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Reviewed, UniProtKB/Swiss-Prot Q96EY9 (ADAT3_HUMAN)

Last modified November 24, 2009. Version 53. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    tRNA-specific adenosine deaminase-like protein 3
Alternative name(s):
    tRNA-specific adenosine-34 deaminase subunit ADAT3
Gene names
Name: ADAT3
OrganismHomo sapiens (Human) [Complete proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length351 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceEvidence at protein level.

General annotation (Comments)

Function

May be involved in deamination of adenosine-34 to inosine in many tRNAs as a regulatory subunit Potential.

Cofactor

Zinc By similarity.

Post-translational modification

Phosphorylated upon DNA damage, probably by ATM or ATR. Ref.2

Sequence similarities

Belongs to the cytidine and deoxycytidylate deaminase family. ADAT3 subfamily.

Caution

Val-225 is present instead of the conserved Glu which is an active site in the cytidine and deoxycytidylate deaminase family of enzymes. It is suggested that this protein may act as a regulatory subunit.

Ontologies

Keywords
   Biological processtRNA processing
   Coding sequence diversityPolymorphism
   LigandMetal-binding
Zinc
   PTMAcetylation
Phosphoprotein
   Technical termComplete proteome
Gene Ontology (GO)
   Biological processtRNA processing

Inferred from electronic annotation. Source: UniProtKB-KW

   Molecular functionhydrolase activity

Inferred from electronic annotation. Source: InterPro

zinc ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 351351tRNA-specific adenosine deaminase-like protein 3
PRO_0000287658

Sites

Metal binding2231Zinc By similarity
Metal binding2911Zinc By similarity
Metal binding2941Zinc By similarity

Amino acid modifications

Modified residue11N-acetylmethionine
Modified residue1671Phosphothreonine Ref.2

Natural variations

Natural variant3321R → C in a breast cancer sample; somatic mutation. Ref.5
VAR_035804

Sequences

Sequence LengthMass (Da)Tools
Q96EY9-1 [UniParc].

Last modified December 1, 2001. Version 1.
Checksum: 6CE25F534BBE92F9

FASTA35138,071
        10         20         30         40         50         60 
MEPAPGLVEQ PKCLEAGSPE PEPAPWQALP VLSEKQSGDV ELVLAYAAPV LDKRQTSRLL 

        70         80         90        100        110        120 
KEVSALHPLP AQPHLKRVRP SRDAGSPHAL EMLLCLAGPA SGPRSLAELL PRPAVDPRGL 

       130        140        150        160        170        180 
GQPFLVPVPA RPPLTRGQFE EARAHWPTSF HEDKQVTSAL AGRLFSTQER AAMQSHMERA 

       190        200        210        220        230        240 
VWAARRAAAR GLRAVGAVVV DPASDRVLAT GHDCSCADNP LLHAVMVCVD LVARGQGRGT 

       250        260        270        280        290        300 
YDFRPFPACS FAPAAAPQAV RAGAVRKLDA DEDGLPYLCT GYDLYVTREP CAMCAMALVH 

       310        320        330        340        350 
ARILRVFYGA PSPDGALGTR FRIHARPDLN HRFQVFRGVL EEQCRWLDPD T 

« Hide

References

[1]"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: 15489334] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Skin.
[2]"ATM and ATR substrate analysis reveals extensive protein networks responsive to DNA damage."
Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III, Hurov K.E., Luo J., Bakalarski C.E., Zhao Z., Solimini N., Lerenthal Y., Shiloh Y., Gygi S.P., Elledge S.J.
Science 316:1160-1166(2007) [PubMed: 17525332] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-167, MASS SPECTROMETRY.
[3]Colinge J., Superti-Furga G., Bennett K.L.
Submitted (OCT-2008) to UniProtKB
Cited for: IDENTIFICATION [LARGE SCALE ANALYSIS], MASS SPECTROMETRY.
[4]"Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
Anal. Chem. 81:4493-4501(2009) [PubMed: 19413330] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, MASS SPECTROMETRY.
[5]"The consensus coding sequences of human breast and colorectal cancers."
Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D., Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., Buckhaults P., Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V. expand/collapse author list , Gazdar A.F., Hartigan J., Wu L., Liu C., Parmigiani G., Park B.H., Bachman K.E., Papadopoulos N., Vogelstein B., Kinzler K.W., Velculescu V.E.
Science 314:268-274(2006) [PubMed: 16959974] [Abstract]
Cited for: VARIANT [LARGE SCALE ANALYSIS] CYS-332.

Cross-references

Sequence databases

BC011824 mRNA. Translation: AAH11824.1.
IPIIPI00061802.
RefSeqNP_612431.1.
UniGeneHs.144980

3D structure databases

HSSPHSSP built from PDB template 2A8N based on UniProtKB Q8UHJ4.
ModBaseSearch...

Protein-protein interaction databases

STRINGQ96EY9.

PTM databases

PhosphoSiteQ96EY9.

Proteomic databases

PRIDEQ96EY9.

Genome annotation databases

EnsemblENST00000329478; ENSP00000332448; ENSG00000213638; Homo sapiens. [Genome view]
GeneID113179.
KEGGhsa:113179.
NMPDRfig|9606.3.peg.15306.
UCSCuc002luh.1. human.

Organism-specific databases

CTD113179.
GeneCardsGC19P001865.
HGNCHGNC:25151. ADAT3.
GenAtlasSearch...

Phylogenomic databases

HOGENOMQ96EY9.
HOVERGENQ96EY9.
OMAPLLHATM
OrthoDBEOG9NW25Q

Gene expression databases

ArrayExpressQ96EY9.
BgeeQ96EY9.
GenevestigatorQ96EY9.

Family and domain databases

InterProIPR002125. CMP_dCMP_Zn_bd.
IPR016193. Cytidine_deaminase-like.
[Graphical view]
PfamPF00383. dCMP_cyt_deam_1. 1 hit.
[Graphical view]
PROSITEPS00903. CYT_DCMP_DEAMINASES. False negative.
[Graphical view]
ProtoNetSearch...

Other Resources

NextBio78777.

Entry information

Entry nameADAT3_HUMAN
AccessionPrimary (citable) accession number: Q96EY9
Entry history
Integrated into UniProtKB/Swiss-Prot: May 15, 2007
Last sequence update: December 1, 2001
Last modified: November 24, 2009
This is version 53 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHPI (Human Proteome Initiative)
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.

Relevant documents

Human chromosome 19

Human chromosome 19: entries, gene names and cross-references to MIM

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents