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Q8WZ79

- DNS2B_HUMAN

UniProt

Q8WZ79 - DNS2B_HUMAN

Protein

Deoxyribonuclease-2-beta

Gene

DNASE2B

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at transcript leveli
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    • History
      Entry version 91 (01 Oct 2014)
      Sequence version 1 (01 Mar 2002)
      Previous versions | rss
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    Functioni

    Hydrolyzes DNA under acidic conditions. Does not require divalent cations for activity. Participates in the degradation of nuclear DNA during lens cell differentiation.2 Publications

    Catalytic activityi

    Endonucleolytic cleavage to nucleoside 3'-phosphates and 3'-phosphooligonucleotide end-products.

    GO - Molecular functioni

    1. deoxyribonuclease II activity Source: RefGenome

    GO - Biological processi

    1. apoptotic DNA fragmentation Source: RefGenome

    Keywords - Molecular functioni

    Endonuclease, Hydrolase, Nuclease

    Enzyme and pathway databases

    BRENDAi3.1.22.1. 2681.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Deoxyribonuclease-2-beta (EC:3.1.22.1)
    Alternative name(s):
    DNase II-like acid DNase
    DNase2-like acid DNase
    Deoxyribonuclease II beta
    Short name:
    DNase II beta
    Endonuclease DLAD
    Gene namesi
    Name:DNASE2B
    Synonyms:DLAD
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 1

    Organism-specific databases

    HGNCiHGNC:28875. DNASE2B.

    Subcellular locationi

    Lysosome Curated

    GO - Cellular componenti

    1. extracellular region Source: Ensembl
    2. intracellular Source: RefGenome
    3. lysosome Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Lysosome

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA134993904.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 2727Sequence AnalysisAdd
    BLAST
    Chaini28 – 361334Deoxyribonuclease-2-betaPRO_0000007295Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Glycosylationi81 – 811N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi103 – 1031N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi119 – 1191N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi278 – 2781N-linked (GlcNAc...)Sequence Analysis

    Keywords - PTMi

    Glycoprotein

    Proteomic databases

    PaxDbiQ8WZ79.
    PRIDEiQ8WZ79.

    PTM databases

    PhosphoSiteiQ8WZ79.

    Expressioni

    Tissue specificityi

    Highly expressed in the eye lens and in salivary gland. Detected at lower levels in lung, prostate and lymph node. Isoform 2 is lung specific.3 Publications

    Gene expression databases

    ArrayExpressiQ8WZ79.
    BgeeiQ8WZ79.
    CleanExiHS_DNASE2B.
    GenevestigatoriQ8WZ79.

    Interactioni

    Protein-protein interaction databases

    BioGridi121838. 2 interactions.
    STRINGi9606.ENSP00000359699.

    Structurei

    3D structure databases

    ProteinModelPortaliQ8WZ79.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the DNase II family.Curated

    Keywords - Domaini

    Signal

    Phylogenomic databases

    eggNOGiNOG145330.
    HOGENOMiHOG000261682.
    HOVERGENiHBG051387.
    InParanoidiQ8WZ79.
    KOiK01158.
    OMAiSSYQDHA.
    OrthoDBiEOG7F5122.
    PhylomeDBiQ8WZ79.
    TreeFamiTF314536.

    Family and domain databases

    InterProiIPR004947. DNase_II.
    [Graphical view]
    PANTHERiPTHR10858. PTHR10858. 1 hit.
    PfamiPF03265. DNase_II. 1 hit.
    [Graphical view]

    Sequences (2)i

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    This entry describes 2 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: Q8WZ79-1) [UniParc]FASTAAdd to Basket

    This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

    « Hide

    MKQKMMARLL RTSFALLFLG LFGVLGAATI SCRNEEGKAV DWFTFYKLPK    50
    RQNKESGETG LEYLYLDSTT RSWRKSEQLM NDTKSVLGRT LQQLYEAYAS 100
    KSNNTAYLIY NDGVPKPVNY SRKYGHTKGL LLWNRVQGFW LIHSIPQFPP 150
    IPEEGYDYPP TGRRNGQSGI CITFKYNQYE AIDSQLLVCN PNVYSCSIPA 200
    TFHQELIHMP QLCTRASSSE IPGRLLTTLQ SAQGQKFLHF AKSDSFLDDI 250
    FAAWMAQRLK THLLTETWQR KRQELPSNCS LPYHVYNIKA IKLSRHSYFS 300
    SYQDHAKWCI SQKGTKNRWT CIGDLNRSPH QAFRSGGFIC TQNWQIYQAF 350
    QGLVLYYESC K 361
    Length:361
    Mass (Da):41,713
    Last modified:March 1, 2002 - v1
    Checksum:iC6FDD3F58F62CAC0
    GO
    Isoform 2 (identifier: Q8WZ79-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-208: Missing.

    Show »
    Length:153
    Mass (Da):17,816
    Checksum:iABF4ED379AFA9FCF
    GO

    Sequence cautioni

    The sequence AAF76893.1 differs from that shown. Reason: Erroneous initiation.

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti3 – 31Q → H.
    Corresponds to variant rs3738573 [ dbSNP | Ensembl ].
    VAR_059250
    Natural varianti47 – 471K → R.
    Corresponds to variant rs3754274 [ dbSNP | Ensembl ].
    VAR_048872
    Natural varianti51 – 511R → K.
    Corresponds to variant rs3754274 [ dbSNP | Ensembl ].
    VAR_059251

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 208208Missing in isoform 2. 1 PublicationVSP_009812Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF333389 mRNA. Translation: AAL34448.1.
    AF334602 Genomic DNA. Translation: AAL34449.1.
    AF274571 mRNA. Translation: AAF76893.1. Different initiation.
    AL359273 Genomic DNA. Translation: CAH73126.1.
    AL359273 Genomic DNA. Translation: CAH73127.1.
    CH471097 Genomic DNA. Translation: EAW73238.1.
    CH471097 Genomic DNA. Translation: EAW73239.1.
    CCDSiCCDS44167.1. [Q8WZ79-1]
    CCDS694.1. [Q8WZ79-2]
    RefSeqiNP_067056.2. NM_021233.2. [Q8WZ79-1]
    NP_490649.1. NM_058248.1. [Q8WZ79-2]
    UniGeneiHs.129142.

    Genome annotation databases

    EnsembliENST00000370662; ENSP00000359696; ENSG00000137976. [Q8WZ79-2]
    ENST00000370665; ENSP00000359699; ENSG00000137976. [Q8WZ79-1]
    GeneIDi58511.
    KEGGihsa:58511.
    UCSCiuc001djt.1. human. [Q8WZ79-1]
    uc001dju.1. human. [Q8WZ79-2]

    Polymorphism databases

    DMDMi46395921.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF333389 mRNA. Translation: AAL34448.1 .
    AF334602 Genomic DNA. Translation: AAL34449.1 .
    AF274571 mRNA. Translation: AAF76893.1 . Different initiation.
    AL359273 Genomic DNA. Translation: CAH73126.1 .
    AL359273 Genomic DNA. Translation: CAH73127.1 .
    CH471097 Genomic DNA. Translation: EAW73238.1 .
    CH471097 Genomic DNA. Translation: EAW73239.1 .
    CCDSi CCDS44167.1. [Q8WZ79-1 ]
    CCDS694.1. [Q8WZ79-2 ]
    RefSeqi NP_067056.2. NM_021233.2. [Q8WZ79-1 ]
    NP_490649.1. NM_058248.1. [Q8WZ79-2 ]
    UniGenei Hs.129142.

    3D structure databases

    ProteinModelPortali Q8WZ79.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 121838. 2 interactions.
    STRINGi 9606.ENSP00000359699.

    PTM databases

    PhosphoSitei Q8WZ79.

    Polymorphism databases

    DMDMi 46395921.

    Proteomic databases

    PaxDbi Q8WZ79.
    PRIDEi Q8WZ79.

    Protocols and materials databases

    DNASUi 58511.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000370662 ; ENSP00000359696 ; ENSG00000137976 . [Q8WZ79-2 ]
    ENST00000370665 ; ENSP00000359699 ; ENSG00000137976 . [Q8WZ79-1 ]
    GeneIDi 58511.
    KEGGi hsa:58511.
    UCSCi uc001djt.1. human. [Q8WZ79-1 ]
    uc001dju.1. human. [Q8WZ79-2 ]

    Organism-specific databases

    CTDi 58511.
    GeneCardsi GC01P084864.
    HGNCi HGNC:28875. DNASE2B.
    MIMi 608057. gene.
    neXtProti NX_Q8WZ79.
    PharmGKBi PA134993904.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG145330.
    HOGENOMi HOG000261682.
    HOVERGENi HBG051387.
    InParanoidi Q8WZ79.
    KOi K01158.
    OMAi SSYQDHA.
    OrthoDBi EOG7F5122.
    PhylomeDBi Q8WZ79.
    TreeFami TF314536.

    Enzyme and pathway databases

    BRENDAi 3.1.22.1. 2681.

    Miscellaneous databases

    GenomeRNAii 58511.
    NextBioi 65041.
    PROi Q8WZ79.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q8WZ79.
    Bgeei Q8WZ79.
    CleanExi HS_DNASE2B.
    Genevestigatori Q8WZ79.

    Family and domain databases

    InterProi IPR004947. DNase_II.
    [Graphical view ]
    PANTHERi PTHR10858. PTHR10858. 1 hit.
    Pfami PF03265. DNase_II. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Isolation and characterization of the DLAD/Dlad genes, which lie head-to-head with the genes for urate oxidase."
      Shiokawa D., Tanuma S.
      Biochem. Biophys. Res. Commun. 288:1119-1128(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORMS 1 AND 2), FUNCTION, TISSUE SPECIFICITY.
      Tissue: Lung.
    2. "The cloning, genomic structure, localization, and expression of human deoxyribonuclease IIbeta."
      Krieser R.J., MacLea K.S., Park J.P., Eastman A.
      Gene 269:205-216(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), TISSUE SPECIFICITY.
    3. "The DNA sequence and biological annotation of human chromosome 1."
      Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.
      , Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.
      Nature 441:315-321(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    5. Cited for: FUNCTION, TISSUE SPECIFICITY.

    Entry informationi

    Entry nameiDNS2B_HUMAN
    AccessioniPrimary (citable) accession number: Q8WZ79
    Secondary accession number(s): Q5VXD0
    , Q5VXD1, Q8WZ80, Q9NQW3
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: April 13, 2004
    Last sequence update: March 1, 2002
    Last modified: October 1, 2014
    This is version 91 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program
    DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. Human chromosome 1
      Human chromosome 1: entries, gene names and cross-references to MIM
    2. Human entries with polymorphisms or disease mutations
      List of human entries with polymorphisms or disease mutations
    3. Human polymorphisms and disease mutations
      Index of human polymorphisms and disease mutations
    4. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    5. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3