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5' exonuclease Apollo (EC 3.1.-.-) (DNA cross-link repair 1B protein) (SNM1 homolog B) (SNMIB) (hSNM1B)

 DCR1B_HUMAN             Reviewed;         532 AA.
Q9H816; Q9H9E5;
16-AUG-2005, integrated into UniProtKB/Swiss-Prot.
01-MAR-2001, sequence version 1.
25-OCT-2017, entry version 134.
RecName: Full=5' exonuclease Apollo;
EC=3.1.-.-;
AltName: Full=DNA cross-link repair 1B protein;
AltName: Full=SNM1 homolog B;
Short=SNMIB;
Short=hSNM1B;
Name=DCLRE1B; Synonyms=SNM1B;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Retinoblastoma, and Teratocarcinoma;
PubMed=14702039; DOI=10.1038/ng1285;
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.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANTS LEU-46; TYR-61 AND
ASN-462.
NIEHS SNPs program;
Submitted (DEC-2004) to the EMBL/GenBank/DDBJ databases.
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=16710414; DOI=10.1038/nature04727;
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.;
"The DNA sequence and biological annotation of human chromosome 1.";
Nature 441:315-321(2006).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Placenta;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[5]
FUNCTION, AND SUBCELLULAR LOCATION.
PubMed=15572677; DOI=10.1128/MCB.24.24.10733-10741.2004;
Ishiai M., Kimura M., Namikoshi K., Yamazoe M., Yamamoto K.,
Arakawa H., Agematsu K., Matsushita N., Takeda S., Buerstedde J.-M.,
Takata M.;
"DNA cross-link repair protein SNM1A interacts with PIAS1 in nuclear
focus formation.";
Mol. Cell. Biol. 24:10733-10741(2004).
[6]
FUNCTION.
PubMed=15467758; DOI=10.1038/sj.onc.1207895;
Demuth I., Digweed M., Concannon P.;
"Human SNM1B is required for normal cellular response to both DNA
interstrand crosslink-inducing agents and ionizing radiation.";
Oncogene 23:8611-8618(2004).
[7]
IDENTIFICATION BY MASS SPECTROMETRY, FUNCTION, SUBCELLULAR LOCATION,
AND INTERACTION WITH TERF2.
PubMed=16730176; DOI=10.1016/j.cub.2006.05.022;
van Overbeek M., de Lange T.;
"Apollo, an Artemis-related nuclease, interacts with TRF2 and protects
human telomeres in S phase.";
Curr. Biol. 16:1295-1302(2006).
[8]
IDENTIFICATION BY MASS SPECTROMETRY, FUNCTION, SUBCELLULAR LOCATION,
AND INTERACTION WITH TERF2.
PubMed=16730175; DOI=10.1016/j.cub.2006.05.021;
Lenain C., Bauwens S., Amiard S., Brunori M., Giraud-Panis M.J.,
Gilson E.;
"The Apollo 5' exonuclease functions together with TRF2 to protect
telomeres from DNA repair.";
Curr. Biol. 16:1303-1310(2006).
[9]
SUBCELLULAR LOCATION, AND INTERACTION WITH TERF2.
PubMed=16606622; DOI=10.1074/jbc.C600038200;
Freibaum B.D., Counter C.M.;
"hSnm1B is a novel telomere-associated protein.";
J. Biol. Chem. 281:15033-15036(2006).
[10]
FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH TERF2.
PubMed=18468965; DOI=10.1016/j.dnarep.2008.03.020;
Demuth I., Bradshaw P.S., Lindner A., Anders M., Heinrich S.,
Kallenbach J., Schmelz K., Digweed M., Meyn M.S., Concannon P.;
"Endogenous hSNM1B/Apollo interacts with TRF2 and stimulates ATM in
response to ionizing radiation.";
DNA Repair 7:1192-1201(2008).
[11]
UBIQUITINATION, AND INTERACTION WITH TERF2.
PubMed=18593705; DOI=10.1074/jbc.M800388200;
Freibaum B.D., Counter C.M.;
"The protein hSnm1B is stabilized when bound to the telomere-binding
protein TRF2.";
J. Biol. Chem. 283:23671-23676(2008).
[12]
FUNCTION, AND INTERACTION WITH MUS81; MRE11 AND FANCD2.
PubMed=18469862; DOI=10.1038/onc.2008.139;
Bae J.B., Mukhopadhyay S.S., Liu L., Zhang N., Tan J., Akhter S.,
Liu X., Shen X., Li L., Legerski R.J.;
"Snm1B/Apollo mediates replication fork collapse and S Phase
checkpoint activation in response to DNA interstrand cross-links.";
Oncogene 27:5045-5056(2008).
[13]
FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH SPAG5, AND
MUTAGENESIS OF ASP-14 AND HIS-276.
PubMed=19197158; DOI=10.4161/cc.8.4.7791;
Liu L., Akhter S., Bae J.B., Mukhopadhyay S.S., Richie C.T., Liu X.,
Legerski R.;
"SNM1B/Apollo interacts with astrin and is required for the prophase
cell cycle checkpoint.";
Cell Cycle 8:628-638(2009).
[14]
FUNCTION, AND INTERACTION WITH HSPA2; HSPA8 AND HSPA14.
PubMed=19411856; DOI=10.4161/cc.8.11.8605;
Anders M., Mattow J., Digweed M., Demuth I.;
"Evidence for hSNM1B/Apollo functioning in the HSP70 mediated DNA
damage response.";
Cell Cycle 8:1725-1732(2009).
[15]
FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH TERF2, AND
MUTAGENESIS OF ASP-14; HIS-33 AND ASP-35.
PubMed=20655466; DOI=10.1016/j.cell.2010.05.032;
Ye J., Lenain C., Bauwens S., Rizzo A., Saint-Leger A., Poulet A.,
Benarroch D., Magdinier F., Morere J., Amiard S., Verhoeyen E.,
Britton S., Calsou P., Salles B., Bizard A., Nadal M., Salvati E.,
Sabatier L., Wu Y., Biroccio A., Londono-Vallejo A.,
Giraud-Panis M.J., Gilson E.;
"TRF2 and Apollo cooperate with topoisomerase 2alpha to protect human
telomeres from replicative damage.";
Cell 142:230-242(2010).
[16]
POSSIBLE INVOLVEMENT IN HHS.
PubMed=20479256; DOI=10.1073/pnas.0914918107;
Touzot F., Callebaut I., Soulier J., Gaillard L., Azerrad C.,
Durandy A., Fischer A., de Villartay J.P., Revy P.;
"Function of Apollo (SNM1B) at telomere highlighted by a splice
variant identified in a patient with Hoyeraal-Hreidarsson syndrome.";
Proc. Natl. Acad. Sci. U.S.A. 107:10097-10102(2010).
[17]
SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-333, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=28112733; DOI=10.1038/nsmb.3366;
Hendriks I.A., Lyon D., Young C., Jensen L.J., Vertegaal A.C.,
Nielsen M.L.;
"Site-specific mapping of the human SUMO proteome reveals co-
modification with phosphorylation.";
Nat. Struct. Mol. Biol. 24:325-336(2017).
[18]
X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 496-530 IN COMPLEX WITH
TERF2, AND MUTAGENESIS OF TYR-504; LEU-506 AND PRO-508.
PubMed=18202258; DOI=10.1126/science.1151804;
Chen Y., Yang Y., van Overbeek M., Donigian J.R., Baciu P.,
de Lange T., Lei M.;
"A shared docking motif in TRF1 and TRF2 used for differential
recruitment of telomeric proteins.";
Science 319:1092-1096(2008).
-!- FUNCTION: 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. {ECO:0000269|PubMed:15467758,
ECO:0000269|PubMed:15572677, ECO:0000269|PubMed:16730175,
ECO:0000269|PubMed:16730176, ECO:0000269|PubMed:18468965,
ECO:0000269|PubMed:18469862, ECO:0000269|PubMed:19197158,
ECO:0000269|PubMed:19411856, ECO:0000269|PubMed:20655466}.
-!- SUBUNIT: Interacts with TERF2; the interaction is direct.
Interacts with MUS81, MRE11 and FANCD2. Interacts with HSPA2,
HSPA8 and HSPA14. Interacts with SPAG5.
{ECO:0000269|PubMed:16606622, ECO:0000269|PubMed:16730175,
ECO:0000269|PubMed:16730176, ECO:0000269|PubMed:18202258,
ECO:0000269|PubMed:18468965, ECO:0000269|PubMed:18469862,
ECO:0000269|PubMed:18593705, ECO:0000269|PubMed:19197158,
ECO:0000269|PubMed:19411856, ECO:0000269|PubMed:20655466}.
-!- INTERACTION:
Q15554:TERF2; NbExp=9; IntAct=EBI-3508943, EBI-706637;
-!- SUBCELLULAR LOCATION: Chromosome, telomere. Nucleus. Cytoplasm,
cytoskeleton, microtubule organizing center, centrosome.
Note=Mainly localizes to telomeres, recruited via its interaction
with TERF2. During mitosis, localizes to the centrosome.
-!- DOMAIN: The TBM domain mediates interaction with TERF2.
-!- PTM: Ubiquitinated, leading to its degradation. Interaction with
TERF2 protects it from ubiquitination.
{ECO:0000269|PubMed:18593705}.
-!- DISEASE: 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. {ECO:0000269|PubMed:20479256}. 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. {ECO:0000269|PubMed:20479256}.
-!- 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.
-!- SIMILARITY: Belongs to the DNA repair metallo-beta-lactamase
(DRMBL) family. {ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=BAB14284.1; Type=Erroneous initiation; Evidence={ECO:0000305};
-!- WEB RESOURCE: Name=NIEHS-SNPs;
URL="http://egp.gs.washington.edu/data/dclre1b/";
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EMBL; AK022872; BAB14284.1; ALT_INIT; mRNA.
EMBL; AK024060; BAB14807.1; -; mRNA.
EMBL; AY849379; AAV97812.1; -; Genomic_DNA.
EMBL; AL137856; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; BC029687; AAH29687.1; -; mRNA.
CCDS; CCDS866.1; -.
RefSeq; NP_001306876.1; NM_001319947.1.
RefSeq; NP_073747.1; NM_022836.3.
UniGene; Hs.591412; -.
UniGene; Hs.628365; -.
PDB; 3BUA; X-ray; 2.50 A; E/F/G/H=495-530.
PDB; 5AHO; X-ray; 2.16 A; A=1-335.
PDBsum; 3BUA; -.
PDBsum; 5AHO; -.
ProteinModelPortal; Q9H816; -.
SMR; Q9H816; -.
BioGrid; 122331; 16.
DIP; DIP-42669N; -.
ELM; Q9H816; -.
IntAct; Q9H816; 14.
MINT; MINT-3372972; -.
STRING; 9606.ENSP00000358576; -.
iPTMnet; Q9H816; -.
PhosphoSitePlus; Q9H816; -.
BioMuta; DCLRE1B; -.
DMDM; 73620756; -.
EPD; Q9H816; -.
PaxDb; Q9H816; -.
PeptideAtlas; Q9H816; -.
PRIDE; Q9H816; -.
DNASU; 64858; -.
Ensembl; ENST00000369563; ENSP00000358576; ENSG00000118655.
GeneID; 64858; -.
KEGG; hsa:64858; -.
UCSC; uc001eeg.4; human.
CTD; 64858; -.
DisGeNET; 64858; -.
EuPathDB; HostDB:ENSG00000118655.4; -.
GeneCards; DCLRE1B; -.
HGNC; HGNC:17641; DCLRE1B.
HPA; HPA064934; -.
MIM; 305000; phenotype.
MIM; 609683; gene.
neXtProt; NX_Q9H816; -.
OpenTargets; ENSG00000118655; -.
PharmGKB; PA27175; -.
eggNOG; KOG1361; Eukaryota.
eggNOG; COG1236; LUCA.
GeneTree; ENSGT00530000063183; -.
HOGENOM; HOG000043118; -.
HOVERGEN; HBG081420; -.
KO; K15341; -.
OMA; PCQVVPI; -.
OrthoDB; EOG091G0DBZ; -.
PhylomeDB; Q9H816; -.
TreeFam; TF329572; -.
Reactome; R-HSA-6783310; Fanconi Anemia Pathway.
EvolutionaryTrace; Q9H816; -.
GeneWiki; DCLRE1B; -.
GenomeRNAi; 64858; -.
PRO; PR:Q9H816; -.
Proteomes; UP000005640; Chromosome 1.
Bgee; ENSG00000118655; -.
CleanEx; HS_DCLRE1B; -.
Genevisible; Q9H816; HS.
GO; GO:0005813; C:centrosome; IDA:UniProtKB.
GO; GO:0000781; C:chromosome, telomeric region; IDA:UniProtKB.
GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
GO; GO:0016604; C:nuclear body; IDA:HPA.
GO; GO:0000784; C:nuclear chromosome, telomeric region; IDA:BHF-UCL.
GO; GO:0005654; C:nucleoplasm; IDA:HPA.
GO; GO:0035312; F:5'-3' exodeoxyribonuclease activity; IBA:GO_Central.
GO; GO:0008409; F:5'-3' exonuclease activity; IDA:UniProtKB.
GO; GO:0003684; F:damaged DNA binding; IBA:GO_Central.
GO; GO:0044877; F:macromolecular complex binding; IPI:BHF-UCL.
GO; GO:0042803; F:protein homodimerization activity; IDA:BHF-UCL.
GO; GO:0000075; P:cell cycle checkpoint; IMP:UniProtKB.
GO; GO:0006303; P:double-strand break repair via nonhomologous end joining; IBA:GO_Central.
GO; GO:0036297; P:interstrand cross-link repair; IMP:BHF-UCL.
GO; GO:0031848; P:protection from non-homologous end joining at telomere; IMP:UniProtKB.
GO; GO:0016233; P:telomere capping; IMP:BHF-UCL.
GO; GO:0000723; P:telomere maintenance; IMP:UniProtKB.
GO; GO:0010833; P:telomere maintenance via telomere lengthening; IMP:BHF-UCL.
GO; GO:0031860; P:telomeric 3' overhang formation; ISS:UniProtKB.
GO; GO:0031627; P:telomeric loop formation; ISS:UniProtKB.
Gene3D; 3.60.15.10; -; 1.
InterPro; IPR011084; DRMBL.
InterPro; IPR036866; Metallo-hydrolase/OxRdtase.
Pfam; PF07522; DRMBL; 1.
SUPFAM; SSF56281; SSF56281; 1.
1: Evidence at protein level;
3D-structure; Chromosome; Complete proteome; Cytoplasm; Cytoskeleton;
DNA damage; DNA repair; Dyskeratosis congenita; Exonuclease;
Hydrolase; Isopeptide bond; Nuclease; Nucleus; Polymorphism;
Reference proteome; Telomere; Ubl conjugation.
CHAIN 1 532 5' exonuclease Apollo.
/FTId=PRO_0000209119.
MOTIF 496 511 TBM.
CROSSLNK 333 333 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:28112733}.
VARIANT 46 46 R -> L (in dbSNP:rs28381069).
{ECO:0000269|Ref.2}.
/FTId=VAR_023292.
VARIANT 61 61 H -> Y (in dbSNP:rs11552449).
{ECO:0000269|Ref.2}.
/FTId=VAR_023293.
VARIANT 462 462 D -> N (in dbSNP:rs28381079).
{ECO:0000269|Ref.2}.
/FTId=VAR_023294.
VARIANT 510 510 N -> Y (in dbSNP:rs35397235).
/FTId=VAR_048891.
MUTAGEN 14 14 D->N: In Apm3; abolishes exonuclease
activity and function on telomere
maintenance. Impairs interaction with
SPAG5. {ECO:0000269|PubMed:19197158,
ECO:0000269|PubMed:20655466}.
MUTAGEN 33 33 H->A: In Apm1; abolishes exonuclease
activity and function on telomere
maintenance; when associated with N-35.
{ECO:0000269|PubMed:20655466}.
MUTAGEN 35 35 D->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. {ECO:0000269|PubMed:20655466}.
MUTAGEN 276 276 H->A: Slightly affects interaction with
SPAG5. {ECO:0000269|PubMed:19197158}.
MUTAGEN 504 504 Y->A: Abolishes interaction with TERF2.
{ECO:0000269|PubMed:18202258}.
MUTAGEN 506 506 L->A: Abolishes interaction with TERF2.
{ECO:0000269|PubMed:18202258}.
MUTAGEN 508 508 P->A: Abolishes interaction with TERF2.
{ECO:0000269|PubMed:18202258}.
CONFLICT 237 237 I -> T (in Ref. 1; BAB14284).
{ECO:0000305}.
STRAND 4 6 {ECO:0000244|PDB:5AHO}.
TURN 7 10 {ECO:0000244|PDB:5AHO}.
STRAND 11 14 {ECO:0000244|PDB:5AHO}.
HELIX 18 21 {ECO:0000244|PDB:5AHO}.
STRAND 26 28 {ECO:0000244|PDB:5AHO}.
HELIX 34 36 {ECO:0000244|PDB:5AHO}.
STRAND 48 50 {ECO:0000244|PDB:5AHO}.
HELIX 52 61 {ECO:0000244|PDB:5AHO}.
TURN 66 68 {ECO:0000244|PDB:5AHO}.
STRAND 69 71 {ECO:0000244|PDB:5AHO}.
STRAND 76 86 {ECO:0000244|PDB:5AHO}.
STRAND 89 96 {ECO:0000244|PDB:5AHO}.
STRAND 98 100 {ECO:0000244|PDB:5AHO}.
STRAND 104 110 {ECO:0000244|PDB:5AHO}.
STRAND 113 117 {ECO:0000244|PDB:5AHO}.
HELIX 125 129 {ECO:0000244|PDB:5AHO}.
HELIX 131 133 {ECO:0000244|PDB:5AHO}.
STRAND 140 144 {ECO:0000244|PDB:5AHO}.
HELIX 158 170 {ECO:0000244|PDB:5AHO}.
STRAND 175 181 {ECO:0000244|PDB:5AHO}.
STRAND 183 185 {ECO:0000244|PDB:5AHO}.
HELIX 187 196 {ECO:0000244|PDB:5AHO}.
HELIX 205 214 {ECO:0000244|PDB:5AHO}.
STRAND 220 222 {ECO:0000244|PDB:5AHO}.
HELIX 224 226 {ECO:0000244|PDB:5AHO}.
STRAND 228 233 {ECO:0000244|PDB:5AHO}.
HELIX 234 236 {ECO:0000244|PDB:5AHO}.
HELIX 239 246 {ECO:0000244|PDB:5AHO}.
STRAND 251 256 {ECO:0000244|PDB:5AHO}.
STRAND 268 271 {ECO:0000244|PDB:5AHO}.
HELIX 279 289 {ECO:0000244|PDB:5AHO}.
STRAND 294 298 {ECO:0000244|PDB:5AHO}.
HELIX 307 309 {ECO:0000244|PDB:5AHO}.
HELIX 500 503 {ECO:0000244|PDB:3BUA}.
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


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