Full text data of FARSB
FARSB
(FARSLB, FRSB)
[Confidence: medium (present in either hRBCD or BSc_CH or PM22954596)]
Phenylalanine--tRNA ligase beta subunit; 6.1.1.20 (Phenylalanyl-tRNA synthetase beta subunit; PheRS)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
Phenylalanine--tRNA ligase beta subunit; 6.1.1.20 (Phenylalanyl-tRNA synthetase beta subunit; PheRS)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
UniProt
Q9NSD9
ID SYFB_HUMAN Reviewed; 589 AA.
AC Q9NSD9; O95708; Q4ZFX1; Q57ZJ5; Q9NZZ6;
DT 08-DEC-2000, integrated into UniProtKB/Swiss-Prot.
read moreDT 18-MAY-2010, sequence version 3.
DT 22-JAN-2014, entry version 128.
DE RecName: Full=Phenylalanine--tRNA ligase beta subunit;
DE EC=6.1.1.20;
DE AltName: Full=Phenylalanyl-tRNA synthetase beta subunit;
DE Short=PheRS;
GN Name=FARSB; Synonyms=FARSLB, FRSB; ORFNames=HSPC173;
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].
RA Motegi H., Noda T., Shiba K.;
RL Submitted (APR-1996) to the EMBL/GenBank/DDBJ databases.
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 [LARGE SCALE MRNA].
RC TISSUE=Umbilical cord blood;
RX PubMed=11042152; DOI=10.1101/gr.140200;
RA Zhang Q.-H., Ye M., Wu X.-Y., Ren S.-X., Zhao M., Zhao C.-J., Fu G.,
RA Shen Y., Fan H.-Y., Lu G., Zhong M., Xu X.-R., Han Z.-G., Zhang J.-W.,
RA Tao J., Huang Q.-H., Zhou J., Hu G.-X., Gu J., Chen S.-J., Chen Z.;
RT "Cloning and functional analysis of cDNAs with open reading frames for
RT 300 previously undefined genes expressed in CD34+ hematopoietic
RT stem/progenitor cells.";
RL Genome Res. 10:1546-1560(2000).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15815621; DOI=10.1038/nature03466;
RA Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H.,
RA Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M.,
RA Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E.,
RA Kremitzki C., Oddy L., Du H., Sun H., Bradshaw-Cordum H., Ali J.,
RA Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C.,
RA Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J.,
RA Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A.,
RA Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K.,
RA Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M.,
RA Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K.,
RA McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C.,
RA Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N.,
RA Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M.,
RA Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E.,
RA Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P.,
RA Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A.,
RA Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A.,
RA Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T.,
RA Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D.,
RA Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X.,
RA McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C.,
RA Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S.,
RA Miller W., Eichler E.E., Bork P., Suyama M., Torrents D.,
RA Waterston R.H., Wilson R.K.;
RT "Generation and annotation of the DNA sequences of human chromosomes 2
RT and 4.";
RL Nature 434:724-731(2005).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Testis;
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 [6]
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 [7]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
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 -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity).
CC -!- SIMILARITY: Belongs to the phenylalanyl-tRNA synthetase beta
CC subunit family. Type 2 subfamily.
CC -!- SIMILARITY: Contains 1 B5 domain.
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; D84430; BAA95608.1; -; mRNA.
DR EMBL; AF042346; AAD02220.1; -; mRNA.
DR EMBL; AF161521; AAF29136.1; -; mRNA.
DR EMBL; AC097461; AAX88958.1; -; Genomic_DNA.
DR EMBL; AC104772; AAX81986.1; -; Genomic_DNA.
DR EMBL; BC017783; AAH17783.1; -; mRNA.
DR RefSeq; NP_005678.3; NM_005687.3.
DR UniGene; Hs.471452; -.
DR PDB; 3L4G; X-ray; 3.30 A; B/D/F/H/J/L/N/P=1-589.
DR PDBsum; 3L4G; -.
DR ProteinModelPortal; Q9NSD9; -.
DR SMR; Q9NSD9; 1-589.
DR DIP; DIP-32869N; -.
DR IntAct; Q9NSD9; 7.
DR MINT; MINT-3073662; -.
DR STRING; 9606.ENSP00000281828; -.
DR DrugBank; DB00120; L-Phenylalanine.
DR PhosphoSite; Q9NSD9; -.
DR DMDM; 296452943; -.
DR PaxDb; Q9NSD9; -.
DR PRIDE; Q9NSD9; -.
DR Ensembl; ENST00000281828; ENSP00000281828; ENSG00000116120.
DR GeneID; 10056; -.
DR KEGG; hsa:10056; -.
DR UCSC; uc002vne.1; human.
DR CTD; 10056; -.
DR GeneCards; GC02M223435; -.
DR H-InvDB; HIX0002878; -.
DR HGNC; HGNC:17800; FARSB.
DR HPA; HPA036678; -.
DR MIM; 609690; gene.
DR neXtProt; NX_Q9NSD9; -.
DR PharmGKB; PA162388068; -.
DR eggNOG; COG0072; -.
DR HOGENOM; HOG000105095; -.
DR HOVERGEN; HBG009523; -.
DR InParanoid; Q9NSD9; -.
DR KO; K01890; -.
DR OMA; SEYCENQ; -.
DR OrthoDB; EOG7R2BJ6; -.
DR PhylomeDB; Q9NSD9; -.
DR BRENDA; 6.1.1.20; 2681.
DR Reactome; REACT_71; Gene Expression.
DR ChiTaRS; FARSB; human.
DR GeneWiki; FARSB; -.
DR GenomeRNAi; 10056; -.
DR NextBio; 37993; -.
DR PRO; PR:Q9NSD9; -.
DR ArrayExpress; Q9NSD9; -.
DR Bgee; Q9NSD9; -.
DR CleanEx; HS_FARSB; -.
DR Genevestigator; Q9NSD9; -.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR GO; GO:0004826; F:phenylalanine-tRNA ligase activity; TAS:ProtInc.
DR GO; GO:0003723; F:RNA 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; 3.30.56.20; -; 1.
DR InterPro; IPR005146; B3/B4_tRNA-bd.
DR InterPro; IPR009061; DNA-bd_dom_put.
DR InterPro; IPR004531; Phe-tRNA-synth_IIc_bsu_arc.
DR InterPro; IPR020825; Phe-tRNA_synthase_B3/B4.
DR InterPro; IPR005147; tRNA_synthase_B5-dom.
DR Pfam; PF03483; B3_4; 1.
DR Pfam; PF03484; B5; 1.
DR SMART; SM00873; B3_4; 1.
DR SMART; SM00874; B5; 1.
DR SUPFAM; SSF46955; SSF46955; 2.
DR SUPFAM; SSF56037; SSF56037; 1.
DR TIGRFAMs; TIGR00471; pheT_arch; 1.
DR PROSITE; PS51483; B5; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Aminoacyl-tRNA synthetase; ATP-binding;
KW Complete proteome; Cytoplasm; Ligase; Nucleotide-binding;
KW Protein biosynthesis; Reference proteome.
FT CHAIN 1 589 Phenylalanine--tRNA ligase beta subunit.
FT /FTId=PRO_0000127016.
FT DOMAIN 302 379 B5.
FT CONFLICT 281 281 Q -> R (in Ref. 3; AAF29136).
FT CONFLICT 555 555 G -> V (in Ref. 1; BAA95608).
FT CONFLICT 585 585 V -> I (in Ref. 1; BAA95608, 2; AAD02220,
FT 3; AAF29136 and 5; AAH17783).
FT STRAND 3 7
FT HELIX 8 15
FT HELIX 23 30
FT STRAND 34 40
FT HELIX 41 45
FT STRAND 48 50
FT STRAND 56 66
FT HELIX 77 87
FT STRAND 97 99
FT STRAND 107 110
FT TURN 112 117
FT STRAND 120 126
FT HELIX 133 145
FT TURN 146 155
FT STRAND 156 163
FT HELIX 164 166
FT STRAND 171 176
FT STRAND 178 180
FT HELIX 194 200
FT TURN 205 214
FT STRAND 220 224
FT TURN 234 236
FT STRAND 237 240
FT STRAND 251 258
FT HELIX 260 274
FT HELIX 275 277
FT STRAND 281 285
FT STRAND 287 290
FT STRAND 296 299
FT STRAND 305 310
FT HELIX 311 318
FT HELIX 324 333
FT STRAND 337 340
FT STRAND 342 351
FT HELIX 361 372
FT HELIX 374 376
FT HELIX 392 406
FT STRAND 416 418
FT HELIX 420 423
FT HELIX 425 427
FT STRAND 438 441
FT HELIX 445 447
FT STRAND 448 450
FT HELIX 455 464
FT TURN 465 467
FT STRAND 472 483
FT STRAND 490 505
FT HELIX 508 521
FT TURN 528 531
FT STRAND 532 537
FT STRAND 543 553
FT STRAND 556 564
FT HELIX 566 571
FT STRAND 578 584
FT HELIX 586 588
SQ SEQUENCE 589 AA; 66116 MW; 6425BA46D124BC08 CRC64;
MPTVSVKRDL LFQALGRTYT DEEFDELCFE FGLELDEITS EKEIISKEQG NVKAAGASDV
VLYKIDVPAN RYDLLCLEGL VRGLQVFKER IKAPVYKRVM PDGKIQKLII TEETAKIRPF
AVAAVLRNIK FTKDRYDSFI ELQEKLHQNI CRKRALVAIG THDLDTLSGP FTYTAKRPSD
IKFKPLNKTK EYTACELMNI YKTDNHLKHY LHIIENKPLY PVIYDSNGVV LSMPPIINGD
HSRITVNTRN IFIECTGTDF TKAKIVLDII VTMFSEYCEN QFTVEAAEVV FPNGKSHTFP
ELAYRKEMVR ADLINKKVGI RETPENLAKL LTRMYLKSEV IGDGNQIEIE IPPTRADIIH
ACDIVEDAAI AYGYNNIQMT LPKTYTIANQ FPLNKLTELL RHDMAAAGFT EALTFALCSQ
EDIADKLGVD ISATKAVHIS NPKTAEFQVA RTTLLPGLLK TIAANRKMPL PLKLFEISDI
VIKDSNTDVG AKNYRHLCAV YYNKNPGFEI IHGLLDRIMQ LLDVPPGEDK GGYVIKASEG
PAFFPGRCAE IFARGQSVGK LGVLHPDVIT KFELTMPCSS LEINVGPFL
//
ID SYFB_HUMAN Reviewed; 589 AA.
AC Q9NSD9; O95708; Q4ZFX1; Q57ZJ5; Q9NZZ6;
DT 08-DEC-2000, integrated into UniProtKB/Swiss-Prot.
read moreDT 18-MAY-2010, sequence version 3.
DT 22-JAN-2014, entry version 128.
DE RecName: Full=Phenylalanine--tRNA ligase beta subunit;
DE EC=6.1.1.20;
DE AltName: Full=Phenylalanyl-tRNA synthetase beta subunit;
DE Short=PheRS;
GN Name=FARSB; Synonyms=FARSLB, FRSB; ORFNames=HSPC173;
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].
RA Motegi H., Noda T., Shiba K.;
RL Submitted (APR-1996) to the EMBL/GenBank/DDBJ databases.
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 [LARGE SCALE MRNA].
RC TISSUE=Umbilical cord blood;
RX PubMed=11042152; DOI=10.1101/gr.140200;
RA Zhang Q.-H., Ye M., Wu X.-Y., Ren S.-X., Zhao M., Zhao C.-J., Fu G.,
RA Shen Y., Fan H.-Y., Lu G., Zhong M., Xu X.-R., Han Z.-G., Zhang J.-W.,
RA Tao J., Huang Q.-H., Zhou J., Hu G.-X., Gu J., Chen S.-J., Chen Z.;
RT "Cloning and functional analysis of cDNAs with open reading frames for
RT 300 previously undefined genes expressed in CD34+ hematopoietic
RT stem/progenitor cells.";
RL Genome Res. 10:1546-1560(2000).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15815621; DOI=10.1038/nature03466;
RA Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H.,
RA Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M.,
RA Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E.,
RA Kremitzki C., Oddy L., Du H., Sun H., Bradshaw-Cordum H., Ali J.,
RA Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C.,
RA Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J.,
RA Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A.,
RA Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K.,
RA Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M.,
RA Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K.,
RA McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C.,
RA Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N.,
RA Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M.,
RA Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E.,
RA Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P.,
RA Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A.,
RA Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A.,
RA Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T.,
RA Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D.,
RA Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X.,
RA McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C.,
RA Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S.,
RA Miller W., Eichler E.E., Bork P., Suyama M., Torrents D.,
RA Waterston R.H., Wilson R.K.;
RT "Generation and annotation of the DNA sequences of human chromosomes 2
RT and 4.";
RL Nature 434:724-731(2005).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Testis;
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 [6]
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 [7]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
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 -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity).
CC -!- SIMILARITY: Belongs to the phenylalanyl-tRNA synthetase beta
CC subunit family. Type 2 subfamily.
CC -!- SIMILARITY: Contains 1 B5 domain.
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; D84430; BAA95608.1; -; mRNA.
DR EMBL; AF042346; AAD02220.1; -; mRNA.
DR EMBL; AF161521; AAF29136.1; -; mRNA.
DR EMBL; AC097461; AAX88958.1; -; Genomic_DNA.
DR EMBL; AC104772; AAX81986.1; -; Genomic_DNA.
DR EMBL; BC017783; AAH17783.1; -; mRNA.
DR RefSeq; NP_005678.3; NM_005687.3.
DR UniGene; Hs.471452; -.
DR PDB; 3L4G; X-ray; 3.30 A; B/D/F/H/J/L/N/P=1-589.
DR PDBsum; 3L4G; -.
DR ProteinModelPortal; Q9NSD9; -.
DR SMR; Q9NSD9; 1-589.
DR DIP; DIP-32869N; -.
DR IntAct; Q9NSD9; 7.
DR MINT; MINT-3073662; -.
DR STRING; 9606.ENSP00000281828; -.
DR DrugBank; DB00120; L-Phenylalanine.
DR PhosphoSite; Q9NSD9; -.
DR DMDM; 296452943; -.
DR PaxDb; Q9NSD9; -.
DR PRIDE; Q9NSD9; -.
DR Ensembl; ENST00000281828; ENSP00000281828; ENSG00000116120.
DR GeneID; 10056; -.
DR KEGG; hsa:10056; -.
DR UCSC; uc002vne.1; human.
DR CTD; 10056; -.
DR GeneCards; GC02M223435; -.
DR H-InvDB; HIX0002878; -.
DR HGNC; HGNC:17800; FARSB.
DR HPA; HPA036678; -.
DR MIM; 609690; gene.
DR neXtProt; NX_Q9NSD9; -.
DR PharmGKB; PA162388068; -.
DR eggNOG; COG0072; -.
DR HOGENOM; HOG000105095; -.
DR HOVERGEN; HBG009523; -.
DR InParanoid; Q9NSD9; -.
DR KO; K01890; -.
DR OMA; SEYCENQ; -.
DR OrthoDB; EOG7R2BJ6; -.
DR PhylomeDB; Q9NSD9; -.
DR BRENDA; 6.1.1.20; 2681.
DR Reactome; REACT_71; Gene Expression.
DR ChiTaRS; FARSB; human.
DR GeneWiki; FARSB; -.
DR GenomeRNAi; 10056; -.
DR NextBio; 37993; -.
DR PRO; PR:Q9NSD9; -.
DR ArrayExpress; Q9NSD9; -.
DR Bgee; Q9NSD9; -.
DR CleanEx; HS_FARSB; -.
DR Genevestigator; Q9NSD9; -.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR GO; GO:0004826; F:phenylalanine-tRNA ligase activity; TAS:ProtInc.
DR GO; GO:0003723; F:RNA 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; 3.30.56.20; -; 1.
DR InterPro; IPR005146; B3/B4_tRNA-bd.
DR InterPro; IPR009061; DNA-bd_dom_put.
DR InterPro; IPR004531; Phe-tRNA-synth_IIc_bsu_arc.
DR InterPro; IPR020825; Phe-tRNA_synthase_B3/B4.
DR InterPro; IPR005147; tRNA_synthase_B5-dom.
DR Pfam; PF03483; B3_4; 1.
DR Pfam; PF03484; B5; 1.
DR SMART; SM00873; B3_4; 1.
DR SMART; SM00874; B5; 1.
DR SUPFAM; SSF46955; SSF46955; 2.
DR SUPFAM; SSF56037; SSF56037; 1.
DR TIGRFAMs; TIGR00471; pheT_arch; 1.
DR PROSITE; PS51483; B5; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Aminoacyl-tRNA synthetase; ATP-binding;
KW Complete proteome; Cytoplasm; Ligase; Nucleotide-binding;
KW Protein biosynthesis; Reference proteome.
FT CHAIN 1 589 Phenylalanine--tRNA ligase beta subunit.
FT /FTId=PRO_0000127016.
FT DOMAIN 302 379 B5.
FT CONFLICT 281 281 Q -> R (in Ref. 3; AAF29136).
FT CONFLICT 555 555 G -> V (in Ref. 1; BAA95608).
FT CONFLICT 585 585 V -> I (in Ref. 1; BAA95608, 2; AAD02220,
FT 3; AAF29136 and 5; AAH17783).
FT STRAND 3 7
FT HELIX 8 15
FT HELIX 23 30
FT STRAND 34 40
FT HELIX 41 45
FT STRAND 48 50
FT STRAND 56 66
FT HELIX 77 87
FT STRAND 97 99
FT STRAND 107 110
FT TURN 112 117
FT STRAND 120 126
FT HELIX 133 145
FT TURN 146 155
FT STRAND 156 163
FT HELIX 164 166
FT STRAND 171 176
FT STRAND 178 180
FT HELIX 194 200
FT TURN 205 214
FT STRAND 220 224
FT TURN 234 236
FT STRAND 237 240
FT STRAND 251 258
FT HELIX 260 274
FT HELIX 275 277
FT STRAND 281 285
FT STRAND 287 290
FT STRAND 296 299
FT STRAND 305 310
FT HELIX 311 318
FT HELIX 324 333
FT STRAND 337 340
FT STRAND 342 351
FT HELIX 361 372
FT HELIX 374 376
FT HELIX 392 406
FT STRAND 416 418
FT HELIX 420 423
FT HELIX 425 427
FT STRAND 438 441
FT HELIX 445 447
FT STRAND 448 450
FT HELIX 455 464
FT TURN 465 467
FT STRAND 472 483
FT STRAND 490 505
FT HELIX 508 521
FT TURN 528 531
FT STRAND 532 537
FT STRAND 543 553
FT STRAND 556 564
FT HELIX 566 571
FT STRAND 578 584
FT HELIX 586 588
SQ SEQUENCE 589 AA; 66116 MW; 6425BA46D124BC08 CRC64;
MPTVSVKRDL LFQALGRTYT DEEFDELCFE FGLELDEITS EKEIISKEQG NVKAAGASDV
VLYKIDVPAN RYDLLCLEGL VRGLQVFKER IKAPVYKRVM PDGKIQKLII TEETAKIRPF
AVAAVLRNIK FTKDRYDSFI ELQEKLHQNI CRKRALVAIG THDLDTLSGP FTYTAKRPSD
IKFKPLNKTK EYTACELMNI YKTDNHLKHY LHIIENKPLY PVIYDSNGVV LSMPPIINGD
HSRITVNTRN IFIECTGTDF TKAKIVLDII VTMFSEYCEN QFTVEAAEVV FPNGKSHTFP
ELAYRKEMVR ADLINKKVGI RETPENLAKL LTRMYLKSEV IGDGNQIEIE IPPTRADIIH
ACDIVEDAAI AYGYNNIQMT LPKTYTIANQ FPLNKLTELL RHDMAAAGFT EALTFALCSQ
EDIADKLGVD ISATKAVHIS NPKTAEFQVA RTTLLPGLLK TIAANRKMPL PLKLFEISDI
VIKDSNTDVG AKNYRHLCAV YYNKNPGFEI IHGLLDRIMQ LLDVPPGEDK GGYVIKASEG
PAFFPGRCAE IFARGQSVGK LGVLHPDVIT KFELTMPCSS LEINVGPFL
//
MIM
609690
*RECORD*
*FIELD* NO
609690
*FIELD* TI
*609690 PHENYLALANINE-tRNA SYNTHETASE, BETA SUBUNIT; FARSB
;;PHENYLALANINE-tRNA SYNTHETASE, CYTOPLASMIC, BETA SUBUNIT; FRSB;;
read morePHENYLALANINE-tRNA SYNTHETASE-LIKE, BETA SUBUNIT; FARSLB
*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 (602918), and a
regulatory beta subunit, FARSB (Rodova et al., 1999).
CLONING
By database analysis, RT-PCR using embryonic kidney cell RNA, and
screening a fetal kidney cDNA library, Rodova et al. (1999) cloned
FARSB. The 589-amino acid protein has a predicted molecular mass of 66
kD. Sequence alignment of FARSB orthologs from multiple species showed
conservation of DNA-binding domains and suggested the heterodimer of
FARSB and FARSA form a 4-helix bundle interface similar to that seen in
Thermus thermophilus. Human FARSB is approximately 200 amino acids
shorter than its prokaryotic homologs and does not contain the RNP
domain that binds to anticodons. Northern blot analysis detected a
2.4-kb FARSB transcript in heart, brain, placenta, skeletal muscle,
kidney, and pancreas. FARSB expression was stronger in malignant cell
lines compared to normal tissue lines.
Using differential display and Northern blot analysis, Zhou et al.
(1999) identified murine Farsb as a gene downregulated during
suberoylanilide hydroxamic acid-induced differentiation of
erythroleukemia cells. Human FARSB shares 93% amino acid identity with
its mouse homolog.
GENE FUNCTION
Rodova et al. (1999) showed that COS-7 cells transfected with FARSB and
FARSA increased phenylalanine charging of tRNA, whereas transfection of
FARSB alone caused a decrease in activity of the endogenous
heterodimeric enzyme.
MAPPING
Using database analysis, Zhou et al. (1999) mapped the FARSB gene to
chromosome 2 near the PAX3 gene (606597).
*FIELD* RF
1. 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.
2. Zhou, X.; Richon, V. M.; Ngo, L.; Rifkind, R. A.; Marks, P. A.
: Cloning of the cDNA encoding phenylalanyl tRNA synthetase regulatory
alpha-subunit-like protein whose expression is down-regulated during
differentiation. Gene 233: 13-19, 1999.
*FIELD* CD
Laura L. Baxter: 10/27/2005
*FIELD* ED
wwang: 11/08/2007
wwang: 11/8/2007
wwang: 9/19/2006
wwang: 10/28/2005
*RECORD*
*FIELD* NO
609690
*FIELD* TI
*609690 PHENYLALANINE-tRNA SYNTHETASE, BETA SUBUNIT; FARSB
;;PHENYLALANINE-tRNA SYNTHETASE, CYTOPLASMIC, BETA SUBUNIT; FRSB;;
read morePHENYLALANINE-tRNA SYNTHETASE-LIKE, BETA SUBUNIT; FARSLB
*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 (602918), and a
regulatory beta subunit, FARSB (Rodova et al., 1999).
CLONING
By database analysis, RT-PCR using embryonic kidney cell RNA, and
screening a fetal kidney cDNA library, Rodova et al. (1999) cloned
FARSB. The 589-amino acid protein has a predicted molecular mass of 66
kD. Sequence alignment of FARSB orthologs from multiple species showed
conservation of DNA-binding domains and suggested the heterodimer of
FARSB and FARSA form a 4-helix bundle interface similar to that seen in
Thermus thermophilus. Human FARSB is approximately 200 amino acids
shorter than its prokaryotic homologs and does not contain the RNP
domain that binds to anticodons. Northern blot analysis detected a
2.4-kb FARSB transcript in heart, brain, placenta, skeletal muscle,
kidney, and pancreas. FARSB expression was stronger in malignant cell
lines compared to normal tissue lines.
Using differential display and Northern blot analysis, Zhou et al.
(1999) identified murine Farsb as a gene downregulated during
suberoylanilide hydroxamic acid-induced differentiation of
erythroleukemia cells. Human FARSB shares 93% amino acid identity with
its mouse homolog.
GENE FUNCTION
Rodova et al. (1999) showed that COS-7 cells transfected with FARSB and
FARSA increased phenylalanine charging of tRNA, whereas transfection of
FARSB alone caused a decrease in activity of the endogenous
heterodimeric enzyme.
MAPPING
Using database analysis, Zhou et al. (1999) mapped the FARSB gene to
chromosome 2 near the PAX3 gene (606597).
*FIELD* RF
1. 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.
2. Zhou, X.; Richon, V. M.; Ngo, L.; Rifkind, R. A.; Marks, P. A.
: Cloning of the cDNA encoding phenylalanyl tRNA synthetase regulatory
alpha-subunit-like protein whose expression is down-regulated during
differentiation. Gene 233: 13-19, 1999.
*FIELD* CD
Laura L. Baxter: 10/27/2005
*FIELD* ED
wwang: 11/08/2007
wwang: 11/8/2007
wwang: 9/19/2006
wwang: 10/28/2005