Human Gene RTEL1 (ENST00000508582.6) Description and Page Index

Description: Homo sapiens regulator of telomere elongation helicase 1 (RTEL1), transcript variant 2, mRNA. (from RefSeq NM_032957)
Gencode Transcript: ENST00000508582.6
Gencode Gene: ENSG00000258366.9
Transcript (Including UTRs)
Position: hg38 chr20:63,658,291-63,695,980 Size: 37,690 Total Exon Count: 35 Strand: +
Coding Region
Position: hg38 chr20:63,659,403-63,695,785 Size: 36,383 Coding Exon Count: 34

Page Index

Sequence and Links

UniProtKB Comments

Protein Structure

Other Names

Methods

Data last updated at UCSC: 2021-06-20 19:51:40

Comments and Description Text from UniProtKB


	ID: RTEL1_HUMAN DESCRIPTION: RecName: Full=Regulator of telomere elongation helicase 1; EC=3.6.4.12; AltName: Full=Novel helicase-like; FUNCTION: ATP-dependent DNA helicase required to suppress inappropriate homologous recombination, thereby playing a central role DNA repair and in the maintenance of genomic stability. Antagonizes homologous recombination by promoting the disassembly of D loop recombination intermediates. Also required to regulate telomere length; probably due to its anti-recombinase function. CATALYTIC ACTIVITY: ATP + H(2)O = ADP + phosphate. SUBCELLULAR LOCATION: Nucleus (By similarity). MISCELLANEOUS: Amplified in gastric tumors. SIMILARITY: Belongs to the helicase family. RAD3/XPD subfamily. SIMILARITY: Contains 1 helicase ATP-binding domain. SEQUENCE CAUTION: Sequence=CAI17958.1; Type=Erroneous gene model prediction; Sequence=CAM25345.1; Type=Erroneous gene model prediction;

Protein Domain and Structure Information

InterPro Domains: Graphical view of domain structure
IPR006555 - 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

Pfam Domains:
PF06733 - DEAD_2
PF13307 - Helicase C-terminal domain

ModBase Predicted Comparative 3D Structure on Q9NZ71


Front	Top	Side

The pictures above may be empty if there is no ModBase structure for the protein. The ModBase structure frequently covers just a fragment of the protein. You may be asked to log onto ModBase the first time you click on the pictures. It is simplest after logging in to just click on the picture again to get to the specific info on that model.