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Q9H816

- DCR1B_HUMAN

UniProt

Q9H816 - DCR1B_HUMAN

Protein

5' exonuclease Apollo

Gene

DCLRE1B

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 108 (01 Oct 2014)
      Sequence version 1 (01 Mar 2001)
      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.9 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. DNA repair Source: UniProtKB-KW
    3. nucleic acid phosphodiester bond hydrolysis Source: GOC
    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
    Short name:
    SNMIB
    Short name:
    hSNM1B
    Gene namesi
    Name:DCLRE1B
    Synonyms:SNM1B
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 1

    Organism-specific databases

    HGNCiHGNC:17641. DCLRE1B.

    Subcellular locationi

    Chromosometelomere. Nucleus. Cytoplasmcytoskeletonmicrotubule organizing centercentrosome
    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: UniProtKB-SubCell

    Keywords - Cellular componenti

    Chromosome, Cytoplasm, Cytoskeleton, Nucleus, Telomere

    Pathology & Biotechi

    Involvement in diseasei

    Hoyeraal-Hreidarsson syndrome (HHS) [MIM:305000]: A clinically severe variant of dyskeratosis congenita that is characterized by multisystem involvement, early onset in utero, and often results in death in childhood. Affected individuals show intrauterine growth retardation, microcephaly, cerebellar hypoplasia, delayed development, and bone marrow failure resulting in immunodeficiency.1 Publication
    Note: The gene represented in this entry may be involved in disease pathogenesis. An aberrant splice variant of DCLRE1B, designated Apollo-Delta, has been found in a patient with Hoyeraal-Hreidarsson syndrome (PubMed:20479256). Apollo-Delta hampers the proper replication of telomeres, leading to major telomeric dysfunction and cellular senescence, but maintains its DNA interstrand cross-link repair function in the whole genome.1 Publication

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi14 – 141D → N in Apm3; abolishes exonuclease activity and function on telomere maintenance. Impairs interaction with SPAG5. 2 Publications
    Mutagenesisi33 – 331H → A in Apm1; abolishes exonuclease activity and function on telomere maintenance; when associated with N-35. 1 Publication
    Mutagenesisi35 – 351D → N in Apm2; abolishes exonuclease activity and function on telomere maintenance. In Apm1; abolishes exonuclease activity and function on telomere maintenance; when associated with A-33. 1 Publication
    Mutagenesisi276 – 2761H → A: Slightly affects interaction with SPAG5. 1 Publication
    Mutagenesisi504 – 5041Y → A: Abolishes interaction with TERF2. 1 Publication
    Mutagenesisi506 – 5061L → A: Abolishes interaction with TERF2. 1 Publication
    Mutagenesisi508 – 5081P → A: Abolishes interaction with TERF2. 1 Publication

    Keywords - Diseasei

    Dyskeratosis congenita

    Organism-specific databases

    MIMi305000. phenotype.
    PharmGKBiPA27175.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 5325325' exonuclease ApolloPRO_0000209119Add
    BLAST

    Post-translational modificationi

    Ubiquitinated, leading to its degradation. Interaction with TERF2 protects it from ubiquitination.1 Publication

    Keywords - PTMi

    Ubl conjugation

    Proteomic databases

    PaxDbiQ9H816.
    PRIDEiQ9H816.

    PTM databases

    PhosphoSiteiQ9H816.

    Expressioni

    Gene expression databases

    BgeeiQ9H816.
    CleanExiHS_DCLRE1B.
    GenevestigatoriQ9H816.

    Interactioni

    Subunit structurei

    Interacts with TERF2; the interaction is direct. Interacts with MUS81, MRE11 and FANCD2. Interacts with HSPA2, HSPA8 and HSPA14. Interacts with SPAG5.10 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    TERF2Q155546EBI-3508943,EBI-706637

    Protein-protein interaction databases

    BioGridi122331. 6 interactions.
    DIPiDIP-42669N.
    IntActiQ9H816. 3 interactions.
    MINTiMINT-3372972.
    STRINGi9606.ENSP00000358576.

    Structurei

    Secondary structure

    1
    532
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi9 – 146
    Helixi18 – 214
    Beta strandi26 – 283
    Helixi34 – 363
    Beta strandi48 – 503
    Helixi52 – 6211
    Turni66 – 683
    Beta strandi69 – 713
    Beta strandi76 – 8712
    Beta strandi89 – 968
    Beta strandi98 – 1003
    Beta strandi104 – 1107
    Beta strandi113 – 1175
    Helixi125 – 1295
    Helixi131 – 1333
    Beta strandi140 – 1445
    Helixi158 – 17013
    Beta strandi175 – 1817
    Beta strandi183 – 1853
    Helixi187 – 19711
    Helixi205 – 2139
    Beta strandi220 – 2223
    Helixi224 – 2263
    Beta strandi228 – 2336
    Helixi234 – 2363
    Helixi239 – 24810
    Beta strandi251 – 2566
    Beta strandi268 – 2714
    Helixi279 – 28911
    Beta strandi294 – 2974
    Helixi307 – 3093
    Helixi500 – 5034

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    3BUAX-ray2.50E/F/G/H495-530[»]
    3ZDKX-ray2.16A1-335[»]
    ProteinModelPortaliQ9H816.
    SMRiQ9H816. Positions 1-313.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ9H816.

    Family & Domainsi

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi496 – 51116TBMAdd
    BLAST

    Domaini

    The TBM domain mediates interaction with TERF2.

    Sequence similaritiesi

    Phylogenomic databases

    eggNOGiCOG1236.
    HOGENOMiHOG000043118.
    HOVERGENiHBG081420.
    InParanoidiQ9H816.
    KOiK15341.
    OMAiPCQVVPI.
    OrthoDBiEOG71VSSC.
    PhylomeDBiQ9H816.
    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.

    Sequencei

    Sequence statusi: Complete.

    Q9H816-1 [UniParc]FASTAAdd to Basket

    « Hide

    MNGVLIPHTP IAVDFWSLRR AGTARLFFLS HMHSDHTVGL SSTWARPLYC    50
    SPITAHLLHR HLQVSKQWIQ ALEVGESHVL PLDEIGQETM TVTLLDANHC 100
    PGSVMFLFEG YFGTILYTGD FRYTPSMLKE PALTLGKQIH TLYLDNTNCN 150
    PALVLPSRQE AAHQIVQLIR KHPQHNIKIG LYSLGKESLL EQLALEFQTW 200
    VVLSPRRLEL VQLLGLADVF TVEEKAGRIH AVDHMEICHS NMLRWNQTHP 250
    TIAILPTSRK IHSSHPDIHV IPYSDHSSYS ELRAFVAALK PCQVVPIVSR 300
    RPCGGFQDSL SPRISVPLIP DSVQQYMSSS SRKPSLLWLL ERRLKRPRTQ 350
    GVVFESPEES ADQSQADRDS KKAKKEKLSP WPADLEKQPS HHPLRIKKQL 400
    FPDLYSKEWN KAVPFCESQK RVTMLTAPLG FSVHLRSTDE EFISQKTREE 450
    IGLGSPLVPM GDDDGGPEAT GNQSAWMGHG SPLSHSSKGT PLLATEFRGL 500
    ALKYLLTPVN FFQAGYSSRR FDQQVEKYHK PC 532
    Length:532
    Mass (Da):60,002
    Last modified:March 1, 2001 - v1
    Checksum:i601A800CCD43CFDA
    GO

    Sequence cautioni

    The sequence BAB14284.1 differs from that shown. Reason: Erroneous initiation.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti237 – 2371I → T in BAB14284. (PubMed:14702039)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti46 – 461R → L.1 Publication
    Corresponds to variant rs28381069 [ dbSNP | Ensembl ].
    VAR_023292
    Natural varianti61 – 611H → Y.1 Publication
    Corresponds to variant rs11552449 [ dbSNP | Ensembl ].
    VAR_023293
    Natural varianti462 – 4621D → N.1 Publication
    Corresponds to variant rs28381079 [ dbSNP | Ensembl ].
    VAR_023294
    Natural varianti510 – 5101N → Y.
    Corresponds to variant rs35397235 [ dbSNP | Ensembl ].
    VAR_048891

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AK022872 mRNA. Translation: BAB14284.1. Different initiation.
    AK024060 mRNA. Translation: BAB14807.1.
    AY849379 Genomic DNA. Translation: AAV97812.1.
    AL137856 Genomic DNA. Translation: CAI19076.1.
    BC029687 mRNA. Translation: AAH29687.1.
    CCDSiCCDS866.1.
    RefSeqiNP_073747.1. NM_022836.3.
    UniGeneiHs.591412.

    Genome annotation databases

    EnsembliENST00000369563; ENSP00000358576; ENSG00000118655.
    GeneIDi64858.
    KEGGihsa:64858.
    UCSCiuc001eeg.3. human.

    Polymorphism databases

    DMDMi73620756.

    Keywords - Coding sequence diversityi

    Polymorphism

    Cross-referencesi

    Web resourcesi

    NIEHS-SNPs

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AK022872 mRNA. Translation: BAB14284.1 . Different initiation.
    AK024060 mRNA. Translation: BAB14807.1 .
    AY849379 Genomic DNA. Translation: AAV97812.1 .
    AL137856 Genomic DNA. Translation: CAI19076.1 .
    BC029687 mRNA. Translation: AAH29687.1 .
    CCDSi CCDS866.1.
    RefSeqi NP_073747.1. NM_022836.3.
    UniGenei Hs.591412.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    3BUA X-ray 2.50 E/F/G/H 495-530 [» ]
    3ZDK X-ray 2.16 A 1-335 [» ]
    ProteinModelPortali Q9H816.
    SMRi Q9H816. Positions 1-313.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 122331. 6 interactions.
    DIPi DIP-42669N.
    IntActi Q9H816. 3 interactions.
    MINTi MINT-3372972.
    STRINGi 9606.ENSP00000358576.

    PTM databases

    PhosphoSitei Q9H816.

    Polymorphism databases

    DMDMi 73620756.

    Proteomic databases

    PaxDbi Q9H816.
    PRIDEi Q9H816.

    Protocols and materials databases

    DNASUi 64858.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000369563 ; ENSP00000358576 ; ENSG00000118655 .
    GeneIDi 64858.
    KEGGi hsa:64858.
    UCSCi uc001eeg.3. human.

    Organism-specific databases

    CTDi 64858.
    GeneCardsi GC01P114447.
    HGNCi HGNC:17641. DCLRE1B.
    MIMi 305000. phenotype.
    609683. gene.
    neXtProti NX_Q9H816.
    PharmGKBi PA27175.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG1236.
    HOGENOMi HOG000043118.
    HOVERGENi HBG081420.
    InParanoidi Q9H816.
    KOi K15341.
    OMAi PCQVVPI.
    OrthoDBi EOG71VSSC.
    PhylomeDBi Q9H816.
    TreeFami TF329572.

    Miscellaneous databases

    EvolutionaryTracei Q9H816.
    GeneWikii DCLRE1B.
    GenomeRNAii 64858.
    NextBioi 67007.
    PROi Q9H816.
    SOURCEi Search...

    Gene expression databases

    Bgeei Q9H816.
    CleanExi HS_DCLRE1B.
    Genevestigatori Q9H816.

    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. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
      Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
      , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
      Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Tissue: Retinoblastoma and Teratocarcinoma.
    2. NIEHS SNPs program
      Submitted (DEC-2004) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANTS LEU-46; TYR-61 AND ASN-462.
    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. "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].
      Tissue: Placenta.
    5. Cited for: FUNCTION, SUBCELLULAR LOCATION.
    6. "Human SNM1B is required for normal cellular response to both DNA interstrand crosslink-inducing agents and ionizing radiation."
      Demuth I., Digweed M., Concannon P.
      Oncogene 23:8611-8618(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    7. "Apollo, an Artemis-related nuclease, interacts with TRF2 and protects human telomeres in S phase."
      van Overbeek M., de Lange T.
      Curr. Biol. 16:1295-1302(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY, FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH TERF2.
    8. "The Apollo 5' exonuclease functions together with TRF2 to protect telomeres from DNA repair."
      Lenain C., Bauwens S., Amiard S., Brunori M., Giraud-Panis M.J., Gilson E.
      Curr. Biol. 16:1303-1310(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY, FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH TERF2.
    9. "hSnm1B is a novel telomere-associated protein."
      Freibaum B.D., Counter C.M.
      J. Biol. Chem. 281:15033-15036(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBCELLULAR LOCATION, INTERACTION WITH TERF2.
    10. "Endogenous hSNM1B/Apollo interacts with TRF2 and stimulates ATM in response to ionizing radiation."
      Demuth I., Bradshaw P.S., Lindner A., Anders M., Heinrich S., Kallenbach J., Schmelz K., Digweed M., Meyn M.S., Concannon P.
      DNA Repair 7:1192-1201(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH TERF2.
    11. "The protein hSnm1B is stabilized when bound to the telomere-binding protein TRF2."
      Freibaum B.D., Counter C.M.
      J. Biol. Chem. 283:23671-23676(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: UBIQUITINATION, INTERACTION WITH TERF2.
    12. "Snm1B/Apollo mediates replication fork collapse and S Phase checkpoint activation in response to DNA interstrand cross-links."
      Bae J.B., Mukhopadhyay S.S., Liu L., Zhang N., Tan J., Akhter S., Liu X., Shen X., Li L., Legerski R.J.
      Oncogene 27:5045-5056(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH MUS81; MRE11 AND FANCD2.
    13. "SNM1B/Apollo interacts with astrin and is required for the prophase cell cycle checkpoint."
      Liu L., Akhter S., Bae J.B., Mukhopadhyay S.S., Richie C.T., Liu X., Legerski R.
      Cell Cycle 8:628-638(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH SPAG5, MUTAGENESIS OF ASP-14 AND HIS-276.
    14. "Evidence for hSNM1B/Apollo functioning in the HSP70 mediated DNA damage response."
      Anders M., Mattow J., Digweed M., Demuth I.
      Cell Cycle 8:1725-1732(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH HSPA2; HSPA8 AND HSPA14.
    15. Cited for: FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH TERF2, MUTAGENESIS OF ASP-14; HIS-33 AND ASP-35.
    16. "Function of Apollo (SNM1B) at telomere highlighted by a splice variant identified in a patient with Hoyeraal-Hreidarsson syndrome."
      Touzot F., Callebaut I., Soulier J., Gaillard L., Azerrad C., Durandy A., Fischer A., de Villartay J.P., Revy P.
      Proc. Natl. Acad. Sci. U.S.A. 107:10097-10102(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: POSSIBLE INVOLVEMENT IN HHS.
    17. "A shared docking motif in TRF1 and TRF2 used for differential recruitment of telomeric proteins."
      Chen Y., Yang Y., van Overbeek M., Donigian J.R., Baciu P., de Lange T., Lei M.
      Science 319:1092-1096(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 496-530 IN COMPLEX WITH TERF2, MUTAGENESIS OF TYR-504; LEU-506 AND PRO-508.

    Entry informationi

    Entry nameiDCR1B_HUMAN
    AccessioniPrimary (citable) accession number: Q9H816
    Secondary accession number(s): Q9H9E5
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: August 16, 2005
    Last sequence update: March 1, 2001
    Last modified: October 1, 2014
    This is version 108 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

    Miscellaneous

    Was named 'Apollo' in reference to the twin brother of 'Artemis' in Greek mythology (PubMed:16730175 and PubMed:16730176). Artemis/DCLRE1C is a related nuclease.

    Keywords - Technical termi

    3D-structure, 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. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    6. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3