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Protein

Phenylalanine--tRNA ligase alpha subunit

Gene

FARSA

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 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. phenylalanine-tRNA ligase activity Source: ProtInc
  3. poly(A) RNA binding Source: UniProtKB
  4. tRNA binding Source: InterPro

GO - Biological processi

  1. gene expression Source: Reactome
  2. phenylalanyl-tRNA aminoacylation Source: InterPro
  3. tRNA aminoacylation for protein translation Source: Reactome
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 alpha subunit (EC:6.1.1.20)
Alternative name(s):
CML33
Phenylalanyl-tRNA synthetase alpha subunit
Short name:
PheRS
Gene namesi
Name:FARSA
Synonyms:FARS, FARSL, FARSLA
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 19

Organism-specific databases

HGNCiHGNC:3592. FARSA.

Subcellular locationi

Cytoplasm By similarity

GO - Cellular componenti

  1. cytoplasm Source: ProtInc
  2. cytosol Source: Reactome
  3. membrane Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA28005.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed5 Publications
Chaini2 – 508507Phenylalanine--tRNA ligase alpha subunitPRO_0000126824Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylalanine4 Publications
Modified residuei193 – 1931Phosphoserine1 Publication
Modified residuei311 – 3111N6-acetyllysine1 Publication

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

MaxQBiQ9Y285.
PaxDbiQ9Y285.
PeptideAtlasiQ9Y285.
PRIDEiQ9Y285.

PTM databases

PhosphoSiteiQ9Y285.

Expressioni

Gene expression databases

BgeeiQ9Y285.
CleanExiHS_FARSA.
ExpressionAtlasiQ9Y285. baseline and differential.
GenevestigatoriQ9Y285.

Organism-specific databases

HPAiHPA001911.

Interactioni

Subunit structurei

Tetramer of two alpha and two beta subunits.By similarity

Binary interactionsi

WithEntry#Exp.IntActNotes
ECSITQ9BQ952EBI-725361,EBI-712452

Protein-protein interaction databases

BioGridi108487. 30 interactions.
DIPiDIP-53610N.
IntActiQ9Y285. 12 interactions.
MINTiMINT-1378519.
STRINGi9606.ENSP00000320309.

Structurei

Secondary structure

1
508
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Turni194 – 1985Combined sources
Turni201 – 2044Combined sources
Beta strandi212 – 2143Combined sources
Helixi226 – 24015Combined sources
Beta strandi251 – 2544Combined sources
Helixi255 – 2584Combined sources
Helixi260 – 2623Combined sources
Beta strandi266 – 2683Combined sources
Turni273 – 2753Combined sources
Beta strandi278 – 2803Combined sources
Helixi290 – 30112Combined sources
Helixi316 – 3194Combined sources
Beta strandi321 – 3244Combined sources
Helixi329 – 34012Combined sources
Beta strandi342 – 3443Combined sources
Beta strandi348 – 35710Combined sources
Beta strandi364 – 3663Combined sources
Beta strandi368 – 38114Combined sources
Helixi384 – 39613Combined sources
Turni397 – 3993Combined sources
Beta strandi404 – 4074Combined sources
Beta strandi414 – 4218Combined sources
Beta strandi430 – 4367Combined sources
Helixi440 – 4434Combined sources
Helixi444 – 4463Combined sources
Beta strandi452 – 46110Combined sources
Helixi462 – 4654Combined sources
Turni466 – 4705Combined sources
Helixi474 – 4763Combined sources
Helixi484 – 4896Combined sources
Turni497 – 4993Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3L4GX-ray3.30A/C/E/G/I/K/M/O1-508[»]
ProteinModelPortaliQ9Y285.
SMRiQ9Y285. Positions 1-508.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

eggNOGiCOG0016.
GeneTreeiENSGT00390000006387.
HOGENOMiHOG000230294.
HOVERGENiHBG068046.
InParanoidiQ9Y285.
KOiK01889.
PhylomeDBiQ9Y285.
TreeFamiTF300647.

Family and domain databases

Gene3Di1.10.10.10. 1 hit.
InterProiIPR006195. aa-tRNA-synth_II.
IPR004529. Phe-tRNA-synth_IIc_asu.
IPR002319. Phenylalanyl-tRNA_Synthase.
IPR011991. WHTH_DNA-bd_dom.
[Graphical view]
PfamiPF01409. tRNA-synt_2d. 1 hit.
[Graphical view]
TIGRFAMsiTIGR00468. pheS. 1 hit.
PROSITEiPS50862. AA_TRNA_LIGASE_II. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

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

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q9Y285-1) [UniParc]FASTAAdd to basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MADGQVAELL LRRLEASDGG LDSAELAAEL GMEHQAVVGA VKSLQALGEV
60 70 80 90 100
IEAELRSTKH WELTAEGEEI AREGSHEARV FRSIPPEGLA QSELMRLPSG
110 120 130 140 150
KVGFSKAMSN KWIRVDKSAA DGPRVFRVVD SMEDEVQRRL QLVRGGQAEK
160 170 180 190 200
LGEKERSELR KRKLLAEVTL KTYWVSKGSA FSTSISKQET ELSPEMISSG
210 220 230 240 250
SWRDRPFKPY NFLAHGVLPD SGHLHPLLKV RSQFRQIFLE MGFTEMPTDN
260 270 280 290 300
FIESSFWNFD ALFQPQQHPA RDQHDTFFLR DPAEALQLPM DYVQRVKRTH
310 320 330 340 350
SQGGYGSQGY KYNWKLDEAR KNLLRTHTTS ASARALYRLA QKKPFTPVKY
360 370 380 390 400
FSIDRVFRNE TLDATHLAEF HQIEGVVADH GLTLGHLMGV LREFFTKLGI
410 420 430 440 450
TQLRFKPAYN PYTEPSMEVF SYHQGLKKWV EVGNSGVFRP EMLLPMGLPE
460 470 480 490 500
NVSVIAWGLS LERPTMIKYG INNIRELVGH KVNLQMVYDS PLCRLDAEPR

PPPTQEAA
Length:508
Mass (Da):57,564
Last modified:January 23, 2007 - v3
Checksum:i99BC12E1F3C5FCFD
GO
Isoform 2 (identifier: Q9Y285-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     169-199: Missing.

Note: No experimental confirmation available.

Show »
Length:477
Mass (Da):54,158
Checksum:i156A50E73126F137
GO

Sequence cautioni

The sequence AAB51175.1 differs from that shown. Reason: Erroneous gene model prediction. Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti179 – 1791S → G in BAA95666 (Ref. 3) Curated
Sequence conflicti376 – 3761V → L in BAA95666 (Ref. 3) Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti341 – 3411Q → R.
Corresponds to variant rs35087277 [ dbSNP | Ensembl ].
VAR_052641

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei169 – 19931Missing in isoform 2. 1 PublicationVSP_056196Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U07424 mRNA. Translation: AAB61694.1.
AF042347 mRNA. Translation: AAD02221.1.
D84471 mRNA. Translation: BAA95666.1.
BT007198 mRNA. Translation: AAP35862.1.
AK304587 mRNA. Translation: BAG65375.1.
AD000092 Genomic DNA. Translation: AAB51175.1. Sequence problems.
BC006495 mRNA. Translation: AAH06495.1.
BC043565 mRNA. Translation: AAH43565.1.
CCDSiCCDS12287.1. [Q9Y285-1]
PIRiT45074.
RefSeqiNP_004452.1. NM_004461.2. [Q9Y285-1]
UniGeneiHs.23111.

Genome annotation databases

EnsembliENST00000314606; ENSP00000320309; ENSG00000179115. [Q9Y285-1]
ENST00000423140; ENSP00000396548; ENSG00000179115. [Q9Y285-2]
GeneIDi2193.
KEGGihsa:2193.
UCSCiuc002mvs.2. human. [Q9Y285-1]

Polymorphism databases

DMDMi12643946.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U07424 mRNA. Translation: AAB61694.1.
AF042347 mRNA. Translation: AAD02221.1.
D84471 mRNA. Translation: BAA95666.1.
BT007198 mRNA. Translation: AAP35862.1.
AK304587 mRNA. Translation: BAG65375.1.
AD000092 Genomic DNA. Translation: AAB51175.1. Sequence problems.
BC006495 mRNA. Translation: AAH06495.1.
BC043565 mRNA. Translation: AAH43565.1.
CCDSiCCDS12287.1. [Q9Y285-1]
PIRiT45074.
RefSeqiNP_004452.1. NM_004461.2. [Q9Y285-1]
UniGeneiHs.23111.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3L4GX-ray3.30A/C/E/G/I/K/M/O1-508[»]
ProteinModelPortaliQ9Y285.
SMRiQ9Y285. Positions 1-508.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi108487. 30 interactions.
DIPiDIP-53610N.
IntActiQ9Y285. 12 interactions.
MINTiMINT-1378519.
STRINGi9606.ENSP00000320309.

Chemistry

DrugBankiDB00120. L-Phenylalanine.

PTM databases

PhosphoSiteiQ9Y285.

Polymorphism databases

DMDMi12643946.

Proteomic databases

MaxQBiQ9Y285.
PaxDbiQ9Y285.
PeptideAtlasiQ9Y285.
PRIDEiQ9Y285.

Protocols and materials databases

DNASUi2193.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000314606; ENSP00000320309; ENSG00000179115. [Q9Y285-1]
ENST00000423140; ENSP00000396548; ENSG00000179115. [Q9Y285-2]
GeneIDi2193.
KEGGihsa:2193.
UCSCiuc002mvs.2. human. [Q9Y285-1]

Organism-specific databases

CTDi2193.
GeneCardsiGC19M013033.
HGNCiHGNC:3592. FARSA.
HPAiHPA001911.
MIMi602918. gene.
neXtProtiNX_Q9Y285.
PharmGKBiPA28005.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiCOG0016.
GeneTreeiENSGT00390000006387.
HOGENOMiHOG000230294.
HOVERGENiHBG068046.
InParanoidiQ9Y285.
KOiK01889.
PhylomeDBiQ9Y285.
TreeFamiTF300647.

Enzyme and pathway databases

BRENDAi6.1.1.20. 2681.
ReactomeiREACT_15306. Cytosolic tRNA aminoacylation.

Miscellaneous databases

GeneWikiiFARSA_(gene).
GenomeRNAii2193.
NextBioi35477457.
PROiQ9Y285.
SOURCEiSearch...

Gene expression databases

BgeeiQ9Y285.
CleanExiHS_FARSA.
ExpressionAtlasiQ9Y285. baseline and differential.
GenevestigatoriQ9Y285.

Family and domain databases

Gene3Di1.10.10.10. 1 hit.
InterProiIPR006195. aa-tRNA-synth_II.
IPR004529. Phe-tRNA-synth_IIc_asu.
IPR002319. Phenylalanyl-tRNA_Synthase.
IPR011991. WHTH_DNA-bd_dom.
[Graphical view]
PfamiPF01409. tRNA-synt_2d. 1 hit.
[Graphical view]
TIGRFAMsiTIGR00468. pheS. 1 hit.
PROSITEiPS50862. AA_TRNA_LIGASE_II. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "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."
    Sen S., Zhou H., Ripmaster T., Hittelman W.N., Schimmel P., White R.A.
    Proc. Natl. Acad. Sci. U.S.A. 94:6164-6169(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
  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] (ISOFORM 1).
  3. Motegi H., Noda T., Shiba K.
    Submitted (APR-1996) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    Tissue: Testis.
  4. "Cloning of human full-length CDSs in BD Creator(TM) system donor vector."
    Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., Phelan M., Farmer A.
    Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
  5. "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] (ISOFORM 2).
    Tissue: Uterus.
  6. "The DNA sequence and biology of human chromosome 19."
    Grimwood J., Gordon L.A., Olsen A.S., Terry A., Schmutz J., Lamerdin J.E., Hellsten U., Goodstein D., Couronne O., Tran-Gyamfi M., Aerts A., Altherr M., Ashworth L., Bajorek E., Black S., Branscomb E., Caenepeel S., Carrano A.V.
    , Caoile C., Chan Y.M., Christensen M., Cleland C.A., Copeland A., Dalin E., Dehal P., Denys M., Detter J.C., Escobar J., Flowers D., Fotopulos D., Garcia C., Georgescu A.M., Glavina T., Gomez M., Gonzales E., Groza M., Hammon N., Hawkins T., Haydu L., Ho I., Huang W., Israni S., Jett J., Kadner K., Kimball H., Kobayashi A., Larionov V., Leem S.-H., Lopez F., Lou Y., Lowry S., Malfatti S., Martinez D., McCready P.M., Medina C., Morgan J., Nelson K., Nolan M., Ovcharenko I., Pitluck S., Pollard M., Popkie A.P., Predki P., Quan G., Ramirez L., Rash S., Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A., She X., Smith D., Slezak T., Solovyev V., Thayer N., Tice H., Tsai M., Ustaszewska A., Vo N., Wagner M., Wheeler J., Wu K., Xie G., Yang J., Dubchak I., Furey T.S., DeJong P., Dickson M., Gordon D., Eichler E.E., Pennacchio L.A., Richardson P., Stubbs L., Rokhsar D.S., Myers R.M., Rubin E.M., Lucas S.M.
    Nature 428:529-535(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  7. "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] (ISOFORM 1).
    Tissue: Leukocyte and Lung.
  8. "Exploring proteomes and analyzing protein processing by mass spectrometric identification of sorted N-terminal peptides."
    Gevaert K., Goethals M., Martens L., Van Damme J., Staes A., Thomas G.R., Vandekerckhove J.
    Nat. Biotechnol. 21:566-569(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 2-12.
    Tissue: Platelet.
  9. Bienvenut W.V.
    Submitted (OCT-2004) to UniProtKB
    Cited for: PROTEIN SEQUENCE OF 2-12 AND 326-334, ACETYLATION AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY.
    Tissue: B-cell lymphoma.
  10. "Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle."
    Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., Greff Z., Keri G., Stemmann O., Mann M.
    Mol. Cell 31:438-448(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-193, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  11. "Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
    Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
    Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
  12. "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-311, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  13. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  14. "Comparative large-scale characterisation of plant vs. mammal proteins reveals similar and idiosyncratic N-alpha acetylation features."
    Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T., Giglione C.
    Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
  15. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiSYFA_HUMAN
AccessioniPrimary (citable) accession number: Q9Y285
Secondary accession number(s): B4E363, Q9NSD8, Q9Y4W8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 8, 2000
Last sequence update: January 23, 2007
Last modified: March 4, 2015
This is version 150 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, Direct protein sequencing, Reference proteome

Documents

  1. Aminoacyl-tRNA synthetases
    List of aminoacyl-tRNA synthetase entries
  2. Human chromosome 19
    Human chromosome 19: 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.