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P49591

- SYSC_HUMAN

UniProt

P49591 - SYSC_HUMAN

Protein

Serine--tRNA ligase, cytoplasmic

Gene

SARS

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 135 (01 Oct 2014)
      Sequence version 3 (23 Jan 2007)
      Previous versions | rss
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    Functioni

    Catalyzes the attachment of serine to tRNA(Ser). Is also probably able to aminoacylate tRNA(Sec) with serine, to form the misacylated tRNA L-seryl-tRNA(Sec), which will be further converted into selenocysteinyl-tRNA(Sec).1 Publication

    Catalytic activityi

    ATP + L-serine + tRNA(Ser) = AMP + diphosphate + L-seryl-tRNA(Ser).
    ATP + L-serine + tRNA(Sec) = AMP + diphosphate + L-seryl-tRNA(Sec).

    Pathwayi

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei318 – 3181ATP; via amide nitrogen and carbonyl oxygenBy similarity
    Binding sitei325 – 3251SerineBy similarity
    Binding sitei429 – 4291SerineBy similarity

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi302 – 3043ATPBy similarity
    Nucleotide bindingi391 – 3944ATPBy similarity

    GO - Molecular functioni

    1. ATP binding Source: UniProtKB-KW
    2. RNA binding Source: ProtInc
    3. serine-tRNA ligase activity Source: Reactome

    GO - Biological processi

    1. gene expression Source: Reactome
    2. selenocysteinyl-tRNA(Sec) biosynthetic process Source: UniProtKB-UniPathway
    3. seryl-tRNA aminoacylation Source: InterPro
    4. translation Source: ProtInc
    5. tRNA aminoacylation for protein translation Source: Reactome
    6. tRNA processing Source: ProtInc

    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.
    UniPathwayiUPA00906; UER00895.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Serine--tRNA ligase, cytoplasmic (EC:6.1.1.11)
    Alternative name(s):
    Seryl-tRNA synthetase
    Short name:
    SerRS
    Seryl-tRNA(Ser/Sec) synthetase
    Gene namesi
    Name:SARS
    Synonyms:SERS
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 1

    Organism-specific databases

    HGNCiHGNC:10537. SARS.

    Subcellular locationi

    GO - Cellular componenti

    1. cytoplasm Source: HPA
    2. cytosol Source: Reactome
    3. extracellular vesicular exosome Source: UniProt
    4. mitochondrion Source: Ensembl

    Keywords - Cellular componenti

    Cytoplasm

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA34945.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 514514Serine--tRNA ligase, cytoplasmicPRO_0000122191Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei1 – 11N-acetylmethionine1 Publication
    Modified residuei241 – 2411Phosphoserine1 Publication
    Modified residuei323 – 3231N6-acetyllysine1 Publication

    Keywords - PTMi

    Acetylation, Phosphoprotein

    Proteomic databases

    MaxQBiP49591.
    PaxDbiP49591.
    PRIDEiP49591.

    PTM databases

    PhosphoSiteiP49591.

    Miscellaneous databases

    PMAP-CutDBP49591.

    Expressioni

    Gene expression databases

    ArrayExpressiP49591.
    BgeeiP49591.
    CleanExiHS_SARS.
    GenevestigatoriP49591.

    Organism-specific databases

    HPAiHPA016939.

    Interactioni

    Subunit structurei

    Homodimer. The tRNA molecule binds across the dimer By similarity.By similarity

    Protein-protein interaction databases

    BioGridi112208. 31 interactions.
    DIPiDIP-38215N.
    IntActiP49591. 4 interactions.
    STRINGi9606.ENSP00000234677.

    Structurei

    Secondary structure

    1
    514
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi5 – 73
    Helixi10 – 123
    Helixi16 – 2510
    Helixi31 – 7040
    Helixi82 – 843
    Beta strandi86 – 894
    Helixi92 – 965
    Beta strandi100 – 1023
    Helixi103 – 11210
    Helixi118 – 13114
    Helixi132 – 1343
    Helixi149 – 1524
    Beta strandi154 – 1607
    Helixi170 – 1767
    Helixi183 – 1897
    Beta strandi195 – 1973
    Helixi199 – 21719
    Beta strandi221 – 2244
    Beta strandi227 – 2304
    Helixi231 – 2377
    Helixi240 – 2456
    Beta strandi249 – 2513
    Beta strandi254 – 2563
    Beta strandi266 – 2683
    Helixi273 – 2775
    Turni278 – 2825
    Beta strandi283 – 2853
    Turni287 – 2893
    Beta strandi292 – 30110
    Beta strandi308 – 3114
    Beta strandi315 – 3173
    Beta strandi319 – 33012
    Helixi336 – 35419
    Beta strandi359 – 3635
    Helixi366 – 3683
    Beta strandi374 – 38310
    Turni384 – 3874
    Beta strandi388 – 39710
    Helixi401 – 4066
    Beta strandi409 – 4113
    Beta strandi424 – 4329
    Helixi433 – 44412
    Beta strandi447 – 4515
    Helixi454 – 4574
    Beta strandi464 – 4696

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    3VBBX-ray2.89A/B/C/D/E/F1-514[»]
    4L87X-ray2.90A2-477[»]
    ProteinModelPortaliP49591.
    SMRiP49591. Positions 2-477.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni271 – 2733Serine bindingBy similarity

    Domaini

    Consists of two distinct domains, a catalytic core and a N-terminal extension that is involved in tRNA binding.By similarity

    Sequence similaritiesi

    Phylogenomic databases

    eggNOGiCOG0172.
    HOGENOMiHOG000035937.
    HOVERGENiHBG023172.
    KOiK01875.
    OrthoDBiEOG7Z95KZ.
    PhylomeDBiP49591.
    TreeFamiTF300762.

    Family and domain databases

    Gene3Di1.10.287.40. 1 hit.
    InterProiIPR002314. aa-tRNA-synt_IIb_cons-dom.
    IPR006195. aa-tRNA-synth_II.
    IPR002317. Ser-tRNA-ligase_type_1.
    IPR015866. Ser-tRNA-synth_1_N.
    IPR010978. tRNA-bd_arm.
    [Graphical view]
    PANTHERiPTHR11778. PTHR11778. 1 hit.
    PfamiPF02403. Seryl_tRNA_N. 1 hit.
    PF00587. tRNA-synt_2b. 1 hit.
    [Graphical view]
    PIRSFiPIRSF001529. Ser-tRNA-synth_IIa. 1 hit.
    PRINTSiPR00981. TRNASYNTHSER.
    SUPFAMiSSF46589. SSF46589. 2 hits.
    TIGRFAMsiTIGR00414. serS. 1 hit.
    PROSITEiPS50862. AA_TRNA_LIGASE_II. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    P49591-1 [UniParc]FASTAAdd to Basket

    « Hide

    MVLDLDLFRV DKGGDPALIR ETQEKRFKDP GLVDQLVKAD SEWRRCRFRA    50
    DNLNKLKNLC SKTIGEKMKK KEPVGDDESV PENVLSFDDL TADALANLKV 100
    SQIKKVRLLI DEAILKCDAE RIKLEAERFE NLREIGNLLH PSVPISNDED 150
    VDNKVERIWG DCTVRKKYSH VDLVVMVDGF EGEKGAVVAG SRGYFLKGVL 200
    VFLEQALIQY ALRTLGSRGY IPIYTPFFMR KEVMQEVAQL SQFDEELYKV 250
    IGKGSEKSDD NSYDEKYLIA TSEQPIAALH RDEWLRPEDL PIKYAGLSTC 300
    FRQEVGSHGR DTRGIFRVHQ FEKIEQFVYS SPHDNKSWEM FEEMITTAEE 350
    FYQSLGIPYH IVNIVSGSLN HAASKKLDLE AWFPGSGAFR ELVSCSNCTD 400
    YQARRLRIRY GQTKKMMDKV EFVHMLNATM CATTRTICAI LENYQTEKGI 450
    TVPEKLKEFM PPGLQELIPF VKPAPIEQEP SKKQKKQHEG SKKKAAARDV 500
    TLENRLQNME VTDA 514
    Length:514
    Mass (Da):58,777
    Last modified:January 23, 2007 - v3
    Checksum:iF59DA8E55F193ACB
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti54 – 541N → S in CAA62635. (PubMed:9431993)Curated
    Sequence conflicti435 – 4351R → C in AAH09390. (PubMed:15489334)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X91257 mRNA. Translation: CAA62635.1.
    D49914 mRNA. Translation: BAA95602.1.
    AK312771 mRNA. Translation: BAG35636.1.
    AL356389 Genomic DNA. Translation: CAI13599.1.
    CH471122 Genomic DNA. Translation: EAW56369.1.
    BC000716 mRNA. Translation: AAH00716.1.
    BC009390 mRNA. Translation: AAH09390.1.
    CCDSiCCDS795.1.
    PIRiG01026.
    RefSeqiNP_006504.2. NM_006513.3.
    UniGeneiHs.531176.

    Genome annotation databases

    EnsembliENST00000234677; ENSP00000234677; ENSG00000031698.
    GeneIDi6301.
    KEGGihsa:6301.
    UCSCiuc001dwu.2. human.

    Polymorphism databases

    DMDMi19860217.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X91257 mRNA. Translation: CAA62635.1 .
    D49914 mRNA. Translation: BAA95602.1 .
    AK312771 mRNA. Translation: BAG35636.1 .
    AL356389 Genomic DNA. Translation: CAI13599.1 .
    CH471122 Genomic DNA. Translation: EAW56369.1 .
    BC000716 mRNA. Translation: AAH00716.1 .
    BC009390 mRNA. Translation: AAH09390.1 .
    CCDSi CCDS795.1.
    PIRi G01026.
    RefSeqi NP_006504.2. NM_006513.3.
    UniGenei Hs.531176.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    3VBB X-ray 2.89 A/B/C/D/E/F 1-514 [» ]
    4L87 X-ray 2.90 A 2-477 [» ]
    ProteinModelPortali P49591.
    SMRi P49591. Positions 2-477.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 112208. 31 interactions.
    DIPi DIP-38215N.
    IntActi P49591. 4 interactions.
    STRINGi 9606.ENSP00000234677.

    Chemistry

    DrugBanki DB00133. L-Serine.

    PTM databases

    PhosphoSitei P49591.

    Polymorphism databases

    DMDMi 19860217.

    Proteomic databases

    MaxQBi P49591.
    PaxDbi P49591.
    PRIDEi P49591.

    Protocols and materials databases

    DNASUi 6301.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000234677 ; ENSP00000234677 ; ENSG00000031698 .
    GeneIDi 6301.
    KEGGi hsa:6301.
    UCSCi uc001dwu.2. human.

    Organism-specific databases

    CTDi 6301.
    GeneCardsi GC01P109756.
    HGNCi HGNC:10537. SARS.
    HPAi HPA016939.
    MIMi 607529. gene.
    neXtProti NX_P49591.
    PharmGKBi PA34945.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG0172.
    HOGENOMi HOG000035937.
    HOVERGENi HBG023172.
    KOi K01875.
    OrthoDBi EOG7Z95KZ.
    PhylomeDBi P49591.
    TreeFami TF300762.

    Enzyme and pathway databases

    UniPathwayi UPA00906 ; UER00895 .
    Reactomei REACT_15306. Cytosolic tRNA aminoacylation.

    Miscellaneous databases

    ChiTaRSi SARS. human.
    GeneWikii SARS_(gene).
    GenomeRNAii 6301.
    NextBioi 24463.
    PMAP-CutDB P49591.
    PROi P49591.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P49591.
    Bgeei P49591.
    CleanExi HS_SARS.
    Genevestigatori P49591.

    Family and domain databases

    Gene3Di 1.10.287.40. 1 hit.
    InterProi IPR002314. aa-tRNA-synt_IIb_cons-dom.
    IPR006195. aa-tRNA-synth_II.
    IPR002317. Ser-tRNA-ligase_type_1.
    IPR015866. Ser-tRNA-synth_1_N.
    IPR010978. tRNA-bd_arm.
    [Graphical view ]
    PANTHERi PTHR11778. PTHR11778. 1 hit.
    Pfami PF02403. Seryl_tRNA_N. 1 hit.
    PF00587. tRNA-synt_2b. 1 hit.
    [Graphical view ]
    PIRSFi PIRSF001529. Ser-tRNA-synth_IIa. 1 hit.
    PRINTSi PR00981. TRNASYNTHSER.
    SUPFAMi SSF46589. SSF46589. 2 hits.
    TIGRFAMsi TIGR00414. serS. 1 hit.
    PROSITEi PS50862. AA_TRNA_LIGASE_II. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Genomic organization, cDNA sequence, bacterial expression, and purification of human seryl-tRNA synthase."
      Vincent C., Tarbouriech N., Haertlein M.
      Eur. J. Biochem. 250:77-84(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION.
      Tissue: Brain.
    2. "Isolation and characterization of human seryl-tRNA synthetase cDNA."
      Shiba K., Yu R., Motegi H., Martinis S., Noda T.
      Submitted (MAR-1995) to the EMBL/GenBank/DDBJ databases
      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: Testis.
    4. "The DNA sequence and biological annotation of human chromosome 1."
      Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.
      , Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.
      Nature 441:315-321(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    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: Brain and Placenta.
    7. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-241, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Embryonic kidney.
    8. "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].
    9. "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-323, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    10. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    11. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

    Entry informationi

    Entry nameiSYSC_HUMAN
    AccessioniPrimary (citable) accession number: P49591
    Secondary accession number(s): B2R6Y9, Q5T5C8, Q9NSE3
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: February 1, 1996
    Last sequence update: January 23, 2007
    Last modified: October 1, 2014
    This is version 135 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, 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. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    4. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    5. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    6. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3