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Q9H816

- DCR1B_HUMAN

UniProt

Q9H816 - DCR1B_HUMAN

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Protein
5' exonuclease Apollo
Gene
DCLRE1B, SNM1B
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
  2. protein binding Source: UniProtKB

GO - Biological processi

  1. DNA repair Source: UniProtKB-KW
  2. cell cycle checkpoint Source: UniProtKB
  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.7 Publications

GO - Cellular componenti

  1. centrosome Source: UniProtKB
  2. chromosome, telomeric region Source: UniProtKB
  3. cytoplasm Source: UniProtKB-KW
  4. nucleus Source: UniProtKB-SubCell
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.
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 (1 Publication). 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 Apollo
PRO_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 SPAG5.9 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

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.

Miscellaneous databases

EvolutionaryTraceiQ9H816.

Family & Domainsi

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi496 – 51116TBM
Add
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.

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 conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti237 – 2371I → T in BAB14284. 1 Publication

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

« 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: July 9, 2014
This is version 107 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 (1 Publication and 1 Publication). 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

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