DTWD2_HUMAN
ID DTWD2_HUMAN Reviewed; 298 AA.
AC Q8NBA8; J3KND6;
DT 09-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2002, sequence version 1.
DT 03-AUG-2022, entry version 118.
DE RecName: Full=tRNA-uridine aminocarboxypropyltransferase 2 {ECO:0000305};
DE EC=2.5.1.25 {ECO:0000269|PubMed:31804502};
DE AltName: Full=DTW domain-containing protein 2;
GN Name=DTWD2 {ECO:0000303|PubMed:31804502, ECO:0000312|HGNC:HGNC:19334};
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Skin;
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., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., 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., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA 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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15372022; DOI=10.1038/nature02919;
RA Schmutz J., Martin J., Terry A., Couronne O., Grimwood J., Lowry S.,
RA Gordon L.A., Scott D., Xie G., Huang W., Hellsten U., Tran-Gyamfi M.,
RA She X., Prabhakar S., Aerts A., Altherr M., Bajorek E., Black S.,
RA Branscomb E., Caoile C., Challacombe J.F., Chan Y.M., Denys M.,
RA Detter J.C., Escobar J., Flowers D., Fotopulos D., Glavina T., Gomez M.,
RA Gonzales E., Goodstein D., Grigoriev I., Groza M., Hammon N., Hawkins T.,
RA Haydu L., Israni S., Jett J., Kadner K., Kimball H., Kobayashi A.,
RA Lopez F., Lou Y., Martinez D., Medina C., Morgan J., Nandkeshwar R.,
RA Noonan J.P., Pitluck S., Pollard M., Predki P., Priest J., Ramirez L.,
RA Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A., Thayer N.,
RA Tice H., Tsai M., Ustaszewska A., Vo N., Wheeler J., Wu K., Yang J.,
RA Dickson M., Cheng J.-F., Eichler E.E., Olsen A., Pennacchio L.A.,
RA Rokhsar D.S., Richardson P., Lucas S.M., Myers R.M., Rubin E.M.;
RT "The DNA sequence and comparative analysis of human chromosome 5.";
RL Nature 431:268-274(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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 project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [5]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND IDENTIFICATION BY MASS
RP 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., Timmerman E.,
RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-terminal
RT acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-132, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [7]
RP FUNCTION, CATALYTIC ACTIVITY, AND SUBCELLULAR LOCATION.
RX PubMed=31804502; DOI=10.1038/s41467-019-13525-3;
RA Takakura M., Ishiguro K., Akichika S., Miyauchi K., Suzuki T.;
RT "Biogenesis and functions of aminocarboxypropyluridine in tRNA.";
RL Nat. Commun. 10:5542-5542(2019).
CC -!- FUNCTION: Catalyzes the formation of 3-(3-amino-3-carboxypropyl)uridine
CC (acp3U) at position 20a in the D-loop of several cytoplasmic tRNAs
CC (acp3U(20a)) (PubMed:31804502). Also has a weak activity to form acp3U
CC at position 20 in the D-loop of tRNAs (acp3U(20)) (PubMed:31804502).
CC {ECO:0000269|PubMed:31804502}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a uridine in tRNA + S-adenosyl-L-methionine = a 3-[(3S)-3-
CC amino-3-carboxypropyl]uridine in tRNA + H(+) + S-methyl-5'-
CC thioadenosine; Xref=Rhea:RHEA:62432, Rhea:RHEA-COMP:13339, Rhea:RHEA-
CC COMP:16092, ChEBI:CHEBI:15378, ChEBI:CHEBI:17509, ChEBI:CHEBI:59789,
CC ChEBI:CHEBI:65315, ChEBI:CHEBI:82930; EC=2.5.1.25;
CC Evidence={ECO:0000269|PubMed:31804502};
CC -!- SUBCELLULAR LOCATION: [Isoform 1]: Cytoplasm
CC {ECO:0000269|PubMed:31804502}.
CC -!- SUBCELLULAR LOCATION: [Isoform 2]: Nucleus
CC {ECO:0000269|PubMed:31804502}. Cytoplasm {ECO:0000269|PubMed:31804502}.
CC Note=Localizes mainly in the nucleus. {ECO:0000269|PubMed:31804502}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1; Synonyms=DTWD2L {ECO:0000303|PubMed:31804502}, Long
CC {ECO:0000303|PubMed:31804502};
CC IsoId=Q8NBA8-1; Sequence=Displayed;
CC Name=2; Synonyms=DTWD2S {ECO:0000303|PubMed:31804502}, Short
CC {ECO:0000303|PubMed:31804502};
CC IsoId=Q8NBA8-2; Sequence=VSP_060608;
CC -!- DOMAIN: Contains 1 DXTW motif.
CC -!- SIMILARITY: Belongs to the TDD superfamily. DTWD2 family.
CC {ECO:0000305}.
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DR EMBL; AK091296; BAC03630.1; -; mRNA.
DR EMBL; AC008629; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC010462; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471086; EAW48925.1; -; Genomic_DNA.
DR EMBL; BC114508; AAI14509.1; -; mRNA.
DR EMBL; BC114955; AAI14956.1; -; mRNA.
DR CCDS; CCDS34216.1; -. [Q8NBA8-1]
DR CCDS; CCDS78050.1; -. [Q8NBA8-2]
DR RefSeq; NP_001295010.1; NM_001308081.1. [Q8NBA8-2]
DR RefSeq; NP_775937.1; NM_173666.3. [Q8NBA8-1]
DR AlphaFoldDB; Q8NBA8; -.
DR BioGRID; 130156; 29.
DR IntAct; Q8NBA8; 8.
DR STRING; 9606.ENSP00000425048; -.
DR iPTMnet; Q8NBA8; -.
DR PhosphoSitePlus; Q8NBA8; -.
DR BioMuta; DTWD2; -.
DR DMDM; 74730106; -.
DR EPD; Q8NBA8; -.
DR jPOST; Q8NBA8; -.
DR MassIVE; Q8NBA8; -.
DR MaxQB; Q8NBA8; -.
DR PaxDb; Q8NBA8; -.
DR PeptideAtlas; Q8NBA8; -.
DR PRIDE; Q8NBA8; -.
DR ProteomicsDB; 72753; -.
DR Antibodypedia; 52885; 66 antibodies from 14 providers.
DR DNASU; 285605; -.
DR Ensembl; ENST00000304058.8; ENSP00000302892.4; ENSG00000169570.10. [Q8NBA8-2]
DR Ensembl; ENST00000510708.6; ENSP00000425048.1; ENSG00000169570.10. [Q8NBA8-1]
DR GeneID; 285605; -.
DR KEGG; hsa:285605; -.
DR MANE-Select; ENST00000510708.6; ENSP00000425048.1; NM_173666.4; NP_775937.1.
DR UCSC; uc003ksa.4; human. [Q8NBA8-1]
DR UCSC; uc063ggh.1; human.
DR CTD; 285605; -.
DR DisGeNET; 285605; -.
DR GeneCards; DTWD2; -.
DR HGNC; HGNC:19334; DTWD2.
DR HPA; ENSG00000169570; Low tissue specificity.
DR neXtProt; NX_Q8NBA8; -.
DR OpenTargets; ENSG00000169570; -.
DR PharmGKB; PA142671943; -.
DR VEuPathDB; HostDB:ENSG00000169570; -.
DR eggNOG; KOG4382; Eukaryota.
DR GeneTree; ENSGT00390000006867; -.
DR HOGENOM; CLU_066458_3_0_1; -.
DR InParanoid; Q8NBA8; -.
DR OMA; HTLCKYQ; -.
DR OrthoDB; 910985at2759; -.
DR PhylomeDB; Q8NBA8; -.
DR TreeFam; TF324734; -.
DR PathwayCommons; Q8NBA8; -.
DR SignaLink; Q8NBA8; -.
DR BioGRID-ORCS; 285605; 10 hits in 1077 CRISPR screens.
DR ChiTaRS; DTWD2; human.
DR GenomeRNAi; 285605; -.
DR Pharos; Q8NBA8; Tdark.
DR PRO; PR:Q8NBA8; -.
DR Proteomes; UP000005640; Chromosome 5.
DR RNAct; Q8NBA8; protein.
DR Bgee; ENSG00000169570; Expressed in secondary oocyte and 179 other tissues.
DR ExpressionAtlas; Q8NBA8; baseline and differential.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0016432; F:tRNA-uridine aminocarboxypropyltransferase activity; IDA:UniProtKB.
DR GO; GO:0006400; P:tRNA modification; IDA:UniProtKB.
DR InterPro; IPR005636; DTW.
DR InterPro; IPR039262; DTWD2/YfiP.
DR PANTHER; PTHR21392; PTHR21392; 1.
DR Pfam; PF03942; DTW; 1.
DR SMART; SM01144; DTW; 1.
PE 1: Evidence at protein level;
KW Acetylation; Alternative splicing; Cytoplasm; Nucleus; Phosphoprotein;
KW Reference proteome; S-adenosyl-L-methionine; Transferase; tRNA processing.
FT CHAIN 1..298
FT /note="tRNA-uridine aminocarboxypropyltransferase 2"
FT /id="PRO_0000271128"
FT REGION 1..53
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 178..181
FT /note="DXTW"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0007744|PubMed:22814378"
FT MOD_RES 132
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT VAR_SEQ 1..73
FT /note="MESQKEARTLQEPVARPSGASSSQTPNDKERREGGAVPAAAALGAEADDDSA
FT DGLWELPVEPAERRPECTRCS -> MPGTATY (in isoform 2)"
FT /id="VSP_060608"
SQ SEQUENCE 298 AA; 33416 MW; E8409E8FBB4A4899 CRC64;
MESQKEARTL QEPVARPSGA SSSQTPNDKE RREGGAVPAA AALGAEADDD SADGLWELPV
EPAERRPECT RCSRPQKVCL CPFLPAHPLH ISTHLYIIQH PAEENKVLRT VPLLAACLPQ
DKCKVKIGRR FSEERDPELS TVCRKSGTLI LYPGAEAANL EEFILDSPVY PSTIIIIDGT
WSQAKDIFYK NSLFRHPKQV QLKTSISSQY VIRMQPTNRC LSTLECAAVA LSILEKNNYI
QETLLRPLQA LCSFQLQHGA QIRLSKEHLL KNGLYPKPMP KNKRKLRKME LLMNSVKI
