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Q8CGC7

- SYEP_MOUSE

UniProt

Q8CGC7 - SYEP_MOUSE

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Protein

Bifunctional glutamate/proline--tRNA ligase

Gene

Eprs

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

Functioni

Catalyzes the attachment of the cognate amino acid to the corresponding tRNA in a two-step reaction: the amino acid is first activated by ATP to form a covalent intermediate with AMP and is then transferred to the acceptor end of the cognate tRNA (By similarity). Component of the GAIT (gamma interferon-activated inhibitor of translation) complex which mediates interferon-gamma-induced transcript-selective translation inhibition in inflammation processes. Upon interferon-gamma activation and subsequent phosphorylation dissociates from the multisynthetase complex and assembles into the GAIT complex which binds to stem loop-containing GAIT elements in the 3'-UTR of diverse inflammatory mRNAs (such as ceruplasmin) and suppresses their translation.By similarity1 Publication

Catalytic activityi

ATP + L-glutamate + tRNA(Glu) = AMP + diphosphate + L-glutamyl-tRNA(Glu).
ATP + L-proline + tRNA(Pro) = AMP + diphosphate + L-prolyl-tRNA(Pro).

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei211 – 2111ATPBy similarity
Binding sitei398 – 3981ATPBy similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi432 – 4365ATPBy similarity

GO - Molecular functioni

  1. ATP binding Source: UniProtKB-KW
  2. glutamate-tRNA ligase activity Source: UniProtKB-EC
  3. proline-tRNA ligase activity Source: UniProtKB-EC
  4. RNA stem-loop binding Source: UniProtKB

GO - Biological processi

  1. cellular response to interferon-gamma Source: UniProtKB
  2. glutamyl-tRNA aminoacylation Source: InterPro
  3. negative regulation of translation Source: UniProtKB
  4. prolyl-tRNA aminoacylation Source: InterPro
Complete GO annotation...

Keywords - Molecular functioni

Aminoacyl-tRNA synthetase, Ligase

Keywords - Biological processi

Protein biosynthesis, Translation regulation

Keywords - Ligandi

ATP-binding, Nucleotide-binding, RNA-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Bifunctional glutamate/proline--tRNA ligase
Alternative name(s):
Bifunctional aminoacyl-tRNA synthetase
Including the following 2 domains:
Glutamate--tRNA ligase (EC:6.1.1.17)
Alternative name(s):
Glutamyl-tRNA synthetase
Short name:
GluRS
Proline--tRNA ligase (EC:6.1.1.15)
Alternative name(s):
Prolyl-tRNA synthetase
Short name:
ProRS
Gene namesi
Name:Eprs
Synonyms:Qprs
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Chromosome 1

Organism-specific databases

MGIiMGI:97838. Eprs.

Subcellular locationi

GO - Cellular componenti

  1. aminoacyl-tRNA synthetase multienzyme complex Source: MGI
  2. cytoplasm Source: InterPro
  3. GAIT complex Source: UniProtKB
  4. ribonucleoprotein complex Source: Ensembl
Complete GO annotation...

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi999 – 9991S → A: Not active in translation inhibition. 1 Publication
Mutagenesisi999 – 9991S → D: Active in translation inhibition (phosphomimetic). 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 15121512Bifunctional glutamate/proline--tRNA ligasePRO_0000119744Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei300 – 3001N6-acetyllysine; alternate1 Publication
Modified residuei300 – 3001N6-malonyllysine; alternateBy similarity
Modified residuei417 – 4171N6-acetyllysineBy similarity
Modified residuei498 – 4981N6-acetyllysineBy similarity
Modified residuei535 – 5351N6-acetyllysineBy similarity
Modified residuei542 – 5421N6-acetyllysineBy similarity
Modified residuei637 – 6371N6-acetyllysineBy similarity
Modified residuei788 – 7881N6-acetyllysine1 Publication
Modified residuei861 – 8611N6-acetyllysine1 Publication
Modified residuei872 – 8721PhosphotyrosineBy similarity
Modified residuei885 – 8851PhosphoserineBy similarity
Modified residuei999 – 9991Phosphoserine1 Publication
Modified residuei1503 – 15031N6-acetyllysineBy similarity

Post-translational modificationi

Phosphorylated at Ser-999 in macrophages in a IFN-gamma-dependent manner; the phosphorylation is involving CDK5 and is causing release from the multisynthetase complex, association with the GAIT complex and subsequent involvement in transcript-selective translation inhibition. Phosphorylation at Ser-999 is specifically required for the interaction of GAIT complex-associated RPL13A with eIF4G (By similarity).By similarity

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

MaxQBiQ8CGC7.
PaxDbiQ8CGC7.
PRIDEiQ8CGC7.

PTM databases

PhosphoSiteiQ8CGC7.

Expressioni

Gene expression databases

BgeeiQ8CGC7.
CleanExiMM_EPRS.
ExpressionAtlasiQ8CGC7. baseline and differential.
GenevestigatoriQ8CGC7.

Interactioni

Subunit structurei

Component of the multisynthetase complex which is comprised of a bifunctional glutamyl-prolyl-tRNA synthetase, the monospecific isoleucyl, leucyl, glutaminyl, methionyl, lysyl, arginyl, and aspartyl-tRNA synthetases as well as three auxiliary proteins, p18, p48 and p43. Interacts with DUS2L (By similarity). Component of the GAIT complex.By similarity1 Publication

Protein-protein interaction databases

BioGridi223350. 11 interactions.
IntActiQ8CGC7. 3 interactions.
MINTiMINT-1869828.

Structurei

3D structure databases

ProteinModelPortaliQ8CGC7.
SMRiQ8CGC7. Positions 749-804, 826-875, 900-952, 1016-1512.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini749 – 80557WHEP-TRS 1Add
BLAST
Domaini822 – 87857WHEP-TRS 2Add
BLAST
Domaini900 – 95657WHEP-TRS 3Add
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni164 – 759596Glutamate--tRNA ligaseAdd
BLAST
Regioni760 – 9561973 X 57 AA approximate repeatsAdd
BLAST
Regioni1007 – 1512506Proline--tRNA ligaseAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi204 – 21411"HIGH" regionAdd
BLAST
Motifi432 – 4365"KMSKS" region

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi959 – 99133Asp/Glu/Lys-richAdd
BLAST

Domaini

The WHEP-TRS domain is involved in RNA binding.By similarity

Sequence similaritiesi

In the N-terminal section; belongs to the class-I aminoacyl-tRNA synthetase family.Curated
In the C-terminal section; belongs to the class-II aminoacyl-tRNA synthetase family.Curated
Contains 3 WHEP-TRS domains.Curated

Keywords - Domaini

Repeat

Phylogenomic databases

eggNOGiCOG0442.
GeneTreeiENSGT00550000074815.
HOGENOMiHOG000022047.
HOVERGENiHBG017875.
InParanoidiQ8CGC7.
KOiK14163.
OMAiVAMLHIK.
OrthoDBiEOG754HNH.
TreeFamiTF300380.

Family and domain databases

Gene3Di1.10.1160.10. 1 hit.
1.10.287.10. 3 hits.
1.20.1050.10. 1 hit.
2.40.240.10. 2 hits.
3.30.110.30. 1 hit.
3.40.50.620. 2 hits.
3.40.50.800. 1 hit.
HAMAPiMF_01571. Pro_tRNA_synth_type3.
InterProiIPR002314. aa-tRNA-synt_IIb_cons-dom.
IPR001412. aa-tRNA-synth_I_CS.
IPR006195. aa-tRNA-synth_II.
IPR004154. Anticodon-bd.
IPR004526. Glu-tRNA-synth_arc/euk.
IPR000924. Glu/Gln-tRNA-synth.
IPR020061. Glu/Gln-tRNA-synth_Ib_a-bdl.
IPR020058. Glu/Gln-tRNA-synth_Ib_cat-dom.
IPR020059. Glu/Gln-tRNA-synth_Ib_codon-bd.
IPR010987. Glutathione-S-Trfase_C-like.
IPR004046. GST_C.
IPR004499. Pro-tRNA-ligase_IIa_arc-type.
IPR016061. Pro-tRNA_ligase_II_C.
IPR017449. Pro-tRNA_synth_II.
IPR020056. Rbsml_L25/Gln-tRNA_synth_b-brl.
IPR011035. Ribosomal_L25/Gln-tRNA_synth.
IPR014729. Rossmann-like_a/b/a_fold.
IPR009068. S15_NS1_RNA-bd.
IPR000738. WHEP-TRS.
[Graphical view]
PANTHERiPTHR10119. PTHR10119. 1 hit.
PfamiPF14497. GST_C_3. 1 hit.
PF03129. HGTP_anticodon. 1 hit.
PF09180. ProRS-C_1. 1 hit.
PF00749. tRNA-synt_1c. 1 hit.
PF03950. tRNA-synt_1c_C. 1 hit.
PF00587. tRNA-synt_2b. 1 hit.
PF00458. WHEP-TRS. 3 hits.
[Graphical view]
PRINTSiPR00987. TRNASYNTHGLU.
SMARTiSM00946. ProRS-C_1. 1 hit.
SM00991. WHEP-TRS. 3 hits.
[Graphical view]
SUPFAMiSSF47060. SSF47060. 3 hits.
SSF47616. SSF47616. 1 hit.
SSF50715. SSF50715. 1 hit.
SSF52954. SSF52954. 1 hit.
SSF64586. SSF64586. 1 hit.
TIGRFAMsiTIGR00463. gltX_arch. 1 hit.
TIGR00408. proS_fam_I. 1 hit.
PROSITEiPS00178. AA_TRNA_LIGASE_I. 1 hit.
PS50862. AA_TRNA_LIGASE_II. 1 hit.
PS00762. WHEP_TRS_1. 2 hits.
PS51185. WHEP_TRS_2. 3 hits.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q8CGC7-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MAALCLTVNA GNPPLEALLA VEHVKGDVSI SVEEGKENLL RVSETVAFTD
60 70 80 90 100
VNSILRYLAR IATTSGLYGT NLMEHTEIDH WLEFSATKLS SCDRLTSAIN
110 120 130 140 150
ELNHCLSLRT YLVGNSLTLA DLCVWATLKG SAAWQEHLKQ NKTLVHVKRW
160 170 180 190 200
FGFLEAQQAF RSVGTKWDVS GNRATVAPDK KQDVGKFVEL PGAEMGKVTV
210 220 230 240 250
RFPPEASGYL HIGHAKAALL NQHYQVNFKG KLIMRFDDTN PEKEKEDFEK
260 270 280 290 300
VILEDVAMLH IKPDQFTYTS DHFETIMKYA EKLIQEGKAY VDDTPAEQMK
310 320 330 340 350
AEREQRTESK HRKNSVEKNL QMWEEMKKGS QFGQSCCLRA KIDMSSNNGC
360 370 380 390 400
MRDPTLYRCK IQPHPRTGNK YNVYPTYDFA CPIVDSIEGV THALRTTEYH
410 420 430 440 450
DRDEQFYWII EALGIRKPYI WEYSRLNLNN TVLSKRKLTW FVNEGLVDGW
460 470 480 490 500
DDPRFPTVRG VLRRGMTVEG LKQFIAAQGS SRSVVNMEWD KIWAFNKKVI
510 520 530 540 550
DPVAPRYVAL LKKEVVPVNV LDAQEEMKEV ARHPKNPDVG LKPVWYSPKV
560 570 580 590 600
FIEGADAETF SEGEMVTFIN WGNINITKIH KNADGKITSL DAKLNLENKD
610 620 630 640 650
YKKTTKITWL AESTHALSIP AVCVTYEHLI TKPVLGKDED FKQYINKDSK
660 670 680 690 700
HEELMLGDPC LKDLKKGDII QLQRRGFFIC DQPYEPVSPY SCREAPCILI
710 720 730 740 750
YIPDGHTKEM PTSGSKEKTK VEISKKETSS APKERPAPAV SSTCATAEDS
760 770 780 790 800
SVLYSRVAVQ GDVVRELKAK KAPKEDIDAA VKQLLTLKAE YKEKTGQEYK
810 820 830 840 850
PGNPSAAAVQ TVSTKSSSNT VESTSLYNKV AAQGEVVRKL KAEKAPKAKV
860 870 880 890 900
TEAVECLLSL KAEYKEKTGK DYVPGQPPAS QNSHSNPVSN AQPAGAEKPE
910 920 930 940 950
AKVLFDRVAC QGEVVRKLKA EKASKDQVDS AVQELLQLKA QYKSLTGIEY
960 970 980 990 1000
KPVSATGAED KDKKKKEKEN KSEKQNKPQK QNDGQGKDSS KSQGSGLSSG
1010 1020 1030 1040 1050
GAGEGQGPKK QTRLGLEAKK EENLAEWYSQ VITKSEMIEY YDVSGCYILR
1060 1070 1080 1090 1100
PWSYSIWESI KDFFDAEIKK LGVENCYFPI FVSQAALEKE KNHIEDFAPE
1110 1120 1130 1140 1150
VAWVTRSGKT ELAEPIAIRP TSETVMYPAY AKWVQSHRDL PVRLNQWCNV
1160 1170 1180 1190 1200
VRWEFKHPQP FLRTREFLWQ EGHSAFATFE EAADEVLQIL ELYARVYEEL
1210 1220 1230 1240 1250
LAIPVVRGRK TEKEKFAGGD YTTTIEAFIS ASGRAIQGAT SHHLGQNFSK
1260 1270 1280 1290 1300
MCEIVFEDPK TPGEKQFAYQ CSWGLTTRTI GVMVMVHGDN MGLVLPPRVA
1310 1320 1330 1340 1350
SVQVVVIPCG ITNALSEEDR EALMAKCNEY RRRLLGANIR VRVDLRDNYS
1360 1370 1380 1390 1400
PGWKFNHWEL KGVPVRLEVG PRDMKSCQFV AVRRDTGEKL TIAEKEAEAK
1410 1420 1430 1440 1450
LEKVLEDIQL NLFTRASEDL KTHMVVSNTL EDFQKVLDAG KVAQIPFCGE
1460 1470 1480 1490 1500
IDCEDWIKKM TARDQDVEPG APSMGAKSLC IPFNPLCELQ PGAMCVCGKN
1510
PAKFYTLFGR SY
Length:1,512
Mass (Da):170,079
Last modified:July 27, 2011 - v4
Checksum:iD14F6EA015B1BB6A
GO

Sequence cautioni

The sequence AAH40802.1 differs from that shown. Reason: Contaminating sequence. Potential poly-A sequence.Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti94 – 941R → G in AAH40802. (PubMed:15489334)Curated
Sequence conflicti172 – 1721N → S in AAH40802. (PubMed:15489334)Curated
Sequence conflicti618 – 6181S → P in AAH40802. (PubMed:15489334)Curated
Sequence conflicti986 – 9861G → R in X54327. 1 PublicationCurated
Sequence conflicti1290 – 12901N → S in AAH94679. (PubMed:15489334)Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti871 – 8711D → E.

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AC129195 Genomic DNA. No translation available.
AC131980 Genomic DNA. No translation available.
BC040802 mRNA. Translation: AAH40802.1. Sequence problems.
BC094679 mRNA. Translation: AAH94679.1.
AK148463 mRNA. Translation: BAE28568.1.
X54327 mRNA. No translation available.
CCDSiCCDS35818.1.
RefSeqiNP_084011.1. NM_029735.1.
UniGeneiMm.154511.
Mm.490980.

Genome annotation databases

EnsembliENSMUST00000046514; ENSMUSP00000045841; ENSMUSG00000026615.
GeneIDi107508.
KEGGimmu:107508.
UCSCiuc007dze.1. mouse.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AC129195 Genomic DNA. No translation available.
AC131980 Genomic DNA. No translation available.
BC040802 mRNA. Translation: AAH40802.1 . Sequence problems.
BC094679 mRNA. Translation: AAH94679.1 .
AK148463 mRNA. Translation: BAE28568.1 .
X54327 mRNA. No translation available.
CCDSi CCDS35818.1.
RefSeqi NP_084011.1. NM_029735.1.
UniGenei Mm.154511.
Mm.490980.

3D structure databases

ProteinModelPortali Q8CGC7.
SMRi Q8CGC7. Positions 749-804, 826-875, 900-952, 1016-1512.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 223350. 11 interactions.
IntActi Q8CGC7. 3 interactions.
MINTi MINT-1869828.

PTM databases

PhosphoSitei Q8CGC7.

Proteomic databases

MaxQBi Q8CGC7.
PaxDbi Q8CGC7.
PRIDEi Q8CGC7.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSMUST00000046514 ; ENSMUSP00000045841 ; ENSMUSG00000026615 .
GeneIDi 107508.
KEGGi mmu:107508.
UCSCi uc007dze.1. mouse.

Organism-specific databases

CTDi 2058.
MGIi MGI:97838. Eprs.

Phylogenomic databases

eggNOGi COG0442.
GeneTreei ENSGT00550000074815.
HOGENOMi HOG000022047.
HOVERGENi HBG017875.
InParanoidi Q8CGC7.
KOi K14163.
OMAi VAMLHIK.
OrthoDBi EOG754HNH.
TreeFami TF300380.

Miscellaneous databases

ChiTaRSi Eprs. mouse.
NextBioi 358934.
PROi Q8CGC7.
SOURCEi Search...

Gene expression databases

Bgeei Q8CGC7.
CleanExi MM_EPRS.
ExpressionAtlasi Q8CGC7. baseline and differential.
Genevestigatori Q8CGC7.

Family and domain databases

Gene3Di 1.10.1160.10. 1 hit.
1.10.287.10. 3 hits.
1.20.1050.10. 1 hit.
2.40.240.10. 2 hits.
3.30.110.30. 1 hit.
3.40.50.620. 2 hits.
3.40.50.800. 1 hit.
HAMAPi MF_01571. Pro_tRNA_synth_type3.
InterProi IPR002314. aa-tRNA-synt_IIb_cons-dom.
IPR001412. aa-tRNA-synth_I_CS.
IPR006195. aa-tRNA-synth_II.
IPR004154. Anticodon-bd.
IPR004526. Glu-tRNA-synth_arc/euk.
IPR000924. Glu/Gln-tRNA-synth.
IPR020061. Glu/Gln-tRNA-synth_Ib_a-bdl.
IPR020058. Glu/Gln-tRNA-synth_Ib_cat-dom.
IPR020059. Glu/Gln-tRNA-synth_Ib_codon-bd.
IPR010987. Glutathione-S-Trfase_C-like.
IPR004046. GST_C.
IPR004499. Pro-tRNA-ligase_IIa_arc-type.
IPR016061. Pro-tRNA_ligase_II_C.
IPR017449. Pro-tRNA_synth_II.
IPR020056. Rbsml_L25/Gln-tRNA_synth_b-brl.
IPR011035. Ribosomal_L25/Gln-tRNA_synth.
IPR014729. Rossmann-like_a/b/a_fold.
IPR009068. S15_NS1_RNA-bd.
IPR000738. WHEP-TRS.
[Graphical view ]
PANTHERi PTHR10119. PTHR10119. 1 hit.
Pfami PF14497. GST_C_3. 1 hit.
PF03129. HGTP_anticodon. 1 hit.
PF09180. ProRS-C_1. 1 hit.
PF00749. tRNA-synt_1c. 1 hit.
PF03950. tRNA-synt_1c_C. 1 hit.
PF00587. tRNA-synt_2b. 1 hit.
PF00458. WHEP-TRS. 3 hits.
[Graphical view ]
PRINTSi PR00987. TRNASYNTHGLU.
SMARTi SM00946. ProRS-C_1. 1 hit.
SM00991. WHEP-TRS. 3 hits.
[Graphical view ]
SUPFAMi SSF47060. SSF47060. 3 hits.
SSF47616. SSF47616. 1 hit.
SSF50715. SSF50715. 1 hit.
SSF52954. SSF52954. 1 hit.
SSF64586. SSF64586. 1 hit.
TIGRFAMsi TIGR00463. gltX_arch. 1 hit.
TIGR00408. proS_fam_I. 1 hit.
PROSITEi PS00178. AA_TRNA_LIGASE_I. 1 hit.
PS50862. AA_TRNA_LIGASE_II. 1 hit.
PS00762. WHEP_TRS_1. 2 hits.
PS51185. WHEP_TRS_2. 3 hits.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: C57BL/6J.
  2. "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].
    Strain: C57BL/6 and FVB/N.
    Tissue: Eye and Mammary tumor.
  3. "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] OF 1-962.
    Strain: C57BL/6J.
    Tissue: Pancreas.
  4. "M.musculus mRNA for glutamyl-tRNA synthetase."
    Knippers R.
    Submitted (JUL-1990) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 406-1512.
  5. "Immunoaffinity profiling of tyrosine phosphorylation in cancer cells."
    Rush J., Moritz A., Lee K.A., Guo A., Goss V.L., Spek E.J., Zhang H., Zha X.-M., Polakiewicz R.D., Comb M.J.
    Nat. Biotechnol. 23:94-101(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  6. "Heterotrimeric GAIT complex drives transcript-selective translation inhibition in murine macrophages."
    Arif A., Chatterjee P., Moodt R.A., Fox P.L.
    Mol. Cell. Biol. 32:5046-5055(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, PHOSPHORYLATION AT SER-999, SUBUNIT, RECONSTITUTION OF THE GAIT COMPLEX, MUTAGENESIS OF SER-999.
  7. "SIRT5-mediated lysine desuccinylation impacts diverse metabolic pathways."
    Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y., Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.
    Mol. Cell 50:919-930(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-300; LYS-788 AND LYS-861, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Embryonic fibroblast.

Entry informationi

Entry nameiSYEP_MOUSE
AccessioniPrimary (citable) accession number: Q8CGC7
Secondary accession number(s): E9QKC4, Q3UFJ2, Q4VC16
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 19, 2004
Last sequence update: July 27, 2011
Last modified: November 26, 2014
This is version 106 of the entry and version 4 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Multifunctional enzyme, 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. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3