DNPH1_HUMAN
ID DNPH1_HUMAN Reviewed; 174 AA.
AC O43598; B2LUJ9;
DT 10-MAY-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-1998, sequence version 1.
DT 03-AUG-2022, entry version 165.
DE RecName: Full=2'-deoxynucleoside 5'-phosphate N-hydrolase 1 {ECO:0000255|HAMAP-Rule:MF_03036};
DE EC=3.2.2.- {ECO:0000255|HAMAP-Rule:MF_03036, ECO:0000269|PubMed:24260472, ECO:0000269|PubMed:25108359};
DE AltName: Full=c-Myc-responsive protein RCL {ECO:0000255|HAMAP-Rule:MF_03036};
GN Name=DNPH1 {ECO:0000255|HAMAP-Rule:MF_03036};
GN Synonyms=C6orf108, RCL {ECO:0000255|HAMAP-Rule:MF_03036};
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).
RC TISSUE=Liver;
RX PubMed=9271375; DOI=10.1128/mcb.17.9.4967;
RA Lewis B.C., Shim H., Li Q., Wu C.S., Lee L.A., Maity A., Dang C.V.;
RT "Identification of putative c-Myc-responsive genes: characterization of
RT rcl, a novel growth-related gene.";
RL Mol. Cell. Biol. 17:4967-4978(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), SUBCELLULAR LOCATION, TISSUE
RP SPECIFICITY, AND INDUCTION.
RC TISSUE=Kidney;
RX PubMed=18726892; DOI=10.1002/jcb.21884;
RA Shin S., Bosc D.G., Ingle J.N., Spelsberg T.C., Janknecht R.;
RT "Rcl is a novel ETV1/ER81 target gene upregulated in breast tumors.";
RL J. Cell. Biochem. 105:866-874(2008).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC TISSUE=Liver;
RX PubMed=14574404; DOI=10.1038/nature02055;
RA Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L.,
RA Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., Gilbert J.G.R.,
RA Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D.,
RA Andrews T.D., Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J.,
RA Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H.,
RA Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J.,
RA Brown J.Y., Burford D.C., Burrill W., Burton J., Carder C., Carter N.P.,
RA Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V.,
RA Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J.,
RA Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., Ellington A.E.,
RA Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J.,
RA French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J.,
RA Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C.,
RA Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A.,
RA Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R.,
RA Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M.,
RA Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K.,
RA Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R.,
RA Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M.,
RA Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A.,
RA Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L.,
RA Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I.,
RA Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y.,
RA Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E.,
RA Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A.,
RA Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W.,
RA Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M.,
RA West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J.,
RA Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M.,
RA Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I.,
RA Rogers J., Beck S.;
RT "The DNA sequence and analysis of human chromosome 6.";
RL Nature 425:805-811(2003).
RN [4]
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC TISSUE=Uterus;
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 [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-169, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
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 [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-28 AND SER-169, AND
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 [8]
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 [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-169, 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 [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-169, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [11]
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., Buerckstuemmer 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 [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-169, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T.,
RA Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.;
RT "System-wide temporal characterization of the proteome and phosphoproteome
RT of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [13]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=22223895; DOI=10.1074/mcp.m111.015131;
RA Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T.,
RA Giglione C.;
RT "Comparative large-scale characterisation of plant vs. mammal proteins
RT reveals similar and idiosyncratic N-alpha acetylation features.";
RL Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012).
RN [14]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [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 [15]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-28; SER-123 AND SER-169, AND
RP IDENTIFICATION BY 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).
RN [16]
RP FUNCTION, CATALYTIC ACTIVITY, AND BIOPHYSICOCHEMICAL PROPERTIES.
RX PubMed=24260472; DOI=10.1371/journal.pone.0080755;
RA Amiable C., Pochet S., Padilla A., Labesse G., Kaminski P.A.;
RT "N (6)-substituted AMPs inhibit mammalian deoxynucleotide N-hydrolase
RT DNPH1.";
RL PLoS ONE 8:E80755-E80755(2013).
RN [17]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-98; SER-128; SER-138 AND
RP SER-169, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [18]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25944712; DOI=10.1002/pmic.201400617;
RA Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., Ayoub D.,
RA Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
RT "N-terminome analysis of the human mitochondrial proteome.";
RL Proteomics 15:2519-2524(2015).
RN [19]
RP X-RAY CRYSTALLOGRAPHY (1.35 ANGSTROMS) OF 20-162 IN COMPLEX WITH THE
RP SUBSTRATE ANALOG
RP 6-(NAPHTHALEN-2-YL)-9-(5-O-PHOSPHONO-BETA-D-RIBOFURANOSYL)-9H-PURINE,
RP CATALYTIC ACTIVITY, FUNCTION, AND SUBUNIT.
RX PubMed=25108359; DOI=10.1016/j.ejmech.2014.07.110;
RA Amiable C., Paoletti J., Haouz A., Padilla A., Labesse G., Kaminski P.A.,
RA Pochet S.;
RT "6-(Hetero)Arylpurine nucleotides as inhibitors of the oncogenic target
RT DNPH1: Synthesis, structural studies and cytotoxic activities.";
RL Eur. J. Med. Chem. 85C:418-437(2014).
CC -!- FUNCTION: Catalyzes the cleavage of the N-glycosidic bond of
CC deoxyribonucleoside 5'-monophosphates to yield deoxyribose 5-phosphate
CC and a purine or pyrimidine base. Deoxyribonucleoside 5'-monophosphates
CC containing purine bases are preferred to those containing pyrimidine
CC bases. {ECO:0000255|HAMAP-Rule:MF_03036, ECO:0000269|PubMed:24260472,
CC ECO:0000269|PubMed:25108359}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a pyrimidine 2'-deoxyribonucleoside 5'-phosphate + H2O = 2-
CC deoxy-D-ribose 5-phosphate + a pyrimidine nucleobase;
CC Xref=Rhea:RHEA:57852, ChEBI:CHEBI:15377, ChEBI:CHEBI:26432,
CC ChEBI:CHEBI:62877, ChEBI:CHEBI:142209; Evidence={ECO:0000255|HAMAP-
CC Rule:MF_03036, ECO:0000269|PubMed:24260472,
CC ECO:0000269|PubMed:25108359};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a purine 2'-deoxyribonucleoside 5'-phosphate + H2O = 2-deoxy-
CC D-ribose 5-phosphate + a purine nucleobase; Xref=Rhea:RHEA:51132,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:26386, ChEBI:CHEBI:62877,
CC ChEBI:CHEBI:142198; Evidence={ECO:0000255|HAMAP-Rule:MF_03036,
CC ECO:0000269|PubMed:24260472, ECO:0000269|PubMed:25108359};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=57 uM for dGMP {ECO:0000269|PubMed:24260472};
CC KM=97 uM for dAMP {ECO:0000269|PubMed:24260472};
CC KM=104 uM for dIMP {ECO:0000269|PubMed:24260472};
CC KM=2500 uM for dCMP {ECO:0000269|PubMed:24260472};
CC KM=7800 uM for dUMP {ECO:0000269|PubMed:24260472};
CC KM=25000 uM for dTMP {ECO:0000269|PubMed:24260472};
CC Note=kcat is 0.002 sec(-1) with dGMP as substrate. kcat is 0.0025
CC sec(-1) with dAMP as substrate. kcat is 0.0016 sec(-1) with dIMP as
CC substrate. kcat is 0.2 sec(-1) with dUMP as substrate. kcat is 0.0083
CC sec(-1) with dCMP as substrate. kcat is 0.025 sec(-1) with dTMP as
CC substrate. {ECO:0000269|PubMed:24260472};
CC -!- SUBUNIT: Monomer and homodimer. {ECO:0000255|HAMAP-Rule:MF_03036,
CC ECO:0000269|PubMed:25108359}.
CC -!- INTERACTION:
CC O43598; Q96D03: DDIT4L; NbExp=5; IntAct=EBI-748674, EBI-742054;
CC O43598; O43598: DNPH1; NbExp=5; IntAct=EBI-748674, EBI-748674;
CC O43598; Q92993: KAT5; NbExp=3; IntAct=EBI-748674, EBI-399080;
CC O43598; Q8TAP4-4: LMO3; NbExp=3; IntAct=EBI-748674, EBI-11742507;
CC O43598; P17252: PRKCA; NbExp=3; IntAct=EBI-748674, EBI-1383528;
CC O43598; Q15047-2: SETDB1; NbExp=3; IntAct=EBI-748674, EBI-9090795;
CC O43598; P54274: TERF1; NbExp=2; IntAct=EBI-748674, EBI-710997;
CC O43598; P61981: YWHAG; NbExp=3; IntAct=EBI-748674, EBI-359832;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_03036,
CC ECO:0000269|PubMed:18726892}. Nucleus {ECO:0000255|HAMAP-
CC Rule:MF_03036}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=O43598-1; Sequence=Displayed;
CC Name=2;
CC IsoId=O43598-2; Sequence=VSP_040509, VSP_040510;
CC -!- TISSUE SPECIFICITY: Expressed at low levels in brain, colon, lung,
CC peripheral blood leukocytes, placenta, small intestine, and thymus.
CC Expressed at high levels in heart, kidney, liver, skeletal muscle and
CC spleen. Overexpressed in a significant proportion of breast cancers.
CC {ECO:0000269|PubMed:18726892}.
CC -!- INDUCTION: Expression is induced by ETV1.
CC {ECO:0000269|PubMed:18726892}.
CC -!- SIMILARITY: Belongs to the 2'-deoxynucleoside 5'-phosphate N-hydrolase
CC 1 family. {ECO:0000255|HAMAP-Rule:MF_03036}.
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; AF040105; AAB96766.1; -; mRNA.
DR EMBL; EU585603; ACB87500.1; -; mRNA.
DR EMBL; AL133375; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471081; EAX04166.1; -; Genomic_DNA.
DR EMBL; BC011683; AAH11683.1; -; mRNA.
DR EMBL; BQ052226; -; NOT_ANNOTATED_CDS; mRNA.
DR CCDS; CCDS43465.1; -. [O43598-2]
DR CCDS; CCDS4891.1; -. [O43598-1]
DR RefSeq; NP_006434.1; NM_006443.2. [O43598-1]
DR RefSeq; NP_954653.1; NM_199184.1. [O43598-2]
DR PDB; 4P5E; X-ray; 1.35 A; A/B=20-162.
DR PDBsum; 4P5E; -.
DR AlphaFoldDB; O43598; -.
DR SMR; O43598; -.
DR BioGRID; 115840; 19.
DR IntAct; O43598; 11.
DR STRING; 9606.ENSP00000230431; -.
DR BindingDB; O43598; -.
DR ChEMBL; CHEMBL3351218; -.
DR DrugCentral; O43598; -.
DR GlyGen; O43598; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; O43598; -.
DR PhosphoSitePlus; O43598; -.
DR SwissPalm; O43598; -.
DR BioMuta; DNPH1; -.
DR EPD; O43598; -.
DR jPOST; O43598; -.
DR MassIVE; O43598; -.
DR MaxQB; O43598; -.
DR PaxDb; O43598; -.
DR PeptideAtlas; O43598; -.
DR PRIDE; O43598; -.
DR ProteomicsDB; 49070; -. [O43598-1]
DR ProteomicsDB; 49071; -. [O43598-2]
DR TopDownProteomics; O43598-1; -. [O43598-1]
DR Antibodypedia; 30354; 195 antibodies from 31 providers.
DR DNASU; 10591; -.
DR Ensembl; ENST00000230431.11; ENSP00000230431.7; ENSG00000112667.13. [O43598-1]
DR Ensembl; ENST00000393987.2; ENSP00000377556.2; ENSG00000112667.13. [O43598-2]
DR GeneID; 10591; -.
DR KEGG; hsa:10591; -.
DR MANE-Select; ENST00000230431.11; ENSP00000230431.7; NM_006443.3; NP_006434.1.
DR UCSC; uc003ouo.4; human. [O43598-1]
DR CTD; 10591; -.
DR DisGeNET; 10591; -.
DR GeneCards; DNPH1; -.
DR HGNC; HGNC:21218; DNPH1.
DR HPA; ENSG00000112667; Low tissue specificity.
DR MIM; 618762; gene.
DR neXtProt; NX_O43598; -.
DR OpenTargets; ENSG00000112667; -.
DR PharmGKB; PA134918815; -.
DR VEuPathDB; HostDB:ENSG00000112667; -.
DR eggNOG; ENOG502S2J2; Eukaryota.
DR GeneTree; ENSGT00390000001216; -.
DR OMA; MHIYFCG; -.
DR OrthoDB; 1533988at2759; -.
DR PhylomeDB; O43598; -.
DR TreeFam; TF329719; -.
DR PathwayCommons; O43598; -.
DR Reactome; R-HSA-74259; Purine catabolism.
DR SignaLink; O43598; -.
DR BioGRID-ORCS; 10591; 7 hits in 1074 CRISPR screens.
DR ChiTaRS; DNPH1; human.
DR GenomeRNAi; 10591; -.
DR Pharos; O43598; Tchem.
DR PRO; PR:O43598; -.
DR Proteomes; UP000005640; Chromosome 6.
DR RNAct; O43598; protein.
DR Bgee; ENSG00000112667; Expressed in right uterine tube and 157 other tissues.
DR ExpressionAtlas; O43598; baseline and differential.
DR Genevisible; O43598; HS.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0070694; F:deoxyribonucleoside 5'-monophosphate N-glycosidase activity; IDA:UniProtKB.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0042803; F:protein homodimerization activity; IEA:UniProtKB-UniRule.
DR GO; GO:0009159; P:deoxyribonucleoside monophosphate catabolic process; IDA:UniProtKB.
DR GO; GO:0030855; P:epithelial cell differentiation; IEP:UniProtKB.
DR GO; GO:0009116; P:nucleoside metabolic process; IEA:UniProtKB-UniRule.
DR GO; GO:0030307; P:positive regulation of cell growth; ISS:UniProtKB.
DR GO; GO:0006195; P:purine nucleotide catabolic process; TAS:Reactome.
DR HAMAP; MF_03036; Nuc_phosphate_hydrolase; 1.
DR InterPro; IPR028607; DNPH1.
DR InterPro; IPR007710; Nucleoside_deoxyribTrfase.
DR Pfam; PF05014; Nuc_deoxyrib_tr; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Alternative splicing; Cytoplasm; Glycosidase;
KW Hydrolase; Nucleotide metabolism; Nucleus; Phosphoprotein;
KW Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0007744|PubMed:22223895,
FT ECO:0007744|PubMed:22814378"
FT CHAIN 2..174
FT /note="2'-deoxynucleoside 5'-phosphate N-hydrolase 1"
FT /id="PRO_0000097200"
FT BINDING 24..30
FT /ligand="substrate"
FT /ligand_note="ligand shared between homodimeric partners"
FT /note="in other chain"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03036,
FT ECO:0000269|PubMed:25108359"
FT BINDING 39
FT /ligand="substrate"
FT /ligand_note="ligand shared between homodimeric partners"
FT /note="in other chain"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03036"
FT BINDING 56
FT /ligand="substrate"
FT /ligand_note="ligand shared between homodimeric partners"
FT /note="in other chain"
FT /evidence="ECO:0000269|PubMed:25108359"
FT BINDING 104
FT /ligand="substrate"
FT /ligand_note="ligand shared between homodimeric partners"
FT /note="in other chain"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03036,
FT ECO:0000269|PubMed:25108359"
FT BINDING 128..130
FT /ligand="substrate"
FT /ligand_note="ligand shared between homodimeric partners"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03036"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0007744|PubMed:22223895,
FT ECO:0007744|PubMed:22814378"
FT MOD_RES 28
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 98
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 123
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 128
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 138
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 169
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17081983,
FT ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:19690332,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
FT ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569"
FT VAR_SEQ 126..148
FT /note="VLSAMIRGAADGSRFQVWDYEEG -> GEHPKPPSWLSMDPALSSFPGGL
FT (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_040509"
FT VAR_SEQ 149..174
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_040510"
FT STRAND 22..26
FT /evidence="ECO:0007829|PDB:4P5E"
FT HELIX 36..46
FT /evidence="ECO:0007829|PDB:4P5E"
FT TURN 47..49
FT /evidence="ECO:0007829|PDB:4P5E"
FT STRAND 50..53
FT /evidence="ECO:0007829|PDB:4P5E"
FT HELIX 55..58
FT /evidence="ECO:0007829|PDB:4P5E"
FT TURN 68..71
FT /evidence="ECO:0007829|PDB:4P5E"
FT HELIX 73..86
FT /evidence="ECO:0007829|PDB:4P5E"
FT STRAND 88..93
FT /evidence="ECO:0007829|PDB:4P5E"
FT HELIX 99..110
FT /evidence="ECO:0007829|PDB:4P5E"
FT STRAND 115..119
FT /evidence="ECO:0007829|PDB:4P5E"
FT HELIX 121..123
FT /evidence="ECO:0007829|PDB:4P5E"
FT HELIX 129..134
FT /evidence="ECO:0007829|PDB:4P5E"
FT STRAND 137..144
FT /evidence="ECO:0007829|PDB:4P5E"
FT HELIX 147..149
FT /evidence="ECO:0007829|PDB:4P5E"
FT HELIX 150..160
FT /evidence="ECO:0007829|PDB:4P5E"
SQ SEQUENCE 174 AA; 19108 MW; C148641A60F383A3 CRC64;
MAAAMVPGRS ESWERGEPGR PALYFCGSIR GGREDRTLYE RIVSRLRRFG TVLTEHVAAA
ELGARGEEAA GGDRLIHEQD LEWLQQADVV VAEVTQPSLG VGYELGRAVA FNKRILCLFR
PQSGRVLSAM IRGAADGSRF QVWDYEEGEV EALLDRYFEA DPPGQVAASP DPTT
