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Reviewed, UniProtKB/Swiss-Prot P56192 (SYMC_HUMAN)

Last modified July 7, 2009. Version 94. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (7) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Binary interactions · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    Methionyl-tRNA synthetase, cytoplasmic
    EC=6.1.1.10
Alternative name(s):
    Methionine--tRNA ligase
      Short name=MetRS
Gene names
Name: MARS
OrganismHomo sapiens (Human) [Complete proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length900 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceEvidence at protein level.

General annotation (Comments)

Catalytic activity

ATP + L-methionine + tRNA(Met) = AMP + diphosphate + L-methionyl-tRNA(Met).

Subunit structure

Component of the multisynthetase complex which is comprised of a bifunctional glutamyl-prolyl-tRNA synthetase, the monospecific isoleucyl, leucyl, glutaminyl, methionyl, lysyl, arginyl, and aspartyl-tRNA synthetases as well as three auxiliary proteins, p18, p48 and p43.

Subcellular location

Cytoplasm Probable.

Sequence similarities

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

Contains 1 GST C-terminal domain.

Contains 1 WHEP-TRS domain.

Ontologies

Keywords
   Biological processProtein biosynthesis
   Cellular componentCytoplasm
   Coding sequence diversityPolymorphism
   LigandATP-binding
Nucleotide-binding
RNA-binding
tRNA-binding
   Molecular functionAminoacyl-tRNA synthetase
Ligase
   Technical term3D-structure
Complete proteome
Gene Ontology (GO)
   Biological processmethionyl-tRNA aminoacylation

Inferred from electronic annotation. Source: InterPro

   Cellular componentcytoplasm

Inferred from direct assay. Source: HPA

plasma membrane

Inferred from direct assay. Source: HPA

   Molecular functionATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

methionine-tRNA ligase activity Ref.1

Traceable author statement. Source: ProtInc

protein binding

Inferred from physical interaction. Source: IntAct

tRNA binding

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 900900Methionyl-tRNA synthetase, cytoplasmic
PRO_0000139262

Regions

Domain74 – 198125GST C-terminal
Domain841 – 89757WHEP-TRS
Motif273 – 28311"HIGH" region
Motif593 – 5975"KMSKS" region

Sites

Binding site5961ATP By similarity

Natural variations

Natural variant6831A → D: dbSNP rs1054403.
VAR_020459

Experimental info

Sequence conflict531L → V in CAA64381. Ref.1
Sequence conflict991A → P in CAA64381. Ref.1
Sequence conflict1521L → Q in CAA64381. Ref.1
Sequence conflict1721W → S in AAH15011. Ref.5
Sequence conflict2501L → P in BAD96487. Ref.4
Sequence conflict6831A → G in CAA64381. Ref.1
Sequence conflict6831A → G in CAA89153. Ref.1

Secondary structure

......... 900
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P56192-1 [UniParc].

Last modified April 16, 2002. Version 2.
Checksum: 3D687C77E17C5C96

FASTA900101,116
        10         20         30         40         50         60 
MRLFVSDGVP GCLPVLAAAG RARGRAEVLI STVGPEDCVV PFLTRPKVPV LQLDSGNYLF 

        70         80         90        100        110        120 
STSAICRYFF LLSGWEQDDL TNQWLEWEAT ELQPALSAAL YYLVVQGKKG EDVLGSVRRA 

       130        140        150        160        170        180 
LTHIDHSLSR QNCPFLAGET ESLADIVLWG ALYPLLQDPA YLPEELSALH SWFQTLSTQE 

       190        200        210        220        230        240 
PCQRAAETVL KQQGVLALRP YLQKQPQPSP AEGRAVTNEP EEEELATLSE EEIAMAVTAW 

       250        260        270        280        290        300 
EKGLESLPPL RPQQNPVLPV AGERNVLITS ALPYVNNVPH LGNIIGCVLS ADVFARYSRL 

       310        320        330        340        350        360 
RQWNTLYLCG TDEYGTATET KALEEGLTPQ EICDKYHIIH ADIYRWFNIS FDIFGRTTTP 

       370        380        390        400        410        420 
QQTKITQDIF QQLLKRGFVL QDTVEQLRCE HCARFLADRF VEGVCPFCGY EEARGDQCDK 

       430        440        450        460        470        480 
CGKLINAVEL KKPQCKVCRS CPVVQSSQHL FLDLPKLEKR LEEWLGRTLP GSDWTPNAQF 

       490        500        510        520        530        540 
ITRSWLRDGL KPRCITRDLK WGTPVPLEGF EDKVFYVWFD ATIGYLSITA NYTDQWERWW 

       550        560        570        580        590        600 
KNPEQVDLYQ FMAKDNVPFH SLVFPCSALG AEDNYTLVSH LIATEYLNYE DGKFSKSRGV 

       610        620        630        640        650        660 
GVFGDMAQDT GIPADIWRFY LLYIRPEGQD SAFSWTDLLL KNNSELLNNL GNFINRAGMF 

       670        680        690        700        710        720 
VSKFFGGYVP EMVLTPDDQR LLAHVTLELQ HYHQLLEKVR IRDALRSILT ISRHGNQYIQ 

       730        740        750        760        770        780 
VNEPWKRIKG SEADRQRAGT VTGLAVNIAA LLSVMLQPYM PTVSATIQAQ LQLPPPACSI 

       790        800        810        820        830        840 
LLTNFLCTLP AGHQIGTVSP LFQKLENDQI ESLRQRFGGG QAKTSPKPAV VETVTTAKPQ 

       850        860        870        880        890        900 
QIQALMDEVT KQGNIVRELK AQKADKNEVA AEVAKLLDLK KQLAVAEGKP PEAPKGKKKK 

« Hide

References

« Hide 'large scale' references
[1]"Cloning of a human cDNA encoding a protein with high homology to yeast methionyl-tRNA synthetase."
Lage H., Dietel M.
Gene 178:187-189(1996) [PubMed: 8921912] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Gastric carcinoma.
[2]"Cloning and sequence determination of a human cytoplasmic methionyl-tRNA synthetase gene."
Motegi H., Noda T., Shiba K.
Submitted (FEB-1996) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Brain.
[3]"Cloning of human full-length CDSs in BD Creator(TM) system donor vector."
Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., Phelan M., Farmer A.
Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[4]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.
[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: 15489334] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Brain, Colon and Muscle.
[6]Colinge J., Superti-Furga G., Bennett K.L.
Submitted (OCT-2008) to UniProtKB
Cited for: IDENTIFICATION [LARGE SCALE ANALYSIS], MASS SPECTROMETRY.
[7]"Solution structures of the WHEP-TRS domain of human methionyl-tRNA synthetase."
RIKEN structural genomics initiative (RSGI)
Submitted (OCT-2006) to the PDB data bank
Cited for: STRUCTURE BY NMR OF 835-900.
+Additional computationally mapped references.

Cross-references

Sequence databases

X94754 mRNA. Translation: CAA64381.1.
Z49216 mRNA. Translation: CAA89153.1.
D84224 mRNA. Translation: BAA95668.1.
BT007338 mRNA. Translation: AAP36002.1.
AK222767 mRNA. Translation: BAD96487.1.
BC002384 mRNA. Translation: AAH02384.1.
BC006328 mRNA. Translation: AAH06328.1.
BC011639 mRNA. Translation: AAH11639.1.
BC011849 mRNA. Translation: AAH11849.1.
BC015011 mRNA. Translation: AAH15011.1.
IPIIPI00008240.
PIRJC5224.
RefSeqNP_004981.2.
UniGeneHs.632707

3D structure databases

EntryMethodResolution (Å)ChainPositionsPDBsum
2DJVNMR-A835-900[»]
ModBaseSearch...

Protein-protein interaction databases

IntActP56192. 20 interactions.

PTM databases

PhosphoSiteP56192.

Proteomic databases

PeptideAtlasP56192.
PRIDEP56192.

Genome annotation databases

EnsemblENSG00000166986. Homo sapiens. [Contig view]
GeneID4141.
KEGGhsa:4141.
NMPDRfig|9606.3.peg.7802.
UCSCuc001sog.1. human.

Organism-specific databases

GeneCardsGC12P056167.
H-InvDBHIX0022196.
HGNCHGNC:6898. MARS.
HPACAB017097.
HPA004125.
MIM156560. gene.
PharmGKBPA30642.
GenAtlasSearch...

Phylogenomic databases

HOVERGENP56192.
OMAP56192. CEAVPES.

Enzyme and pathway databases

BRENDA6.1.1.10. 247.
ReactomeREACT_71. Gene Expression.

Gene expression databases

BgeeP56192.
CleanExHS_MARS.
GermOnlineENSG00000166986. Homo sapiens.

Family and domain databases

InterProIPR015413. aa-tRNA-synt_I.
IPR001412. aa-tRNA-synth_I_CS.
IPR010987. Glutathione-S-Trfase_C-like.
IPR017933. Glutathione_S_Trfase/Cl_chnl_C.
IPR004046. GST_C.
IPR002304. Met-tRNA-synth_Ia.
IPR014729. Rossmann-like_a/b/a_fold.
IPR009068. S15_NS1_RNA_bd.
IPR014758. tRNA-synt_met_N.
IPR000738. WHEP-TRS.
[Graphical view]
Gene3DG3DSA:1.20.1050.10. GST_C_like. 1 hit.
G3DSA:3.40.50.620. Rossmann-like_a/b/a_fold. 1 hit.
G3DSA:1.10.287.10. S15_NS1_RNA_bd. 1 hit.
PfamPF00043. GST_C. 1 hit.
PF09334. tRNA-synt_1g. 1 hit.
PF00458. WHEP-TRS. 1 hit.
[Graphical view]
PRINTSPR01041. TRNASYNTHMET.
TIGRFAMsTIGR00398. metG. 1 hit.
PROSITEPS00178. AA_TRNA_LIGASE_I. 1 hit.
PS50405. GST_CTER. 1 hit.
PS00762. WHEP_TRS_1. 1 hit.
PS51185. WHEP_TRS_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other Resources

DrugBankDB00134. L-Methionine.
NextBio16264.
SOURCESearch...

Entry information

Entry nameSYMC_HUMAN
AccessionPrimary (citable) accession number: P56192
Secondary accession number(s): Q14895 expand/collapse secondary AC list , Q53H14, Q96A15, Q96BZ0, Q9NSE0
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: April 16, 2002
Last modified: July 7, 2009
This is version 94 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHPI (Human Proteome Initiative)

Relevant documents

Aminoacyl-tRNA synthetases

List of aminoacyl-tRNA synthetase entries

Human chromosome 12

Human chromosome 12: entries, gene names and cross-references to MIM

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

MIM cross-references

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

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Binary interactions · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents