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Protein

tRNA-specific adenosine deaminase 1

Gene

Adat1

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

Functioni

Specifically deaminates adenosine-37 to inosine in tRNA-Ala.1 Publication

Catalytic activityi

Adenine(37) in tRNA(Ala) + H2O = hypoxanthine(37) in tRNA(Ala) + NH3.1 Publication

Cofactori

1D-myo-inositol hexakisphosphateBy similarityNote: Binds 1 myo-inositol hexakisphosphate (IP6) per subunit.By similarity

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi87 – 871ZincPROSITE-ProRule annotation
Active sitei89 – 891Proton donorPROSITE-ProRule annotation
Binding sitei93 – 931Inositol hexakisphosphateBy similarity
Binding sitei94 – 941Inositol hexakisphosphateBy similarity
Metal bindingi142 – 1421ZincPROSITE-ProRule annotation
Metal bindingi294 – 2941ZincPROSITE-ProRule annotation
Binding sitei297 – 2971Inositol hexakisphosphateBy similarity
Binding sitei300 – 3001Inositol hexakisphosphateBy similarity
Binding sitei430 – 4301Inositol hexakisphosphateBy similarity
Binding sitei466 – 4661Inositol hexakisphosphateBy similarity

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Hydrolase

Keywords - Biological processi

tRNA processing

Keywords - Ligandi

Metal-binding, Zinc

Names & Taxonomyi

Protein namesi
Recommended name:
tRNA-specific adenosine deaminase 1 (EC:3.5.4.34)
Short name:
mADAT1
Alternative name(s):
tRNA-specific adenosine-37 deaminase
Gene namesi
Name:Adat1
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 8

Organism-specific databases

MGIiMGI:1353631. Adat1.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 499499tRNA-specific adenosine deaminase 1PRO_0000287648Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei191 – 1911PhosphoserineCombined sources

Keywords - PTMi

Phosphoprotein

Proteomic databases

EPDiQ9JHI2.
MaxQBiQ9JHI2.
PaxDbiQ9JHI2.
PeptideAtlasiQ9JHI2.
PRIDEiQ9JHI2.

PTM databases

iPTMnetiQ9JHI2.
PhosphoSiteiQ9JHI2.

Expressioni

Gene expression databases

BgeeiQ9JHI2.
CleanExiMM_ADAT1.
ExpressionAtlasiQ9JHI2. baseline and differential.
GenevisibleiQ9JHI2. MM.

Interactioni

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000034427.

Structurei

3D structure databases

ProteinModelPortaliQ9JHI2.
SMRiQ9JHI2. Positions 60-147, 285-498.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini63 – 498436A to I editasePROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Belongs to the ADAT1 family.Curated
Contains 1 A to I editase domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiKOG2777. Eukaryota.
ENOG410XT0Z. LUCA.
GeneTreeiENSGT00550000074412.
HOGENOMiHOG000237320.
HOVERGENiHBG059724.
InParanoidiQ9JHI2.
KOiK15440.
OMAiMRKNGDI.
OrthoDBiEOG7NKKK6.
PhylomeDBiQ9JHI2.
TreeFamiTF315806.

Family and domain databases

InterProiIPR002466. A_deamin.
[Graphical view]
PfamiPF02137. A_deamin. 1 hit.
[Graphical view]
SMARTiSM00552. ADEAMc. 1 hit.
[Graphical view]
PROSITEiPS50141. A_DEAMIN_EDITASE. 1 hit.
[Graphical view]

Sequences (3)i

Sequence statusi: Complete.

This entry describes 3 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q9JHI2-1) [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
MWTADEIAQL CYAHYNVRLP KQGKPEPNRE WTLLAAVVKI QASANQACDI
60 70 80 90 100
PEKEVQVTKE VVSMGTGTKC IGQSKMRESG DILNDSHAEI IARRSFQRYL
110 120 130 140 150
LHQLHLAAVL KEDSIFVPGT QRGLWRLRPD LSFVFFSSHT PCGDASIIPM
160 170 180 190 200
LEFEEQPCCP VIRSWANNSP VQETENLEDS KDKRNCEDPA SPVAKKMRLG
210 220 230 240 250
TPARSLSNCV AHHGTQESGP VKPDVSSSDL TKEEPDAANG IASGSFRVVD
260 270 280 290 300
VYRTGAKCVP GETGDLREPG AAYHQVGLLR VKPGRGDRTC SMSCSDKMAR
310 320 330 340 350
WNVLGCQGAL LMHFLEKPIY LSAVVIGKCP YSQEAMRRAL TGRCEETLVL
360 370 380 390 400
PRGFGVQELE IQQSGLLFEQ SRCAVHRKRG DSPGRLVPCG AAISWSAVPQ
410 420 430 440 450
QPLDVTANGF PQGTTKKEIG SPRARSRISK VELFRSFQKL LSSIADDEQP
460 470 480 490
DSIRVTKKLD TYQEYKDAAS AYQEAWGALR RIQPFASWIR NPPDYHQFK
Length:499
Mass (Da):55,355
Last modified:October 1, 2000 - v1
Checksum:i8080BD40C1EE5E71
GO
Isoform 2 (identifier: Q9JHI2-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     455-499: Missing.

Show »
Length:454
Mass (Da):49,984
Checksum:i92AF500A9DE3D8A9
GO
Isoform 3 (identifier: Q9JHI2-3) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     343-424: Missing.
     455-499: Missing.

Note: No experimental confirmation available.
Show »
Length:372
Mass (Da):41,143
Checksum:iE5C257214B3A6AA3
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti201 – 2011T → A in BAE36167 (PubMed:16141072).Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei343 – 42482Missing in isoform 3. CuratedVSP_025580Add
BLAST
Alternative sequencei455 – 49945Missing in isoform 2 and isoform 3. 2 PublicationsVSP_025581Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF192375 mRNA. Translation: AAF36820.1.
AF192374
, AF192367, AF192368, AF192369, AF192370, AF192371, AF192372, AF192373 Genomic DNA. Translation: AAF36821.1.
AK035614 mRNA. Translation: BAC29125.1.
AK039699 mRNA. Translation: BAC30422.1.
AK082399 mRNA. Translation: BAC38487.1.
AK161044 mRNA. Translation: BAE36167.1.
BC019976 mRNA. Translation: AAH19976.1.
CCDSiCCDS22684.1. [Q9JHI2-1]
RefSeqiNP_038953.1. NM_013925.4. [Q9JHI2-1]
UniGeneiMm.282162.

Genome annotation databases

EnsembliENSMUST00000034427; ENSMUSP00000034427; ENSMUSG00000031949. [Q9JHI2-1]
ENSMUST00000139820; ENSMUSP00000117279; ENSMUSG00000031949. [Q9JHI2-2]
GeneIDi30947.
KEGGimmu:30947.
UCSCiuc009nnc.1. mouse. [Q9JHI2-1]
uc012gkz.1. mouse. [Q9JHI2-3]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF192375 mRNA. Translation: AAF36820.1.
AF192374
, AF192367, AF192368, AF192369, AF192370, AF192371, AF192372, AF192373 Genomic DNA. Translation: AAF36821.1.
AK035614 mRNA. Translation: BAC29125.1.
AK039699 mRNA. Translation: BAC30422.1.
AK082399 mRNA. Translation: BAC38487.1.
AK161044 mRNA. Translation: BAE36167.1.
BC019976 mRNA. Translation: AAH19976.1.
CCDSiCCDS22684.1. [Q9JHI2-1]
RefSeqiNP_038953.1. NM_013925.4. [Q9JHI2-1]
UniGeneiMm.282162.

3D structure databases

ProteinModelPortaliQ9JHI2.
SMRiQ9JHI2. Positions 60-147, 285-498.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000034427.

PTM databases

iPTMnetiQ9JHI2.
PhosphoSiteiQ9JHI2.

Proteomic databases

EPDiQ9JHI2.
MaxQBiQ9JHI2.
PaxDbiQ9JHI2.
PeptideAtlasiQ9JHI2.
PRIDEiQ9JHI2.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000034427; ENSMUSP00000034427; ENSMUSG00000031949. [Q9JHI2-1]
ENSMUST00000139820; ENSMUSP00000117279; ENSMUSG00000031949. [Q9JHI2-2]
GeneIDi30947.
KEGGimmu:30947.
UCSCiuc009nnc.1. mouse. [Q9JHI2-1]
uc012gkz.1. mouse. [Q9JHI2-3]

Organism-specific databases

CTDi23536.
MGIiMGI:1353631. Adat1.

Phylogenomic databases

eggNOGiKOG2777. Eukaryota.
ENOG410XT0Z. LUCA.
GeneTreeiENSGT00550000074412.
HOGENOMiHOG000237320.
HOVERGENiHBG059724.
InParanoidiQ9JHI2.
KOiK15440.
OMAiMRKNGDI.
OrthoDBiEOG7NKKK6.
PhylomeDBiQ9JHI2.
TreeFamiTF315806.

Miscellaneous databases

PROiQ9JHI2.
SOURCEiSearch...

Gene expression databases

BgeeiQ9JHI2.
CleanExiMM_ADAT1.
ExpressionAtlasiQ9JHI2. baseline and differential.
GenevisibleiQ9JHI2. MM.

Family and domain databases

InterProiIPR002466. A_deamin.
[Graphical view]
PfamiPF02137. A_deamin. 1 hit.
[Graphical view]
SMARTiSM00552. ADEAMc. 1 hit.
[Graphical view]
PROSITEiPS50141. A_DEAMIN_EDITASE. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Sequence, genomic organization and functional expression of the murine tRNA-specific adenosine deaminase ADAT1."
    Maas S., Kim Y.-G., Rich A.
    Gene 243:59-66(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORM 1), FUNCTION, ENZYME ACTIVITY.
    Strain: 129/Sv.
  2. "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] (ISOFORMS 1 AND 2).
    Strain: C57BL/6J.
    Tissue: Cerebellum, Skin, Spinal cord and Urinary bladder.
  3. "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] (ISOFORM 2).
    Strain: FVB/N.
    Tissue: Mammary tumor.
  4. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-191, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  5. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-191, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver and Pancreas.

Entry informationi

Entry nameiADAT1_MOUSE
AccessioniPrimary (citable) accession number: Q9JHI2
Secondary accession number(s): Q3TU04, Q8CBP0, Q8VE23
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 15, 2007
Last sequence update: October 1, 2000
Last modified: July 6, 2016
This is version 102 of the entry and version 1 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.