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P49588

- SYAC_HUMAN

UniProt

P49588 - SYAC_HUMAN

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Protein
Alanine--tRNA ligase, cytoplasmic
Gene
AARS
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 bindingi605 – 6051Zinc Reviewed prediction
Metal bindingi609 – 6091Zinc Reviewed prediction
Metal bindingi723 – 7231Zinc Reviewed prediction
Metal bindingi727 – 7271Zinc Reviewed prediction

GO - Molecular functioni

  1. ATP binding Source: UniProtKB-KW
  2. alanine-tRNA ligase activity Source: UniProtKB-EC
  3. amino acid binding Source: Ensembl
  4. aminoacyl-tRNA editing activity Source: Ensembl
  5. metal ion binding Source: UniProtKB-KW
  6. tRNA binding Source: ProtInc
Complete GO annotation...

GO - Biological processi

  1. alanyl-tRNA aminoacylation Source: ProtInc
  2. cell death Source: UniProtKB-KW
  3. cerebellar Purkinje cell layer development Source: Ensembl
  4. endoplasmic reticulum unfolded protein response Source: Ensembl
  5. gene expression Source: Reactome
  6. hair follicle development Source: Ensembl
  7. negative regulation of neuron apoptotic process Source: Ensembl
  8. neuromuscular process controlling balance Source: Ensembl
  9. protein folding Source: Ensembl
  10. response to amino acid Source: Ensembl
  11. tRNA aminoacylation for protein translation Source: Reactome
  12. tRNA modification Source: Ensembl
  13. tRNA processing Source: ProtInc
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_15306. Cytosolic tRNA aminoacylation.

Names & Taxonomyi

Protein namesi
Recommended name:
Alanine--tRNA ligase, cytoplasmic (EC:6.1.1.7)
Alternative name(s):
Alanyl-tRNA synthetase
Short name:
AlaRS
Renal carcinoma antigen NY-REN-42
Gene namesi
Name:AARS
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 16

Organism-specific databases

HGNCiHGNC:20. AARS.

Subcellular locationi

Cytoplasm By similarity UniRule annotation

GO - Cellular componenti

  1. cytoplasm Source: HPA
  2. cytosol Source: Reactome
  3. extracellular vesicular exosome Source: UniProt
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Involvement in diseasei

Charcot-Marie-Tooth disease 2N (CMT2N) [MIM:613287]: An axonal form of Charcot-Marie-Tooth disease, a disorder of the peripheral nervous system, characterized by progressive weakness and atrophy, initially of the peroneal muscles and later of the distal muscles of the arms. Charcot-Marie-Tooth disease is classified in two main groups on the basis of electrophysiologic properties and histopathology: primary peripheral demyelinating neuropathies (designated CMT1 when they are dominantly inherited) and primary peripheral axonal neuropathies (CMT2). Neuropathies of the CMT2 group are characterized by signs of axonal degeneration in the absence of obvious myelin alterations, normal or slightly reduced nerve conduction velocities, and progressive distal muscle weakness and atrophy. Nerve conduction velocities are normal or slightly reduced.
Note: The disease is caused by mutations affecting the gene represented in this entry.3 Publications
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti71 – 711N → Y in CMT2N. 1 Publication
VAR_067084
Natural varianti329 – 3291R → H in CMT2N; severely reduces enzyme activity. 2 Publications
VAR_063527

Keywords - Diseasei

Charcot-Marie-Tooth disease, Disease mutation, Neurodegeneration, Neuropathy

Organism-specific databases

MIMi613287. phenotype.
Orphaneti228174. Autosomal dominant Charcot-Marie-Tooth disease type 2N.
PharmGKBiPA24367.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 968968Alanine--tRNA ligase, cytoplasmicUniRule annotation
PRO_0000075281Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei1 – 11N-acetylmethionine4 Publications
Modified residuei19 – 191N6-acetyllysine1 Publication
Modified residuei399 – 3991Phosphoserine1 Publication
Modified residuei555 – 5551Phosphoserine1 Publication
Modified residuei876 – 8761N6-acetyllysine1 Publication

Post-translational modificationi

ISGylated.1 Publication

Keywords - PTMi

Acetylation, Phosphoprotein, Ubl conjugation

Proteomic databases

MaxQBiP49588.
PaxDbiP49588.
PRIDEiP49588.

PTM databases

PhosphoSiteiP49588.

Expressioni

Gene expression databases

BgeeiP49588.
CleanExiHS_AARS.
GenevestigatoriP49588.

Organism-specific databases

HPAiCAB034261.
HPA040870.
HPA044223.

Interactioni

Subunit structurei

Monomer.

Protein-protein interaction databases

BioGridi106534. 42 interactions.
IntActiP49588. 4 interactions.
MINTiMINT-1490092.
STRINGi9606.ENSP00000261772.

Structurei

3D structure databases

ProteinModelPortaliP49588.
SMRiP49588. Positions 6-757.

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.1 Publication
The C-terminal C-Ala domain (residues 756 to 968), along with tRNA(Ala), serves as a bridge to cooperatively bring together the editing and aminoacylation centers thus stimulating deacylation of misacylated tRNAs. The human domain can be used in vitro to replace the corresponding domain in E.coli.1 Publication

Sequence similaritiesi

Phylogenomic databases

eggNOGiCOG0013.
HOGENOMiHOG000156964.
HOVERGENiHBG017874.
InParanoidiP49588.
KOiK01872.
OMAiYFEGDAK.
OrthoDBiEOG7M3HZH.
PhylomeDBiP49588.
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.

P49588-1 [UniParc]FASTAAdd to Basket

« Hide

MDSTLTASEI RQRFIDFFKR NEHTYVHSSA TIPLDDPTLL FANAGMNQFK    50
PIFLNTIDPS HPMAKLSRAA NTQKCIRAGG KHNDLDDVGK DVYHHTFFEM 100
LGSWSFGDYF KELACKMALE LLTQEFGIPI ERLYVTYFGG DEAAGLEADL 150
ECKQIWQNLG LDDTKILPGN MKDNFWEMGD TGPCGPCSEI HYDRIGGRDA 200
AHLVNQDDPN VLEIWNLVFI QYNREADGIL KPLPKKSIDT GMGLERLVSV 250
LQNKMSNYDT DLFVPYFEAI QKGTGARPYT GKVGAEDADG IDMAYRVLAD 300
HARTITVALA DGGRPDNTGR GYVLRRILRR AVRYAHEKLN ASRGFFATLV 350
DVVVQSLGDA FPELKKDPDM VKDIINEEEV QFLKTLSRGR RILDRKIQSL 400
GDSKTIPGDT AWLLYDTYGF PVDLTGLIAE EKGLVVDMDG FEEERKLAQL 450
KSQGKGAGGE DLIMLDIYAI EELRARGLEV TDDSPKYNYH LDSSGSYVFE 500
NTVATVMALR REKMFVEEVS TGQECGVVLD KTCFYAEQGG QIYDEGYLVK 550
VDDSSEDKTE FTVKNAQVRG GYVLHIGTIY GDLKVGDQVW LFIDEPRRRP 600
IMSNHTATHI LNFALRSVLG EADQKGSLVA PDRLRFDFTA KGAMSTQQIK 650
KAEEIANEMI EAAKAVYTQD CPLAAAKAIQ GLRAVFDETY PDPVRVVSIG 700
VPVSELLDDP SGPAGSLTSV EFCGGTHLRN SSHAGAFVIV TEEAIAKGIR 750
RIVAVTGAEA QKALRKAESL KKCLSVMEAK VKAQTAPNKD VQREIADLGE 800
ALATAVIPQW QKDELRETLK SLKKVMDDLD RASKADVQKR VLEKTKQFID 850
SNPNQPLVIL EMESGASAKA LNEALKLFKM HSPQTSAMLF TVDNEAGKIT 900
CLCQVPQNAA NRGLKASEWV QQVSGLMDGK GGGKDVSAQA TGKNVGCLQE 950
ALQLATSFAQ LRLGDVKN 968
Length:968
Mass (Da):106,810
Last modified:October 3, 2006 - v2
Checksum:i8683F111CEE42506
GO

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti71 – 711N → Y in CMT2N. 1 Publication
VAR_067084
Natural varianti275 – 2751G → D.
Corresponds to variant rs11537667 [ dbSNP | Ensembl ].
VAR_028204
Natural varianti329 – 3291R → H in CMT2N; severely reduces enzyme activity. 2 Publications
VAR_063527

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti82 – 821H → Q in BAA06808. 1 Publication
Sequence conflicti867 – 8671S → T in BAD96544. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
D32050 mRNA. Translation: BAA06808.1.
AK222824 mRNA. Translation: BAD96544.1.
AC012184 Genomic DNA. No translation available.
CH471241 Genomic DNA. Translation: EAW51839.1.
BC011451 mRNA. Translation: AAH11451.1.
CCDSiCCDS32474.1.
PIRiI60107.
RefSeqiNP_001596.2. NM_001605.2.
UniGeneiHs.315137.

Genome annotation databases

EnsembliENST00000261772; ENSP00000261772; ENSG00000090861.
GeneIDi16.
KEGGihsa:16.
UCSCiuc002eyn.1. human.

Polymorphism databases

DMDMi115502460.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
D32050 mRNA. Translation: BAA06808.1 .
AK222824 mRNA. Translation: BAD96544.1 .
AC012184 Genomic DNA. No translation available.
CH471241 Genomic DNA. Translation: EAW51839.1 .
BC011451 mRNA. Translation: AAH11451.1 .
CCDSi CCDS32474.1.
PIRi I60107.
RefSeqi NP_001596.2. NM_001605.2.
UniGenei Hs.315137.

3D structure databases

ProteinModelPortali P49588.
SMRi P49588. Positions 6-757.
ModBasei Search...

Protein-protein interaction databases

BioGridi 106534. 42 interactions.
IntActi P49588. 4 interactions.
MINTi MINT-1490092.
STRINGi 9606.ENSP00000261772.

Chemistry

BindingDBi P49588.
ChEMBLi CHEMBL3574.
DrugBanki DB00160. L-Alanine.

PTM databases

PhosphoSitei P49588.

Polymorphism databases

DMDMi 115502460.

Proteomic databases

MaxQBi P49588.
PaxDbi P49588.
PRIDEi P49588.

Protocols and materials databases

DNASUi 16.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000261772 ; ENSP00000261772 ; ENSG00000090861 .
GeneIDi 16.
KEGGi hsa:16.
UCSCi uc002eyn.1. human.

Organism-specific databases

CTDi 16.
GeneCardsi GC16M070286.
GeneReviewsi AARS.
HGNCi HGNC:20. AARS.
HPAi CAB034261.
HPA040870.
HPA044223.
MIMi 601065. gene.
613287. phenotype.
neXtProti NX_P49588.
Orphaneti 228174. Autosomal dominant Charcot-Marie-Tooth disease type 2N.
PharmGKBi PA24367.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG0013.
HOGENOMi HOG000156964.
HOVERGENi HBG017874.
InParanoidi P49588.
KOi K01872.
OMAi YFEGDAK.
OrthoDBi EOG7M3HZH.
PhylomeDBi P49588.
TreeFami TF300737.

Enzyme and pathway databases

Reactomei REACT_15306. Cytosolic tRNA aminoacylation.

Miscellaneous databases

ChiTaRSi AARS. human.
GenomeRNAii 16.
NextBioi 39.
PROi P49588.
SOURCEi Search...

Gene expression databases

Bgeei P49588.
CleanExi HS_AARS.
Genevestigatori P49588.

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.
IPR003156. DHHA1_dom.
IPR018163. Thr/Ala-tRNA-synth_IIc_edit.
IPR009000. Transl_B-barrel.
IPR012947. tRNA_SAD.
[Graphical view ]
Pfami PF02272. DHHA1. 1 hit.
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. "Human alanyl-tRNA synthetase: conservation in evolution of catalytic core and microhelix recognition."
    Shiba K., Ripmaster T.L., Suzuki N., Nichols R., Plotz P., Noda T., Schimmel P.
    Biochemistry 34:10340-10349(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  2. Suzuki Y., Sugano S., Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S.
    Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Liver.
  3. "The sequence and analysis of duplication-rich human chromosome 16."
    Martin J., Han C., Gordon L.A., Terry A., Prabhakar S., She X., Xie G., Hellsten U., Chan Y.M., Altherr M., Couronne O., Aerts A., Bajorek E., Black S., Blumer H., Branscomb E., Brown N.C., Bruno W.J.
    , Buckingham J.M., Callen D.F., Campbell C.S., Campbell M.L., Campbell E.W., Caoile C., Challacombe J.F., Chasteen L.A., Chertkov O., Chi H.C., Christensen M., Clark L.M., Cohn J.D., Denys M., Detter J.C., Dickson M., Dimitrijevic-Bussod M., Escobar J., Fawcett J.J., Flowers D., Fotopulos D., Glavina T., Gomez M., Gonzales E., Goodstein D., Goodwin L.A., Grady D.L., Grigoriev I., Groza M., Hammon N., Hawkins T., Haydu L., Hildebrand C.E., Huang W., Israni S., Jett J., Jewett P.B., Kadner K., Kimball H., Kobayashi A., Krawczyk M.-C., Leyba T., Longmire J.L., Lopez F., Lou Y., Lowry S., Ludeman T., Manohar C.F., Mark G.A., McMurray K.L., Meincke L.J., Morgan J., Moyzis R.K., Mundt M.O., Munk A.C., Nandkeshwar R.D., Pitluck S., Pollard M., Predki P., Parson-Quintana B., Ramirez L., Rash S., Retterer J., Ricke D.O., Robinson D.L., Rodriguez A., Salamov A., Saunders E.H., Scott D., Shough T., Stallings R.L., Stalvey M., Sutherland R.D., Tapia R., Tesmer J.G., Thayer N., Thompson L.S., Tice H., Torney D.C., Tran-Gyamfi M., Tsai M., Ulanovsky L.E., Ustaszewska A., Vo N., White P.S., Williams A.L., Wills P.L., Wu J.-R., Wu K., Yang J., DeJong P., Bruce D., Doggett N.A., Deaven L., Schmutz J., Grimwood J., Richardson P., Rokhsar D.S., Eichler E.E., Gilna P., Lucas S.M., Myers R.M., Rubin E.M., Pennacchio L.A.
    Nature 432:988-994(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  5. "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].
    Tissue: Placenta.
  6. Bienvenut W.V., Glen H., Brunton V.G., Frame M.C.
    Submitted (JUL-2007) to UniProtKB
    Cited for: PROTEIN SEQUENCE OF 1-11; 304-320 AND 684-695, ACETYLATION AT MET-1, IDENTIFICATION BY MASS SPECTROMETRY.
    Tissue: Osteosarcoma.
  7. Cited for: IDENTIFICATION AS A RENAL CANCER ANTIGEN.
    Tissue: Renal cell carcinoma.
  8. Cited for: ISGYLATION.
  9. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-555, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  10. "Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
    Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
    Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  11. "The C-Ala domain brings together editing and aminoacylation functions on one tRNA."
    Guo M., Chong Y.E., Beebe K., Shapiro R., Yang X.-L., Schimmel P.
    Science 325:744-747(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: DOMAIN EXCHANGE EXPERIMENTS.
  12. "Lysine acetylation targets protein complexes and co-regulates major cellular functions."
    Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M.
    Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-19 AND LYS-876, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  13. "Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
    Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
    Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-399, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  14. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  15. "Comparative large-scale characterisation of plant vs. mammal proteins reveals similar and idiosyncratic N-alpha acetylation features."
    Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T., Giglione C.
    Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  16. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  17. "A major determinant for binding and aminoacylation of tRNA(Ala) in cytoplasmic Alanyl-tRNA synthetase is mutated in dominant axonal Charcot-Marie-Tooth disease."
    Latour P., Thauvin-Robinet C., Baudelet-Mery C., Soichot P., Cusin V., Faivre L., Locatelli M.C., Mayencon M., Sarcey A., Broussolle E., Camu W., David A., Rousson R.
    Am. J. Hum. Genet. 86:77-82(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANT CMT2N HIS-329.
  18. "The mutational spectrum in a cohort of Charcot-Marie-Tooth disease type 2 among the Han Chinese in Taiwan."
    Lin K.P., Soong B.W., Yang C.C., Huang L.W., Chang M.H., Lee I.H., Antonellis A., Lee Y.C.
    PLoS ONE 6:E29393-E29393(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANT CMT2N TYR-71.
  19. "A recurrent loss-of-function alanyl-tRNA synthetase (AARS) mutation in patients with Charcot-Marie-Tooth disease type 2N (CMT2N)."
    McLaughlin H.M., Sakaguchi R., Giblin W., Wilson T.E., Biesecker L., Lupski J.R., Talbot K., Vance J.M., Zuchner S., Lee Y.C., Kennerson M., Hou Y.M., Nicholson G., Antonellis A.
    Hum. Mutat. 33:244-253(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANT CMT2N HIS-329, CHARACTERIZATION OF VARIANT CMT2N HIS-329.

Entry informationi

Entry nameiSYAC_HUMAN
AccessioniPrimary (citable) accession number: P49588
Secondary accession number(s): A6NF14, Q53GV7, Q96FA0
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 1996
Last sequence update: October 3, 2006
Last modified: September 3, 2014
This is version 135 of the entry and version 2 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, Direct protein sequencing, Reference proteome

Documents

  1. Aminoacyl-tRNA synthetases
    List of aminoacyl-tRNA synthetase entries
  2. Human chromosome 16
    Human chromosome 16: 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