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Q5JTZ9 (SYAM_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 86. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Alanine--tRNA ligase, mitochondrial

EC=6.1.1.7
Alternative name(s):
Alanyl-tRNA synthetase
Short name=AlaRS
Gene names
Name:AARS2
Synonyms:AARSL, KIAA1270
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length985 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence 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 By similarity. HAMAP-Rule MF_03133

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. HAMAP-Rule MF_03133

Subcellular location

Mitochondrion Ref.5.

Domain

Consists of three domains; the N-terminal catalytic domain, the editing domain and the C-terminal C-Ala domain. The editing domain removes incorrectly charged amino acids, while 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. HAMAP-Rule MF_03133

Involvement in disease

Combined oxidative phosphorylation deficiency 8 (COXPD8) [MIM:614096]: A mitochondrial disease characterized by a lethal infantile hypertrophic cardiomyopathy, generalized muscle dysfunction and some neurologic involvement. The liver is not affected.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.5

Sequence similarities

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

Sequence caution

The sequence BAA86584.1 differs from that shown. Reason: Erroneous initiation.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Transit peptide1 – 2323Mitochondrion Potential
Chain24 – 985962Alanine--tRNA ligase, mitochondrial HAMAP-Rule MF_03133
PRO_0000250725

Sites

Metal binding6321Zinc Potential
Metal binding6361Zinc Potential
Metal binding7491Zinc Potential
Metal binding7531Zinc Potential

Natural variations

Natural variant1551L → R in COXPD8. Ref.5
VAR_065956
Natural variant3391I → V. Ref.1 Ref.3
Corresponds to variant rs324136 [ dbSNP | Ensembl ].
VAR_027609
Natural variant4841A → D.
Corresponds to variant rs495294 [ dbSNP | Ensembl ].
VAR_027610
Natural variant5921R → W in COXPD8. Ref.5
VAR_065957
Natural variant8501M → V.
Corresponds to variant rs35783144 [ dbSNP | Ensembl ].
VAR_057357

Sequences

Sequence LengthMass (Da)Tools
Q5JTZ9 [UniParc].

Last modified February 15, 2005. Version 1.
Checksum: 721368BD05474F86

FASTA985107,340
        10         20         30         40         50         60 
MAASVAAAAR RLRRAIRRSP AWRGLSHRPL SSEPPAAKAS AVRAAFLNFF RDRHGHRLVP 

        70         80         90        100        110        120 
SASVRPRGDP SLLFVNAGMN QFKPIFLGTV DPRSEMAGFR RVANSQKCVR AGGHHNDLED 

       130        140        150        160        170        180 
VGRDLSHHTF FEMLGNWAFG GEYFKEEACN MAWELLTQVY GIPEERLWIS YFDGDPKAGL 

       190        200        210        220        230        240 
DPDLETRDIW LSLGVPASRV LSFGPQENFW EMGDTGPCGP CTEIHYDLAG GVGAPQLVEL 

       250        260        270        280        290        300 
WNLVFMQHNR EADGSLQPLP QRHVDTGMGL ERLVAVLQGK HSTYDTDLFS PLLNAIQQGC 

       310        320        330        340        350        360 
RAPPYLGRVG VADEGRTDTA YRVVADHIRT LSVCISDGIF PGMSGPPLVL RRILRRAVRF 

       370        380        390        400        410        420 
SMEILKAPPG FLGSLVPVVV ETLGDAYPEL QRNSAQIANL VSEDEAAFLA SLERGRRIID 

       430        440        450        460        470        480 
RTLRTLGPSD MFPAEVAWSL SLCGDLGLPL DMVELMLEEK GVQLDSAGLE RLAQEEAQHR 

       490        500        510        520        530        540 
ARQAEPVQKQ GLWLDVHALG ELQRQGVPPT DDSPKYNYSL RPSGSYEFGT CEAQVLQLYT 

       550        560        570        580        590        600 
EDGTAVASVG KGQRCGLLLD RTNFYAEQGG QASDRGYLVR AGQEDVLFPV ARAQVCGGFI 

       610        620        630        640        650        660 
LHEAVAPECL RLGDQVQLHV DEAWRLGCMA KHTATHLLNW ALRQTLGPGT EQQGSHLNPE 

       670        680        690        700        710        720 
QLRLDVTTQT PLTPEQLRAV ENTVQEAVGQ DEAVYMEEVP LALTAQVPGL RSLDEVYPDP 

       730        740        750        760        770        780 
VRVVSVGVPV AHALDPASQA ALQTSVELCC GTHLLRTGAV GDLVIIGDRQ LSKGTTRLLA 

       790        800        810        820        830        840 
VTGEQAQQAR ELGQSLAQEV KAATERLSLG SRDVAEALRL SKDIGRLIEA VETAVMPQWQ 

       850        860        870        880        890        900 
RRELLATVKM LQRRANTAIR KLQMGQAAKK TQELLERHSK GPLIVDTVSA ESLSVLVKVV 

       910        920        930        940        950        960 
RQLCEQAPST SVLLLSPQPM GKVLCACQVA QGAMPTFTAE AWALAVCSHM GGKAWGSRVV 

       970        980 
AQGTGSTTDL EAALSIAQTY ALSQL 

« Hide

References

« Hide 'large scale' references
[1]"Prediction of the coding sequences of unidentified human genes. XV. The complete sequences of 100 new cDNA clones from brain which code for large proteins in vitro."
Nagase T., Ishikawa K., Kikuno R., Hirosawa M., Nomura N., Ohara O.
DNA Res. 6:337-345(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], VARIANT VAL-339.
Tissue: Brain.
[2]"The DNA sequence and analysis of human chromosome 6."
Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L., Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., Gilbert J.G.R., Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D., Andrews T.D. expand/collapse author list , Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H., Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J., Brown J.Y., Burford D.C., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V., Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J., Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., Ellington A.E., Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J., French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J., Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C., Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A., Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R., Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M., Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A., Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L., Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I., Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y., Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E., Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A., Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W., Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M., West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J., Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M., Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I., Rogers J., Beck S.
Nature 425:805-811(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[3]"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], VARIANT VAL-339.
Tissue: Lung.
[4]"Toward the full set of human mitochondrial aminoacyl-tRNA synthetases: characterization of AspRS and TyrRS."
Bonnefond L., Fender A., Rudinger-Thirion J., Giege R., Florentz C., Sissler M.
Biochemistry 44:4805-4816(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION.
[5]"Exome sequencing identifies mitochondrial alanyl-tRNA synthetase mutations in infantile mitochondrial cardiomyopathy."
Gotz A., Tyynismaa H., Euro L., Ellonen P., Hyotylainen T., Ojala T., Hamalainen R.H., Tommiska J., Raivio T., Oresic M., Karikoski R., Tammela O., Simola K.O., Paetau A., Tyni T., Suomalainen A.
Am. J. Hum. Genet. 88:635-642(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION, VARIANTS COXPD8 ARG-155 AND TRP-592.
[6]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AB033096 mRNA. Translation: BAA86584.1. Different initiation.
AL353588 Genomic DNA. Translation: CAI40747.1.
BC013593 mRNA. Translation: AAH13593.1.
BC033169 mRNA. Translation: AAH33169.1.
BC131728 mRNA. Translation: AAI31729.1.
RefSeqNP_065796.1. NM_020745.3.
UniGeneHs.158381.

3D structure databases

ProteinModelPortalQ5JTZ9.
SMRQ5JTZ9. Positions 37-784.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid121569. 2 interactions.
IntActQ5JTZ9. 2 interactions.
MINTMINT-8051598.
STRING9606.ENSP00000244571.

Chemistry

DrugBankDB00160. L-Alanine.

PTM databases

PhosphoSiteQ5JTZ9.

Polymorphism databases

DMDM74742244.

Proteomic databases

PaxDbQ5JTZ9.
PeptideAtlasQ5JTZ9.
PRIDEQ5JTZ9.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000244571; ENSP00000244571; ENSG00000124608.
GeneID57505.
KEGGhsa:57505.
UCSCuc010jza.1. human.

Organism-specific databases

CTD57505.
GeneCardsGC06M044266.
HGNCHGNC:21022. AARS2.
HPAHPA035636.
MIM612035. gene.
614096. phenotype.
neXtProtNX_Q5JTZ9.
Orphanet319504. Combined oxidative phosphorylation defect type 8.
PharmGKBPA162375129.
HUGESearch...
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG0013.
HOGENOMHOG000156964.
HOVERGENHBG017874.
InParanoidQ5JTZ9.
KOK01872.
OMAISQPSIR.
OrthoDBEOG7M3HZH.
PhylomeDBQ5JTZ9.
TreeFamTF300737.

Enzyme and pathway databases

ReactomeREACT_71. Gene Expression.

Gene expression databases

BgeeQ5JTZ9.
CleanExHS_AARS2.
GenevestigatorQ5JTZ9.

Family and domain databases

HAMAPMF_00036_B. Ala_tRNA_synth_B.
InterProIPR002318. 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.
IPR018163. Thr/Ala-tRNA-synth_IIc_edit.
IPR009000. Transl_B-barrel.
IPR012947. tRNA_SAD.
[Graphical view]
PANTHERPTHR11777:SF6. PTHR11777:SF6. 1 hit.
PfamPF01411. tRNA-synt_2c. 1 hit.
PF07973. tRNA_SAD. 1 hit.
[Graphical view]
PRINTSPR00980. TRNASYNTHALA.
SMARTSM00863. tRNA_SAD. 1 hit.
[Graphical view]
SUPFAMSSF101353. SSF101353. 1 hit.
SSF50447. SSF50447. 1 hit.
SSF55186. SSF55186. 1 hit.
TIGRFAMsTIGR00344. alaS. 1 hit.
PROSITEPS50860. AA_TRNA_LIGASE_II_ALA. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

GeneWikiAARS2.
GenomeRNAi57505.
NextBio63841.
PROQ5JTZ9.
SOURCESearch...

Entry information

Entry nameSYAM_HUMAN
AccessionPrimary (citable) accession number: Q5JTZ9
Secondary accession number(s): A2RRN5 expand/collapse secondary AC list , Q8N198, Q96D02, Q9ULF0
Entry history
Integrated into UniProtKB/Swiss-Prot: October 3, 2006
Last sequence update: February 15, 2005
Last modified: April 16, 2014
This is version 86 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Relevant documents

SIMILARITY comments

Index of protein domains and families

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 6

Human chromosome 6: entries, gene names and cross-references to MIM

Aminoacyl-tRNA synthetases

List of aminoacyl-tRNA synthetase entries