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Protein

Regulator of telomere elongation helicase 1

Gene

RTEL1

Organism
Homo sapiens (Human)
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 annotation3 Publications

Catalytic activityi

ATP + H2O = ADP + phosphate.UniRule annotation

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi145 – 1451Iron-sulfur (4Fe-4S)UniRule annotation
Metal bindingi163 – 1631Iron-sulfur (4Fe-4S)UniRule annotation
Metal bindingi172 – 1721Iron-sulfur (4Fe-4S)UniRule annotation
Metal bindingi207 – 2071Iron-sulfur (4Fe-4S)UniRule annotation

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi42 – 498ATPCurated

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
  • metal ion binding Source: UniProtKB-HAMAP

GO - Biological processi

  • DNA duplex unwinding Source: BHF-UCL
  • 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: BHF-UCL
  • positive regulation of telomere maintenance Source: BHF-UCL
  • positive regulation of telomere maintenance via telomere lengthening Source: BHF-UCL
  • 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
  • strand displacement Source: Reactome
  • telomere maintenance Source: UniProtKB
  • 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-HSA-2564830. Cytosolic iron-sulfur cluster assembly.
R-HSA-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)
Alternative name(s):
Novel helicase-like
Gene namesi
Name:RTEL1UniRule annotation
Synonyms:C20orf41, KIAA1088, NHL
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 20

Organism-specific databases

HGNCiHGNC:15888. RTEL1.

Subcellular locationi

  • Nucleus UniRule annotation

  • Note: Colocalizes with PCNA within the replication foci in S-phase cells.UniRule annotation

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Involvement in diseasei

Dyskeratosis congenita, autosomal recessive, 5 (DKCB5)5 Publications
The disease is caused by mutations affecting the gene represented in this entry. RTEL1 mutations have also been found in patients with a dyskeratosis congenita-like phenotype consisting of one feature of dyskeratosis congenita and short telomeres, in the absence of the typical DKC diagnostic triad (PubMed:23329068).1 Publication
Disease descriptionA form of dyskeratosis congenita, a rare multisystem disorder caused by defective telomere maintenance. It is characterized by progressive bone marrow failure, and the clinical triad of reticulated skin hyperpigmentation, nail dystrophy, and mucosal leukoplakia. Common but variable features include premature graying, aplastic anemia, low platelets, osteoporosis, pulmonary fibrosis, and liver fibrosis among others. Early mortality is often associated with bone marrow failure, infections, fatal pulmonary complications, or malignancy. DKCB5 is characterized by onset of bone marrow failure and immunodeficiency in early childhood. Most patients also have growth and developmental delay and cerebellar hypoplasia, consistent with a clinical diagnosis of Hoyeraal-Hreidarsson syndrome.
See also OMIM:615190
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti251 – 2511E → K in DKCB5; severe form consistent with Hoyeraal-Hreidarsson syndrome. 1 Publication
VAR_069714
Natural varianti492 – 4921M → I in DKCB5; severe form consistent with Hoyeraal-Hreidarsson syndrome. 2 Publications
VAR_069715
Natural varianti591 – 5911E → D in DKCB5; severe form consistent with Hoyeraal-Hreidarsson syndrome. 1 Publication
VAR_069716
Natural varianti699 – 6991I → M in DKCB5; severe form consistent with Hoyeraal-Hreidarsson syndrome. 1 Publication
VAR_069719
Natural varianti710 – 7101L → R in DKCB5; severe form consistent with Hoyeraal-Hreidarsson syndrome. 1 Publication
VAR_069720
Natural varianti739 – 7391G → V in DKCB5; severe form consistent with Hoyeraal-Hreidarsson syndrome. 1 Publication
VAR_069721
Natural varianti745 – 7451V → M in DKCB5; severe form consistent with Hoyeraal-Hreidarsson syndrome. 1 Publication
VAR_069722
Natural varianti897 – 8971K → E in DKCB5; severe form consistent with Hoyeraal-Hreidarsson syndrome. 1 Publication
VAR_069725
Natural varianti957 – 9571R → W in DKCB5; severe form consistent with Hoyeraal-Hreidarsson syndrome. 1 Publication
VAR_069727
Natural varianti964 – 9641F → L in DKCB5; severe form consistent with Hoyeraal-Hreidarsson syndrome. 1 Publication
VAR_069728
Isoform 5 (identifier: Q9NZ71-5)
Natural varianti489 – 4891C → R in DKCB5, severe form consistent with Hoyeraal-Hreidarsson syndrome.
Natural varianti509 – 5091R → H in DKCB5, abolishes activity.
Isoform 1 (identifier: Q9NZ71-2)
Natural varianti1244 – 12441C → R in DKCB5, severe form consistent with Hoyeraal-Hreidarsson syndrome. Curated
Isoform 6 (identifier: Q9NZ71-6)
Natural varianti1244 – 12441C → R in DKCB5, severe form consistent with Hoyeraal-Hreidarsson syndrome.
Natural varianti1264 – 12641R → H in DKCB5, abolishes activity.
Dyskeratosis congenita, autosomal dominant, 4 (DKCA4)1 Publication
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionA rare multisystem disorder caused by defective telomere maintenance. It is characterized by progressive bone marrow failure, and the clinical triad of reticulated skin hyperpigmentation, nail dystrophy, and mucosal leukoplakia. Common but variable features include premature graying, aplastic anemia, low platelets, osteoporosis, pulmonary fibrosis, and liver fibrosis among others. Early mortality is often associated with bone marrow failure, infections, fatal pulmonary complications, or malignancy.
See also OMIM:615190
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti621 – 6211A → T in DKCA4. 1 Publication
VAR_069717
Pulmonary fibrosis, and/or bone marrow failure, telomere-related, 3 (PFBMFT3)1 Publication
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionA disease associated with shortened telomeres. Pulmonary fibrosis is the most common manifestation. Other manifestations include aplastic anemia due to bone marrow failure, hepatic fibrosis, and increased cancer risk, particularly myelodysplastic syndrome and acute myeloid leukemia. Phenotype, age at onset, and severity are determined by telomere length.
See also OMIM:616373
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti484 – 4841P → L in PFBMFT3. 1 Publication
VAR_073795
Natural varianti647 – 6471P → L in PFBMFT3. 1 Publication
VAR_073796
Natural varianti1124 – 11241H → P in PFBMFT3. 1 Publication
VAR_073797

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi48 – 481K → R: Abolishes ATPase activity. 1 Publication

Keywords - Diseasei

Disease mutation, Dyskeratosis congenita

Organism-specific databases

MalaCardsiRTEL1.
MIMi615190. phenotype.
616373. phenotype.
Orphaneti1775. Dyskeratosis congenita.
3322. Hoyeraal-Hreidarsson syndrome.
PharmGKBiPA134915625.

Polymorphism and mutation databases

BioMutaiRTEL1.
DMDMi229462743.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 12191219Regulator of telomere elongation helicase 1PRO_0000101985Add
BLAST

Proteomic databases

EPDiQ9NZ71.
MaxQBiQ9NZ71.
PaxDbiQ9NZ71.
PRIDEiQ9NZ71.

PTM databases

iPTMnetiQ9NZ71.
PhosphoSiteiQ9NZ71.

Expressioni

Gene expression databases

BgeeiQ9NZ71.
ExpressionAtlasiQ9NZ71. baseline and differential.
GenevisibleiQ9NZ71. HS.

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 annotation2 Publications

Protein-protein interaction databases

BioGridi119711. 46 interactions.
IntActiQ9NZ71. 7 interactions.
STRINGi9606.ENSP00000359035.

Structurei

3D structure databases

ProteinModelPortaliQ9NZ71.
SMRiQ9NZ71. Positions 22-272.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini7 – 296290Helicase ATP-bindingUniRule annotationAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi151 – 16717Nuclear localization signalUniRule annotationAdd
BLAST
Motifi250 – 2534DEAH box
Motifi871 – 8777Nuclear localization signalUniRule annotation
Motifi1178 – 11858PIP-box

Domaini

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

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.
HOVERGENiHBG108423.
InParanoidiQ9NZ71.
KOiK11136.
OrthoDBiEOG7N8ZTR.
PhylomeDBiQ9NZ71.

Family and domain databases

Gene3Di3.40.50.300. 3 hits.
HAMAPiMF_03065. RTEL1.
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 (8)i

Sequence statusi: Complete.

This entry describes 8 isoformsi produced by alternative splicing. AlignAdd to basket

Note: Additional isoforms seem to exist.

Isoform 2 (identifier: Q9NZ71-1) [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
MPKIVLNGVT VDFPFQPYKC QQEYMTKVLE CLQQKVNGIL ESPTGTGKTL
60 70 80 90 100
CLLCTTLAWR EHLRDGISAR KIAERAQGEL FPDRALSSWG NAAAAAGDPI
110 120 130 140 150
ACYTDIPKII YASRTHSQLT QVINELRNTS YRPKVCVLGS REQLCIHPEV
160 170 180 190 200
KKQESNHLQI HLCRKKVASR SCHFYNNVEE KSLEQELASP ILDIEDLVKS
210 220 230 240 250
GSKHRVCPYY LSRNLKQQAD IIFMPYNYLL DAKSRRAHNI DLKGTVVIFD
260 270 280 290 300
EAHNVEKMCE ESASFDLTPH DLASGLDVID QVLEEQTKAA QQGEPHPEFS
310 320 330 340 350
ADSPSPGLNM ELEDIAKLKM ILLRLEGAID AVELPGDDSG VTKPGSYIFE
360 370 380 390 400
LFAEAQITFQ TKGCILDSLD QIIQHLAGRA GVFTNTAGLQ KLADIIQIVF
410 420 430 440 450
SVDPSEGSPG SPAGLGALQS YKVHIHPDAG HRRTAQRSDA WSTTAARKRG
460 470 480 490 500
KVLSYWCFSP GHSMHELVRQ GVRSLILTSG TLAPVSSFAL EMQIPFPVCL
510 520 530 540 550
ENPHIIDKHQ IWVGVVPRGP DGAQLSSAFD RRFSEECLSS LGKALGNIAR
560 570 580 590 600
VVPYGLLIFF PSYPVMEKSL EFWRARDLAR KMEALKPLFV EPRSKGSFSE
610 620 630 640 650
TISAYYARVA APGSTGATFL AVCRGKASEG LDFSDTNGRG VIVTGLPYPP
660 670 680 690 700
RMDPRVVLKM QFLDEMKGQG GAGGQFLSGQ EWYRQQASRA VNQAIGRVIR
710 720 730 740 750
HRQDYGAVFL CDHRFAFADA RAQLPSWVRP HVRVYDNFGH VIRDVAQFFR
760 770 780 790 800
VAERTMPAPA PRATAPSVRG EDAVSEAKSP GPFFSTRKAK SLDLHVPSLK
810 820 830 840 850
QRSSGSPAAG DPESSLCVEY EQEPVPARQR PRGLLAALEH SEQRAGSPGE
860 870 880 890 900
EQAHSCSTLS LLSEKRPAEE PRGGRKKIRL VSHPEEPVAG AQTDRAKLFM
910 920 930 940 950
VAVKQELSQA NFATFTQALQ DYKGSDDFAA LAACLGPLFA EDPKKHNLLQ
960 970 980 990 1000
GFYQFVRPHH KQQFEEVCIQ LTGRGCGYRP EHSIPRRQRA QPVLDPTGRT
1010 1020 1030 1040 1050
APDPKLTVST AAAQQLDPQE HLNQGRPHLS PRPPPTGDPG SQPQWGSGVP
1060 1070 1080 1090 1100
RAGKQGQHAV SAYLADARRA LGSAGCSQLL AALTAYKQDD DLDKVLAVLA
1110 1120 1130 1140 1150
ALTTAKPEDF PLLHRFSMFV RPHHKQRFSQ TCTDLTGRPY PGMEPPGPQE
1160 1170 1180 1190 1200
ERLAVPPVLT HRAPQPGPSR SEKTGKTQSK ISSFLRQRPA GTVGAGGEDA
1210
GPSQSSGPPH GPAASEWGL
Length:1,219
Mass (Da):133,683
Last modified:May 5, 2009 - v2
Checksum:i28DFCFCC48BC0055
GO
Isoform 1 (identifier: Q9NZ71-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1219-1219: L → EPHGRDIAGQ...PLLQRPLRGA

Note: Variant in position: 1264:R->H (in DKCB5), abolishes activity.Curated
Show »
Length:1,400
Mass (Da):152,374
Checksum:iF3F2BB93D48ED3D9
GO
Isoform 4 (identifier: Q9NZ71-4) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     999-1023: RTAPDPKLTVSTAAAQQLDPQEHLN → NFPDALDQLCGSTSLHQEERRRIPS
     1024-1219: Missing.

Note: No experimental confirmation available.
Show »
Length:1,023
Mass (Da):113,184
Checksum:i43650D4EC91B6DEA
GO
Isoform 5 (identifier: Q9NZ71-5) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-755: Missing.
     1219-1219: L → EPHGRDIAGQ...VMQVFWPEPQ

Note: No experimental confirmation available.
Show »
Length:545
Mass (Da):58,545
Checksum:iA08763FAE15AE678
GO
Isoform 6 (identifier: Q9NZ71-6) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1219-1219: L → EPHGRDIAGQ...VMQVFWPEPQ

Note: No experimental confirmation available.
Show »
Length:1,300
Mass (Da):142,367
Checksum:iE2A1CD6CC3211479
GO
Isoform 7 (identifier: Q9NZ71-7) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     131-131: Y → YRSRCRATLWVLETAPPRPTVLSPT

Note: No experimental confirmation available.
Show »
Length:1,243
Mass (Da):136,373
Checksum:i5AFDE395097DDC14
GO
Isoform 8 (identifier: Q9NZ71-8) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     998-1219: GRTAPDPKLT...HGPAASEWGL → ERRRIPS

Note: No experimental confirmation available.
Show »
Length:1,004
Mass (Da):111,170
Checksum:iD3F25736F4CD034A
GO
Isoform 9 (identifier: Q9NZ71-9) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-223: Missing.

Note: No experimental confirmation available.
Show »
Length:996
Mass (Da):108,457
Checksum:i6CD391EF1A61C675
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti41 – 411E → G in BAG63785 (PubMed:14702039).Curated
Sequence conflicti48 – 481K → R in BAG61337 (PubMed:14702039).Curated
Sequence conflicti845 – 8451A → V in BAG63785 (PubMed:14702039).Curated
Sequence conflicti986 – 9861R → Q in BAG61337 (PubMed:14702039).Curated
Isoform 1 (identifier: Q9NZ71-2)
Sequence conflicti1352 – 13521C → R in BAA83040 (PubMed:10470851).Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti124 – 1241N → S.1 Publication
Corresponds to variant rs3848668 [ dbSNP | Ensembl ].
VAR_054970
Natural varianti251 – 2511E → K in DKCB5; severe form consistent with Hoyeraal-Hreidarsson syndrome. 1 Publication
VAR_069714
Natural varianti484 – 4841P → L in PFBMFT3. 1 Publication
VAR_073795
Natural varianti492 – 4921M → I in DKCB5; severe form consistent with Hoyeraal-Hreidarsson syndrome. 2 Publications
VAR_069715
Natural varianti591 – 5911E → D in DKCB5; severe form consistent with Hoyeraal-Hreidarsson syndrome. 1 Publication
VAR_069716
Natural varianti621 – 6211A → T in DKCA4. 1 Publication
VAR_069717
Natural varianti647 – 6471P → L in PFBMFT3. 1 Publication
VAR_073796
Natural varianti684 – 6841R → Q.1 Publication
Corresponds to variant rs35640778 [ dbSNP | Ensembl ].
VAR_069718
Natural varianti699 – 6991I → M in DKCB5; severe form consistent with Hoyeraal-Hreidarsson syndrome. 1 Publication
VAR_069719
Natural varianti710 – 7101L → R in DKCB5; severe form consistent with Hoyeraal-Hreidarsson syndrome. 1 Publication
VAR_069720
Natural varianti739 – 7391G → V in DKCB5; severe form consistent with Hoyeraal-Hreidarsson syndrome. 1 Publication
VAR_069721
Natural varianti745 – 7451V → M in DKCB5; severe form consistent with Hoyeraal-Hreidarsson syndrome. 1 Publication
VAR_069722
Natural varianti829 – 8291Q → P.1 Publication
VAR_069723
Natural varianti849 – 8491G → D.1 Publication
Corresponds to variant rs190887884 [ dbSNP | Ensembl ].
VAR_069724
Natural varianti897 – 8971K → E in DKCB5; severe form consistent with Hoyeraal-Hreidarsson syndrome. 1 Publication
VAR_069725
Natural varianti929 – 9291A → T.2 Publications
Corresponds to variant rs61736615 [ dbSNP | Ensembl ].
VAR_069726
Natural varianti957 – 9571R → W in DKCB5; severe form consistent with Hoyeraal-Hreidarsson syndrome. 1 Publication
VAR_069727
Natural varianti964 – 9641F → L in DKCB5; severe form consistent with Hoyeraal-Hreidarsson syndrome. 1 Publication
VAR_069728
Natural varianti1034 – 10341P → H.1 Publication
Corresponds to variant rs115610405 [ dbSNP | Ensembl ].
VAR_069729
Natural varianti1042 – 10421Q → H.3 Publications
Corresponds to variant rs3208008 [ dbSNP | Ensembl ].
VAR_054971
Natural varianti1059 – 10591A → T.1 Publication
Corresponds to variant rs115303435 [ dbSNP | Ensembl ].
VAR_069730
Natural varianti1124 – 11241H → P in PFBMFT3. 1 Publication
VAR_073797
Isoform 5 (identifier: Q9NZ71-5)
Natural varianti489 – 4891C → R in DKCB5, severe form consistent with Hoyeraal-Hreidarsson syndrome.
Natural varianti509 – 5091R → H in DKCB5, abolishes activity.
Isoform 1 (identifier: Q9NZ71-2)
Natural varianti1244 – 12441C → R in DKCB5, severe form consistent with Hoyeraal-Hreidarsson syndrome. Curated
Isoform 6 (identifier: Q9NZ71-6)
Natural varianti1244 – 12441C → R in DKCB5, severe form consistent with Hoyeraal-Hreidarsson syndrome.
Natural varianti1264 – 12641R → H in DKCB5, abolishes activity.

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 755755Missing in isoform 5. 1 PublicationVSP_017093Add
BLAST
Alternative sequencei1 – 223223Missing in isoform 9. 1 PublicationVSP_036937Add
BLAST
Alternative sequencei131 – 1311Y → YRSRCRATLWVLETAPPRPT VLSPT in isoform 7. 1 PublicationVSP_036938
Alternative sequencei998 – 1219222GRTAP…SEWGL → ERRRIPS in isoform 8. 1 PublicationVSP_036939Add
BLAST
Alternative sequencei999 – 102325RTAPD…QEHLN → NFPDALDQLCGSTSLHQEER RRIPS in isoform 4. 1 PublicationVSP_007076Add
BLAST
Alternative sequencei1024 – 1219196Missing in isoform 4. 1 PublicationVSP_007077Add
BLAST
Alternative sequencei1219 – 12191L → EPHGRDIAGQQATGAPGGPL SAGCVCQGCGAEDVVPFQCP ACDFQRCQACWQRHLQASRM CPACHTASRKQSVMQVFWPE PHKDHEGAGGARPVAAVPGV GAACPAAGAGCTRSGRNTHL PLAGRRDRGAAGVCPVPPRH LCAAAVPPRQPHDVWPVSTA PLHAVLELPGALPLLQRPLR GA in isoform 1. 2 PublicationsVSP_036940
Alternative sequencei1219 – 12191L → EPHGRDIAGQQATGAPGGPL SAGCVCQGCGAEDVVPFQCP ACDFQRCQACWQRHLQASRM CPACHTASRKQSVMQVFWPE PQ in isoform 5 and isoform 6. 1 PublicationVSP_017094

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF217795 mRNA. Translation: AAF33687.1.
AF217796 Genomic DNA. Translation: AAF35243.1.
AB029011 mRNA. Translation: BAA83040.3.
AK000485 mRNA. Translation: BAA91197.1.
AK302508 mRNA. Translation: BAG63785.1.
AK299332 mRNA. Translation: BAG61337.1.
AK304798 mRNA. Translation: BAG65548.1.
AL353715 Genomic DNA. No translation available.
CH471077 Genomic DNA. Translation: EAW75238.1.
CH471077 Genomic DNA. Translation: EAW75239.1.
CH471077 Genomic DNA. Translation: EAW75240.1.
CH471077 Genomic DNA. Translation: EAW75241.1.
CH471077 Genomic DNA. Translation: EAW75245.1.
AL080127 mRNA. Translation: CAB45725.1.
CCDSiCCDS13530.3. [Q9NZ71-7]
CCDS13531.1. [Q9NZ71-1]
CCDS63331.1. [Q9NZ71-6]
CCDS74751.1. [Q9NZ71-9]
PIRiT12516.
T45294.
RefSeqiNP_001269938.1. NM_001283009.1. [Q9NZ71-6]
NP_001269939.1. NM_001283010.1. [Q9NZ71-9]
NP_057518.1. NM_016434.3. [Q9NZ71-1]
NP_116575.3. NM_032957.4. [Q9NZ71-7]
UniGeneiHs.745057.

Genome annotation databases

EnsembliENST00000318100; ENSP00000322287; ENSG00000258366. [Q9NZ71-9]
ENST00000360203; ENSP00000353332; ENSG00000258366. [Q9NZ71-6]
ENST00000370003; ENSP00000359020; ENSG00000258366. [Q9NZ71-5]
ENST00000370018; ENSP00000359035; ENSG00000258366. [Q9NZ71-1]
ENST00000508582; ENSP00000424307; ENSG00000258366. [Q9NZ71-7]
GeneIDi51750.
KEGGihsa:51750.
UCSCiuc002yfu.3. human. [Q9NZ71-1]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF217795 mRNA. Translation: AAF33687.1.
AF217796 Genomic DNA. Translation: AAF35243.1.
AB029011 mRNA. Translation: BAA83040.3.
AK000485 mRNA. Translation: BAA91197.1.
AK302508 mRNA. Translation: BAG63785.1.
AK299332 mRNA. Translation: BAG61337.1.
AK304798 mRNA. Translation: BAG65548.1.
AL353715 Genomic DNA. No translation available.
CH471077 Genomic DNA. Translation: EAW75238.1.
CH471077 Genomic DNA. Translation: EAW75239.1.
CH471077 Genomic DNA. Translation: EAW75240.1.
CH471077 Genomic DNA. Translation: EAW75241.1.
CH471077 Genomic DNA. Translation: EAW75245.1.
AL080127 mRNA. Translation: CAB45725.1.
CCDSiCCDS13530.3. [Q9NZ71-7]
CCDS13531.1. [Q9NZ71-1]
CCDS63331.1. [Q9NZ71-6]
CCDS74751.1. [Q9NZ71-9]
PIRiT12516.
T45294.
RefSeqiNP_001269938.1. NM_001283009.1. [Q9NZ71-6]
NP_001269939.1. NM_001283010.1. [Q9NZ71-9]
NP_057518.1. NM_016434.3. [Q9NZ71-1]
NP_116575.3. NM_032957.4. [Q9NZ71-7]
UniGeneiHs.745057.

3D structure databases

ProteinModelPortaliQ9NZ71.
SMRiQ9NZ71. Positions 22-272.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi119711. 46 interactions.
IntActiQ9NZ71. 7 interactions.
STRINGi9606.ENSP00000359035.

PTM databases

iPTMnetiQ9NZ71.
PhosphoSiteiQ9NZ71.

Polymorphism and mutation databases

BioMutaiRTEL1.
DMDMi229462743.

Proteomic databases

EPDiQ9NZ71.
MaxQBiQ9NZ71.
PaxDbiQ9NZ71.
PRIDEiQ9NZ71.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000318100; ENSP00000322287; ENSG00000258366. [Q9NZ71-9]
ENST00000360203; ENSP00000353332; ENSG00000258366. [Q9NZ71-6]
ENST00000370003; ENSP00000359020; ENSG00000258366. [Q9NZ71-5]
ENST00000370018; ENSP00000359035; ENSG00000258366. [Q9NZ71-1]
ENST00000508582; ENSP00000424307; ENSG00000258366. [Q9NZ71-7]
GeneIDi51750.
KEGGihsa:51750.
UCSCiuc002yfu.3. human. [Q9NZ71-1]

Organism-specific databases

CTDi51750.
GeneCardsiRTEL1.
HGNCiHGNC:15888. RTEL1.
MalaCardsiRTEL1.
MIMi608833. gene.
615190. phenotype.
616373. phenotype.
neXtProtiNX_Q9NZ71.
Orphaneti1775. Dyskeratosis congenita.
3322. Hoyeraal-Hreidarsson syndrome.
PharmGKBiPA134915625.
HUGEiSearch...
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG1132. Eukaryota.
COG1199. LUCA.
GeneTreeiENSGT00530000063199.
HOVERGENiHBG108423.
InParanoidiQ9NZ71.
KOiK11136.
OrthoDBiEOG7N8ZTR.
PhylomeDBiQ9NZ71.

Enzyme and pathway databases

ReactomeiR-HSA-2564830. Cytosolic iron-sulfur cluster assembly.
R-HSA-5693554. Resolution of D-loop Structures through Synthesis-Dependent Strand Annealing (SDSA).

Miscellaneous databases

ChiTaRSiRTEL1. human.
GenomeRNAii51750.
PROiQ9NZ71.
SOURCEiSearch...

Gene expression databases

BgeeiQ9NZ71.
ExpressionAtlasiQ9NZ71. baseline and differential.
GenevisibleiQ9NZ71. HS.

Family and domain databases

Gene3Di3.40.50.300. 3 hits.
HAMAPiMF_03065. RTEL1.
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...

Publicationsi

« Hide 'large scale' publications
  1. "Overexpression of M68/DcR3 in human gastrointestinal tract tumors independent of gene amplification and its location in a four-gene cluster."
    Bai C., Connolly B., Metzker M.L., Hilliard C.A., Liu X., Sandig V., Soderman A., Galloway S.M., Liu Q., Austin C.P., Caskey C.T.
    Proc. Natl. Acad. Sci. U.S.A. 97:1230-1235(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORMS 1 AND 2), AMPLIFICATION IN GASTRIC TUMORS.
  2. "Prediction of the coding sequences of unidentified human genes. XIV. The complete sequences of 100 new cDNA clones from brain which code for large proteins in vitro."
    Kikuno R., Nagase T., Ishikawa K., Hirosawa M., Miyajima N., Tanaka A., Kotani H., Nomura N., Ohara O.
    DNA Res. 6:197-205(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), VARIANT HIS-1042.
    Tissue: Brain.
  3. "Construction of expression-ready cDNA clones for KIAA genes: manual curation of 330 KIAA cDNA clones."
    Nakajima D., Okazaki N., Yamakawa H., Kikuno R., Ohara O., Nagase T.
    DNA Res. 9:99-106(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: SEQUENCE REVISION.
  4. Ohara O., Nagase T., Kikuno R.
    Submitted (FEB-2012) to the EMBL/GenBank/DDBJ databases
    Cited for: SEQUENCE REVISION TO 291-292.
  5. "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] (ISOFORMS 5; 7; 8 AND 9), VARIANTS THR-929 AND HIS-1042.
    Tissue: Colon carcinoma, Teratocarcinoma, Testis and Uterus.
  6. "The DNA sequence and comparative analysis of human chromosome 20."
    Deloukas P., Matthews L.H., Ashurst J.L., Burton J., Gilbert J.G.R., Jones M., Stavrides G., Almeida J.P., Babbage A.K., Bagguley C.L., Bailey J., Barlow K.F., Bates K.N., Beard L.M., Beare D.M., Beasley O.P., Bird C.P., Blakey S.E.
    , Bridgeman A.M., Brown A.J., Buck D., Burrill W.D., Butler A.P., Carder C., Carter N.P., Chapman J.C., Clamp M., Clark G., Clark L.N., Clark S.Y., Clee C.M., Clegg S., Cobley V.E., Collier R.E., Connor R.E., Corby N.R., Coulson A., Coville G.J., Deadman R., Dhami P.D., Dunn M., Ellington A.G., Frankland J.A., Fraser A., French L., Garner P., Grafham D.V., Griffiths C., Griffiths M.N.D., Gwilliam R., Hall R.E., Hammond S., Harley J.L., Heath P.D., Ho S., Holden J.L., Howden P.J., Huckle E., Hunt A.R., Hunt S.E., Jekosch K., Johnson C.M., Johnson D., Kay M.P., Kimberley A.M., King A., Knights A., Laird G.K., Lawlor S., Lehvaeslaiho M.H., Leversha M.A., Lloyd C., Lloyd D.M., Lovell J.D., Marsh V.L., Martin S.L., McConnachie L.J., McLay K., McMurray A.A., Milne S.A., Mistry D., Moore M.J.F., Mullikin J.C., Nickerson T., Oliver K., Parker A., Patel R., Pearce T.A.V., Peck A.I., Phillimore B.J.C.T., Prathalingam S.R., Plumb R.W., Ramsay H., Rice C.M., Ross M.T., Scott C.E., Sehra H.K., Shownkeen R., Sims S., Skuce C.D., Smith M.L., Soderlund C., Steward C.A., Sulston J.E., Swann R.M., Sycamore N., Taylor R., Tee L., Thomas D.W., Thorpe A., Tracey A., Tromans A.C., Vaudin M., Wall M., Wallis J.M., Whitehead S.L., Whittaker P., Willey D.L., Williams L., Williams S.A., Wilming L., Wray P.W., Hubbard T., Durbin R.M., Bentley D.R., Beck S., Rogers J.
    Nature 414:865-871(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], ALTERNATIVE SPLICING (ISOFORMS 2; 5 AND 6).
  7. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  8. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 708-1219 (ISOFORM 4).
    Tissue: Testis.
  9. Cited for: FUNCTION, MUTAGENESIS OF LYS-48.
  10. "MMS19 links cytoplasmic iron-sulfur cluster assembly to DNA metabolism."
    Gari K., Leon Ortiz A.M., Borel V., Flynn H., Skehel J.M., Boulton S.J.
    Science 337:243-245(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH MMS19.
  11. "Constitutional mutations in RTEL1 cause severe dyskeratosis congenita."
    Walne A.J., Vulliamy T., Kirwan M., Plagnol V., Dokal I.
    Am. J. Hum. Genet. 92:448-453(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, VARIANTS DKCB5 LYS-251; ILE-492; ARG-710; VAL-739; GLU-897; TRP-957 AND LEU-964, VARIANT DKCB5 HIS-509 (ISOFORM 5), VARIANT DKCB5 HIS-1264 (ISOFORMS 1 AND 6).
  12. Cited for: INTERACTION WITH TERF1, VARIANT DKCB5 ILE-492.
  13. Cited for: INVOLVEMENT IN PFBMFT3, VARIANTS PFBMFT3 LEU-484; LEU-647 AND PRO-1124.
  14. "Germline mutations of regulator of telomere elongation helicase 1, RTEL1, in dyskeratosis congenita."
    Ballew B.J., Yeager M., Jacobs K., Giri N., Boland J., Burdett L., Alter B.P., Savage S.A.
    Hum. Genet. 132:473-480(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANT DKCB5 ASP-591, VARIANT DKCA4 THR-621, VARIANTS SER-124; GLN-684; PRO-829; ASP-849; THR-929; HIS-1034; HIS-1042 AND THR-1059.
  15. Cited for: VARIANTS DKCB5 MET-699 AND MET-745, VARIANT DKCB5 ARG-489 (ISOFORM 5), VARIANT DKCB5 ARG-1244 (ISOFORMS 1 AND 6).
  16. "A recessive founder mutation in regulator of telomere elongation helicase 1, RTEL1, underlies severe immunodeficiency and features of Hoyeraal Hreidarsson syndrome."
    Ballew B.J., Joseph V., De S., Sarek G., Vannier J.B., Stracker T., Schrader K.A., Small T.N., O'Reilly R., Manschreck C., Harlan Fleischut M.M., Zhang L., Sullivan J., Stratton K., Yeager M., Jacobs K., Giri N., Alter B.P.
    , Boland J., Burdett L., Offit K., Boulton S.J., Savage S.A., Petrini J.H.
    PLoS Genet. 9:E1003695-E1003695(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANTS DKCB5 HIS-509 (ISOFORM 5) AND HIS-1264 (ISOFORMS 1 AND 6), FUNCTION, CHARACTERIZATION OF VARIANTS DKCB5 HIS-509 (ISOFORM 5) AND HIS-1264 (ISOFORMS 1 AND 6).

Entry informationi

Entry nameiRTEL1_HUMAN
AccessioniPrimary (citable) accession number: Q9NZ71
Secondary accession number(s): A2A397
, A2A398, B4DRM5, B4DYM3, B4E3N6, E1P5J4, E1P5J5, Q5JTV3, Q5JTV4, Q9BW37, Q9H402, Q9H4X6, Q9NX25, Q9NZ73, Q9UPR4, Q9Y4R6
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 28, 2003
Last sequence update: May 5, 2009
Last modified: June 8, 2016
This is version 140 of the entry and version 2 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

Amplified in gastric tumors.

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Human chromosome 20
    Human chromosome 20: 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. 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.