Hmdb loader
Survey
You are using an unsupported browser. Please upgrade your browser to a newer version to get the best experience on Human Metabolome Database.
Identification
HMDB Protein ID HMDBP08885
Secondary Accession Numbers
  • 14613
Name tRNA 2'-phosphotransferase 1
Synonyms Not Available
Gene Name TRPT1
Protein Type Unknown
Biological Properties
General Function Involved in transferase activity, transferring phosphorus-containing groups
Specific Function Catalyzes the last step of tRNA splicing, the transfer of the splice junction 2'-phosphate from ligated tRNA to NAD to produce ADP-ribose 1''-2'' cyclic phosphate (Probable).
Pathways Not Available
Reactions
2'-phospho-[ligated tRNA] + NAD → mature tRNA + ADP ribose 1'',2''-phosphate + Niacinamide + Water details
GO Classification
Biological Process
tRNA splicing, via endonucleolytic cleavage and ligation
Function
catalytic activity
transferase activity
transferase activity, transferring phosphorus-containing groups
Molecular Function
transferase activity, transferring phosphorus-containing groups
tRNA 2'-phosphotransferase activity
Process
rna metabolic process
metabolic process
macromolecule metabolic process
cellular macromolecule metabolic process
rna processing
rna splicing
rna splicing, via endonucleolytic cleavage and ligation
trna splicing, via endonucleolytic cleavage and ligation
Cellular Location Not Available
Gene Properties
Chromosome Location 11
Locus 11q13.1
SNPs TRPT1
Gene Sequence
>762 bp
ATGAACTTCTCTGGAGGAGGGAGGCAGGAAGCAGCAGGGTCCAGGGGTAGAAGGGCTCCC
AGACCCCGAGAACAGGACCGAGACGTGCAGCTGTCCAAGGCTCTGTCCTATGCCCTGCGC
CATGGGGCCTTGAAGCTGGGGCTTCCCATGGGAGCTGATGGCTTCGTGCCCCTGGGCACC
CTCCTGCAGTTGCCCCAGTTCCGCGGCTTCTCTGCTGAAGATGTGCAGCGCGTGGTGGAC
ACCAATAGGAAGCAGCGGTTCGCCCTGCAGCTGGGGGATCCCAGCACTGGCCTTCTCATC
CGGGCCAACCAGGGCCATTCCCTGCAGGTACCTAAGTTGGAGCTGATGCCCCTGGAGACA
CCGCAGGCCCTGCCCCCGATGCTAGTCCATGGTACATTCTGGAAGCACTGGCCATCCATC
CTACTCAAAGGCCTGTCCTGCCAGGGAAGGACGCACATTCACCTGGCCCCAGGACTGCCT
GGAGACCCCGGTATCATCAGTGGCATGCGGTCCCATTGTGAAATAGCTGTGTTCATCGAT
GGACCCCTGGCTCTGGCAGATGGAATACCCTTCTTCCGCTCTGCCAATGGGGTGATTCTG
ACTCCAGGGAATACTGATGGCTTCCTCCTTCCCAAGTACTTCAAGGAGGCCCTGCAGCTA
CGCCCTACCCGAAAGCCCCTTTCCTTGGCTGGTGATGAAGAGACAGAGTGTCAGAGTAGC
CCCAAGCACAGCTCCAGAGAAAGGAGGAGGATCCAACAATAA
Protein Properties
Number of Residues 253
Molecular Weight 27741.69
Theoretical pI 9.985
Pfam Domain Function
Signals Not Available
Transmembrane Regions Not Available
Protein Sequence
>tRNA 2'-phosphotransferase 1
MNFSGGGRQEAAGSRGRRAPRPREQDRDVQLSKALSYALRHGALKLGLPMGADGFVPLGT
LLQLPQFRGFSAEDVQRVVDTNRKQRFALQLGDPSTGLLIRANQGHSLQVPKLELMPLET
PQALPPMLVHGTFWKHWPSILLKGLSCQGRTHIHLAPGLPGDPGIISGMRSHCEIAVFID
GPLALADGIPFFRSANGVILTPGNTDGFLLPKYFKEALQLRPTRKPLSLAGDEETECQSS
PKHSSRERRRIQQ
GenBank ID Protein 238550153
UniProtKB/Swiss-Prot ID Q86TN4
UniProtKB/Swiss-Prot Entry Name TRPT1_HUMAN
PDB IDs Not Available
GenBank Gene ID NM_001033678.3
GeneCard ID TRPT1
GenAtlas ID TRPT1
HGNC ID HGNC:20316
References
General References
  1. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed:15489334 ]
  2. Mayya V, Lundgren DH, Hwang SI, Rezaul K, Wu L, Eng JK, Rodionov V, Han DK: Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions. Sci Signal. 2009 Aug 18;2(84):ra46. doi: 10.1126/scisignal.2000007. [PubMed:19690332 ]
  3. Gauci S, Helbig AO, Slijper M, Krijgsveld J, Heck AJ, Mohammed S: Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach. Anal Chem. 2009 Jun 1;81(11):4493-501. doi: 10.1021/ac9004309. [PubMed:19413330 ]
  4. Taylor TD, Noguchi H, Totoki Y, Toyoda A, Kuroki Y, Dewar K, Lloyd C, Itoh T, Takeda T, Kim DW, She X, Barlow KF, Bloom T, Bruford E, Chang JL, Cuomo CA, Eichler E, FitzGerald MG, Jaffe DB, LaButti K, Nicol R, Park HS, Seaman C, Sougnez C, Yang X, Zimmer AR, Zody MC, Birren BW, Nusbaum C, Fujiyama A, Hattori M, Rogers J, Lander ES, Sakaki Y: Human chromosome 11 DNA sequence and analysis including novel gene identification. Nature. 2006 Mar 23;440(7083):497-500. [PubMed:16554811 ]
  5. Hu QD, Lu H, Huo K, Ying K, Li J, Xie Y, Mao Y, Li YY: A human homolog of the yeast gene encoding tRNA 2'-phosphotransferase: cloning, characterization and complementation analysis. Cell Mol Life Sci. 2003 Aug;60(8):1725-32. [PubMed:14504659 ]