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Q5JTZ9

- SYAM_HUMAN

UniProt

Q5JTZ9 - SYAM_HUMAN

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Protein
Alanine--tRNA ligase, mitochondrial
Gene
AARS2, AARSL, KIAA1270
Organism
Homo sapiens (Human)
Status
Reviewed - 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 By similarity.UniRule annotation

Catalytic activityi

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

Cofactori

Binds 1 zinc ion per subunit Reviewed prediction.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi632 – 6321Zinc Reviewed prediction
Metal bindingi636 – 6361Zinc Reviewed prediction
Metal bindingi749 – 7491Zinc Reviewed prediction
Metal bindingi753 – 7531Zinc Reviewed prediction

GO - Molecular functioni

  1. ATP binding Source: UniProtKB-KW
  2. alanine-tRNA ligase activity Source: BHF-UCL
  3. metal ion binding Source: UniProtKB-KW
  4. tRNA binding Source: UniProtKB-KW

GO - Biological processi

  1. gene expression Source: Reactome
  2. mitochondrial alanyl-tRNA aminoacylation Source: BHF-UCL
  3. mitochondrial respiratory chain complex assembly Source: BHF-UCL
  4. tRNA aminoacylation for protein translation Source: Reactome
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

Enzyme and pathway databases

ReactomeiREACT_15302. Mitochondrial tRNA aminoacylation.

Names & Taxonomyi

Protein namesi
Recommended name:
Alanine--tRNA ligase, mitochondrial (EC:6.1.1.7)
Alternative name(s):
Alanyl-tRNA synthetase
Short name:
AlaRS
Gene namesi
Name:AARS2
Synonyms:AARSL, KIAA1270
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 6

Organism-specific databases

HGNCiHGNC:21022. AARS2.

Subcellular locationi

Mitochondrion 1 Publication

GO - Cellular componenti

  1. mitochondrion Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Mitochondrion

Pathology & Biotechi

Involvement in diseasei

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.1 Publication
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti155 – 1551L → R in COXPD8. 1 Publication
VAR_065956
Natural varianti592 – 5921R → W in COXPD8. 1 Publication
VAR_065957

Keywords - Diseasei

Cardiomyopathy, Disease mutation

Organism-specific databases

MIMi614096. phenotype.
Orphaneti319504. Combined oxidative phosphorylation defect type 8.
PharmGKBiPA162375129.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transit peptidei1 – 2323Mitochondrion Reviewed prediction
Add
BLAST
Chaini24 – 985962Alanine--tRNA ligase, mitochondrialUniRule annotation
PRO_0000250725Add
BLAST

Proteomic databases

MaxQBiQ5JTZ9.
PaxDbiQ5JTZ9.
PeptideAtlasiQ5JTZ9.
PRIDEiQ5JTZ9.

PTM databases

PhosphoSiteiQ5JTZ9.

Expressioni

Gene expression databases

BgeeiQ5JTZ9.
CleanExiHS_AARS2.
GenevestigatoriQ5JTZ9.

Organism-specific databases

HPAiHPA035636.

Interactioni

Subunit structurei

Monomer By similarity.UniRule annotation

Protein-protein interaction databases

BioGridi121569. 4 interactions.
IntActiQ5JTZ9. 2 interactions.
MINTiMINT-8051598.
STRINGi9606.ENSP00000244571.

Structurei

3D structure databases

ProteinModelPortaliQ5JTZ9.
SMRiQ5JTZ9. Positions 37-784.

Family & Domainsi

Domaini

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.UniRule annotation

Sequence similaritiesi

Keywords - Domaini

Transit peptide

Phylogenomic databases

eggNOGiCOG0013.
HOGENOMiHOG000156964.
HOVERGENiHBG017874.
InParanoidiQ5JTZ9.
KOiK01872.
OMAiWASKGSP.
OrthoDBiEOG7M3HZH.
PhylomeDBiQ5JTZ9.
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.
IPR018163. Thr/Ala-tRNA-synth_IIc_edit.
IPR009000. Transl_B-barrel.
IPR012947. tRNA_SAD.
[Graphical view]
PfamiPF01411. 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.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q5JTZ9-1 [UniParc]FASTAAdd to Basket

« Hide

MAASVAAAAR RLRRAIRRSP AWRGLSHRPL SSEPPAAKAS AVRAAFLNFF    50
RDRHGHRLVP SASVRPRGDP SLLFVNAGMN QFKPIFLGTV DPRSEMAGFR 100
RVANSQKCVR AGGHHNDLED VGRDLSHHTF FEMLGNWAFG GEYFKEEACN 150
MAWELLTQVY GIPEERLWIS YFDGDPKAGL DPDLETRDIW LSLGVPASRV 200
LSFGPQENFW EMGDTGPCGP CTEIHYDLAG GVGAPQLVEL WNLVFMQHNR 250
EADGSLQPLP QRHVDTGMGL ERLVAVLQGK HSTYDTDLFS PLLNAIQQGC 300
RAPPYLGRVG VADEGRTDTA YRVVADHIRT LSVCISDGIF PGMSGPPLVL 350
RRILRRAVRF SMEILKAPPG FLGSLVPVVV ETLGDAYPEL QRNSAQIANL 400
VSEDEAAFLA SLERGRRIID RTLRTLGPSD MFPAEVAWSL SLCGDLGLPL 450
DMVELMLEEK GVQLDSAGLE RLAQEEAQHR ARQAEPVQKQ GLWLDVHALG 500
ELQRQGVPPT DDSPKYNYSL RPSGSYEFGT CEAQVLQLYT EDGTAVASVG 550
KGQRCGLLLD RTNFYAEQGG QASDRGYLVR AGQEDVLFPV ARAQVCGGFI 600
LHEAVAPECL RLGDQVQLHV DEAWRLGCMA KHTATHLLNW ALRQTLGPGT 650
EQQGSHLNPE QLRLDVTTQT PLTPEQLRAV ENTVQEAVGQ DEAVYMEEVP 700
LALTAQVPGL RSLDEVYPDP VRVVSVGVPV AHALDPASQA ALQTSVELCC 750
GTHLLRTGAV GDLVIIGDRQ LSKGTTRLLA VTGEQAQQAR ELGQSLAQEV 800
KAATERLSLG SRDVAEALRL SKDIGRLIEA VETAVMPQWQ RRELLATVKM 850
LQRRANTAIR KLQMGQAAKK TQELLERHSK GPLIVDTVSA ESLSVLVKVV 900
RQLCEQAPST SVLLLSPQPM GKVLCACQVA QGAMPTFTAE AWALAVCSHM 950
GGKAWGSRVV AQGTGSTTDL EAALSIAQTY ALSQL 985
Length:985
Mass (Da):107,340
Last modified:February 15, 2005 - v1
Checksum:i721368BD05474F86
GO

Sequence cautioni

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

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti155 – 1551L → R in COXPD8. 1 Publication
VAR_065956
Natural varianti339 – 3391I → V.2 Publications
Corresponds to variant rs324136 [ dbSNP | Ensembl ].
VAR_027609
Natural varianti484 – 4841A → D.
Corresponds to variant rs495294 [ dbSNP | Ensembl ].
VAR_027610
Natural varianti592 – 5921R → W in COXPD8. 1 Publication
VAR_065957
Natural varianti850 – 8501M → V.
Corresponds to variant rs35783144 [ dbSNP | Ensembl ].
VAR_057357

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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.
CCDSiCCDS34464.1.
RefSeqiNP_065796.1. NM_020745.3.
UniGeneiHs.158381.

Genome annotation databases

EnsembliENST00000244571; ENSP00000244571; ENSG00000124608.
GeneIDi57505.
KEGGihsa:57505.
UCSCiuc010jza.1. human.

Polymorphism databases

DMDMi74742244.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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 .
CCDSi CCDS34464.1.
RefSeqi NP_065796.1. NM_020745.3.
UniGenei Hs.158381.

3D structure databases

ProteinModelPortali Q5JTZ9.
SMRi Q5JTZ9. Positions 37-784.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 121569. 4 interactions.
IntActi Q5JTZ9. 2 interactions.
MINTi MINT-8051598.
STRINGi 9606.ENSP00000244571.

Chemistry

DrugBanki DB00160. L-Alanine.

PTM databases

PhosphoSitei Q5JTZ9.

Polymorphism databases

DMDMi 74742244.

Proteomic databases

MaxQBi Q5JTZ9.
PaxDbi Q5JTZ9.
PeptideAtlasi Q5JTZ9.
PRIDEi Q5JTZ9.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000244571 ; ENSP00000244571 ; ENSG00000124608 .
GeneIDi 57505.
KEGGi hsa:57505.
UCSCi uc010jza.1. human.

Organism-specific databases

CTDi 57505.
GeneCardsi GC06M044266.
HGNCi HGNC:21022. AARS2.
HPAi HPA035636.
MIMi 612035. gene.
614096. phenotype.
neXtProti NX_Q5JTZ9.
Orphaneti 319504. Combined oxidative phosphorylation defect type 8.
PharmGKBi PA162375129.
HUGEi Search...
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG0013.
HOGENOMi HOG000156964.
HOVERGENi HBG017874.
InParanoidi Q5JTZ9.
KOi K01872.
OMAi WASKGSP.
OrthoDBi EOG7M3HZH.
PhylomeDBi Q5JTZ9.
TreeFami TF300737.

Enzyme and pathway databases

Reactomei REACT_15302. Mitochondrial tRNA aminoacylation.

Miscellaneous databases

GeneWikii AARS2.
GenomeRNAii 57505.
NextBioi 63841.
PROi Q5JTZ9.
SOURCEi Search...

Gene expression databases

Bgeei Q5JTZ9.
CleanExi HS_AARS2.
Genevestigatori Q5JTZ9.

Family and domain databases

HAMAPi MF_00036_B. Ala_tRNA_synth_B.
InterProi 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.
IPR018163. Thr/Ala-tRNA-synth_IIc_edit.
IPR009000. Transl_B-barrel.
IPR012947. tRNA_SAD.
[Graphical view ]
Pfami PF01411. tRNA-synt_2c. 1 hit.
PF07973. tRNA_SAD. 1 hit.
[Graphical view ]
PRINTSi PR00980. TRNASYNTHALA.
SMARTi SM00863. tRNA_SAD. 1 hit.
[Graphical view ]
SUPFAMi SSF101353. SSF101353. 1 hit.
SSF50447. SSF50447. 1 hit.
SSF55186. SSF55186. 1 hit.
TIGRFAMsi TIGR00344. alaS. 1 hit.
PROSITEi PS50860. AA_TRNA_LIGASE_II_ALA. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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.
    , 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. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiSYAM_HUMAN
AccessioniPrimary (citable) accession number: Q5JTZ9
Secondary accession number(s): A2RRN5
, Q8N198, Q96D02, Q9ULF0
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 3, 2006
Last sequence update: February 15, 2005
Last modified: September 3, 2014
This is version 90 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (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.

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Aminoacyl-tRNA synthetases
    List of aminoacyl-tRNA synthetase entries
  2. Human chromosome 6
    Human chromosome 6: entries, gene names and cross-references to MIM
  3. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  4. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  5. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  6. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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