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Protein

Ribonuclease H1

Gene

RNASEH1

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Endonuclease that specifically degrades the RNA of RNA-DNA hybrids (PubMed:10497183). Plays a role in RNA polymerase II (RNAp II) transcription termination by degrading R-loop RNA-DNA hybrid formation at G-rich pause sites located downstream of the poly(A) site and behind the elongating RNAp II (PubMed:21700224).2 Publications

Catalytic activityi

Endonucleolytic cleavage to 5'-phosphomonoester.PROSITE-ProRule annotation

Cofactori

Mg2+Note: Binds 1 Mg2+ ion per subunit. May bind a second metal ion at a regulatory site, or after substrate binding.

Enzyme regulationi

In the presence of magnesium, manganese is inhibitory.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Metal bindingi145Magnesium 1PROSITE-ProRule annotation1
Metal bindingi145Magnesium 2PROSITE-ProRule annotation1
Metal bindingi186Magnesium 1PROSITE-ProRule annotation1
Metal bindingi210Magnesium 1PROSITE-ProRule annotation1
Metal bindingi274Magnesium 2PROSITE-ProRule annotation1

GO - Molecular functioni

  • magnesium ion binding Source: InterPro
  • nucleic acid binding Source: ProtInc
  • ribonuclease activity Source: ProtInc
  • RNA binding Source: ProtInc
  • RNA-DNA hybrid ribonuclease activity Source: UniProtKB

GO - Biological processi

  • DNA replication, removal of RNA primer Source: GO_Central
  • RNA catabolic process Source: ProtInc
Complete GO annotation...

Keywords - Molecular functioni

Endonuclease, Hydrolase, Nuclease

Keywords - Ligandi

Magnesium, Metal-binding

Enzyme and pathway databases

BioCyciZFISH:HS10407-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
Ribonuclease H1 (EC:3.1.26.4)
Short name:
RNase H1
Alternative name(s):
Ribonuclease H type II
Gene namesi
Name:RNASEH1
Synonyms:RNH1
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 2

Organism-specific databases

HGNCiHGNC:18466. RNASEH1.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Involvement in diseasei

Progressive external ophthalmoplegia with mitochondrial DNA deletions, autosomal recessive 2 (PEOB2)1 Publication
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionA form of progressive external ophthalmoplegia, a mitochondrial myopathy characterized by progressive paralysis of the levator palpebrae, orbicularis oculi, and extraocular muscles. PEOB2 patients manifest exercise intolerance, muscle weakness, and signs and symptoms of spinocerebellar ataxia, such as impaired gait and dysarthria. Some patients may have respiratory insufficiency.
See also OMIM:616479
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_074561142V → I in PEOB2; has partial residual endonuclase activity. 1 PublicationCorresponds to variant rs766294940dbSNPEnsembl.1
Natural variantiVAR_074562185A → V in PEOB2; has partial residual endonuclase activity. 1 Publication1

Keywords - Diseasei

Disease mutation, Progressive external ophthalmoplegia

Organism-specific databases

DisGeNETi246243.
MIMi616479. phenotype.
OpenTargetsiENSG00000171865.
PharmGKBiPA38543.

Chemistry databases

ChEMBLiCHEMBL5893.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001954331 – 286Ribonuclease H1Add BLAST286

Proteomic databases

EPDiO60930.
MaxQBiO60930.
PaxDbiO60930.
PeptideAtlasiO60930.
PRIDEiO60930.

PTM databases

iPTMnetiO60930.
PhosphoSitePlusiO60930.

Expressioni

Tissue specificityi

Ubiquitous.

Gene expression databases

BgeeiENSG00000171865.
CleanExiHS_RNASEH1.
HS_RNH1.
ExpressionAtlasiO60930. baseline and differential.
GenevisibleiO60930. HS.

Organism-specific databases

HPAiHPA043037.

Interactioni

Subunit structurei

Monomer.Curated

Protein-protein interaction databases

BioGridi128882. 10 interactors.
IntActiO60930. 4 interactors.
STRINGi9606.ENSP00000313350.

Chemistry databases

BindingDBiO60930.

Structurei

Secondary structure

1286
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi28 – 36Combined sources9
Beta strandi38 – 42Combined sources5
Helixi43 – 50Combined sources8
Beta strandi57 – 63Combined sources7
Helixi64 – 72Combined sources9
Beta strandi139 – 149Combined sources11
Turni150 – 152Combined sources3
Beta strandi153 – 155Combined sources3
Beta strandi157 – 163Combined sources7
Beta strandi172 – 175Combined sources4
Helixi182 – 199Combined sources18
Beta strandi204 – 210Combined sources7
Helixi212 – 219Combined sources8
Helixi221 – 226Combined sources6
Turni227 – 229Combined sources3
Beta strandi235 – 237Combined sources3
Helixi241 – 251Combined sources11
Beta strandi255 – 260Combined sources6
Beta strandi263 – 265Combined sources3
Helixi268 – 281Combined sources14

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2QK9X-ray2.55A136-286[»]
2QKBX-ray2.40A/B136-286[»]
2QKKX-ray3.20A/B/E/F/I/J/M/N/R/S/W136-286[»]
3BSUX-ray2.10A/B/C/F/G/H27-76[»]
ProteinModelPortaliO60930.
SMRiO60930.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiO60930.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini136 – 282RNase HPROSITE-ProRule annotationAdd BLAST147

Sequence similaritiesi

Belongs to the RNase H family.Curated
Contains 1 RNase H domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiKOG3752. Eukaryota.
COG0328. LUCA.
GeneTreeiENSGT00390000003466.
HOGENOMiHOG000040465.
HOVERGENiHBG002135.
InParanoidiO60930.
KOiK03469.
OMAiECKSQVD.
OrthoDBiEOG091G0RCI.
PhylomeDBiO60930.
TreeFamiTF313356.

Family and domain databases

Gene3Di3.30.420.10. 1 hit.
3.40.970.10. 1 hit.
InterProiIPR009027. Ribosomal_L9/RNase_H1_N.
IPR017067. RNase_H1_euk.
IPR011320. RNase_H1_N.
IPR012337. RNaseH-like_dom.
IPR002156. RNaseH_domain.
[Graphical view]
PfamiPF01693. Cauli_VI. 1 hit.
PF00075. RNase_H. 1 hit.
[Graphical view]
PIRSFiPIRSF036852. Ribonuclease_H1_euk. 1 hit.
SUPFAMiSSF53098. SSF53098. 1 hit.
SSF55658. SSF55658. 1 hit.
PROSITEiPS50879. RNASE_H. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

O60930-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSWLLFLAHR VALAALPCRR GSRGFGMFYA VRRGRKTGVF LTWNECRAQV
60 70 80 90 100
DRFPAARFKK FATEDEAWAF VRKSASPEVS EGHENQHGQE SEAKASKRLR
110 120 130 140 150
EPLDGDGHES AEPYAKHMKP SVEPAPPVSR DTFSYMGDFV VVYTDGCCSS
160 170 180 190 200
NGRRRPRAGI GVYWGPGHPL NVGIRLPGRQ TNQRAEIHAA CKAIEQAKTQ
210 220 230 240 250
NINKLVLYTD SMFTINGITN WVQGWKKNGW KTSAGKEVIN KEDFVALERL
260 270 280
TQGMDIQWMH VPGHSGFIGN EEADRLAREG AKQSED
Length:286
Mass (Da):32,064
Last modified:April 27, 2001 - v2
Checksum:i400FE04E7E85CA6A
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti24G → R in AAV38476 (Ref. 5) Curated1
Sequence conflicti33R → K in CAG46619 (Ref. 4) Curated1
Sequence conflicti68W → R in AAV38476 (Ref. 5) Curated1
Sequence conflicti89Q → R in CAA11835 (PubMed:9894807).Curated1
Sequence conflicti136M → I in CAG46619 (Ref. 4) Curated1
Sequence conflicti223Q → R in CAA11835 (PubMed:9894807).Curated1

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_0234694L → F.2 PublicationsCorresponds to variant rs1136545dbSNPEnsembl.1
Natural variantiVAR_074561142V → I in PEOB2; has partial residual endonuclase activity. 1 PublicationCorresponds to variant rs766294940dbSNPEnsembl.1
Natural variantiVAR_074562185A → V in PEOB2; has partial residual endonuclase activity. 1 Publication1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF048995 mRNA. Translation: AAC78564.1.
AF048994 mRNA. Translation: AAC78563.1.
AF039652 mRNA. Translation: AAC09261.1.
AJ224117 mRNA. Translation: CAA11835.1.
CR541820 mRNA. Translation: CAG46619.1.
BT019670 mRNA. Translation: AAV38476.1.
AK075490 mRNA. Translation: BAG52156.1.
AC108488 Genomic DNA. Translation: AAX82026.1.
CH471053 Genomic DNA. Translation: EAX01061.1.
BC002973 mRNA. Translation: AAH02973.1.
CCDSiCCDS1647.1.
RefSeqiNP_001273763.1. NM_001286834.1.
NP_001273766.1. NM_001286837.1.
NP_002927.2. NM_002936.4.
UniGeneiHs.568006.

Genome annotation databases

EnsembliENST00000315212; ENSP00000313350; ENSG00000171865.
GeneIDi246243.
KEGGihsa:246243.
UCSCiuc002qxt.5. human.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Web resourcesi

Wikipedia

RNase H entry

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF048995 mRNA. Translation: AAC78564.1.
AF048994 mRNA. Translation: AAC78563.1.
AF039652 mRNA. Translation: AAC09261.1.
AJ224117 mRNA. Translation: CAA11835.1.
CR541820 mRNA. Translation: CAG46619.1.
BT019670 mRNA. Translation: AAV38476.1.
AK075490 mRNA. Translation: BAG52156.1.
AC108488 Genomic DNA. Translation: AAX82026.1.
CH471053 Genomic DNA. Translation: EAX01061.1.
BC002973 mRNA. Translation: AAH02973.1.
CCDSiCCDS1647.1.
RefSeqiNP_001273763.1. NM_001286834.1.
NP_001273766.1. NM_001286837.1.
NP_002927.2. NM_002936.4.
UniGeneiHs.568006.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2QK9X-ray2.55A136-286[»]
2QKBX-ray2.40A/B136-286[»]
2QKKX-ray3.20A/B/E/F/I/J/M/N/R/S/W136-286[»]
3BSUX-ray2.10A/B/C/F/G/H27-76[»]
ProteinModelPortaliO60930.
SMRiO60930.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi128882. 10 interactors.
IntActiO60930. 4 interactors.
STRINGi9606.ENSP00000313350.

Chemistry databases

BindingDBiO60930.
ChEMBLiCHEMBL5893.

PTM databases

iPTMnetiO60930.
PhosphoSitePlusiO60930.

Proteomic databases

EPDiO60930.
MaxQBiO60930.
PaxDbiO60930.
PeptideAtlasiO60930.
PRIDEiO60930.

Protocols and materials databases

DNASUi246243.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000315212; ENSP00000313350; ENSG00000171865.
GeneIDi246243.
KEGGihsa:246243.
UCSCiuc002qxt.5. human.

Organism-specific databases

CTDi246243.
DisGeNETi246243.
GeneCardsiRNASEH1.
H-InvDBHIX0039191.
HGNCiHGNC:18466. RNASEH1.
HPAiHPA043037.
MIMi604123. gene.
616479. phenotype.
neXtProtiNX_O60930.
OpenTargetsiENSG00000171865.
PharmGKBiPA38543.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG3752. Eukaryota.
COG0328. LUCA.
GeneTreeiENSGT00390000003466.
HOGENOMiHOG000040465.
HOVERGENiHBG002135.
InParanoidiO60930.
KOiK03469.
OMAiECKSQVD.
OrthoDBiEOG091G0RCI.
PhylomeDBiO60930.
TreeFamiTF313356.

Enzyme and pathway databases

BioCyciZFISH:HS10407-MONOMER.

Miscellaneous databases

EvolutionaryTraceiO60930.
GeneWikiiRNASEH1.
GenomeRNAii246243.
PROiO60930.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000171865.
CleanExiHS_RNASEH1.
HS_RNH1.
ExpressionAtlasiO60930. baseline and differential.
GenevisibleiO60930. HS.

Family and domain databases

Gene3Di3.30.420.10. 1 hit.
3.40.970.10. 1 hit.
InterProiIPR009027. Ribosomal_L9/RNase_H1_N.
IPR017067. RNase_H1_euk.
IPR011320. RNase_H1_N.
IPR012337. RNaseH-like_dom.
IPR002156. RNaseH_domain.
[Graphical view]
PfamiPF01693. Cauli_VI. 1 hit.
PF00075. RNase_H. 1 hit.
[Graphical view]
PIRSFiPIRSF036852. Ribonuclease_H1_euk. 1 hit.
SUPFAMiSSF53098. SSF53098. 1 hit.
SSF55658. SSF55658. 1 hit.
PROSITEiPS50879. RNASE_H. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiRNH1_HUMAN
AccessioniPrimary (citable) accession number: O60930
Secondary accession number(s): B3KQU4
, O60523, O60857, Q57Z93, Q5U0C1, Q6FHD4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 27, 2001
Last sequence update: April 27, 2001
Last modified: November 2, 2016
This is version 157 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

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 2
    Human chromosome 2: 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.