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Protein

5' exonuclease Apollo

Gene

DCLRE1B

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: 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

GO - Biological processi

  • cell cycle checkpoint Source: UniProtKB
  • double-strand break repair via nonhomologous end joining Source: GO_Central
  • interstrand cross-link repair Source: GO_Central
  • protection from non-homologous end joining at telomere Source: UniProtKB
  • telomere maintenance Source: UniProtKB
  • telomeric 3' overhang formation Source: UniProtKB
  • telomeric loop formation Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Exonuclease, Hydrolase, Nuclease

Keywords - Biological processi

DNA damage, DNA repair

Enzyme and pathway databases

BioCyciZFISH:ENSG00000118655-MONOMER.
ReactomeiR-HSA-6783310. Fanconi Anemia Pathway.

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
Proteomesi
  • UP000005640 Componenti: Chromosome 1

Organism-specific databases

HGNCiHGNC:17641. DCLRE1B.

Subcellular locationi

GO - Cellular componenti

  • centrosome Source: UniProtKB
  • chromosome, telomeric region Source: UniProtKB
  • cytoplasm Source: UniProtKB-KW
  • nuclear chromosome, telomeric region Source: BHF-UCL
Complete GO annotation...

Keywords - Cellular componenti

Chromosome, Cytoplasm, Cytoskeleton, Nucleus, Telomere

Pathology & Biotechi

Involvement in diseasei

Hoyeraal-Hreidarsson syndrome (HHS)1 Publication
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
Disease descriptionA 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.
See also OMIM:305000

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi14D → N in Apm3; abolishes exonuclease activity and function on telomere maintenance. Impairs interaction with SPAG5. 2 Publications1
Mutagenesisi33H → A in Apm1; abolishes exonuclease activity and function on telomere maintenance; when associated with N-35. 1 Publication1
Mutagenesisi35D → 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 Publication1
Mutagenesisi276H → A: Slightly affects interaction with SPAG5. 1 Publication1
Mutagenesisi504Y → A: Abolishes interaction with TERF2. 1 Publication1
Mutagenesisi506L → A: Abolishes interaction with TERF2. 1 Publication1
Mutagenesisi508P → A: Abolishes interaction with TERF2. 1 Publication1

Keywords - Diseasei

Dyskeratosis congenita

Organism-specific databases

DisGeNETi64858.
MIMi305000. phenotype.
OpenTargetsiENSG00000118655.
PharmGKBiPA27175.

Polymorphism and mutation databases

BioMutaiDCLRE1B.
DMDMi73620756.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00002091191 – 5325' exonuclease ApolloAdd BLAST532

Post-translational modificationi

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

Keywords - PTMi

Ubl conjugation

Proteomic databases

EPDiQ9H816.
PaxDbiQ9H816.
PeptideAtlasiQ9H816.
PRIDEiQ9H816.

PTM databases

iPTMnetiQ9H816.
PhosphoSitePlusiQ9H816.

Expressioni

Gene expression databases

BgeeiENSG00000118655.
CleanExiHS_DCLRE1B.
GenevisibleiQ9H816. HS.

Organism-specific databases

HPAiHPA064934.

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
TERF2Q155547EBI-3508943,EBI-706637

Protein-protein interaction databases

BioGridi122331. 16 interactors.
DIPiDIP-42669N.
IntActiQ9H816. 14 interactors.
MINTiMINT-3372972.
STRINGi9606.ENSP00000358576.

Structurei

Secondary structure

1532
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi4 – 6Combined sources3
Turni7 – 10Combined sources4
Beta strandi11 – 14Combined sources4
Helixi18 – 21Combined sources4
Beta strandi26 – 28Combined sources3
Helixi34 – 36Combined sources3
Beta strandi48 – 50Combined sources3
Helixi52 – 61Combined sources10
Turni66 – 68Combined sources3
Beta strandi69 – 71Combined sources3
Beta strandi76 – 86Combined sources11
Beta strandi89 – 96Combined sources8
Beta strandi98 – 100Combined sources3
Beta strandi104 – 110Combined sources7
Beta strandi113 – 117Combined sources5
Helixi125 – 129Combined sources5
Helixi131 – 133Combined sources3
Beta strandi140 – 144Combined sources5
Helixi158 – 170Combined sources13
Beta strandi175 – 181Combined sources7
Beta strandi183 – 185Combined sources3
Helixi187 – 196Combined sources10
Helixi205 – 214Combined sources10
Beta strandi220 – 222Combined sources3
Helixi224 – 226Combined sources3
Beta strandi228 – 233Combined sources6
Helixi234 – 236Combined sources3
Helixi239 – 246Combined sources8
Beta strandi251 – 256Combined sources6
Beta strandi268 – 271Combined sources4
Helixi279 – 289Combined sources11
Beta strandi294 – 298Combined sources5
Helixi307 – 309Combined sources3
Helixi500 – 503Combined sources4

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
3BUAX-ray2.50E/F/G/H495-530[»]
5AHOX-ray2.16A1-335[»]
ProteinModelPortaliQ9H816.
SMRiQ9H816.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ9H816.

Family & Domainsi

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Motifi496 – 511TBMAdd BLAST16

Domaini

The TBM domain mediates interaction with TERF2.

Sequence similaritiesi

Phylogenomic databases

eggNOGiKOG1361. Eukaryota.
COG1236. LUCA.
GeneTreeiENSGT00530000063183.
HOGENOMiHOG000043118.
HOVERGENiHBG081420.
KOiK15341.
OMAiPCQVVPI.
OrthoDBiEOG091G0DBZ.
PhylomeDBiQ9H816.
TreeFamiTF329572.

Family and domain databases

Gene3Di3.60.15.10. 1 hit.
InterProiIPR011084. DRMBL.
IPR001279. Metallo-B-lactamas.
[Graphical view]
PfamiPF07522. DRMBL. 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 differs from that shown. Reason: Erroneous initiation.Curated

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti237I → T in BAB14284 (PubMed:14702039).Curated1

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_02329246R → L.1 PublicationCorresponds to variant rs28381069dbSNPEnsembl.1
Natural variantiVAR_02329361H → Y.1 PublicationCorresponds to variant rs11552449dbSNPEnsembl.1
Natural variantiVAR_023294462D → N.1 PublicationCorresponds to variant rs28381079dbSNPEnsembl.1
Natural variantiVAR_048891510N → Y.Corresponds to variant rs35397235dbSNPEnsembl.1

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_001306876.1. NM_001319947.1.
NP_073747.1. NM_022836.3.
UniGeneiHs.591412.
Hs.628365.

Genome annotation databases

EnsembliENST00000369563; ENSP00000358576; ENSG00000118655.
GeneIDi64858.
KEGGihsa:64858.
UCSCiuc001eeg.4. human.

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.
CCDSiCCDS866.1.
RefSeqiNP_001306876.1. NM_001319947.1.
NP_073747.1. NM_022836.3.
UniGeneiHs.591412.
Hs.628365.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
3BUAX-ray2.50E/F/G/H495-530[»]
5AHOX-ray2.16A1-335[»]
ProteinModelPortaliQ9H816.
SMRiQ9H816.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi122331. 16 interactors.
DIPiDIP-42669N.
IntActiQ9H816. 14 interactors.
MINTiMINT-3372972.
STRINGi9606.ENSP00000358576.

PTM databases

iPTMnetiQ9H816.
PhosphoSitePlusiQ9H816.

Polymorphism and mutation databases

BioMutaiDCLRE1B.
DMDMi73620756.

Proteomic databases

EPDiQ9H816.
PaxDbiQ9H816.
PeptideAtlasiQ9H816.
PRIDEiQ9H816.

Protocols and materials databases

DNASUi64858.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000369563; ENSP00000358576; ENSG00000118655.
GeneIDi64858.
KEGGihsa:64858.
UCSCiuc001eeg.4. human.

Organism-specific databases

CTDi64858.
DisGeNETi64858.
GeneCardsiDCLRE1B.
HGNCiHGNC:17641. DCLRE1B.
HPAiHPA064934.
MIMi305000. phenotype.
609683. gene.
neXtProtiNX_Q9H816.
OpenTargetsiENSG00000118655.
PharmGKBiPA27175.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG1361. Eukaryota.
COG1236. LUCA.
GeneTreeiENSGT00530000063183.
HOGENOMiHOG000043118.
HOVERGENiHBG081420.
KOiK15341.
OMAiPCQVVPI.
OrthoDBiEOG091G0DBZ.
PhylomeDBiQ9H816.
TreeFamiTF329572.

Enzyme and pathway databases

BioCyciZFISH:ENSG00000118655-MONOMER.
ReactomeiR-HSA-6783310. Fanconi Anemia Pathway.

Miscellaneous databases

EvolutionaryTraceiQ9H816.
GeneWikiiDCLRE1B.
GenomeRNAii64858.
PROiQ9H816.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000118655.
CleanExiHS_DCLRE1B.
GenevisibleiQ9H816. HS.

Family and domain databases

Gene3Di3.60.15.10. 1 hit.
InterProiIPR011084. DRMBL.
IPR001279. Metallo-B-lactamas.
[Graphical view]
PfamiPF07522. DRMBL. 1 hit.
[Graphical view]
SUPFAMiSSF56281. SSF56281. 1 hit.
ProtoNetiSearch...

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 2, 2016
This is version 128 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.