TRPT1_HUMAN
ID TRPT1_HUMAN Reviewed; 253 AA.
AC Q86TN4; A8MU17; A8MYC9; F5H2B2; Q9BSB9;
DT 23-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 139.
DE RecName: Full=tRNA 2'-phosphotransferase 1;
DE EC=2.7.1.160;
GN Name=TRPT1;
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 [MRNA] (ISOFORM 1), FUNCTION, TISSUE SPECIFICITY, AND
RP VARIANT ARG-172.
RC TISSUE=Fetal brain;
RX PubMed=14504659; DOI=10.1007/s00018-003-3107-7;
RA Hu Q.-D., Lu H., Huo K., Ying K., Li J., Xie Y., Mao Y., Li Y.-Y.;
RT "A human homolog of the yeast gene encoding tRNA 2'-phosphotransferase:
RT cloning, characterization and complementation analysis.";
RL Cell. Mol. Life Sci. 60:1725-1732(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16554811; DOI=10.1038/nature04632;
RA Taylor T.D., Noguchi H., Totoki Y., Toyoda A., Kuroki Y., Dewar K.,
RA Lloyd C., Itoh T., Takeda T., Kim D.-W., She X., Barlow K.F., Bloom T.,
RA Bruford E., Chang J.L., Cuomo C.A., Eichler E., FitzGerald M.G.,
RA Jaffe D.B., LaButti K., Nicol R., Park H.-S., Seaman C., Sougnez C.,
RA Yang X., Zimmer A.R., Zody M.C., Birren B.W., Nusbaum C., Fujiyama A.,
RA Hattori M., Rogers J., Lander E.S., Sakaki Y.;
RT "Human chromosome 11 DNA sequence and analysis including novel gene
RT identification.";
RL Nature 440:497-500(2006).
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 (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2 AND 3), AND VARIANT
RP ARG-172.
RC TISSUE=Epidermal carcinoma, and Ovary;
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 IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
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 [6]
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., Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a
RT refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-240, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
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 [8]
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 [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-240, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma, and 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).
CC -!- FUNCTION: Catalyzes the last step of tRNA splicing, the transfer of the
CC splice junction 2'-phosphate from ligated tRNA to NAD to produce ADP-
CC ribose 1''-2'' cyclic phosphate. {ECO:0000305|PubMed:14504659}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2'-phospho-[ligated tRNA] + NAD(+) = ADP-beta-D-ribose
CC 1'',2''-cyclic phosphate + mature tRNA + nicotinamide;
CC Xref=Rhea:RHEA:23324, Rhea:RHEA-COMP:11106, Rhea:RHEA-COMP:11107,
CC ChEBI:CHEBI:17154, ChEBI:CHEBI:57540, ChEBI:CHEBI:76596,
CC ChEBI:CHEBI:82883, ChEBI:CHEBI:85027; EC=2.7.1.160;
CC -!- INTERACTION:
CC Q86TN4-2; Q9H8Y8: GORASP2; NbExp=3; IntAct=EBI-12403619, EBI-739467;
CC Q86TN4-2; Q12933: TRAF2; NbExp=3; IntAct=EBI-12403619, EBI-355744;
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Name=1;
CC IsoId=Q86TN4-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q86TN4-2; Sequence=VSP_022524;
CC Name=3;
CC IsoId=Q86TN4-3; Sequence=VSP_045273;
CC Name=4;
CC IsoId=Q86TN4-4; Sequence=VSP_045827;
CC -!- TISSUE SPECIFICITY: Widely expressed. Weakly or not expressed in lung,
CC spleen, small intestine and peripheral blood leukocytes.
CC {ECO:0000269|PubMed:14504659}.
CC -!- SIMILARITY: Belongs to the KptA/TPT1 family. {ECO:0000305}.
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DR EMBL; AY211494; AAO62941.1; -; mRNA.
DR EMBL; AP005668; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AP006334; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471076; EAW74202.1; -; Genomic_DNA.
DR EMBL; BC005133; AAH05133.1; -; mRNA.
DR EMBL; BQ672032; -; NOT_ANNOTATED_CDS; mRNA.
DR CCDS; CCDS31595.1; -. [Q86TN4-1]
DR CCDS; CCDS44639.1; -. [Q86TN4-2]
DR CCDS; CCDS53652.1; -. [Q86TN4-4]
DR CCDS; CCDS53653.1; -. [Q86TN4-3]
DR RefSeq; NP_001028850.2; NM_001033678.3. [Q86TN4-1]
DR RefSeq; NP_001153861.1; NM_001160389.1. [Q86TN4-4]
DR RefSeq; NP_001153862.1; NM_001160390.1. [Q86TN4-1]
DR RefSeq; NP_001153864.1; NM_001160392.1. [Q86TN4-3]
DR RefSeq; NP_001153865.1; NM_001160393.1.
DR RefSeq; NP_001317227.1; NM_001330298.1.
DR RefSeq; NP_113660.1; NM_031472.3. [Q86TN4-2]
DR AlphaFoldDB; Q86TN4; -.
DR SMR; Q86TN4; -.
DR BioGRID; 123736; 14.
DR IntAct; Q86TN4; 5.
DR STRING; 9606.ENSP00000378050; -.
DR iPTMnet; Q86TN4; -.
DR PhosphoSitePlus; Q86TN4; -.
DR BioMuta; TRPT1; -.
DR DMDM; 124053420; -.
DR EPD; Q86TN4; -.
DR jPOST; Q86TN4; -.
DR MassIVE; Q86TN4; -.
DR MaxQB; Q86TN4; -.
DR PaxDb; Q86TN4; -.
DR PeptideAtlas; Q86TN4; -.
DR PRIDE; Q86TN4; -.
DR ProteomicsDB; 2072; -.
DR ProteomicsDB; 25919; -.
DR ProteomicsDB; 69716; -. [Q86TN4-1]
DR ProteomicsDB; 69717; -. [Q86TN4-2]
DR Antibodypedia; 51851; 34 antibodies from 14 providers.
DR DNASU; 83707; -.
DR Ensembl; ENST00000317459.11; ENSP00000314073.6; ENSG00000149743.14. [Q86TN4-1]
DR Ensembl; ENST00000394546.6; ENSP00000378050.2; ENSG00000149743.14. [Q86TN4-4]
DR Ensembl; ENST00000394547.7; ENSP00000378051.3; ENSG00000149743.14. [Q86TN4-2]
DR Ensembl; ENST00000541278.5; ENSP00000438683.1; ENSG00000149743.14. [Q86TN4-3]
DR GeneID; 83707; -.
DR KEGG; hsa:83707; -.
DR MANE-Select; ENST00000317459.11; ENSP00000314073.6; NM_001033678.4; NP_001028850.2.
DR UCSC; uc001nyn.4; human. [Q86TN4-1]
DR CTD; 83707; -.
DR GeneCards; TRPT1; -.
DR HGNC; HGNC:20316; TRPT1.
DR HPA; ENSG00000149743; Tissue enhanced (skeletal).
DR MIM; 610470; gene.
DR neXtProt; NX_Q86TN4; -.
DR OpenTargets; ENSG00000149743; -.
DR PharmGKB; PA134964265; -.
DR VEuPathDB; HostDB:ENSG00000149743; -.
DR eggNOG; KOG2278; Eukaryota.
DR GeneTree; ENSGT00390000002731; -.
DR OMA; YLYHGTV; -.
DR OrthoDB; 1460780at2759; -.
DR PhylomeDB; Q86TN4; -.
DR TreeFam; TF324127; -.
DR BRENDA; 2.7.1.160; 2681.
DR PathwayCommons; Q86TN4; -.
DR SignaLink; Q86TN4; -.
DR BioGRID-ORCS; 83707; 20 hits in 1080 CRISPR screens.
DR ChiTaRS; TRPT1; human.
DR GeneWiki; TRPT1; -.
DR GenomeRNAi; 83707; -.
DR Pharos; Q86TN4; Tdark.
DR PRO; PR:Q86TN4; -.
DR Proteomes; UP000005640; Chromosome 11.
DR RNAct; Q86TN4; protein.
DR Bgee; ENSG00000149743; Expressed in gastrocnemius and 173 other tissues.
DR ExpressionAtlas; Q86TN4; baseline and differential.
DR Genevisible; Q86TN4; HS.
DR GO; GO:0000215; F:tRNA 2'-phosphotransferase activity; IBA:GO_Central.
DR GO; GO:0045859; P:regulation of protein kinase activity; IEA:Ensembl.
DR GO; GO:0008033; P:tRNA processing; IBA:GO_Central.
DR GO; GO:0006388; P:tRNA splicing, via endonucleolytic cleavage and ligation; IBA:GO_Central.
DR Gene3D; 1.10.10.970; -; 1.
DR Gene3D; 3.20.170.30; -; 1.
DR InterPro; IPR002745; Ptrans_KptA/Tpt1.
DR InterPro; IPR042081; RNA_2'-PTrans_C.
DR InterPro; IPR042080; RNA_2'-PTrans_N.
DR PANTHER; PTHR12684; PTHR12684; 1.
DR Pfam; PF01885; PTS_2-RNA; 1.
PE 1: Evidence at protein level;
KW Acetylation; Alternative splicing; NAD; Phosphoprotein; Reference proteome;
KW Transferase; tRNA processing.
FT CHAIN 1..253
FT /note="tRNA 2'-phosphotransferase 1"
FT /id="PRO_0000273363"
FT REGION 1..29
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 225..253
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 14..29
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 227..253
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0007744|PubMed:22814378"
FT MOD_RES 240
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19690332,
FT ECO:0007744|PubMed:23186163"
FT VAR_SEQ 1..49
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_022524"
FT VAR_SEQ 109
FT /note="Q -> QVG (in isoform 4)"
FT /evidence="ECO:0000305"
FT /id="VSP_045827"
FT VAR_SEQ 187..224
FT /note="DGIPFFRSANGVILTPGNTDGFLLPKYFKEALQLRPTR -> G (in
FT isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_045273"
FT VARIANT 3
FT /note="F -> L (in dbSNP:rs12788168)"
FT /id="VAR_030134"
FT VARIANT 172
FT /note="H -> R (in dbSNP:rs1059440)"
FT /evidence="ECO:0000269|PubMed:14504659,
FT ECO:0000269|PubMed:15489334"
FT /id="VAR_030135"
FT VARIANT 221
FT /note="R -> C (in dbSNP:rs11549690)"
FT /id="VAR_030136"
SQ SEQUENCE 253 AA; 27742 MW; 6209F45DC3DB5CBF CRC64;
MNFSGGGRQE AAGSRGRRAP RPREQDRDVQ LSKALSYALR HGALKLGLPM GADGFVPLGT
LLQLPQFRGF SAEDVQRVVD TNRKQRFALQ LGDPSTGLLI RANQGHSLQV PKLELMPLET
PQALPPMLVH GTFWKHWPSI LLKGLSCQGR THIHLAPGLP GDPGIISGMR SHCEIAVFID
GPLALADGIP FFRSANGVIL TPGNTDGFLL PKYFKEALQL RPTRKPLSLA GDEETECQSS
PKHSSRERRR IQQ
