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P54136

- SYRC_HUMAN

UniProt

P54136 - SYRC_HUMAN

Protein

Arginine--tRNA ligase, cytoplasmic

Gene

RARS

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 146 (01 Oct 2014)
      Sequence version 2 (16 Apr 2002)
      Previous versions | rss
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    Functioni

    Forms part of a macromolecular complex that catalyzes the attachment of specific amino acids to cognate tRNAs during protein synthesis. Modulates the secretion of AIMP1 and may be involved in generation of the inflammatory cytokine EMAP2 from AIMP1.1 Publication

    Catalytic activityi

    ATP + L-arginine + tRNA(Arg) = AMP + diphosphate + L-arginyl-tRNA(Arg).

    Kineticsi

    1. KM=3.9 µM for arginine (ATP-PPi exchange at 37 degrees Celsius)1 Publication
    2. KM=3.5 µM for arginine (arginylation at 37 degrees Celsius)1 Publication
    3. KM=1183 µM for ATP (ATP-PPi exchange at 37 Celsius)1 Publication
    4. KM=910 µM for ATP (arginylation at 37 Celsius)1 Publication
    5. KM=0.05 µM for calf liver tRNA-Arg (ATP-PPi exchange at 37 Celsius)1 Publication
    6. KM=0.41 µM for calf liver tRNA-Arg (arginylation at 37 Celsius)1 Publication

    GO - Molecular functioni

    1. arginine binding Source: Ensembl
    2. arginine-tRNA ligase activity Source: Reactome
    3. ATP binding Source: UniProtKB-KW
    4. protein binding Source: IntAct
    5. tRNA binding Source: Ensembl

    GO - Biological processi

    1. arginyl-tRNA aminoacylation Source: ProtInc
    2. gene expression Source: Reactome
    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

    ReactomeiREACT_15306. Cytosolic tRNA aminoacylation.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Arginine--tRNA ligase, cytoplasmic (EC:6.1.1.19)
    Alternative name(s):
    Arginyl-tRNA synthetase
    Short name:
    ArgRS
    Gene namesi
    Name:RARS
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 5

    Organism-specific databases

    HGNCiHGNC:9870. RARS.

    Subcellular locationi

    Cytoplasm 2 Publications

    GO - Cellular componenti

    1. aminoacyl-tRNA synthetase multienzyme complex Source: Ensembl
    2. cytoplasm Source: HPA
    3. cytosol Source: Reactome
    4. extracellular vesicular exosome Source: UniProt
    5. membrane Source: UniProtKB
    6. mitochondrion Source: Ensembl
    7. nucleus Source: HPA

    Keywords - Cellular componenti

    Cytoplasm

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA34231.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 660660Arginine--tRNA ligase, cytoplasmicPRO_0000035797Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei1 – 11N-acetylmethionine3 Publications

    Keywords - PTMi

    Acetylation

    Proteomic databases

    MaxQBiP54136.
    PaxDbiP54136.
    PeptideAtlasiP54136.
    PRIDEiP54136.

    PTM databases

    PhosphoSiteiP54136.

    Expressioni

    Gene expression databases

    ArrayExpressiP54136.
    BgeeiP54136.
    CleanExiHS_RARS.
    GenevestigatoriP54136.

    Organism-specific databases

    HPAiHPA003979.
    HPA004130.

    Interactioni

    Subunit structurei

    Interacts (via N-terminus) with AIMP1 (via N-terminus); this stimulates its catalytic activity. Interacts (via N-terminus) with LARS2 (via C-terminus). Monomer; also part of a multisubunit complex that groups tRNA ligases for Arg, Asp, Glu, Gln, Ile, Leu, Lys, Met and Pro. Interacts with QARS.4 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    LARSQ9P2J53EBI-355482,EBI-356077

    Protein-protein interaction databases

    BioGridi111852. 37 interactions.
    IntActiP54136. 8 interactions.
    MINTiMINT-5006018.
    STRINGi9606.ENSP00000231572.

    Structurei

    3D structure databases

    ProteinModelPortaliP54136.
    SMRiP54136. Positions 74-659.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni1 – 7272Could be involved in the assembly of the multisynthetase complexAdd
    BLAST

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi201 – 21212"HIGH" regionAdd
    BLAST

    Domaini

    The N-terminus (AA 1-72) has two regions predicted to be alpha-helical that might be involved in the multisynthetase complex assembly.

    Sequence similaritiesi

    Phylogenomic databases

    eggNOGiCOG0018.
    HOGENOMiHOG000247212.
    HOVERGENiHBG029238.
    InParanoidiP54136.
    KOiK01887.
    OMAiIRNTIND.
    OrthoDBiEOG764725.
    PhylomeDBiP54136.
    TreeFamiTF106111.

    Family and domain databases

    Gene3Di1.10.730.10. 1 hit.
    3.30.1360.70. 1 hit.
    3.40.50.620. 1 hit.
    HAMAPiMF_00123. Arg_tRNA_synth.
    InterProiIPR001412. aa-tRNA-synth_I_CS.
    IPR001278. Arg-tRNA-ligase.
    IPR005148. Arg-tRNA-synth_N.
    IPR008909. DALR_anticod-bd.
    IPR014729. Rossmann-like_a/b/a_fold.
    IPR009080. tRNAsynth_1a_anticodon-bd.
    [Graphical view]
    PANTHERiPTHR11956. PTHR11956. 1 hit.
    PfamiPF03485. Arg_tRNA_synt_N. 1 hit.
    PF05746. DALR_1. 1 hit.
    PF00750. tRNA-synt_1d. 1 hit.
    [Graphical view]
    PRINTSiPR01038. TRNASYNTHARG.
    SMARTiSM01016. Arg_tRNA_synt_N. 1 hit.
    SM00836. DALR_1. 1 hit.
    [Graphical view]
    SUPFAMiSSF47323. SSF47323. 1 hit.
    SSF55190. SSF55190. 1 hit.
    TIGRFAMsiTIGR00456. argS. 1 hit.
    PROSITEiPS00178. AA_TRNA_LIGASE_I. 1 hit.
    [Graphical view]

    Sequences (2)i

    Sequence statusi: Complete.

    This entry describes 2 isoformsi produced by alternative initiation. Align

    Isoform Complexed (identifier: P54136-1) [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

    MDVLVSECSA RLLQQEEEIK SLTAEIDRLK NCGCLGASPN LEQLQEENLK    50
    LKYRLNILRK SLQAERNKPT KNMINIISRL QEVFGHAIKA AYPDLENPPL 100
    LVTPSQQAKF GDYQCNSAMG ISQMLKTKEQ KVNPREIAEN ITKHLPDNEC 150
    IEKVEIAGPG FINVHLRKDF VSEQLTSLLV NGVQLPALGE NKKVIVDFSS 200
    PNIAKEMHVG HLRSTIIGES ISRLFEFAGY DVLRLNHVGD WGTQFGMLIA 250
    HLQDKFPDYL TVSPPIGDLQ VFYKESKKRF DTEEEFKKRA YQCVVLLQGK 300
    NPDITKAWKL ICDVSRQELN KIYDALDVSL IERGESFYQD RMNDIVKEFE 350
    DRGFVQVDDG RKIVFVPGCS IPLTIVKSDG GYTYDTSDLA AIKQRLFEEK 400
    ADMIIYVVDN GQSVHFQTIF AAAQMIGWYD PKVTRVFHAG FGVVLGEDKK 450
    KFKTRSGETV RLMDLLGEGL KRSMDKLKEK ERDKVLTAEE LNAAQTSVAY 500
    GCIKYADLSH NRLNDYIFSF DKMLDDRGNT AAYLLYAFTR IRSIARLANI 550
    DEEMLQKAAR ETKILLDHEK EWKLGRCILR FPEILQKILD DLFLHTLCDY 600
    IYELATAFTE FYDSCYCVEK DRQTGKILKV NMWRMLLCEA VAAVMAKGFD 650
    ILGIKPVQRM 660
    Length:660
    Mass (Da):75,379
    Last modified:April 16, 2002 - v2
    Checksum:iFE9FB5C910709956
    GO
    Isoform Monomeric (identifier: P54136-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-72: Missing.

    Show »
    Length:588
    Mass (Da):67,140
    Checksum:i857EA1F69F3B6A3B
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti39 – 391P → S in AAB35627. (PubMed:7590355)Curated
    Sequence conflicti130 – 1312QK → PE in AAB35627. (PubMed:7590355)Curated
    Sequence conflicti135 – 1373REI → GEF in AAB35627. (PubMed:7590355)Curated
    Sequence conflicti147 – 15610DNECIEKVEI → AMDVLKRVEF in AAB35627. (PubMed:7590355)Curated
    Sequence conflicti164 – 1641V → G in AAB35627. (PubMed:7590355)Curated
    Sequence conflicti278 – 2781K → N in BAG37326. (PubMed:14702039)Curated
    Sequence conflicti308 – 3125WKLIC → YLLMS in AAB35627. (PubMed:7590355)Curated
    Sequence conflicti341 – 3411R → G in BAD96517. 1 PublicationCurated
    Sequence conflicti358 – 3581D → G in BAG37326. (PubMed:14702039)Curated
    Sequence conflicti487 – 4871T → A in BAD96517. 1 PublicationCurated
    Sequence conflicti567 – 5671D → V in AAB35627. (PubMed:7590355)Curated
    Sequence conflicti635 – 6406MLLCEA → ILCET in AAB35627. (PubMed:7590355)Curated
    Sequence conflicti651 – 6511I → T in AAB35627. (PubMed:7590355)Curated
    Sequence conflicti657 – 6604VQRM → GPRV in AAB35627. (PubMed:7590355)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti3 – 31V → I.
    Corresponds to variant rs244903 [ dbSNP | Ensembl ].
    VAR_020106
    Natural varianti135 – 1351R → G.
    Corresponds to variant rs1059443 [ dbSNP | Ensembl ].
    VAR_052635
    Natural varianti397 – 3971F → Y.
    Corresponds to variant rs2305734 [ dbSNP | Ensembl ].
    VAR_020107

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 7272Missing in isoform Monomeric. CuratedVSP_018905Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    S80343 mRNA. Translation: AAB35627.1.
    BT007394 mRNA. Translation: AAP36058.1.
    AK314795 mRNA. Translation: BAG37326.1.
    AK222797 mRNA. Translation: BAD96517.1.
    BC000528 mRNA. Translation: AAH00528.1.
    BC014619 mRNA. Translation: AAH14619.1.
    CCDSiCCDS4367.1. [P54136-1]
    PIRiJC4365.
    RefSeqiNP_002878.2. NM_002887.3. [P54136-1]
    UniGeneiHs.654907.

    Genome annotation databases

    EnsembliENST00000231572; ENSP00000231572; ENSG00000113643. [P54136-1]
    GeneIDi5917.
    KEGGihsa:5917.
    UCSCiuc003lzx.3. human. [P54136-1]

    Polymorphism databases

    DMDMi20178331.

    Keywords - Coding sequence diversityi

    Alternative initiation, Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    S80343 mRNA. Translation: AAB35627.1 .
    BT007394 mRNA. Translation: AAP36058.1 .
    AK314795 mRNA. Translation: BAG37326.1 .
    AK222797 mRNA. Translation: BAD96517.1 .
    BC000528 mRNA. Translation: AAH00528.1 .
    BC014619 mRNA. Translation: AAH14619.1 .
    CCDSi CCDS4367.1. [P54136-1 ]
    PIRi JC4365.
    RefSeqi NP_002878.2. NM_002887.3. [P54136-1 ]
    UniGenei Hs.654907.

    3D structure databases

    ProteinModelPortali P54136.
    SMRi P54136. Positions 74-659.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 111852. 37 interactions.
    IntActi P54136. 8 interactions.
    MINTi MINT-5006018.
    STRINGi 9606.ENSP00000231572.

    Chemistry

    BindingDBi P54136.
    ChEMBLi CHEMBL2824.

    PTM databases

    PhosphoSitei P54136.

    Polymorphism databases

    DMDMi 20178331.

    Proteomic databases

    MaxQBi P54136.
    PaxDbi P54136.
    PeptideAtlasi P54136.
    PRIDEi P54136.

    Protocols and materials databases

    DNASUi 5917.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000231572 ; ENSP00000231572 ; ENSG00000113643 . [P54136-1 ]
    GeneIDi 5917.
    KEGGi hsa:5917.
    UCSCi uc003lzx.3. human. [P54136-1 ]

    Organism-specific databases

    CTDi 5917.
    GeneCardsi GC05P167846.
    HGNCi HGNC:9870. RARS.
    HPAi HPA003979.
    HPA004130.
    MIMi 107820. gene.
    neXtProti NX_P54136.
    PharmGKBi PA34231.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG0018.
    HOGENOMi HOG000247212.
    HOVERGENi HBG029238.
    InParanoidi P54136.
    KOi K01887.
    OMAi IRNTIND.
    OrthoDBi EOG764725.
    PhylomeDBi P54136.
    TreeFami TF106111.

    Enzyme and pathway databases

    Reactomei REACT_15306. Cytosolic tRNA aminoacylation.

    Miscellaneous databases

    GeneWikii RARS_(gene).
    GenomeRNAii 5917.
    NextBioi 23038.
    PROi P54136.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P54136.
    Bgeei P54136.
    CleanExi HS_RARS.
    Genevestigatori P54136.

    Family and domain databases

    Gene3Di 1.10.730.10. 1 hit.
    3.30.1360.70. 1 hit.
    3.40.50.620. 1 hit.
    HAMAPi MF_00123. Arg_tRNA_synth.
    InterProi IPR001412. aa-tRNA-synth_I_CS.
    IPR001278. Arg-tRNA-ligase.
    IPR005148. Arg-tRNA-synth_N.
    IPR008909. DALR_anticod-bd.
    IPR014729. Rossmann-like_a/b/a_fold.
    IPR009080. tRNAsynth_1a_anticodon-bd.
    [Graphical view ]
    PANTHERi PTHR11956. PTHR11956. 1 hit.
    Pfami PF03485. Arg_tRNA_synt_N. 1 hit.
    PF05746. DALR_1. 1 hit.
    PF00750. tRNA-synt_1d. 1 hit.
    [Graphical view ]
    PRINTSi PR01038. TRNASYNTHARG.
    SMARTi SM01016. Arg_tRNA_synt_N. 1 hit.
    SM00836. DALR_1. 1 hit.
    [Graphical view ]
    SUPFAMi SSF47323. SSF47323. 1 hit.
    SSF55190. SSF55190. 1 hit.
    TIGRFAMsi TIGR00456. argS. 1 hit.
    PROSITEi PS00178. AA_TRNA_LIGASE_I. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Cloning and characterization of cDNA encoding a human arginyl-tRNA synthetase."
      Girjes A.A., Hobson K., Chen P., Lavin M.F.
      Gene 164:347-350(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    2. "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].
    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].
    4. Suzuki Y., Sugano S., 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: Liver.
    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] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Tissue: Muscle.
    6. "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 1-11.
      Tissue: Platelet.
    7. "Precursor of pro-apoptotic cytokine modulates aminoacylation activity of tRNA synthetase."
      Park S.G., Jung K.H., Lee J.S., Jo Y.J., Motegi H., Kim S., Shiba K.
      J. Biol. Chem. 274:16673-16676(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH AIMP1.
    8. "The C-terminal appended domain of human cytosolic leucyl-tRNA synthetase is indispensable in its interaction with arginyl-tRNA synthetase in the multi-tRNA synthetase complex."
      Ling C., Yao Y.N., Zheng Y.G., Wei H., Wang L., Wu X.F., Wang E.D.
      J. Biol. Chem. 280:34755-34763(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: BIOPHYSICOCHEMICAL PROPERTIES, SUBCELLULAR LOCATION, INTERACTION WITH LARS2.
    9. "Two forms of human cytoplasmic arginyl-tRNA synthetase produced from two translation initiations by a single mRNA."
      Zheng Y.-G., Wei H., Ling C., Xu M.-G., Wang E.-D.
      Biochemistry 45:1338-1344(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBCELLULAR LOCATION, ALTERNATIVE INITIATION.
    10. "Proteasomes and RARS modulate AIMP1/EMAP II secretion in human cancer cell lines."
      Bottoni A., Vignali C., Piccin D., Tagliati F., Luchin A., Zatelli M.C., Uberti E.C.
      J. Cell. Physiol. 212:293-297(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH AIMP1.
    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 MET-1, 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: 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 MET-1, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    15. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    16. "Mutations in QARS, encoding glutaminyl-tRNA synthetase, cause progressive microcephaly, cerebral-cerebellar atrophy, and intractable seizures."
      Zhang X., Ling J., Barcia G., Jing L., Wu J., Barry B.J., Mochida G.H., Hill R.S., Weimer J.M., Stein Q., Poduri A., Partlow J.N., Ville D., Dulac O., Yu T.W., Lam A.T., Servattalab S., Rodriguez J.
      , Boddaert N., Munnich A., Colleaux L., Zon L.I., Soll D., Walsh C.A., Nabbout R.
      Am. J. Hum. Genet. 94:547-558(2014) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH QARS.

    Entry informationi

    Entry nameiSYRC_HUMAN
    AccessioniPrimary (citable) accession number: P54136
    Secondary accession number(s): B2RBS9, Q53GY4, Q9BWA1
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: October 1, 1996
    Last sequence update: April 16, 2002
    Last modified: October 1, 2014
    This is version 146 of the entry and version 2 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

    Complete proteome, Direct protein sequencing, Reference proteome

    Documents

    1. Aminoacyl-tRNA synthetases
      List of aminoacyl-tRNA synthetase entries
    2. Human chromosome 5
      Human chromosome 5: 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. SIMILARITY comments
      Index of protein domains and families

    External Data

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