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Q9NSD9

- SYFB_HUMAN

UniProt

Q9NSD9 - SYFB_HUMAN

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Protein
Phenylalanine--tRNA ligase beta subunit
Gene
FARSB, FARSLB, FRSB, HSPC173
Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 4 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. RNA binding Source: InterPro
  3. magnesium ion binding Source: InterPro
  4. phenylalanine-tRNA ligase activity Source: ProtInc
Complete GO annotation...

GO - Biological processi

  1. gene expression Source: Reactome
  2. phenylalanyl-tRNA aminoacylation Source: InterPro
  3. tRNA aminoacylation for protein translation Source: Reactome
  4. translation Source: ProtInc
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 beta subunit (EC:6.1.1.20)
Alternative name(s):
Phenylalanyl-tRNA synthetase beta subunit
Short name:
PheRS
Gene namesi
Name:FARSB
Synonyms:FARSLB, FRSB
ORF Names:HSPC173
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 2

Organism-specific databases

HGNCiHGNC:17800. FARSB.

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

PharmGKBiPA162388068.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 589589Phenylalanine--tRNA ligase beta subunit
PRO_0000127016Add
BLAST

Proteomic databases

MaxQBiQ9NSD9.
PaxDbiQ9NSD9.
PRIDEiQ9NSD9.

PTM databases

PhosphoSiteiQ9NSD9.

Expressioni

Gene expression databases

ArrayExpressiQ9NSD9.
BgeeiQ9NSD9.
CleanExiHS_FARSB.
GenevestigatoriQ9NSD9.

Organism-specific databases

HPAiHPA036678.

Interactioni

Subunit structurei

Tetramer of two alpha and two beta subunits By similarity.

Protein-protein interaction databases

BioGridi115367. 31 interactions.
DIPiDIP-32869N.
IntActiQ9NSD9. 7 interactions.
MINTiMINT-3073662.
STRINGi9606.ENSP00000281828.

Structurei

Secondary structure

Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi3 – 75
Helixi8 – 158
Helixi23 – 308
Beta strandi34 – 407
Helixi41 – 455
Beta strandi48 – 503
Beta strandi56 – 6611
Helixi77 – 8711
Beta strandi97 – 993
Beta strandi107 – 1104
Turni112 – 1176
Beta strandi120 – 1267
Helixi133 – 14513
Turni146 – 15510
Beta strandi156 – 1638
Helixi164 – 1663
Beta strandi171 – 1766
Beta strandi178 – 1803
Helixi194 – 2007
Turni205 – 21410
Beta strandi220 – 2245
Turni234 – 2363
Beta strandi237 – 2404
Beta strandi251 – 2588
Helixi260 – 27415
Helixi275 – 2773
Beta strandi281 – 2855
Beta strandi287 – 2904
Beta strandi296 – 2994
Beta strandi305 – 3106
Helixi311 – 3188
Helixi324 – 33310
Beta strandi337 – 3404
Beta strandi342 – 35110
Helixi361 – 37212
Helixi374 – 3763
Helixi392 – 40615
Beta strandi416 – 4183
Helixi420 – 4234
Helixi425 – 4273
Beta strandi438 – 4414
Helixi445 – 4473
Beta strandi448 – 4503
Helixi455 – 46410
Turni465 – 4673
Beta strandi472 – 48312
Beta strandi490 – 50516
Helixi508 – 52114
Turni528 – 5314
Beta strandi532 – 5376
Beta strandi543 – 55311
Beta strandi556 – 5649
Helixi566 – 5716
Beta strandi578 – 5847
Helixi586 – 5883

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3L4GX-ray3.30B/D/F/H/J/L/N/P1-589[»]
ProteinModelPortaliQ9NSD9.
SMRiQ9NSD9. Positions 1-589.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini302 – 37978B5
Add
BLAST

Sequence similaritiesi

Contains 1 B5 domain.

Phylogenomic databases

eggNOGiCOG0072.
HOGENOMiHOG000105095.
HOVERGENiHBG009523.
InParanoidiQ9NSD9.
KOiK01890.
OMAiEVMPLIL.
OrthoDBiEOG7R2BJ6.
PhylomeDBiQ9NSD9.
TreeFamiTF105681.

Family and domain databases

Gene3Di3.30.56.20. 1 hit.
InterProiIPR005146. B3/B4_tRNA-bd.
IPR009061. DNA-bd_dom_put.
IPR004531. Phe-tRNA-synth_IIc_bsu_arc.
IPR020825. Phe-tRNA_synthase_B3/B4.
IPR005147. tRNA_synthase_B5-dom.
[Graphical view]
PfamiPF03483. B3_4. 1 hit.
PF03484. B5. 1 hit.
[Graphical view]
SMARTiSM00873. B3_4. 1 hit.
SM00874. B5. 1 hit.
[Graphical view]
SUPFAMiSSF46955. SSF46955. 2 hits.
SSF56037. SSF56037. 1 hit.
TIGRFAMsiTIGR00471. pheT_arch. 1 hit.
PROSITEiPS51483. B5. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q9NSD9-1 [UniParc]FASTAAdd to Basket

« Hide

MPTVSVKRDL LFQALGRTYT DEEFDELCFE FGLELDEITS EKEIISKEQG    50
NVKAAGASDV VLYKIDVPAN RYDLLCLEGL VRGLQVFKER IKAPVYKRVM 100
PDGKIQKLII TEETAKIRPF AVAAVLRNIK FTKDRYDSFI ELQEKLHQNI 150
CRKRALVAIG THDLDTLSGP FTYTAKRPSD IKFKPLNKTK EYTACELMNI 200
YKTDNHLKHY LHIIENKPLY PVIYDSNGVV LSMPPIINGD HSRITVNTRN 250
IFIECTGTDF TKAKIVLDII VTMFSEYCEN QFTVEAAEVV FPNGKSHTFP 300
ELAYRKEMVR ADLINKKVGI RETPENLAKL LTRMYLKSEV IGDGNQIEIE 350
IPPTRADIIH ACDIVEDAAI AYGYNNIQMT LPKTYTIANQ FPLNKLTELL 400
RHDMAAAGFT EALTFALCSQ EDIADKLGVD ISATKAVHIS NPKTAEFQVA 450
RTTLLPGLLK TIAANRKMPL PLKLFEISDI VIKDSNTDVG AKNYRHLCAV 500
YYNKNPGFEI IHGLLDRIMQ LLDVPPGEDK GGYVIKASEG PAFFPGRCAE 550
IFARGQSVGK LGVLHPDVIT KFELTMPCSS LEINVGPFL 589
Length:589
Mass (Da):66,116
Last modified:May 18, 2010 - v3
Checksum:i6425BA46D124BC08
GO

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti281 – 2811Q → R in AAF29136. 1 Publication
Sequence conflicti555 – 5551G → V in BAA95608. 1 Publication
Sequence conflicti585 – 5851V → I in BAA95608. 1 Publication
Sequence conflicti585 – 5851V → I in AAD02220. 1 Publication
Sequence conflicti585 – 5851V → I in AAF29136. 1 Publication
Sequence conflicti585 – 5851V → I in AAH17783. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
D84430 mRNA. Translation: BAA95608.1.
AF042346 mRNA. Translation: AAD02220.1.
AF161521 mRNA. Translation: AAF29136.1.
AC097461 Genomic DNA. Translation: AAX88958.1.
AC104772 Genomic DNA. Translation: AAX81986.1.
BC017783 mRNA. Translation: AAH17783.1.
CCDSiCCDS2454.1.
RefSeqiNP_005678.3. NM_005687.3.
UniGeneiHs.471452.

Genome annotation databases

EnsembliENST00000281828; ENSP00000281828; ENSG00000116120.
GeneIDi10056.
KEGGihsa:10056.
UCSCiuc002vne.1. human.

Polymorphism databases

DMDMi296452943.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
D84430 mRNA. Translation: BAA95608.1 .
AF042346 mRNA. Translation: AAD02220.1 .
AF161521 mRNA. Translation: AAF29136.1 .
AC097461 Genomic DNA. Translation: AAX88958.1 .
AC104772 Genomic DNA. Translation: AAX81986.1 .
BC017783 mRNA. Translation: AAH17783.1 .
CCDSi CCDS2454.1.
RefSeqi NP_005678.3. NM_005687.3.
UniGenei Hs.471452.

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 B/D/F/H/J/L/N/P 1-589 [» ]
ProteinModelPortali Q9NSD9.
SMRi Q9NSD9. Positions 1-589.
ModBasei Search...

Protein-protein interaction databases

BioGridi 115367. 31 interactions.
DIPi DIP-32869N.
IntActi Q9NSD9. 7 interactions.
MINTi MINT-3073662.
STRINGi 9606.ENSP00000281828.

Chemistry

DrugBanki DB00120. L-Phenylalanine.

PTM databases

PhosphoSitei Q9NSD9.

Polymorphism databases

DMDMi 296452943.

Proteomic databases

MaxQBi Q9NSD9.
PaxDbi Q9NSD9.
PRIDEi Q9NSD9.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000281828 ; ENSP00000281828 ; ENSG00000116120 .
GeneIDi 10056.
KEGGi hsa:10056.
UCSCi uc002vne.1. human.

Organism-specific databases

CTDi 10056.
GeneCardsi GC02M223435.
H-InvDB HIX0002878.
HGNCi HGNC:17800. FARSB.
HPAi HPA036678.
MIMi 609690. gene.
neXtProti NX_Q9NSD9.
PharmGKBi PA162388068.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG0072.
HOGENOMi HOG000105095.
HOVERGENi HBG009523.
InParanoidi Q9NSD9.
KOi K01890.
OMAi EVMPLIL.
OrthoDBi EOG7R2BJ6.
PhylomeDBi Q9NSD9.
TreeFami TF105681.

Enzyme and pathway databases

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

Miscellaneous databases

ChiTaRSi FARSB. human.
GeneWikii FARSB.
GenomeRNAii 10056.
NextBioi 37993.
PROi Q9NSD9.
SOURCEi Search...

Gene expression databases

ArrayExpressi Q9NSD9.
Bgeei Q9NSD9.
CleanExi HS_FARSB.
Genevestigatori Q9NSD9.

Family and domain databases

Gene3Di 3.30.56.20. 1 hit.
InterProi IPR005146. B3/B4_tRNA-bd.
IPR009061. DNA-bd_dom_put.
IPR004531. Phe-tRNA-synth_IIc_bsu_arc.
IPR020825. Phe-tRNA_synthase_B3/B4.
IPR005147. tRNA_synthase_B5-dom.
[Graphical view ]
Pfami PF03483. B3_4. 1 hit.
PF03484. B5. 1 hit.
[Graphical view ]
SMARTi SM00873. B3_4. 1 hit.
SM00874. B5. 1 hit.
[Graphical view ]
SUPFAMi SSF46955. SSF46955. 2 hits.
SSF56037. SSF56037. 1 hit.
TIGRFAMsi TIGR00471. pheT_arch. 1 hit.
PROSITEi PS51483. B5. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. Motegi H., Noda T., Shiba K.
    Submitted (APR-1996) to the EMBL/GenBank/DDBJ databases
    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. "Cloning and functional analysis of cDNAs with open reading frames for 300 previously undefined genes expressed in CD34+ hematopoietic stem/progenitor cells."
    Zhang Q.-H., Ye M., Wu X.-Y., Ren S.-X., Zhao M., Zhao C.-J., Fu G., Shen Y., Fan H.-Y., Lu G., Zhong M., Xu X.-R., Han Z.-G., Zhang J.-W., Tao J., Huang Q.-H., Zhou J., Hu G.-X.
    , Gu J., Chen S.-J., Chen Z.
    Genome Res. 10:1546-1560(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Umbilical cord blood.
  4. "Generation and annotation of the DNA sequences of human chromosomes 2 and 4."
    Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L., Du H.
    , Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K., McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C., Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S., Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H., Wilson R.K.
    Nature 434:724-731(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  5. "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: Testis.
  6. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  7. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiSYFB_HUMAN
AccessioniPrimary (citable) accession number: Q9NSD9
Secondary accession number(s): O95708
, Q4ZFX1, Q57ZJ5, Q9NZZ6
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 8, 2000
Last sequence update: May 18, 2010
Last modified: September 3, 2014
This is version 134 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, Reference proteome

Documents

  1. Aminoacyl-tRNA synthetases
    List of aminoacyl-tRNA synthetase entries
  2. Human chromosome 2
    Human chromosome 2: entries, gene names and cross-references to MIM
  3. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  4. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  5. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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