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Q9H816

- DCR1B_HUMAN

UniProt

Q9H816 - DCR1B_HUMAN

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Protein

5' exonuclease Apollo

Gene

DCLRE1B

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

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

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
Complete GO annotation...

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-KW
Complete GO annotation...

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. 7 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 – 146Combined sources
Helixi18 – 214Combined sources
Beta strandi26 – 283Combined sources
Helixi34 – 363Combined sources
Beta strandi48 – 503Combined sources
Helixi52 – 6211Combined sources
Turni66 – 683Combined sources
Beta strandi69 – 713Combined sources
Beta strandi76 – 8712Combined sources
Beta strandi89 – 968Combined sources
Beta strandi98 – 1003Combined sources
Beta strandi104 – 1107Combined sources
Beta strandi113 – 1175Combined sources
Helixi125 – 1295Combined sources
Helixi131 – 1333Combined sources
Beta strandi140 – 1445Combined sources
Helixi158 – 17013Combined sources
Beta strandi175 – 1817Combined sources
Beta strandi183 – 1853Combined sources
Helixi187 – 19711Combined sources
Helixi205 – 2139Combined sources
Beta strandi220 – 2223Combined sources
Helixi224 – 2263Combined sources
Beta strandi228 – 2336Combined sources
Helixi234 – 2363Combined sources
Helixi239 – 24810Combined sources
Beta strandi251 – 2566Combined sources
Beta strandi268 – 2714Combined sources
Helixi279 – 28911Combined sources
Beta strandi294 – 2974Combined sources
Helixi307 – 3093Combined sources
Helixi500 – 5034Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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.
GeneTreeiENSGT00530000063183.
HOGENOMiHOG000043118.
HOVERGENiHBG081420.
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

        10         20         30         40         50
MNGVLIPHTP IAVDFWSLRR AGTARLFFLS HMHSDHTVGL SSTWARPLYC
60 70 80 90 100
SPITAHLLHR HLQVSKQWIQ ALEVGESHVL PLDEIGQETM TVTLLDANHC
110 120 130 140 150
PGSVMFLFEG YFGTILYTGD FRYTPSMLKE PALTLGKQIH TLYLDNTNCN
160 170 180 190 200
PALVLPSRQE AAHQIVQLIR KHPQHNIKIG LYSLGKESLL EQLALEFQTW
210 220 230 240 250
VVLSPRRLEL VQLLGLADVF TVEEKAGRIH AVDHMEICHS NMLRWNQTHP
260 270 280 290 300
TIAILPTSRK IHSSHPDIHV IPYSDHSSYS ELRAFVAALK PCQVVPIVSR
310 320 330 340 350
RPCGGFQDSL SPRISVPLIP DSVQQYMSSS SRKPSLLWLL ERRLKRPRTQ
360 370 380 390 400
GVVFESPEES ADQSQADRDS KKAKKEKLSP WPADLEKQPS HHPLRIKKQL
410 420 430 440 450
FPDLYSKEWN KAVPFCESQK RVTMLTAPLG FSVHLRSTDE EFISQKTREE
460 470 480 490 500
IGLGSPLVPM GDDDGGPEAT GNQSAWMGHG SPLSHSSKGT PLLATEFRGL
510 520 530
ALKYLLTPVN FFQAGYSSRR FDQQVEKYHK PC
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. Curated

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:
EMBLi
GenBanki
DDBJi
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:
EMBLi
GenBanki
DDBJi
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:
PDBei
RCSB PDBi
PDBji
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. 7 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.
GeneTreei ENSGT00530000063183.
HOGENOMi HOG000043118.
HOVERGENi HBG081420.
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

« Hide 'large scale' publications
  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: November 26, 2014
This is version 110 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