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Protein Page:
AARS (human)
p Phosphorylation
a Acetylation
m Methylation
m1 Mono-methylation
m2 Di-methylation
m3 Tri-methylation
u Ubiquitination
s Sumoylation
n Neddylation
g O-GlcNAc
h Palmitoylation
ad Adenylylation
sn S-Nitrosylation
ca Caspase cleavage

Overview
AARS 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. Defects in AARS are the cause of Charcot-Marie-Tooth disease type 2N (CMT2N). It is an axonal form of Charcot-Marie-Tooth disease, a disorder of the peripheral nervous system, characterized by progressive weakness and atrophy, initially of the peroneal muscles and later of the distal muscles of the arms. Charcot-Marie-Tooth disease is classified in two main groups on the basis of electrophysiologic properties and histopathology: primary peripheral demyelinating neuropathies(designated CMT1 when they are dominantly inherited) and primary peripheral axonal neuropathies (CMT2). Neuropathies of the CMT2 group are characterized by signs of axonal regeneration in the absence of obvious myelin alterations, normal or slightly reduced nerve conduction velocities, and progressive distal muscle weakness and atrophy. Nerve conduction velocities are normal or slightly reduced. Belongs to the class-II aminoacyl-tRNA synthetase family. Note: This description may include information from UniProtKB.
Protein type: EC 6.1.1.7; Ligase; Translation
Cellular Component: cytoplasm; cytosol
Molecular Function: amino acid binding; metal ion binding; alanine-tRNA ligase activity; ATP binding; tRNA binding
Biological Process: skin development; protein folding; unfolded protein response; tRNA processing; cerebellar Purkinje cell layer development; tRNA modification; response to amino acid stimulus; tRNA aminoacylation for protein translation; hair follicle development; gene expression; negative regulation of neuron apoptosis; neuromuscular process controlling balance; alanyl-tRNA aminoacylation
Reference #:  P49588 (UniProtKB)
Alt. Names/Synonyms: AARS; alanine tRNA ligase 1, cytoplasmic; Alanine--tRNA ligase; alanyl-tRNA synthetase; Alanyl-tRNA synthetase, cytoplasmic; AlaRS; CMT2N; Renal carcinoma antigen NY-REN-42; SYAC
Gene Symbols: AARS
Molecular weight: 106,810 Da
Basal Isoelectric point: 5.34  Predict pI for various phosphorylation states
Select Structure to View Below

AARS

Protein Structure Not Found.


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Modification Sites and Domains Show Modification Legend
Click here to view phosphorylation modifications only

Modification Sites in Parent Protein, Orthologs, and Isoforms Show Modification Legend
 

Show Multiple Sequence Alignment


 SS 

SS: The number of records in which this modification site was determined using site-specific methods. SS methods include amino acid sequencing, site-directed mutagenesis, modification site-specific antibodies, specific MS strategies, etc.


 MS 

MS: The number of records in which this modification site was assigned using ONLY proteomic discovery-mode mass spectrometry.


       human

 
0 2 K19-a QRFIDFFkRNEHTYV
0 1 K19-u QRFIDFFkRNEHTYV
0 1 T72 KLSRAANTQKCIRAG
0 1 K74 SRAANTQKCIRAGGk
0 2 K81-a KCIRAGGkHNDLDDV
0 1 K81-u KCIRAGGkHNDLDDV
0 3 Y192-p GPCSEIHyDRIGGRD
0 10 K231-u READGILkPLPKkSI
0 1 K236-u ILkPLPKkSIDTGMG
0 1 K282-u GARPYTGkVGAEDAD
0 2 K338-u AVRYAHEkLNASRGF
0 1 K366-u DAFPELKkDPDMVkD
0 3 K366-a DAFPELKkDPDMVkD
0 1 K372-u KkDPDMVkDIINEEE
0 11 K384-u EEEVQFLkTLSRGRR
0 2 K396-u GRRILDRkIQsLGDS
0 3 S399-p ILDRkIQsLGDSKTI
0 2 K451-u ERKLAQLkSQGKGAG
0 1 K486-u EVTDDSPkYNYHLDS
0 2 K513-u VMALRREkMFVEEVS
0 3 Y543-p AEQGGQIyDEGYLVK
0 1 S555-p LVKVDDSsEDKTEFT
0 15 K564-u DKTEFTVkNAQVRGG
0 18 K625-u VLGEADQkGsLVAPD
0 1 S627-p GEADQkGsLVAPDRL
0 9 K641-u LRFDFTAkGAMSTQQ
0 3 K650-u AMSTQQIkkAEEIAN
0 1 K651-u MSTQQIkkAEEIANE
0 2 K664-u NEMIEAAkAVyTQDC
0 15 Y667-p IEAAkAVyTQDCPLA
0 16 K677-u DCPLAAAkAIQGLRA
0 1 T689-p LRAVFDEtyPDPVRV
0 5 Y690-p RAVFDEtyPDPVRVV
0 62 K747-u VTEEAIAkGIRRIVA
0 19 K762-u VTGAEAQkALRKAES
0 6 K772-u RKAESLKkCLSVMEA
0 1 K780-u CLSVMEAkVKAQTAP
0 1 K789-u KAQTAPNkDVQREIA
0 2 K812-u AVIPQWQkDELRETL
0 2 K820-u DELRETLkSLKKVMD
0 1 K846 KRVLEKTKQFIDSNP
0 2 K876-a KALNEALkLFKMHSP
0 5 K876-u KALNEALkLFKMHSP
0 1 K879 NEALkLFKMHSPQTS
0 2 K930-a VSGLMDGkGGGkDVs
0 1 K930-u VSGLMDGkGGGkDVs
0 4 K934-u MDGkGGGkDVsAQAt
0 1 S937-p kGGGkDVsAQAtGkN
0 1 T941-p kDVsAQAtGkNVGCL
0 1 K943-u VsAQAtGkNVGCLQE
  mouse

 
R19 ERFINFFRRNEHTYV
R19 ERFINFFRRNEHTYV
T72-p KLSRAANtQkCIRAG
K74-u SRAANtQkCIRAGGK
K81 kCIRAGGKHNDLDDV
K81 kCIRAGGKHNDLDDV
Y192-p GPCSEIHyDRIGGRD
K231-u RESDGVLkPLPKKSI
K236 VLkPLPKKSIDTGMG
K282 GARPYTGKVGAEDAD
K338 AVRYSHEKLNASRGF
K366 DAFPELKKDPEMVKD
K366 DAFPELKKDPEMVKD
K372 KKDPEMVKDIINEEE
K384-u EEEVQFLkTLSRGRR
K396 GRRILDRKIQsLGDC
S399-p ILDRKIQsLGDCKTI
K451 ERRLAQLKSQGKGAG
K486 EATDDSPKYNYQSDS
K513 VLALRREKMFVDEVV
Y543 AEQGGQIYDEGYLVK
S555 LVKVDDSSEDKTEFT
K564 DKTEFTVKNAQVRGG
K625-u VLGEADQkGSLVAPD
S627 GEADQkGSLVAPDRL
K641-u LRFDFTAkGAMSTQQ
K650 AMSTQQIKKAEEIVN
K651 MSTQQIKKAEEIVNG
K664 NGMIEAAKPVYTQDC
Y667 IEAAKPVYTQDCPLA
K677 DCPLAAAKAIQGLRA
T689 LRAVFDETYPDPVRV
Y690 RAVFDETYPDPVRVV
K747-u VTEEAIAkGIRRIVA
K762 VTGAEAQKALRKSET
K772 RKSETLKKSLSAMEA
K780 SLSAMEAKVKAQTAP
K789 KAQTAPNKDVQREIA
K812 AVIPQWQKDEQRETL
K820-u DEQRETLkSLKKVMD
K846-u KRVLEKTkQLIDSNP
K876 KALNEALKLFkTHSP
K876-u KALNEALkLFkTHSP
K879-u NEALkLFkTHSPQTS
K930-a VSGLMDGkGGGKDMS
K930 VSGLMDGKGGGKDMS
K934 MDGkGGGKDMSAQAT
S937 kGGGKDMSAQATGKN
T941 KDMSAQATGKNVGCL
K943 MSAQATGKNVGCLQE
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