SubmitCancel

Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

Q8C7W7

- DCR1B_MOUSE

UniProt

Q8C7W7 - DCR1B_MOUSE

(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Protein
5' exonuclease Apollo
Gene
Dclre1b, Snm1b
Organism
Mus musculus (Mouse)
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.2 Publications

GO - Molecular functioni

  1. 5'-3' exonuclease activity Source: UniProtKB
  2. protein binding Source: UniProtKB

GO - Biological processi

  1. cell cycle checkpoint Source: UniProtKB
  2. nucleic acid phosphodiester bond hydrolysis Source: GOC
  3. nucleotide-excision repair Source: MGI
  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
Gene namesi
Name:Dclre1b
Synonyms:Snm1b
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Chromosome 3

Organism-specific databases

MGIiMGI:2156057. Dclre1b.

Subcellular locationi

Chromosometelomere. Nucleus By similarity. Cytoplasmcytoskeletonmicrotubule organizing centercentrosome By similarity
Note: Mainly localizes to telomeres, recruited via its interaction with TERF2. During mitosis, localizes to the centrosome.2 Publications

GO - Cellular componenti

  1. centrosome Source: UniProtKB
  2. chromosome, telomeric region Source: UniProtKB
  3. cytoplasm Source: UniProtKB-KW
  4. nucleus Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Chromosome, Cytoplasm, Cytoskeleton, Nucleus, Telomere

Pathology & Biotechi

Disruption phenotypei

Embryos are smaller than wild-type embryos and neonates die at postnatal day 0 (P0). Cells activate the ATM kinase at their telomeres in S phase and show leading-end telomere fusions which are accompanied by a reduction in the telomeric overhang signal.2 Publications

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi14 – 141D → A: Abolishes exonuclease activity without affecting the telomere localization, leading to impaired 3'-overhang at the leading end telomeres. 1 Publication
Mutagenesisi31 – 355HMHCD → AMACN: Abolishes exonuclease activity, leading to activate the ATM signaling pathway; when associated with A-230. 1 Publication
Mutagenesisi230 – 2301H → A: Abolishes exonuclease activity, leading to activate the ATM signaling pathway; when associated with 31-A--N-35. 1 Publication
Mutagenesisi500 – 5045Missing: Abolishes interaction with TERF2 and localization to telomeres, leading to activate the ATM signaling pathway. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 5415415' exonuclease Apollo
PRO_0000209120Add
BLAST

Post-translational modificationi

Ubiquitinated, leading to its degradation. Interaction with TERF2 protects it from ubiquitination By similarity.

Keywords - PTMi

Ubl conjugation

Proteomic databases

PRIDEiQ8C7W7.

Expressioni

Gene expression databases

ArrayExpressiQ8C7W7.
BgeeiQ8C7W7.
GenevestigatoriQ8C7W7.

Interactioni

Subunit structurei

Interacts with MUS81, MRE11 and FANCD2. Interacts with HSPA2, HSPA8 and HSPA14. Interacts with SPAG5 By similarity. Interacts with TERF2; the interaction is direct.1 Publication

Structurei

3D structure databases

ProteinModelPortaliQ8C7W7.
SMRiQ8C7W7. Positions 1-314.

Family & Domainsi

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi492 – 50716TBM
Add
BLAST

Domaini

The TBM domain mediates interaction with TERF2 By similarity.

Sequence similaritiesi

Phylogenomic databases

eggNOGiCOG1236.
GeneTreeiENSGT00530000063183.
HOVERGENiHBG081420.
InParanoidiB0V3P0.
KOiK15341.
OMAiPCQVVPI.
OrthoDBiEOG71VSSC.
PhylomeDBiQ8C7W7.
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.

Sequences (3)i

Sequence statusi: Complete.

This entry describes 3 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: Q8C7W7-1) [UniParc]FASTAAdd to Basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

MNGVVIPQTP IAVDFWSLRR AGSARLFFLT HMHCDHTVGL SSTWARPLYC    50
SPITACLLHR RLQVSKHWIR ALEVGESHVL PLDEIGQETM TVTLIDANHC 100
PGSVMFLFEG YFGTILYTGD FRYTPSMLKE PALILGKQIH TLYLDNTNCN 150
PALVLPSRQE ATQQIVQLIR QFPQHNIKIG LYSLGKESLL EQLALEFRTW 200
VVLSPQRLEL VQLLGLADVF TVEEEAGRIH AVDHTEICHS AMLQWNQSHP 250
TIAIFPTSRK VRSPHPSIYT VPYSDHSSYS ELRAFVAALR PCQVVPIVHQ 300
KPCGEFFQDS LSPRLAMPLI PHSVQQYMSS SSRKTNVLWQ LERRLKRPRT 350
QGVVFESPEE KANQVKVDRD SKKHKKENLS PWAGHLERLC PHPLQARKQL 400
FPDFCRKERD EPVLFCDSNK MATVLTAPLE FSVQLQPIDE FLFPETREKI 450
GLESPLLSRG DSGSPARGNQ SDCVGCGSPP AHISRAVPLT PESRGLALKY 500
LLTPVHFLQA GFSSRNFDKQ VEKHQRVQRS SPAVLSPVDV G 541
Length:541
Mass (Da):61,069
Last modified:August 16, 2005 - v2
Checksum:i884FB1A8E452A76C
GO
Isoform 2 (identifier: Q8C7W7-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-126: Missing.

Show »
Length:415
Mass (Da):46,864
Checksum:iD887FB35BE7747E3
GO
Isoform 3 (identifier: Q8C7W7-3) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     181-213: LYSLGKESLLEQLALEFRTWVVLSPQRLELVQL → ERFPFFFHSCLVNQNSLKVLIVFQIFVPCSPFL
     214-541: Missing.

Note: No experimental confirmation available.

Show »
Length:213
Mass (Da):24,254
Checksum:i56845E3156F33971
GO

Sequence cautioni

The sequence BAC39165.1 differs from that shown. Reason: Frameshift at position 55.
The sequence AAH11094.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.
The sequence BAE23379.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 126126Missing in isoform 2.
VSP_015174Add
BLAST
Alternative sequencei181 – 21333LYSLG…ELVQL → ERFPFFFHSCLVNQNSLKVL IVFQIFVPCSPFL in isoform 3.
VSP_015175Add
BLAST
Alternative sequencei214 – 541328Missing in isoform 3.
VSP_015176Add
BLAST

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti49 – 491Y → D in BAE23379. 1 Publication
Sequence conflicti162 – 1621T → S in BAC33550. 1 Publication
Sequence conflicti327 – 3271Y → H in AAI25278. 1 Publication
Sequence conflicti412 – 4121P → L in AAI25278. 1 Publication
Sequence conflicti540 – 5401V → D in BAE23700. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AK046571 mRNA. Translation: BAC32791.1.
AK049115 mRNA. Translation: BAC33550.1.
AK084347 mRNA. Translation: BAC39165.1. Frameshift.
AK134324 mRNA. Translation: BAE22098.1.
AK137495 mRNA. Translation: BAE23379.1. Different initiation.
AK138568 mRNA. Translation: BAE23700.1.
AK154124 mRNA. Translation: BAE32389.1.
CU210953 Genomic DNA. Translation: CAQ12168.1.
CU210953 Genomic DNA. Translation: CAQ12169.1.
BC011094 mRNA. Translation: AAH11094.1. Different initiation.
BC067017 mRNA. Translation: AAH67017.1.
BC125277 mRNA. Translation: AAI25278.1.
CCDSiCCDS17694.1. [Q8C7W7-1]
CCDS17695.1. [Q8C7W7-2]
RefSeqiNP_001020483.1. NM_001025312.1. [Q8C7W7-2]
NP_598626.2. NM_133865.2. [Q8C7W7-1]
UniGeneiMm.374850.

Genome annotation databases

EnsembliENSMUST00000029435; ENSMUSP00000029435; ENSMUSG00000027845. [Q8C7W7-1]
ENSMUST00000063502; ENSMUSP00000067695; ENSMUSG00000027845. [Q8C7W7-2]
ENSMUST00000106832; ENSMUSP00000102445; ENSMUSG00000027845. [Q8C7W7-3]
ENSMUST00000106834; ENSMUSP00000102447; ENSMUSG00000027845. [Q8C7W7-1]
GeneIDi140917.
KEGGimmu:140917.
UCSCiuc008qtl.1. mouse. [Q8C7W7-1]
uc008qto.1. mouse. [Q8C7W7-3]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AK046571 mRNA. Translation: BAC32791.1 .
AK049115 mRNA. Translation: BAC33550.1 .
AK084347 mRNA. Translation: BAC39165.1 . Frameshift.
AK134324 mRNA. Translation: BAE22098.1 .
AK137495 mRNA. Translation: BAE23379.1 . Different initiation.
AK138568 mRNA. Translation: BAE23700.1 .
AK154124 mRNA. Translation: BAE32389.1 .
CU210953 Genomic DNA. Translation: CAQ12168.1 .
CU210953 Genomic DNA. Translation: CAQ12169.1 .
BC011094 mRNA. Translation: AAH11094.1 . Different initiation.
BC067017 mRNA. Translation: AAH67017.1 .
BC125277 mRNA. Translation: AAI25278.1 .
CCDSi CCDS17694.1. [Q8C7W7-1 ]
CCDS17695.1. [Q8C7W7-2 ]
RefSeqi NP_001020483.1. NM_001025312.1. [Q8C7W7-2 ]
NP_598626.2. NM_133865.2. [Q8C7W7-1 ]
UniGenei Mm.374850.

3D structure databases

ProteinModelPortali Q8C7W7.
SMRi Q8C7W7. Positions 1-314.
ModBasei Search...
MobiDBi Search...

Proteomic databases

PRIDEi Q8C7W7.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSMUST00000029435 ; ENSMUSP00000029435 ; ENSMUSG00000027845 . [Q8C7W7-1 ]
ENSMUST00000063502 ; ENSMUSP00000067695 ; ENSMUSG00000027845 . [Q8C7W7-2 ]
ENSMUST00000106832 ; ENSMUSP00000102445 ; ENSMUSG00000027845 . [Q8C7W7-3 ]
ENSMUST00000106834 ; ENSMUSP00000102447 ; ENSMUSG00000027845 . [Q8C7W7-1 ]
GeneIDi 140917.
KEGGi mmu:140917.
UCSCi uc008qtl.1. mouse. [Q8C7W7-1 ]
uc008qto.1. mouse. [Q8C7W7-3 ]

Organism-specific databases

CTDi 64858.
MGIi MGI:2156057. Dclre1b.

Phylogenomic databases

eggNOGi COG1236.
GeneTreei ENSGT00530000063183.
HOVERGENi HBG081420.
InParanoidi B0V3P0.
KOi K15341.
OMAi PCQVVPI.
OrthoDBi EOG71VSSC.
PhylomeDBi Q8C7W7.
TreeFami TF329572.

Miscellaneous databases

NextBioi 370035.
PROi Q8C7W7.
SOURCEi Search...

Gene expression databases

ArrayExpressi Q8C7W7.
Bgeei Q8C7W7.
Genevestigatori Q8C7W7.

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. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 2 AND 3).
    Strain: C57BL/6J and NOD.
    Tissue: Adipose tissue, Bone, Eye, Spinal cord and Testis.
  2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: C57BL/6J.
  3. "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] (ISOFORM 2), NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 82-541 (ISOFORM 1).
    Strain: Czech II.
    Tissue: Brain and Mammary gland.
  4. "SNMIB/Apollo protects leading-strand telomeres against NHEJ-mediated repair."
    Lam Y.C., Akhter S., Gu P., Ye J., Poulet A., Giraud-Panis M.J., Bailey S.M., Gilson E., Legerski R.J., Chang S.
    EMBO J. 29:2230-2241(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION, DISRUPTION PHENOTYPE, MUTAGENESIS OF ASP-14.
  5. "Apollo contributes to G overhang maintenance and protects leading-end telomeres."
    Wu P., van Overbeek M., Rooney S., de Lange T.
    Mol. Cell 39:606-617(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH TERF2, DISRUPTION PHENOTYPE, MUTAGENESIS OF 31-HIS--ASP-35; HIS-230 AND 500-TYR--PRO-504.

Entry informationi

Entry nameiDCR1B_MOUSE
AccessioniPrimary (citable) accession number: Q8C7W7
Secondary accession number(s): A0JLW2
, B0V3N9, B0V3P0, Q3U4P2, Q3UUC7, Q3UV92, Q6NXL4, Q8BN95, Q8BQS8, Q921S0
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 16, 2005
Last sequence update: August 16, 2005
Last modified: July 9, 2014
This is version 83 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi