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Bifunctional glutamate/proline--tRNA ligase (Bifunctional aminoacyl-tRNA synthetase) [Includes: Glutamate--tRNA ligase (EC 6.1.1.17) (Glutamyl-tRNA synthetase) (GluRS); Proline--tRNA ligase (EC 6.1.1.15) (Prolyl-tRNA synthetase) (ProRS)]

 SYEP_MOUSE              Reviewed;        1512 AA.
Q8CGC7; E9QKC4; Q3UFJ2; Q4VC16;
19-JUL-2004, integrated into UniProtKB/Swiss-Prot.
27-JUL-2011, sequence version 4.
23-MAY-2018, entry version 136.
RecName: Full=Bifunctional glutamate/proline--tRNA ligase;
AltName: Full=Bifunctional aminoacyl-tRNA synthetase;
Includes:
RecName: Full=Glutamate--tRNA ligase;
EC=6.1.1.17;
AltName: Full=Glutamyl-tRNA synthetase;
Short=GluRS;
Includes:
RecName: Full=Proline--tRNA ligase;
EC=6.1.1.15 {ECO:0000250|UniProtKB:P07814};
AltName: Full=Prolyl-tRNA synthetase;
Short=ProRS;
Name=Eprs; Synonyms=Qprs;
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=C57BL/6J;
PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
Lindblad-Toh K., Eichler E.E., Ponting C.P.;
"Lineage-specific biology revealed by a finished genome assembly of
the mouse.";
PLoS Biol. 7:E1000112-E1000112(2009).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=C57BL/6J, and FVB/N; TISSUE=Eye, and Mammary tumor;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-962.
STRAIN=C57BL/6J; TISSUE=Pancreas;
PubMed=16141072; DOI=10.1126/science.1112014;
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.;
"The transcriptional landscape of the mammalian genome.";
Science 309:1559-1563(2005).
[4]
NUCLEOTIDE SEQUENCE [MRNA] OF 406-1512.
Knippers R.;
"M.musculus mRNA for glutamyl-tRNA synthetase.";
Submitted (JUL-1990) to the EMBL/GenBank/DDBJ databases.
[5]
SUBUNIT.
PubMed=12060739; DOI=10.1073/pnas.122110199;
Kim J.Y., Kang Y.-S., Lee J.-W., Kim H.J., Ahn Y.H., Park H.,
Ko Y.-G., Kim S.;
"p38 is essential for the assembly and stability of macromolecular
tRNA synthetase complex: implications for its physiological
significance.";
Proc. Natl. Acad. Sci. U.S.A. 99:7912-7916(2002).
[6]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=15592455; DOI=10.1038/nbt1046;
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.;
"Immunoaffinity profiling of tyrosine phosphorylation in cancer
cells.";
Nat. Biotechnol. 23:94-101(2005).
[7]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung,
Pancreas, Spleen, and Testis;
PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
"A tissue-specific atlas of mouse protein phosphorylation and
expression.";
Cell 143:1174-1189(2010).
[8]
FUNCTION, PHOSPHORYLATION AT SER-999, SUBUNIT, RECONSTITUTION OF THE
GAIT COMPLEX, AND MUTAGENESIS OF SER-999.
PubMed=23071094; DOI=10.1128/MCB.01168-12;
Arif A., Chatterjee P., Moodt R.A., Fox P.L.;
"Heterotrimeric GAIT complex drives transcript-selective translation
inhibition in murine macrophages.";
Mol. Cell. Biol. 32:5046-5055(2012).
[9]
ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-300; LYS-788 AND LYS-861,
AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Embryonic fibroblast;
PubMed=23806337; DOI=10.1016/j.molcel.2013.06.001;
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.;
"SIRT5-mediated lysine desuccinylation impacts diverse metabolic
pathways.";
Mol. Cell 50:919-930(2013).
[10]
FUNCTION, INTERACTION WITH SLC27A1, SUBCELLULAR LOCATION, TOPOLOGY,
PHOSPHORYLATION AT SER-999 BY RPS6KB1, AND MUTAGENESIS OF SER-999.
PubMed=28178239; DOI=10.1038/nature21380;
Arif A., Terenzi F., Potdar A.A., Jia J., Sacks J., China A.,
Halawani D., Vasu K., Li X., Brown J.M., Chen J., Kozma S.C.,
Thomas G., Fox P.L.;
"EPRS is a critical mTORC1-S6K1 effector that influences adiposity in
mice.";
Nature 542:357-361(2017).
-!- FUNCTION: Multifunctional protein which is primarily part of the
aminoacyl-tRNA synthetase multienzyme complex, also know as
multisynthetase complex, that 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). The
phosphorylation of EPRS, induced by interferon-gamma, dissociates
the protein from the aminoacyl-tRNA synthetase multienzyme complex
and recruits it to the GAIT complex that binds to stem loop-
containing GAIT elements in the 3'-UTR of diverse inflammatory
mRNAs (such as ceruplasmin), suppressing their translation.
Interferon-gamma can therefore redirect, in specific cells, the
EPRS function from protein synthesis to translation inhibition
(PubMed:23071094). Also functions as an effector of the mTORC1
signaling pathway by promoting, through SLC27A1, the uptake of
long-chain fatty acid by adipocytes. Thereby, it also plays a role
in fat metabolism and more indirectly influences lifespan
(PubMed:28178239). {ECO:0000250|UniProtKB:P07814,
ECO:0000269|PubMed:23071094, ECO:0000269|PubMed:28178239}.
-!- CATALYTIC ACTIVITY: ATP + L-glutamate + tRNA(Glu) = AMP +
diphosphate + L-glutamyl-tRNA(Glu).
-!- CATALYTIC ACTIVITY: ATP + L-proline + tRNA(Pro) = AMP +
diphosphate + L-prolyl-tRNA(Pro). {ECO:0000250|UniProtKB:P07814}.
-!- SUBUNIT: Homodimer. Part of the aminoacyl-tRNA synthetase
multienzyme complex, also know as multisynthetase complex, that is
composed of the tRNA ligases for Arg (RARS), Asp (DARS), Gln
(QARS), Ile (IARS), Leu (LARS), Lys (KARS), Met (MARS) the
bifunctional ligase for Glu and Pro (EPRS) and the auxiliary
subunits AIMP1/p43, AIMP2/p38 and EEF1E1/p18. Forms a linear
complex that contains MARS, EEF1E1, EPRS and AIMP2 that is at the
core of the multisubunit complex (PubMed:12060739). Interacts with
DUS2L (By similarity). Component of the GAIT complex which is
composed of EPRS, RPL13A and GAPDH (PubMed:23071094). Interacts
(phosphorylated at Ser-999) with SLC27A1; mediates the
translocation of SLC27A1 from the cytoplasm to the plasma membrane
thereby increasing the uptake of long-chain fatty acids
(PubMed:28178239). {ECO:0000250|UniProtKB:P07814,
ECO:0000269|PubMed:12060739, ECO:0000269|PubMed:23071094,
ECO:0000269|PubMed:28178239}.
-!- SUBCELLULAR LOCATION: Cytoplasm, cytosol
{ECO:0000250|UniProtKB:P07814}. Membrane
{ECO:0000269|PubMed:28178239}; Peripheral membrane protein
{ECO:0000305|PubMed:28178239}. Note=Translocates from cytosol to
membranes upon phosphorylation at Ser-999.
{ECO:0000305|PubMed:28178239}.
-!- DOMAIN: The WHEP-TRS domains are involved in RNA binding.
{ECO:0000250|UniProtKB:Q7SIA2}.
-!- PTM: Phosphorylated at Ser-999 by RPS6KB1; triggers EPRS release
from the aminoacyl-tRNA synthetase multienzyme complex. In
monocytes, the IFN-gamma-induced phosphorylation at Ser-999
releases EPRS from the aminoacyl-tRNA synthetase multienzyme
complex, allowing its association with the GAIT complex.
Phosphorylation at Ser-999 is specifically required for the
RPL13A-mediated interaction of the GAIT complex with eIF4G (By
similarity). Phosphorylation at Ser-999 by RPS6KB1, is also
induced by insulin through activation of the mTORC1 signaling
pathway and promotes the interaction of EPRS with SLC27A1
(PubMed:28178239). {ECO:0000250|UniProtKB:P07814,
ECO:0000269|PubMed:28178239}.
-!- SIMILARITY: In the N-terminal section; belongs to the class-I
aminoacyl-tRNA synthetase family. Glutamate--tRNA ligase type 2
subfamily. {ECO:0000305}.
-!- SIMILARITY: In the C-terminal section; belongs to the class-II
aminoacyl-tRNA synthetase family. {ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=AAH40802.1; Type=Miscellaneous discrepancy; Note=Contaminating sequence. Potential poly-A sequence.; Evidence={ECO:0000305};
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EMBL; AC129195; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AC131980; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; BC040802; AAH40802.1; ALT_SEQ; mRNA.
EMBL; BC094679; AAH94679.1; -; mRNA.
EMBL; AK148463; BAE28568.1; -; mRNA.
EMBL; X54327; -; NOT_ANNOTATED_CDS; mRNA.
CCDS; CCDS35818.1; -.
RefSeq; NP_084011.1; NM_029735.1.
UniGene; Mm.154511; -.
UniGene; Mm.490980; -.
ProteinModelPortal; Q8CGC7; -.
SMR; Q8CGC7; -.
BioGrid; 223350; 4.
IntAct; Q8CGC7; 7.
MINT; Q8CGC7; -.
STRING; 10090.ENSMUSP00000045841; -.
iPTMnet; Q8CGC7; -.
PhosphoSitePlus; Q8CGC7; -.
SwissPalm; Q8CGC7; -.
EPD; Q8CGC7; -.
MaxQB; Q8CGC7; -.
PaxDb; Q8CGC7; -.
PeptideAtlas; Q8CGC7; -.
PRIDE; Q8CGC7; -.
Ensembl; ENSMUST00000046514; ENSMUSP00000045841; ENSMUSG00000026615.
GeneID; 107508; -.
KEGG; mmu:107508; -.
UCSC; uc007dze.1; mouse.
CTD; 2058; -.
MGI; MGI:97838; Eprs.
eggNOG; KOG1147; Eukaryota.
eggNOG; KOG4163; Eukaryota.
eggNOG; COG0008; LUCA.
eggNOG; COG0442; LUCA.
GeneTree; ENSGT00550000074815; -.
HOGENOM; HOG000022047; -.
HOVERGEN; HBG017875; -.
InParanoid; Q8CGC7; -.
KO; K14163; -.
OMA; VAMLHIK; -.
OrthoDB; EOG091G04TK; -.
TreeFam; TF300380; -.
ChiTaRS; Eprs; mouse.
PRO; PR:Q8CGC7; -.
Proteomes; UP000000589; Chromosome 1.
Bgee; ENSMUSG00000026615; -.
CleanEx; MM_EPRS; -.
ExpressionAtlas; Q8CGC7; baseline and differential.
Genevisible; Q8CGC7; MM.
GO; GO:0017101; C:aminoacyl-tRNA synthetase multienzyme complex; IDA:UniProtKB.
GO; GO:0005737; C:cytoplasm; ISO:MGI.
GO; GO:0005829; C:cytosol; ISO:MGI.
GO; GO:0097452; C:GAIT complex; IDA:UniProtKB.
GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
GO; GO:1990904; C:ribonucleoprotein complex; IEA:Ensembl.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0004818; F:glutamate-tRNA ligase activity; IBA:GO_Central.
GO; GO:0051020; F:GTPase binding; ISO:MGI.
GO; GO:0042802; F:identical protein binding; ISO:MGI.
GO; GO:0004827; F:proline-tRNA ligase activity; IMP:CAFA.
GO; GO:0042803; F:protein homodimerization activity; ISO:MGI.
GO; GO:0035613; F:RNA stem-loop binding; ISS:UniProtKB.
GO; GO:0008270; F:zinc ion binding; ISS:UniProtKB.
GO; GO:0032869; P:cellular response to insulin stimulus; IMP:UniProtKB.
GO; GO:0071346; P:cellular response to interferon-gamma; IDA:UniProtKB.
GO; GO:0006424; P:glutamyl-tRNA aminoacylation; IBA:GO_Central.
GO; GO:0044539; P:long-chain fatty acid import; IMP:UniProtKB.
GO; GO:0017148; P:negative regulation of translation; IDA:UniProtKB.
GO; GO:0006433; P:prolyl-tRNA aminoacylation; IDA:CAFA.
CDD; cd00778; ProRS_core_arch_euk; 1.
Gene3D; 2.40.240.10; -; 3.
Gene3D; 3.30.110.30; -; 1.
Gene3D; 3.40.50.620; -; 1.
Gene3D; 3.40.50.800; -; 1.
HAMAP; MF_02076; Glu_tRNA_synth_type2; 1.
HAMAP; MF_01571; Pro_tRNA_synth_type3; 1.
InterPro; IPR002314; aa-tRNA-synt_IIb.
InterPro; IPR001412; aa-tRNA-synth_I_CS.
InterPro; IPR006195; aa-tRNA-synth_II.
InterPro; IPR004154; Anticodon-bd.
InterPro; IPR036621; Anticodon-bd_dom_sf.
InterPro; IPR004526; Glu-tRNA-synth_arc/euk.
InterPro; IPR000924; Glu/Gln-tRNA-synth.
InterPro; IPR020058; Glu/Gln-tRNA-synth_Ib_cat-dom.
InterPro; IPR020059; Glu/Gln-tRNA-synth_Ib_codon-bd.
InterPro; IPR036282; Glutathione-S-Trfase_C_sf.
InterPro; IPR004046; GST_C.
InterPro; IPR004499; Pro-tRNA-ligase_IIa_arc-type.
InterPro; IPR016061; Pro-tRNA_ligase_II_C.
InterPro; IPR017449; Pro-tRNA_synth_II.
InterPro; IPR033721; ProRS_core_arch_euk.
InterPro; IPR020056; Rbsml_L25/Gln-tRNA_synth_N.
InterPro; IPR011035; Ribosomal_L25/Gln-tRNA_synth.
InterPro; IPR014729; Rossmann-like_a/b/a_fold.
InterPro; IPR009068; S15_NS1_RNA-bd.
InterPro; IPR000738; WHEP-TRS_dom.
Pfam; PF00043; GST_C; 1.
Pfam; PF03129; HGTP_anticodon; 1.
Pfam; PF09180; ProRS-C_1; 1.
Pfam; PF00749; tRNA-synt_1c; 1.
Pfam; PF03950; tRNA-synt_1c_C; 1.
Pfam; PF00587; tRNA-synt_2b; 1.
Pfam; PF00458; WHEP-TRS; 3.
PRINTS; PR00987; TRNASYNTHGLU.
SMART; SM00946; ProRS-C_1; 1.
SMART; SM00991; WHEP-TRS; 3.
SUPFAM; SSF47060; SSF47060; 3.
SUPFAM; SSF47616; SSF47616; 1.
SUPFAM; SSF50715; SSF50715; 1.
SUPFAM; SSF64586; SSF64586; 1.
TIGRFAMs; TIGR00463; gltX_arch; 1.
TIGRFAMs; TIGR00408; proS_fam_I; 1.
PROSITE; PS00178; AA_TRNA_LIGASE_I; 1.
PROSITE; PS50862; AA_TRNA_LIGASE_II; 1.
PROSITE; PS00762; WHEP_TRS_1; 2.
PROSITE; PS51185; WHEP_TRS_2; 3.
1: Evidence at protein level;
Acetylation; Aminoacyl-tRNA synthetase; ATP-binding;
Complete proteome; Cytoplasm; Ligase; Membrane; Metal-binding;
Methylation; Multifunctional enzyme; Nucleotide-binding;
Phosphoprotein; Protein biosynthesis; Reference proteome; Repeat;
RNA-binding; Translation regulation; Zinc.
CHAIN 1 1512 Bifunctional glutamate/proline--tRNA
ligase.
/FTId=PRO_0000119744.
DOMAIN 749 805 WHEP-TRS 1.
DOMAIN 822 878 WHEP-TRS 2.
DOMAIN 900 956 WHEP-TRS 3.
NP_BIND 432 436 ATP. {ECO:0000250}.
NP_BIND 1152 1154 ATP. {ECO:0000250|UniProtKB:P07814}.
NP_BIND 1163 1164 ATP. {ECO:0000250|UniProtKB:P07814}.
NP_BIND 1237 1240 ATP. {ECO:0000250|UniProtKB:P07814}.
REGION 164 759 Glutamate--tRNA ligase.
REGION 760 956 3 X 57 AA approximate repeats.
REGION 1007 1512 Proline--tRNA ligase.
REGION 1121 1123 L-proline binding.
{ECO:0000250|UniProtKB:P07814}.
MOTIF 204 214 "HIGH" region.
MOTIF 432 436 "KMSKS" region.
COMPBIAS 961 991 Lys-rich. {ECO:0000255|PROSITE-
ProRule:PRU00012}.
METAL 1448 1448 Zinc. {ECO:0000250|UniProtKB:P07814}.
METAL 1453 1453 Zinc. {ECO:0000250|UniProtKB:P07814}.
METAL 1495 1495 Zinc. {ECO:0000250|UniProtKB:P07814}.
METAL 1497 1497 Zinc. {ECO:0000250|UniProtKB:P07814}.
BINDING 211 211 ATP. {ECO:0000250}.
BINDING 398 398 ATP. {ECO:0000250}.
BINDING 1152 1152 L-proline.
{ECO:0000250|UniProtKB:P07814}.
BINDING 1242 1242 L-proline.
{ECO:0000250|UniProtKB:P07814}.
BINDING 1276 1276 ATP. {ECO:0000250|UniProtKB:P07814}.
MOD_RES 300 300 N6-acetyllysine; alternate.
{ECO:0000244|PubMed:23806337}.
MOD_RES 300 300 N6-malonyllysine; alternate.
{ECO:0000250|UniProtKB:P07814}.
MOD_RES 355 355 Phosphothreonine.
{ECO:0000250|UniProtKB:P07814}.
MOD_RES 417 417 N6-acetyllysine.
{ECO:0000250|UniProtKB:P07814}.
MOD_RES 434 434 Phosphoserine.
{ECO:0000250|UniProtKB:P07814}.
MOD_RES 498 498 N6-acetyllysine.
{ECO:0000250|UniProtKB:P07814}.
MOD_RES 535 535 N6-acetyllysine.
{ECO:0000250|UniProtKB:P07814}.
MOD_RES 542 542 N6-acetyllysine.
{ECO:0000250|UniProtKB:P07814}.
MOD_RES 637 637 N6-acetyllysine.
{ECO:0000250|UniProtKB:P07814}.
MOD_RES 788 788 N6-acetyllysine.
{ECO:0000244|PubMed:23806337}.
MOD_RES 861 861 N6-acetyllysine.
{ECO:0000244|PubMed:23806337}.
MOD_RES 872 872 Phosphotyrosine.
{ECO:0000250|UniProtKB:P07814}.
MOD_RES 885 885 Phosphoserine.
{ECO:0000250|UniProtKB:P07814}.
MOD_RES 998 998 Phosphoserine.
{ECO:0000250|UniProtKB:P07814}.
MOD_RES 999 999 Phosphoserine; by RPS6KB1.
{ECO:0000269|PubMed:23071094}.
MOD_RES 1152 1152 Omega-N-methylarginine.
{ECO:0000250|UniProtKB:P07814}.
MOD_RES 1350 1350 Phosphoserine.
{ECO:0000250|UniProtKB:P07814}.
MOD_RES 1503 1503 N6-acetyllysine.
{ECO:0000250|UniProtKB:P07814}.
MUTAGEN 999 999 S->A: Loss of function in translation
inhibition. Loss of interaction with
SLC27A1. Mutant mice have no apparent
developmental defect but display reduced
adiposity associated with decreased
insulin levels and adipocytes size. They
also display increased lipolysis and
fatty acid beta-oxidation and an extended
lifespan. Adipocytes display decreased
insulin-stimulated long-chain fatty acid
uptake. {ECO:0000269|PubMed:23071094,
ECO:0000269|PubMed:28178239}.
MUTAGEN 999 999 S->D: Constitutively active in
translation inhibition (phosphomimetic).
Mutant mice have no apparent
developmental defect and do not display
overt phenotype related to adiposity or
lifespan. {ECO:0000269|PubMed:23071094,
ECO:0000269|PubMed:28178239}.
CONFLICT 94 94 R -> G (in Ref. 2; AAH40802).
{ECO:0000305}.
CONFLICT 172 172 N -> S (in Ref. 2; AAH40802).
{ECO:0000305}.
CONFLICT 618 618 S -> P (in Ref. 2; AAH40802).
{ECO:0000305}.
CONFLICT 986 986 G -> R (in Ref. 4; X54327).
{ECO:0000305}.
CONFLICT 1290 1290 N -> S (in Ref. 2; AAH94679).
{ECO:0000305}.
SEQUENCE 1512 AA; 170079 MW; D14F6EA015B1BB6A CRC64;
MAALCLTVNA GNPPLEALLA VEHVKGDVSI SVEEGKENLL RVSETVAFTD VNSILRYLAR
IATTSGLYGT NLMEHTEIDH WLEFSATKLS SCDRLTSAIN ELNHCLSLRT YLVGNSLTLA
DLCVWATLKG SAAWQEHLKQ NKTLVHVKRW FGFLEAQQAF RSVGTKWDVS GNRATVAPDK
KQDVGKFVEL PGAEMGKVTV RFPPEASGYL HIGHAKAALL NQHYQVNFKG KLIMRFDDTN
PEKEKEDFEK VILEDVAMLH IKPDQFTYTS DHFETIMKYA EKLIQEGKAY VDDTPAEQMK
AEREQRTESK HRKNSVEKNL QMWEEMKKGS QFGQSCCLRA KIDMSSNNGC MRDPTLYRCK
IQPHPRTGNK YNVYPTYDFA CPIVDSIEGV THALRTTEYH DRDEQFYWII EALGIRKPYI
WEYSRLNLNN TVLSKRKLTW FVNEGLVDGW DDPRFPTVRG VLRRGMTVEG LKQFIAAQGS
SRSVVNMEWD KIWAFNKKVI DPVAPRYVAL LKKEVVPVNV LDAQEEMKEV ARHPKNPDVG
LKPVWYSPKV FIEGADAETF SEGEMVTFIN WGNINITKIH KNADGKITSL DAKLNLENKD
YKKTTKITWL AESTHALSIP AVCVTYEHLI TKPVLGKDED FKQYINKDSK HEELMLGDPC
LKDLKKGDII QLQRRGFFIC DQPYEPVSPY SCREAPCILI YIPDGHTKEM PTSGSKEKTK
VEISKKETSS APKERPAPAV SSTCATAEDS SVLYSRVAVQ GDVVRELKAK KAPKEDIDAA
VKQLLTLKAE YKEKTGQEYK PGNPSAAAVQ TVSTKSSSNT VESTSLYNKV AAQGEVVRKL
KAEKAPKAKV TEAVECLLSL KAEYKEKTGK DYVPGQPPAS QNSHSNPVSN AQPAGAEKPE
AKVLFDRVAC QGEVVRKLKA EKASKDQVDS AVQELLQLKA QYKSLTGIEY KPVSATGAED
KDKKKKEKEN KSEKQNKPQK QNDGQGKDSS KSQGSGLSSG GAGEGQGPKK QTRLGLEAKK
EENLAEWYSQ VITKSEMIEY YDVSGCYILR PWSYSIWESI KDFFDAEIKK LGVENCYFPI
FVSQAALEKE KNHIEDFAPE VAWVTRSGKT ELAEPIAIRP TSETVMYPAY AKWVQSHRDL
PVRLNQWCNV VRWEFKHPQP FLRTREFLWQ EGHSAFATFE EAADEVLQIL ELYARVYEEL
LAIPVVRGRK TEKEKFAGGD YTTTIEAFIS ASGRAIQGAT SHHLGQNFSK MCEIVFEDPK
TPGEKQFAYQ CSWGLTTRTI GVMVMVHGDN MGLVLPPRVA SVQVVVIPCG ITNALSEEDR
EALMAKCNEY RRRLLGANIR VRVDLRDNYS PGWKFNHWEL KGVPVRLEVG PRDMKSCQFV
AVRRDTGEKL TIAEKEAEAK LEKVLEDIQL NLFTRASEDL KTHMVVSNTL EDFQKVLDAG
KVAQIPFCGE IDCEDWIKKM TARDQDVEPG APSMGAKSLC IPFNPLCELQ PGAMCVCGKN
PAKFYTLFGR SY


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