Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Serine--tRNA ligase, cytoplasmic

Gene

Sars

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: -Experimental evidence at protein leveli

Functioni

Catalyzes the attachment of serine to tRNA(Ser) in a two-step reaction: serine is first activated by ATP to form Ser-AMP and then transferred to the acceptor end of tRNA(Ser). Is probably also able to aminoacylate tRNA(Sec) with serine, to form the misacylated tRNA L-seryl-tRNA(Sec), which will be further converted into selenocysteinyl-tRNA(Sec). In the nucleus, binds to the VEGFA core promoter and prevents MYC binding and transcriptional activation by MYC. Recruits SIRT2 to the VEGFA promoter, promoting deacetylation of histone H4 at 'Lys-16' (H4K16). Thereby, inhibits the production of VEGFA and sprouting angiogenesis mediated by VEGFA.By similarity

Catalytic activityi

ATP + L-serine + tRNA(Ser) = AMP + diphosphate + L-seryl-tRNA(Ser).By similarity
ATP + L-serine + tRNA(Sec) = AMP + diphosphate + L-seryl-tRNA(Sec).By similarity

Pathwayi: selenocysteinyl-tRNA(Sec) biosynthesis

This protein is involved in step 1 of the subpathway that synthesizes L-seryl-tRNA(Sec) from L-serine and tRNA(Sec).
Proteins known to be involved in this subpathway in this organism are:
  1. Serine--tRNA ligase, mitochondrial (Sars2), Serine--tRNA ligase, cytoplasmic (Sars)
This subpathway is part of the pathway selenocysteinyl-tRNA(Sec) biosynthesis, which is itself part of Aminoacyl-tRNA biosynthesis.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes L-seryl-tRNA(Sec) from L-serine and tRNA(Sec), the pathway selenocysteinyl-tRNA(Sec) biosynthesis and in Aminoacyl-tRNA biosynthesis.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Binding sitei271L-serineBy similarity1
Binding sitei302L-serineBy similarity1
Binding sitei325L-serineBy similarity1
Binding sitei427L-serineBy similarity1
Binding sitei429Important for serine bindingBy similarity1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi302 – 304ATPBy similarity3
Nucleotide bindingi318 – 321ATPBy similarity4
Nucleotide bindingi391 – 394ATPBy similarity4

GO - Molecular functioni

GO - Biological processi

Keywordsi

Molecular functionAminoacyl-tRNA synthetase, DNA-binding, Ligase
Biological processProtein biosynthesis
LigandATP-binding, Nucleotide-binding

Enzyme and pathway databases

UniPathwayiUPA00906; UER00895

Names & Taxonomyi

Protein namesi
Recommended name:
Serine--tRNA ligase, cytoplasmic (EC:6.1.1.11By similarity)
Alternative name(s):
Seryl-tRNA synthetase
Short name:
SerRS
Seryl-tRNA(Ser/Sec) synthetase
Gene namesi
Name:Sars
Synonyms:Sars1, Sers
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaMyomorphaMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 3

Organism-specific databases

MGIiMGI:102809 Sars

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Keywords - Cellular componenti

Cytoplasm, Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001221921 – 512Serine--tRNA ligase, cytoplasmicAdd BLAST512

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei1N-acetylmethionineBy similarity1
Modified residuei241PhosphoserineBy similarity1
Modified residuei323N6-acetyllysineBy similarity1
Modified residuei506PhosphoserineCombined sources1

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

EPDiP26638
MaxQBiP26638
PaxDbiP26638
PeptideAtlasiP26638
PRIDEiP26638

2D gel databases

REPRODUCTION-2DPAGEiP26638

PTM databases

iPTMnetiP26638
PhosphoSitePlusiP26638
SwissPalmiP26638

Expressioni

Gene expression databases

BgeeiENSMUSG00000068739
CleanExiMM_SARS
ExpressionAtlasiP26638 baseline and differential
GenevisibleiP26638 MM

Interactioni

Subunit structurei

Homodimer. The tRNA molecule may bind across the dimer. Interacts with SIRT2.By similarity

GO - Molecular functioni

Protein-protein interaction databases

BioGridi203074, 9 interactors
IntActiP26638, 9 interactors
MINTiP26638
STRINGi10090.ENSMUSP00000099685

Structurei

3D structure databases

ProteinModelPortaliP26638
SMRiP26638
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni9 – 61Interaction with tRNABy similarityAdd BLAST53

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Motifi482 – 494Nuclear localization signalBy similarityAdd BLAST13

Domaini

Consists of two distinct domains, a catalytic core and a N-terminal extension that is involved in tRNA binding.By similarity

Sequence similaritiesi

Phylogenomic databases

eggNOGiKOG2509 Eukaryota
COG0172 LUCA
GeneTreeiENSGT00790000123098
HOGENOMiHOG000035937
HOVERGENiHBG023172
InParanoidiP26638
KOiK01875

Family and domain databases

CDDicd00770 SerRS_core, 1 hit
InterProiView protein in InterPro
IPR002314 aa-tRNA-synt_IIb
IPR006195 aa-tRNA-synth_II
IPR002317 Ser-tRNA-ligase_type_1
IPR015866 Ser-tRNA-synth_1_N
IPR033729 SerRS_core
IPR010978 tRNA-bd_arm
PANTHERiPTHR11778 PTHR11778, 1 hit
PfamiView protein in Pfam
PF02403 Seryl_tRNA_N, 1 hit
PF00587 tRNA-synt_2b, 1 hit
PIRSFiPIRSF001529 Ser-tRNA-synth_IIa, 1 hit
PRINTSiPR00981 TRNASYNTHSER
SUPFAMiSSF46589 SSF46589, 2 hits
TIGRFAMsiTIGR00414 serS, 1 hit
PROSITEiView protein in PROSITE
PS50862 AA_TRNA_LIGASE_II, 1 hit

Sequencei

Sequence statusi: Complete.

P26638-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MVLDLDLFRV DKGGDPALIR ETQEKRFKDP GLVDQLVKAD SEWRRCRFRA
60 70 80 90 100
DNLNKLKNLC SKTIGEKMKK KEAVGDDESV PENVLNFDDL TADALAALKV
110 120 130 140 150
SQIKKVRLLI DEAIQKCDGE RVKLEAERFE NLREIGNLLH PSVPISNDED
160 170 180 190 200
ADNKVERIWG DCTVRKKYSH VDLVVMVDGF EGEKGAVVAG SRGYFLKGPL
210 220 230 240 250
VFLEQALIQY ALRTLGSRGY TPIYTPFFMR KEVMQEVAQL SQFDEELYKV
260 270 280 290 300
IGKGSEKSDD NSYDEKYLIA TSEQPIAALH RDEWLRPEDL PIKYAGLSTC
310 320 330 340 350
FRQEVGSHGR DTRGIFRVHQ FEKIEQFVYS SPHDNKSWEM FDEMIATAEE
360 370 380 390 400
FYQSLGIPYH IVNIVSGSLN HAASKKLDLE AWFPGSGAFR ELVSCSNCTD
410 420 430 440 450
YQARRLRIRY GQTKKMMDKV EFVHMLNATM CATTRTICAI LENYQAEKGI
460 470 480 490 500
AVPEKLREFM PPGLQELIPF VKPAPIDQEP SKKQKKQHEG SKKKAKEVPL
510
ENQLQSMEVT EA
Length:512
Mass (Da):58,389
Last modified:January 23, 2007 - v3
Checksum:i7EF2C68DB20C6FA0
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti96A → R in AAA40108 (PubMed:1918033).Curated1
Sequence conflicti192 – 199RGYFLKGP → PGVLPEGA in AAA40108 (PubMed:1918033).Curated8
Sequence conflicti283E → A in AAA40108 (PubMed:1918033).Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK075827 mRNA Translation: BAC35990.1
AL672200 Genomic DNA No translation available.
BC008612 mRNA Translation: AAH08612.1
M74012 mRNA Translation: AAA40108.1
CCDSiCCDS57254.1
RefSeqiNP_001191908.1, NM_001204979.1
UniGeneiMm.28688

Genome annotation databases

EnsembliENSMUST00000090553; ENSMUSP00000088041; ENSMUSG00000068739
GeneIDi20226
KEGGimmu:20226
UCSCiuc008qzb.2 mouse

Similar proteinsi

Entry informationi

Entry nameiSYSC_MOUSE
AccessioniPrimary (citable) accession number: P26638
Secondary accession number(s): A2AFR8
Entry historyiIntegrated into UniProtKB/Swiss-Prot: August 1, 1992
Last sequence update: January 23, 2007
Last modified: March 28, 2018
This is version 151 of the entry and version 3 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome
UniProt is an ELIXIR core data resource
Main funding by: National Institutes of Health