UniProtKB - Q6P799 (SYSC_RAT)
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Protein
Serine--tRNA ligase, cytoplasmic
Gene
Sars
Organism
Rattus norvegicus (Rat)
Status
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
: selenocysteinyl-tRNA(Sec) biosynthesis Pathwayi
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:
- Serine--tRNA ligase, cytoplasmic (Sars)
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 key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Binding sitei | 271 | L-serineBy similarity | 1 | |
Binding sitei | 302 | L-serineBy similarity | 1 | |
Binding sitei | 325 | L-serineBy similarity | 1 | |
Binding sitei | 427 | L-serineBy similarity | 1 | |
Binding sitei | 429 | Important for serine bindingBy similarity | 1 |
Regions
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Nucleotide bindingi | 302 – 304 | ATPBy similarity | 3 | |
Nucleotide bindingi | 318 – 321 | ATPBy similarity | 4 | |
Nucleotide bindingi | 391 – 394 | ATPBy similarity | 4 |
GO - Molecular functioni
- ATP binding Source: UniProtKB-KW
- core promoter sequence-specific DNA binding Source: UniProtKB
- protein homodimerization activity Source: RGD
- serine-tRNA ligase activity Source: UniProtKB
GO - Biological processi
- negative regulation of angiogenesis Source: UniProtKB
- negative regulation of transcription by RNA polymerase II Source: UniProtKB
- negative regulation of vascular endothelial growth factor production Source: UniProtKB
- selenocysteinyl-tRNA(Sec) biosynthetic process Source: UniProtKB-UniPathway
- seryl-tRNA aminoacylation Source: UniProtKB
Keywordsi
Molecular function | Aminoacyl-tRNA synthetase, DNA-binding, Ligase |
Biological process | Protein biosynthesis |
Ligand | ATP-binding, Nucleotide-binding |
Enzyme and pathway databases
UniPathwayi | UPA00906; 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 |
Organismi | Rattus norvegicus (Rat) |
Taxonomic identifieri | 10116 [NCBI] |
Taxonomic lineagei | Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Myomorpha › Muroidea › Muridae › Murinae › Rattus |
Proteomesi |
|
Organism-specific databases
RGDi | 628813. Sars. |
PTM / Processingi
Molecule processing
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
ChainiPRO_0000270765 | 1 – 512 | Serine--tRNA ligase, cytoplasmicAdd BLAST | 512 |
Amino acid modifications
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Modified residuei | 1 | N-acetylmethionineBy similarity | 1 | |
Modified residuei | 241 | PhosphoserineBy similarity | 1 | |
Modified residuei | 323 | N6-acetyllysineBy similarity | 1 |
Keywords - PTMi
Acetylation, PhosphoproteinProteomic databases
PaxDbi | Q6P799. |
PRIDEi | Q6P799. |
PTM databases
iPTMneti | Q6P799. |
PhosphoSitePlusi | Q6P799. |
Expressioni
Gene expression databases
Bgeei | ENSRNOG00000020255. |
ExpressionAtlasi | Q6P799. baseline and differential. |
Genevisiblei | Q6P799. RN. |
Interactioni
Subunit structurei
Homodimer. The tRNA molecule may bind across the dimer. Interacts with SIRT2.By similarity
GO - Molecular functioni
- protein homodimerization activity Source: RGD
Protein-protein interaction databases
IntActi | Q6P799. 1 interactor. |
STRINGi | 10116.ENSRNOP00000038448. |
Structurei
3D structure databases
ProteinModelPortali | Q6P799. |
SMRi | Q6P799. |
ModBasei | Search... |
MobiDBi | Search... |
Family & Domainsi
Region
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Regioni | 9 – 61 | Interaction with tRNABy similarityAdd BLAST | 53 |
Motif
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Motifi | 482 – 494 | Nuclear localization signalBy similarityAdd BLAST | 13 |
Domaini
Consists of two distinct domains, a catalytic core and a N-terminal extension that is involved in tRNA binding.By similarity
Sequence similaritiesi
Belongs to the class-II aminoacyl-tRNA synthetase family. Type-1 seryl-tRNA synthetase subfamily.Curated
Phylogenomic databases
eggNOGi | KOG2509. Eukaryota. COG0172. LUCA. |
GeneTreei | ENSGT00790000123098. |
HOGENOMi | HOG000035937. |
HOVERGENi | HBG023172. |
InParanoidi | Q6P799. |
KOi | K01875. |
PhylomeDBi | Q6P799. |
Family and domain databases
CDDi | cd00770. SerRS_core. 1 hit. |
InterProi | View 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. |
PANTHERi | PTHR11778. PTHR11778. 1 hit. |
Pfami | View protein in Pfam PF02403. Seryl_tRNA_N. 1 hit. PF00587. tRNA-synt_2b. 1 hit. |
PIRSFi | PIRSF001529. Ser-tRNA-synth_IIa. 1 hit. |
PRINTSi | PR00981. TRNASYNTHSER. |
SUPFAMi | SSF46589. SSF46589. 1 hit. |
TIGRFAMsi | TIGR00414. serS. 1 hit. |
PROSITEi | View protein in PROSITE PS50862. AA_TRNA_LIGASE_II. 1 hit. |
i Sequence
Sequence statusi: Complete.
Q6P799-1 [UniParc]FASTAAdd to basket
10 20 30 40 50
MVLDLDLFRV DKGGDPALIR ETQEKRFKDP GLVDQLVKAD SEWRRCRFRA
60 70 80 90 100
DNLNKLKNLC SKTIGEKMKK KEPVGEDESI PEDVLNFDDL TADTLAALKV
110 120 130 140 150
SQIKKVRLLV DEAIQKCDGE RVKLEAERFE NLREIGNLLH PSVPISNDED
160 170 180 190 200
ADNKVERIWG DCTVRKKYSH VDLVVMVDGF EGEKGAVVAG SRGYFLKGVL
210 220 230 240 250
VFLEQALIQY ALRTLGSRGY TPIYTPFFMR KEVMQEVAQL SQFDEELYKV
260 270 280 290 300
IGKGSEKSDD SSYDEKYLIA TSEQPIAALH RDEWLRPEDL PIKYAGFSTC
310 320 330 340 350
FRQEVGSHGR DTRGIFRVHQ FEKIEQFVYS SPHDNKSWEM FDEMITTAEE
360 370 380 390 400
FYQSLGIPYH IVNIVSGSLN HAASKKLDLE AWFPGSGAFR ELVSCSNCTD
410 420 430 440 450
YQARRLRIRY GQTKKMMDKV EFVHMLNATM CATTRTICAI LENYQTEKGI
460 470 480 490 500
VVPEKLREFM PPGLQELIPF VKPAPIDQEP SKKQKKQHEG SKKKAKEVTL
510
ENQLQNMEVT EA
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | BC061765 mRNA. Translation: AAH61765.1. AY145052 mRNA. Translation: AAN52758.1. |
RefSeqi | NP_001007607.1. NM_001007606.1. |
UniGenei | Rn.73067. |
Genome annotation databases
Ensembli | ENSRNOT00000033015; ENSRNOP00000038448; ENSRNOG00000020255. |
GeneIDi | 266975. |
KEGGi | rno:266975. |
UCSCi | RGD:628813. rat. |
Similar proteinsi
Entry informationi
Entry namei | SYSC_RAT | |
Accessioni | Q6P799Primary (citable) accession number: Q6P799 Secondary accession number(s): Q8CIQ8 | |
Entry historyi | Integrated into UniProtKB/Swiss-Prot: | January 9, 2007 |
Last sequence update: | January 23, 2007 | |
Last modified: | March 28, 2018 | |
This is version 119 of the entry and version 3 of the sequence. See complete history. | ||
Entry statusi | Reviewed (UniProtKB/Swiss-Prot) | |
Annotation program | Chordata Protein Annotation Program |