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Protein

Alanyl-tRNA editing protein Aarsd1

Gene

Aarsd1

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

Functioni

Functions in trans to edit the amino acid moiety from incorrectly charged Ser-tRNA(Ala).1 Publication

Cofactori

Zn2+CuratedNote: Binds 1 zinc ion per subunit.Curated

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi109 – 1091ZincSequence analysis
Metal bindingi113 – 1131ZincSequence analysis
Metal bindingi209 – 2091ZincSequence analysis
Metal bindingi213 – 2131ZincSequence analysis

GO - Molecular functioni

  • alanine-tRNA ligase activity Source: InterPro
  • aminoacyl-tRNA editing activity Source: UniProtKB
  • ATP binding Source: InterPro
  • metal ion binding Source: UniProtKB-KW
  • nucleic acid binding Source: InterPro
  • Ser-tRNA(Ala) hydrolase activity Source: MGI

GO - Biological processi

  • alanyl-tRNA aminoacylation Source: InterPro
  • regulation of translational fidelity Source: MGI
Complete GO annotation...

Keywords - Biological processi

Protein biosynthesis

Keywords - Ligandi

Metal-binding, Zinc

Names & Taxonomyi

Protein namesi
Recommended name:
Alanyl-tRNA editing protein Aarsd1
Alternative name(s):
Alanyl-tRNA deacylase alaX
Short name:
AlaX
Short name:
AlaXp-II
Alanyl-tRNA synthetase domain-containing protein 1
Gene namesi
Name:Aarsd1
Synonyms:Alax
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 11

Organism-specific databases

MGIiMGI:1916934. Aarsd1.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 412412Alanyl-tRNA editing protein Aarsd1PRO_0000277466Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei174 – 1741PhosphoserineBy similarity

Keywords - PTMi

Phosphoprotein

Proteomic databases

EPDiQ3THG9.
MaxQBiQ3THG9.
PaxDbiQ3THG9.
PRIDEiQ3THG9.

PTM databases

iPTMnetiQ3THG9.
PhosphoSiteiQ3THG9.

Expressioni

Gene expression databases

BgeeiQ3THG9.
CleanExiMM_AARSD1.
GenevisibleiQ3THG9. MM.

Interactioni

Binary interactionsi

WithEntry#Exp.IntActNotes
Irak1Q62406-14EBI-646572,EBI-488313

Protein-protein interaction databases

IntActiQ3THG9. 2 interactions.
MINTiMINT-4387552.
STRINGi10090.ENSMUSP00000067912.

Structurei

3D structure databases

ProteinModelPortaliQ3THG9.
SMRiQ3THG9. Positions 8-406.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

eggNOGiKOG2105. Eukaryota.
COG2872. LUCA.
GeneTreeiENSGT00510000046493.
HOGENOMiHOG000230967.
HOVERGENiHBG080017.
InParanoidiQ3THG9.
KOiK07050.
OrthoDBiEOG71RXJT.
PhylomeDBiQ3THG9.
TreeFamiTF323735.

Family and domain databases

InterProiIPR018165. Ala-tRNA-synth_IIc_core.
IPR018164. Ala-tRNA-synth_IIc_N.
IPR018163. Thr/Ala-tRNA-synth_IIc_edit.
IPR009000. Transl_B-barrel.
IPR012947. tRNA_SAD.
[Graphical view]
PfamiPF01411. tRNA-synt_2c. 1 hit.
PF07973. tRNA_SAD. 1 hit.
[Graphical view]
SMARTiSM00863. tRNA_SAD. 1 hit.
[Graphical view]
SUPFAMiSSF50447. SSF50447. 1 hit.
SSF55186. SSF55186. 1 hit.
PROSITEiPS50860. AA_TRNA_LIGASE_II_ALA. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q3THG9-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAFLCQRDSY AREFTTTVVS CSPAELQTDA SGGKKEVLSG FHVVLEDTLL
60 70 80 90 100
FPEGGGQPDD RGTINDISVL RVTRRGAQAD HFTESPLSPG SQVQVRVDWE
110 120 130 140 150
RRFDHMQQHS GQHLITAVAD LLFGLKTTSW ELGRLRSVIE LDSPSVTAEQ
160 170 180 190 200
VAAIEQSVNQ KIRDRLPVSV RELSLDDPEV EQVRGRGLPD DHAGPIRVVT
210 220 230 240 250
IEGVDSNMCC GTHVSNLSDL QVIKILGTEK GKKNKSNLIF LAGNRVLKWM
260 270 280 290 300
ERSHGSEKAL TSLLKCGVED HVEAVKKLQN ATKLLQKNNL NLLRDLAVHT
310 320 330 340 350
AHSLRSSPAW GGVVTLHRKE GDSEFMNIIA NEIGSEETLL FLTVGDEKGA
360 370 380 390 400
GLFLLAGPAE AVETLGPRVA EVLEGKGAGK KGRFQGKATK MSRRAEAQAL
410
LQDYVSTQSA EE
Length:412
Mass (Da):44,971
Last modified:February 6, 2007 - v2
Checksum:i3FFD32304A379B44
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti80 – 801D → G in BAE22937 (PubMed:16141072).Curated
Sequence conflicti175 – 1751L → M in BAE40227 (PubMed:16141072).Curated
Sequence conflicti292 – 2921L → H in BAE22937 (PubMed:16141072).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK078016 mRNA. Translation: BAC37098.1.
AK136332 mRNA. Translation: BAE22937.1.
AK168281 mRNA. Translation: BAE40227.1.
BC005711 mRNA. Translation: AAH05711.1.
CCDSiCCDS25467.1.
RefSeqiNP_659078.1. NM_144829.1.
UniGeneiMm.146283.

Genome annotation databases

EnsembliENSMUST00000070395; ENSMUSP00000067912; ENSMUSG00000075528.
GeneIDi69684.
KEGGimmu:69684.
UCSCiuc007los.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK078016 mRNA. Translation: BAC37098.1.
AK136332 mRNA. Translation: BAE22937.1.
AK168281 mRNA. Translation: BAE40227.1.
BC005711 mRNA. Translation: AAH05711.1.
CCDSiCCDS25467.1.
RefSeqiNP_659078.1. NM_144829.1.
UniGeneiMm.146283.

3D structure databases

ProteinModelPortaliQ3THG9.
SMRiQ3THG9. Positions 8-406.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiQ3THG9. 2 interactions.
MINTiMINT-4387552.
STRINGi10090.ENSMUSP00000067912.

PTM databases

iPTMnetiQ3THG9.
PhosphoSiteiQ3THG9.

Proteomic databases

EPDiQ3THG9.
MaxQBiQ3THG9.
PaxDbiQ3THG9.
PRIDEiQ3THG9.

Protocols and materials databases

DNASUi69684.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000070395; ENSMUSP00000067912; ENSMUSG00000075528.
GeneIDi69684.
KEGGimmu:69684.
UCSCiuc007los.1. mouse.

Organism-specific databases

CTDi80755.
MGIiMGI:1916934. Aarsd1.

Phylogenomic databases

eggNOGiKOG2105. Eukaryota.
COG2872. LUCA.
GeneTreeiENSGT00510000046493.
HOGENOMiHOG000230967.
HOVERGENiHBG080017.
InParanoidiQ3THG9.
KOiK07050.
OrthoDBiEOG71RXJT.
PhylomeDBiQ3THG9.
TreeFamiTF323735.

Miscellaneous databases

ChiTaRSiAarsd1. mouse.
PROiQ3THG9.
SOURCEiSearch...

Gene expression databases

BgeeiQ3THG9.
CleanExiMM_AARSD1.
GenevisibleiQ3THG9. MM.

Family and domain databases

InterProiIPR018165. Ala-tRNA-synth_IIc_core.
IPR018164. Ala-tRNA-synth_IIc_N.
IPR018163. Thr/Ala-tRNA-synth_IIc_edit.
IPR009000. Transl_B-barrel.
IPR012947. tRNA_SAD.
[Graphical view]
PfamiPF01411. tRNA-synt_2c. 1 hit.
PF07973. tRNA_SAD. 1 hit.
[Graphical view]
SMARTiSM00863. tRNA_SAD. 1 hit.
[Graphical view]
SUPFAMiSSF50447. SSF50447. 1 hit.
SSF55186. SSF55186. 1 hit.
PROSITEiPS50860. AA_TRNA_LIGASE_II_ALA. 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: BALB/cJ and C57BL/6J.
    Tissue: Embryonic head and Embryonic testis.
  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: FVB/N.
    Tissue: Mammary gland.
  3. "Distinct domains of tRNA synthetase recognize the same base pair."
    Beebe K., Mock M., Merriman E., Schimmel P.
    Nature 451:90-93(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION AS TRNA(ALA) EDITING PROTEIN.
  4. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Brain, Kidney, Pancreas, Spleen and Testis.

Entry informationi

Entry nameiAASD1_MOUSE
AccessioniPrimary (citable) accession number: Q3THG9
Secondary accession number(s): Q3UWH8, Q8BVJ6, Q99JS9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 6, 2007
Last sequence update: February 6, 2007
Last modified: June 8, 2016
This is version 89 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. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. 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.