Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Basket 0
(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Q9Y285

- SYFA_HUMAN

UniProt

Q9Y285 - SYFA_HUMAN

Protein

Phenylalanine--tRNA ligase alpha subunit

Gene

FARSA

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 145 (01 Oct 2014)
      Sequence version 3 (23 Jan 2007)
      Previous versions | rss
    • Help video
    • Feedback
    • Comment

    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. protein binding Source: IntAct
    5. 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

    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

    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

    ArrayExpressiQ9Y285.
    BgeeiQ9Y285.
    CleanExiHS_FARSA.
    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. 27 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 – 1985
    Turni201 – 2044
    Beta strandi212 – 2143
    Helixi226 – 24015
    Beta strandi251 – 2544
    Helixi255 – 2584
    Helixi260 – 2623
    Beta strandi266 – 2683
    Turni273 – 2753
    Beta strandi278 – 2803
    Helixi290 – 30112
    Helixi316 – 3194
    Beta strandi321 – 3244
    Helixi329 – 34012
    Beta strandi342 – 3443
    Beta strandi348 – 35710
    Beta strandi364 – 3663
    Beta strandi368 – 38114
    Helixi384 – 39613
    Turni397 – 3993
    Beta strandi404 – 4074
    Beta strandi414 – 4218
    Beta strandi430 – 4367
    Helixi440 – 4434
    Helixi444 – 4463
    Beta strandi452 – 46110
    Helixi462 – 4654
    Turni466 – 4705
    Helixi474 – 4763
    Helixi484 – 4896
    Turni497 – 4993

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    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.
    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. Align

    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

    MADGQVAELL LRRLEASDGG LDSAELAAEL GMEHQAVVGA VKSLQALGEV    50
    IEAELRSTKH WELTAEGEEI AREGSHEARV FRSIPPEGLA QSELMRLPSG 100
    KVGFSKAMSN KWIRVDKSAA DGPRVFRVVD SMEDEVQRRL QLVRGGQAEK 150
    LGEKERSELR KRKLLAEVTL KTYWVSKGSA FSTSISKQET ELSPEMISSG 200
    SWRDRPFKPY NFLAHGVLPD SGHLHPLLKV RSQFRQIFLE MGFTEMPTDN 250
    FIESSFWNFD ALFQPQQHPA RDQHDTFFLR DPAEALQLPM DYVQRVKRTH 300
    SQGGYGSQGY KYNWKLDEAR KNLLRTHTTS ASARALYRLA QKKPFTPVKY 350
    FSIDRVFRNE TLDATHLAEF HQIEGVVADH GLTLGHLMGV LREFFTKLGI 400
    TQLRFKPAYN PYTEPSMEVF SYHQGLKKWV EVGNSGVFRP EMLLPMGLPE 450
    NVSVIAWGLS LERPTMIKYG INNIRELVGH KVNLQMVYDS PLCRLDAEPR 500
    PPPTQEAA 508
    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.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti179 – 1791S → G in BAA95666. 1 PublicationCurated
    Sequence conflicti376 – 3761V → L in BAA95666. 1 PublicationCurated

    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:
    EMBL
    GenBank
    DDBJ
    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.
    PIRiT45074.
    RefSeqiNP_004452.1. NM_004461.2.
    UniGeneiHs.23111.

    Genome annotation databases

    EnsembliENST00000314606; ENSP00000320309; ENSG00000179115.
    ENST00000423140; ENSP00000396548; ENSG00000179115.
    GeneIDi2193.
    KEGGihsa:2193.
    UCSCiuc002mvs.2. human.

    Polymorphism databases

    DMDMi12643946.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    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 .
    CCDSi CCDS12287.1.
    PIRi T45074.
    RefSeqi NP_004452.1. NM_004461.2.
    UniGenei Hs.23111.

    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 A/C/E/G/I/K/M/O 1-508 [» ]
    ProteinModelPortali Q9Y285.
    SMRi Q9Y285. Positions 1-508.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 108487. 27 interactions.
    DIPi DIP-53610N.
    IntActi Q9Y285. 12 interactions.
    MINTi MINT-1378519.
    STRINGi 9606.ENSP00000320309.

    Chemistry

    DrugBanki DB00120. L-Phenylalanine.

    PTM databases

    PhosphoSitei Q9Y285.

    Polymorphism databases

    DMDMi 12643946.

    Proteomic databases

    MaxQBi Q9Y285.
    PaxDbi Q9Y285.
    PeptideAtlasi Q9Y285.
    PRIDEi Q9Y285.

    Protocols and materials databases

    DNASUi 2193.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000314606 ; ENSP00000320309 ; ENSG00000179115 .
    ENST00000423140 ; ENSP00000396548 ; ENSG00000179115 .
    GeneIDi 2193.
    KEGGi hsa:2193.
    UCSCi uc002mvs.2. human.

    Organism-specific databases

    CTDi 2193.
    GeneCardsi GC19M013033.
    HGNCi HGNC:3592. FARSA.
    HPAi HPA001911.
    MIMi 602918. gene.
    neXtProti NX_Q9Y285.
    PharmGKBi PA28005.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG0016.
    HOGENOMi HOG000230294.
    HOVERGENi HBG068046.
    InParanoidi Q9Y285.
    KOi K01889.
    PhylomeDBi Q9Y285.
    TreeFami TF300647.

    Enzyme and pathway databases

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

    Miscellaneous databases

    GeneWikii FARSA_(gene).
    GenomeRNAii 2193.
    NextBioi 8865.
    PROi Q9Y285.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q9Y285.
    Bgeei Q9Y285.
    CleanExi HS_FARSA.
    Genevestigatori Q9Y285.

    Family and domain databases

    Gene3Di 1.10.10.10. 1 hit.
    InterProi IPR006195. aa-tRNA-synth_II.
    IPR004529. Phe-tRNA-synth_IIc_asu.
    IPR002319. Phenylalanyl-tRNA_Synthase.
    IPR011991. WHTH_DNA-bd_dom.
    [Graphical view ]
    Pfami PF01409. tRNA-synt_2d. 1 hit.
    [Graphical view ]
    TIGRFAMsi TIGR00468. pheS. 1 hit.
    PROSITEi PS50862. AA_TRNA_LIGASE_II. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    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].
    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].
    15. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [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: October 1, 2014
    This is version 145 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