MARS1

Protein identityUniProt · HPA

UniProt accession

P56192

Gene

MARS1

Ensembl

ENSG00000166986

Chromosome

12

Canonical length

900 aa

Protein class

Disease related genes, Enzymes, Human disease related genes, Metabolic proteins, Potential drug targets, Predicted intracellular proteins, Predicted membrane proteins

Subcellular location

Cytosol,Mid piece,Principal piece,End piece

OverviewNCBI Gene

This gene encodes a member of the class I family of aminoacyl-tRNA synthetases. These enzymes play a critical role in protein biosynthesis by charging tRNAs with their cognate amino acids. The encoded protein is a component of the multi-tRNA synthetase complex and catalyzes the ligation of methionine to tRNA molecules. [provided by RefSeq, Jan 2011]

Canonical amino-acid sequenceUniProt

900 residues, UniProt reviewed canonical sequence.

>P56192|MARS1
     1  MRLFVSDGVP GCLPVLAAAG RARGRAEVLI STVGPEDCVV PFLTRPKVPV LQLDSGNYLF
    61  STSAICRYFF LLSGWEQDDL TNQWLEWEAT ELQPALSAAL YYLVVQGKKG EDVLGSVRRA
   121  LTHIDHSLSR QNCPFLAGET ESLADIVLWG ALYPLLQDPA YLPEELSALH SWFQTLSTQE
   181  PCQRAAETVL KQQGVLALRP YLQKQPQPSP AEGRAVTNEP EEEELATLSE EEIAMAVTAW
   241  EKGLESLPPL RPQQNPVLPV AGERNVLITS ALPYVNNVPH LGNIIGCVLS ADVFARYSRL
   301  RQWNTLYLCG TDEYGTATET KALEEGLTPQ EICDKYHIIH ADIYRWFNIS FDIFGRTTTP
   361  QQTKITQDIF QQLLKRGFVL QDTVEQLRCE HCARFLADRF VEGVCPFCGY EEARGDQCDK
   421  CGKLINAVEL KKPQCKVCRS CPVVQSSQHL FLDLPKLEKR LEEWLGRTLP GSDWTPNAQF
   481  ITRSWLRDGL KPRCITRDLK WGTPVPLEGF EDKVFYVWFD ATIGYLSITA NYTDQWERWW
   541  KNPEQVDLYQ FMAKDNVPFH SLVFPCSALG AEDNYTLVSH LIATEYLNYE DGKFSKSRGV
   601  GVFGDMAQDT GIPADIWRFY LLYIRPEGQD SAFSWTDLLL KNNSELLNNL GNFINRAGMF
   661  VSKFFGGYVP EMVLTPDDQR LLAHVTLELQ HYHQLLEKVR IRDALRSILT ISRHGNQYIQ
   721  VNEPWKRIKG SEADRQRAGT VTGLAVNIAA LLSVMLQPYM PTVSATIQAQ LQLPPPACSI
   781  LLTNFLCTLP AGHQIGTVSP LFQKLENDQI ESLRQRFGGG QAKTSPKPAV VETVTTAKPQ
   841  QIQALMDEVT KQGNIVRELK AQKADKNEVA AEVAKLLDLK KQLAVAEGKP PEAPKGKKKK

LocalizationUniProt · AlphaFold · HPA

Whether an antibody against MARS1 can act on the native protein depends on physical access: surface and secreted proteins are reachable by circulating antibodies, intracellular proteins usually are not.

Antibody reachability

Intracellular

Secreted

No

Transmembrane segments

0

Mean surface accessibility (rSASA)

0.26

Highest tissue expression

65 nTPM

Expression across tissuesHPA

DiseaseUniProt · ClinVar · IEDB · PubMed

Four sources answering four different questions about MARS1.

Disease | AllUniProt

Conditions MARS1 is implicated in, by any mechanism.

• Interstitial lung and liver disease (ILLD) MIM:615486
• Charcot-Marie-Tooth disease, axonal, type 2U (CMT2U) MIM:616280
• Trichothiodystrophy 9, non-photosensitive (TTD9) MIM:619692
• Spastic paraplegia 70, autosomal recessive (SPG70) MIM:620323

Disease | GeneticClinVar

8 pathogenic / likely-pathogenic of 950 ClinVar records.

Conditions with pathogenic or likely-pathogenic variants.

• Severe early-onset pulmonary alveolar proteinosis due to MARS deficiency
• Autosomal recessive spastic paraplegia type 70
• Pulmonary alveolar proteinosis
• Charcot-Marie-Tooth disease axonal type 2U
• Germ cell tumor of testis

Genetic constraint and essentialitygnomAD · DepMap

Does the body need this protein intact? Low LOEUF or a strong DepMap dependency means loss or blockade of the protein is likely to be felt.

gnomAD LOEUF (loss-of-function intolerance)

0.78

gnomAD pLI

0

DepMap mean gene effect

-1.69

DepMap dependency class

pan

Cancer expressionTCGA

Across TCGA tumor cohorts, this protein is over-expressed in roughly 8% of surveyed tumor types (aggregate summary; per-cohort expression, alteration, and survival load in the interactive view).

OntologyGO

Biological processes

• cellular response to epidermal growth factor stimulus
• cellular response to platelet-derived growth factor stimulus
• methionyl-tRNA aminoacylation
• positive regulation of transcription of nucleolar large rRNA by RNA polymerase I
• rRNA transcription
• tRNA aminoacylation for protein translation

Molecular functions

• ATP binding
• methionine-tRNA ligase activity
• tRNA binding

Cellular components

• aminoacyl-tRNA synthetase multienzyme complex
• cytoplasm
• cytosol
• extracellular exosome
• membrane
• nucleolus
• sperm end piece
• sperm midpiece
• sperm principal piece

Protein domainsUniProt · Pfam · InterPro

• WHEP-TRS domain
• Aminoacyl-tRNA synthetase, class I, conserved site
• Glutathione S-transferase, C-terminal
• uS15/NS1, RNA-binding domain superfamily
• Aminoacyl-tRNA synthetase, class Ia, anticodon-binding
• Glutathione S-transferase, C-terminal-like
• Rossmann-like alpha/beta/alpha sandwich fold
• Methionyl-tRNA synthetase
• Methionyl/Leucyl tRNA synthetase
• Methioninyl-tRNA synthetase core domain
• Glutathione S-transferase, C-terminal domain superfamily
• Methionyl-tRNA synthetase, anticodon-binding domain
• Glutathione S-transferase, C-terminal domain
• WHEP-TRS domain
• tRNA synthetases class I (M)
• Anticodon binding domain of methionyl tRNA ligase
• Methionine-tRNA ligase, type 1
• Methionyl-tRNA synthetase, Zn-domain
• Methionine--tRNA ligase, N-terminal
• Glutathione S-transferase, N-terminal domain

KeywordsUniProt

• Aminoacyl-tRNA synthetase
• ATP-binding
• Charcot-Marie-Tooth disease
• Cytoplasm
• Hereditary spastic paraplegia
• Ligase
• Neurodegeneration
• Neuropathy
• Nucleotide-binding
• Nucleus
• Phosphoprotein
• Protein biosynthesis
• RNA-binding
• tRNA-binding

InteractionsUniProt · HPA

Protein binding partners of MARS1 in the human serome: UniProt-annotated complex subunits plus reported interactors. Each links to its own Seroatlas record.

• IARS1
• LARS1
• MYC
• QARS1