CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-016408
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Alanine--tRNA ligase, cytoplasmic 
Protein Synonyms/Alias
 Alanyl-tRNA synthetase; AlaRS 
Gene Name
 Aars 
Gene Synonyms/Alias
  
Created Date
 July 27, 2013 
Organism
 Mus musculus (Mouse) 
NCBI Taxa ID
 10090 
Lysine Modification
Position
Peptide
Type
References
74SRAANTQKCIRAGGKubiquitination[1]
384EEEVQFLKTLSRGRRubiquitination[1]
625VLGEADQKGSLVAPDubiquitination[1]
641LRFDFTAKGAMSTQQubiquitination[1]
747VTEEAIAKGIRRIVAubiquitination[1]
820DEQRETLKSLKKVMDubiquitination[1]
846KRVLEKTKQLIDSNPubiquitination[1]
876KALNEALKLFKTHSPacetylation[2]
876KALNEALKLFKTHSPubiquitination[1]
879NEALKLFKTHSPQTSubiquitination[1]
Reference
 [1] Proteomic analyses reveal divergent ubiquitylation site patterns in murine tissues.
 Wagner SA, Beli P, Weinert BT, Schölz C, Kelstrup CD, Young C, Nielsen ML, Olsen JV, Brakebusch C, Choudhary C.
 Mol Cell Proteomics. 2012 Dec;11(12):1578-85. [PMID: 22790023]
 [2] Quantitative acetylome analysis reveals the roles of SIRT1 in regulating diverse substrates and cellular pathways.
 Chen Y, Zhao W, Yang JS, Cheng Z, Luo H, Lu Z, Tan M, Gu W, Zhao Y.
 Mol Cell Proteomics. 2012 Oct;11(10):1048-62. [PMID: 22826441
Functional Description
 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. 
Sequence Annotation
 METAL 605 605 Zinc (Potential).
 METAL 609 609 Zinc (Potential).
 METAL 723 723 Zinc (Potential).
 METAL 727 727 Zinc (Potential).
 MOD_RES 1 1 N-acetylmethionine (By similarity).
 MOD_RES 399 399 Phosphoserine (By similarity).
 MOD_RES 555 555 Phosphoserine (By similarity).
 MOD_RES 876 876 N6-acetyllysine (By similarity).  
Keyword
 Acetylation; Aminoacyl-tRNA synthetase; ATP-binding; Complete proteome; Cytoplasm; Ligase; Metal-binding; Nucleotide-binding; Phosphoprotein; Protein biosynthesis; Reference proteome; RNA-binding; tRNA-binding; Ubl conjugation; Zinc. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 968 AA 
Protein Sequence
MDATLTAREI RERFINFFRR NEHTYVHSSA TIPLDDPTLL FANAGMNQFK PIFLNTIDPS 60
HPMAKLSRAA NTQKCIRAGG KHNDLDDVGK DVYHHTFFEM LGSWSFGDYF KELACKMALE 120
LLTQEFGIPV ERLYVTYFGG DEAAGLEPDL ECRQIWQNLG LDEARILPGN MKDNFWEMGD 180
TGPCGPCSEI HYDRIGGRDA AHLVNQDDPN VLEIWNLVFI QYNRESDGVL KPLPKKSIDT 240
GMGLERLVSV LQNKMSNYDT DLFMPYFEAI QKGTGARPYT GKVGAEDADG IDMAYRVLAD 300
HARTITVALA DGGRPDNTGR GYVLRRILRR AVRYSHEKLN ASRGFFATLV DVVVQSLGDA 360
FPELKKDPEM VKDIINEEEV QFLKTLSRGR RILDRKIQSL GDCKTIPGDT AWLLYDTYGF 420
PVDLTGLIAE EKGLVVDMNG FEEERRLAQL KSQGKGAGDE DLIMLDIYAI EELRAKGLEA 480
TDDSPKYNYQ SDSSGSYVFE CTVATVLALR REKMFVDEVV TGQECGVVLD KTCFYAEQGG 540
QIYDEGYLVK VDDSSEDKTE FTVKNAQVRG GYVLHIGTIY GNLKVGDQVR LFIDEPRRRP 600
VMSNHTATHI LNFALRSVLG EADQKGSLVA PDRLRFDFTA KGAMSTQQIK KAEEIVNGMI 660
EAAKPVYTQD CPLAAAKAIQ GLRAVFDETY PDPVRVVSIG VPVSELLDDP CGPAGSLTSV 720
EFCGGTHLRN SSHAGAFVIV TEEAIAKGIR RIVAVTGAEA QKALRKSETL KKSLSAMEAK 780
VKAQTAPNKD VQREIADLGE ALATAVIPQW QKDEQRETLK SLKKVMDDLD RASKADVQKR 840
VLEKTKQLID SNPNQPLVIL EMESGASAKA LNEALKLFKT HSPQTSAMLF TVDNEAGKIT 900
CLCQVPQNAA NRGLKASEWV QQVSGLMDGK GGGKDMSAQA TGKNVGCLQE ALQLATSFAQ 960
LRLGDVKN 968 
Gene Ontology
 GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
 GO:0004813; F:alanine-tRNA ligase activity; IEA:EC.
 GO:0016597; F:amino acid binding; IEA:Compara.
 GO:0002161; F:aminoacyl-tRNA editing activity; IDA:UniProtKB.
 GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
 GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
 GO:0000049; F:tRNA binding; IEA:UniProtKB-KW.
 GO:0006419; P:alanyl-tRNA aminoacylation; IMP:MGI.
 GO:0021680; P:cerebellar Purkinje cell layer development; IMP:MGI.
 GO:0030968; P:endoplasmic reticulum unfolded protein response; IMP:MGI.
 GO:0001942; P:hair follicle development; IMP:MGI.
 GO:0043524; P:negative regulation of neuron apoptotic process; IMP:MGI.
 GO:0050885; P:neuromuscular process controlling balance; IMP:MGI.
 GO:0006457; P:protein folding; IMP:MGI.
 GO:0043200; P:response to amino acid stimulus; IMP:MGI.
 GO:0043588; P:skin development; IMP:MGI.
 GO:0006400; P:tRNA modification; IMP:MGI. 
Interpro
 IPR002318; Ala-tRNA-lgiase_IIc.
 IPR018162; Ala-tRNA-ligase_IIc_anticod-bd.
 IPR018165; Ala-tRNA-synth_IIc_core.
 IPR018164; Ala-tRNA-synth_IIc_N.
 IPR023033; Ala_tRNA_ligase_euk/bac.
 IPR003156; Pesterase_DHHA1.
 IPR018163; Thr/Ala-tRNA-synth_IIc_edit.
 IPR012947; tRNA_SAD. 
Pfam
 PF02272; DHHA1
 PF01411; tRNA-synt_2c
 PF07973; tRNA_SAD 
SMART
 SM00863; tRNA_SAD 
PROSITE
 PS50860; AA_TRNA_LIGASE_II_ALA 
PRINTS
 PR00980; TRNASYNTHALA.