectrometric identification of sorted N-terminal peptides.";
RL Nat. Biotechnol. 21:566-569(2003).
RN [8]
RP PROTEIN SEQUENCE OF 2-12 AND 326-334, ACETYLATION AT ALA-2, AND MASS
RP SPECTROMETRY.
RC TISSUE=B-cell lymphoma;
RA Bienvenut W.V.;
RL Submitted (OCT-2004) to UniProtKB.
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-193, AND MASS
RP SPECTROMETRY.
RC TISSUE=Cervix carcinoma;
RX PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007;
RA Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,
RA Greff Z., Keri G., Stemmann O., Mann M.;
RT "Kinase-selective enrichment enables quantitative phosphoproteomics of
RT the kinome across the cell cycle.";
RL Mol. Cell 31:438-448(2008).
RN [10]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, AND MASS SPECTROMETRY.
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,
RA Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in
RT a refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [11]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-311, AND MASS SPECTROMETRY.
RX PubMed=19608861; DOI=10.1126/science.1175371;
RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M.,
RA Walther T.C., Olsen J.V., Mann M.;
RT "Lysine acetylation targets protein complexes and co-regulates major
RT cellular functions.";
RL Science 325:834-840(2009).
RN [12]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
RA Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [13]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, AND MASS SPECTROMETRY.
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E.,
RA Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K.,
RA Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-
RT terminal acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
CC -!- CATALYTIC ACTIVITY: ATP + L-phenylalanine + tRNA(Phe) = AMP +
CC diphosphate + L-phenylalanyl-tRNA(Phe).
CC -!- SUBUNIT: Tetramer of two alpha and two beta subunits (By
CC similarity).
CC -!- INTERACTION:
CC Q9BQ95:ECSIT; NbExp=2; IntAct=EBI-725361, EBI-712452;
CC -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity).
CC -!- SIMILARITY: Belongs to the class-II aminoacyl-tRNA synthetase
CC family. Phe-tRNA synthetase alpha subunit type 2 subfamily.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAB51175.1; Type=Erroneous gene model prediction;
CC -----------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution-NoDerivs License
CC -----------------------------------------------------------------------
DR EMBL; U07424; AAB61694.1; -; mRNA.
DR EMBL; AF042347; AAD02221.1; -; mRNA.
DR EMBL; D84471; BAA95666.1; -; mRNA.
DR EMBL; BT007198; AAP35862.1; -; mRNA.
DR EMBL; AD000092; AAB51175.1; ALT_SEQ; Genomic_DNA.
DR EMBL; BC006495; AAH06495.1; -; mRNA.
DR EMBL; BC043565; AAH43565.1; -; mRNA.
DR PIR; T45074; T45074.
DR RefSeq; NP_004452.1; NM_004461.2.
DR UniGene; Hs.23111; -.
DR PDB; 3L4G; X-ray; 3.30 A; A/C/E/G/I/K/M/O=1-508.
DR PDBsum; 3L4G; -.
DR ProteinModelPortal; Q9Y285; -.
DR SMR; Q9Y285; 1-508.
DR DIP; DIP-53610N; -.
DR IntAct; Q9Y285; 9.
DR MINT; MINT-1378519; -.
DR STRING; 9606.ENSP00000320309; -.
DR DrugBank; DB00120; L-Phenylalanine.
DR PhosphoSite; Q9Y285; -.
DR DMDM; 12643946; -.
DR PaxDb; Q9Y285; -.
DR PeptideAtlas; Q9Y285; -.
DR PRIDE; Q9Y285; -.
DR DNASU; 2193; -.
DR Ensembl; ENST00000314606; ENSP00000320309; ENSG00000179115.
DR GeneID; 2193; -.
DR KEGG; hsa:2193; -.
DR UCSC; uc002mvs.2; human.
DR CTD; 2193; -.
DR GeneCards; GC19M013033; -.
DR HGNC; HGNC:3592; FARSA.
DR HPA; HPA001911; -.
DR MIM; 602918; gene.
DR neXtProt; NX_Q9Y285; -.
DR PharmGKB; PA28005; -.
DR eggNOG; COG0016; -.
DR HOGENOM; HOG000230294; -.
DR HOVERGEN; HBG068046; -.
DR InParanoid; Q9Y285; -.
DR KO; K01889; -.
DR PhylomeDB; Q9Y285; -.
DR BRENDA; 6.1.1.20; 2681.
DR Reactome; REACT_71; Gene Expression.
DR GeneWiki; FARSA_(gene); -.
DR GenomeRNAi; 2193; -.
DR NextBio; 8865; -.
DR PRO; PR:Q9Y285; -.
DR ArrayExpress; Q9Y285; -.
DR Bgee; Q9Y285; -.
DR CleanEx; HS_FARSA; -.
DR Genevestigator; Q9Y285; -.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004826; F:phenylalanine-tRNA ligase activity; TAS:ProtInc.
DR GO; GO:0000049; F:tRNA binding; IEA:InterPro.
DR GO; GO:0006432; P:phenylalanyl-tRNA aminoacylation; IEA:InterPro.
DR GO; GO:0006418; P:tRNA aminoacylation for protein translation; TAS:Reactome.
DR Gene3D; 1.10.10.10; -; 1.
DR InterPro; IPR006195; aa-tRNA-synth_II.
DR InterPro; IPR004529; Phe-tRNA-synth_IIc_asu.
DR InterPro; IPR002319; Phenylalanyl-tRNA_Synthase.
DR InterPro; IPR011991; WHTH_DNA-bd_dom.
DR Pfam; PF01409; tRNA-synt_2d; 1.
DR TIGRFAMs; TIGR00468; pheS; 1.
DR PROSITE; PS50862; AA_TRNA_LIGASE_II; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Aminoacyl-tRNA synthetase; ATP-binding;
KW Complete proteome; Cytoplasm; Direct protein sequencing; Ligase;
KW Nucleotide-binding; Phosphoprotein; Polymorphism;
KW Protein biosynthesis; Reference proteome.
FT INIT_MET 1 1 Removed.
FT CHAIN 2 508 Phenylalanine--tRNA ligase alpha subunit.
FT /FTId=PRO_0000126824.
FT MOD_RES 2 2 N-acetylalanine.
FT MOD_RES 193 193 Phosphoserine.
FT MOD_RES 311 311 N6-acetyllysine.
FT VARIANT 341 341 Q -> R (in dbSNP:rs35087277).
FT /FTId=VAR_052641.
FT CONFLICT 179 179 S -> G (in Ref. 3; BAA95666).
FT CONFLICT 376 376 V -> L (in Ref. 3; BAA95666).
FT TURN 194 198
FT TURN 201 204
FT STRAND 212 214
FT HELIX 226 240
FT STRAND 251 254
FT HELIX 255 258
FT HELIX 260 262
FT STRAND 266 268
FT TURN 273 275
FT STRAND 278 280
FT HELIX 290 301
FT HELIX 316 319
FT STRAND 321 324
FT HELIX 329 340
FT STRAND 342 344
FT STRAND 348 357
FT STRAND 364 366
FT STRAND 368 381
FT HELIX 384 396
FT TURN 397 399
FT STRAND 404 407
FT STRAND 414 421
FT STRAND 430 436
FT HELIX 440 443
FT HELIX 444 446
FT STRAND 452 461
FT HELIX 462 465
FT TURN 466 470
FT HELIX 474 476
FT HELIX 484 489
FT TURN 497 499
SQ SEQUENCE 508 AA; 57564 MW; 99BC12E1F3C5FCFD CRC64;
MADGQVAELL LRRLEASDGG LDSAELAAEL GMEHQAVVGA VKSLQALGEV IEAELRSTKH
WELTAEGEEI AREGSHEARV FRSIPPEGLA QSELMRLPSG KVGFSKAMSN KWIRVDKSAA
DGPRVFRVVD SMEDEVQRRL QLVRGGQAEK LGEKERSELR KRKLLAEVTL KTYWVSKGSA
FSTSISKQET ELSPEMISSG SWRDRPFKPY NFLAHGVLPD SGHLHPLLKV RSQFRQIFLE
MGFTEMPTDN FIESSFWNFD ALFQPQQHPA RDQHDTFFLR DPAEALQLPM DYVQRVKRTH
SQGGYGSQGY KYNWKLDEAR KNLLRTHTTS ASARALYRLA QKKPFTPVKY FSIDRVFRNE
TLDATHLAEF HQIEGVVADH GLTLGHLMGV LREFFTKLGI TQLRFKPAYN PYTEPSMEVF
SYHQGLKKWV EVGNSGVFRP EMLLPMGLPE NVSVIAWGLS LERPTMIKYG INNIRELVGH
KVNLQMVYDS PLCRLDAEPR PPPTQEAA
//
MIM
602918
*RECORD*
*FIELD* NO
602918
*FIELD* TI
*602918 PHENYLALANINE-tRNA SYNTHETASE, ALPHA SUBUNIT; FARSA
;;PHENYLALANINE-tRNA SYNTHETASE, CYTOPLASMIC, ALPHA SUBUNIT; FRSA;;
read morePHENYLALANINE-tRNA SYNTHETASE-LIKE, ALPHA SUBUNIT; FARSLA;;
CML33
*FIELD* TX
DESCRIPTION
Aminoacyl-tRNA synthetases are enzymes that charge tRNAs with specific
amino acids. Cytoplasmic phenylalanine-tRNA synthetase is a heterodimer
consisting of a catalytic alpha subunit, FARSA, and a regulatory beta
subunit, FARSB (609690) (Rodova et al., 1999).
CLONING
Using subtractive hybridization, Sen et al. (1997) identified a gene
that is differentially expressed between a tumorigenic human acute-phase
chronic myeloid leukemia (CML; 608232) cell line and its nontumorigenic
variant. Sequence analysis of the predicted 508-amino acid protein,
called CML33, revealed that it has homology to the catalytic subunit of
prokaryotic and S. cerevisiae phenylalanyl-tRNA synthetases (PheRS).
Recombinant CML33 reacted with antibodies against sheep liver PheRS on
Western blots. Since CML33 does not have the leader sequence
characteristic of mitochondrial proteins and does not resemble yeast
mitochondrial PheRS, Sen et al. (1997) suggested that it is a subunit of
human cytoplasmic PheRS. Using Northern blot analysis, the authors
determined that CML33 expression is sensitive to the stage of the cell
cycle and to induction of differentiation. Expression of the 1.8-kb
transcript is also substantially enhanced in tumorigenic cells. Sen et
al. (1997) noted that CML33 is the first member of the tRNA synthetase
gene family shown to exhibit this type of regulated expression.
By database analysis, RT-PCR using embryonic kidney cell RNA, and
screening a fetal kidney cDNA library, Rodova et al. (1999) cloned
FARSA. The 508-amino acid protein has a calculated molecular mass of 57
kD. Sequence alignment of FARSA orthologs from multiple species showed
conservation of active site regions and suggested that the heterodimer
of FARSA and FARSB forms a 4-helix bundle interface similar to that in
Thermus thermophilus. Northern blot analysis detected a 2.4-kb
transcript in heart, brain, placenta, skeletal muscle, kidney, and
pancreas. Expression was stronger in malignant cell lines compared with
normal tissue.
GENE FUNCTION
Rodova et al. (1999) showed that COS-7 cells transfected with FARSA and
FARSB increase phenylalanine charging of tRNA.
MAPPING
By analysis of a somatic cell hybrid panel, Sen et al. (1997) mapped the
CML33 gene to chromosome 19. Rasooly (1998) noted that the CML33 gene
was contained within genomic clones from chromosomal region 19p13.2
(Genbank GENBANK AD000092).
*FIELD* RF
1. Rasooly, R. S.: Personal Communication. Baltimore, Md. 7/29/1998.
2. Rodova, M.; Ankilova, V.; Safro, M. G.: 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. Biochem.
Biophys. Res. Commun. 255: 765-773, 1999.
3. Sen, S.; Zhou, H.; Ripmaster, T.; Hittelman, W. N.; Schimmel, P.;
White, R. A.: 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. Proc. Nat. Acad.
Sci. 94: 6164-6169, 1997.
*FIELD* CN
Laura L. Baxter - updated: 10/28/2005
*FIELD* CD
Rebekah S. Rasooly: 8/3/1998
*FIELD* ED
wwang: 11/08/2007
wwang: 11/8/2007
wwang: 10/28/2005
alopez: 11/17/2003
alopez: 8/3/1998
*RECORD*
*FIELD* NO
602918
*FIELD* TI
*602918 PHENYLALANINE-tRNA SYNTHETASE, ALPHA SUBUNIT; FARSA
;;PHENYLALANINE-tRNA SYNTHETASE, CYTOPLASMIC, ALPHA SUBUNIT; FRSA;;
read morePHENYLALANINE-tRNA SYNTHETASE-LIKE, ALPHA SUBUNIT; FARSLA;;
CML33
*FIELD* TX
DESCRIPTION
Aminoacyl-tRNA synthetases are enzymes that charge tRNAs with specific
amino acids. Cytoplasmic phenylalanine-tRNA synthetase is a heterodimer
consisting of a catalytic alpha subunit, FARSA, and a regulatory beta
subunit, FARSB (609690) (Rodova et al., 1999).
CLONING
Using subtractive hybridization, Sen et al. (1997) identified a gene
that is differentially expressed between a tumorigenic human acute-phase
chronic myeloid leukemia (CML; 608232) cell line and its nontumorigenic
variant. Sequence analysis of the predicted 508-amino acid protein,
called CML33, revealed that it has homology to the catalytic subunit of
prokaryotic and S. cerevisiae phenylalanyl-tRNA synthetases (PheRS).
Recombinant CML33 reacted with antibodies against sheep liver PheRS on
Western blots. Since CML33 does not have the leader sequence
characteristic of mitochondrial proteins and does not resemble yeast
mitochondrial PheRS, Sen et al. (1997) suggested that it is a subunit of
human cytoplasmic PheRS. Using Northern blot analysis, the authors
determined that CML33 expression is sensitive to the stage of the cell
cycle and to induction of differentiation. Expression of the 1.8-kb
transcript is also substantially enhanced in tumorigenic cells. Sen et
al. (1997) noted that CML33 is the first member of the tRNA synthetase
gene family shown to exhibit this type of regulated expression.
By database analysis, RT-PCR using embryonic kidney cell RNA, and
screening a fetal kidney cDNA library, Rodova et al. (1999) cloned
FARSA. The 508-amino acid protein has a calculated molecular mass of 57
kD. Sequence alignment of FARSA orthologs from multiple species showed
conservation of active site regions and suggested that the heterodimer
of FARSA and FARSB forms a 4-helix bundle interface similar to that in
Thermus thermophilus. Northern blot analysis detected a 2.4-kb
transcript in heart, brain, placenta, skeletal muscle, kidney, and
pancreas. Expression was stronger in malignant cell lines compared with
normal tissue.
GENE FUNCTION
Rodova et al. (1999) showed that COS-7 cells transfected with FARSA and
FARSB increase phenylalanine charging of tRNA.
MAPPING
By analysis of a somatic cell hybrid panel, Sen et al. (1997) mapped the
CML33 gene to chromosome 19. Rasooly (1998) noted that the CML33 gene
was contained within genomic clones from chromosomal region 19p13.2
(Genbank GENBANK AD000092).
*FIELD* RF
1. Rasooly, R. S.: Personal Communication. Baltimore, Md. 7/29/1998.
2. Rodova, M.; Ankilova, V.; Safro, M. G.: 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. Biochem.
Biophys. Res. Commun. 255: 765-773, 1999.
3. Sen, S.; Zhou, H.; Ripmaster, T.; Hittelman, W. N.; Schimmel, P.;
White, R. A.: 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. Proc. Nat. Acad.
Sci. 94: 6164-6169, 1997.
*FIELD* CN
Laura L. Baxter - updated: 10/28/2005
*FIELD* CD
Rebekah S. Rasooly: 8/3/1998
*FIELD* ED
wwang: 11/08/2007
wwang: 11/8/2007
wwang: 10/28/2005
alopez: 11/17/2003
alopez: 8/3/1998