A0A6Q8PF33 · A0A6Q8PF33_HUMAN

  • Protein
    Alanine--tRNA ligase
  • Gene
    AARS1
  • Status
    UniProtKB unreviewed (TrEMBL)
  • Amino acids
  • Protein existence
    Evidence at protein level
  • Annotation score
    3/5

Function

function

Catalyzes the attachment of alanine to tRNA(Ala) in a two-step reaction: alanine is first activated by ATP to form Ala-AMP and then transferred to the acceptor end of tRNA(Ala). Also edits incorrectly charged tRNA(Ala) via its editing domain.

Catalytic activity

Cofactor

Zn2+ (UniProtKB | Rhea| CHEBI:29105 )

Note: Binds 1 zinc ion per subunit.

Features

Showing features for binding site.

1961100200300400500600700800900
TypeIDPosition(s)Description
Binding site598Zn2+ (UniProtKB | ChEBI)
Binding site602Zn2+ (UniProtKB | ChEBI)
Binding site716Zn2+ (UniProtKB | ChEBI)
Binding site720Zn2+ (UniProtKB | ChEBI)

GO annotations

AspectTerm
Cellular Componentcytosol
Molecular Functionalanine-tRNA ligase activity
Molecular FunctionATP binding
Molecular FunctiontRNA binding
Molecular Functionzinc ion binding
Biological Processalanyl-tRNA aminoacylation

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    Alanine--tRNA ligase
  • EC number
  • Alternative names
    • Protein lactyltransferase AARS1

Gene names

    • Name
      AARS1
    • Synonyms
      AARS

Organism names

  • Taxonomic identifier
  • Organism
  • Taxonomic lineage
    Eukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Primates > Haplorrhini > Catarrhini > Hominidae > Homo

Accessions

  • Primary accession
    A0A6Q8PF33

Proteomes

Organism-specific databases

Subcellular Location

Keywords

  • Cellular component

Disease & Variants

Variants

We now provide the "Disease & Variants" viewer in its own tab.

The viewer provides 1,148 variants from UniProt as well as other sources including ClinVar and dbSNP.

Go to variant viewer

Genetic variation databases

PTM/Processing

Features

Showing features for modified residue, modified residue (large scale data).

Type
IDPosition(s)Source
Description
Modified residue1UniProtN-acetylmethionine
Modified residue (large scale data)399PRIDEPhosphoserine
Modified residue (large scale data)403PRIDEPhosphoserine
Modified residue (large scale data)484PRIDEPhosphoserine
Modified residue (large scale data)660PRIDEPhosphotyrosine

Post-translational modification

ISGylated.

Keywords

Proteomic databases

Expression

Gene expression databases

Interaction

Subunit

Monomer. Interacts with ANKRD16; the interaction is direct.

Family & Domains

Features

Showing features for domain.

TypeIDPosition(s)Description
Domain5-759Alanyl-transfer RNA synthetases family profile

Domain

Consists of three domains; the N-terminal catalytic domain, the editing domain and the C-terminal C-Ala domain. The editing domain removes incorrectly charged amino acids, while the C-Ala domain, along with tRNA(Ala), serves as a bridge to cooperatively bring together the editing and aminoacylation centers thus stimulating deacylation of misacylated tRNAs.

Sequence similarities

Belongs to the class-II aminoacyl-tRNA synthetase family. Alax-L subfamily.

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    961
  • Mass (Da)
    106,063
  • Last updated
    2020-12-02 v1
  • Checksum
    C74957FC42BCF19F
MDSTLTASEIRQRFIDFFKRNEHTYVHSSATIPLDDPTLLFANAGMNQFKPIFLNTIDPSHPMAKLSRAANTQKCIRAGGKHNDLDDVGKDVYHHTFFEMLGSWSFGDYFKELACKMALELLTQEFGIPIERLYVTYFGGDEAAGLEADLECKQIWQNLGLDDTKILPGNMKDNFWEMGDTGPCGPCSEIHYDRIGGRDAAHLVNQDDPNVLEIWNLVFIQYNREADGILKPLPKKSIDTGMGLERLVSVLQNKMSNYDTDLFVPYFEAIQKGTGARPYTGKVGAEDADGIDMAYRVLADHARTITVALADGGRPDNTGRGYVLRRILRRAVRYAHEKLNASRGFFATLVDVVVQSLGDAFPELKKDPDMVKDIINEEEVQFLKTLSRGRRILDRKIQSLGDSKTIPGDTAWLLYDTYGFPVDLTGLIAEEKGLVVDMDGFEEERKLAQLKSQGKGAGGEDLIMLDIYAIEELRARGLEVTDDSPKYNYHLDSSGSYVFENTVATVMALRREKMFVEEVSTGQECGVVLDKTCFYAEQGGQIYDEGYLVKKTEFTVKNAQVRGGYVLHIGTIYGDLKVGDQVWLFIDEPRRRPIMSNHTATHILNFALRSVLGEADQKGSLVAPDRLRFDFTAKGAMSTQQIKKAEEIANEMIEAAKAVYTQDCPLAAAKAIQGLRAVFDETYPDPVRVVSIGVPVSELLDDPSGPAGSLTSVEFCGGTHLRNSSHAGAFVIVTEEAIAKGIRRIVAVTGAEAQKALRKAESLKKCLSVMEAKVKAQTAPNKDVQREIADLGEALATAVIPQWQKDELRETLKSLKKVMDDLDRASKADVQKRVLEKTKQFIDSNPNQPLVILEMESGASAKALNEALKLFKMHSPQTSAMLFTVDNEAGKITCLCQVPQNAANRGLKASEWVQQVSGLMDGKGGGKDVSAQATGKNVGCLQEALQLATSFAQLRLGDVKN

Computationally mapped potential isoform sequences

There are 17 potential isoforms mapped to this entry

View all
EntryEntry nameGene nameLength
P49588SYAC_HUMANAARS1968
A0A6Q8PFK3A0A6Q8PFK3_HUMANAARS1772
A0A6Q8PFY2A0A6Q8PFY2_HUMANAARS1977
A0A6Q8PG28A0A6Q8PG28_HUMANAARS1327
A0A6Q8PG62A0A6Q8PG62_HUMANAARS1278
A0A6Q8PGN5A0A6Q8PGN5_HUMANAARS1984
A0A6Q8PGE8A0A6Q8PGE8_HUMANAARS1959
A0A6Q8PGI8A0A6Q8PGI8_HUMANAARS1275
A0A6Q8PGB5A0A6Q8PGB5_HUMANAARS1925
A0A6Q8PGR9A0A6Q8PGR9_HUMANAARS1940
A0A6Q8PH44A0A6Q8PH44_HUMANAARS1734
A0A6Q8PF77A0A6Q8PF77_HUMANAARS1521
A0A6Q8PHN5A0A6Q8PHN5_HUMANAARS148
A0A6Q8PHP3A0A6Q8PHP3_HUMANAARS1535
A0A6Q8PHP7A0A6Q8PHP7_HUMANAARS1560
A0A6Q8PHJ2A0A6Q8PHJ2_HUMANAARS1789
H3BPK7H3BPK7_HUMANAARS1999

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
AC009060
EMBL· GenBank· DDBJ
-Genomic DNA No translation available.
AC012184
EMBL· GenBank· DDBJ
-Genomic DNA No translation available.
AC093491
EMBL· GenBank· DDBJ
-Genomic DNA No translation available.

Genome annotation databases

Similar Proteins

Disclaimer

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