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Q8TEA8 (DTD1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 109. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
D-tyrosyl-tRNA(Tyr) deacylase 1

EC=3.1.-.-
Alternative name(s):
DNA-unwinding element-binding protein B
Short name=DUE-B
Histidyl-tRNA synthase-related
Gene names
Name:DTD1
Synonyms:C20orf88, DUEB, HARS2
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length209 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

ATPase involved in DNA replication, may facilitate loading of CDC45 onto pre-replication complexes. May hydrolyze D-tyrosyl-tRNA(Tyr) into D-tyrosine and free tRNA(Tyr), a possible defense mechanism against a harmful effect of D-tyrosine. Ref.6 Ref.11

Subunit structure

Homodimer. Interacts with CDC45 and TOPBP1. Ref.11 Ref.16

Subcellular location

Nucleus. Cytoplasm Potential. Note: Associated with chromatin at some replication origins containing functional DNA-unwinding elements. Ref.6 Ref.11

Tissue specificity

Expressed in many adult and fetal tissues. Highest levels in testis, ovary, spleen and in adult and fetal brain. Ref.1

Post-translational modification

Preferentially phosphorylated in cells arrested early in S phase. Phosphorylation in the C-terminus weakens the interaction with CDC45. Ref.6 Ref.11

Sequence similarities

Belongs to the DTD family.

Sequence caution

The sequence BAB85044.1 differs from that shown. Reason: Presence of Alu-repeat DNA.

Ontologies

Keywords
   Biological processDNA replication
   Cellular componentCytoplasm
Nucleus
   LigandDNA-binding
Metal-binding
   Molecular functionHydrolase
   PTMPhosphoprotein
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processD-amino acid catabolic process

Inferred from electronic annotation. Source: InterPro

DNA replication

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular_componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

nucleus

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionDNA binding

Inferred from electronic annotation. Source: UniProtKB-KW

hydrolase activity, acting on ester bonds

Inferred from electronic annotation. Source: InterPro

metal ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 209209D-tyrosyl-tRNA(Tyr) deacylase 1 HAMAP-Rule MF_00518
PRO_0000164626

Sites

Active site811Nucleophile By similarity
Metal binding41Magnesium; via carbonyl oxygen
Metal binding61Magnesium
Metal binding281Magnesium; via carbonyl oxygen

Amino acid modifications

Modified residue1971Phosphoserine Ref.8 Ref.10 Ref.14
Modified residue2051Phosphoserine Ref.8 Ref.10

Experimental info

Sequence conflict941H → N in AAH45167. Ref.5
Sequence conflict1341H → R in AAL57046. Ref.1

Secondary structure

...................... 209
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q8TEA8 [UniParc].

Last modified March 28, 2003. Version 2.
Checksum: F006ED14974ACC92

FASTA20923,424
        10         20         30         40         50         60 
MKAVVQRVTR ASVTVGGEQI SAIGRGICVL LGISLEDTQK ELEHMVRKIL NLRVFEDESG 

        70         80         90        100        110        120 
KHWSKSVMDK QYEILCVSQF TLQCVLKGNK PDFHLAMPTE QAEGFYNSFL EQLRKTYRPE 

       130        140        150        160        170        180 
LIKDGKFGAY MQVHIQNDGP VTIELESPAP GTATSDPKQL SKLEKQQQRK EKTRAKGPSE 

       190        200 
SSKERNTPRK EDRSASSGAE GDVSSEREP 

« Hide

References

« Hide 'large scale' references
[1]"Cloning and identification of a novel cDNA which may be associated with FKBP25."
Meng X.X., Chen J.J., Yang Q.Q., Wang S., Chao Y., Ying K., Xie Y., Mao Y.
Biochem. Genet. 40:303-310(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY.
Tissue: Fetal brain.
[2]"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. expand/collapse author list , 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].
Tissue: Brain and Hepatoma.
[3]"The DNA sequence and comparative analysis of human chromosome 20."
Deloukas P., Matthews L.H., Ashurst J.L., Burton J., Gilbert J.G.R., Jones M., Stavrides G., Almeida J.P., Babbage A.K., Bagguley C.L., Bailey J., Barlow K.F., Bates K.N., Beard L.M., Beare D.M., Beasley O.P., Bird C.P., Blakey S.E. expand/collapse author list , Bridgeman A.M., Brown A.J., Buck D., Burrill W.D., Butler A.P., Carder C., Carter N.P., Chapman J.C., Clamp M., Clark G., Clark L.N., Clark S.Y., Clee C.M., Clegg S., Cobley V.E., Collier R.E., Connor R.E., Corby N.R., Coulson A., Coville G.J., Deadman R., Dhami P.D., Dunn M., Ellington A.G., Frankland J.A., Fraser A., French L., Garner P., Grafham D.V., Griffiths C., Griffiths M.N.D., Gwilliam R., Hall R.E., Hammond S., Harley J.L., Heath P.D., Ho S., Holden J.L., Howden P.J., Huckle E., Hunt A.R., Hunt S.E., Jekosch K., Johnson C.M., Johnson D., Kay M.P., Kimberley A.M., King A., Knights A., Laird G.K., Lawlor S., Lehvaeslaiho M.H., Leversha M.A., Lloyd C., Lloyd D.M., Lovell J.D., Marsh V.L., Martin S.L., McConnachie L.J., McLay K., McMurray A.A., Milne S.A., Mistry D., Moore M.J.F., Mullikin J.C., Nickerson T., Oliver K., Parker A., Patel R., Pearce T.A.V., Peck A.I., Phillimore B.J.C.T., Prathalingam S.R., Plumb R.W., Ramsay H., Rice C.M., Ross M.T., Scott C.E., Sehra H.K., Shownkeen R., Sims S., Skuce C.D., Smith M.L., Soderlund C., Steward C.A., Sulston J.E., Swann R.M., Sycamore N., Taylor R., Tee L., Thomas D.W., Thorpe A., Tracey A., Tromans A.C., Vaudin M., Wall M., Wallis J.M., Whitehead S.L., Whittaker P., Willey D.L., Williams L., Williams S.A., Wilming L., Wray P.W., Hubbard T., Durbin R.M., Bentley D.R., Beck S., Rogers J.
Nature 414:865-871(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[4]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases
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].
Tissue: Brain and Skin.
[6]"The c-myc DNA-unwinding element-binding protein modulates the assembly of DNA replication complexes in vitro."
Casper J.M., Kemp M.G., Ghosh M., Randall G.M., Vaillant A., Leffak M.
J. Biol. Chem. 280:13071-13083(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, PHOSPHORYLATION, SUBCELLULAR LOCATION.
[7]"Phosphoproteome of resting human platelets."
Zahedi R.P., Lewandrowski U., Wiesner J., Wortelkamp S., Moebius J., Schuetz C., Walter U., Gambaryan S., Sickmann A.
J. Proteome Res. 7:526-534(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Platelet.
[8]"A quantitative atlas of mitotic phosphorylation."
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-197 AND SER-205, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[9]"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] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[10]"Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-197 AND SER-205, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Leukemic T-cell.
[11]"The DNA unwinding element binding protein DUE-B interacts with Cdc45 in preinitiation complex formation."
Chowdhury A., Liu G., Kemp M., Chen X., Katrangi N., Myers S., Ghosh M., Yao J., Gao Y., Bubulya P., Leffak M.
Mol. Cell. Biol. 30:1495-1507(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, SUBCELLULAR LOCATION, PHOSPHORYLATION, INTERACTION WITH CDC45 AND TOPBP1.
[12]"Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[13]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[14]"System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-197, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[15]"N-terminal acetylome analyses and functional insights of the N-terminal acetyltransferase NatB."
Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A., Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[16]"Structure and function of the c-myc DNA-unwinding element-binding protein DUE-B."
Kemp M., Bae B., Yu J.P., Ghosh M., Leffak M., Nair S.K.
J. Biol. Chem. 282:10441-10448(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS), SUBUNIT, MAGNESIUM-BINDING SITES.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF332356 mRNA. Translation: AAL57046.1.
AK074304 mRNA. Translation: BAB85044.1. Sequence problems.
AK291440 mRNA. Translation: BAF84129.1.
AL121900, AL121780 Genomic DNA. Translation: CAH73147.1.
AL121780, AL121900 Genomic DNA. Translation: CAI15669.1.
CH471133 Genomic DNA. Translation: EAX10227.1.
BC000599 mRNA. No translation available.
CH471133 Genomic DNA. Translation: EAX10228.1.
BC045167 mRNA. Translation: AAH45167.1.
BC100923 mRNA. Translation: AAI00924.1.
BC100924 mRNA. Translation: AAI00925.1.
BC100925 mRNA. Translation: AAI00926.1.
CCDSCCDS13138.1.
RefSeqNP_543010.3. NM_080820.4.
UniGeneHs.659442.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2OKVX-ray2.00A/B/C/D1-209[»]
ProteinModelPortalQ8TEA8.
SMRQ8TEA8. Positions 1-150.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid124965. 7 interactions.
IntActQ8TEA8. 1 interaction.
STRING9606.ENSP00000366672.

PTM databases

PhosphoSiteQ8TEA8.

Polymorphism databases

DMDM29427856.

Proteomic databases

MaxQBQ8TEA8.
PaxDbQ8TEA8.
PeptideAtlasQ8TEA8.
PRIDEQ8TEA8.

Protocols and materials databases

DNASU92675.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000377452; ENSP00000366672; ENSG00000125821.
GeneID92675.
KEGGhsa:92675.
UCSCuc002wrf.4. human.

Organism-specific databases

CTD92675.
GeneCardsGC20P018568.
HGNCHGNC:16219. DTD1.
HPAHPA040981.
HPA042653.
MIM610996. gene.
neXtProtNX_Q8TEA8.
PharmGKBPA162384107.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG1490.
HOVERGENHBG039436.
InParanoidQ8TEA8.
KOK07560.
OMAGDENDKM.
OrthoDBEOG7SR4P0.
PhylomeDBQ8TEA8.
TreeFamTF314886.

Gene expression databases

BgeeQ8TEA8.
CleanExHS_DTD1.
HS_HARS2.
GenevestigatorQ8TEA8.

Family and domain databases

Gene3D3.50.80.10. 1 hit.
HAMAPMF_00518. Tyr_Deacylase_Dtd.
InterProIPR023509. DTD-like_dom.
IPR003732. DTyrtRNA_deacyls.
[Graphical view]
PANTHERPTHR10472. PTHR10472. 1 hit.
PfamPF02580. Tyr_Deacylase. 1 hit.
[Graphical view]
SUPFAMSSF69500. SSF69500. 1 hit.
TIGRFAMsTIGR00256. TIGR00256. 1 hit.
ProtoNetSearch...

Other

ChiTaRSDTD1. human.
EvolutionaryTraceQ8TEA8.
GenomeRNAi92675.
NextBio77831.
PROQ8TEA8.
SOURCESearch...

Entry information

Entry nameDTD1_HUMAN
AccessionPrimary (citable) accession number: Q8TEA8
Secondary accession number(s): A8K5X5 expand/collapse secondary AC list , D3DW37, Q496D1, Q5W184, Q8WXU8, Q9BW67, Q9H464, Q9H474
Entry history
Integrated into UniProtKB/Swiss-Prot: March 28, 2003
Last sequence update: March 28, 2003
Last modified: July 9, 2014
This is version 109 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human chromosome 20

Human chromosome 20: entries, gene names and cross-references to MIM