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   27-MAR-2024, entry version 147.
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-alpha-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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
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   PDB; 7YW3; X-ray; 2.50 A; A=1-253.
DR   PDBsum; 7YW3; -.
DR   AlphaFoldDB; Q86TN4; -.
DR   SMR; Q86TN4; -.
DR   BioGRID; 123736; 15.
DR   IntAct; Q86TN4; 6.
DR   MINT; Q86TN4; -.
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; 9606-ENSP00000378050; -.
DR   PeptideAtlas; Q86TN4; -.
DR   ProteomicsDB; 2072; -.
DR   ProteomicsDB; 25919; -.
DR   ProteomicsDB; 69716; -. [Q86TN4-1]
DR   ProteomicsDB; 69717; -. [Q86TN4-2]
DR   Pumba; Q86TN4; -.
DR   Antibodypedia; 51851; 40 antibodies from 15 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   AGR; HGNC:20316; -.
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   InParanoid; Q86TN4; -.
DR   OMA; YLYHGTV; -.
DR   OrthoDB; 443016at2759; -.
DR   PhylomeDB; Q86TN4; -.
DR   TreeFam; TF324127; -.
DR   BRENDA; 2.7.1.160; 2681.
DR   PathwayCommons; Q86TN4; -.
DR   SignaLink; Q86TN4; -.
DR   BioGRID-ORCS; 83707; 21 hits in 1155 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 175 other cell types or tissues.
DR   ExpressionAtlas; Q86TN4; baseline and differential.
DR   GO; GO:0000215; F:tRNA 2'-phosphotransferase activity; IBA:GO_Central.
DR   GO; GO:0006388; P:tRNA splicing, via endonucleolytic cleavage and ligation; IBA:GO_Central.
DR   Gene3D; 3.20.170.30; -; 1.
DR   Gene3D; 1.10.10.970; RNA 2'-phosphotransferase, Tpt1/KptA family, N-terminal domain; 1.
DR   InterPro; IPR002745; Ptrans_KptA/Tpt1.
DR   InterPro; IPR042081; RNA_2'-PTrans_C.
DR   InterPro; IPR042080; RNA_2'-PTrans_N.
DR   PANTHER; PTHR12684; PUTATIVE PHOSPHOTRANSFERASE; 1.
DR   PANTHER; PTHR12684:SF2; TRNA 2'-PHOSPHOTRANSFERASE 1; 1.
DR   Pfam; PF01885; PTS_2-RNA; 1.
DR   SUPFAM; SSF56399; ADP-ribosylation; 1.
DR   Genevisible; Q86TN4; HS.
PE   1: Evidence at protein level;
KW   3D-structure; Acetylation; Alternative splicing; NAD; Phosphoprotein;
KW   Reference proteome; 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"
FT   HELIX           26..40
FT                   /evidence="ECO:0007829|PDB:7YW3"
FT   TURN            44..47
FT                   /evidence="ECO:0007829|PDB:7YW3"
FT   HELIX           58..62
FT                   /evidence="ECO:0007829|PDB:7YW3"
FT   TURN            65..69
FT                   /evidence="ECO:0007829|PDB:7YW3"
FT   HELIX           72..81
FT                   /evidence="ECO:0007829|PDB:7YW3"
FT   STRAND          87..93
FT                   /evidence="ECO:0007829|PDB:7YW3"
FT   TURN            94..96
FT                   /evidence="ECO:0007829|PDB:7YW3"
FT   STRAND          97..104
FT                   /evidence="ECO:0007829|PDB:7YW3"
FT   STRAND          115..117
FT                   /evidence="ECO:0007829|PDB:7YW3"
FT   HELIX           121..123
FT                   /evidence="ECO:0007829|PDB:7YW3"
FT   STRAND          128..132
FT                   /evidence="ECO:0007829|PDB:7YW3"
FT   TURN            134..136
FT                   /evidence="ECO:0007829|PDB:7YW3"
FT   HELIX           137..143
FT                   /evidence="ECO:0007829|PDB:7YW3"
FT   STRAND          150..158
FT                   /evidence="ECO:0007829|PDB:7YW3"
FT   STRAND          174..179
FT                   /evidence="ECO:0007829|PDB:7YW3"
FT   HELIX           181..186
FT                   /evidence="ECO:0007829|PDB:7YW3"
FT   STRAND          192..194
FT                   /evidence="ECO:0007829|PDB:7YW3"
FT   STRAND          199..201
FT                   /evidence="ECO:0007829|PDB:7YW3"
FT   STRAND          204..209
FT                   /evidence="ECO:0007829|PDB:7YW3"
FT   HELIX           211..213
FT                   /evidence="ECO:0007829|PDB:7YW3"
FT   STRAND          214..219
FT                   /evidence="ECO:0007829|PDB:7YW3"
FT   STRAND          221..223
FT                   /evidence="ECO:0007829|PDB:7YW3"
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
//