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Q8C7W7

- DCR1B_MOUSE

UniProt

Q8C7W7 - DCR1B_MOUSE

Protein

5' exonuclease Apollo

Gene

Dclre1b

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 84 (01 Oct 2014)
      Sequence version 2 (16 Aug 2005)
      Previous versions | rss
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    Functioni

    5'-3' exonuclease that plays a central role in telomere maintenance and protection during S-phase. Participates in the protection of telomeres against non-homologous end-joining (NHEJ)-mediated repair, thereby ensuring that telomeres do not fuse. Plays a key role in telomeric loop (T loop) formation by being recruited by TERF2 at the leading end telomeres and by processing leading-end telomeres immediately after their replication via its exonuclease activity: generates 3' single-stranded overhang at the leading end telomeres avoiding blunt leading-end telomeres that are vulnerable to end-joining reactions and expose the telomere end in a manner that activates the DNA repair pathways. Together with TERF2, required to protect telomeres from replicative damage during replication by controlling the amount of DNA topoisomerase (TOP1, TOP2A and TOP2B) needed for telomere replication during fork passage and prevent aberrant telomere topology. Also involved in response to DNA damage: plays a role in response to DNA interstrand cross-links (ICLs) by facilitating double-strand break formation. In case of spindle stress, involved in prophase checkpoint.2 Publications

    GO - Molecular functioni

    1. 5'-3' exonuclease activity Source: UniProtKB
    2. protein binding Source: UniProtKB

    GO - Biological processi

    1. cell cycle checkpoint Source: UniProtKB
    2. nucleic acid phosphodiester bond hydrolysis Source: GOC
    3. nucleotide-excision repair Source: MGI
    4. protection from non-homologous end joining at telomere Source: UniProtKB
    5. telomere maintenance Source: UniProtKB
    6. telomeric 3' overhang formation Source: UniProtKB
    7. telomeric loop formation Source: UniProtKB

    Keywords - Molecular functioni

    Exonuclease, Hydrolase, Nuclease

    Keywords - Biological processi

    DNA damage, DNA repair

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    5' exonuclease Apollo (EC:3.1.-.-)
    Alternative name(s):
    DNA cross-link repair 1B protein
    SNM1 homolog B
    Gene namesi
    Name:Dclre1b
    Synonyms:Snm1b
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome 3

    Organism-specific databases

    MGIiMGI:2156057. Dclre1b.

    Subcellular locationi

    Chromosometelomere 2 Publications. Nucleus By similarity. Cytoplasmcytoskeletonmicrotubule organizing centercentrosome By similarity
    Note: Mainly localizes to telomeres, recruited via its interaction with TERF2. During mitosis, localizes to the centrosome.

    GO - Cellular componenti

    1. centrosome Source: UniProtKB
    2. chromosome, telomeric region Source: UniProtKB
    3. cytoplasm Source: UniProtKB-KW
    4. nucleus Source: MGI

    Keywords - Cellular componenti

    Chromosome, Cytoplasm, Cytoskeleton, Nucleus, Telomere

    Pathology & Biotechi

    Disruption phenotypei

    Embryos are smaller than wild-type embryos and neonates die at postnatal day 0 (P0). Cells activate the ATM kinase at their telomeres in S phase and show leading-end telomere fusions which are accompanied by a reduction in the telomeric overhang signal.2 Publications

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi14 – 141D → A: Abolishes exonuclease activity without affecting the telomere localization, leading to impaired 3'-overhang at the leading end telomeres. 1 Publication
    Mutagenesisi31 – 355HMHCD → AMACN: Abolishes exonuclease activity, leading to activate the ATM signaling pathway; when associated with A-230.
    Mutagenesisi230 – 2301H → A: Abolishes exonuclease activity, leading to activate the ATM signaling pathway; when associated with 31-A--N-35. 1 Publication
    Mutagenesisi500 – 5045Missing: Abolishes interaction with TERF2 and localization to telomeres, leading to activate the ATM signaling pathway.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 5415415' exonuclease ApolloPRO_0000209120Add
    BLAST

    Post-translational modificationi

    Ubiquitinated, leading to its degradation. Interaction with TERF2 protects it from ubiquitination By similarity.By similarity

    Keywords - PTMi

    Ubl conjugation

    Proteomic databases

    PRIDEiQ8C7W7.

    Expressioni

    Gene expression databases

    ArrayExpressiQ8C7W7.
    BgeeiQ8C7W7.
    GenevestigatoriQ8C7W7.

    Interactioni

    Subunit structurei

    Interacts with MUS81, MRE11 and FANCD2. Interacts with HSPA2, HSPA8 and HSPA14. Interacts with SPAG5 By similarity. Interacts with TERF2; the interaction is direct.By similarity1 Publication

    Structurei

    3D structure databases

    ProteinModelPortaliQ8C7W7.
    SMRiQ8C7W7. Positions 1-314.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi492 – 50716TBMAdd
    BLAST

    Domaini

    The TBM domain mediates interaction with TERF2.By similarity

    Sequence similaritiesi

    Phylogenomic databases

    eggNOGiCOG1236.
    GeneTreeiENSGT00530000063183.
    HOVERGENiHBG081420.
    InParanoidiB0V3P0.
    KOiK15341.
    OMAiPCQVVPI.
    OrthoDBiEOG71VSSC.
    PhylomeDBiQ8C7W7.
    TreeFamiTF329572.

    Family and domain databases

    Gene3Di3.60.15.10. 1 hit.
    InterProiIPR001279. Beta-lactamas-like.
    IPR011084. DRMBL.
    [Graphical view]
    PfamiPF07522. DRMBL. 1 hit.
    [Graphical view]
    SMARTiSM00849. Lactamase_B. 1 hit.
    [Graphical view]
    SUPFAMiSSF56281. SSF56281. 1 hit.

    Sequences (3)i

    Sequence statusi: Complete.

    This entry describes 3 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: Q8C7W7-1) [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

    MNGVVIPQTP IAVDFWSLRR AGSARLFFLT HMHCDHTVGL SSTWARPLYC    50
    SPITACLLHR RLQVSKHWIR ALEVGESHVL PLDEIGQETM TVTLIDANHC 100
    PGSVMFLFEG YFGTILYTGD FRYTPSMLKE PALILGKQIH TLYLDNTNCN 150
    PALVLPSRQE ATQQIVQLIR QFPQHNIKIG LYSLGKESLL EQLALEFRTW 200
    VVLSPQRLEL VQLLGLADVF TVEEEAGRIH AVDHTEICHS AMLQWNQSHP 250
    TIAIFPTSRK VRSPHPSIYT VPYSDHSSYS ELRAFVAALR PCQVVPIVHQ 300
    KPCGEFFQDS LSPRLAMPLI PHSVQQYMSS SSRKTNVLWQ LERRLKRPRT 350
    QGVVFESPEE KANQVKVDRD SKKHKKENLS PWAGHLERLC PHPLQARKQL 400
    FPDFCRKERD EPVLFCDSNK MATVLTAPLE FSVQLQPIDE FLFPETREKI 450
    GLESPLLSRG DSGSPARGNQ SDCVGCGSPP AHISRAVPLT PESRGLALKY 500
    LLTPVHFLQA GFSSRNFDKQ VEKHQRVQRS SPAVLSPVDV G 541
    Length:541
    Mass (Da):61,069
    Last modified:August 16, 2005 - v2
    Checksum:i884FB1A8E452A76C
    GO
    Isoform 2 (identifier: Q8C7W7-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-126: Missing.

    Show »
    Length:415
    Mass (Da):46,864
    Checksum:iD887FB35BE7747E3
    GO
    Isoform 3 (identifier: Q8C7W7-3) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         181-213: LYSLGKESLLEQLALEFRTWVVLSPQRLELVQL → ERFPFFFHSCLVNQNSLKVLIVFQIFVPCSPFL
         214-541: Missing.

    Note: No experimental confirmation available.

    Show »
    Length:213
    Mass (Da):24,254
    Checksum:i56845E3156F33971
    GO

    Sequence cautioni

    The sequence BAC39165.1 differs from that shown. Reason: Frameshift at position 55.
    The sequence AAH11094.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.
    The sequence BAE23379.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti49 – 491Y → D in BAE23379. (PubMed:16141072)Curated
    Sequence conflicti162 – 1621T → S in BAC33550. (PubMed:16141072)Curated
    Sequence conflicti327 – 3271Y → H in AAI25278. (PubMed:15489334)Curated
    Sequence conflicti412 – 4121P → L in AAI25278. (PubMed:15489334)Curated
    Sequence conflicti540 – 5401V → D in BAE23700. (PubMed:16141072)Curated

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 126126Missing in isoform 2. 2 PublicationsVSP_015174Add
    BLAST
    Alternative sequencei181 – 21333LYSLG…ELVQL → ERFPFFFHSCLVNQNSLKVL IVFQIFVPCSPFL in isoform 3. 1 PublicationVSP_015175Add
    BLAST
    Alternative sequencei214 – 541328Missing in isoform 3. 1 PublicationVSP_015176Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AK046571 mRNA. Translation: BAC32791.1.
    AK049115 mRNA. Translation: BAC33550.1.
    AK084347 mRNA. Translation: BAC39165.1. Frameshift.
    AK134324 mRNA. Translation: BAE22098.1.
    AK137495 mRNA. Translation: BAE23379.1. Different initiation.
    AK138568 mRNA. Translation: BAE23700.1.
    AK154124 mRNA. Translation: BAE32389.1.
    CU210953 Genomic DNA. Translation: CAQ12168.1.
    CU210953 Genomic DNA. Translation: CAQ12169.1.
    BC011094 mRNA. Translation: AAH11094.1. Different initiation.
    BC067017 mRNA. Translation: AAH67017.1.
    BC125277 mRNA. Translation: AAI25278.1.
    CCDSiCCDS17694.1. [Q8C7W7-1]
    CCDS17695.1. [Q8C7W7-2]
    RefSeqiNP_001020483.1. NM_001025312.1. [Q8C7W7-2]
    NP_598626.2. NM_133865.2. [Q8C7W7-1]
    UniGeneiMm.374850.

    Genome annotation databases

    EnsembliENSMUST00000029435; ENSMUSP00000029435; ENSMUSG00000027845. [Q8C7W7-1]
    ENSMUST00000063502; ENSMUSP00000067695; ENSMUSG00000027845. [Q8C7W7-2]
    ENSMUST00000106832; ENSMUSP00000102445; ENSMUSG00000027845. [Q8C7W7-3]
    ENSMUST00000106834; ENSMUSP00000102447; ENSMUSG00000027845. [Q8C7W7-1]
    GeneIDi140917.
    KEGGimmu:140917.
    UCSCiuc008qtl.1. mouse. [Q8C7W7-1]
    uc008qto.1. mouse. [Q8C7W7-3]

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AK046571 mRNA. Translation: BAC32791.1 .
    AK049115 mRNA. Translation: BAC33550.1 .
    AK084347 mRNA. Translation: BAC39165.1 . Frameshift.
    AK134324 mRNA. Translation: BAE22098.1 .
    AK137495 mRNA. Translation: BAE23379.1 . Different initiation.
    AK138568 mRNA. Translation: BAE23700.1 .
    AK154124 mRNA. Translation: BAE32389.1 .
    CU210953 Genomic DNA. Translation: CAQ12168.1 .
    CU210953 Genomic DNA. Translation: CAQ12169.1 .
    BC011094 mRNA. Translation: AAH11094.1 . Different initiation.
    BC067017 mRNA. Translation: AAH67017.1 .
    BC125277 mRNA. Translation: AAI25278.1 .
    CCDSi CCDS17694.1. [Q8C7W7-1 ]
    CCDS17695.1. [Q8C7W7-2 ]
    RefSeqi NP_001020483.1. NM_001025312.1. [Q8C7W7-2 ]
    NP_598626.2. NM_133865.2. [Q8C7W7-1 ]
    UniGenei Mm.374850.

    3D structure databases

    ProteinModelPortali Q8C7W7.
    SMRi Q8C7W7. Positions 1-314.
    ModBasei Search...
    MobiDBi Search...

    Proteomic databases

    PRIDEi Q8C7W7.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000029435 ; ENSMUSP00000029435 ; ENSMUSG00000027845 . [Q8C7W7-1 ]
    ENSMUST00000063502 ; ENSMUSP00000067695 ; ENSMUSG00000027845 . [Q8C7W7-2 ]
    ENSMUST00000106832 ; ENSMUSP00000102445 ; ENSMUSG00000027845 . [Q8C7W7-3 ]
    ENSMUST00000106834 ; ENSMUSP00000102447 ; ENSMUSG00000027845 . [Q8C7W7-1 ]
    GeneIDi 140917.
    KEGGi mmu:140917.
    UCSCi uc008qtl.1. mouse. [Q8C7W7-1 ]
    uc008qto.1. mouse. [Q8C7W7-3 ]

    Organism-specific databases

    CTDi 64858.
    MGIi MGI:2156057. Dclre1b.

    Phylogenomic databases

    eggNOGi COG1236.
    GeneTreei ENSGT00530000063183.
    HOVERGENi HBG081420.
    InParanoidi B0V3P0.
    KOi K15341.
    OMAi PCQVVPI.
    OrthoDBi EOG71VSSC.
    PhylomeDBi Q8C7W7.
    TreeFami TF329572.

    Miscellaneous databases

    NextBioi 370035.
    PROi Q8C7W7.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q8C7W7.
    Bgeei Q8C7W7.
    Genevestigatori Q8C7W7.

    Family and domain databases

    Gene3Di 3.60.15.10. 1 hit.
    InterProi IPR001279. Beta-lactamas-like.
    IPR011084. DRMBL.
    [Graphical view ]
    Pfami PF07522. DRMBL. 1 hit.
    [Graphical view ]
    SMARTi SM00849. Lactamase_B. 1 hit.
    [Graphical view ]
    SUPFAMi SSF56281. SSF56281. 1 hit.
    ProtoNeti Search...

    Publicationsi

    1. "The transcriptional landscape of the mammalian genome."
      Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
      , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
      Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 2 AND 3).
      Strain: C57BL/6J and NOD.
      Tissue: Adipose tissue, Bone, Eye, Spinal cord and Testis.
    2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: C57BL/6J.
    3. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
      The MGC Project Team
      Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 82-541 (ISOFORM 1).
      Strain: Czech II.
      Tissue: Brain and Mammary gland.
    4. "SNMIB/Apollo protects leading-strand telomeres against NHEJ-mediated repair."
      Lam Y.C., Akhter S., Gu P., Ye J., Poulet A., Giraud-Panis M.J., Bailey S.M., Gilson E., Legerski R.J., Chang S.
      EMBO J. 29:2230-2241(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, SUBCELLULAR LOCATION, DISRUPTION PHENOTYPE, MUTAGENESIS OF ASP-14.
    5. "Apollo contributes to G overhang maintenance and protects leading-end telomeres."
      Wu P., van Overbeek M., Rooney S., de Lange T.
      Mol. Cell 39:606-617(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH TERF2, DISRUPTION PHENOTYPE, MUTAGENESIS OF 31-HIS--ASP-35; HIS-230 AND 500-TYR--PRO-504.

    Entry informationi

    Entry nameiDCR1B_MOUSE
    AccessioniPrimary (citable) accession number: Q8C7W7
    Secondary accession number(s): A0JLW2
    , B0V3N9, B0V3P0, Q3U4P2, Q3UUC7, Q3UV92, Q6NXL4, Q8BN95, Q8BQS8, Q921S0
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: August 16, 2005
    Last sequence update: August 16, 2005
    Last modified: October 1, 2014
    This is version 84 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. MGD cross-references
      Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
    2. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3