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P49589

- SYCC_HUMAN

UniProt

P49589 - SYCC_HUMAN

Protein

Cysteine--tRNA ligase, cytoplasmic

Gene

CARS

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 138 (01 Oct 2014)
      Sequence version 3 (31 Jan 2002)
      Previous versions | rss
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    Functioni

    Catalytic activityi

    ATP + L-cysteine + tRNA(Cys) = AMP + diphosphate + L-cysteinyl-tRNA(Cys).

    Cofactori

    Binds 1 zinc ion per subunit.By similarity

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Metal bindingi55 – 551ZincBy similarity
    Metal bindingi348 – 3481ZincBy similarity
    Metal bindingi373 – 3731ZincBy similarity
    Metal bindingi377 – 3771ZincBy similarity
    Binding sitei409 – 4091ATPBy similarity

    GO - Molecular functioni

    1. ATP binding Source: UniProtKB
    2. cysteine-tRNA ligase activity Source: UniProtKB
    3. metal ion binding Source: UniProtKB-KW
    4. protein binding Source: UniProtKB
    5. protein homodimerization activity Source: UniProtKB
    6. tRNA binding Source: UniProtKB

    GO - Biological processi

    1. cysteinyl-tRNA aminoacylation Source: UniProtKB
    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, Metal-binding, Nucleotide-binding, Zinc

    Enzyme and pathway databases

    ReactomeiREACT_15306. Cytosolic tRNA aminoacylation.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Cysteine--tRNA ligase, cytoplasmic (EC:6.1.1.16)
    Alternative name(s):
    Cysteinyl-tRNA synthetase
    Short name:
    CysRS
    Gene namesi
    Name:CARS
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 11

    Organism-specific databases

    HGNCiHGNC:1493. CARS.

    Subcellular locationi

    GO - Cellular componenti

    1. cytoplasm Source: UniProtKB
    2. cytosol Source: RefGenome

    Keywords - Cellular componenti

    Cytoplasm

    Pathology & Biotechi

    Involvement in diseasei

    A chromosomal aberration involving CARS is associated with inflammatory myofibroblastic tumors (IMTs). Translocation t(2;11)(p23;p15) with ALK.

    Keywords - Diseasei

    Proto-oncogene

    Organism-specific databases

    Orphaneti178342. Inflammatory myofibroblastic tumor.
    PharmGKBiPA26079.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed1 Publication
    Chaini2 – 748747Cysteine--tRNA ligase, cytoplasmicPRO_0000159550Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei2 – 21N-acetylalanine1 Publication
    Modified residuei503 – 5031N6-acetyllysine1 Publication
    Modified residuei746 – 7461Phosphoserine2 Publications

    Keywords - PTMi

    Acetylation, Phosphoprotein

    Proteomic databases

    MaxQBiP49589.
    PaxDbiP49589.
    PRIDEiP49589.

    PTM databases

    PhosphoSiteiP49589.

    Expressioni

    Gene expression databases

    ArrayExpressiP49589.
    BgeeiP49589.
    CleanExiHS_CARS.
    GenevestigatoriP49589.

    Organism-specific databases

    HPAiHPA002383.
    HPA002384.

    Interactioni

    Subunit structurei

    Monomer.By similarity

    Protein-protein interaction databases

    BioGridi107283. 32 interactions.
    IntActiP49589. 4 interactions.
    STRINGi9606.ENSP00000369897.

    Structurei

    3D structure databases

    ProteinModelPortaliP49589.
    SMRiP49589. Positions 18-134, 214-496.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi57 – 6711"HIGH" regionAdd
    BLAST
    Motifi406 – 4105"KMSKS" region

    Sequence similaritiesi

    Phylogenomic databases

    eggNOGiCOG0215.
    HOGENOMiHOG000245252.
    HOVERGENiHBG002089.
    KOiK01883.
    OMAiEMFLSES.
    PhylomeDBiP49589.
    TreeFamiTF300384.

    Family and domain databases

    Gene3Di3.40.50.620. 2 hits.
    HAMAPiMF_00041. Cys_tRNA_synth.
    InterProiIPR015803. Cys-tRNA-ligase.
    IPR024909. Cys-tRNA/MSH_ligase.
    IPR014729. Rossmann-like_a/b/a_fold.
    IPR009080. tRNAsynth_1a_anticodon-bd.
    [Graphical view]
    PANTHERiPTHR10890. PTHR10890. 1 hit.
    PfamiPF01406. tRNA-synt_1e. 1 hit.
    [Graphical view]
    PRINTSiPR00983. TRNASYNTHCYS.
    SUPFAMiSSF47323. SSF47323. 1 hit.
    TIGRFAMsiTIGR00435. cysS. 1 hit.

    Sequences (3)i

    Sequence statusi: Complete.

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

    This entry describes 3 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: P49589-1) [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

    MADSSGQQGK GRRVQPQWSP PAGTQPCRLH LYNSLTRNKE VFIPQDGKKV    50
    TWYCCGPTVY DASHMGHARS YISFDILRRV LKDYFKFDVF YCMNITDIDD 100
    KIIKRARQNH LFEQYREKRP EAAQLLEDVQ AALKPFSVKL NETTDPDKKQ 150
    MLERIQHAVQ LATEPLEKAV QSRLTGEEVN SCVEVLLEEA KDLLSDWLDS 200
    TLGCDVTDNS IFSKLPKFWE GDFHRDMEAL NVLPPDVLTR VSEYVPEIVN 250
    FVQKIVDNGY GYVSNGSVYF DTAKFASSEK HSYGKLVPEA VGDQKALQEG 300
    EGDLSISADR LSEKRSPNDF ALWKASKPGE PSWPCPWGKG RPGWHIECSA 350
    MAGTLLGASM DIHGGGFDLR FPHHDNELAQ SEAYFENDCW VRYFLHTGHL 400
    TIAGCKMSKS LKNFITIKDA LKKHSARQLR LAFLMHSWKD TLDYSSNTME 450
    SALQYEKFLN EFFLNVKDIL RAPVDITGQF EKWGEEEAEL NKNFYDKKTA 500
    IHKALCDNVD TRTVMEEMRA LVSQCNLYMA ARKAVRKRPN QALLENIALY 550
    LTHMLKIFGA VEEDSSLGFP VGGPGTSLSL EATVMPYLQV LSEFREGVRK 600
    IAREQKVPEI LQLSDALRDN ILPELGVRFE DHEGLPTVVK LVDRNTLLKE 650
    REEKRRVEEE KRKKKEEAAR RKQEQEAAKL AKMKIPPSEM FLSETDKYSK 700
    FDENGLPTHD MEGKELSKGQ AKKLKKLFEA QEKLYKEYLQ MAQNGSFQ 748
    Length:748
    Mass (Da):85,473
    Last modified:January 31, 2002 - v3
    Checksum:iD0B7A29EC03AA87F
    GO
    Isoform 2 (identifier: P49589-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         705-748: GLPTHDMEGKELSKGQAKKLKKLFEAQEKLYKEYLQMAQNGSFQ → VSMVCPHMTWRAKSSAKGKPRS

    Note: Found in 20% of the mRNAs.

    Show »
    Length:726
    Mass (Da):82,846
    Checksum:i92C51DF9289FE47D
    GO
    Isoform 3 (identifier: P49589-3) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         9-9: G → APDYRSILSI...KGQPCRLQAS

    Note: Contains a phosphoserine at position 79.

    Show »
    Length:831
    Mass (Da):94,638
    Checksum:iC0080CD332F79B8F
    GO

    Sequence cautioni

    The sequence AAA73901.1 differs from that shown. Reason: Frameshift at position 619.

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei9 – 91G → APDYRSILSISDEAARAQAL NEHLSTRSYVQGYSLSQADV DAFRQLSAPPADPQLFHVAR WFRHIEALLGSPCGKGQPCR LQAS in isoform 3. 2 PublicationsVSP_043571
    Alternative sequencei705 – 74844GLPTH…NGSFQ → VSMVCPHMTWRAKSSAKGKP RS in isoform 2. 2 PublicationsVSP_006312Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    L06845 mRNA. Translation: AAA73901.1. Frameshift.
    AF288206 mRNA. Translation: AAG00578.1.
    AF288207 mRNA. Translation: AAG00579.1.
    BT009913 mRNA. Translation: AAP88915.1.
    AK302644 mRNA. Translation: BAG63885.1.
    BX647906 mRNA. Translation: CAI46108.1.
    AC108448 Genomic DNA. No translation available.
    AC131971 Genomic DNA. No translation available.
    CH471158 Genomic DNA. Translation: EAX02541.1.
    BC002880 mRNA. Translation: AAH02880.1.
    CCDSiCCDS41600.1. [P49589-3]
    CCDS41602.1. [P49589-2]
    CCDS7742.1. [P49589-1]
    RefSeqiNP_001014437.1. NM_001014437.2. [P49589-3]
    NP_001742.1. NM_001751.5. [P49589-1]
    NP_644802.1. NM_139273.3. [P49589-2]
    UniGeneiHs.274873.

    Genome annotation databases

    EnsembliENST00000278224; ENSP00000278224; ENSG00000110619. [P49589-2]
    ENST00000380525; ENSP00000369897; ENSG00000110619. [P49589-3]
    ENST00000397111; ENSP00000380300; ENSG00000110619. [P49589-1]
    GeneIDi833.
    KEGGihsa:833.
    UCSCiuc001lxf.3. human. [P49589-3]
    uc001lxg.3. human. [P49589-2]
    uc001lxh.3. human. [P49589-1]

    Polymorphism databases

    DMDMi20141641.

    Keywords - Coding sequence diversityi

    Alternative splicing, Chromosomal rearrangement

    Cross-referencesi

    Web resourcesi

    Atlas of Genetics and Cytogenetics in Oncology and Haematology

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    L06845 mRNA. Translation: AAA73901.1 . Frameshift.
    AF288206 mRNA. Translation: AAG00578.1 .
    AF288207 mRNA. Translation: AAG00579.1 .
    BT009913 mRNA. Translation: AAP88915.1 .
    AK302644 mRNA. Translation: BAG63885.1 .
    BX647906 mRNA. Translation: CAI46108.1 .
    AC108448 Genomic DNA. No translation available.
    AC131971 Genomic DNA. No translation available.
    CH471158 Genomic DNA. Translation: EAX02541.1 .
    BC002880 mRNA. Translation: AAH02880.1 .
    CCDSi CCDS41600.1. [P49589-3 ]
    CCDS41602.1. [P49589-2 ]
    CCDS7742.1. [P49589-1 ]
    RefSeqi NP_001014437.1. NM_001014437.2. [P49589-3 ]
    NP_001742.1. NM_001751.5. [P49589-1 ]
    NP_644802.1. NM_139273.3. [P49589-2 ]
    UniGenei Hs.274873.

    3D structure databases

    ProteinModelPortali P49589.
    SMRi P49589. Positions 18-134, 214-496.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 107283. 32 interactions.
    IntActi P49589. 4 interactions.
    STRINGi 9606.ENSP00000369897.

    Chemistry

    DrugBanki DB00151. L-Cysteine.

    PTM databases

    PhosphoSitei P49589.

    Polymorphism databases

    DMDMi 20141641.

    Proteomic databases

    MaxQBi P49589.
    PaxDbi P49589.
    PRIDEi P49589.

    Protocols and materials databases

    DNASUi 833.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000278224 ; ENSP00000278224 ; ENSG00000110619 . [P49589-2 ]
    ENST00000380525 ; ENSP00000369897 ; ENSG00000110619 . [P49589-3 ]
    ENST00000397111 ; ENSP00000380300 ; ENSG00000110619 . [P49589-1 ]
    GeneIDi 833.
    KEGGi hsa:833.
    UCSCi uc001lxf.3. human. [P49589-3 ]
    uc001lxg.3. human. [P49589-2 ]
    uc001lxh.3. human. [P49589-1 ]

    Organism-specific databases

    CTDi 833.
    GeneCardsi GC11M003022.
    H-InvDB HIX0128660.
    HGNCi HGNC:1493. CARS.
    HPAi HPA002383.
    HPA002384.
    MIMi 123859. gene.
    neXtProti NX_P49589.
    Orphaneti 178342. Inflammatory myofibroblastic tumor.
    PharmGKBi PA26079.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG0215.
    HOGENOMi HOG000245252.
    HOVERGENi HBG002089.
    KOi K01883.
    OMAi EMFLSES.
    PhylomeDBi P49589.
    TreeFami TF300384.

    Enzyme and pathway databases

    Reactomei REACT_15306. Cytosolic tRNA aminoacylation.

    Miscellaneous databases

    ChiTaRSi CARS. human.
    GenomeRNAii 833.
    NextBioi 3450.
    PROi P49589.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P49589.
    Bgeei P49589.
    CleanExi HS_CARS.
    Genevestigatori P49589.

    Family and domain databases

    Gene3Di 3.40.50.620. 2 hits.
    HAMAPi MF_00041. Cys_tRNA_synth.
    InterProi IPR015803. Cys-tRNA-ligase.
    IPR024909. Cys-tRNA/MSH_ligase.
    IPR014729. Rossmann-like_a/b/a_fold.
    IPR009080. tRNAsynth_1a_anticodon-bd.
    [Graphical view ]
    PANTHERi PTHR10890. PTHR10890. 1 hit.
    Pfami PF01406. tRNA-synt_1e. 1 hit.
    [Graphical view ]
    PRINTSi PR00983. TRNASYNTHCYS.
    SUPFAMi SSF47323. SSF47323. 1 hit.
    TIGRFAMsi TIGR00435. cysS. 1 hit.
    ProtoNeti Search...

    Publicationsi

    1. "Nucleotide and deduced amino acid sequence of human cysteinyl-tRNA synthetase."
      Cruzen M.E., Arfin S.M.
      DNA Seq. 4:243-248(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
      Tissue: Brain.
    2. "Isolation of two cDNAs encoding functional human cytoplasmic cysteinyl-tRNA synthetase."
      Davidson E., Caffarella J., Vitseva O., Hou Y.M., King M.P.
      Biol. Chem. 382:399-406(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2).
    3. "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 (AUG-2003) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    4. "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 3).
      Tissue: Testis.
    5. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
      Tissue: Cervix.
    6. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    7. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    8. "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: Lung.
    9. "Identification of novel fusion partners of ALK, the anaplastic lymphoma kinase, in anaplastic large-cell lymphoma and inflammatory myofibroblastic tumor."
      Cools J., Wlodarska I., Somers R., Mentens N., Pedeutour F., Maes B., De Wolf-Peeters C., Pauwels P., Hagemeijer A., Marynen P.
      Genes Chromosomes Cancer 34:354-362(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: CHROMOSOMAL TRANSLOCATION WITH ALK.
    10. "Immunoaffinity profiling of tyrosine phosphorylation in cancer cells."
      Rush J., Moritz A., Lee K.A., Guo A., Goss V.L., Spek E.J., Zhang H., Zha X.-M., Polakiewicz R.D., Comb M.J.
      Nat. Biotechnol. 23:94-101(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    11. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-746, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    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-503, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    13. "Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
      Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
      Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-746, PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-79 (ISOFORM 3), IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    14. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [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 nameiSYCC_HUMAN
    AccessioniPrimary (citable) accession number: P49589
    Secondary accession number(s): Q53XI8
    , Q5HYE4, Q9HD24, Q9HD25
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: February 1, 1996
    Last sequence update: January 31, 2002
    Last modified: October 1, 2014
    This is version 138 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

    Complete proteome, Reference proteome

    Documents

    1. Aminoacyl-tRNA synthetases
      List of aminoacyl-tRNA synthetase entries
    2. Human chromosome 11
      Human chromosome 11: entries, gene names and cross-references to MIM
    3. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    4. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3