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Protein

Alanine--tRNA ligase, cytoplasmic

Gene

Aars

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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.UniRule annotation1 Publication

Catalytic activityi

ATP + L-alanine + tRNA(Ala) = AMP + diphosphate + L-alanyl-tRNA(Ala).UniRule annotation

Cofactori

Zn2+UniRule annotationNote: Binds 1 zinc ion per subunit.UniRule annotation

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi605 – 6051ZincUniRule annotation
Metal bindingi609 – 6091ZincUniRule annotation
Metal bindingi723 – 7231ZincUniRule annotation
Metal bindingi727 – 7271ZincUniRule annotation

GO - Molecular functioni

GO - Biological processi

  • alanyl-tRNA aminoacylation Source: MGI
  • cellular response to unfolded protein Source: MGI
  • cerebellar Purkinje cell layer development Source: MGI
  • endoplasmic reticulum unfolded protein response Source: MGI
  • hair follicle development Source: MGI
  • negative regulation of neuron apoptotic process Source: MGI
  • neuromuscular process Source: MGI
  • neuromuscular process controlling balance Source: MGI
  • protein folding Source: MGI
  • regulation of translational fidelity Source: GOC
  • response to amino acid Source: MGI
  • skin development Source: MGI
  • tRNA modification Source: MGI
Complete GO annotation...

Keywords - Molecular functioni

Aminoacyl-tRNA synthetase, Ligase

Keywords - Biological processi

Protein biosynthesis

Keywords - Ligandi

ATP-binding, Metal-binding, Nucleotide-binding, RNA-binding, tRNA-binding, Zinc

Names & Taxonomyi

Protein namesi
Recommended name:
Alanine--tRNA ligase, cytoplasmicUniRule annotation (EC:6.1.1.7UniRule annotation)
Alternative name(s):
Alanyl-tRNA synthetaseUniRule annotation
Short name:
AlaRSUniRule annotation
Gene namesi
Name:Aars
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 8

Organism-specific databases

MGIiMGI:2384560. Aars.

Subcellular locationi

  • Cytoplasm UniRule annotation

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 968968Alanine--tRNA ligase, cytoplasmicPRO_0000075282Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei1 – 11N-acetylmethionineUniRule annotationBy similarity
Modified residuei399 – 3991PhosphoserineBy similarity
Modified residuei555 – 5551PhosphoserineBy similarity
Modified residuei876 – 8761N6-acetyllysineBy similarity

Post-translational modificationi

ISGylated.UniRule annotation1 Publication

Keywords - PTMi

Acetylation, Phosphoprotein, Ubl conjugation

Proteomic databases

EPDiQ8BGQ7.
MaxQBiQ8BGQ7.
PaxDbiQ8BGQ7.
PRIDEiQ8BGQ7.

PTM databases

iPTMnetiQ8BGQ7.
PhosphoSiteiQ8BGQ7.
SwissPalmiQ8BGQ7.

Expressioni

Gene expression databases

BgeeiQ8BGQ7.
CleanExiMM_AARS.
GenevisibleiQ8BGQ7. MM.

Interactioni

Subunit structurei

Monomer.UniRule annotation

Protein-protein interaction databases

BioGridi231572. 2 interactions.
IntActiQ8BGQ7. 4 interactions.
MINTiMINT-1854740.
STRINGi10090.ENSMUSP00000034441.

Structurei

3D structure databases

ProteinModelPortaliQ8BGQ7.
SMRiQ8BGQ7. Positions 6-843.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domaini

Consists of three domains; the N-terminal catalytic domain, the editing domain and the C-terminal C-Ala domain. 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 (By similarity). The editing domain removes incorrectly charged amino acids from Gly-tRNA(Ala) and Ser-tRNA(Ala) to yield uncharged tRNA(Ala) and the amino acid.By similarity

Sequence similaritiesi

Belongs to the class-II aminoacyl-tRNA synthetase family.UniRule annotation

Phylogenomic databases

eggNOGiKOG0188. Eukaryota.
COG0013. LUCA.
GeneTreeiENSGT00390000016019.
HOGENOMiHOG000156964.
HOVERGENiHBG017874.
InParanoidiQ8BGQ7.
KOiK01872.
OMAiFDFNCPR.
OrthoDBiEOG7M3HZH.
PhylomeDBiQ8BGQ7.
TreeFamiTF300737.

Family and domain databases

HAMAPiMF_00036_B. Ala_tRNA_synth_B.
InterProiIPR002318. 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. DHHA1_dom.
IPR018163. Thr/Ala-tRNA-synth_IIc_edit.
IPR009000. Transl_B-barrel.
IPR012947. tRNA_SAD.
[Graphical view]
PfamiPF02272. DHHA1. 1 hit.
PF01411. tRNA-synt_2c. 1 hit.
PF07973. tRNA_SAD. 1 hit.
[Graphical view]
PRINTSiPR00980. TRNASYNTHALA.
SMARTiSM00863. tRNA_SAD. 1 hit.
[Graphical view]
SUPFAMiSSF101353. SSF101353. 1 hit.
SSF50447. SSF50447. 1 hit.
SSF55186. SSF55186. 1 hit.
TIGRFAMsiTIGR00344. alaS. 1 hit.
PROSITEiPS50860. AA_TRNA_LIGASE_II_ALA. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q8BGQ7-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MDATLTAREI RERFINFFRR NEHTYVHSSA TIPLDDPTLL FANAGMNQFK
60 70 80 90 100
PIFLNTIDPS HPMAKLSRAA NTQKCIRAGG KHNDLDDVGK DVYHHTFFEM
110 120 130 140 150
LGSWSFGDYF KELACKMALE LLTQEFGIPV ERLYVTYFGG DEAAGLEPDL
160 170 180 190 200
ECRQIWQNLG LDEARILPGN MKDNFWEMGD TGPCGPCSEI HYDRIGGRDA
210 220 230 240 250
AHLVNQDDPN VLEIWNLVFI QYNRESDGVL KPLPKKSIDT GMGLERLVSV
260 270 280 290 300
LQNKMSNYDT DLFMPYFEAI QKGTGARPYT GKVGAEDADG IDMAYRVLAD
310 320 330 340 350
HARTITVALA DGGRPDNTGR GYVLRRILRR AVRYSHEKLN ASRGFFATLV
360 370 380 390 400
DVVVQSLGDA FPELKKDPEM VKDIINEEEV QFLKTLSRGR RILDRKIQSL
410 420 430 440 450
GDCKTIPGDT AWLLYDTYGF PVDLTGLIAE EKGLVVDMNG FEEERRLAQL
460 470 480 490 500
KSQGKGAGDE DLIMLDIYAI EELRAKGLEA TDDSPKYNYQ SDSSGSYVFE
510 520 530 540 550
CTVATVLALR REKMFVDEVV TGQECGVVLD KTCFYAEQGG QIYDEGYLVK
560 570 580 590 600
VDDSSEDKTE FTVKNAQVRG GYVLHIGTIY GNLKVGDQVR LFIDEPRRRP
610 620 630 640 650
VMSNHTATHI LNFALRSVLG EADQKGSLVA PDRLRFDFTA KGAMSTQQIK
660 670 680 690 700
KAEEIVNGMI EAAKPVYTQD CPLAAAKAIQ GLRAVFDETY PDPVRVVSIG
710 720 730 740 750
VPVSELLDDP CGPAGSLTSV EFCGGTHLRN SSHAGAFVIV TEEAIAKGIR
760 770 780 790 800
RIVAVTGAEA QKALRKSETL KKSLSAMEAK VKAQTAPNKD VQREIADLGE
810 820 830 840 850
ALATAVIPQW QKDEQRETLK SLKKVMDDLD RASKADVQKR VLEKTKQLID
860 870 880 890 900
SNPNQPLVIL EMESGASAKA LNEALKLFKT HSPQTSAMLF TVDNEAGKIT
910 920 930 940 950
CLCQVPQNAA NRGLKASEWV QQVSGLMDGK GGGKDMSAQA TGKNVGCLQE
960
ALQLATSFAQ LRLGDVKN
Length:968
Mass (Da):106,909
Last modified:March 1, 2003 - v1
Checksum:i7CDF2556C81A89EC
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti369 – 3691E → D in BAC31927 (PubMed:16141072).Curated
Sequence conflicti630 – 6301A → T in BAC31927 (PubMed:16141072).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK044451 mRNA. Translation: BAC31927.1.
AK085725 mRNA. Translation: BAC39520.1.
BC033273 mRNA. Translation: AAH33273.1.
CCDSiCCDS40478.1.
RefSeqiNP_666329.2. NM_146217.4.
XP_006530984.1. XM_006530921.1.
XP_006530985.1. XM_006530922.1.
XP_006530987.1. XM_006530924.1.
UniGeneiMm.24174.
Mm.491269.

Genome annotation databases

EnsembliENSMUST00000034441; ENSMUSP00000034441; ENSMUSG00000031960.
GeneIDi234734.
KEGGimmu:234734.
UCSCiuc009nlo.2. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK044451 mRNA. Translation: BAC31927.1.
AK085725 mRNA. Translation: BAC39520.1.
BC033273 mRNA. Translation: AAH33273.1.
CCDSiCCDS40478.1.
RefSeqiNP_666329.2. NM_146217.4.
XP_006530984.1. XM_006530921.1.
XP_006530985.1. XM_006530922.1.
XP_006530987.1. XM_006530924.1.
UniGeneiMm.24174.
Mm.491269.

3D structure databases

ProteinModelPortaliQ8BGQ7.
SMRiQ8BGQ7. Positions 6-843.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi231572. 2 interactions.
IntActiQ8BGQ7. 4 interactions.
MINTiMINT-1854740.
STRINGi10090.ENSMUSP00000034441.

PTM databases

iPTMnetiQ8BGQ7.
PhosphoSiteiQ8BGQ7.
SwissPalmiQ8BGQ7.

Proteomic databases

EPDiQ8BGQ7.
MaxQBiQ8BGQ7.
PaxDbiQ8BGQ7.
PRIDEiQ8BGQ7.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000034441; ENSMUSP00000034441; ENSMUSG00000031960.
GeneIDi234734.
KEGGimmu:234734.
UCSCiuc009nlo.2. mouse.

Organism-specific databases

CTDi16.
MGIiMGI:2384560. Aars.

Phylogenomic databases

eggNOGiKOG0188. Eukaryota.
COG0013. LUCA.
GeneTreeiENSGT00390000016019.
HOGENOMiHOG000156964.
HOVERGENiHBG017874.
InParanoidiQ8BGQ7.
KOiK01872.
OMAiFDFNCPR.
OrthoDBiEOG7M3HZH.
PhylomeDBiQ8BGQ7.
TreeFamiTF300737.

Miscellaneous databases

PROiQ8BGQ7.
SOURCEiSearch...

Gene expression databases

BgeeiQ8BGQ7.
CleanExiMM_AARS.
GenevisibleiQ8BGQ7. MM.

Family and domain databases

HAMAPiMF_00036_B. Ala_tRNA_synth_B.
InterProiIPR002318. 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. DHHA1_dom.
IPR018163. Thr/Ala-tRNA-synth_IIc_edit.
IPR009000. Transl_B-barrel.
IPR012947. tRNA_SAD.
[Graphical view]
PfamiPF02272. DHHA1. 1 hit.
PF01411. tRNA-synt_2c. 1 hit.
PF07973. tRNA_SAD. 1 hit.
[Graphical view]
PRINTSiPR00980. TRNASYNTHALA.
SMARTiSM00863. tRNA_SAD. 1 hit.
[Graphical view]
SUPFAMiSSF101353. SSF101353. 1 hit.
SSF50447. SSF50447. 1 hit.
SSF55186. SSF55186. 1 hit.
TIGRFAMsiTIGR00344. alaS. 1 hit.
PROSITEiPS50860. AA_TRNA_LIGASE_II_ALA. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: C57BL/6J.
    Tissue: Mammary gland and Retina.
  2. "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].
    Strain: FVB/N.
    Tissue: Liver.
  3. Cited for: ISGYLATION.
  4. "Paradox of mistranslation of serine for alanine caused by AlaRS recognition dilemma."
    Guo M., Chong Y.E., Shapiro R., Beebe K., Yang X.L., Schimmel P.
    Nature 462:808-812(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN EDITING ACTIVITY ON MISCHARGED TRNA(ALA).
  5. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas, Spleen and Testis.

Entry informationi

Entry nameiSYAC_MOUSE
AccessioniPrimary (citable) accession number: Q8BGQ7
Secondary accession number(s): Q8BXR0
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 10, 2004
Last sequence update: March 1, 2003
Last modified: June 8, 2016
This is version 114 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Aminoacyl-tRNA synthetases
    List of aminoacyl-tRNA synthetase entries
  2. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  3. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.