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Protein

Alanine--tRNA ligase, mitochondrial

Gene

AARS2

Organism
Homo sapiens (Human)
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 annotation

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 bindingi632 – 6321ZincUniRule annotation
Metal bindingi636 – 6361ZincUniRule annotation
Metal bindingi749 – 7491ZincUniRule annotation
Metal bindingi753 – 7531ZincUniRule annotation

GO - Molecular functioni

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

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

BRENDAi6.1.1.7. 2681.
ReactomeiREACT_15302. Mitochondrial tRNA aminoacylation.

Names & Taxonomyi

Protein namesi
Recommended name:
Alanine--tRNA ligase, mitochondrialUniRule annotation (EC:6.1.1.7UniRule annotation)
Alternative name(s):
Alanyl-tRNA synthetaseUniRule annotation
Short name:
AlaRSUniRule annotation
Gene namesi
Name:AARS2UniRule annotation
Synonyms:AARSL, KIAA1270
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome 6

Organism-specific databases

HGNCiHGNC:21022. AARS2.

Subcellular locationi

  1. Mitochondrion UniRule annotation1 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)1 Publication

The disease is caused by mutations affecting the gene represented in this entry.

Disease descriptionA mitochondrial disease characterized by a lethal infantile hypertrophic cardiomyopathy, generalized muscle dysfunction and some neurologic involvement. The liver is not affected.

See also OMIM:614096
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
Leukoencephalopathy, progressive, with ovarian failure (LKENP)1 Publication

The disease is caused by mutations affecting the gene represented in this entry.

Disease descriptionAn autosomal recessive neurodegenerative disorder characterized by childhood- to adulthood-onset of signs of neurologic deterioration consisting of ataxia, spasticity, and cognitive decline with features of frontal lobe dysfunction. Brain MRI shows leukoencephalopathy with striking involvement of deep white matter, and cerebellar atrophy. All female patients develop premature ovarian failure.

See also OMIM:615889
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti50 – 501F → C in LKENP; deleterious only under stress conditions. 1 Publication
VAR_071837
Natural varianti405 – 4051E → K in LKENP. 1 Publication
VAR_071841
Natural varianti965 – 9651G → R in LKENP. 1 Publication
VAR_071843

Keywords - Diseasei

Cardiomyopathy, Disease mutation, Premature ovarian failure

Organism-specific databases

MIMi614096. phenotype.
615889. phenotype.
Orphaneti319504. Combined oxidative phosphorylation defect type 8.
PharmGKBiPA162375129.

Chemistry

DrugBankiDB00160. L-Alanine.

Polymorphism and mutation databases

BioMutaiAARS2.
DMDMi74742244.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transit peptidei1 – 2323MitochondrionUniRule annotationAdd
BLAST
Chaini24 – 985962Alanine--tRNA ligase, mitochondrialPRO_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.UniRule annotation

Protein-protein interaction databases

BioGridi121569. 11 interactions.
IntActiQ5JTZ9. 2 interactions.
MINTiMINT-8051598.
STRINGi9606.ENSP00000244571.

Structurei

3D structure databases

ProteinModelPortaliQ5JTZ9.
SMRiQ5JTZ9. Positions 22-884.
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 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.UniRule annotation

Sequence similaritiesi

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

Keywords - Domaini

Transit peptide

Phylogenomic databases

eggNOGiCOG0013.
GeneTreeiENSGT00390000016019.
HOGENOMiHOG000156964.
HOVERGENiHBG017874.
InParanoidiQ5JTZ9.
KOiK01872.
OMAiFPAEVAW.
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

        10         20         30         40         50
MAASVAAAAR RLRRAIRRSP AWRGLSHRPL SSEPPAAKAS AVRAAFLNFF
60 70 80 90 100
RDRHGHRLVP SASVRPRGDP SLLFVNAGMN QFKPIFLGTV DPRSEMAGFR
110 120 130 140 150
RVANSQKCVR AGGHHNDLED VGRDLSHHTF FEMLGNWAFG GEYFKEEACN
160 170 180 190 200
MAWELLTQVY GIPEERLWIS YFDGDPKAGL DPDLETRDIW LSLGVPASRV
210 220 230 240 250
LSFGPQENFW EMGDTGPCGP CTEIHYDLAG GVGAPQLVEL WNLVFMQHNR
260 270 280 290 300
EADGSLQPLP QRHVDTGMGL ERLVAVLQGK HSTYDTDLFS PLLNAIQQGC
310 320 330 340 350
RAPPYLGRVG VADEGRTDTA YRVVADHIRT LSVCISDGIF PGMSGPPLVL
360 370 380 390 400
RRILRRAVRF SMEILKAPPG FLGSLVPVVV ETLGDAYPEL QRNSAQIANL
410 420 430 440 450
VSEDEAAFLA SLERGRRIID RTLRTLGPSD MFPAEVAWSL SLCGDLGLPL
460 470 480 490 500
DMVELMLEEK GVQLDSAGLE RLAQEEAQHR ARQAEPVQKQ GLWLDVHALG
510 520 530 540 550
ELQRQGVPPT DDSPKYNYSL RPSGSYEFGT CEAQVLQLYT EDGTAVASVG
560 570 580 590 600
KGQRCGLLLD RTNFYAEQGG QASDRGYLVR AGQEDVLFPV ARAQVCGGFI
610 620 630 640 650
LHEAVAPECL RLGDQVQLHV DEAWRLGCMA KHTATHLLNW ALRQTLGPGT
660 670 680 690 700
EQQGSHLNPE QLRLDVTTQT PLTPEQLRAV ENTVQEAVGQ DEAVYMEEVP
710 720 730 740 750
LALTAQVPGL RSLDEVYPDP VRVVSVGVPV AHALDPASQA ALQTSVELCC
760 770 780 790 800
GTHLLRTGAV GDLVIIGDRQ LSKGTTRLLA VTGEQAQQAR ELGQSLAQEV
810 820 830 840 850
KAATERLSLG SRDVAEALRL SKDIGRLIEA VETAVMPQWQ RRELLATVKM
860 870 880 890 900
LQRRANTAIR KLQMGQAAKK TQELLERHSK GPLIVDTVSA ESLSVLVKVV
910 920 930 940 950
RQLCEQAPST SVLLLSPQPM GKVLCACQVA QGAMPTFTAE AWALAVCSHM
960 970 980
GGKAWGSRVV AQGTGSTTDL EAALSIAQTY ALSQL
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. Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti50 – 501F → C in LKENP; deleterious only under stress conditions. 1 Publication
VAR_071837
Natural varianti77 – 771A → V Found in patient with leukoencephalopathy; unknown pathological significance. 1 Publication
VAR_071838
Natural varianti131 – 1311Missing Found in patient with leukoencephalopathy; unknown pathological significance. 1 Publication
VAR_071839
Natural varianti155 – 1551L → R in COXPD8. 1 Publication
VAR_065956
Natural varianti199 – 1991R → C Found in patient with leukoencephalopathy; unknown pathological significance. 1 Publication
VAR_071840
Natural varianti339 – 3391I → V.2 Publications
Corresponds to variant rs324136 [ dbSNP | Ensembl ].
VAR_027609
Natural varianti405 – 4051E → K in LKENP. 1 Publication
VAR_071841
Natural varianti484 – 4841A → D.
Corresponds to variant rs495294 [ dbSNP | Ensembl ].
VAR_027610
Natural varianti592 – 5921R → W in COXPD8. 1 Publication
VAR_065957
Natural varianti730 – 7301V → M Found in patient with leukoencephalopathy; unknown pathological significance. 1 Publication
VAR_071842
Natural varianti850 – 8501M → V.
Corresponds to variant rs35783144 [ dbSNP | Ensembl ].
VAR_057357
Natural varianti965 – 9651G → R in LKENP. 1 Publication
VAR_071843

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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 and mutation databases

BioMutaiAARS2.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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.

3D structure databases

ProteinModelPortaliQ5JTZ9.
SMRiQ5JTZ9. Positions 22-884.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi121569. 11 interactions.
IntActiQ5JTZ9. 2 interactions.
MINTiMINT-8051598.
STRINGi9606.ENSP00000244571.

Chemistry

DrugBankiDB00160. L-Alanine.

PTM databases

PhosphoSiteiQ5JTZ9.

Polymorphism and mutation databases

BioMutaiAARS2.
DMDMi74742244.

Proteomic databases

MaxQBiQ5JTZ9.
PaxDbiQ5JTZ9.
PeptideAtlasiQ5JTZ9.
PRIDEiQ5JTZ9.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

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

Organism-specific databases

CTDi57505.
GeneCardsiGC06M044266.
HGNCiHGNC:21022. AARS2.
HPAiHPA035636.
MIMi612035. gene.
614096. phenotype.
615889. phenotype.
neXtProtiNX_Q5JTZ9.
Orphaneti319504. Combined oxidative phosphorylation defect type 8.
PharmGKBiPA162375129.
HUGEiSearch...
GenAtlasiSearch...

Phylogenomic databases

eggNOGiCOG0013.
GeneTreeiENSGT00390000016019.
HOGENOMiHOG000156964.
HOVERGENiHBG017874.
InParanoidiQ5JTZ9.
KOiK01872.
OMAiFPAEVAW.
OrthoDBiEOG7M3HZH.
PhylomeDBiQ5JTZ9.
TreeFamiTF300737.

Enzyme and pathway databases

BRENDAi6.1.1.7. 2681.
ReactomeiREACT_15302. Mitochondrial tRNA aminoacylation.

Miscellaneous databases

GeneWikiiAARS2.
GenomeRNAii57505.
NextBioi63841.
PROiQ5JTZ9.
SOURCEiSearch...

Gene expression databases

BgeeiQ5JTZ9.
CleanExiHS_AARS2.
GenevestigatoriQ5JTZ9.

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]
ProtoNetiSearch...

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].
  7. "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome."
    Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., Ye M., Zou H.
    J. Proteomics 96:253-262(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  8. Cited for: INVOLVEMENT IN LKENP, VARIANTS LKENP CYS-50; LYS-405 AND ARG-965, VARIANTS VAL-77; PHE-131 DEL; CYS-199 AND MET-730, CHARACTERIZATION OF VARIANT LKENP CYS-50.

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: April 29, 2015
This is version 97 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

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 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.