DNS2B_HUMAN
ID DNS2B_HUMAN Reviewed; 361 AA.
AC Q8WZ79; Q5VXD0; Q5VXD1; Q8WZ80; Q9NQW3;
DT 13-APR-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2002, sequence version 1.
DT 03-AUG-2022, entry version 144.
DE RecName: Full=Deoxyribonuclease-2-beta;
DE EC=3.1.22.1;
DE AltName: Full=DNase II-like acid DNase;
DE AltName: Full=DNase2-like acid DNase;
DE AltName: Full=Deoxyribonuclease II beta;
DE Short=DNase II beta;
DE AltName: Full=Endonuclease DLAD;
DE Flags: Precursor;
GN Name=DNASE2B; Synonyms=DLAD;
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 [GENOMIC DNA / MRNA] (ISOFORMS 1 AND 2), FUNCTION, AND
RP TISSUE SPECIFICITY.
RC TISSUE=Lung;
RX PubMed=11700027; DOI=10.1006/bbrc.2001.5894;
RA Shiokawa D., Tanuma S.;
RT "Isolation and characterization of the DLAD/Dlad genes, which lie head-to-
RT head with the genes for urate oxidase.";
RL Biochem. Biophys. Res. Commun. 288:1119-1128(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND TISSUE SPECIFICITY.
RX PubMed=11376952; DOI=10.1016/s0378-1119(01)00434-6;
RA Krieser R.J., MacLea K.S., Park J.P., Eastman A.;
RT "The cloning, genomic structure, localization, and expression of human
RT deoxyribonuclease IIbeta.";
RL Gene 269:205-216(2001).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16710414; DOI=10.1038/nature04727;
RA Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A.,
RA Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C.,
RA Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.,
RA Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C.,
RA Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W.,
RA Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J.,
RA Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J.,
RA Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y.,
RA Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J.,
RA Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
RA Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
RA Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
RA Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S.,
RA Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K.,
RA Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R.,
RA Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M.,
RA Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S.,
RA Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J.,
RA Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W.,
RA McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
RA Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
RA Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
RA Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
RA Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S.,
RA Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M.,
RA White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H.,
RA Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E.,
RA Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G.,
RA Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.;
RT "The DNA sequence and biological annotation of human chromosome 1.";
RL Nature 441:315-321(2006).
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 (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP FUNCTION, AND TISSUE SPECIFICITY.
RX PubMed=12944971; DOI=10.1038/nature01895;
RA Nishimoto S., Kawane K., Watanabe-Fukunaga R., Fukuyama H., Ohsawa Y.,
RA Uchiyama Y., Hashida N., Ohguro N., Tano Y., Morimoto T., Fukuda Y.,
RA Nagata S.;
RT "Nuclear cataract caused by a lack of DNA degradation in the mouse eye
RT lens.";
RL Nature 424:1071-1074(2003).
CC -!- FUNCTION: Hydrolyzes DNA under acidic conditions. Does not require
CC divalent cations for activity. Participates in the degradation of
CC nuclear DNA during lens cell differentiation.
CC {ECO:0000269|PubMed:11700027, ECO:0000269|PubMed:12944971}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Endonucleolytic cleavage to nucleoside 3'-phosphates and 3'-
CC phosphooligonucleotide end-products.; EC=3.1.22.1;
CC -!- SUBCELLULAR LOCATION: Lysosome {ECO:0000305}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q8WZ79-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8WZ79-2; Sequence=VSP_009812;
CC -!- TISSUE SPECIFICITY: Highly expressed in the eye lens and in salivary
CC gland. Detected at lower levels in lung, prostate and lymph node.
CC Isoform 2 is lung specific. {ECO:0000269|PubMed:11376952,
CC ECO:0000269|PubMed:11700027, ECO:0000269|PubMed:12944971}.
CC -!- SIMILARITY: Belongs to the DNase II family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAF76893.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AF333389; AAL34448.1; -; mRNA.
DR EMBL; AF334602; AAL34449.1; -; Genomic_DNA.
DR EMBL; AF274571; AAF76893.1; ALT_INIT; mRNA.
DR EMBL; AL359273; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471097; EAW73238.1; -; Genomic_DNA.
DR EMBL; CH471097; EAW73239.1; -; Genomic_DNA.
DR CCDS; CCDS44167.1; -. [Q8WZ79-1]
DR CCDS; CCDS694.1; -. [Q8WZ79-2]
DR RefSeq; NP_067056.2; NM_021233.2. [Q8WZ79-1]
DR RefSeq; NP_490649.1; NM_058248.1. [Q8WZ79-2]
DR RefSeq; XP_011540180.1; XM_011541878.2. [Q8WZ79-2]
DR AlphaFoldDB; Q8WZ79; -.
DR SMR; Q8WZ79; -.
DR BioGRID; 121838; 43.
DR IntAct; Q8WZ79; 20.
DR STRING; 9606.ENSP00000359699; -.
DR GlyGen; Q8WZ79; 4 sites.
DR iPTMnet; Q8WZ79; -.
DR PhosphoSitePlus; Q8WZ79; -.
DR BioMuta; DNASE2B; -.
DR DMDM; 46395921; -.
DR EPD; Q8WZ79; -.
DR PaxDb; Q8WZ79; -.
DR PeptideAtlas; Q8WZ79; -.
DR PRIDE; Q8WZ79; -.
DR ProteomicsDB; 75235; -. [Q8WZ79-1]
DR ProteomicsDB; 75236; -. [Q8WZ79-2]
DR Antibodypedia; 19765; 101 antibodies from 21 providers.
DR DNASU; 58511; -.
DR Ensembl; ENST00000370662.3; ENSP00000359696.3; ENSG00000137976.8. [Q8WZ79-2]
DR Ensembl; ENST00000370665.4; ENSP00000359699.3; ENSG00000137976.8. [Q8WZ79-1]
DR GeneID; 58511; -.
DR KEGG; hsa:58511; -.
DR MANE-Select; ENST00000370665.4; ENSP00000359699.3; NM_021233.3; NP_067056.2.
DR UCSC; uc001djt.2; human. [Q8WZ79-1]
DR CTD; 58511; -.
DR DisGeNET; 58511; -.
DR GeneCards; DNASE2B; -.
DR HGNC; HGNC:28875; DNASE2B.
DR HPA; ENSG00000137976; Tissue enriched (salivary).
DR MIM; 608057; gene.
DR neXtProt; NX_Q8WZ79; -.
DR OpenTargets; ENSG00000137976; -.
DR PharmGKB; PA134993904; -.
DR VEuPathDB; HostDB:ENSG00000137976; -.
DR eggNOG; KOG3825; Eukaryota.
DR GeneTree; ENSGT00390000002634; -.
DR HOGENOM; CLU_053867_0_1_1; -.
DR InParanoid; Q8WZ79; -.
DR OMA; HMPQLCA; -.
DR PhylomeDB; Q8WZ79; -.
DR TreeFam; TF314536; -.
DR BRENDA; 3.1.22.1; 2681.
DR PathwayCommons; Q8WZ79; -.
DR SignaLink; Q8WZ79; -.
DR SIGNOR; Q8WZ79; -.
DR BioGRID-ORCS; 58511; 11 hits in 1065 CRISPR screens.
DR GenomeRNAi; 58511; -.
DR Pharos; Q8WZ79; Tbio.
DR PRO; PR:Q8WZ79; -.
DR Proteomes; UP000005640; Chromosome 1.
DR RNAct; Q8WZ79; protein.
DR Bgee; ENSG00000137976; Expressed in parotid gland and 76 other tissues.
DR Genevisible; Q8WZ79; HS.
DR GO; GO:0005576; C:extracellular region; IEA:Ensembl.
DR GO; GO:0005764; C:lysosome; IEA:UniProtKB-SubCell.
DR GO; GO:0004531; F:deoxyribonuclease II activity; IBA:GO_Central.
DR GO; GO:0006309; P:apoptotic DNA fragmentation; IBA:GO_Central.
DR InterPro; IPR004947; DNase_II.
DR PANTHER; PTHR10858; PTHR10858; 1.
DR Pfam; PF03265; DNase_II; 1.
PE 2: Evidence at transcript level;
KW Alternative splicing; Endonuclease; Glycoprotein; Hydrolase; Lysosome;
KW Nuclease; Reference proteome; Signal.
FT SIGNAL 1..27
FT /evidence="ECO:0000255"
FT CHAIN 28..361
FT /note="Deoxyribonuclease-2-beta"
FT /id="PRO_0000007295"
FT CARBOHYD 81
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 103
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 119
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 278
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT VAR_SEQ 1..208
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:11700027"
FT /id="VSP_009812"
FT VARIANT 3
FT /note="Q -> H (in dbSNP:rs3738573)"
FT /id="VAR_059250"
FT VARIANT 47
FT /note="K -> R (in dbSNP:rs3754274)"
FT /id="VAR_048872"
FT VARIANT 51
FT /note="R -> K (in dbSNP:rs3754274)"
FT /id="VAR_059251"
SQ SEQUENCE 361 AA; 41713 MW; C6FDD3F58F62CAC0 CRC64;
MKQKMMARLL RTSFALLFLG LFGVLGAATI SCRNEEGKAV DWFTFYKLPK RQNKESGETG
LEYLYLDSTT RSWRKSEQLM NDTKSVLGRT LQQLYEAYAS KSNNTAYLIY NDGVPKPVNY
SRKYGHTKGL LLWNRVQGFW LIHSIPQFPP IPEEGYDYPP TGRRNGQSGI CITFKYNQYE
AIDSQLLVCN PNVYSCSIPA TFHQELIHMP QLCTRASSSE IPGRLLTTLQ SAQGQKFLHF
AKSDSFLDDI FAAWMAQRLK THLLTETWQR KRQELPSNCS LPYHVYNIKA IKLSRHSYFS
SYQDHAKWCI SQKGTKNRWT CIGDLNRSPH QAFRSGGFIC TQNWQIYQAF QGLVLYYESC
K
