Skip Header

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

P38088

- SYG_YEAST

UniProt

P38088 - SYG_YEAST

(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Protein

Glycine--tRNA ligase 1, mitochondrial

Gene

GRS1

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

Functioni

Catalyzes the attachment of glycine to tRNA(Gly). Is also able produce diadenosine tetraphosphate (Ap4A), a universal pleiotropic signaling molecule needed for cell regulation pathways, by direct condensation of 2 ATPs (By similarity).By similarity

Catalytic activityi

ATP + glycine + tRNA(Gly) = AMP + diphosphate + glycyl-tRNA(Gly).

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei132 – 1321SubstrateBy similarity
Binding sitei251 – 2511SubstrateBy similarity
Binding sitei388 – 3881SubstrateBy similarity
Binding sitei388 – 3881Substrate; via carbonyl oxygenBy similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi283 – 2853ATPBy similarity
Nucleotide bindingi293 – 2986ATPBy similarity
Nucleotide bindingi410 – 4112ATPBy similarity
Nucleotide bindingi535 – 5384ATPBy similarity

GO - Molecular functioni

  1. ATP binding Source: UniProtKB-KW
  2. glycine-tRNA ligase activity Source: UniProtKB
  3. protein dimerization activity Source: UniProtKB

GO - Biological processi

  1. diadenosine tetraphosphate biosynthetic process Source: UniProtKB
  2. DNA-templated transcription, termination Source: SGD
  3. glycyl-tRNA aminoacylation Source: SGD
  4. mitochondrial glycyl-tRNA aminoacylation Source: SGD
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

BioCyciYEAST:G3O-29078-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
Glycine--tRNA ligase 1, mitochondrial (EC:6.1.1.14)
Alternative name(s):
Diadenosine tetraphosphate synthetase
Short name:
AP-4-A synthetase
Glycyl-tRNA synthetase 1
Short name:
GlyRS 1
Short name:
GlyRS1
Gene namesi
Name:GRS1
Ordered Locus Names:YBR121C
ORF Names:YBR0917
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
ProteomesiUP000002311: Chromosome II

Organism-specific databases

CYGDiYBR121c.
SGDiS000000325. GRS1.

Subcellular locationi

GO - Cellular componenti

  1. cytoplasm Source: SGD
  2. mitochondrion Source: SGD
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Mitochondrion

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transit peptidei1 – 2424MitochondrionSequence AnalysisAdd
BLAST
Chaini25 – 690666Glycine--tRNA ligase 1, mitochondrialPRO_0000073005Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei25 – 251N-acetylserine1 Publication
Modified residuei226 – 2261Phosphoserine4 Publications
Modified residuei476 – 4761Phosphoserine2 Publications
Modified residuei528 – 5281Phosphoserine1 Publication
Modified residuei689 – 6891Phosphothreonine1 Publication

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

MaxQBiP38088.
PaxDbiP38088.
PeptideAtlasiP38088.
PRIDEiP38088.

Expressioni

Gene expression databases

GenevestigatoriP38088.

Interactioni

Subunit structurei

Homodimer.

Protein-protein interaction databases

BioGridi32823. 42 interactions.
DIPiDIP-6526N.
IntActiP38088. 13 interactions.
MINTiMINT-690383.
STRINGi4932.YBR121C.

Structurei

3D structure databases

ProteinModelPortaliP38088.
SMRiP38088. Positions 39-671.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni298 – 3025Substrate bindingBy similarity
Regioni531 – 5355Substrate bindingBy similarity

Sequence similaritiesi

Keywords - Domaini

Transit peptide

Phylogenomic databases

eggNOGiCOG0423.
HOGENOMiHOG000242015.
InParanoidiP38088.
KOiK01880.
OMAiLMFQTTI.
OrthoDBiEOG76TB17.

Family and domain databases

Gene3Di3.40.50.800. 1 hit.
InterProiIPR002314. aa-tRNA-synt_IIb_cons-dom.
IPR006195. aa-tRNA-synth_II.
IPR004154. Anticodon-bd.
IPR027031. Gly-tRNA_synthase/POLG2.
IPR002315. tRNA-synt_gly.
[Graphical view]
PANTHERiPTHR10745. PTHR10745. 1 hit.
PfamiPF03129. HGTP_anticodon. 1 hit.
PF00587. tRNA-synt_2b. 1 hit.
[Graphical view]
PRINTSiPR01043. TRNASYNTHGLY.
SUPFAMiSSF52954. SSF52954. 1 hit.
TIGRFAMsiTIGR00389. glyS_dimeric. 1 hit.
PROSITEiPS50862. AA_TRNA_LIGASE_II. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

This entry describes 2 isoformsi produced by alternative initiation. Align

Isoform Mitochondrial (identifier: P38088-1) [UniParc]FASTAAdd to Basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MSFFNISRRF YSQIVKKSVK IKRMSVEDIK KARAAVPFNR EQLESVLRGR
60 70 80 90 100
FFYAPAFDLY GGVSGLYDYG PPGCAFQNNI IDAWRKHFIL EEDMLEVDCT
110 120 130 140 150
MLTPYEVLKT SGHVDKFSDW MCRDLKTGEI FRADHLVEEV LEARLKGDQE
160 170 180 190 200
ARGLVEDANA AAKDDAEKKK RKKKVKQIKA VKLDDDVVKE YEEILAKIDG
210 220 230 240 250
YSGPELGELM EKYDIGNPVT GETLESPRAF NLMFETAIGP SGQLKGYLRP
260 270 280 290 300
ETAQGQFLNF NKLLEFNNSK TPFASASIGK SFRNEISPRA GLLRVREFLM
310 320 330 340 350
AEIEHFVDPL DKSHPKFNEI KDIKLSFLPR DVQEAGSTEP IVKTVGEAVA
360 370 380 390 400
SRMVDNETLG YFIARIYQFL MKIGVDESKL RFRQHMANEM AHYAADCWDG
410 420 430 440 450
ELKTSYGWIE CVGCADRSAY DLTVHSKKTK EKLVVRQKLD NPIEVTKWEI
460 470 480 490 500
DLTKKLFGPK FRKDAPKVES HLLNMSQDDL ASKAELLKAN GKFTIKVDGV
510 520 530 540 550
DGEVELDDKL VKIEQRTKVE HVREYVPSVI EPSFGIGRII YSVFEHSFWN
560 570 580 590 600
RPEDNARSVL SFPPLVAPTK VLLVPLSNHK DLVPVTTEVA KILRKSQIPF
610 620 630 640 650
KIDDSGVSIG KRYARNDELG TPFGVTIDFE SAKDHSVTLR ERDSTKQVRG
660 670 680 690
SVENVIKAIR DITYNGASWE EGTKDLTPFI AQAEAEAETD

Note: Produced by alternative initiation at an upstream UUG codon in-frame of the first AUG used for isoform Cytoplasmic.

Length:690
Mass (Da):78,184
Last modified:July 27, 2011 - v3
Checksum:i4EBDE6F0A942F7F6
GO
Isoform Cytoplasmic (identifier: P38088-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-23: Missing.

Show »
Length:667
Mass (Da):75,339
Checksum:iB62E3DDAD7E87552
GO

Sequence cautioni

The sequence CAA55623.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated
The sequence CAA85078.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated
The sequence DAA07239.2 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti586 – 5872TT → HH in CAA55623. (PubMed:7900426)Curated
Sequence conflicti586 – 5872TT → HH in CAA85078. (PubMed:7813418)Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 2323Missing in isoform Cytoplasmic. CuratedVSP_041147Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X78993 Genomic DNA. Translation: CAA55623.1. Different initiation.
Z35990 Genomic DNA. Translation: CAA85078.1. Different initiation.
BK006936 Genomic DNA. Translation: DAA07239.2. Different initiation.
PIRiS48285.
RefSeqiNP_009679.2. NM_001178469.2. [P38088-2]

Genome annotation databases

GeneIDi852418.
KEGGisce:YBR121C.

Keywords - Coding sequence diversityi

Alternative initiation

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X78993 Genomic DNA. Translation: CAA55623.1 . Different initiation.
Z35990 Genomic DNA. Translation: CAA85078.1 . Different initiation.
BK006936 Genomic DNA. Translation: DAA07239.2 . Different initiation.
PIRi S48285.
RefSeqi NP_009679.2. NM_001178469.2. [P38088-2 ]

3D structure databases

ProteinModelPortali P38088.
SMRi P38088. Positions 39-671.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 32823. 42 interactions.
DIPi DIP-6526N.
IntActi P38088. 13 interactions.
MINTi MINT-690383.
STRINGi 4932.YBR121C.

Proteomic databases

MaxQBi P38088.
PaxDbi P38088.
PeptideAtlasi P38088.
PRIDEi P38088.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

GeneIDi 852418.
KEGGi sce:YBR121C.

Organism-specific databases

CYGDi YBR121c.
SGDi S000000325. GRS1.

Phylogenomic databases

eggNOGi COG0423.
HOGENOMi HOG000242015.
InParanoidi P38088.
KOi K01880.
OMAi LMFQTTI.
OrthoDBi EOG76TB17.

Enzyme and pathway databases

BioCyci YEAST:G3O-29078-MONOMER.

Miscellaneous databases

NextBioi 971279.

Gene expression databases

Genevestigatori P38088.

Family and domain databases

Gene3Di 3.40.50.800. 1 hit.
InterProi IPR002314. aa-tRNA-synt_IIb_cons-dom.
IPR006195. aa-tRNA-synth_II.
IPR004154. Anticodon-bd.
IPR027031. Gly-tRNA_synthase/POLG2.
IPR002315. tRNA-synt_gly.
[Graphical view ]
PANTHERi PTHR10745. PTHR10745. 1 hit.
Pfami PF03129. HGTP_anticodon. 1 hit.
PF00587. tRNA-synt_2b. 1 hit.
[Graphical view ]
PRINTSi PR01043. TRNASYNTHGLY.
SUPFAMi SSF52954. SSF52954. 1 hit.
TIGRFAMsi TIGR00389. glyS_dimeric. 1 hit.
PROSITEi PS50862. AA_TRNA_LIGASE_II. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Analysis of a 70 kb region on the right arm of yeast chromosome II."
    Mannhaupt G., Stucka R., Ehnle S., Vetter I., Feldmann H.
    Yeast 10:1363-1381(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: ATCC 204508 / S288c.
  2. "Complete DNA sequence of yeast chromosome II."
    Feldmann H., Aigle M., Aljinovic G., Andre B., Baclet M.C., Barthe C., Baur A., Becam A.-M., Biteau N., Boles E., Brandt T., Brendel M., Brueckner M., Bussereau F., Christiansen C., Contreras R., Crouzet M., Cziepluch C.
    , Demolis N., Delaveau T., Doignon F., Domdey H., Duesterhus S., Dubois E., Dujon B., El Bakkoury M., Entian K.-D., Feuermann M., Fiers W., Fobo G.M., Fritz C., Gassenhuber J., Glansdorff N., Goffeau A., Grivell L.A., de Haan M., Hein C., Herbert C.J., Hollenberg C.P., Holmstroem K., Jacq C., Jacquet M., Jauniaux J.-C., Jonniaux J.-L., Kallesoee T., Kiesau P., Kirchrath L., Koetter P., Korol S., Liebl S., Logghe M., Lohan A.J.E., Louis E.J., Li Z.Y., Maat M.J., Mallet L., Mannhaupt G., Messenguy F., Miosga T., Molemans F., Mueller S., Nasr F., Obermaier B., Perea J., Pierard A., Piravandi E., Pohl F.M., Pohl T.M., Potier S., Proft M., Purnelle B., Ramezani Rad M., Rieger M., Rose M., Schaaff-Gerstenschlaeger I., Scherens B., Schwarzlose C., Skala J., Slonimski P.P., Smits P.H.M., Souciet J.-L., Steensma H.Y., Stucka R., Urrestarazu L.A., van der Aart Q.J.M., Van Dyck L., Vassarotti A., Vetter I., Vierendeels F., Vissers S., Wagner G., de Wergifosse P., Wolfe K.H., Zagulski M., Zimmermann F.K., Mewes H.-W., Kleine K.
    EMBO J. 13:5795-5809(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 204508 / S288c.
  3. Cited for: GENOME REANNOTATION, SEQUENCE REVISION TO 586-587.
    Strain: ATCC 204508 / S288c.
  4. "One of two genes encoding glycyl-tRNA synthetase in Saccharomyces cerevisiae provides mitochondrial and cytoplasmic functions."
    Turner R.J., Lovato M., Schimmel P.
    J. Biol. Chem. 275:27681-27688(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION.
  5. Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
  6. "Translation initiation from a naturally occurring non-AUG codon in Saccharomyces cerevisiae."
    Chang K.J., Wang C.C.
    J. Biol. Chem. 279:13778-13785(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: ALTERNATIVE INITIATION.
  7. "Quantitative phosphoproteomics applied to the yeast pheromone signaling pathway."
    Gruhler A., Olsen J.V., Mohammed S., Mortensen P., Faergeman N.J., Mann M., Jensen O.N.
    Mol. Cell. Proteomics 4:310-327(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-226, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Strain: YAL6B.
  8. "Large-scale phosphorylation analysis of alpha-factor-arrested Saccharomyces cerevisiae."
    Li X., Gerber S.A., Rudner A.D., Beausoleil S.A., Haas W., Villen J., Elias J.E., Gygi S.P.
    J. Proteome Res. 6:1190-1197(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-226, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Strain: ADR376.
  9. "A multidimensional chromatography technology for in-depth phosphoproteome analysis."
    Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.
    Mol. Cell. Proteomics 7:1389-1396(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-226; SER-476 AND SER-528, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  10. "Global analysis of Cdk1 substrate phosphorylation sites provides insights into evolution."
    Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.
    Science 325:1682-1686(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-226; SER-476 AND THR-689, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  11. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT SER-25, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiSYG_YEAST
AccessioniPrimary (citable) accession number: P38088
Secondary accession number(s): D6VQB9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1994
Last sequence update: July 27, 2011
Last modified: October 29, 2014
This is version 132 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Miscellaneous

Present with 98400 molecules/cell in log phase SD medium.1 Publication

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Aminoacyl-tRNA synthetases
    List of aminoacyl-tRNA synthetase entries
  2. SIMILARITY comments
    Index of protein domains and families
  3. Yeast
    Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD
  4. Yeast chromosome II
    Yeast (Saccharomyces cerevisiae) chromosome II: entries and gene names

External Data

Dasty 3