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Protein

Regulator of telomere elongation helicase 1

Gene

Rtel1

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

ATP-dependent DNA helicase implicated in telomere-length regulation, DNA repair and the maintenance of genomic stability. Acts as an anti-recombinase to counteract toxic recombination and limit crossover during meiosis. Regulates meiotic recombination and crossover homeostasis by physically dissociating strand invasion events and thereby promotes noncrossover repair by meiotic synthesis dependent strand annealing (SDSA) as well as disassembly of D loop recombination intermediates. Also disassembles T loops and prevents telomere fragility by counteracting telomeric G4-DNA structures, which together ensure the dynamics and stability of the telomere.UniRule annotation4 Publications

Catalytic activityi

ATP + H2O = ADP + phosphate.UniRule annotation

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Metal bindingi145Iron-sulfur (4Fe-4S)UniRule annotation1
Metal bindingi163Iron-sulfur (4Fe-4S)UniRule annotation1
Metal bindingi172Iron-sulfur (4Fe-4S)UniRule annotation1
Metal bindingi207Iron-sulfur (4Fe-4S)UniRule annotation1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi42 – 49ATPUniRule annotation8

GO - Molecular functioni

  • 4 iron, 4 sulfur cluster binding Source: UniProtKB-HAMAP
  • ATP binding Source: UniProtKB
  • ATP-dependent DNA helicase activity Source: UniProtKB
  • DNA binding Source: UniProtKB-HAMAP
  • DNA polymerase binding Source: BHF-UCL
  • helicase activity Source: BHF-UCL
  • metal ion binding Source: UniProtKB-HAMAP

GO - Biological processi

  • DNA duplex unwinding Source: BHF-UCL
  • DNA recombination Source: InterPro
  • DNA repair Source: UniProtKB-HAMAP
  • mitotic telomere maintenance via semi-conservative replication Source: BHF-UCL
  • negative regulation of t-circle formation Source: BHF-UCL
  • negative regulation of telomere maintenance in response to DNA damage Source: BHF-UCL
  • positive regulation of telomere capping Source: MGI
  • positive regulation of telomere maintenance Source: BHF-UCL
  • positive regulation of telomere maintenance via telomere lengthening Source: MGI
  • positive regulation of telomeric loop disassembly Source: BHF-UCL
  • regulation of double-strand break repair via homologous recombination Source: UniProtKB
  • replication fork processing Source: BHF-UCL
  • telomere maintenance Source: MGI
  • telomere maintenance in response to DNA damage Source: BHF-UCL
  • telomeric loop disassembly Source: BHF-UCL
Complete GO annotation...

Keywords - Molecular functioni

Helicase, Hydrolase

Keywords - Biological processi

DNA damage, DNA repair

Keywords - Ligandi

4Fe-4S, ATP-binding, DNA-binding, Iron, Iron-sulfur, Metal-binding, Nucleotide-binding

Enzyme and pathway databases

ReactomeiR-MMU-5693554. Resolution of D-loop Structures through Synthesis-Dependent Strand Annealing (SDSA).

Names & Taxonomyi

Protein namesi
Recommended name:
Regulator of telomere elongation helicase 1UniRule annotation (EC:3.6.4.12UniRule annotation)
Gene namesi
Name:Rtel1
Synonyms:Kiaa1088, Rtel
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 2

Organism-specific databases

MGIiMGI:2139369. Rtel1.

Subcellular locationi

GO - Cellular componenti

  • nucleus Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Disruption phenotypei

Death between days 10 and 11.5 of gestation with defects in the nervous system, heart, vasculature and extraembryonic tissues. Effects are due to severe genome instability and stochastic telomere loss in embryonic stem cells which display many chromosome breaks and fusions upon differentiation in vitro.2 Publications

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi48K → R: Abolishes G4-DNA unwinding activity. 1 Publication1
Mutagenesisi1160Q → A: Abolishes interaction with PCNA. 1 Publication1
Mutagenesisi1163I → A: Abolishes interaction with PCNA. 1 Publication1
Mutagenesisi1166F → A: Abolishes interaction with PCNA. 1 Publication1
Mutagenesisi1167F → A: Abolishes interaction with PCNA. 1 Publication1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00003706101 – 1203Regulator of telomere elongation helicase 1Add BLAST1203

Proteomic databases

MaxQBiQ0VGM9.
PaxDbiQ0VGM9.
PRIDEiQ0VGM9.

PTM databases

iPTMnetiQ0VGM9.
PhosphoSitePlusiQ0VGM9.

Expressioni

Tissue specificityi

Widely expressed. Expressed in spleen, thymus, Peyer patches, kidney, and intestine. Not expressed in brain, heart, lung, skeletal muscles, skin and white fat. In the adult gonad, it is highly expressed in the testis, mainly in the spermatogonia and meiotic spermatocytes.1 Publication

Developmental stagei

Widely expressed in E8.5 and E9.5 embryos with a more restricted expression pattern at E13.5-E15.5. In general, expression in embryos coincides with areas of actively proliferating cells.

Gene expression databases

BgeeiENSMUSG00000038685.
ExpressionAtlasiQ0VGM9. baseline and differential.
GenevisibleiQ0VGM9. MM.

Interactioni

Subunit structurei

Interacts with TERF1. Interacts (via PIP-box) with PCNA; the interaction is direct and essential for suppressing telomere fragility. Interacts with MMS19; the interaction mediates the association of RTEL1 with the cytosolic iron-sulfur protein assembly (CIA) complex.UniRule annotation1 Publication

GO - Molecular functioni

  • DNA polymerase binding Source: BHF-UCL

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000053120.

Structurei

3D structure databases

ProteinModelPortaliQ0VGM9.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini7 – 296Helicase ATP-bindingUniRule annotationAdd BLAST290

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Motifi151 – 167Nuclear localization signalUniRule annotationAdd BLAST17
Motifi250 – 253DEAH box4
Motifi871 – 877Nuclear localization signalUniRule annotation7
Motifi1160 – 1167PIP-box8

Domaini

The PIP-box (PCNA interacting peptide) motif mediates the interaction with PCNA and localization to replication foci.UniRule annotation1 Publication

Sequence similaritiesi

Belongs to the helicase family. RAD3/XPD subfamily.UniRule annotation
Contains 1 helicase ATP-binding domain.UniRule annotation

Phylogenomic databases

eggNOGiKOG1132. Eukaryota.
COG1199. LUCA.
GeneTreeiENSGT00530000063199.
InParanoidiQ0VGM9.
KOiK11136.
OMAiFALEMQI.
OrthoDBiEOG091G035L.
TreeFamiTF317291.

Family and domain databases

Gene3Di3.40.50.300. 3 hits.
HAMAPiMF_03065. RTEL1. 1 hit.
InterProiIPR006555. ATP-dep_Helicase_C.
IPR010614. DEAD_2.
IPR013020. DNA_helicase_DNA-repair_Rad3.
IPR014013. Helic_SF1/SF2_ATP-bd_DinG/Rad3.
IPR006554. Helicase-like_DEXD_c2.
IPR027417. P-loop_NTPase.
IPR030845. RTEL1.
[Graphical view]
PfamiPF06733. DEAD_2. 1 hit.
PF13307. Helicase_C_2. 1 hit.
[Graphical view]
SMARTiSM00488. DEXDc2. 1 hit.
SM00491. HELICc2. 1 hit.
[Graphical view]
SUPFAMiSSF52540. SSF52540. 8 hits.
TIGRFAMsiTIGR00604. rad3. 1 hit.
PROSITEiPS51193. HELICASE_ATP_BIND_2. 1 hit.
[Graphical view]

Sequences (6)i

Sequence statusi: Complete.

This entry describes 6 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q0VGM9-1) [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

        10         20         30         40         50
MPRVVLNGVT VDFPFQPYPC QQEYMTKVLE CLQKKVNGIL ESPTGTGKTL
60 70 80 90 100
CLLCSTLAWQ QHLRDAVSSL KIAERVQGEL FASRTLSSWG SAAAASGDSI
110 120 130 140 150
ECYTDIPKII YASRTHSQLT QVIRELRNTA YRPKVCVLGS REQLCIHPEV
160 170 180 190 200
KKQESNHMQI SLCRKKVASR SCHFYNNVEA KFLEQDLATP ILDIEDLVKN
210 220 230 240 250
GSKQKMCPYY LSRNMKQQAD IIFMPYNYLL DAKSRKAHSI DLKGTVVIFD
260 270 280 290 300
EAHNVEKICE ESASFDLTPR DVASGLEIIN QVLEEQARVT QQGELQQEFI
310 320 330 340 350
VDTSSSGLNM ELEDIAKLKM ILLRLEEAID AVQLPGDDRG VTKPGSYIFE
360 370 380 390 400
LFAEAQITFQ TKGCILESLD QIIQHLAGRT GVFTNTAGLQ KLMDIIQIVF
410 420 430 440 450
SVDPPEGSPG SLVGLGISHS YKVHIHPETS HRRAAKRSDA WSTTASRKQG
460 470 480 490 500
KVLSYWCFSP SQSMRELVCQ GVRTLILTSG TLAPLSSFAL EMQIPFPVCL
510 520 530 540 550
ENPHIIDKNQ LWVGIVPRGP DGVQLSSAYD KRFSEECLSS LGKALSNIAR
560 570 580 590 600
VVPHGLLVFF PSYPVMEKSL EFWQVQGLAR KVEALKPLFV EPRNKGSFSE
610 620 630 640 650
VIDAYYQQVA SPASNGATFL AVCRGKASEG LDFSDMNGRG VIVTGLPYPP
660 670 680 690 700
RMDPRVVLKM QFLDEMRGRS GVGGQCLSGQ EWYQQQASRA VNQAIGRVIR
710 720 730 740 750
HRHDYGAIFL CDHRFAYADA RAQLPSWVRP YLKVYDNFGH VIRDVAQFFR
760 770 780 790 800
VAQKTMPLPV PQAVTSSVSE GEIALKDATL SSYSLSTRKA MSLDVHVPSL
810 820 830 840 850
RQKPIGLPAA GDSESSLCGE YEQQTFSAQQ RPMGLLAALE YNEQKAGASE
860 870 880 890 900
EQALGSSTPS LRCEKRLSTE QKGGRKKVRL VNHPEEPMAG TQAGRAKMFM
910 920 930 940 950
VAVKQALSQA NFDTFTQALQ HYKSSDDFEA LVASLTCLFA EDPKKHTLLK
960 970 980 990 1000
GFYQFVRPHH KQQFEDICFQ LTGQRCGYQP GKRELESKLT LSEGVDRQLD
1010 1020 1030 1040 1050
PGQHLNQGQP HLSAHPTSKG HTSHCTKVGC AVEKPGQPAV SDYLSDVHKA
1060 1070 1080 1090 1100
LGSASCNQLT AALRAYKQDD DLDKVVAVVA ALTTAKPEHL PLLQRFGMFV
1110 1120 1130 1140 1150
RRHHKPQFLQ TCADLMGLPT TGKDLELEGP RDESPTVPPE LTHEDLKPGP
1160 1170 1180 1190 1200
SMSKKPEKTQ SKISSFFRQR PDESVRSDDT TPKPMQLPPR LPHELMKPHR

SKQ
Length:1,203
Mass (Da):133,767
Last modified:May 5, 2009 - v2
Checksum:i670573FEF1E2D1B1
GO
Isoform 2 (identifier: Q0VGM9-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1019-1019: K → KAHFSKP

Show »
Length:1,209
Mass (Da):134,435
Checksum:iC32760C3E6338652
GO
Isoform 3 (identifier: Q0VGM9-3) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     981-1019: GKRELESKLTLSEGVDRQLDPGQHLNQGQPHLSAHPTSK → AHFSKP

Show »
Length:1,170
Mass (Da):130,163
Checksum:iE7F3C92BE6DB121D
GO
Isoform 4 (identifier: Q0VGM9-4) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1021-1095: Missing.

Show »
Length:1,128
Mass (Da):125,832
Checksum:i54033FCBB9727478
GO
Isoform 5 (identifier: Q0VGM9-5) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     981-1019: Missing.

Show »
Length:1,164
Mass (Da):129,495
Checksum:i934A4C88FEB9BCA3
GO
Isoform 6 (identifier: Q0VGM9-6) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     451-527: KVLSYWCFSP...RGPDGVQLSS → TNLHCRKLYL...HYYYYFVFSR
     528-1203: Missing.

Note: No experimental confirmation available.
Show »
Length:527
Mass (Da):59,317
Checksum:iC258999E8C8B6E81
GO

Sequence cautioni

The sequence BAD32375 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.Curated
The sequence CAM26418 differs from that shown. Reason: Erroneous gene model prediction.Curated

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti180A → T in AAI05579 (PubMed:19468303).Curated1
Sequence conflicti381G → R in AAR27234 (PubMed:15210109).Curated1
Sequence conflicti381G → R in AAR27235 (PubMed:15210109).Curated1
Sequence conflicti381G → R in AAR27236 (PubMed:15210109).Curated1
Sequence conflicti381G → R in AAR27237 (PubMed:15210109).Curated1
Sequence conflicti381G → R in AAR27238 (PubMed:15210109).Curated1
Sequence conflicti383F → S in AAI05579 (PubMed:19468303).Curated1
Sequence conflicti402V → A in AAI05579 (PubMed:19468303).Curated1
Sequence conflicti416G → S in AAR27234 (PubMed:15210109).Curated1
Sequence conflicti416G → S in AAR27235 (PubMed:15210109).Curated1
Sequence conflicti416G → S in AAR27236 (PubMed:15210109).Curated1
Sequence conflicti416G → S in AAR27237 (PubMed:15210109).Curated1
Sequence conflicti416G → S in AAR27238 (PubMed:15210109).Curated1
Sequence conflicti619F → L in AAI05579 (PubMed:19468303).Curated1
Sequence conflicti633F → S in AAI05579 (PubMed:19468303).Curated1
Sequence conflicti796H → R in AAI05579 (PubMed:19468303).Curated1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_036945451 – 527KVLSY…VQLSS → TNLHCRKLYLAQPLHNNNIT SGVMPTESQRQEALLSTQRH LLGQWQNPGSARPPLPDLGY IIINHYRHYYYYFVFSR in isoform 6. 1 PublicationAdd BLAST77
Alternative sequenceiVSP_036946528 – 1203Missing in isoform 6. 1 PublicationAdd BLAST676
Alternative sequenceiVSP_036947981 – 1019GKREL…HPTSK → AHFSKP in isoform 3. 1 PublicationAdd BLAST39
Alternative sequenceiVSP_036948981 – 1019Missing in isoform 5. 1 PublicationAdd BLAST39
Alternative sequenceiVSP_0369491019K → KAHFSKP in isoform 2. 2 Publications1
Alternative sequenceiVSP_0369501021 – 1095Missing in isoform 4. 1 PublicationAdd BLAST75

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY481619 mRNA. Translation: AAR27234.1.
AY481620 mRNA. Translation: AAR27235.1.
AY481621 mRNA. Translation: AAR27236.1.
AY481622 mRNA. Translation: AAR27237.1.
AY481623 mRNA. Translation: AAR27238.1.
AK173097 mRNA. Translation: BAD32375.1. Different initiation.
AK145145 mRNA. Translation: BAE26258.1.
AL928965 Genomic DNA. Translation: CAM26413.1.
AL928965 Genomic DNA. Translation: CAM26414.1.
AL928965 Genomic DNA. Translation: CAM26415.1.
AL928965 Genomic DNA. Translation: CAM26416.1.
AL928965 Genomic DNA. Translation: CAM26417.1.
AL928965 Genomic DNA. Translation: CAM26418.1. Sequence problems.
BC105578 mRNA. Translation: AAI05579.1.
BC144977 mRNA. Translation: AAI44978.1.
BC144978 mRNA. Translation: AAI44979.1.
BC145658 mRNA. Translation: AAI45659.1.
CCDSiCCDS17208.1. [Q0VGM9-2]
CCDS50849.1. [Q0VGM9-1]
CCDS50850.1. [Q0VGM9-4]
CCDS50851.1. [Q0VGM9-3]
CCDS50852.1. [Q0VGM9-5]
RefSeqiNP_001001882.3. NM_001001882.3. [Q0VGM9-2]
NP_001160137.1. NM_001166665.1. [Q0VGM9-1]
NP_001160138.1. NM_001166666.1. [Q0VGM9-3]
NP_001160139.1. NM_001166667.1. [Q0VGM9-5]
NP_001160140.1. NM_001166668.1. [Q0VGM9-4]
UniGeneiMm.11333.

Genome annotation databases

EnsembliENSMUST00000048608; ENSMUSP00000043563; ENSMUSG00000038685. [Q0VGM9-4]
ENSMUST00000054622; ENSMUSP00000053120; ENSMUSG00000038685. [Q0VGM9-2]
ENSMUST00000098971; ENSMUSP00000096571; ENSMUSG00000038685. [Q0VGM9-3]
ENSMUST00000108814; ENSMUSP00000104442; ENSMUSG00000038685. [Q0VGM9-1]
ENSMUST00000108815; ENSMUSP00000104443; ENSMUSG00000038685. [Q0VGM9-5]
GeneIDi269400.
KEGGimmu:269400.
UCSCiuc008olu.2. mouse. [Q0VGM9-6]
uc008olv.2. mouse. [Q0VGM9-2]
uc008olw.2. mouse. [Q0VGM9-1]
uc008olx.2. mouse. [Q0VGM9-3]
uc012cmk.1. mouse. [Q0VGM9-5]
uc012cml.1. mouse. [Q0VGM9-4]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY481619 mRNA. Translation: AAR27234.1.
AY481620 mRNA. Translation: AAR27235.1.
AY481621 mRNA. Translation: AAR27236.1.
AY481622 mRNA. Translation: AAR27237.1.
AY481623 mRNA. Translation: AAR27238.1.
AK173097 mRNA. Translation: BAD32375.1. Different initiation.
AK145145 mRNA. Translation: BAE26258.1.
AL928965 Genomic DNA. Translation: CAM26413.1.
AL928965 Genomic DNA. Translation: CAM26414.1.
AL928965 Genomic DNA. Translation: CAM26415.1.
AL928965 Genomic DNA. Translation: CAM26416.1.
AL928965 Genomic DNA. Translation: CAM26417.1.
AL928965 Genomic DNA. Translation: CAM26418.1. Sequence problems.
BC105578 mRNA. Translation: AAI05579.1.
BC144977 mRNA. Translation: AAI44978.1.
BC144978 mRNA. Translation: AAI44979.1.
BC145658 mRNA. Translation: AAI45659.1.
CCDSiCCDS17208.1. [Q0VGM9-2]
CCDS50849.1. [Q0VGM9-1]
CCDS50850.1. [Q0VGM9-4]
CCDS50851.1. [Q0VGM9-3]
CCDS50852.1. [Q0VGM9-5]
RefSeqiNP_001001882.3. NM_001001882.3. [Q0VGM9-2]
NP_001160137.1. NM_001166665.1. [Q0VGM9-1]
NP_001160138.1. NM_001166666.1. [Q0VGM9-3]
NP_001160139.1. NM_001166667.1. [Q0VGM9-5]
NP_001160140.1. NM_001166668.1. [Q0VGM9-4]
UniGeneiMm.11333.

3D structure databases

ProteinModelPortaliQ0VGM9.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000053120.

PTM databases

iPTMnetiQ0VGM9.
PhosphoSitePlusiQ0VGM9.

Proteomic databases

MaxQBiQ0VGM9.
PaxDbiQ0VGM9.
PRIDEiQ0VGM9.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000048608; ENSMUSP00000043563; ENSMUSG00000038685. [Q0VGM9-4]
ENSMUST00000054622; ENSMUSP00000053120; ENSMUSG00000038685. [Q0VGM9-2]
ENSMUST00000098971; ENSMUSP00000096571; ENSMUSG00000038685. [Q0VGM9-3]
ENSMUST00000108814; ENSMUSP00000104442; ENSMUSG00000038685. [Q0VGM9-1]
ENSMUST00000108815; ENSMUSP00000104443; ENSMUSG00000038685. [Q0VGM9-5]
GeneIDi269400.
KEGGimmu:269400.
UCSCiuc008olu.2. mouse. [Q0VGM9-6]
uc008olv.2. mouse. [Q0VGM9-2]
uc008olw.2. mouse. [Q0VGM9-1]
uc008olx.2. mouse. [Q0VGM9-3]
uc012cmk.1. mouse. [Q0VGM9-5]
uc012cml.1. mouse. [Q0VGM9-4]

Organism-specific databases

CTDi51750.
MGIiMGI:2139369. Rtel1.
RougeiSearch...

Phylogenomic databases

eggNOGiKOG1132. Eukaryota.
COG1199. LUCA.
GeneTreeiENSGT00530000063199.
InParanoidiQ0VGM9.
KOiK11136.
OMAiFALEMQI.
OrthoDBiEOG091G035L.
TreeFamiTF317291.

Enzyme and pathway databases

ReactomeiR-MMU-5693554. Resolution of D-loop Structures through Synthesis-Dependent Strand Annealing (SDSA).

Miscellaneous databases

ChiTaRSiRtel1. mouse.
PROiQ0VGM9.
SOURCEiSearch...

Gene expression databases

BgeeiENSMUSG00000038685.
ExpressionAtlasiQ0VGM9. baseline and differential.
GenevisibleiQ0VGM9. MM.

Family and domain databases

Gene3Di3.40.50.300. 3 hits.
HAMAPiMF_03065. RTEL1. 1 hit.
InterProiIPR006555. ATP-dep_Helicase_C.
IPR010614. DEAD_2.
IPR013020. DNA_helicase_DNA-repair_Rad3.
IPR014013. Helic_SF1/SF2_ATP-bd_DinG/Rad3.
IPR006554. Helicase-like_DEXD_c2.
IPR027417. P-loop_NTPase.
IPR030845. RTEL1.
[Graphical view]
PfamiPF06733. DEAD_2. 1 hit.
PF13307. Helicase_C_2. 1 hit.
[Graphical view]
SMARTiSM00488. DEXDc2. 1 hit.
SM00491. HELICc2. 1 hit.
[Graphical view]
SUPFAMiSSF52540. SSF52540. 8 hits.
TIGRFAMsiTIGR00604. rad3. 1 hit.
PROSITEiPS51193. HELICASE_ATP_BIND_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiRTEL1_MOUSE
AccessioniPrimary (citable) accession number: Q0VGM9
Secondary accession number(s): A2AU09
, A2AU10, A2AU11, A2AU12, A2AU13, A2AU14, Q3UM40, Q5F0J8, Q69ZS1, Q6H1L0, Q6H1L1, Q6H1L2, Q6H1L3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 5, 2009
Last sequence update: May 5, 2009
Last modified: November 2, 2016
This is version 91 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Miscellaneous

Able to elongate M.spretus telomeres in crosses between M.musculus and M.spretus.

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

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.