Q9NSD9 (SYFB_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Phenylalanine--tRNA ligase beta chain
EC=6.1.1.20

Alternative name(s):
Phenylalanyl-tRNA synthetase beta chain
Short name=PheRS

Gene names

Name:	FARSB
Synonyms:	FARSLB, FRSB
ORF Names:	HSPC173

Organism

Homo sapiens (Human)

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length	589 AA.
Sequence status	Complete.
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 chains By similarity.
Subcellular location	Cytoplasm By similarity.
Sequence similarities	Belongs to the phenylalanyl-tRNA synthetase beta chain family. Type 2 subfamily. Contains 1 B5 domain.

Ontologies

Keywords
Biological process	Protein biosynthesis
Cellular component	Cytoplasm
Ligand	ATP-binding Nucleotide-binding
Molecular function	Aminoacyl-tRNA synthetase Ligase
PTM	Acetylation Phosphoprotein
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological process	phenylalanyl-tRNA aminoacylation Inferred from electronic annotation. Source: InterPro
Cellular component	cytosol Traceable author statement. Source: Reactome soluble fraction Traceable author statement. Source: ProtInc
Molecular function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW RNA binding Inferred from electronic annotation. Source: InterPro magnesium ion binding Inferred from electronic annotation. Source: InterPro phenylalanine-tRNA ligase activity Traceable author statement. Source: ProtInc
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 589

589

Phenylalanine--tRNA ligase beta chain

PRO_0000127016

Regions

Domain

302 – 379

78

B5

Amino acid modifications

Modified residue

63

1

Phosphotyrosine Ref.6

Modified residue

72

1

Phosphotyrosine Ref.6

Modified residue

329

1

N6-acetyllysine Ref.7

Experimental info

Sequence conflict

281

1

Q → R in AAF29136. Ref.3

Sequence conflict

555

1

G → V in BAA95608. Ref.1

Sequence conflict

585

1

V → I in BAA95608. Ref.1

Sequence conflict

585

1

V → I in AAD02220. Ref.2

Sequence conflict

585

1

V → I in AAF29136. Ref.3

Sequence conflict

585

1

V → I in AAH17783. Ref.5

Secondary structure

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589

Helix Strand Turn

Details...

Beta strand

3 – 7

5

Helix

8 – 14

7

Helix

23 – 30

8

Beta strand

34 – 40

7

Helix

41 – 45

5

Beta strand

59 – 66

8

Turn

85 – 89

5

Beta strand

97 – 99

3

Beta strand

107 – 110

4

Turn

112 – 117

6

Beta strand

122 – 126

5

Helix

133 – 145

13

Turn

146 – 155

10

Beta strand

156 – 158

3

Helix

164 – 166

3

Beta strand

172 – 176

5

Beta strand

178 – 180

3

Helix

194 – 200

7

Turn

205 – 214

10

Beta strand

220 – 224

5

Turn

234 – 236

3

Beta strand

251 – 256

6

Helix

260 – 274

15

Helix

275 – 277

3

Beta strand

281 – 285

5

Beta strand

287 – 290

4

Beta strand

296 – 299

4

Beta strand

305 – 310

6

Helix

311 – 317

7

Helix

324 – 333

10

Beta strand

337 – 340

4

Beta strand

346 – 351

6

Helix

361 – 371

11

Helix

392 – 406

15

Beta strand

416 – 418

3

Helix

420 – 423

4

Turn

424 – 426

3

Beta strand

438 – 441

4

Helix

445 – 447

3

Beta strand

448 – 450

3

Helix

459 – 464

6

Turn

465 – 467

3

Beta strand

472 – 482

11

Beta strand

492 – 504

13

Turn

509 – 511

3

Helix

515 – 521

7

Beta strand

534 – 537

4

Beta strand

543 – 545

3

Beta strand

547 – 552

6

Helix

566 – 571

6

Beta strand

578 – 584

7

Sequences

	Sequence		Length	Mass (Da)
	Q9NSD9 [UniParc]. Last modified May 18, 2010. Version 3. Checksum: 6425BA46D124BC08	FASTA	589	66,116
	10 20 30 40 50 60 MPTVSVKRDL LFQALGRTYT DEEFDELCFE FGLELDEITS EKEIISKEQG NVKAAGASDV 70 80 90 100 110 120 VLYKIDVPAN RYDLLCLEGL VRGLQVFKER IKAPVYKRVM PDGKIQKLII TEETAKIRPF 130 140 150 160 170 180 AVAAVLRNIK FTKDRYDSFI ELQEKLHQNI CRKRALVAIG THDLDTLSGP FTYTAKRPSD 190 200 210 220 230 240 IKFKPLNKTK EYTACELMNI YKTDNHLKHY LHIIENKPLY PVIYDSNGVV LSMPPIINGD 250 260 270 280 290 300 HSRITVNTRN IFIECTGTDF TKAKIVLDII VTMFSEYCEN QFTVEAAEVV FPNGKSHTFP 310 320 330 340 350 360 ELAYRKEMVR ADLINKKVGI RETPENLAKL LTRMYLKSEV IGDGNQIEIE IPPTRADIIH 370 380 390 400 410 420 ACDIVEDAAI AYGYNNIQMT LPKTYTIANQ FPLNKLTELL RHDMAAAGFT EALTFALCSQ 430 440 450 460 470 480 EDIADKLGVD ISATKAVHIS NPKTAEFQVA RTTLLPGLLK TIAANRKMPL PLKLFEISDI 490 500 510 520 530 540 VIKDSNTDVG AKNYRHLCAV YYNKNPGFEI IHGLLDRIMQ LLDVPPGEDK GGYVIKASEG 550 560 570 580 PAFFPGRCAE IFARGQSVGK LGVLHPDVIT KFELTMPCSS LEINVGPFL

References

	« Hide 'large scale' referencesShow 'large scale' references »
[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: 10049785] [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: 11042152] [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: 15815621] [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: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Testis.
[6]	"Tyrosine phosphorylated Par3 regulates epithelial tight junction assembly promoted by EGFR signaling." Wang Y., Du D., Fang L., Yang G., Zhang C., Zeng R., Ullrich A., Lottspeich F., Chen Z. EMBO J. 25:5058-5070(2006) [PubMed: 17053785] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-63 AND TYR-72, MASS SPECTROMETRY. Tissue: Embryonic kidney.
[7]	"Lysine acetylation targets protein complexes and co-regulates major cellular functions." Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T., Olsen J.V., Mann M. Science 325:834-840(2009) [PubMed: 19608861] [Abstract] Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-329, MASS SPECTROMETRY.
[8]	"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: 21269460] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

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.

IPI

IPI00300074.

RefSeq

NP_005678.3. NM_005687.3.

UniGene

Hs.471452.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
3L4G	X-ray	3.30	B/D/F/H/J/L/N/P	1-589	[»]

ProteinModelPortal

Q9NSD9.

SMR

Q9NSD9. Positions 1-589.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-32869N.

IntAct

Q9NSD9. 3 interactions.

STRING

Q9NSD9.

PTM databases

PhosphoSite

Q9NSD9.

Polymorphism databases

DMDM

296452943.

Proteomic databases

PRIDE

Q9NSD9.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000281828; ENSP00000281828; ENSG00000116120.

GeneID

10056.

KEGG

hsa:10056.

Organism-specific databases

CTD

10056.

GeneCards

GC02M223435.

H-InvDB

HIX0002878.

HGNC

HGNC:17800. FARSB.

HPA

HPA036678.

MIM

609690. gene.

neXtProt

NX_Q9NSD9.

PharmGKB

PA162388068.

GenAtlas

Search...

Phylogenomic databases

eggNOG

prNOG09796.

GeneTree

ENSGT00530000063489.

HOGENOM

HBG497667.

HOVERGEN

HBG009523.

InParanoid

Q9NSD9.

OMA

LLTRMCL.

OrthoDB

EOG4FXR74.

PhylomeDB

Q9NSD9.

Enzyme and pathway databases

BRENDA

6.1.1.20. 2681.

Reactome

REACT_71. Gene Expression.

Gene expression databases

ArrayExpress

Q9NSD9.

Bgee

Q9NSD9.

CleanEx

HS_FARSB.

Genevestigator

Q9NSD9.

GermOnline

ENSG00000116120. Homo sapiens.

Family and domain databases

InterPro

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]

Gene3D

G3DSA:3.30.56.20. B5. 1 hit.

KO

K01890.

Pfam

PF03483. B3_4. 1 hit.
PF03484. B5. 1 hit.
[Graphical view]

SMART

SM00873. B3_4. 1 hit.
SM00874. B5. 1 hit.
[Graphical view]

SUPFAM

SSF56037. B3_4. 1 hit.
SSF46955. Putativ_DNA_bind. 2 hits.

TIGRFAMs

TIGR00471. PheT_arch. 1 hit.

PROSITE

PS51483. B5. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

DrugBank

DB00120. L-Phenylalanine.

NextBio

37993.

SOURCE

Search...

Entry information

Entry name

SYFB_HUMAN

Accession

Primary (citable) accession number: Q9NSD9
Secondary accession number(s): O95708 , Q4ZFX1, Q57ZJ5, Q9NZZ6

Entry history

Integrated into UniProtKB/Swiss-Prot:	December 8, 2000
Last sequence update:	May 18, 2010
Last modified:	January 25, 2012
This is version 111 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.