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Protein

Serine--tRNA ligase, cytoplasmic

Gene

Sars

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Catalyzes the attachment of serine to tRNA(Ser). Is 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) (By similarity).By similarity

Catalytic activityi

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

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, cytoplasmic (Sars), Serine--tRNA ligase, mitochondrial (Sars2)
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)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei318 – 3181ATP; via amide nitrogen and carbonyl oxygenBy similarity
Binding sitei325 – 3251SerineBy similarity
Binding sitei429 – 4291SerineBy similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi302 – 3043ATPBy similarity
Nucleotide bindingi391 – 3944ATPBy similarity

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Aminoacyl-tRNA synthetase, Ligase

Keywords - Biological processi

Protein biosynthesis

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Enzyme and pathway databases

UniPathwayiUPA00906; UER00895.

Names & Taxonomyi

Protein namesi
Recommended name:
Serine--tRNA ligase, cytoplasmic (EC:6.1.1.11)
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 lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 3

Organism-specific databases

MGIiMGI:102809. Sars.

Subcellular locationi

GO - Cellular componenti

  • cytoplasm Source: MGI
  • extracellular exosome Source: MGI
  • mitochondrion Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 512512Serine--tRNA ligase, cytoplasmicPRO_0000122192Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei1 – 11N-acetylmethionineBy similarity
Modified residuei241 – 2411PhosphoserineBy similarity
Modified residuei323 – 3231N6-acetyllysineBy similarity
Modified residuei506 – 5061PhosphoserineCombined sources

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

EPDiP26638.
MaxQBiP26638.
PaxDbiP26638.
PeptideAtlasiP26638.
PRIDEiP26638.

2D gel databases

REPRODUCTION-2DPAGEP26638.

PTM databases

iPTMnetiP26638.
PhosphoSiteiP26638.
SwissPalmiP26638.

Expressioni

Gene expression databases

BgeeiP26638.
CleanExiMM_SARS.
ExpressionAtlasiP26638. baseline and differential.
GenevisibleiP26638. MM.

Interactioni

Subunit structurei

Homodimer. The tRNA molecule binds across the dimer (By similarity).By similarity

Protein-protein interaction databases

BioGridi203074. 9 interactions.
IntActiP26638. 9 interactions.
MINTiMINT-4136532.
STRINGi10090.ENSMUSP00000099685.

Structurei

3D structure databases

ProteinModelPortaliP26638.
SMRiP26638. Positions 2-477.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni271 – 2733Serine bindingBy similarity

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.
OrthoDBiEOG7Z95KZ.

Family and domain databases

Gene3Di1.10.287.40. 1 hit.
InterProiIPR002314. aa-tRNA-synt_IIb.
IPR006195. aa-tRNA-synth_II.
IPR002317. Ser-tRNA-ligase_type_1.
IPR015866. Ser-tRNA-synth_1_N.
IPR010978. tRNA-bd_arm.
[Graphical view]
PANTHERiPTHR11778. PTHR11778. 1 hit.
PfamiPF02403. Seryl_tRNA_N. 1 hit.
PF00587. tRNA-synt_2b. 1 hit.
[Graphical view]
PIRSFiPIRSF001529. Ser-tRNA-synth_IIa. 1 hit.
PRINTSiPR00981. TRNASYNTHSER.
SUPFAMiSSF46589. SSF46589. 2 hits.
TIGRFAMsiTIGR00414. serS. 1 hit.
PROSITEiPS50862. AA_TRNA_LIGASE_II. 1 hit.
[Graphical view]

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)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti96 – 961A → R in AAA40108 (PubMed:1918033).Curated
Sequence conflicti192 – 1998RGYFLKGP → PGVLPEGA in AAA40108 (PubMed:1918033).Curated
Sequence conflicti283 – 2831E → A in AAA40108 (PubMed:1918033).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK075827 mRNA. Translation: BAC35990.1.
AL672200 Genomic DNA. Translation: CAM22589.1.
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.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK075827 mRNA. Translation: BAC35990.1.
AL672200 Genomic DNA. Translation: CAM22589.1.
BC008612 mRNA. Translation: AAH08612.1.
M74012 mRNA. Translation: AAA40108.1.
CCDSiCCDS57254.1.
RefSeqiNP_001191908.1. NM_001204979.1.
UniGeneiMm.28688.

3D structure databases

ProteinModelPortaliP26638.
SMRiP26638. Positions 2-477.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi203074. 9 interactions.
IntActiP26638. 9 interactions.
MINTiMINT-4136532.
STRINGi10090.ENSMUSP00000099685.

PTM databases

iPTMnetiP26638.
PhosphoSiteiP26638.
SwissPalmiP26638.

2D gel databases

REPRODUCTION-2DPAGEP26638.

Proteomic databases

EPDiP26638.
MaxQBiP26638.
PaxDbiP26638.
PeptideAtlasiP26638.
PRIDEiP26638.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

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

Organism-specific databases

CTDi6301.
MGIiMGI:102809. Sars.

Phylogenomic databases

eggNOGiKOG2509. Eukaryota.
COG0172. LUCA.
GeneTreeiENSGT00790000123098.
HOGENOMiHOG000035937.
HOVERGENiHBG023172.
InParanoidiP26638.
KOiK01875.
OrthoDBiEOG7Z95KZ.

Enzyme and pathway databases

UniPathwayiUPA00906; UER00895.

Miscellaneous databases

ChiTaRSiSars. mouse.
PROiP26638.
SOURCEiSearch...

Gene expression databases

BgeeiP26638.
CleanExiMM_SARS.
ExpressionAtlasiP26638. baseline and differential.
GenevisibleiP26638. MM.

Family and domain databases

Gene3Di1.10.287.40. 1 hit.
InterProiIPR002314. aa-tRNA-synt_IIb.
IPR006195. aa-tRNA-synth_II.
IPR002317. Ser-tRNA-ligase_type_1.
IPR015866. Ser-tRNA-synth_1_N.
IPR010978. tRNA-bd_arm.
[Graphical view]
PANTHERiPTHR11778. PTHR11778. 1 hit.
PfamiPF02403. Seryl_tRNA_N. 1 hit.
PF00587. tRNA-synt_2b. 1 hit.
[Graphical view]
PIRSFiPIRSF001529. Ser-tRNA-synth_IIa. 1 hit.
PRINTSiPR00981. TRNASYNTHSER.
SUPFAMiSSF46589. SSF46589. 2 hits.
TIGRFAMsiTIGR00414. serS. 1 hit.
PROSITEiPS50862. AA_TRNA_LIGASE_II. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: C57BL/6J.
    Tissue: Stomach.
  2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: C57BL/6J.
  3. "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: Mammary tumor.
  4. "Mammalian seryl-tRNA synthetase associates with mRNA in vivo and has homology to elongation factor 1 alpha."
    Miseta A., Woodley C.L., Greenberg J.R., Slobin L.I.
    J. Biol. Chem. 266:19158-19161(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1-283.
  5. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-506, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas, Spleen and Testis.

Entry informationi

Entry nameiSYSC_MOUSE
AccessioniPrimary (citable) accession number: P26638
Secondary accession number(s): A2AFR8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 1, 1992
Last sequence update: January 23, 2007
Last modified: July 6, 2016
This is version 138 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Aminoacyl-tRNA synthetases
    List of aminoacyl-tRNA synthetase entries
  2. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  3. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  4. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.