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P54577

- SYYC_HUMAN

UniProt

P54577 - SYYC_HUMAN

Protein

Tyrosine--tRNA ligase, cytoplasmic

Gene

YARS

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 157 (01 Oct 2014)
      Sequence version 4 (23 Jan 2007)
      Previous versions | rss
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    Functioni

    Catalyzes the attachment of tyrosine to tRNA(Tyr) in a two-step reaction: tyrosine is first activated by ATP to form Tyr-AMP and then transferred to the acceptor end of tRNA(Tyr).By similarity

    Catalytic activityi

    ATP + L-tyrosine + tRNA(Tyr) = AMP + diphosphate + L-tyrosyl-tRNA(Tyr).

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei39 – 391Tyrosine1 Publication
    Binding sitei166 – 1661Tyrosine1 Publication
    Binding sitei170 – 1701Tyrosine1 Publication
    Binding sitei173 – 1731Tyrosine1 Publication
    Binding sitei188 – 1881Tyrosine1 Publication

    GO - Molecular functioni

    1. ATP binding Source: UniProtKB-KW
    2. interleukin-8 receptor binding Source: ProtInc
    3. poly(A) RNA binding Source: UniProtKB
    4. signal transducer activity Source: ProtInc
    5. tRNA binding Source: UniProtKB-KW
    6. tyrosine-tRNA ligase activity Source: Reactome

    GO - Biological processi

    1. apoptotic process Source: ProtInc
    2. gene expression Source: Reactome
    3. signal transduction Source: GOC
    4. tRNA aminoacylation for protein translation Source: Reactome
    5. tyrosyl-tRNA aminoacylation Source: ProtInc

    Keywords - Molecular functioni

    Aminoacyl-tRNA synthetase, Ligase

    Keywords - Biological processi

    Protein biosynthesis

    Keywords - Ligandi

    ATP-binding, Nucleotide-binding, RNA-binding, tRNA-binding

    Enzyme and pathway databases

    ReactomeiREACT_15306. Cytosolic tRNA aminoacylation.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Tyrosine--tRNA ligase, cytoplasmic (EC:6.1.1.1)
    Alternative name(s):
    Tyrosyl-tRNA synthetase
    Short name:
    TyrRS
    Cleaved into the following chain:
    Gene namesi
    Name:YARS
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 1

    Organism-specific databases

    HGNCiHGNC:12840. YARS.

    Subcellular locationi

    Cytoplasm 1 Publication

    GO - Cellular componenti

    1. cytoplasm Source: HPA
    2. cytosol Source: Reactome
    3. extracellular space Source: ProtInc
    4. nucleus Source: HPA

    Keywords - Cellular componenti

    Cytoplasm

    Pathology & Biotechi

    Involvement in diseasei

    Charcot-Marie-Tooth disease, dominant, intermediate type, C (CMTDIC) [MIM:608323]: A form of Charcot-Marie-Tooth disease, a disorder of the peripheral nervous system, characterized by progressive weakness and atrophy, initially of the peroneal muscles and later of the distal muscles of the arms. The dominant intermediate type C is characterized by clinical and pathologic features intermediate between demyelinating and axonal peripheral neuropathies, and motor median nerve conduction velocities ranging from 25 to 45 m/sec.1 Publication
    Note: The disease is caused by mutations affecting the gene represented in this entry.
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti41 – 411G → R in CMTDIC; partial loss of activity. 1 Publication
    VAR_026681
    Natural varianti153 – 1564Missing in CMTDIC.
    VAR_026682
    Natural varianti196 – 1961E → K in CMTDIC; partial loss of activity. 1 Publication
    VAR_026684

    Keywords - Diseasei

    Charcot-Marie-Tooth disease, Disease mutation, Neurodegeneration, Neuropathy

    Organism-specific databases

    MIMi608323. phenotype.
    Orphaneti100045. Autosomal dominant intermediate Charcot-Marie-Tooth disease type C.
    PharmGKBiPA37431.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 528528Tyrosine--tRNA ligase, cytoplasmicPRO_0000423285Add
    BLAST
    Initiator methioninei1 – 11Removed; alternate2 Publications
    Chaini2 – 528527Tyrosine--tRNA ligase, cytoplasmic, N-terminally processedPRO_0000055673Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei1 – 11N-acetylmethionine1 Publication
    Modified residuei2 – 21N-acetylglycine; in Tyrosine--tRNA ligase, cytoplasmic, N-terminally processed2 Publications
    Modified residuei197 – 1971N6-acetyllysine1 Publication
    Modified residuei206 – 2061N6-acetyllysine1 Publication
    Modified residuei474 – 4741N6-acetyllysine1 Publication
    Modified residuei482 – 4821N6-acetyllysine1 Publication
    Modified residuei490 – 4901N6-acetyllysine1 Publication

    Keywords - PTMi

    Acetylation

    Proteomic databases

    MaxQBiP54577.
    PaxDbiP54577.
    PeptideAtlasiP54577.
    PRIDEiP54577.

    2D gel databases

    REPRODUCTION-2DPAGEIPI00007074.

    PTM databases

    PhosphoSiteiP54577.

    Miscellaneous databases

    PMAP-CutDBP54577.

    Expressioni

    Gene expression databases

    BgeeiP54577.
    CleanExiHS_YARS.
    GenevestigatoriP54577.

    Organism-specific databases

    HPAiHPA017936.
    HPA018950.
    HPA018954.

    Interactioni

    Subunit structurei

    Homodimer.2 Publications

    Protein-protein interaction databases

    BioGridi114134. 15 interactions.
    IntActiP54577. 1 interaction.
    STRINGi9606.ENSP00000362576.

    Structurei

    Secondary structure

    1
    528
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi7 – 159
    Beta strandi19 – 224
    Helixi24 – 318
    Beta strandi37 – 426
    Helixi50 – 523
    Helixi53 – 6412
    Beta strandi68 – 736
    Helixi75 – 806
    Turni81 – 844
    Helixi87 – 10822
    Beta strandi115 – 1195
    Helixi120 – 1223
    Turni123 – 1253
    Helixi127 – 13711
    Helixi142 – 1487
    Turni149 – 1524
    Helixi161 – 17616
    Beta strandi180 – 1856
    Helixi186 – 1883
    Helixi189 – 19810
    Helixi199 – 2024
    Beta strandi208 – 2125
    Helixi238 – 2469
    Beta strandi247 – 2493
    Helixi259 – 2668
    Turni267 – 2737
    Beta strandi275 – 2773
    Helixi281 – 2833
    Beta strandi287 – 2915
    Helixi292 – 3009
    Helixi306 – 32722
    Helixi331 – 34010
    Helixi365 – 3673
    Beta strandi370 – 38011
    Beta strandi388 – 3936
    Beta strandi395 – 3984
    Beta strandi400 – 4056
    Turni407 – 4093
    Helixi412 – 4143
    Turni415 – 4173
    Beta strandi419 – 4235
    Beta strandi429 – 4313
    Beta strandi434 – 4363
    Beta strandi442 – 45413
    Beta strandi466 – 4694
    Beta strandi479 – 4813
    Helixi483 – 4853
    Helixi487 – 4926
    Beta strandi495 – 4973
    Beta strandi501 – 5055
    Beta strandi508 – 5125
    Beta strandi526 – 5283

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1N3LX-ray1.18A1-364[»]
    1NTGX-ray2.21A/B/C/D359-528[»]
    1Q11X-ray1.60A1-364[»]
    ProteinModelPortaliP54577.
    SMRiP54577. Positions 4-342, 360-528.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP54577.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini364 – 468105tRNA-bindingPROSITE-ProRule annotationAdd
    BLAST

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi44 – 529"HIGH" region
    Motifi222 – 2265"KMSKS" region

    Sequence similaritiesi

    Contains 1 tRNA-binding domain.PROSITE-ProRule annotation

    Phylogenomic databases

    eggNOGiCOG0162.
    HOGENOMiHOG000228237.
    HOVERGENiHBG080113.
    InParanoidiP54577.
    KOiK01866.
    OMAiNRQVEPL.
    OrthoDBiEOG79CXZ2.
    PhylomeDBiP54577.
    TreeFamiTF300898.

    Family and domain databases

    Gene3Di2.40.50.140. 1 hit.
    3.40.50.620. 1 hit.
    InterProiIPR002305. aa-tRNA-synth_Ic.
    IPR012340. NA-bd_OB-fold.
    IPR014729. Rossmann-like_a/b/a_fold.
    IPR002547. tRNA-bd_dom.
    IPR002307. Tyr-tRNA-ligase.
    [Graphical view]
    PfamiPF00579. tRNA-synt_1b. 1 hit.
    PF01588. tRNA_bind. 1 hit.
    [Graphical view]
    PRINTSiPR01040. TRNASYNTHTYR.
    SUPFAMiSSF50249. SSF50249. 1 hit.
    TIGRFAMsiTIGR00234. tyrS. 1 hit.
    PROSITEiPS50886. TRBD. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

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

    P54577-1 [UniParc]FASTAAdd to Basket

    « Hide

    MGDAPSPEEK LHLITRNLQE VLGEEKLKEI LKERELKIYW GTATTGKPHV    50
    AYFVPMSKIA DFLKAGCEVT ILFADLHAYL DNMKAPWELL ELRVSYYENV 100
    IKAMLESIGV PLEKLKFIKG TDYQLSKEYT LDVYRLSSVV TQHDSKKAGA 150
    EVVKQVEHPL LSGLLYPGLQ ALDEEYLKVD AQFGGIDQRK IFTFAEKYLP 200
    ALGYSKRVHL MNPMVPGLTG SKMSSSEEES KIDLLDRKED VKKKLKKAFC 250
    EPGNVENNGV LSFIKHVLFP LKSEFVILRD EKWGGNKTYT AYVDLEKDFA 300
    AEVVHPGDLK NSVEVALNKL LDPIREKFNT PALKKLASAA YPDPSKQKPM 350
    AKGPAKNSEP EEVIPSRLDI RVGKIITVEK HPDADSLYVE KIDVGEAEPR 400
    TVVSGLVQFV PKEELQDRLV VVLCNLKPQK MRGVESQGML LCASIEGINR 450
    QVEPLDPPAG SAPGEHVFVK GYEKGQPDEE LKPKKKVFEK LQADFKISEE 500
    CIAQWKQTNF MTKLGSISCK SLKGGNIS 528
    Length:528
    Mass (Da):59,143
    Last modified:January 23, 2007 - v4
    Checksum:i00C7E88843905780
    GO

    Sequence cautioni

    The sequence AAB39406.1 differs from that shown. Reason: Frameshift at position 354.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti143 – 1431H → R in BAD97328. 1 PublicationCurated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti41 – 411G → R in CMTDIC; partial loss of activity. 1 Publication
    VAR_026681
    Natural varianti153 – 1564Missing in CMTDIC.
    VAR_026682
    Natural varianti170 – 1701Q → H.
    Corresponds to variant rs2128600 [ dbSNP | Ensembl ].
    VAR_026683
    Natural varianti196 – 1961E → K in CMTDIC; partial loss of activity. 1 Publication
    VAR_026684

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U40714 mRNA. Translation: AAB39406.1. Frameshift.
    U89436 mRNA. Translation: AAB88409.1.
    AK125213 mRNA. Translation: BAG54166.1.
    AK223608 mRNA. Translation: BAD97328.1.
    CH471059 Genomic DNA. Translation: EAX07506.1.
    CH471059 Genomic DNA. Translation: EAX07507.1.
    BC001933 mRNA. Translation: AAH01933.1.
    BC004151 mRNA. Translation: AAH04151.1.
    BC016689 mRNA. Translation: AAH16689.1.
    CCDSiCCDS368.1.
    RefSeqiNP_003671.1. NM_003680.3.
    UniGeneiHs.213264.

    Genome annotation databases

    EnsembliENST00000373477; ENSP00000362576; ENSG00000134684.
    GeneIDi8565.
    KEGGihsa:8565.
    UCSCiuc001bvy.1. human.

    Polymorphism databases

    DMDMi13638438.

    Keywords - Coding sequence diversityi

    Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U40714 mRNA. Translation: AAB39406.1 . Frameshift.
    U89436 mRNA. Translation: AAB88409.1 .
    AK125213 mRNA. Translation: BAG54166.1 .
    AK223608 mRNA. Translation: BAD97328.1 .
    CH471059 Genomic DNA. Translation: EAX07506.1 .
    CH471059 Genomic DNA. Translation: EAX07507.1 .
    BC001933 mRNA. Translation: AAH01933.1 .
    BC004151 mRNA. Translation: AAH04151.1 .
    BC016689 mRNA. Translation: AAH16689.1 .
    CCDSi CCDS368.1.
    RefSeqi NP_003671.1. NM_003680.3.
    UniGenei Hs.213264.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1N3L X-ray 1.18 A 1-364 [» ]
    1NTG X-ray 2.21 A/B/C/D 359-528 [» ]
    1Q11 X-ray 1.60 A 1-364 [» ]
    ProteinModelPortali P54577.
    SMRi P54577. Positions 4-342, 360-528.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 114134. 15 interactions.
    IntActi P54577. 1 interaction.
    STRINGi 9606.ENSP00000362576.

    Chemistry

    BindingDBi P54577.
    ChEMBLi CHEMBL3179.
    DrugBanki DB00135. L-Tyrosine.

    PTM databases

    PhosphoSitei P54577.

    Polymorphism databases

    DMDMi 13638438.

    2D gel databases

    REPRODUCTION-2DPAGE IPI00007074.

    Proteomic databases

    MaxQBi P54577.
    PaxDbi P54577.
    PeptideAtlasi P54577.
    PRIDEi P54577.

    Protocols and materials databases

    DNASUi 8565.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000373477 ; ENSP00000362576 ; ENSG00000134684 .
    GeneIDi 8565.
    KEGGi hsa:8565.
    UCSCi uc001bvy.1. human.

    Organism-specific databases

    CTDi 8565.
    GeneCardsi GC01M033240.
    HGNCi HGNC:12840. YARS.
    HPAi HPA017936.
    HPA018950.
    HPA018954.
    MIMi 603623. gene.
    608323. phenotype.
    neXtProti NX_P54577.
    Orphaneti 100045. Autosomal dominant intermediate Charcot-Marie-Tooth disease type C.
    PharmGKBi PA37431.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG0162.
    HOGENOMi HOG000228237.
    HOVERGENi HBG080113.
    InParanoidi P54577.
    KOi K01866.
    OMAi NRQVEPL.
    OrthoDBi EOG79CXZ2.
    PhylomeDBi P54577.
    TreeFami TF300898.

    Enzyme and pathway databases

    Reactomei REACT_15306. Cytosolic tRNA aminoacylation.

    Miscellaneous databases

    ChiTaRSi YARS. human.
    EvolutionaryTracei P54577.
    GeneWikii YARS.
    GenomeRNAii 8565.
    NextBioi 32113.
    PMAP-CutDB P54577.
    PROi P54577.
    SOURCEi Search...

    Gene expression databases

    Bgeei P54577.
    CleanExi HS_YARS.
    Genevestigatori P54577.

    Family and domain databases

    Gene3Di 2.40.50.140. 1 hit.
    3.40.50.620. 1 hit.
    InterProi IPR002305. aa-tRNA-synth_Ic.
    IPR012340. NA-bd_OB-fold.
    IPR014729. Rossmann-like_a/b/a_fold.
    IPR002547. tRNA-bd_dom.
    IPR002307. Tyr-tRNA-ligase.
    [Graphical view ]
    Pfami PF00579. tRNA-synt_1b. 1 hit.
    PF01588. tRNA_bind. 1 hit.
    [Graphical view ]
    PRINTSi PR01040. TRNASYNTHTYR.
    SUPFAMi SSF50249. SSF50249. 1 hit.
    TIGRFAMsi TIGR00234. tyrS. 1 hit.
    PROSITEi PS50886. TRBD. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Evidence that two present-day components needed for the genetic code appeared after nucleated cells separated from eubacteria."
      Ribas de Pouplana L., Frugier M., Quinn C.L., Schimmel P.
      Proc. Natl. Acad. Sci. U.S.A. 93:166-170(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    2. "Human tyrosyl-tRNA synthetase shares amino acid sequence homology with a putative cytokine."
      Kleeman T.A., Wei D., Simpson K.L., First E.A.
      J. Biol. Chem. 272:14420-14425(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    3. "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].
      Tissue: Brain.
    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].
    5. 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: Bone and Lung.
    7. "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 2-16.
      Tissue: Platelet.
    8. Bienvenut W.V.
      Submitted (OCT-2004) to UniProtKB
      Cited for: PROTEIN SEQUENCE OF 2-16, ACETYLATION AT GLY-2, IDENTIFICATION BY MASS SPECTROMETRY.
      Tissue: B-cell lymphoma.
    9. "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 MET-1 AND GLY-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    10. "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-197; LYS-206; LYS-474; LYS-482 AND LYS-490, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    11. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    12. "Crystal structure of a human aminoacyl-tRNA synthetase cytokine."
      Yang X.-L., Skene R.J., McRee D.E., Schimmel P.
      Proc. Natl. Acad. Sci. U.S.A. 99:15369-15374(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.18 ANGSTROMS) OF 1-342, SUBUNIT.
    13. "Crystal structures that suggest late development of genetic code components for differentiating aromatic side chains."
      Yang X.-L., Otero F.J., Skene R.J., McRee D.E., Schimmel P., Ribas de Pouplana L.
      Proc. Natl. Acad. Sci. U.S.A. 100:15376-15380(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.6 ANGSTROMS) OF 1-364 IN COMPLEX WITH TYROSINE.
    14. Cited for: SUBCELLULAR LOCATION, VARIANTS CMTDIC 153-VAL--VAL-156 DEL; ARG-41 AND LYS-196, CHARACTERIZATION OF VARIANTS CMTDIC ARG-41 AND LYS-196.

    Entry informationi

    Entry nameiSYYC_HUMAN
    AccessioniPrimary (citable) accession number: P54577
    Secondary accession number(s): B3KWK4
    , D3DPQ4, O43276, Q53EN1
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: October 1, 1996
    Last sequence update: January 23, 2007
    Last modified: October 1, 2014
    This is version 157 of the entry and version 4 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 1
      Human chromosome 1: 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