Details for: AARS1

Gene ID: 16

Symbol: AARS1

Ensembl ID: ENSG00000090861

Description: alanyl-tRNA synthetase 1

Associated with

Other Information

Genular Protein ID: 145001487

Symbol: SYAC_HUMAN

Name: Renal carcinoma antigen NY-REN-42

UniProtKB Accession Codes:

Database IDs:

Citations:

PubMed ID: 7654687

Title: Human alanyl-tRNA synthetase: conservation in evolution of catalytic core and microhelix recognition.

PubMed ID: 7654687

DOI: 10.1021/bi00033a004

PubMed ID: 14702039

Title: Complete sequencing and characterization of 21,243 full-length human cDNAs.

PubMed ID: 14702039

DOI: 10.1038/ng1285

PubMed ID: 15616553

Title: The sequence and analysis of duplication-rich human chromosome 16.

PubMed ID: 15616553

DOI: 10.1038/nature03187

PubMed ID: 15489334

Title: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).

PubMed ID: 15489334

DOI: 10.1101/gr.2596504

PubMed ID: 10508479

Title: Antigens recognized by autologous antibody in patients with renal-cell carcinoma.

PubMed ID: 10508479

DOI: 10.1002/(sici)1097-0215(19991112)83:4<456::aid-ijc4>3.0.co;2-5

PubMed ID: 16139798

Title: Proteomic identification of proteins conjugated to ISG15 in mouse and human cells.

PubMed ID: 16139798

DOI: 10.1016/j.bbrc.2005.08.132

PubMed ID: 18669648

Title: A quantitative atlas of mitotic phosphorylation.

PubMed ID: 18669648

DOI: 10.1073/pnas.0805139105

PubMed ID: 19413330

Title: Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach.

PubMed ID: 19413330

DOI: 10.1021/ac9004309

PubMed ID: 19661429

Title: The C-Ala domain brings together editing and aminoacylation functions on one tRNA.

PubMed ID: 19661429

DOI: 10.1126/science.1174343

PubMed ID: 19608861

Title: Lysine acetylation targets protein complexes and co-regulates major cellular functions.

PubMed ID: 19608861

DOI: 10.1126/science.1175371

PubMed ID: 20068231

Title: Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis.

PubMed ID: 20068231

DOI: 10.1126/scisignal.2000475

PubMed ID: 21269460

Title: Initial characterization of the human central proteome.

PubMed ID: 21269460

DOI: 10.1186/1752-0509-5-17

PubMed ID: 22223895

Title: Comparative large-scale characterisation of plant vs. mammal proteins reveals similar and idiosyncratic N-alpha acetylation features.

PubMed ID: 22223895

DOI: 10.1074/mcp.m111.015131

PubMed ID: 22814378

Title: N-terminal acetylome analyses and functional insights of the N-terminal acetyltransferase NatB.

PubMed ID: 22814378

DOI: 10.1073/pnas.1210303109

PubMed ID: 23186163

Title: Toward a comprehensive characterization of a human cancer cell phosphoproteome.

PubMed ID: 23186163

DOI: 10.1021/pr300630k

PubMed ID: 24275569

Title: An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome.

PubMed ID: 24275569

DOI: 10.1016/j.jprot.2013.11.014

PubMed ID: 25817015

Title: Loss-of-function alanyl-tRNA synthetase mutations cause an autosomal-recessive early-onset epileptic encephalopathy with persistent myelination defect.

PubMed ID: 25817015

DOI: 10.1016/j.ajhg.2015.02.012

PubMed ID: 25944712

Title: N-terminome analysis of the human mitochondrial proteome.

PubMed ID: 25944712

DOI: 10.1002/pmic.201400617

PubMed ID: 31775912

Title: An AARS variant as the likely cause of Swedish type hereditary diffuse leukoencephalopathy with spheroids.

PubMed ID: 31775912

DOI: 10.1186/s40478-019-0843-y

PubMed ID: 33909043

Title: Protein instability associated with AARS1 and MARS1 mutations causes trichothiodystrophy.

PubMed ID: 33909043

DOI: 10.1093/hmg/ddab123

PubMed ID: 27622773

Title: Evolutionary Gain of Alanine Mischarging to Noncognate tRNAs with a G4:U69 Base Pair.

PubMed ID: 27622773

DOI: 10.1021/jacs.6b07121

PubMed ID: 27911835

Title: Two crystal structures reveal design for repurposing the C-Ala domain of human AlaRS.

PubMed ID: 27911835

DOI: 10.1073/pnas.1617316113

PubMed ID: 32611769

Title: Methyltransferase-like 21C (METTL21C) methylates alanine tRNA synthetase at Lys-943 in muscle tissue.

PubMed ID: 32611769

DOI: 10.1074/jbc.ra120.014505

PubMed ID: 20045102

Title: A major determinant for binding and aminoacylation of tRNA(Ala) in cytoplasmic Alanyl-tRNA synthetase is mutated in dominant axonal Charcot-Marie-Tooth disease.

PubMed ID: 20045102

DOI: 10.1016/j.ajhg.2009.12.005

PubMed ID: 22206013

Title: The mutational spectrum in a cohort of Charcot-Marie-Tooth disease type 2 among the Han Chinese in Taiwan.

PubMed ID: 22206013

DOI: 10.1371/journal.pone.0029393

PubMed ID: 22009580

Title: A recurrent loss-of-function alanyl-tRNA synthetase (AARS) mutation in patients with Charcot-Marie-Tooth disease type 2N (CMT2N).

PubMed ID: 22009580

DOI: 10.1002/humu.21635

PubMed ID: 24627108

Title: Whole-exome sequencing in patients with inherited neuropathies: outcome and challenges.

PubMed ID: 24627108

DOI: 10.1007/s00415-014-7289-8

PubMed ID: 28493438

Title: Deficient activity of alanyl-tRNA synthetase underlies an autosomal recessive syndrome of progressive microcephaly, hypomyelination, and epileptic encephalopathy.

PubMed ID: 28493438

DOI: 10.1002/humu.23250

Sequence Information:

  • Length: 968
  • Mass: 106810
  • Checksum: 8683F111CEE42506
  • Sequence:
  • MDSTLTASEI RQRFIDFFKR NEHTYVHSSA TIPLDDPTLL FANAGMNQFK PIFLNTIDPS 
    HPMAKLSRAA NTQKCIRAGG KHNDLDDVGK DVYHHTFFEM LGSWSFGDYF KELACKMALE 
    LLTQEFGIPI ERLYVTYFGG DEAAGLEADL ECKQIWQNLG LDDTKILPGN MKDNFWEMGD 
    TGPCGPCSEI HYDRIGGRDA AHLVNQDDPN VLEIWNLVFI QYNREADGIL KPLPKKSIDT 
    GMGLERLVSV LQNKMSNYDT DLFVPYFEAI QKGTGARPYT GKVGAEDADG IDMAYRVLAD 
    HARTITVALA DGGRPDNTGR GYVLRRILRR AVRYAHEKLN ASRGFFATLV DVVVQSLGDA 
    FPELKKDPDM VKDIINEEEV QFLKTLSRGR RILDRKIQSL GDSKTIPGDT AWLLYDTYGF 
    PVDLTGLIAE EKGLVVDMDG FEEERKLAQL KSQGKGAGGE DLIMLDIYAI EELRARGLEV 
    TDDSPKYNYH LDSSGSYVFE NTVATVMALR REKMFVEEVS TGQECGVVLD KTCFYAEQGG 
    QIYDEGYLVK VDDSSEDKTE FTVKNAQVRG GYVLHIGTIY GDLKVGDQVW LFIDEPRRRP 
    IMSNHTATHI LNFALRSVLG EADQKGSLVA PDRLRFDFTA KGAMSTQQIK KAEEIANEMI 
    EAAKAVYTQD CPLAAAKAIQ GLRAVFDETY PDPVRVVSIG VPVSELLDDP SGPAGSLTSV 
    EFCGGTHLRN SSHAGAFVIV TEEAIAKGIR RIVAVTGAEA QKALRKAESL KKCLSVMEAK 
    VKAQTAPNKD VQREIADLGE ALATAVIPQW QKDELRETLK SLKKVMDDLD RASKADVQKR 
    VLEKTKQFID SNPNQPLVIL EMESGASAKA LNEALKLFKM HSPQTSAMLF TVDNEAGKIT 
    CLCQVPQNAA NRGLKASEWV QQVSGLMDGK GGGKDVSAQA TGKNVGCLQE ALQLATSFAQ 
    LRLGDVKN

Database document:

This is a preview of the gene's schema. Only a few entries are kept for 'singleCellExpressions,' 'mRNAExpressions,' and other large data arrays for visualization purposes. You can zoom in with the mouse wheel for a closer view, and the text will adjust automatically if necessary. For the full schema, download it here.