ID G3V5H9_HUMAN Unreviewed; 259 AA. AC G3V5H9; DT 16-NOV-2011, integrated into UniProtKB/TrEMBL. DT 16-NOV-2011, sequence version 1. DT 27-MAR-2024, entry version 73. DE SubName: Full=Tyrosyl-DNA phosphodiesterase 1 {ECO:0000313|Ensembl:ENSP00000452363.1}; GN Name=TDP1 {ECO:0000313|Ensembl:ENSP00000452363.1}; 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 {ECO:0000313|Ensembl:ENSP00000452363.1, ECO:0000313|Proteomes:UP000005640}; RN [1] {ECO:0000313|Ensembl:ENSP00000452363.1, ECO:0000313|Proteomes:UP000005640} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=12508121; DOI=10.1038/nature01348; RA Heilig R., Eckenberg R., Petit J.-L., Fonknechten N., Da Silva C., RA Cattolico L., Levy M., Barbe V., De Berardinis V., Ureta-Vidal A., RA Pelletier E., Vico V., Anthouard V., Rowen L., Madan A., Qin S., Sun H., RA Du H., Pepin K., Artiguenave F., Robert C., Cruaud C., Bruels T., RA Jaillon O., Friedlander L., Samson G., Brottier P., Cure S., Segurens B., RA Aniere F., Samain S., Crespeau H., Abbasi N., Aiach N., Boscus D., RA Dickhoff R., Dors M., Dubois I., Friedman C., Gouyvenoux M., James R., RA Madan A., Mairey-Estrada B., Mangenot S., Martins N., Menard M., Oztas S., RA Ratcliffe A., Shaffer T., Trask B., Vacherie B., Bellemere C., Belser C., RA Besnard-Gonnet M., Bartol-Mavel D., Boutard M., Briez-Silla S., RA Combette S., Dufosse-Laurent V., Ferron C., Lechaplais C., Louesse C., RA Muselet D., Magdelenat G., Pateau E., Petit E., Sirvain-Trukniewicz P., RA Trybou A., Vega-Czarny N., Bataille E., Bluet E., Bordelais I., Dubois M., RA Dumont C., Guerin T., Haffray S., Hammadi R., Muanga J., Pellouin V., RA Robert D., Wunderle E., Gauguet G., Roy A., Sainte-Marthe L., Verdier J., RA Verdier-Discala C., Hillier L.W., Fulton L., McPherson J., Matsuda F., RA Wilson R., Scarpelli C., Gyapay G., Wincker P., Saurin W., Quetier F., RA Waterston R., Hood L., Weissenbach J.; RT "The DNA sequence and analysis of human chromosome 14."; RL Nature 421:601-607(2003). RN [2] {ECO:0007829|PubMed:17081983} RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=17081983; DOI=10.1016/j.cell.2006.09.026; RA Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.; RT "Global, in vivo, and site-specific phosphorylation dynamics in signaling RT networks."; RL Cell 127:635-648(2006). RN [3] {ECO:0007829|PubMed:18669648} RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. 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 [4] {ECO:0007829|PubMed:19690332} RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. 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 [5] {ECO:0007829|PubMed:21269460} RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=21269460; DOI=10.1186/1752-0509-5-17; RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Burckstummer T., RA Bennett K.L., Superti-Furga G., Colinge J.; RT "Initial characterization of the human central proteome."; RL BMC Syst. Biol. 5:17-17(2011). RN [6] {ECO:0007829|PubMed:23186163} RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=23186163; 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] {ECO:0000313|Ensembl:ENSP00000452363.1} RP IDENTIFICATION. RG Ensembl; RL Submitted (NOV-2023) to UniProtKB. CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}. CC -!- SIMILARITY: Belongs to the tyrosyl-DNA phosphodiesterase family. CC {ECO:0000256|ARBA:ARBA00010205}. 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; AL137128; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR AlphaFoldDB; G3V5H9; -. DR SMR; G3V5H9; -. DR MassIVE; G3V5H9; -. DR MaxQB; G3V5H9; -. DR PeptideAtlas; G3V5H9; -. DR ProteomicsDB; 33530; -. DR Ensembl; ENST00000555178.5; ENSP00000452363.1; ENSG00000042088.14. DR UCSC; uc059efr.1; human. DR HGNC; HGNC:18884; TDP1. DR VEuPathDB; HostDB:ENSG00000042088; -. DR GeneTree; ENSGT00390000002211; -. DR ChiTaRS; TDP1; human. DR Proteomes; UP000005640; Chromosome 14. DR Bgee; ENSG00000042088; Expressed in oocyte and 143 other cell types or tissues. DR ExpressionAtlas; G3V5H9; baseline and differential. DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell. DR GO; GO:0004518; F:nuclease activity; IEA:UniProtKB-KW. DR GO; GO:0008081; F:phosphoric diester hydrolase activity; IEA:InterPro. DR GO; GO:0006281; P:DNA repair; IEA:UniProtKB-KW. DR Gene3D; 3.30.870.10; Endonuclease Chain A; 1. DR InterPro; IPR010347; Tdp1. DR PANTHER; PTHR12415; TYROSYL-DNA PHOSPHODIESTERASE 1; 1. DR PANTHER; PTHR12415:SF0; TYROSYL-DNA PHOSPHODIESTERASE 1; 1. DR Pfam; PF06087; Tyr-DNA_phospho; 1. DR SUPFAM; SSF56024; Phospholipase D/nuclease; 1. PE 1: Evidence at protein level; KW DNA damage {ECO:0000256|ARBA:ARBA00022763}; KW DNA repair {ECO:0000256|ARBA:ARBA00023204}; KW Hydrolase {ECO:0000256|ARBA:ARBA00022801}; KW Nuclease {ECO:0000256|ARBA:ARBA00022722}; KW Nucleus {ECO:0000256|ARBA:ARBA00023242}; KW Proteomics identification {ECO:0007829|EPD:G3V5H9, KW ECO:0007829|MaxQB:G3V5H9}; KW Reference proteome {ECO:0000313|Proteomes:UP000005640}. FT REGION 1..101 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 13..27 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 64..88 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" SQ SEQUENCE 259 AA; 29042 MW; E26A1F2AA60DA632 CRC64; MSQEGDYGRW TISSSDESEE EKPKPDKPST SSLLCARQGA ANEPRYTCSE AQKAAHKRKI SPVKFSNTDS VLPPKRQKSG SQEDLGWCLS SSDDELQPEM PQKQAEKVVI KKEKDISAPN DGTAQRTENH GAPACHRLKE EEDEYETSGE GQDIWDMLDK GNPFQFYLTR VSGVKPKYNS GALHIKDILS PLFGTLVSSA QFNYCFDVDW LVKQYPPEFR KKPILLVHGD KREAKAHLHA QAKPYENISL CQENDAAAL //