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O95363

- SYFM_HUMAN

UniProt

O95363 - SYFM_HUMAN

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Protein
Phenylalanine--tRNA ligase, mitochondrial
Gene
FARS2, FARS1, HSPC320
Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

Is responsible for the charging of tRNA(Phe) with phenylalanine in mitochondrial translation. To a lesser extent, also catalyzes direct attachment of m-Tyr (an oxidized version of Phe) to tRNA(Phe), thereby opening the way for delivery of the misacylated tRNA to the ribosome and incorporation of ROS-damaged amino acid into proteins.2 Publications

Catalytic activityi

ATP + L-phenylalanine + tRNA(Phe) = AMP + diphosphate + L-phenylalanyl-tRNA(Phe).2 Publications

Kineticsi

kcat is 2.8 min(-1), 2.0 min(-1) and 3.1 min(-1) with L-phenylalanine, L-tyrosine and m-tyrosine as substrate, respectively. Thus, the catalytic efficiency of the m-Tyr attachment is only 5-fold lower than that of the correct amino acid, while that of Tyr attachment is 1000-fold lower (1 Publication

).

  1. KM=2.2 µM for L-phenylalanine (1 Publication)2 Publications
  2. KM=1900 µM for L-tyrosine (1 Publication)
  3. KM=11.7 µM for DL-m-tyrosine (1 Publication)
  4. KM=7.3 µM for L-phenylalanine (1 Publication)
  5. KM=2.9 mM for ATP (1 Publication)
  6. KM=1.2 µM for tRNA(Phe) (1 Publication)

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei179 – 1791Substrate
Binding sitei287 – 2871Substrate; via carbonyl oxygen
Binding sitei312 – 3121Substrate; via carbonyl oxygen

GO - Molecular functioni

  1. ATP binding Source: UniProtKB-KW
  2. magnesium ion binding Source: InterPro
  3. phenylalanine-tRNA ligase activity Source: UniProtKB
  4. tRNA binding Source: UniProtKB

GO - Biological processi

  1. gene expression Source: Reactome
  2. phenylalanyl-tRNA aminoacylation Source: UniProtKB
  3. tRNA aminoacylation for protein translation Source: Reactome
  4. tRNA processing Source: UniProtKB
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

ReactomeiREACT_15302. Mitochondrial tRNA aminoacylation.

Names & Taxonomyi

Protein namesi
Recommended name:
Phenylalanine--tRNA ligase, mitochondrial (EC:6.1.1.20)
Alternative name(s):
Phenylalanyl-tRNA synthetase
Short name:
PheRS
Gene namesi
Name:FARS2
Synonyms:FARS1
ORF Names:HSPC320
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 6

Organism-specific databases

HGNCiHGNC:21062. FARS2.

Subcellular locationi

Mitochondrion matrix Reviewed prediction

GO - Cellular componenti

  1. mitochondrial matrix Source: Reactome
Complete GO annotation...

Keywords - Cellular componenti

Mitochondrion

Pathology & Biotechi

Involvement in diseasei

Combined oxidative phosphorylation deficiency 14 (COXPD14) [MIM:614946]: A severe multisystemic autosomal recessive disorder characterized by neonatal onset of global developmental delay, refractory seizures, and lactic acidosis. Biochemical studies show deficiencies of multiple mitochondrial respiratory enzymes.
Note: The disease is caused by mutations affecting the gene represented in this entry.2 Publications
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti144 – 1441Y → C in COXPD14; results in decreased affinity for tRNA causing a decrease in the catalytic efficiency for tRNA charging; does not affect ATP or Phe binding. 2 Publications
VAR_069487
Natural varianti329 – 3291I → T in COXPD14; results in a 4-fold decrease in the catalytic efficiency of amino acid activation mainly due to a decreased affinity for ATP; does not affect Phe binding; affects the stability of the enzyme, leading to a significant decrease in overall charging capacity. 1 Publication
VAR_069488
Natural varianti391 – 3911D → V in COXPD14; results in a decrease in affinity for Phe causing a decrease in aminoacylation activity; affects the stability of the enzyme, leading to a significant decrease in overall charging capacity. 1 Publication
VAR_069489

Keywords - Diseasei

Disease mutation

Organism-specific databases

MIMi614946. phenotype.
Orphaneti319519. Combined oxidative phosphorylation defect type 14.
PharmGKBiPA134954893.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini? – 451Phenylalanine--tRNA ligase, mitochondrialPRO_0000035813
Transit peptidei1 – ?Mitochondrion Reviewed prediction

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei202 – 2021N6-acetyllysine1 Publication

Keywords - PTMi

Acetylation

Proteomic databases

MaxQBiO95363.
PaxDbiO95363.
PeptideAtlasiO95363.
PRIDEiO95363.

PTM databases

PhosphoSiteiO95363.

Expressioni

Gene expression databases

ArrayExpressiO95363.
BgeeiO95363.
CleanExiHS_FARS2.
GenevestigatoriO95363.

Organism-specific databases

HPAiHPA018148.
HPA028836.

Interactioni

Subunit structurei

Monomer.2 Publications

Protein-protein interaction databases

BioGridi115909. 8 interactions.
IntActiO95363. 4 interactions.
MINTiMINT-3077661.
STRINGi9606.ENSP00000274680.

Structurei

Secondary structure

Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi49 – 535
Beta strandi56 – 594
Helixi68 – 714
Turni72 – 754
Helixi78 – 803
Beta strandi81 – 844
Helixi85 – 10319
Beta strandi105 – 1073
Beta strandi111 – 1133
Beta strandi118 – 1214
Helixi122 – 1254
Helixi127 – 1293
Helixi136 – 1383
Helixi140 – 1423
Beta strandi145 – 1528
Helixi156 – 1594
Helixi160 – 1656
Beta strandi169 – 17810
Beta strandi184 – 1863
Beta strandi189 – 20113
Helixi202 – 2054
Turni206 – 2083
Helixi212 – 2143
Helixi233 – 25523
Helixi256 – 2583
Beta strandi261 – 2688
Beta strandi271 – 28111
Beta strandi284 – 29411
Helixi296 – 3016
Beta strandi307 – 3159
Helixi316 – 3238
Helixi329 – 3335
Helixi337 – 3404
Helixi341 – 3433
Beta strandi363 – 3708
Helixi378 – 38912
Helixi390 – 3923
Beta strandi393 – 40311
Turni405 – 4073
Beta strandi410 – 4189
Beta strandi421 – 4233
Helixi427 – 44418
Beta strandi448 – 4514

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3CMQX-ray2.20A38-451[»]
3HFVX-ray2.60A38-451[»]
3TEGX-ray2.20A38-451[»]
3TUPX-ray3.05A38-451[»]
ProteinModelPortaliO95363.
SMRiO95363. Positions 47-451.

Miscellaneous databases

EvolutionaryTraceiO95363.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini358 – 45093FDX-ACB
Add
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni157 – 1604Substrate binding
Regioni186 – 1883Substrate binding
Regioni193 – 1953Substrate binding

Sequence similaritiesi

Contains 1 FDX-ACB domain.

Keywords - Domaini

Transit peptide

Phylogenomic databases

eggNOGiCOG0016.
HOGENOMiHOG000165163.
HOVERGENiHBG082540.
InParanoidiO95363.
KOiK01889.
OMAiEFTHPKT.
OrthoDBiEOG7CG6ZS.
PhylomeDBiO95363.
TreeFamiTF105798.

Family and domain databases

Gene3Di3.30.70.380. 1 hit.
InterProiIPR006195. aa-tRNA-synth_II.
IPR004530. Phe-tRNA-synth_IIc_mito.
IPR002319. Phenylalanyl-tRNA_Synthase.
IPR005121. PheS_beta_Fdx_antiC-bd.
[Graphical view]
PfamiPF03147. FDX-ACB. 1 hit.
PF01409. tRNA-synt_2d. 2 hits.
[Graphical view]
SMARTiSM00896. FDX-ACB. 1 hit.
[Graphical view]
SUPFAMiSSF54991. SSF54991. 1 hit.
TIGRFAMsiTIGR00469. pheS_mito. 1 hit.
PROSITEiPS50862. AA_TRNA_LIGASE_II. 1 hit.
PS51447. FDX_ACB. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

O95363-1 [UniParc]FASTAAdd to Basket

« Hide

MVGSALRRGA HAYVYLVSKA SHISRGHQHQ AWGSRPPAAE CATQRAPGSV    50
VELLGKSYPQ DDHSNLTRKV LTRVGRNLHN QQHHPLWLIK ERVKEHFYKQ 100
YVGRFGTPLF SVYDNLSPVV TTWQNFDSLL IPADHPSRKK GDNYYLNRTH 150
MLRAHTSAHQ WDLLHAGLDA FLVVGDVYRR DQIDSQHYPI FHQLEAVRLF 200
SKHELFAGIK DGESLQLFEQ SSRSAHKQET HTMEAVKLVE FDLKQTLTRL 250
MAHLFGDELE IRWVDCYFPF THPSFEMEIN FHGEWLEVLG CGVMEQQLVN 300
SAGAQDRIGW AFGLGLERLA MILYDIPDIR LFWCEDERFL KQFCVSNINQ 350
KVKFQPLSKY PAVINDISFW LPSENYAEND FYDLVRTIGG DLVEKVDLID 400
KFVHPKTHKT SHCYRITYRH MERTLSQREV RHIHQALQEA AVQLLGVEGR 450
F 451
Length:451
Mass (Da):52,357
Last modified:May 1, 1999 - v1
Checksum:i1E5CC647A4A7193B
GO

Sequence cautioni

The sequence AAF28998.1 differs from that shown. Reason: Frameshift at position 414.

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti57 – 571S → C.
Corresponds to variant rs34382405 [ dbSNP | Ensembl ].
VAR_052642
Natural varianti144 – 1441Y → C in COXPD14; results in decreased affinity for tRNA causing a decrease in the catalytic efficiency for tRNA charging; does not affect ATP or Phe binding. 2 Publications
VAR_069487
Natural varianti280 – 2801N → S.3 Publications
Corresponds to variant rs11243011 [ dbSNP | Ensembl ].
VAR_052643
Natural varianti329 – 3291I → T in COXPD14; results in a 4-fold decrease in the catalytic efficiency of amino acid activation mainly due to a decreased affinity for ATP; does not affect Phe binding; affects the stability of the enzyme, leading to a significant decrease in overall charging capacity. 1 Publication
VAR_069488
Natural varianti391 – 3911D → V in COXPD14; results in a decrease in affinity for Phe causing a decrease in aminoacylation activity; affects the stability of the enzyme, leading to a significant decrease in overall charging capacity. 1 Publication
VAR_069489

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti158 – 1581A → T in BAD97143. 1 Publication
Sequence conflicti361 – 3611P → T in AAF28998. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AF097441 mRNA. Translation: AAC83802.1.
AK312454 mRNA. Translation: BAG35361.1.
CR542279 mRNA. Translation: CAG47075.1.
AK223423 mRNA. Translation: BAD97143.1.
AL133473
, AL022097, AL590868, AL121978, AL392184 Genomic DNA. Translation: CAI19901.1.
AL022097
, AL121978, AL392184, AL590868, AL133473 Genomic DNA. Translation: CAI19950.1.
AL392184
, AL121978, AL590868, AL133473, AL022097 Genomic DNA. Translation: CAI20375.1.
AL121978
, AL133473, AL022097, AL392184, AL590868 Genomic DNA. Translation: CAI21657.1.
AL590868
, AL392184, AL133473, AL121978, AL022097 Genomic DNA. Translation: CAI39442.1.
BC020239 mRNA. Translation: AAH20239.1.
BC021112 mRNA. Translation: AAH21112.1.
AF161438 mRNA. Translation: AAF28998.1. Frameshift.
CCDSiCCDS4494.1.
RefSeqiNP_006558.1. NM_006567.3.
XP_005248868.1. XM_005248811.1.
XP_005248869.1. XM_005248812.2.
UniGeneiHs.484547.

Genome annotation databases

EnsembliENST00000274680; ENSP00000274680; ENSG00000145982.
ENST00000324331; ENSP00000316335; ENSG00000145982.
GeneIDi10667.
KEGGihsa:10667.
UCSCiuc003mwr.2. human.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AF097441 mRNA. Translation: AAC83802.1 .
AK312454 mRNA. Translation: BAG35361.1 .
CR542279 mRNA. Translation: CAG47075.1 .
AK223423 mRNA. Translation: BAD97143.1 .
AL133473
, AL022097 , AL590868 , AL121978 , AL392184 Genomic DNA. Translation: CAI19901.1 .
AL022097
, AL121978 , AL392184 , AL590868 , AL133473 Genomic DNA. Translation: CAI19950.1 .
AL392184
, AL121978 , AL590868 , AL133473 , AL022097 Genomic DNA. Translation: CAI20375.1 .
AL121978
, AL133473 , AL022097 , AL392184 , AL590868 Genomic DNA. Translation: CAI21657.1 .
AL590868
, AL392184 , AL133473 , AL121978 , AL022097 Genomic DNA. Translation: CAI39442.1 .
BC020239 mRNA. Translation: AAH20239.1 .
BC021112 mRNA. Translation: AAH21112.1 .
AF161438 mRNA. Translation: AAF28998.1 . Frameshift.
CCDSi CCDS4494.1.
RefSeqi NP_006558.1. NM_006567.3.
XP_005248868.1. XM_005248811.1.
XP_005248869.1. XM_005248812.2.
UniGenei Hs.484547.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
3CMQ X-ray 2.20 A 38-451 [» ]
3HFV X-ray 2.60 A 38-451 [» ]
3TEG X-ray 2.20 A 38-451 [» ]
3TUP X-ray 3.05 A 38-451 [» ]
ProteinModelPortali O95363.
SMRi O95363. Positions 47-451.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 115909. 8 interactions.
IntActi O95363. 4 interactions.
MINTi MINT-3077661.
STRINGi 9606.ENSP00000274680.

Chemistry

BindingDBi O95363.
ChEMBLi CHEMBL2511.
DrugBanki DB00120. L-Phenylalanine.

PTM databases

PhosphoSitei O95363.

Proteomic databases

MaxQBi O95363.
PaxDbi O95363.
PeptideAtlasi O95363.
PRIDEi O95363.

Protocols and materials databases

DNASUi 10667.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000274680 ; ENSP00000274680 ; ENSG00000145982 .
ENST00000324331 ; ENSP00000316335 ; ENSG00000145982 .
GeneIDi 10667.
KEGGi hsa:10667.
UCSCi uc003mwr.2. human.

Organism-specific databases

CTDi 10667.
GeneCardsi GC06P005207.
HGNCi HGNC:21062. FARS2.
HPAi HPA018148.
HPA028836.
MIMi 611592. gene.
614946. phenotype.
neXtProti NX_O95363.
Orphaneti 319519. Combined oxidative phosphorylation defect type 14.
PharmGKBi PA134954893.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG0016.
HOGENOMi HOG000165163.
HOVERGENi HBG082540.
InParanoidi O95363.
KOi K01889.
OMAi EFTHPKT.
OrthoDBi EOG7CG6ZS.
PhylomeDBi O95363.
TreeFami TF105798.

Enzyme and pathway databases

Reactomei REACT_15302. Mitochondrial tRNA aminoacylation.

Miscellaneous databases

EvolutionaryTracei O95363.
GeneWikii FARS2.
GenomeRNAii 10667.
NextBioi 40563.
PROi O95363.
SOURCEi Search...

Gene expression databases

ArrayExpressi O95363.
Bgeei O95363.
CleanExi HS_FARS2.
Genevestigatori O95363.

Family and domain databases

Gene3Di 3.30.70.380. 1 hit.
InterProi IPR006195. aa-tRNA-synth_II.
IPR004530. Phe-tRNA-synth_IIc_mito.
IPR002319. Phenylalanyl-tRNA_Synthase.
IPR005121. PheS_beta_Fdx_antiC-bd.
[Graphical view ]
Pfami PF03147. FDX-ACB. 1 hit.
PF01409. tRNA-synt_2d. 2 hits.
[Graphical view ]
SMARTi SM00896. FDX-ACB. 1 hit.
[Graphical view ]
SUPFAMi SSF54991. SSF54991. 1 hit.
TIGRFAMsi TIGR00469. pheS_mito. 1 hit.
PROSITEi PS50862. AA_TRNA_LIGASE_II. 1 hit.
PS51447. FDX_ACB. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Expression and characterization of a human mitochondrial phenylalanyl-tRNA synthetase."
    Bullard J.M., Cai Y.-C., Demeler B., Spremulli L.L.
    J. Mol. Biol. 288:567-577(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], SUBUNIT.
  2. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
    Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
    , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
    Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], VARIANT SER-280.
    Tissue: Caudate nucleus.
  3. "Cloning of human full open reading frames in Gateway(TM) system entry vector (pDONR201)."
    Halleck A., Ebert L., Mkoundinya M., Schick M., Eisenstein S., Neubert P., Kstrang K., Schatten R., Shen B., Henze S., Mar W., Korn B., Zuo D., Hu Y., LaBaer J.
    Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], VARIANT SER-280.
  4. Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S.
    Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Kidney epithelium.
  5. "The DNA sequence and analysis of human chromosome 6."
    Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L., Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., Gilbert J.G.R., Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D., Andrews T.D.
    , Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H., Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J., Brown J.Y., Burford D.C., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V., Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J., Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., Ellington A.E., Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J., French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J., Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C., Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A., Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R., Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M., Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A., Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L., Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I., Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y., Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E., Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A., Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W., Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M., West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J., Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M., Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I., Rogers J., Beck S.
    Nature 425:805-811(2003) [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: Pancreas.
  7. "Human partial CDS from CD34+ stem cells."
    Ye M., Zhang Q.-H., Zhou J., Shen Y., Wu X.-Y., Guan Z.Q., Wang L., Fan H.-Y., Mao Y.-F., Dai M., Huang Q.-H., Chen S.-J., Chen Z.
    Submitted (MAY-1999) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 108-451, VARIANT SER-280.
    Tissue: Umbilical cord blood.
  8. "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-202, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  9. "The tRNA-induced conformational activation of human mitochondrial phenylalanyl-tRNA synthetase."
    Klipcan L., Levin I., Kessler N., Moor N., Finarov I., Safro M.
    Structure 16:1095-1104(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.20 ANGSTROMS) OF 38-451 IN COMPLEX WITH SUBSTRATE, SUBUNIT.
  10. "Eukaryotic cytosolic and mitochondrial phenylalanyl-tRNA synthetases catalyze the charging of tRNA with the meta-tyrosine."
    Klipcan L., Moor N., Kessler N., Safro M.G.
    Proc. Natl. Acad. Sci. U.S.A. 106:11045-11048(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.60 ANGSTROMS) OF 38-451 IN COMPLEX WITH SUBSTRATE, FUNCTION, CATALYTIC ACTIVITY, SUBSTRATE SPECIFICITY, KINETIC PARAMETERS.
  11. Cited for: VARIANTS COXPD14 THR-329 AND VAL-391, CHARACTERIZATION OF VARIANTS COXPD14 CYS-144; THR-329 AND VAL-391, FUNCTION, CATALYTIC ACTIVITY, KINETIC PARAMETERS.
  12. "Genomic analysis of mitochondrial diseases in a consanguineous population reveals novel candidate disease genes."
    Shamseldin H.E., Alshammari M., Al-Sheddi T., Salih M.A., Alkhalidi H., Kentab A., Repetto G.M., Hashem M., Alkuraya F.S.
    J. Med. Genet. 49:234-241(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANT COXPD14 CYS-144.

Entry informationi

Entry nameiSYFM_HUMAN
AccessioniPrimary (citable) accession number: O95363
Secondary accession number(s): B2R664
, Q53F66, Q5TCS3, Q6FG29, Q9NPY7, Q9P062
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 23, 2004
Last sequence update: May 1, 1999
Last modified: September 3, 2014
This is version 126 of the entry and version 1 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 6
    Human chromosome 6: entries, gene names and cross-references to MIM
  3. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  4. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  5. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  6. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  7. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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