Full text data of DNPH1
DNPH1
(C6orf108, RCL)
[Confidence: low (only semi-automatic identification from reviews)]
2'-deoxynucleoside 5'-phosphate N-hydrolase 1; 3.2.2.- (c-Myc-responsive protein RCL)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
2'-deoxynucleoside 5'-phosphate N-hydrolase 1; 3.2.2.- (c-Myc-responsive protein RCL)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
UniProt
O43598
ID DNPH1_HUMAN Reviewed; 174 AA.
AC O43598; B2LUJ9;
DT 10-MAY-2005, integrated into UniProtKB/Swiss-Prot.
read moreDT 01-JUN-1998, sequence version 1.
DT 22-JAN-2014, entry version 99.
DE RecName: Full=2'-deoxynucleoside 5'-phosphate N-hydrolase 1;
DE EC=3.2.2.-;
DE AltName: Full=c-Myc-responsive protein RCL;
GN Name=DNPH1; Synonyms=C6orf108, RCL;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC TISSUE=Liver;
RX PubMed=9271375;
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
RT of 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.,
RA Gilbert J.G.R., Clamp M.E., Bethel G., Milne S., Ainscough R.,
RA Almeida J.P., Ambrose K.D., Andrews T.D., Ashwell R.I.S.,
RA Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Barker D.J.,
RA Barlow K.F., Bates K., Beare D.M., Beasley H., Beasley O., Bird C.P.,
RA Blakey S.E., Bray-Allen S., Brook J., Brown A.J., Brown J.Y.,
RA 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.,
RA Ellington A.E., Evans K.A., Faulkner L., Francis M.D., Frankish A.,
RA Frankland J., French L., Garner P., Garnett J., Ghori M.J.,
RA Gilby L.M., Gillson C.J., Glithero R.J., Grafham D.V., Grant M.,
RA Gribble S., Griffiths C., Griffiths M.N.D., Hall R., Halls K.S.,
RA Hammond S., Harley J.L., Hart E.A., Heath P.D., Heathcott R.,
RA Holmes S.J., Howden P.J., Howe K.L., Howell G.R., Huckle E.,
RA Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., Joy A.A.,
RA Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., Langford C.,
RA Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., Lloyd D.M.,
RA Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M.,
RA Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K.,
RA McMurray A., Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T.,
RA Novik K.L., Oliver K., Overton-Larty E.K., Parker A., Patel R.,
RA Pearce A.V., Peck A.I., Phillimore B.J.C.T., Phillips S., Plumb R.W.,
RA Porter K.M., Ramsey Y., Ranby S.A., Rice C.M., Ross M.T., Searle S.M.,
RA Sehra H.K., Sheridan E., Skuce C.D., Smith S., Smith M., Spraggon L.,
RA Squares S.L., Steward C.A., Sycamore N., Tamlyn-Hall G., Tester J.,
RA Theaker A.J., Thomas D.W., Thorpe A., Tracey A., Tromans A., Tubby B.,
RA Wall M., Wallis J.M., West A.P., White S.S., Whitehead S.L.,
RA Whittaker H., Wild A., Willey D.J., Wilmer T.E., Wood J.M., Wray P.W.,
RA Wyatt J.C., Young L., Younger R.M., Bentley D.R., Coulson A.,
RA Durbin R.M., Hubbard T., Sulston J.E., Dunham I., 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.,
RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA 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
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-169, AND MASS
RP SPECTROMETRY.
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.,
RA Mann M.;
RT "Global, in vivo, and site-specific phosphorylation dynamics in
RT signaling networks.";
RL Cell 127:635-648(2006).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-28 AND SER-169, AND MASS
RP SPECTROMETRY.
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.,
RA Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in
RT a refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-169, AND MASS
RP SPECTROMETRY.
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 MASS
RP SPECTROMETRY.
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.,
RA Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full
RT phosphorylation 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.,
RA Buerckstuemmer T., 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 MASS
RP SPECTROMETRY.
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J.,
RA Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V.,
RA Blagoev B.;
RT "System-wide temporal characterization of the proteome and
RT phosphoproteome of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [13]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, MASS SPECTROMETRY, AND
RP CLEAVAGE OF INITIATOR METHIONINE.
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.,
RA Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K.,
RA Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-
RT terminal acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
CC -!- FUNCTION: Catalyzes the cleavage of the N-glycosidic bond of
CC deoxyribonucleoside 5'-monophosphates to yield deoxyribose 5-
CC phosphate and a purine or pyrimidine base. Deoxyribonucleoside 5'-
CC monophosphates containing purine bases are preferred to those
CC containing pyrimidine bases (By similarity).
CC -!- CATALYTIC ACTIVITY: A deoxyribonucleoside 5'-monophosphate + H(2)0
CC = deoxyribose 5-monophosphate + a purine or pyrimidine base.
CC -!- SUBUNIT: Monomer and homodimer (By similarity).
CC -!- SUBCELLULAR LOCATION: Cytoplasm. Nucleus (By similarity).
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
CC thymus. Expressed at high levels in heart, kidney, liver, skeletal
CC muscle and spleen. Overexpressed in a significant proportion of
CC breast cancers.
CC -!- INDUCTION: Expression is induced by ETV1.
CC -!- SIMILARITY: Belongs to the 2'-deoxynucleoside 5'-phosphate N-
CC hydrolase 1 family.
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DR EMBL; AF040105; AAB96766.1; -; mRNA.
DR EMBL; EU585603; ACB87500.1; -; mRNA.
DR EMBL; AL133375; CAI20205.1; -; Genomic_DNA.
DR EMBL; CH471081; EAX04166.1; -; Genomic_DNA.
DR EMBL; BC011683; AAH11683.1; -; mRNA.
DR EMBL; BQ052226; -; NOT_ANNOTATED_CDS; mRNA.
DR RefSeq; NP_006434.1; NM_006443.2.
DR RefSeq; NP_954653.1; NM_199184.1.
DR UniGene; Hs.109752; -.
DR ProteinModelPortal; O43598; -.
DR SMR; O43598; 20-160.
DR IntAct; O43598; 1.
DR MINT; MINT-5002237; -.
DR PhosphoSite; O43598; -.
DR PaxDb; O43598; -.
DR PeptideAtlas; O43598; -.
DR PRIDE; O43598; -.
DR Ensembl; ENST00000230431; ENSP00000230431; ENSG00000112667.
DR Ensembl; ENST00000393987; ENSP00000377556; ENSG00000112667.
DR GeneID; 10591; -.
DR KEGG; hsa:10591; -.
DR UCSC; uc003ouo.3; human.
DR CTD; 10591; -.
DR GeneCards; GC06M043193; -.
DR HGNC; HGNC:21218; DNPH1.
DR HPA; HPA029675; -.
DR HPA; HPA029676; -.
DR neXtProt; NX_O43598; -.
DR PharmGKB; PA134918815; -.
DR eggNOG; NOG08389; -.
DR HOGENOM; HOG000015361; -.
DR HOVERGEN; HBG079123; -.
DR InParanoid; O43598; -.
DR OrthoDB; EOG7CNZHC; -.
DR PhylomeDB; O43598; -.
DR GenomeRNAi; 10591; -.
DR NextBio; 40219; -.
DR PRO; PR:O43598; -.
DR ArrayExpress; O43598; -.
DR Bgee; O43598; -.
DR CleanEx; HS_C6orf108; -.
DR Genevestigator; O43598; -.
DR GO; GO:0005737; C:cytoplasm; IDA:HPA.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0070694; F:deoxyribonucleoside 5'-monophosphate N-glycosidase activity; ISS:UniProtKB.
DR GO; GO:0050144; F:nucleoside deoxyribosyltransferase activity; IEA:InterPro.
DR GO; GO:0008283; P:cell proliferation; TAS:ProtInc.
DR GO; GO:0009159; P:deoxyribonucleoside monophosphate catabolic process; ISS:UniProtKB.
DR GO; GO:0009117; P:nucleotide metabolic process; IEA:UniProtKB-KW.
DR GO; GO:0030307; P:positive regulation of cell growth; ISS:UniProtKB.
DR Gene3D; 3.40.50.1810; -; 1.
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 Acetylation; Alternative splicing; Complete proteome; Cytoplasm;
KW Glycosidase; Hydrolase; Nucleotide metabolism; Nucleus;
KW Phosphoprotein; Reference proteome.
FT INIT_MET 1 1 Removed.
FT CHAIN 2 174 2'-deoxynucleoside 5'-phosphate N-
FT hydrolase 1.
FT /FTId=PRO_0000097200.
FT REGION 24 30 Substrate binding (By similarity).
FT REGION 128 130 Substrate binding; shared with
FT homodimeric partner (By similarity).
FT BINDING 39 39 Substrate (By similarity).
FT BINDING 104 104 Substrate (By similarity).
FT MOD_RES 2 2 N-acetylalanine.
FT MOD_RES 28 28 Phosphoserine.
FT MOD_RES 169 169 Phosphoserine.
FT VAR_SEQ 126 148 VLSAMIRGAADGSRFQVWDYEEG -> GEHPKPPSWLSMDP
FT ALSSFPGGL (in isoform 2).
FT /FTId=VSP_040509.
FT VAR_SEQ 149 174 Missing (in isoform 2).
FT /FTId=VSP_040510.
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
//
ID DNPH1_HUMAN Reviewed; 174 AA.
AC O43598; B2LUJ9;
DT 10-MAY-2005, integrated into UniProtKB/Swiss-Prot.
read moreDT 01-JUN-1998, sequence version 1.
DT 22-JAN-2014, entry version 99.
DE RecName: Full=2'-deoxynucleoside 5'-phosphate N-hydrolase 1;
DE EC=3.2.2.-;
DE AltName: Full=c-Myc-responsive protein RCL;
GN Name=DNPH1; Synonyms=C6orf108, RCL;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC TISSUE=Liver;
RX PubMed=9271375;
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
RT of 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.,
RA Gilbert J.G.R., Clamp M.E., Bethel G., Milne S., Ainscough R.,
RA Almeida J.P., Ambrose K.D., Andrews T.D., Ashwell R.I.S.,
RA Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Barker D.J.,
RA Barlow K.F., Bates K., Beare D.M., Beasley H., Beasley O., Bird C.P.,
RA Blakey S.E., Bray-Allen S., Brook J., Brown A.J., Brown J.Y.,
RA 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.,
RA Ellington A.E., Evans K.A., Faulkner L., Francis M.D., Frankish A.,
RA Frankland J., French L., Garner P., Garnett J., Ghori M.J.,
RA Gilby L.M., Gillson C.J., Glithero R.J., Grafham D.V., Grant M.,
RA Gribble S., Griffiths C., Griffiths M.N.D., Hall R., Halls K.S.,
RA Hammond S., Harley J.L., Hart E.A., Heath P.D., Heathcott R.,
RA Holmes S.J., Howden P.J., Howe K.L., Howell G.R., Huckle E.,
RA Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., Joy A.A.,
RA Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., Langford C.,
RA Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., Lloyd D.M.,
RA Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M.,
RA Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K.,
RA McMurray A., Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T.,
RA Novik K.L., Oliver K., Overton-Larty E.K., Parker A., Patel R.,
RA Pearce A.V., Peck A.I., Phillimore B.J.C.T., Phillips S., Plumb R.W.,
RA Porter K.M., Ramsey Y., Ranby S.A., Rice C.M., Ross M.T., Searle S.M.,
RA Sehra H.K., Sheridan E., Skuce C.D., Smith S., Smith M., Spraggon L.,
RA Squares S.L., Steward C.A., Sycamore N., Tamlyn-Hall G., Tester J.,
RA Theaker A.J., Thomas D.W., Thorpe A., Tracey A., Tromans A., Tubby B.,
RA Wall M., Wallis J.M., West A.P., White S.S., Whitehead S.L.,
RA Whittaker H., Wild A., Willey D.J., Wilmer T.E., Wood J.M., Wray P.W.,
RA Wyatt J.C., Young L., Younger R.M., Bentley D.R., Coulson A.,
RA Durbin R.M., Hubbard T., Sulston J.E., Dunham I., 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.,
RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA 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
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-169, AND MASS
RP SPECTROMETRY.
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.,
RA Mann M.;
RT "Global, in vivo, and site-specific phosphorylation dynamics in
RT signaling networks.";
RL Cell 127:635-648(2006).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-28 AND SER-169, AND MASS
RP SPECTROMETRY.
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.,
RA Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in
RT a refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-169, AND MASS
RP SPECTROMETRY.
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 MASS
RP SPECTROMETRY.
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.,
RA Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full
RT phosphorylation 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.,
RA Buerckstuemmer T., 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 MASS
RP SPECTROMETRY.
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J.,
RA Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V.,
RA Blagoev B.;
RT "System-wide temporal characterization of the proteome and
RT phosphoproteome of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [13]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, MASS SPECTROMETRY, AND
RP CLEAVAGE OF INITIATOR METHIONINE.
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.,
RA Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K.,
RA Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-
RT terminal acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
CC -!- FUNCTION: Catalyzes the cleavage of the N-glycosidic bond of
CC deoxyribonucleoside 5'-monophosphates to yield deoxyribose 5-
CC phosphate and a purine or pyrimidine base. Deoxyribonucleoside 5'-
CC monophosphates containing purine bases are preferred to those
CC containing pyrimidine bases (By similarity).
CC -!- CATALYTIC ACTIVITY: A deoxyribonucleoside 5'-monophosphate + H(2)0
CC = deoxyribose 5-monophosphate + a purine or pyrimidine base.
CC -!- SUBUNIT: Monomer and homodimer (By similarity).
CC -!- SUBCELLULAR LOCATION: Cytoplasm. Nucleus (By similarity).
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
CC thymus. Expressed at high levels in heart, kidney, liver, skeletal
CC muscle and spleen. Overexpressed in a significant proportion of
CC breast cancers.
CC -!- INDUCTION: Expression is induced by ETV1.
CC -!- SIMILARITY: Belongs to the 2'-deoxynucleoside 5'-phosphate N-
CC hydrolase 1 family.
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DR EMBL; AF040105; AAB96766.1; -; mRNA.
DR EMBL; EU585603; ACB87500.1; -; mRNA.
DR EMBL; AL133375; CAI20205.1; -; Genomic_DNA.
DR EMBL; CH471081; EAX04166.1; -; Genomic_DNA.
DR EMBL; BC011683; AAH11683.1; -; mRNA.
DR EMBL; BQ052226; -; NOT_ANNOTATED_CDS; mRNA.
DR RefSeq; NP_006434.1; NM_006443.2.
DR RefSeq; NP_954653.1; NM_199184.1.
DR UniGene; Hs.109752; -.
DR ProteinModelPortal; O43598; -.
DR SMR; O43598; 20-160.
DR IntAct; O43598; 1.
DR MINT; MINT-5002237; -.
DR PhosphoSite; O43598; -.
DR PaxDb; O43598; -.
DR PeptideAtlas; O43598; -.
DR PRIDE; O43598; -.
DR Ensembl; ENST00000230431; ENSP00000230431; ENSG00000112667.
DR Ensembl; ENST00000393987; ENSP00000377556; ENSG00000112667.
DR GeneID; 10591; -.
DR KEGG; hsa:10591; -.
DR UCSC; uc003ouo.3; human.
DR CTD; 10591; -.
DR GeneCards; GC06M043193; -.
DR HGNC; HGNC:21218; DNPH1.
DR HPA; HPA029675; -.
DR HPA; HPA029676; -.
DR neXtProt; NX_O43598; -.
DR PharmGKB; PA134918815; -.
DR eggNOG; NOG08389; -.
DR HOGENOM; HOG000015361; -.
DR HOVERGEN; HBG079123; -.
DR InParanoid; O43598; -.
DR OrthoDB; EOG7CNZHC; -.
DR PhylomeDB; O43598; -.
DR GenomeRNAi; 10591; -.
DR NextBio; 40219; -.
DR PRO; PR:O43598; -.
DR ArrayExpress; O43598; -.
DR Bgee; O43598; -.
DR CleanEx; HS_C6orf108; -.
DR Genevestigator; O43598; -.
DR GO; GO:0005737; C:cytoplasm; IDA:HPA.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0070694; F:deoxyribonucleoside 5'-monophosphate N-glycosidase activity; ISS:UniProtKB.
DR GO; GO:0050144; F:nucleoside deoxyribosyltransferase activity; IEA:InterPro.
DR GO; GO:0008283; P:cell proliferation; TAS:ProtInc.
DR GO; GO:0009159; P:deoxyribonucleoside monophosphate catabolic process; ISS:UniProtKB.
DR GO; GO:0009117; P:nucleotide metabolic process; IEA:UniProtKB-KW.
DR GO; GO:0030307; P:positive regulation of cell growth; ISS:UniProtKB.
DR Gene3D; 3.40.50.1810; -; 1.
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 Acetylation; Alternative splicing; Complete proteome; Cytoplasm;
KW Glycosidase; Hydrolase; Nucleotide metabolism; Nucleus;
KW Phosphoprotein; Reference proteome.
FT INIT_MET 1 1 Removed.
FT CHAIN 2 174 2'-deoxynucleoside 5'-phosphate N-
FT hydrolase 1.
FT /FTId=PRO_0000097200.
FT REGION 24 30 Substrate binding (By similarity).
FT REGION 128 130 Substrate binding; shared with
FT homodimeric partner (By similarity).
FT BINDING 39 39 Substrate (By similarity).
FT BINDING 104 104 Substrate (By similarity).
FT MOD_RES 2 2 N-acetylalanine.
FT MOD_RES 28 28 Phosphoserine.
FT MOD_RES 169 169 Phosphoserine.
FT VAR_SEQ 126 148 VLSAMIRGAADGSRFQVWDYEEG -> GEHPKPPSWLSMDP
FT ALSSFPGGL (in isoform 2).
FT /FTId=VSP_040509.
FT VAR_SEQ 149 174 Missing (in isoform 2).
FT /FTId=VSP_040510.
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
//