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Protein

tRNA-specific adenosine deaminase 2

Gene

ADAT2

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Probably participates in deamination of adenosine-34 to inosine in many tRNAs.By similarity

Cofactori

Zn2+By similarity

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi71 – 711Zinc; catalytic1 Publication
Active sitei73 – 731Proton donorBy similarity
Metal bindingi107 – 1071Zinc; catalytic1 Publication
Metal bindingi110 – 1101Zinc; catalytic1 Publication

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Hydrolase

Keywords - Biological processi

tRNA processing

Keywords - Ligandi

Metal-binding, Zinc

Enzyme and pathway databases

ReactomeiR-HSA-6782315. tRNA modification in the nucleus and cytosol.

Names & Taxonomyi

Protein namesi
Recommended name:
tRNA-specific adenosine deaminase 2 (EC:3.5.4.-)
Alternative name(s):
Deaminase domain-containing protein 1
tRNA-specific adenosine-34 deaminase subunit ADAT2
Gene namesi
Name:ADAT2
Synonyms:DEADC1
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 6

Organism-specific databases

HGNCiHGNC:21172. ADAT2.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA162375592.

Polymorphism and mutation databases

BioMutaiADAT2.
DMDMi74750199.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 191191tRNA-specific adenosine deaminase 2PRO_0000287653Add
BLAST

Proteomic databases

EPDiQ7Z6V5.
MaxQBiQ7Z6V5.
PaxDbiQ7Z6V5.
PRIDEiQ7Z6V5.

Expressioni

Gene expression databases

BgeeiQ7Z6V5.
CleanExiHS_ADAT2.
GenevisibleiQ7Z6V5. HS.

Organism-specific databases

HPAiHPA035479.

Interactioni

Binary interactionsi

WithEntry#Exp.IntActNotes
NAV2Q8IVL13EBI-2809203,EBI-741200

Protein-protein interaction databases

BioGridi126410. 3 interactions.
IntActiQ7Z6V5. 2 interactions.
STRINGi9606.ENSP00000237283.

Structurei

Secondary structure

1
191
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi20 – 3819Combined sources
Beta strandi45 – 506Combined sources
Beta strandi53 – 597Combined sources
Helixi62 – 654Combined sources
Helixi72 – 8716Combined sources
Helixi91 – 955Combined sources
Beta strandi98 – 1047Combined sources
Helixi108 – 11710Combined sources
Beta strandi121 – 1266Combined sources
Turni129 – 1313Combined sources
Beta strandi153 – 1553Combined sources
Helixi160 – 17011Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3DH1X-ray2.80A/B/C/D20-185[»]
ProteinModelPortaliQ7Z6V5.
SMRiQ7Z6V5. Positions 18-173.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ7Z6V5.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini20 – 145126CMP/dCMP-type deaminasePROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Contains 1 CMP/dCMP-type deaminase domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiKOG1018. Eukaryota.
COG0590. LUCA.
GeneTreeiENSGT00390000000280.
HOGENOMiHOG000085051.
HOVERGENiHBG055246.
InParanoidiQ7Z6V5.
KOiK15441.
OMAiMEEAMQM.
PhylomeDBiQ7Z6V5.
TreeFamiTF313782.

Family and domain databases

HAMAPiMF_00972. tRNA_aden_deaminase.
InterProiIPR016192. APOBEC/CMP_deaminase_Zn-bd.
IPR002125. CMP_dCMP_Zn-bd.
IPR016193. Cytidine_deaminase-like.
IPR028883. tRNA_aden_deaminase.
[Graphical view]
PfamiPF14437. MafB19-deam. 1 hit.
[Graphical view]
SUPFAMiSSF53927. SSF53927. 1 hit.
PROSITEiPS00903. CYT_DCMP_DEAMINASES_1. 1 hit.
PS51747. CYT_DCMP_DEAMINASES_2. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q7Z6V5-1) [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
MEAKAAPKPA ASGACSVSAE ETEKWMEEAM HMAKEALENT EVPVGCLMVY
60 70 80 90 100
NNEVVGKGRN EVNQTKNATR HAEMVAIDQV LDWCRQSGKS PSEVFEHTVL
110 120 130 140 150
YVTVEPCIMC AAALRLMKIP LVVYGCQNER FGGCGSVLNI ASADLPNTGR
160 170 180 190
PFQCIPGYRA EEAVEMLKTF YKQENPNAPK SKVRKKECQK S
Length:191
Mass (Da):21,046
Last modified:October 1, 2003 - v1
Checksum:i7F2881A100A1782E
GO
Isoform 2 (identifier: Q7Z6V5-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-47: Missing.

Show »
Length:144
Mass (Da):16,100
Checksum:i4A697F09E3651358
GO

Sequence cautioni

The sequence AAH37955.2 differs from that shown. Reason: Erroneous initiation. Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 4747Missing in isoform 2. 2 PublicationsVSP_025582Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK126201 mRNA. Translation: BAG54295.1.
BX538182 mRNA. Translation: CAD98054.1.
AL031320 Genomic DNA. Translation: CAD92490.1.
CH471051 Genomic DNA. Translation: EAW47868.1.
BC037955 mRNA. Translation: AAH37955.2. Different initiation.
CCDSiCCDS43511.1. [Q7Z6V5-1]
CCDS69219.1. [Q7Z6V5-2]
RefSeqiNP_001273188.1. NM_001286259.1. [Q7Z6V5-2]
NP_872309.2. NM_182503.2. [Q7Z6V5-1]
XP_011533742.1. XM_011535440.1. [Q7Z6V5-2]
XP_011533743.1. XM_011535441.1. [Q7Z6V5-2]
XP_011533744.1. XM_011535442.1. [Q7Z6V5-2]
XP_011533746.1. XM_011535444.1. [Q7Z6V5-2]
UniGeneiHs.709561.

Genome annotation databases

EnsembliENST00000237283; ENSP00000237283; ENSG00000189007. [Q7Z6V5-1]
ENST00000606514; ENSP00000475651; ENSG00000189007. [Q7Z6V5-2]
GeneIDi134637.
KEGGihsa:134637.
UCSCiuc003qjj.4. human. [Q7Z6V5-1]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK126201 mRNA. Translation: BAG54295.1.
BX538182 mRNA. Translation: CAD98054.1.
AL031320 Genomic DNA. Translation: CAD92490.1.
CH471051 Genomic DNA. Translation: EAW47868.1.
BC037955 mRNA. Translation: AAH37955.2. Different initiation.
CCDSiCCDS43511.1. [Q7Z6V5-1]
CCDS69219.1. [Q7Z6V5-2]
RefSeqiNP_001273188.1. NM_001286259.1. [Q7Z6V5-2]
NP_872309.2. NM_182503.2. [Q7Z6V5-1]
XP_011533742.1. XM_011535440.1. [Q7Z6V5-2]
XP_011533743.1. XM_011535441.1. [Q7Z6V5-2]
XP_011533744.1. XM_011535442.1. [Q7Z6V5-2]
XP_011533746.1. XM_011535444.1. [Q7Z6V5-2]
UniGeneiHs.709561.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3DH1X-ray2.80A/B/C/D20-185[»]
ProteinModelPortaliQ7Z6V5.
SMRiQ7Z6V5. Positions 18-173.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi126410. 3 interactions.
IntActiQ7Z6V5. 2 interactions.
STRINGi9606.ENSP00000237283.

Polymorphism and mutation databases

BioMutaiADAT2.
DMDMi74750199.

Proteomic databases

EPDiQ7Z6V5.
MaxQBiQ7Z6V5.
PaxDbiQ7Z6V5.
PRIDEiQ7Z6V5.

Protocols and materials databases

DNASUi134637.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000237283; ENSP00000237283; ENSG00000189007. [Q7Z6V5-1]
ENST00000606514; ENSP00000475651; ENSG00000189007. [Q7Z6V5-2]
GeneIDi134637.
KEGGihsa:134637.
UCSCiuc003qjj.4. human. [Q7Z6V5-1]

Organism-specific databases

CTDi134637.
GeneCardsiADAT2.
H-InvDBHIX0025050.
HGNCiHGNC:21172. ADAT2.
HPAiHPA035479.
MIMi615388. gene.
neXtProtiNX_Q7Z6V5.
PharmGKBiPA162375592.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG1018. Eukaryota.
COG0590. LUCA.
GeneTreeiENSGT00390000000280.
HOGENOMiHOG000085051.
HOVERGENiHBG055246.
InParanoidiQ7Z6V5.
KOiK15441.
OMAiMEEAMQM.
PhylomeDBiQ7Z6V5.
TreeFamiTF313782.

Enzyme and pathway databases

ReactomeiR-HSA-6782315. tRNA modification in the nucleus and cytosol.

Miscellaneous databases

ChiTaRSiADAT2. human.
EvolutionaryTraceiQ7Z6V5.
GenomeRNAii134637.
NextBioi83413.
PROiQ7Z6V5.
SOURCEiSearch...

Gene expression databases

BgeeiQ7Z6V5.
CleanExiHS_ADAT2.
GenevisibleiQ7Z6V5. HS.

Family and domain databases

HAMAPiMF_00972. tRNA_aden_deaminase.
InterProiIPR016192. APOBEC/CMP_deaminase_Zn-bd.
IPR002125. CMP_dCMP_Zn-bd.
IPR016193. Cytidine_deaminase-like.
IPR028883. tRNA_aden_deaminase.
[Graphical view]
PfamiPF14437. MafB19-deam. 1 hit.
[Graphical view]
SUPFAMiSSF53927. SSF53927. 1 hit.
PROSITEiPS00903. CYT_DCMP_DEAMINASES_1. 1 hit.
PS51747. CYT_DCMP_DEAMINASES_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
    Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
    , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
    Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
    Tissue: Thymus.
  2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
    Tissue: Esophageal carcinoma.
  3. "The DNA sequence and analysis of human chromosome 6."
    Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L., Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., Gilbert J.G.R., Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D., Andrews T.D.
    , Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H., Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J., Brown J.Y., Burford D.C., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V., Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J., Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., Ellington A.E., Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J., French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J., Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C., Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A., Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R., Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M., Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A., Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L., Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I., Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y., Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E., Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A., Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W., Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M., West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J., Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M., Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I., Rogers J., Beck S.
    Nature 425:805-811(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  5. "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] OF 3-191 (ISOFORM 1).
    Tissue: Duodenum.
  6. "RNA editing by adenosine deaminases generates RNA and protein diversity."
    Schaub M., Keller W.
    Biochimie 84:791-803(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION.
  7. "Crystal structure of human tRNA-specific adenosine-34 deaminase subunit ADAT2."
    Structural genomics consortium (SGC)
    Submitted (FEB-2009) to the PDB data bank
    Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 20-185 IN COMPLEX WITH ZINC IONS.

Entry informationi

Entry nameiADAT2_HUMAN
AccessioniPrimary (citable) accession number: Q7Z6V5
Secondary accession number(s): A6NL12
, B3KWY3, Q7Z327, Q8IY39
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 15, 2007
Last sequence update: October 1, 2003
Last modified: May 11, 2016
This is version 106 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 6
    Human chromosome 6: entries, gene names and cross-references to MIM
  2. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. 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.