Q8BGQ7 (SYAC_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Alanine--tRNA ligase, cytoplasmic
EC=6.1.1.7

Alternative name(s):
Alanyl-tRNA synthetase
Short name=AlaRS

Gene names

Name:

Aars

Organism

Mus musculus (Mouse) [Reference proteome]

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

Protein attributes

Sequence length	968 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

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. Ref.4
Catalytic activity	ATP + L-alanine + tRNA(Ala) = AMP + diphosphate + L-alanyl-tRNA(Ala). HAMAP-Rule MF_03133
Cofactor	Binds 1 zinc ion per subunit Potential.
Subunit structure	Monomer By similarity.
Subcellular location	Cytoplasm By similarity.
Domain	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. HAMAP-Rule MF_03133
Post-translational modification	ISGylated. Ref.3
Sequence similarities	Belongs to the class-II aminoacyl-tRNA synthetase family.

Ontologies

Keywords
Biological process	Protein biosynthesis
Cellular component	Cytoplasm
Ligand	ATP-binding Metal-binding Nucleotide-binding RNA-binding Zinc tRNA-binding
Molecular function	Aminoacyl-tRNA synthetase Ligase
PTM	Acetylation Phosphoprotein Ubl conjugation
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	alanyl-tRNA aminoacylation Inferred from mutant phenotype PubMed 16906134. Source: MGI cerebellar Purkinje cell layer development Inferred from mutant phenotype PubMed 16906134. Source: MGI endoplasmic reticulum unfolded protein response Inferred from mutant phenotype PubMed 16906134. Source: MGI hair follicle development Inferred from mutant phenotype PubMed 16469773. Source: MGI negative regulation of neuron apoptotic process Inferred from mutant phenotype PubMed 16906134. Source: MGI neuromuscular process controlling balance Inferred from mutant phenotype PubMed 16906134. Source: MGI protein folding Inferred from mutant phenotype PubMed 16469773. Source: MGI response to amino acid stimulus Inferred from mutant phenotype PubMed 16469773. Source: MGI skin development Inferred from mutant phenotype PubMed 16469773. Source: MGI tRNA modification Inferred from mutant phenotype PubMed 16906134. Source: MGI
Cellular_component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW alanine-tRNA ligase activity Inferred from electronic annotation. Source: EC amino acid binding Inferred from electronic annotation. Source: Compara aminoacyl-tRNA editing activity Inferred from direct assay Ref.4. Source: UniProtKB metal ion binding Inferred from electronic annotation. Source: UniProtKB-KW tRNA binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 968	968	Alanine--tRNA ligase, cytoplasmic HAMAP-Rule MF_03133		PRO_0000075282
Sites
	Metal binding	605	1	Zinc Potential
	Metal binding	609	1	Zinc Potential
	Metal binding	723	1	Zinc Potential
	Metal binding	727	1	Zinc Potential
Amino acid modifications
	Modified residue	1	1	N-acetylmethionine By similarity
	Modified residue	399	1	Phosphoserine By similarity
	Modified residue	555	1	Phosphoserine By similarity
	Modified residue	876	1	N6-acetyllysine By similarity
Experimental info
	Sequence conflict	369	1	E → D in BAC31927. Ref.1
	Sequence conflict	630	1	A → T in BAC31927. Ref.1

Sequences

	Sequence		Length	Mass (Da)
	Q8BGQ7 [UniParc]. Last modified March 1, 2003. Version 1. Checksum: 7CDF2556C81A89EC	FASTA	968	106,909
	10 20 30 40 50 60 MDATLTAREI RERFINFFRR NEHTYVHSSA TIPLDDPTLL FANAGMNQFK PIFLNTIDPS 70 80 90 100 110 120 HPMAKLSRAA NTQKCIRAGG KHNDLDDVGK DVYHHTFFEM LGSWSFGDYF KELACKMALE 130 140 150 160 170 180 LLTQEFGIPV ERLYVTYFGG DEAAGLEPDL ECRQIWQNLG LDEARILPGN MKDNFWEMGD 190 200 210 220 230 240 TGPCGPCSEI HYDRIGGRDA AHLVNQDDPN VLEIWNLVFI QYNRESDGVL KPLPKKSIDT 250 260 270 280 290 300 GMGLERLVSV LQNKMSNYDT DLFMPYFEAI QKGTGARPYT GKVGAEDADG IDMAYRVLAD 310 320 330 340 350 360 HARTITVALA DGGRPDNTGR GYVLRRILRR AVRYSHEKLN ASRGFFATLV DVVVQSLGDA 370 380 390 400 410 420 FPELKKDPEM VKDIINEEEV QFLKTLSRGR RILDRKIQSL GDCKTIPGDT AWLLYDTYGF 430 440 450 460 470 480 PVDLTGLIAE EKGLVVDMNG FEEERRLAQL KSQGKGAGDE DLIMLDIYAI EELRAKGLEA 490 500 510 520 530 540 TDDSPKYNYQ SDSSGSYVFE CTVATVLALR REKMFVDEVV TGQECGVVLD KTCFYAEQGG 550 560 570 580 590 600 QIYDEGYLVK VDDSSEDKTE FTVKNAQVRG GYVLHIGTIY GNLKVGDQVR LFIDEPRRRP 610 620 630 640 650 660 VMSNHTATHI LNFALRSVLG EADQKGSLVA PDRLRFDFTA KGAMSTQQIK KAEEIVNGMI 670 680 690 700 710 720 EAAKPVYTQD CPLAAAKAIQ GLRAVFDETY PDPVRVVSIG VPVSELLDDP CGPAGSLTSV 730 740 750 760 770 780 EFCGGTHLRN SSHAGAFVIV TEEAIAKGIR RIVAVTGAEA QKALRKSETL KKSLSAMEAK 790 800 810 820 830 840 VKAQTAPNKD VQREIADLGE ALATAVIPQW QKDEQRETLK SLKKVMDDLD RASKADVQKR 850 860 870 880 890 900 VLEKTKQLID SNPNQPLVIL EMESGASAKA LNEALKLFKT HSPQTSAMLF TVDNEAGKIT 910 920 930 940 950 960 CLCQVPQNAA NRGLKASEWV QQVSGLMDGK GGGKDMSAQA TGKNVGCLQE ALQLATSFAQ LRLGDVKN

References

	« Hide 'large scale' referencesShow 'large scale' references »
[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]	"Proteomic identification of proteins conjugated to ISG15 in mouse and human cells." Giannakopoulos N.V., Luo J.K., Papov V., Zou W., Lenschow D.J., Jacobs B.S., Borden E.C., Li J., Virgin H.W., Zhang D.E. Biochem. Biophys. Res. Commun. 336:496-506(2005) [PubMed] [Europe PMC] [Abstract] 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).
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AK044451 mRNA. Translation: BAC31927.1. AK085725 mRNA. Translation: BAC39520.1. BC033273 mRNA. Translation: AAH33273.1.
IPI	IPI00321308.
RefSeq	NP_666329.2. NM_146217.4.
UniGene	Mm.24174.
3D structure databases
ProteinModelPortal	Q8BGQ7.
SMR	Q8BGQ7. Positions 6-757.
ModBase	Search...
PTM databases
PhosphoSite	Q8BGQ7.
Proteomic databases
PaxDb	Q8BGQ7.
PRIDE	Q8BGQ7.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENSMUST00000034441; ENSMUSP00000034441; ENSMUSG00000031960.
GeneID	234734.
KEGG	mmu:234734.
UCSC	uc009nlo.1. mouse.
Organism-specific databases
CTD	16.
MGI	MGI:2384560. Aars.
Phylogenomic databases
eggNOG	COG0013.
GeneTree	ENSGT00390000016019.
HOGENOM	HOG000156964.
HOVERGEN	HBG017874.
InParanoid	Q8BGQ7.
KO	K01872.
OMA	GTHITNT.
OrthoDB	EOG45X7VC.
Gene expression databases
ArrayExpress	Q8BGQ7.
Bgee	Q8BGQ7.
CleanEx	MM_AARS.
Genevestigator	Q8BGQ7.
GermOnline	ENSMUSG00000031960. Mus musculus.
Family and domain databases
HAMAP	MF_00036_B. Ala_tRNA_synth_B.
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. [Graphical view]
PANTHER	PTHR11777:SF6. PTHR11777:SF6. 1 hit.
Pfam	PF02272. DHHA1. 1 hit. PF01411. tRNA-synt_2c. 1 hit. PF07973. tRNA_SAD. 1 hit. [Graphical view]
PRINTS	PR00980. TRNASYNTHALA.
SMART	SM00863. tRNA_SAD. 1 hit. [Graphical view]
SUPFAM	SSF101353. Ala-tRNA-synth_IIc_anticod-bd. 1 hit. SSF55186. Thr/Ala-tRNA-synth_IIc_edit. 1 hit.
TIGRFAMs	TIGR00344. alaS. 1 hit.
PROSITE	PS50860. AA_TRNA_LIGASE_II_ALA. 1 hit. [Graphical view]
ProtoNet	Search...
Other
NextBio	382335.
SOURCE	Search...

Entry information

Entry name

SYAC_MOUSE

Accession

Primary (citable) accession number: Q8BGQ7
Secondary accession number(s): Q8BXR0

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 10, 2004
Last sequence update:	March 1, 2003
Last modified:	May 1, 2013
This is version 82 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program