TYW3_HUMAN
ID TYW3_HUMAN Reviewed; 259 AA.
AC Q6IPR3; B4DSP9; E9PGR7; Q5HYJ0; Q8N7L1;
DT 03-APR-2007, integrated into UniProtKB/Swiss-Prot.
DT 03-MAR-2009, sequence version 2.
DT 03-AUG-2022, entry version 132.
DE RecName: Full=tRNA wybutosine-synthesizing protein 3 homolog;
DE Short=tRNA-yW-synthesizing protein 3;
DE EC=2.1.1.282;
DE AltName: Full=tRNA(Phe) 7-((3-amino-3-carboxypropyl)-4-demethylwyosine(37)-N(4))-methyltransferase;
GN Name=TYW3; Synonyms=C1orf171;
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] (ISOFORMS 1 AND 2), AND VARIANT
RP VAL-121.
RC TISSUE=Brain, and Uterus;
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=16710414; DOI=10.1038/nature04727;
RA Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A.,
RA Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C.,
RA Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.,
RA Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C.,
RA Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W.,
RA Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J.,
RA Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J.,
RA Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y.,
RA Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J.,
RA Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
RA Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
RA Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
RA Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S.,
RA Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K.,
RA Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R.,
RA Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M.,
RA Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S.,
RA Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J.,
RA Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W.,
RA McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
RA Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
RA Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
RA Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
RA Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S.,
RA Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M.,
RA White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H.,
RA Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E.,
RA Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G.,
RA Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.;
RT "The DNA sequence and biological annotation of human chromosome 1.";
RL Nature 441:315-321(2006).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Testis;
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 156-259.
RC TISSUE=Heart;
RX PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D.,
RA Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A.,
RA Wiemann S., Schupp I.;
RT "The full-ORF clone resource of the German cDNA consortium.";
RL BMC Genomics 8:399-399(2007).
CC -!- FUNCTION: Probable S-adenosyl-L-methionine-dependent methyltransferase
CC that acts as a component of the wybutosine biosynthesis pathway.
CC Wybutosine is a hyper modified guanosine with a tricyclic base found at
CC the 3'-position adjacent to the anticodon of eukaryotic phenylalanine
CC tRNA (By similarity). {ECO:0000250}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=4-demethyl-7-[(3S)-3-amino-3-carboxypropyl]wyosine(37) in
CC tRNA(Phe) + S-adenosyl-L-methionine = 7-[(3S)-3-amino-3-
CC carboxypropyl]wyosine(37) in tRNA(Phe) + H(+) + S-adenosyl-L-
CC homocysteine; Xref=Rhea:RHEA:36635, Rhea:RHEA-COMP:10378, Rhea:RHEA-
CC COMP:10379, ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789,
CC ChEBI:CHEBI:73543, ChEBI:CHEBI:73550; EC=2.1.1.282;
CC -!- PATHWAY: tRNA modification; wybutosine-tRNA(Phe) biosynthesis.
CC -!- INTERACTION:
CC Q6IPR3; Q96D03: DDIT4L; NbExp=3; IntAct=EBI-10974426, EBI-742054;
CC Q6IPR3; Q9NRD5: PICK1; NbExp=3; IntAct=EBI-10974426, EBI-79165;
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q6IPR3-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q6IPR3-2; Sequence=VSP_044477;
CC -!- SIMILARITY: Belongs to the TYW3 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAI46106.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AK098237; BAC05267.1; -; mRNA.
DR EMBL; AK299849; BAG61711.1; -; mRNA.
DR EMBL; AC091611; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC071765; AAH71765.1; -; mRNA.
DR EMBL; BX647591; CAI46106.1; ALT_INIT; mRNA.
DR CCDS; CCDS53334.1; -. [Q6IPR3-2]
DR CCDS; CCDS666.1; -. [Q6IPR3-1]
DR RefSeq; NP_001156388.1; NM_001162916.1. [Q6IPR3-2]
DR RefSeq; NP_612476.1; NM_138467.2. [Q6IPR3-1]
DR RefSeq; XP_006710410.1; XM_006710347.1. [Q6IPR3-1]
DR AlphaFoldDB; Q6IPR3; -.
DR SMR; Q6IPR3; -.
DR BioGRID; 126045; 57.
DR IntAct; Q6IPR3; 29.
DR STRING; 9606.ENSP00000359904; -.
DR iPTMnet; Q6IPR3; -.
DR PhosphoSitePlus; Q6IPR3; -.
DR BioMuta; TYW3; -.
DR DMDM; 224471865; -.
DR EPD; Q6IPR3; -.
DR jPOST; Q6IPR3; -.
DR MassIVE; Q6IPR3; -.
DR MaxQB; Q6IPR3; -.
DR PaxDb; Q6IPR3; -.
DR PeptideAtlas; Q6IPR3; -.
DR PRIDE; Q6IPR3; -.
DR ProteomicsDB; 20378; -.
DR ProteomicsDB; 66456; -. [Q6IPR3-1]
DR Antibodypedia; 33463; 53 antibodies from 20 providers.
DR DNASU; 127253; -.
DR Ensembl; ENST00000370867.8; ENSP00000359904.3; ENSG00000162623.16. [Q6IPR3-1]
DR Ensembl; ENST00000457880.6; ENSP00000407025.2; ENSG00000162623.16. [Q6IPR3-2]
DR GeneID; 127253; -.
DR KEGG; hsa:127253; -.
DR MANE-Select; ENST00000370867.8; ENSP00000359904.3; NM_138467.3; NP_612476.1.
DR UCSC; uc001dgn.4; human. [Q6IPR3-1]
DR CTD; 127253; -.
DR GeneCards; TYW3; -.
DR HGNC; HGNC:24757; TYW3.
DR HPA; ENSG00000162623; Low tissue specificity.
DR MIM; 611245; gene.
DR neXtProt; NX_Q6IPR3; -.
DR OpenTargets; ENSG00000162623; -.
DR PharmGKB; PA142672420; -.
DR VEuPathDB; HostDB:ENSG00000162623; -.
DR eggNOG; KOG1228; Eukaryota.
DR GeneTree; ENSGT00940000153304; -.
DR HOGENOM; CLU_047426_1_1_1; -.
DR InParanoid; Q6IPR3; -.
DR OMA; GKWHHYA; -.
DR OrthoDB; 1313208at2759; -.
DR PhylomeDB; Q6IPR3; -.
DR TreeFam; TF329327; -.
DR PathwayCommons; Q6IPR3; -.
DR Reactome; R-HSA-6782861; Synthesis of wybutosine at G37 of tRNA(Phe).
DR SignaLink; Q6IPR3; -.
DR UniPathway; UPA00375; -.
DR BioGRID-ORCS; 127253; 11 hits in 1072 CRISPR screens.
DR ChiTaRS; TYW3; human.
DR GenomeRNAi; 127253; -.
DR Pharos; Q6IPR3; Tdark.
DR PRO; PR:Q6IPR3; -.
DR Proteomes; UP000005640; Chromosome 1.
DR RNAct; Q6IPR3; protein.
DR Bgee; ENSG00000162623; Expressed in epithelial cell of pancreas and 168 other tissues.
DR ExpressionAtlas; Q6IPR3; baseline and differential.
DR Genevisible; Q6IPR3; HS.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0008175; F:tRNA methyltransferase activity; IBA:GO_Central.
DR GO; GO:0030488; P:tRNA methylation; IBA:GO_Central.
DR Gene3D; 3.30.1960.10; -; 1.
DR InterPro; IPR003827; tRNA_yW-synthesising.
DR InterPro; IPR036602; tRNA_yW-synthesising-like_sf.
DR Pfam; PF02676; TYW3; 1.
DR SUPFAM; SSF111278; SSF111278; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Methyltransferase; Phosphoprotein;
KW Reference proteome; S-adenosyl-L-methionine; Transferase; tRNA processing.
FT CHAIN 1..259
FT /note="tRNA wybutosine-synthesizing protein 3 homolog"
FT /id="PRO_0000281842"
FT MOD_RES 25
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8BSA9"
FT VAR_SEQ 86..118
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_044477"
FT VARIANT 110
FT /note="R -> Q (in dbSNP:rs11538281)"
FT /id="VAR_031292"
FT VARIANT 121
FT /note="M -> V (in dbSNP:rs1133891)"
FT /evidence="ECO:0000269|PubMed:14702039"
FT /id="VAR_031293"
FT CONFLICT 143
FT /note="A -> V (in Ref. 3; AAH71765)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 259 AA; 29794 MW; 150BA9247232324D CRC64;
MDRSAEFRKW KAQCLSKADL SRKGSVDEDV VELVQFLNMR DQFFTTSSCA GRILLLDRGI
NGFEVQKQNC CWLLVTHKLC VKDDVIVALK KANGDATLKF EPFVLHVQCR QLQDAQILHS
MAIDSGFRNS GITVGKRGKT MLAVRSTHGL EVPLSHKGKL MVTEEYIDFL LNVANQKMEE
NKKRIERFYN CLQHALERET MTNLHPKIKE KNNSSYIHKK KRNPEKTRAQ CITKESDEEL
ENDDDDDLGI NVTIFPEDY
