DCR1B_HUMAN
ID DCR1B_HUMAN Reviewed; 532 AA.
AC Q9H816; Q9H9E5;
DT 16-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 163.
DE RecName: Full=5' exonuclease Apollo;
DE EC=3.1.-.-;
DE AltName: Full=Beta-lactamase DCLRE1B;
DE EC=3.5.2.6 {ECO:0000269|PubMed:31434986};
DE AltName: Full=DNA cross-link repair 1B protein;
DE AltName: Full=SNM1 homolog B;
DE Short=SNMIB;
DE Short=hSNM1B;
GN Name=DCLRE1B; Synonyms=SNM1B;
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 [LARGE SCALE MRNA].
RC TISSUE=Retinoblastoma, and Teratocarcinoma;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANTS LEU-46; TYR-61 AND ASN-462.
RG NIEHS SNPs program;
RL Submitted (DEC-2004) to the EMBL/GenBank/DDBJ databases.
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 MRNA].
RC TISSUE=Placenta;
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 project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [5]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=15572677; DOI=10.1128/mcb.24.24.10733-10741.2004;
RA Ishiai M., Kimura M., Namikoshi K., Yamazoe M., Yamamoto K., Arakawa H.,
RA Agematsu K., Matsushita N., Takeda S., Buerstedde J.-M., Takata M.;
RT "DNA cross-link repair protein SNM1A interacts with PIAS1 in nuclear focus
RT formation.";
RL Mol. Cell. Biol. 24:10733-10741(2004).
RN [6]
RP FUNCTION.
RX PubMed=15467758; DOI=10.1038/sj.onc.1207895;
RA Demuth I., Digweed M., Concannon P.;
RT "Human SNM1B is required for normal cellular response to both DNA
RT interstrand crosslink-inducing agents and ionizing radiation.";
RL Oncogene 23:8611-8618(2004).
RN [7]
RP IDENTIFICATION BY MASS SPECTROMETRY, FUNCTION, SUBCELLULAR LOCATION, AND
RP INTERACTION WITH TERF2.
RX PubMed=16730176; DOI=10.1016/j.cub.2006.05.022;
RA van Overbeek M., de Lange T.;
RT "Apollo, an Artemis-related nuclease, interacts with TRF2 and protects
RT human telomeres in S phase.";
RL Curr. Biol. 16:1295-1302(2006).
RN [8]
RP IDENTIFICATION BY MASS SPECTROMETRY, FUNCTION, SUBCELLULAR LOCATION, AND
RP INTERACTION WITH TERF2.
RX PubMed=16730175; DOI=10.1016/j.cub.2006.05.021;
RA Lenain C., Bauwens S., Amiard S., Brunori M., Giraud-Panis M.J., Gilson E.;
RT "The Apollo 5' exonuclease functions together with TRF2 to protect
RT telomeres from DNA repair.";
RL Curr. Biol. 16:1303-1310(2006).
RN [9]
RP SUBCELLULAR LOCATION, AND INTERACTION WITH TERF2.
RX PubMed=16606622; DOI=10.1074/jbc.c600038200;
RA Freibaum B.D., Counter C.M.;
RT "hSnm1B is a novel telomere-associated protein.";
RL J. Biol. Chem. 281:15033-15036(2006).
RN [10]
RP FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH TERF2.
RX PubMed=18468965; DOI=10.1016/j.dnarep.2008.03.020;
RA Demuth I., Bradshaw P.S., Lindner A., Anders M., Heinrich S.,
RA Kallenbach J., Schmelz K., Digweed M., Meyn M.S., Concannon P.;
RT "Endogenous hSNM1B/Apollo interacts with TRF2 and stimulates ATM in
RT response to ionizing radiation.";
RL DNA Repair 7:1192-1201(2008).
RN [11]
RP UBIQUITINATION, AND INTERACTION WITH TERF2.
RX PubMed=18593705; DOI=10.1074/jbc.m800388200;
RA Freibaum B.D., Counter C.M.;
RT "The protein hSnm1B is stabilized when bound to the telomere-binding
RT protein TRF2.";
RL J. Biol. Chem. 283:23671-23676(2008).
RN [12]
RP FUNCTION, AND INTERACTION WITH MUS81; MRE11 AND FANCD2.
RX PubMed=18469862; DOI=10.1038/onc.2008.139;
RA Bae J.B., Mukhopadhyay S.S., Liu L., Zhang N., Tan J., Akhter S., Liu X.,
RA Shen X., Li L., Legerski R.J.;
RT "Snm1B/Apollo mediates replication fork collapse and S Phase checkpoint
RT activation in response to DNA interstrand cross-links.";
RL Oncogene 27:5045-5056(2008).
RN [13]
RP FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH SPAG5, AND MUTAGENESIS OF
RP ASP-14 AND HIS-276.
RX PubMed=19197158; DOI=10.4161/cc.8.4.7791;
RA Liu L., Akhter S., Bae J.B., Mukhopadhyay S.S., Richie C.T., Liu X.,
RA Legerski R.;
RT "SNM1B/Apollo interacts with astrin and is required for the prophase cell
RT cycle checkpoint.";
RL Cell Cycle 8:628-638(2009).
RN [14]
RP FUNCTION, AND INTERACTION WITH HSPA2; HSPA8 AND HSPA14.
RX PubMed=19411856; DOI=10.4161/cc.8.11.8605;
RA Anders M., Mattow J., Digweed M., Demuth I.;
RT "Evidence for hSNM1B/Apollo functioning in the HSP70 mediated DNA damage
RT response.";
RL Cell Cycle 8:1725-1732(2009).
RN [15]
RP FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH TERF2, AND MUTAGENESIS OF
RP ASP-14; HIS-33 AND ASP-35.
RX PubMed=20655466; DOI=10.1016/j.cell.2010.05.032;
RA Ye J., Lenain C., Bauwens S., Rizzo A., Saint-Leger A., Poulet A.,
RA Benarroch D., Magdinier F., Morere J., Amiard S., Verhoeyen E., Britton S.,
RA Calsou P., Salles B., Bizard A., Nadal M., Salvati E., Sabatier L., Wu Y.,
RA Biroccio A., Londono-Vallejo A., Giraud-Panis M.J., Gilson E.;
RT "TRF2 and Apollo cooperate with topoisomerase 2alpha to protect human
RT telomeres from replicative damage.";
RL Cell 142:230-242(2010).
RN [16]
RP POSSIBLE INVOLVEMENT IN HHS.
RX PubMed=20479256; DOI=10.1073/pnas.0914918107;
RA Touzot F., Callebaut I., Soulier J., Gaillard L., Azerrad C., Durandy A.,
RA Fischer A., de Villartay J.P., Revy P.;
RT "Function of Apollo (SNM1B) at telomere highlighted by a splice variant
RT identified in a patient with Hoyeraal-Hreidarsson syndrome.";
RL Proc. Natl. Acad. Sci. U.S.A. 107:10097-10102(2010).
RN [17]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-333, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=28112733; DOI=10.1038/nsmb.3366;
RA Hendriks I.A., Lyon D., Young C., Jensen L.J., Vertegaal A.C.,
RA Nielsen M.L.;
RT "Site-specific mapping of the human SUMO proteome reveals co-modification
RT with phosphorylation.";
RL Nat. Struct. Mol. Biol. 24:325-336(2017).
RN [18]
RP FUNCTION, CATALYTIC ACTIVITY, AND ACTIVITY REGULATION.
RX PubMed=31434986; DOI=10.1038/s41598-019-48723-y;
RA Diene S.M., Pinault L., Keshri V., Armstrong N., Khelaifia S.,
RA Chabriere E., Caetano-Anolles G., Colson P., La Scola B., Rolain J.M.,
RA Pontarotti P., Raoult D.;
RT "Human metallo-beta-lactamase enzymes degrade penicillin.";
RL Sci. Rep. 9:12173-12173(2019).
RN [19]
RP X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 496-530 IN COMPLEX WITH TERF2, AND
RP MUTAGENESIS OF TYR-504; LEU-506 AND PRO-508.
RX PubMed=18202258; DOI=10.1126/science.1151804;
RA Chen Y., Yang Y., van Overbeek M., Donigian J.R., Baciu P., de Lange T.,
RA Lei M.;
RT "A shared docking motif in TRF1 and TRF2 used for differential recruitment
RT of telomeric proteins.";
RL Science 319:1092-1096(2008).
CC -!- FUNCTION: 5'-3' exonuclease that plays a central role in telomere
CC maintenance and protection during S-phase. Participates in the
CC protection of telomeres against non-homologous end-joining (NHEJ)-
CC mediated repair, thereby ensuring that telomeres do not fuse. Plays a
CC key role in telomeric loop (T loop) formation by being recruited by
CC TERF2 at the leading end telomeres and by processing leading-end
CC telomeres immediately after their replication via its exonuclease
CC activity: generates 3' single-stranded overhang at the leading end
CC telomeres avoiding blunt leading-end telomeres that are vulnerable to
CC end-joining reactions and expose the telomere end in a manner that
CC activates the DNA repair pathways. Together with TERF2, required to
CC protect telomeres from replicative damage during replication by
CC controlling the amount of DNA topoisomerase (TOP1, TOP2A and TOP2B)
CC needed for telomere replication during fork passage and prevent
CC aberrant telomere topology. Also involved in response to DNA damage:
CC plays a role in response to DNA interstrand cross-links (ICLs) by
CC facilitating double-strand break formation. In case of spindle stress,
CC involved in prophase checkpoint. Possesses beta-lactamase activity,
CC catalyzing the hydrolysis of penicillin G and nitrocefin
CC (PubMed:31434986). Exhibits no activity towards other beta-lactam
CC antibiotic classes including cephalosporins (cefotaxime) and
CC carbapenems (imipenem) (PubMed:31434986). {ECO:0000269|PubMed:15467758,
CC ECO:0000269|PubMed:15572677, ECO:0000269|PubMed:16730175,
CC ECO:0000269|PubMed:16730176, ECO:0000269|PubMed:18468965,
CC ECO:0000269|PubMed:18469862, ECO:0000269|PubMed:19197158,
CC ECO:0000269|PubMed:19411856, ECO:0000269|PubMed:20655466,
CC ECO:0000269|PubMed:31434986}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a beta-lactam + H2O = a substituted beta-amino acid;
CC Xref=Rhea:RHEA:20401, ChEBI:CHEBI:15377, ChEBI:CHEBI:35627,
CC ChEBI:CHEBI:140347; EC=3.5.2.6;
CC Evidence={ECO:0000269|PubMed:31434986};
CC -!- ACTIVITY REGULATION: Beta-lactamase activity is inhibited by sulbactam.
CC {ECO:0000269|PubMed:31434986}.
CC -!- SUBUNIT: Interacts with TERF2; the interaction is direct. Interacts
CC with MUS81, MRE11 and FANCD2. Interacts with HSPA2, HSPA8 and HSPA14.
CC Interacts with SPAG5. {ECO:0000269|PubMed:16606622,
CC ECO:0000269|PubMed:16730175, ECO:0000269|PubMed:16730176,
CC ECO:0000269|PubMed:18202258, ECO:0000269|PubMed:18468965,
CC ECO:0000269|PubMed:18469862, ECO:0000269|PubMed:18593705,
CC ECO:0000269|PubMed:19197158, ECO:0000269|PubMed:19411856,
CC ECO:0000269|PubMed:20655466}.
CC -!- INTERACTION:
CC Q9H816; P02649: APOE; NbExp=3; IntAct=EBI-3508943, EBI-1222467;
CC Q9H816; P54252: ATXN3; NbExp=3; IntAct=EBI-3508943, EBI-946046;
CC Q9H816; P21964-2: COMT; NbExp=3; IntAct=EBI-3508943, EBI-10200977;
CC Q9H816; P50570-2: DNM2; NbExp=3; IntAct=EBI-3508943, EBI-10968534;
CC Q9H816; P26378-2: ELAVL4; NbExp=3; IntAct=EBI-3508943, EBI-21603100;
CC Q9H816; P42858: HTT; NbExp=9; IntAct=EBI-3508943, EBI-466029;
CC Q9H816; Q92597: NDRG1; NbExp=3; IntAct=EBI-3508943, EBI-716486;
CC Q9H816; Q86UR1-2: NOXA1; NbExp=3; IntAct=EBI-3508943, EBI-12025760;
CC Q9H816; P49768-2: PSEN1; NbExp=3; IntAct=EBI-3508943, EBI-11047108;
CC Q9H816; Q7Z699: SPRED1; NbExp=3; IntAct=EBI-3508943, EBI-5235340;
CC Q9H816; Q9NUW8: TDP1; NbExp=3; IntAct=EBI-3508943, EBI-2902553;
CC Q9H816; Q15554: TERF2; NbExp=10; IntAct=EBI-3508943, EBI-706637;
CC Q9H816; O76024: WFS1; NbExp=3; IntAct=EBI-3508943, EBI-720609;
CC -!- SUBCELLULAR LOCATION: Chromosome, telomere. Nucleus. Cytoplasm,
CC cytoskeleton, microtubule organizing center, centrosome. Note=Mainly
CC localizes to telomeres, recruited via its interaction with TERF2.
CC During mitosis, localizes to the centrosome.
CC -!- DOMAIN: The TBM domain mediates interaction with TERF2.
CC -!- PTM: Ubiquitinated, leading to its degradation. Interaction with TERF2
CC protects it from ubiquitination. {ECO:0000269|PubMed:18593705}.
CC -!- DISEASE: Hoyeraal-Hreidarsson syndrome (HHS) [MIM:305000]: A clinically
CC severe variant of dyskeratosis congenita that is characterized by
CC multisystem involvement, early onset in utero, and often results in
CC death in childhood. Affected individuals show intrauterine growth
CC retardation, microcephaly, cerebellar hypoplasia, delayed development,
CC and bone marrow failure resulting in immunodeficiency.
CC {ECO:0000269|PubMed:20479256}. Note=The gene represented in this entry
CC may be involved in disease pathogenesis. An aberrant splice variant of
CC DCLRE1B, designated Apollo-Delta, has been found in a patient with
CC Hoyeraal-Hreidarsson syndrome (PubMed:20479256). Apollo-Delta hampers
CC the proper replication of telomeres, leading to major telomeric
CC dysfunction and cellular senescence, but maintains its DNA interstrand
CC cross-link repair function in the whole genome.
CC {ECO:0000269|PubMed:20479256}.
CC -!- MISCELLANEOUS: Was named 'Apollo' in reference to the twin brother of
CC 'Artemis' in Greek mythology (PubMed:16730175 and PubMed:16730176).
CC Artemis/DCLRE1C is a related nuclease.
CC -!- SIMILARITY: Belongs to the DNA repair metallo-beta-lactamase (DRMBL)
CC family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAB14284.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC -!- WEB RESOURCE: Name=NIEHS-SNPs;
CC URL="http://egp.gs.washington.edu/data/dclre1b/";
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DR EMBL; AK022872; BAB14284.1; ALT_INIT; mRNA.
DR EMBL; AK024060; BAB14807.1; -; mRNA.
DR EMBL; AY849379; AAV97812.1; -; Genomic_DNA.
DR EMBL; AL137856; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC029687; AAH29687.1; -; mRNA.
DR CCDS; CCDS866.1; -.
DR RefSeq; NP_001306876.1; NM_001319947.1.
DR RefSeq; NP_073747.1; NM_022836.3.
DR PDB; 3BUA; X-ray; 2.50 A; E/F/G/H=495-530.
DR PDB; 5AHO; X-ray; 2.16 A; A=1-335.
DR PDB; 7A1F; X-ray; 1.80 A; A/L=1-335.
DR PDB; 7B2X; X-ray; 3.10 A; A=2-335.
DR PDB; 7B9B; X-ray; 2.80 A; A=1-335.
DR PDBsum; 3BUA; -.
DR PDBsum; 5AHO; -.
DR PDBsum; 7A1F; -.
DR PDBsum; 7B2X; -.
DR PDBsum; 7B9B; -.
DR AlphaFoldDB; Q9H816; -.
DR SMR; Q9H816; -.
DR BioGRID; 122331; 32.
DR DIP; DIP-42669N; -.
DR ELM; Q9H816; -.
DR IntAct; Q9H816; 31.
DR MINT; Q9H816; -.
DR STRING; 9606.ENSP00000358576; -.
DR BindingDB; Q9H816; -.
DR ChEMBL; CHEMBL4105944; -.
DR iPTMnet; Q9H816; -.
DR PhosphoSitePlus; Q9H816; -.
DR BioMuta; DCLRE1B; -.
DR DMDM; 73620756; -.
DR EPD; Q9H816; -.
DR MassIVE; Q9H816; -.
DR PaxDb; Q9H816; -.
DR PeptideAtlas; Q9H816; -.
DR PRIDE; Q9H816; -.
DR ProteomicsDB; 81169; -.
DR Antibodypedia; 46943; 161 antibodies from 24 providers.
DR DNASU; 64858; -.
DR Ensembl; ENST00000650450.2; ENSP00000498042.1; ENSG00000118655.7.
DR GeneID; 64858; -.
DR KEGG; hsa:64858; -.
DR MANE-Select; ENST00000650450.2; ENSP00000498042.1; NM_022836.4; NP_073747.1.
DR UCSC; uc001eeg.4; human.
DR CTD; 64858; -.
DR DisGeNET; 64858; -.
DR GeneCards; DCLRE1B; -.
DR HGNC; HGNC:17641; DCLRE1B.
DR HPA; ENSG00000118655; Low tissue specificity.
DR MIM; 305000; phenotype.
DR MIM; 609683; gene.
DR neXtProt; NX_Q9H816; -.
DR OpenTargets; ENSG00000118655; -.
DR PharmGKB; PA27175; -.
DR VEuPathDB; HostDB:ENSG00000118655; -.
DR eggNOG; KOG1361; Eukaryota.
DR GeneTree; ENSGT00940000158175; -.
DR HOGENOM; CLU_034741_0_0_1; -.
DR OMA; KMVTVLT; -.
DR OrthoDB; 1441774at2759; -.
DR PhylomeDB; Q9H816; -.
DR TreeFam; TF329572; -.
DR PathwayCommons; Q9H816; -.
DR Reactome; R-HSA-6783310; Fanconi Anemia Pathway.
DR SignaLink; Q9H816; -.
DR BioGRID-ORCS; 64858; 422 hits in 1102 CRISPR screens.
DR ChiTaRS; DCLRE1B; human.
DR EvolutionaryTrace; Q9H816; -.
DR GeneWiki; DCLRE1B; -.
DR GenomeRNAi; 64858; -.
DR Pharos; Q9H816; Tbio.
DR PRO; PR:Q9H816; -.
DR Proteomes; UP000005640; Chromosome 1.
DR RNAct; Q9H816; protein.
DR Bgee; ENSG00000118655; Expressed in secondary oocyte and 153 other tissues.
DR ExpressionAtlas; Q9H816; baseline and differential.
DR Genevisible; Q9H816; HS.
DR GO; GO:0005813; C:centrosome; IDA:UniProtKB.
DR GO; GO:0000781; C:chromosome, telomeric region; IDA:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR GO; GO:0016604; C:nuclear body; IDA:HPA.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0035312; F:5'-3' exodeoxyribonuclease activity; IBA:GO_Central.
DR GO; GO:0008409; F:5'-3' exonuclease activity; IDA:UniProtKB.
DR GO; GO:0008800; F:beta-lactamase activity; IDA:UniProtKB.
DR GO; GO:0003684; F:damaged DNA binding; IBA:GO_Central.
DR GO; GO:0042803; F:protein homodimerization activity; IDA:BHF-UCL.
DR GO; GO:0044877; F:protein-containing complex binding; IPI:BHF-UCL.
DR GO; GO:0006303; P:double-strand break repair via nonhomologous end joining; IBA:GO_Central.
DR GO; GO:0036297; P:interstrand cross-link repair; IMP:BHF-UCL.
DR GO; GO:0031848; P:protection from non-homologous end joining at telomere; IMP:UniProtKB.
DR GO; GO:0016233; P:telomere capping; IMP:BHF-UCL.
DR GO; GO:0000723; P:telomere maintenance; IMP:UniProtKB.
DR GO; GO:0010833; P:telomere maintenance via telomere lengthening; IMP:BHF-UCL.
DR GO; GO:0031860; P:telomeric 3' overhang formation; ISS:UniProtKB.
DR GO; GO:0031627; P:telomeric loop formation; ISS:UniProtKB.
DR DisProt; DP01268; -.
DR Gene3D; 3.60.15.10; -; 1.
DR IDEAL; IID00116; -.
DR InterPro; IPR011084; DRMBL.
DR InterPro; IPR036866; RibonucZ/Hydroxyglut_hydro.
DR Pfam; PF07522; DRMBL; 1.
DR SUPFAM; SSF56281; SSF56281; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Chromosome; Cytoplasm; Cytoskeleton; DNA damage; DNA repair;
KW Dyskeratosis congenita; Exonuclease; Hydrolase; Isopeptide bond; Nuclease;
KW Nucleus; Reference proteome; Telomere; Ubl conjugation.
FT CHAIN 1..532
FT /note="5' exonuclease Apollo"
FT /id="PRO_0000209119"
FT REGION 350..392
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 453..482
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 496..511
FT /note="TBM"
FT COMPBIAS 361..392
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CROSSLNK 333
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT VARIANT 46
FT /note="R -> L (in dbSNP:rs28381069)"
FT /evidence="ECO:0000269|Ref.2"
FT /id="VAR_023292"
FT VARIANT 61
FT /note="H -> Y (in dbSNP:rs11552449)"
FT /evidence="ECO:0000269|Ref.2"
FT /id="VAR_023293"
FT VARIANT 462
FT /note="D -> N (in dbSNP:rs28381079)"
FT /evidence="ECO:0000269|Ref.2"
FT /id="VAR_023294"
FT VARIANT 510
FT /note="N -> Y (in dbSNP:rs35397235)"
FT /id="VAR_048891"
FT MUTAGEN 14
FT /note="D->N: In Apm3; abolishes exonuclease activity and
FT function on telomere maintenance. Impairs interaction with
FT SPAG5."
FT /evidence="ECO:0000269|PubMed:19197158,
FT ECO:0000269|PubMed:20655466"
FT MUTAGEN 33
FT /note="H->A: In Apm1; abolishes exonuclease activity and
FT function on telomere maintenance; when associated with N-
FT 35."
FT /evidence="ECO:0000269|PubMed:20655466"
FT MUTAGEN 35
FT /note="D->N: In Apm2; abolishes exonuclease activity and
FT function on telomere maintenance. In Apm1; abolishes
FT exonuclease activity and function on telomere maintenance;
FT when associated with A-33."
FT /evidence="ECO:0000269|PubMed:20655466"
FT MUTAGEN 276
FT /note="H->A: Slightly affects interaction with SPAG5."
FT /evidence="ECO:0000269|PubMed:19197158"
FT MUTAGEN 504
FT /note="Y->A: Abolishes interaction with TERF2."
FT /evidence="ECO:0000269|PubMed:18202258"
FT MUTAGEN 506
FT /note="L->A: Abolishes interaction with TERF2."
FT /evidence="ECO:0000269|PubMed:18202258"
FT MUTAGEN 508
FT /note="P->A: Abolishes interaction with TERF2."
FT /evidence="ECO:0000269|PubMed:18202258"
FT CONFLICT 237
FT /note="I -> T (in Ref. 1; BAB14284)"
FT /evidence="ECO:0000305"
FT STRAND 4..6
FT /evidence="ECO:0007829|PDB:5AHO"
FT STRAND 9..14
FT /evidence="ECO:0007829|PDB:7A1F"
FT HELIX 18..20
FT /evidence="ECO:0007829|PDB:7A1F"
FT STRAND 26..28
FT /evidence="ECO:0007829|PDB:7A1F"
FT HELIX 34..36
FT /evidence="ECO:0007829|PDB:7A1F"
FT STRAND 48..50
FT /evidence="ECO:0007829|PDB:7A1F"
FT HELIX 52..62
FT /evidence="ECO:0007829|PDB:7A1F"
FT HELIX 66..68
FT /evidence="ECO:0007829|PDB:7A1F"
FT STRAND 69..71
FT /evidence="ECO:0007829|PDB:7A1F"
FT STRAND 76..86
FT /evidence="ECO:0007829|PDB:7A1F"
FT STRAND 89..96
FT /evidence="ECO:0007829|PDB:7A1F"
FT STRAND 98..100
FT /evidence="ECO:0007829|PDB:7A1F"
FT STRAND 104..110
FT /evidence="ECO:0007829|PDB:7A1F"
FT STRAND 113..117
FT /evidence="ECO:0007829|PDB:7A1F"
FT HELIX 125..128
FT /evidence="ECO:0007829|PDB:7A1F"
FT HELIX 131..133
FT /evidence="ECO:0007829|PDB:7A1F"
FT STRAND 140..144
FT /evidence="ECO:0007829|PDB:7A1F"
FT HELIX 147..149
FT /evidence="ECO:0007829|PDB:7B9B"
FT STRAND 150..152
FT /evidence="ECO:0007829|PDB:7B9B"
FT HELIX 158..170
FT /evidence="ECO:0007829|PDB:7A1F"
FT STRAND 175..181
FT /evidence="ECO:0007829|PDB:7A1F"
FT STRAND 183..185
FT /evidence="ECO:0007829|PDB:5AHO"
FT HELIX 187..196
FT /evidence="ECO:0007829|PDB:7A1F"
FT HELIX 205..211
FT /evidence="ECO:0007829|PDB:7A1F"
FT TURN 212..215
FT /evidence="ECO:0007829|PDB:7A1F"
FT STRAND 220..222
FT /evidence="ECO:0007829|PDB:5AHO"
FT STRAND 226..233
FT /evidence="ECO:0007829|PDB:7A1F"
FT HELIX 234..236
FT /evidence="ECO:0007829|PDB:7A1F"
FT HELIX 239..245
FT /evidence="ECO:0007829|PDB:7A1F"
FT TURN 246..248
FT /evidence="ECO:0007829|PDB:7A1F"
FT STRAND 251..256
FT /evidence="ECO:0007829|PDB:7A1F"
FT STRAND 268..271
FT /evidence="ECO:0007829|PDB:7A1F"
FT HELIX 279..289
FT /evidence="ECO:0007829|PDB:7A1F"
FT STRAND 292..297
FT /evidence="ECO:0007829|PDB:7A1F"
FT HELIX 307..309
FT /evidence="ECO:0007829|PDB:7A1F"
FT HELIX 321..327
FT /evidence="ECO:0007829|PDB:7A1F"
FT HELIX 330..332
FT /evidence="ECO:0007829|PDB:7A1F"
FT HELIX 500..503
FT /evidence="ECO:0007829|PDB:3BUA"
SQ SEQUENCE 532 AA; 60002 MW; 601A800CCD43CFDA CRC64;
MNGVLIPHTP IAVDFWSLRR AGTARLFFLS HMHSDHTVGL SSTWARPLYC SPITAHLLHR
HLQVSKQWIQ ALEVGESHVL PLDEIGQETM TVTLLDANHC PGSVMFLFEG YFGTILYTGD
FRYTPSMLKE PALTLGKQIH TLYLDNTNCN PALVLPSRQE AAHQIVQLIR KHPQHNIKIG
LYSLGKESLL EQLALEFQTW VVLSPRRLEL VQLLGLADVF TVEEKAGRIH AVDHMEICHS
NMLRWNQTHP TIAILPTSRK IHSSHPDIHV IPYSDHSSYS ELRAFVAALK PCQVVPIVSR
RPCGGFQDSL SPRISVPLIP DSVQQYMSSS SRKPSLLWLL ERRLKRPRTQ GVVFESPEES
ADQSQADRDS KKAKKEKLSP WPADLEKQPS HHPLRIKKQL FPDLYSKEWN KAVPFCESQK
RVTMLTAPLG FSVHLRSTDE EFISQKTREE IGLGSPLVPM GDDDGGPEAT GNQSAWMGHG
SPLSHSSKGT PLLATEFRGL ALKYLLTPVN FFQAGYSSRR FDQQVEKYHK PC
