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Q8BMJ2

- SYLC_MOUSE

UniProt

Q8BMJ2 - SYLC_MOUSE

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Protein
Leucine--tRNA ligase, cytoplasmic
Gene
Lars
Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 3 out of 5 - Experimental evidence at protein leveli

Functioni

Catalytic activityi

ATP + L-leucine + tRNA(Leu) = AMP + diphosphate + L-leucyl-tRNA(Leu).

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei721 – 7211ATP By similarity

GO - Molecular functioni

  1. ATP binding Source: UniProtKB-KW
  2. aminoacyl-tRNA editing activity Source: InterPro
  3. leucine-tRNA ligase activity Source: UniProtKB-EC

GO - Biological processi

  1. leucyl-tRNA aminoacylation Source: InterPro
Complete GO annotation...

Keywords - Molecular functioni

Aminoacyl-tRNA synthetase, Ligase

Keywords - Biological processi

Protein biosynthesis

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Leucine--tRNA ligase, cytoplasmic (EC:6.1.1.4)
Alternative name(s):
Leucyl-tRNA synthetase
Short name:
LeuRS
Gene namesi
Name:Lars
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Chromosome 18

Organism-specific databases

MGIiMGI:1913808. Lars.

Subcellular locationi

Cytoplasm By similarity

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 11781178Leucine--tRNA ligase, cytoplasmic
PRO_0000152151Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei972 – 9721N6-acetyllysine1 Publication
Modified residuei1049 – 10491N6-acetyllysine1 Publication

Keywords - PTMi

Acetylation

Proteomic databases

MaxQBiQ8BMJ2.
PaxDbiQ8BMJ2.
PRIDEiQ8BMJ2.

PTM databases

PhosphoSiteiQ8BMJ2.

Expressioni

Gene expression databases

ArrayExpressiQ8BMJ2.
BgeeiQ8BMJ2.
CleanExiMM_LARS.
GenevestigatoriQ8BMJ2.

Interactioni

Protein-protein interaction databases

BioGridi223191. 2 interactions.
IntActiQ8BMJ2. 1 interaction.
MINTiMINT-1848936.

Structurei

3D structure databases

ProteinModelPortaliQ8BMJ2.
SMRiQ8BMJ2. Positions 13-930.

Family & Domainsi

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi55 – 6511"HIGH" region
Add
BLAST
Motifi718 – 7225"KMSKS" region

Sequence similaritiesi

Phylogenomic databases

eggNOGiCOG0495.
GeneTreeiENSGT00390000012163.
HOVERGENiHBG055325.
InParanoidiQ8BMJ2.
KOiK01869.
OMAiYEGVMLV.
OrthoDBiEOG7VB2DJ.
PhylomeDBiQ8BMJ2.
TreeFamiTF105718.

Family and domain databases

Gene3Di1.10.730.10. 1 hit.
3.40.50.620. 3 hits.
3.90.740.10. 1 hit.
InterProiIPR001412. aa-tRNA-synth_I_CS.
IPR002300. aa-tRNA-synth_Ia.
IPR004493. Leu-tRNA-synth_Ia_arc/euk.
IPR014729. Rossmann-like_a/b/a_fold.
IPR009080. tRNAsynth_1a_anticodon-bd.
IPR013155. V/L/I-tRNA-synth_anticodon-bd.
IPR009008. Val/Leu/Ile-tRNA-synth_edit.
[Graphical view]
PfamiPF08264. Anticodon_1. 1 hit.
PF00133. tRNA-synt_1. 2 hits.
[Graphical view]
SUPFAMiSSF47323. SSF47323. 1 hit.
SSF50677. SSF50677. 2 hits.
TIGRFAMsiTIGR00395. leuS_arch. 1 hit.
PROSITEiPS00178. AA_TRNA_LIGASE_I. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q8BMJ2-1 [UniParc]FASTAAdd to Basket

« Hide

MAGRKGTAKV DFLKEIEKEA QQKWEAEKVF EVSASRLEKQ KQSSKGKYFV     50
TFPYPYMNGR LHLGHTFSLS KCEFAVGYQR LKGKSCLFPF GLHCTGMPIK 100
ACADKLKREI ELYGCPPDFP EEEEEEEESS AKPGDIVVRD KAKGKKSKAA 150
AKAGSSKYQW DIMKSLGLSD DDIVKFSEAE HWLDYFPPLA VQDLKTIGLK 200
VDWRRSFITT DVNPYYDSFV RWQFLTLRER NKIKFGKRYT IYSPKDGQPC 250
MDHDRQTGEG VGPQEYTLVK LKVLEPYPSK LSGLKGKNIF LVAATLRPET 300
MFGQTNCWVR PDMKYIGFET ANGDIFICTQ RAARNMSYQG FTKHNGVVPV 350
VKELMGEEIL GASLSAPLTC YKVVYVLPML TIKEDKGTGV VTSVPSDSPD 400
DLAALRDLKK KQALRTKFGI RDDMVLPFEP VPVLEIPGIG NLPAVTVCDE 450
LKIQSQNDRE KLAEAKEKLY LRGFYDGVML VDGFKGQKIQ HVKKTIQKNM 500
IDAGDALIYM EPEKQVMSRS ADECVVALCD QWYLDYGDEN WKKQTFQCLK 550
NMETFCEESR KNFEASLDWL QEHACSRTYG LGTRLPWDEQ WLIESLSDST 600
IYMAFYTVAH LLQGGDLNGQ AESPLGIRPQ QMTKDVWDYV FFKDAPFPKT 650
QIPKEKLDQL KQEFEFWYPV DLRASGKDLI PNHLSYYIYN HVAMWPEQSD 700
KWPVSVRANG HLLLNSEKMS KSTGNFLTLS QAVDKFSADG MRLALADAGD 750
TVEDANFVEA MADAGILRLY TWVEWVKEML ASCSSLRSGP ADSFNDRVFA 800
SEMNAGIIKT DQNYEKMMFK EALKTGFFEF QAAKDKYREL ATEGMHRELV 850
FRFIEVQTIL LTPFCPHLCE HIWTLLGKPD SIMHASWPVA GPVDESLIRS 900
SQYLMEVAHD LRLRLKNYMM PAKGKKTDKQ PAQRPSHCTI YVAKNYPVWQ 950
HITLTTLRSH FEANNGKLPD NKVIASELGS LPELKKYMKK VMPFVAMIKE 1000
NMEKKGPRVL DLELEFDEQA VLMENIVYLT NSLELEHIEV KFASEAEDKV 1050
REECCPGKPL NVFRTEPGVP VSLVNPQPSS GHFSTKIDIR QGDSCESIIR 1100
RLMKTDRGIK DLSKVKLMRF DDPLLGPRRV PVLGREHSEK TLISENAVFH 1150
VDLVSKKVHL TENGLRTDIG DTMVYLVH 1178
Length:1,178
Mass (Da):134,192
Last modified:June 7, 2004 - v2
Checksum:i1186583D5237FFC1
GO

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti218 – 2181S → P in BAC33766. 1 Publication
Sequence conflicti869 – 8691C → S in BAC33766. 1 Publication
Sequence conflicti954 – 9541L → Q in BAC27133. 1 Publication
Sequence conflicti1127 – 11271P → H in BAC27133. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AK030778 mRNA. Translation: BAC27133.1.
AK049472 mRNA. Translation: BAC33766.1.
CCDSiCCDS37796.1.
RefSeqiNP_598898.2. NM_134137.2.
UniGeneiMm.312170.

Genome annotation databases

EnsembliENSMUST00000097590; ENSMUSP00000095197; ENSMUSG00000024493.
GeneIDi107045.
KEGGimmu:107045.
UCSCiuc008etp.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AK030778 mRNA. Translation: BAC27133.1 .
AK049472 mRNA. Translation: BAC33766.1 .
CCDSi CCDS37796.1.
RefSeqi NP_598898.2. NM_134137.2.
UniGenei Mm.312170.

3D structure databases

ProteinModelPortali Q8BMJ2.
SMRi Q8BMJ2. Positions 13-930.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 223191. 2 interactions.
IntActi Q8BMJ2. 1 interaction.
MINTi MINT-1848936.

PTM databases

PhosphoSitei Q8BMJ2.

Proteomic databases

MaxQBi Q8BMJ2.
PaxDbi Q8BMJ2.
PRIDEi Q8BMJ2.

Protocols and materials databases

DNASUi 107045.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSMUST00000097590 ; ENSMUSP00000095197 ; ENSMUSG00000024493 .
GeneIDi 107045.
KEGGi mmu:107045.
UCSCi uc008etp.1. mouse.

Organism-specific databases

CTDi 51520.
MGIi MGI:1913808. Lars.

Phylogenomic databases

eggNOGi COG0495.
GeneTreei ENSGT00390000012163.
HOVERGENi HBG055325.
InParanoidi Q8BMJ2.
KOi K01869.
OMAi YEGVMLV.
OrthoDBi EOG7VB2DJ.
PhylomeDBi Q8BMJ2.
TreeFami TF105718.

Miscellaneous databases

ChiTaRSi LARS. mouse.
NextBioi 358546.
PROi Q8BMJ2.
SOURCEi Search...

Gene expression databases

ArrayExpressi Q8BMJ2.
Bgeei Q8BMJ2.
CleanExi MM_LARS.
Genevestigatori Q8BMJ2.

Family and domain databases

Gene3Di 1.10.730.10. 1 hit.
3.40.50.620. 3 hits.
3.90.740.10. 1 hit.
InterProi IPR001412. aa-tRNA-synth_I_CS.
IPR002300. aa-tRNA-synth_Ia.
IPR004493. Leu-tRNA-synth_Ia_arc/euk.
IPR014729. Rossmann-like_a/b/a_fold.
IPR009080. tRNAsynth_1a_anticodon-bd.
IPR013155. V/L/I-tRNA-synth_anticodon-bd.
IPR009008. Val/Leu/Ile-tRNA-synth_edit.
[Graphical view ]
Pfami PF08264. Anticodon_1. 1 hit.
PF00133. tRNA-synt_1. 2 hits.
[Graphical view ]
SUPFAMi SSF47323. SSF47323. 1 hit.
SSF50677. SSF50677. 2 hits.
TIGRFAMsi TIGR00395. leuS_arch. 1 hit.
PROSITEi PS00178. AA_TRNA_LIGASE_I. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

  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.
  2. "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-972 AND LYS-1049, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Embryonic fibroblast.

Entry informationi

Entry nameiSYLC_MOUSE
AccessioniPrimary (citable) accession number: Q8BMJ2
Secondary accession number(s): Q8BKW9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 7, 2004
Last sequence update: June 7, 2004
Last modified: July 9, 2014
This is version 95 of the entry and version 2 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. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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