Full text data of DTD1
DTD1
(C20orf88, DUEB, HARS2)
[Confidence: medium (present in either hRBCD or BSc_CH or PM22954596)]
D-tyrosyl-tRNA(Tyr) deacylase 1; 3.1.-.- (DNA-unwinding element-binding protein B; DUE-B; Histidyl-tRNA synthase-related)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
D-tyrosyl-tRNA(Tyr) deacylase 1; 3.1.-.- (DNA-unwinding element-binding protein B; DUE-B; Histidyl-tRNA synthase-related)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
UniProt
Q8TEA8
ID DTD1_HUMAN Reviewed; 209 AA.
AC Q8TEA8; A8K5X5; D3DW37; Q496D1; Q5W184; Q8WXU8; Q9BW67; Q9H464;
read moreAC Q9H474;
DT 28-MAR-2003, integrated into UniProtKB/Swiss-Prot.
DT 28-MAR-2003, sequence version 2.
DT 22-JAN-2014, entry version 104.
DE RecName: Full=D-tyrosyl-tRNA(Tyr) deacylase 1;
DE EC=3.1.-.-;
DE AltName: Full=DNA-unwinding element-binding protein B;
DE Short=DUE-B;
DE AltName: Full=Histidyl-tRNA synthase-related;
GN Name=DTD1; Synonyms=C20orf88, DUEB, HARS2;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
RC TISSUE=Fetal brain;
RX PubMed=12392168; DOI=10.1023/A:1020256718720;
RA Meng X.X., Chen J.J., Yang Q.Q., Wang S., Chao Y., Ying K., Xie Y.,
RA Mao Y.;
RT "Cloning and identification of a novel cDNA which may be associated
RT with FKBP25.";
RL Biochem. Genet. 40:303-310(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain, and Hepatoma;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=11780052; DOI=10.1038/414865a;
RA Deloukas P., Matthews L.H., Ashurst J.L., Burton J., Gilbert J.G.R.,
RA Jones M., Stavrides G., Almeida J.P., Babbage A.K., Bagguley C.L.,
RA Bailey J., Barlow K.F., Bates K.N., Beard L.M., Beare D.M.,
RA Beasley O.P., Bird C.P., Blakey S.E., Bridgeman A.M., Brown A.J.,
RA Buck D., Burrill W.D., Butler A.P., Carder C., Carter N.P.,
RA Chapman J.C., Clamp M., Clark G., Clark L.N., Clark S.Y., Clee C.M.,
RA Clegg S., Cobley V.E., Collier R.E., Connor R.E., Corby N.R.,
RA Coulson A., Coville G.J., Deadman R., Dhami P.D., Dunn M.,
RA Ellington A.G., Frankland J.A., Fraser A., French L., Garner P.,
RA Grafham D.V., Griffiths C., Griffiths M.N.D., Gwilliam R., Hall R.E.,
RA Hammond S., Harley J.L., Heath P.D., Ho S., Holden J.L., Howden P.J.,
RA Huckle E., Hunt A.R., Hunt S.E., Jekosch K., Johnson C.M., Johnson D.,
RA Kay M.P., Kimberley A.M., King A., Knights A., Laird G.K., Lawlor S.,
RA Lehvaeslaiho M.H., Leversha M.A., Lloyd C., Lloyd D.M., Lovell J.D.,
RA Marsh V.L., Martin S.L., McConnachie L.J., McLay K., McMurray A.A.,
RA Milne S.A., Mistry D., Moore M.J.F., Mullikin J.C., Nickerson T.,
RA Oliver K., Parker A., Patel R., Pearce T.A.V., Peck A.I.,
RA Phillimore B.J.C.T., Prathalingam S.R., Plumb R.W., Ramsay H.,
RA Rice C.M., Ross M.T., Scott C.E., Sehra H.K., Shownkeen R., Sims S.,
RA Skuce C.D., Smith M.L., Soderlund C., Steward C.A., Sulston J.E.,
RA Swann R.M., Sycamore N., Taylor R., Tee L., Thomas D.W., Thorpe A.,
RA Tracey A., Tromans A.C., Vaudin M., Wall M., Wallis J.M.,
RA Whitehead S.L., Whittaker P., Willey D.L., Williams L., Williams S.A.,
RA Wilming L., Wray P.W., Hubbard T., Durbin R.M., Bentley D.R., Beck S.,
RA Rogers J.;
RT "The DNA sequence and comparative analysis of human chromosome 20.";
RL Nature 414:865-871(2001).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain, and Skin;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [6]
RP FUNCTION, PHOSPHORYLATION, AND SUBCELLULAR LOCATION.
RX PubMed=15653697; DOI=10.1074/jbc.M404754200;
RA Casper J.M., Kemp M.G., Ghosh M., Randall G.M., Vaillant A.,
RA Leffak M.;
RT "The c-myc DNA-unwinding element-binding protein modulates the
RT assembly of DNA replication complexes in vitro.";
RL J. Biol. Chem. 280:13071-13083(2005).
RN [7]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Platelet;
RX PubMed=18088087; DOI=10.1021/pr0704130;
RA Zahedi R.P., Lewandrowski U., Wiesner J., Wortelkamp S., Moebius J.,
RA Schuetz C., Walter U., Gambaryan S., Sickmann A.;
RT "Phosphoproteome of resting human platelets.";
RL J. Proteome Res. 7:526-534(2008).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-197 AND SER-205, AND
RP MASS SPECTROMETRY.
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [9]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,
RA Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in
RT a refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-197 AND SER-205, AND
RP MASS SPECTROMETRY.
RC TISSUE=Leukemic T-cell;
RX PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA Rodionov V., Han D.K.;
RT "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT reveals system-wide modulation of protein-protein interactions.";
RL Sci. Signal. 2:RA46-RA46(2009).
RN [11]
RP FUNCTION, SUBCELLULAR LOCATION, PHOSPHORYLATION, AND INTERACTION WITH
RP CDC45 AND TOPBP1.
RX PubMed=20065034; DOI=10.1128/MCB.00710-09;
RA Chowdhury A., Liu G., Kemp M., Chen X., Katrangi N., Myers S.,
RA Ghosh M., Yao J., Gao Y., Bubulya P., Leffak M.;
RT "The DNA unwinding element binding protein DUE-B interacts with Cdc45
RT in preinitiation complex formation.";
RL Mol. Cell. Biol. 30:1495-1507(2010).
RN [12]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S.,
RA Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full
RT phosphorylation site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [13]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
RA Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [14]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-197, AND MASS
RP SPECTROMETRY.
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J.,
RA Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V.,
RA Blagoev B.;
RT "System-wide temporal characterization of the proteome and
RT phosphoproteome of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [15]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E.,
RA Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K.,
RA Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-
RT terminal acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN [16]
RP X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS), SUBUNIT, AND MAGNESIUM-BINDING
RP SITES.
RX PubMed=17264083; DOI=10.1074/jbc.M609632200;
RA Kemp M., Bae B., Yu J.P., Ghosh M., Leffak M., Nair S.K.;
RT "Structure and function of the c-myc DNA-unwinding element-binding
RT protein DUE-B.";
RL J. Biol. Chem. 282:10441-10448(2007).
CC -!- FUNCTION: ATPase involved in DNA replication, may facilitate
CC loading of CDC45 onto pre-replication complexes. May hydrolyze D-
CC tyrosyl-tRNA(Tyr) into D-tyrosine and free tRNA(Tyr), a possible
CC defense mechanism against a harmful effect of D-tyrosine.
CC -!- SUBUNIT: Homodimer. Interacts with CDC45 and TOPBP1.
CC -!- SUBCELLULAR LOCATION: Nucleus. Cytoplasm (Potential).
CC Note=Associated with chromatin at some replication origins
CC containing functional DNA-unwinding elements.
CC -!- TISSUE SPECIFICITY: Expressed in many adult and fetal tissues.
CC Highest levels in testis, ovary, spleen and in adult and fetal
CC brain.
CC -!- PTM: Preferentially phosphorylated in cells arrested early in S
CC phase. Phosphorylation in the C-terminus weakens the interaction
CC with CDC45.
CC -!- SIMILARITY: Belongs to the DTD family.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAB85044.1; Type=Miscellaneous discrepancy; Note=Presence of Alu-repeat DNA;
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DR EMBL; AF332356; AAL57046.1; -; mRNA.
DR EMBL; AK074304; BAB85044.1; ALT_SEQ; mRNA.
DR EMBL; AK291440; BAF84129.1; -; mRNA.
DR EMBL; AL121900; CAH73147.1; -; Genomic_DNA.
DR EMBL; AL121780; CAH73147.1; JOINED; Genomic_DNA.
DR EMBL; AL121780; CAI15669.1; -; Genomic_DNA.
DR EMBL; AL121900; CAI15669.1; JOINED; Genomic_DNA.
DR EMBL; CH471133; EAX10227.1; -; Genomic_DNA.
DR EMBL; BC000599; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; CH471133; EAX10228.1; -; Genomic_DNA.
DR EMBL; BC045167; AAH45167.1; -; mRNA.
DR EMBL; BC100923; AAI00924.1; -; mRNA.
DR EMBL; BC100924; AAI00925.1; -; mRNA.
DR EMBL; BC100925; AAI00926.1; -; mRNA.
DR RefSeq; NP_543010.3; NM_080820.4.
DR UniGene; Hs.659442; -.
DR PDB; 2OKV; X-ray; 2.00 A; A/B/C/D=1-209.
DR PDBsum; 2OKV; -.
DR ProteinModelPortal; Q8TEA8; -.
DR SMR; Q8TEA8; 1-150.
DR IntAct; Q8TEA8; 1.
DR STRING; 9606.ENSP00000366672; -.
DR PhosphoSite; Q8TEA8; -.
DR DMDM; 29427856; -.
DR PaxDb; Q8TEA8; -.
DR PeptideAtlas; Q8TEA8; -.
DR PRIDE; Q8TEA8; -.
DR DNASU; 92675; -.
DR Ensembl; ENST00000377452; ENSP00000366672; ENSG00000125821.
DR GeneID; 92675; -.
DR KEGG; hsa:92675; -.
DR UCSC; uc002wrf.4; human.
DR CTD; 92675; -.
DR GeneCards; GC20P018568; -.
DR HGNC; HGNC:16219; DTD1.
DR HPA; HPA040981; -.
DR MIM; 610996; gene.
DR neXtProt; NX_Q8TEA8; -.
DR PharmGKB; PA162384107; -.
DR eggNOG; COG1490; -.
DR HOVERGEN; HBG039436; -.
DR InParanoid; Q8TEA8; -.
DR KO; K07560; -.
DR OMA; DGPVTIW; -.
DR OrthoDB; EOG7SR4P0; -.
DR PhylomeDB; Q8TEA8; -.
DR ChiTaRS; DTD1; human.
DR EvolutionaryTrace; Q8TEA8; -.
DR GenomeRNAi; 92675; -.
DR NextBio; 77831; -.
DR PRO; PR:Q8TEA8; -.
DR Bgee; Q8TEA8; -.
DR CleanEx; HS_DTD1; -.
DR CleanEx; HS_HARS2; -.
DR Genevestigator; Q8TEA8; -.
DR GO; GO:0005737; C:cytoplasm; IDA:HPA.
DR GO; GO:0005730; C:nucleolus; IDA:HPA.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0016788; F:hydrolase activity, acting on ester bonds; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0019478; P:D-amino acid catabolic process; IEA:InterPro.
DR GO; GO:0006260; P:DNA replication; IEA:UniProtKB-KW.
DR Gene3D; 3.50.80.10; -; 1.
DR InterPro; IPR023509; DTD-like_dom.
DR InterPro; IPR003732; DTyrtRNA_deacyls.
DR PANTHER; PTHR10472; PTHR10472; 1.
DR Pfam; PF02580; Tyr_Deacylase; 1.
DR SUPFAM; SSF69500; SSF69500; 1.
DR TIGRFAMs; TIGR00256; TIGR00256; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Complete proteome; Cytoplasm; DNA replication;
KW DNA-binding; Hydrolase; Metal-binding; Nucleus; Phosphoprotein;
KW Reference proteome.
FT CHAIN 1 209 D-tyrosyl-tRNA(Tyr) deacylase 1.
FT /FTId=PRO_0000164626.
FT ACT_SITE 81 81 Nucleophile (By similarity).
FT METAL 4 4 Magnesium; via carbonyl oxygen.
FT METAL 6 6 Magnesium.
FT METAL 28 28 Magnesium; via carbonyl oxygen.
FT MOD_RES 197 197 Phosphoserine.
FT MOD_RES 205 205 Phosphoserine.
FT CONFLICT 94 94 H -> N (in Ref. 5; AAH45167).
FT CONFLICT 134 134 H -> R (in Ref. 1; AAL57046).
FT STRAND 2 15
FT STRAND 18 32
FT HELIX 39 51
FT HELIX 67 70
FT STRAND 73 78
FT HELIX 80 82
FT STRAND 87 90
FT HELIX 99 116
FT HELIX 119 121
FT STRAND 122 124
FT STRAND 131 146
SQ SEQUENCE 209 AA; 23424 MW; F006ED14974ACC92 CRC64;
MKAVVQRVTR ASVTVGGEQI SAIGRGICVL LGISLEDTQK ELEHMVRKIL NLRVFEDESG
KHWSKSVMDK QYEILCVSQF TLQCVLKGNK PDFHLAMPTE QAEGFYNSFL EQLRKTYRPE
LIKDGKFGAY MQVHIQNDGP VTIELESPAP GTATSDPKQL SKLEKQQQRK EKTRAKGPSE
SSKERNTPRK EDRSASSGAE GDVSSEREP
//
ID DTD1_HUMAN Reviewed; 209 AA.
AC Q8TEA8; A8K5X5; D3DW37; Q496D1; Q5W184; Q8WXU8; Q9BW67; Q9H464;
read moreAC Q9H474;
DT 28-MAR-2003, integrated into UniProtKB/Swiss-Prot.
DT 28-MAR-2003, sequence version 2.
DT 22-JAN-2014, entry version 104.
DE RecName: Full=D-tyrosyl-tRNA(Tyr) deacylase 1;
DE EC=3.1.-.-;
DE AltName: Full=DNA-unwinding element-binding protein B;
DE Short=DUE-B;
DE AltName: Full=Histidyl-tRNA synthase-related;
GN Name=DTD1; Synonyms=C20orf88, DUEB, HARS2;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
RC TISSUE=Fetal brain;
RX PubMed=12392168; DOI=10.1023/A:1020256718720;
RA Meng X.X., Chen J.J., Yang Q.Q., Wang S., Chao Y., Ying K., Xie Y.,
RA Mao Y.;
RT "Cloning and identification of a novel cDNA which may be associated
RT with FKBP25.";
RL Biochem. Genet. 40:303-310(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain, and Hepatoma;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=11780052; DOI=10.1038/414865a;
RA Deloukas P., Matthews L.H., Ashurst J.L., Burton J., Gilbert J.G.R.,
RA Jones M., Stavrides G., Almeida J.P., Babbage A.K., Bagguley C.L.,
RA Bailey J., Barlow K.F., Bates K.N., Beard L.M., Beare D.M.,
RA Beasley O.P., Bird C.P., Blakey S.E., Bridgeman A.M., Brown A.J.,
RA Buck D., Burrill W.D., Butler A.P., Carder C., Carter N.P.,
RA Chapman J.C., Clamp M., Clark G., Clark L.N., Clark S.Y., Clee C.M.,
RA Clegg S., Cobley V.E., Collier R.E., Connor R.E., Corby N.R.,
RA Coulson A., Coville G.J., Deadman R., Dhami P.D., Dunn M.,
RA Ellington A.G., Frankland J.A., Fraser A., French L., Garner P.,
RA Grafham D.V., Griffiths C., Griffiths M.N.D., Gwilliam R., Hall R.E.,
RA Hammond S., Harley J.L., Heath P.D., Ho S., Holden J.L., Howden P.J.,
RA Huckle E., Hunt A.R., Hunt S.E., Jekosch K., Johnson C.M., Johnson D.,
RA Kay M.P., Kimberley A.M., King A., Knights A., Laird G.K., Lawlor S.,
RA Lehvaeslaiho M.H., Leversha M.A., Lloyd C., Lloyd D.M., Lovell J.D.,
RA Marsh V.L., Martin S.L., McConnachie L.J., McLay K., McMurray A.A.,
RA Milne S.A., Mistry D., Moore M.J.F., Mullikin J.C., Nickerson T.,
RA Oliver K., Parker A., Patel R., Pearce T.A.V., Peck A.I.,
RA Phillimore B.J.C.T., Prathalingam S.R., Plumb R.W., Ramsay H.,
RA Rice C.M., Ross M.T., Scott C.E., Sehra H.K., Shownkeen R., Sims S.,
RA Skuce C.D., Smith M.L., Soderlund C., Steward C.A., Sulston J.E.,
RA Swann R.M., Sycamore N., Taylor R., Tee L., Thomas D.W., Thorpe A.,
RA Tracey A., Tromans A.C., Vaudin M., Wall M., Wallis J.M.,
RA Whitehead S.L., Whittaker P., Willey D.L., Williams L., Williams S.A.,
RA Wilming L., Wray P.W., Hubbard T., Durbin R.M., Bentley D.R., Beck S.,
RA Rogers J.;
RT "The DNA sequence and comparative analysis of human chromosome 20.";
RL Nature 414:865-871(2001).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain, and Skin;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [6]
RP FUNCTION, PHOSPHORYLATION, AND SUBCELLULAR LOCATION.
RX PubMed=15653697; DOI=10.1074/jbc.M404754200;
RA Casper J.M., Kemp M.G., Ghosh M., Randall G.M., Vaillant A.,
RA Leffak M.;
RT "The c-myc DNA-unwinding element-binding protein modulates the
RT assembly of DNA replication complexes in vitro.";
RL J. Biol. Chem. 280:13071-13083(2005).
RN [7]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Platelet;
RX PubMed=18088087; DOI=10.1021/pr0704130;
RA Zahedi R.P., Lewandrowski U., Wiesner J., Wortelkamp S., Moebius J.,
RA Schuetz C., Walter U., Gambaryan S., Sickmann A.;
RT "Phosphoproteome of resting human platelets.";
RL J. Proteome Res. 7:526-534(2008).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-197 AND SER-205, AND
RP MASS SPECTROMETRY.
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [9]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,
RA Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in
RT a refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-197 AND SER-205, AND
RP MASS SPECTROMETRY.
RC TISSUE=Leukemic T-cell;
RX PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA Rodionov V., Han D.K.;
RT "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT reveals system-wide modulation of protein-protein interactions.";
RL Sci. Signal. 2:RA46-RA46(2009).
RN [11]
RP FUNCTION, SUBCELLULAR LOCATION, PHOSPHORYLATION, AND INTERACTION WITH
RP CDC45 AND TOPBP1.
RX PubMed=20065034; DOI=10.1128/MCB.00710-09;
RA Chowdhury A., Liu G., Kemp M., Chen X., Katrangi N., Myers S.,
RA Ghosh M., Yao J., Gao Y., Bubulya P., Leffak M.;
RT "The DNA unwinding element binding protein DUE-B interacts with Cdc45
RT in preinitiation complex formation.";
RL Mol. Cell. Biol. 30:1495-1507(2010).
RN [12]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S.,
RA Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full
RT phosphorylation site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [13]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
RA Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [14]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-197, AND MASS
RP SPECTROMETRY.
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J.,
RA Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V.,
RA Blagoev B.;
RT "System-wide temporal characterization of the proteome and
RT phosphoproteome of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [15]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E.,
RA Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K.,
RA Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-
RT terminal acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN [16]
RP X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS), SUBUNIT, AND MAGNESIUM-BINDING
RP SITES.
RX PubMed=17264083; DOI=10.1074/jbc.M609632200;
RA Kemp M., Bae B., Yu J.P., Ghosh M., Leffak M., Nair S.K.;
RT "Structure and function of the c-myc DNA-unwinding element-binding
RT protein DUE-B.";
RL J. Biol. Chem. 282:10441-10448(2007).
CC -!- FUNCTION: ATPase involved in DNA replication, may facilitate
CC loading of CDC45 onto pre-replication complexes. May hydrolyze D-
CC tyrosyl-tRNA(Tyr) into D-tyrosine and free tRNA(Tyr), a possible
CC defense mechanism against a harmful effect of D-tyrosine.
CC -!- SUBUNIT: Homodimer. Interacts with CDC45 and TOPBP1.
CC -!- SUBCELLULAR LOCATION: Nucleus. Cytoplasm (Potential).
CC Note=Associated with chromatin at some replication origins
CC containing functional DNA-unwinding elements.
CC -!- TISSUE SPECIFICITY: Expressed in many adult and fetal tissues.
CC Highest levels in testis, ovary, spleen and in adult and fetal
CC brain.
CC -!- PTM: Preferentially phosphorylated in cells arrested early in S
CC phase. Phosphorylation in the C-terminus weakens the interaction
CC with CDC45.
CC -!- SIMILARITY: Belongs to the DTD family.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAB85044.1; Type=Miscellaneous discrepancy; Note=Presence of Alu-repeat DNA;
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DR EMBL; AF332356; AAL57046.1; -; mRNA.
DR EMBL; AK074304; BAB85044.1; ALT_SEQ; mRNA.
DR EMBL; AK291440; BAF84129.1; -; mRNA.
DR EMBL; AL121900; CAH73147.1; -; Genomic_DNA.
DR EMBL; AL121780; CAH73147.1; JOINED; Genomic_DNA.
DR EMBL; AL121780; CAI15669.1; -; Genomic_DNA.
DR EMBL; AL121900; CAI15669.1; JOINED; Genomic_DNA.
DR EMBL; CH471133; EAX10227.1; -; Genomic_DNA.
DR EMBL; BC000599; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; CH471133; EAX10228.1; -; Genomic_DNA.
DR EMBL; BC045167; AAH45167.1; -; mRNA.
DR EMBL; BC100923; AAI00924.1; -; mRNA.
DR EMBL; BC100924; AAI00925.1; -; mRNA.
DR EMBL; BC100925; AAI00926.1; -; mRNA.
DR RefSeq; NP_543010.3; NM_080820.4.
DR UniGene; Hs.659442; -.
DR PDB; 2OKV; X-ray; 2.00 A; A/B/C/D=1-209.
DR PDBsum; 2OKV; -.
DR ProteinModelPortal; Q8TEA8; -.
DR SMR; Q8TEA8; 1-150.
DR IntAct; Q8TEA8; 1.
DR STRING; 9606.ENSP00000366672; -.
DR PhosphoSite; Q8TEA8; -.
DR DMDM; 29427856; -.
DR PaxDb; Q8TEA8; -.
DR PeptideAtlas; Q8TEA8; -.
DR PRIDE; Q8TEA8; -.
DR DNASU; 92675; -.
DR Ensembl; ENST00000377452; ENSP00000366672; ENSG00000125821.
DR GeneID; 92675; -.
DR KEGG; hsa:92675; -.
DR UCSC; uc002wrf.4; human.
DR CTD; 92675; -.
DR GeneCards; GC20P018568; -.
DR HGNC; HGNC:16219; DTD1.
DR HPA; HPA040981; -.
DR MIM; 610996; gene.
DR neXtProt; NX_Q8TEA8; -.
DR PharmGKB; PA162384107; -.
DR eggNOG; COG1490; -.
DR HOVERGEN; HBG039436; -.
DR InParanoid; Q8TEA8; -.
DR KO; K07560; -.
DR OMA; DGPVTIW; -.
DR OrthoDB; EOG7SR4P0; -.
DR PhylomeDB; Q8TEA8; -.
DR ChiTaRS; DTD1; human.
DR EvolutionaryTrace; Q8TEA8; -.
DR GenomeRNAi; 92675; -.
DR NextBio; 77831; -.
DR PRO; PR:Q8TEA8; -.
DR Bgee; Q8TEA8; -.
DR CleanEx; HS_DTD1; -.
DR CleanEx; HS_HARS2; -.
DR Genevestigator; Q8TEA8; -.
DR GO; GO:0005737; C:cytoplasm; IDA:HPA.
DR GO; GO:0005730; C:nucleolus; IDA:HPA.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0016788; F:hydrolase activity, acting on ester bonds; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0019478; P:D-amino acid catabolic process; IEA:InterPro.
DR GO; GO:0006260; P:DNA replication; IEA:UniProtKB-KW.
DR Gene3D; 3.50.80.10; -; 1.
DR InterPro; IPR023509; DTD-like_dom.
DR InterPro; IPR003732; DTyrtRNA_deacyls.
DR PANTHER; PTHR10472; PTHR10472; 1.
DR Pfam; PF02580; Tyr_Deacylase; 1.
DR SUPFAM; SSF69500; SSF69500; 1.
DR TIGRFAMs; TIGR00256; TIGR00256; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Complete proteome; Cytoplasm; DNA replication;
KW DNA-binding; Hydrolase; Metal-binding; Nucleus; Phosphoprotein;
KW Reference proteome.
FT CHAIN 1 209 D-tyrosyl-tRNA(Tyr) deacylase 1.
FT /FTId=PRO_0000164626.
FT ACT_SITE 81 81 Nucleophile (By similarity).
FT METAL 4 4 Magnesium; via carbonyl oxygen.
FT METAL 6 6 Magnesium.
FT METAL 28 28 Magnesium; via carbonyl oxygen.
FT MOD_RES 197 197 Phosphoserine.
FT MOD_RES 205 205 Phosphoserine.
FT CONFLICT 94 94 H -> N (in Ref. 5; AAH45167).
FT CONFLICT 134 134 H -> R (in Ref. 1; AAL57046).
FT STRAND 2 15
FT STRAND 18 32
FT HELIX 39 51
FT HELIX 67 70
FT STRAND 73 78
FT HELIX 80 82
FT STRAND 87 90
FT HELIX 99 116
FT HELIX 119 121
FT STRAND 122 124
FT STRAND 131 146
SQ SEQUENCE 209 AA; 23424 MW; F006ED14974ACC92 CRC64;
MKAVVQRVTR ASVTVGGEQI SAIGRGICVL LGISLEDTQK ELEHMVRKIL NLRVFEDESG
KHWSKSVMDK QYEILCVSQF TLQCVLKGNK PDFHLAMPTE QAEGFYNSFL EQLRKTYRPE
LIKDGKFGAY MQVHIQNDGP VTIELESPAP GTATSDPKQL SKLEKQQQRK EKTRAKGPSE
SSKERNTPRK EDRSASSGAE GDVSSEREP
//
MIM
610996
*RECORD*
*FIELD* NO
610996
*FIELD* TI
*610996 D-TYROSYL-tRNA DEACYLASE 1, S. CEREVISIAE, HOMOLOG OF; DTD1
;;CHROMOSOME 20 OPEN READING FRAME 88; C20ORF88
read more*FIELD* TX
By screening a human fetal brain cDNA library, Meng et al. (2002)
identified DTD1. The deduced 209-amino acid protein has a predicted
molecular mass of 23.4 kD and contains potential sites for
phosphorylation and O-glycosylation. DTD1 shares 94% identity with its
mouse ortholog. Northern blot analysis detected a 1.5-kb transcript in
human fetal brain. PCR analysis of human tissues detected high
expression in adult brain, testis, ovary, spleen, and fetal brain, and
moderate expression in adult colon, thymus, and small intestine and
fetal liver, lung, thymus, spleen, heart, and kidney.
GENE STRUCTURE
Meng et al. (2002) determined that the DTD1 gene contains 6 exons.
MAPPING
By genomic sequence analysis, Meng et al. (2002) mapped the DTD1 gene to
chromosome 20p11.
*FIELD* RF
1. Meng, X.; Chen, J.; Yang, Q.; Wang, S.; Chao, Y.; Ying, K.; Xie,
Y.; Mao, Y.: Cloning and identification of a novel cDNA which may
be associated with FKBP25. Biochem. Genet. 40: 303-310, 2002.
*FIELD* CD
Dorothy S. Reilly: 5/7/2007
*FIELD* ED
wwang: 05/07/2007
*RECORD*
*FIELD* NO
610996
*FIELD* TI
*610996 D-TYROSYL-tRNA DEACYLASE 1, S. CEREVISIAE, HOMOLOG OF; DTD1
;;CHROMOSOME 20 OPEN READING FRAME 88; C20ORF88
read more*FIELD* TX
By screening a human fetal brain cDNA library, Meng et al. (2002)
identified DTD1. The deduced 209-amino acid protein has a predicted
molecular mass of 23.4 kD and contains potential sites for
phosphorylation and O-glycosylation. DTD1 shares 94% identity with its
mouse ortholog. Northern blot analysis detected a 1.5-kb transcript in
human fetal brain. PCR analysis of human tissues detected high
expression in adult brain, testis, ovary, spleen, and fetal brain, and
moderate expression in adult colon, thymus, and small intestine and
fetal liver, lung, thymus, spleen, heart, and kidney.
GENE STRUCTURE
Meng et al. (2002) determined that the DTD1 gene contains 6 exons.
MAPPING
By genomic sequence analysis, Meng et al. (2002) mapped the DTD1 gene to
chromosome 20p11.
*FIELD* RF
1. Meng, X.; Chen, J.; Yang, Q.; Wang, S.; Chao, Y.; Ying, K.; Xie,
Y.; Mao, Y.: Cloning and identification of a novel cDNA which may
be associated with FKBP25. Biochem. Genet. 40: 303-310, 2002.
*FIELD* CD
Dorothy S. Reilly: 5/7/2007
*FIELD* ED
wwang: 05/07/2007