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Protein

Ribonuclease H2 subunit B

Gene

RNASEH2B

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

Functioni

Non catalytic subunit of RNase H2, an endonuclease that specifically degrades the RNA of RNA:DNA hybrids. Participates in DNA replication, possibly by mediating the removal of lagging-strand Okazaki fragment RNA primers during DNA replication. Mediates the excision of single ribonucleotides from DNA:RNA duplexes.2 Publications

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Enzyme and pathway databases

BioCyciZFISH:HS13612-MONOMER.
BRENDAi3.1.26.4. 2681.

Names & Taxonomyi

Protein namesi
Recommended name:
Ribonuclease H2 subunit B
Short name:
RNase H2 subunit B
Alternative name(s):
Aicardi-Goutieres syndrome 2 protein
Short name:
AGS2
Deleted in lymphocytic leukemia 8
Ribonuclease HI subunit B
Gene namesi
Name:RNASEH2B
Synonyms:DLEU8
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 13

Organism-specific databases

HGNCiHGNC:25671. RNASEH2B.

Subcellular locationi

GO - Cellular componenti

  • nucleus Source: UniProtKB-SubCell
  • ribonuclease H2 complex Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Involvement in diseasei

Aicardi-Goutieres syndrome 2 (AGS2)3 Publications
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionA form of Aicardi-Goutieres syndrome, a genetically heterogeneous disease characterized by cerebral atrophy, leukoencephalopathy, intracranial calcifications, chronic cerebrospinal fluid (CSF) lymphocytosis, increased CSF alpha-interferon, and negative serologic investigations for common prenatal infection. Clinical features as thrombocytopenia, hepatosplenomegaly and elevated hepatic transaminases along with intermittent fever may erroneously suggest an infective process. Severe neurological dysfunctions manifest in infancy as progressive microcephaly, spasticity, dystonic posturing and profound psychomotor retardation. Death often occurs in early childhood.
See also OMIM:610181
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_07061143P → H in AGS2. 1 PublicationCorresponds to variant rs79564863dbSNPEnsembl.1
Natural variantiVAR_02728060L → R in AGS2; heterozygous compound with T-177. 2 PublicationsCorresponds to variant rs75325951dbSNPEnsembl.1
Natural variantiVAR_07061273W → L in AGS2; reduces stability of the RNase complex. 2 PublicationsCorresponds to variant rs78071087dbSNPEnsembl.1
Natural variantiVAR_07061383G → S in AGS2; reduces stability of the RNase complex. 2 PublicationsCorresponds to variant rs76158094dbSNPEnsembl.1
Natural variantiVAR_02728186H → R in AGS2; heterozygous compound with T-177; reduces stability of the RNase complex. 3 PublicationsCorresponds to variant rs77931005dbSNPEnsembl.1
Natural variantiVAR_070614138L → F in AGS2. 1 PublicationCorresponds to variant rs78705382dbSNPEnsembl.1
Natural variantiVAR_070615159S → I in AGS2. 1 PublicationCorresponds to variant rs76219783dbSNPEnsembl.1
Natural variantiVAR_027282162K → T in AGS2. 2 PublicationsCorresponds to variant rs75971463dbSNPEnsembl.1
Natural variantiVAR_027283163T → I in AGS2; heterozygous compound with T-177. 2 PublicationsCorresponds to variant rs79310911dbSNPEnsembl.1
Natural variantiVAR_027284177A → T in AGS2; frequent mutation. 2 PublicationsCorresponds to variant rs75184679dbSNPEnsembl.1
Natural variantiVAR_070616183V → M in AGS2. 1 PublicationCorresponds to variant rs77377571dbSNPEnsembl.1
Natural variantiVAR_027285185V → G in AGS2. 2 PublicationsCorresponds to variant rs74555752dbSNPEnsembl.1
Natural variantiVAR_027286219Y → H in AGS2; heterozygous compound with a nonsense mutation; reduces stability of the RNase complex. 3 PublicationsCorresponds to variant rs77391331dbSNPEnsembl.1
Natural variantiVAR_070617229S → P in AGS2. 1 PublicationCorresponds to variant rs768565639dbSNPEnsembl.1

Keywords - Diseasei

Aicardi-Goutieres syndrome, Disease mutation

Organism-specific databases

DisGeNETi79621.
MalaCardsiRNASEH2B.
MIMi610181. phenotype.
OpenTargetsiENSG00000136104.
Orphaneti51. Aicardi-Goutieres syndrome.
PharmGKBiPA162401418.

Polymorphism and mutation databases

BioMutaiRNASEH2B.
DMDMi74745929.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemovedCombined sources
ChainiPRO_00002483782 – 312Ribonuclease H2 subunit BAdd BLAST311

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei2N-acetylalanineCombined sources1
Modified residuei295N6-acetyllysineCombined sources1
Modified residuei296PhosphoserineCombined sources1

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

EPDiQ5TBB1.
MaxQBiQ5TBB1.
PaxDbiQ5TBB1.
PeptideAtlasiQ5TBB1.
PRIDEiQ5TBB1.

PTM databases

iPTMnetiQ5TBB1.
PhosphoSitePlusiQ5TBB1.

Expressioni

Tissue specificityi

Widely expressed.1 Publication

Gene expression databases

BgeeiENSG00000136104.
CleanExiHS_RNASEH2B.
ExpressionAtlasiQ5TBB1. baseline and differential.
GenevisibleiQ5TBB1. HS.

Organism-specific databases

HPAiHPA040084.
HPA041469.

Interactioni

Subunit structurei

The RNase H2 complex is a heterotrimer composed of the catalytic subunit RNASEH2A and the non-catalytic subunits RNASEH2B and RNASEH2C.1 Publication

Protein-protein interaction databases

BioGridi122751. 39 interactors.
IntActiQ5TBB1. 30 interactors.
STRINGi9606.ENSP00000337623.

Structurei

Secondary structure

1312
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi14 – 21Combined sources8
Beta strandi36 – 41Combined sources6
Turni43 – 45Combined sources3
Beta strandi47 – 54Combined sources8
Turni55 – 58Combined sources4
Beta strandi59 – 66Combined sources8
Beta strandi72 – 75Combined sources4
Beta strandi78 – 81Combined sources4
Beta strandi85 – 90Combined sources6
Helixi94 – 107Combined sources14
Helixi113 – 116Combined sources4
Helixi123 – 130Combined sources8
Helixi134 – 138Combined sources5
Turni139 – 141Combined sources3
Beta strandi142 – 145Combined sources4
Beta strandi155 – 158Combined sources4
Helixi160 – 181Combined sources22
Helixi206 – 216Combined sources11
Turni217 – 219Combined sources3
Helixi222 – 230Combined sources9
Helixi297 – 299Combined sources3

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
3P56X-ray4.06B/E2-226[»]
3P87X-ray2.99G/H/I/J/K/L290-312[»]
3PUFX-ray3.10B/E/H/K/N/Q14-233[»]
ProteinModelPortaliQ5TBB1.
SMRiQ5TBB1.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ5TBB1.

Family & Domainsi

Sequence similaritiesi

Belongs to the RNase H2 subunit B family.Curated

Phylogenomic databases

eggNOGiKOG4705. Eukaryota.
ENOG410YS7I. LUCA.
GeneTreeiENSGT00390000011439.
HOVERGENiHBG056010.
InParanoidiQ5TBB1.
KOiK10744.
PhylomeDBiQ5TBB1.
TreeFamiTF105250.

Family and domain databases

CDDicd09270. RNase_H2-B. 1 hit.
InterProiIPR019024. RNase_H2_suB.
[Graphical view]
PfamiPF09468. RNase_H2-Ydr279. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q5TBB1-1) [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
MAAGVDCGDG VGARQHVFLV SEYLKDASKK MKNGLMFVKL VNPCSGEGAI
60 70 80 90 100
YLFNMCLQQL FEVKVFKEKH HSWFINQSVQ SGGLLHFATP VDPLFLLLHY
110 120 130 140 150
LIKADKEGKF QPLDQVVVDN VFPNCILLLK LPGLEKLLHH VTEEKGNPEI
160 170 180 190 200
DNKKYYKYSK EKTLKWLEKK VNQTVAALKT NNVNVSSRVQ STAFFSGDQA
210 220 230 240 250
STDKEEDYIR YAHGLISDYI PKELSDDLSK YLKLPEPSAS LPNPPSKKIK
260 270 280 290 300
LSDEPVEAKE DYTKFNTKDL KTEKKNSKMT AAQKALAKVD KSGMKSIDTF
310
FGVKNKKKIG KV
Length:312
Mass (Da):35,139
Last modified:April 12, 2005 - v1
Checksum:i98B1A8E073A50D68
GO
Isoform 2 (identifier: Q5TBB1-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     248-257: KIKLSDEPVE → MAAQRQKRGK
     258-312: Missing.

Note: No experimental confirmation available. Gene prediction based on EST data.
Show »
Length:257
Mass (Da):29,005
Checksum:iD96DCA78CB52F6DF
GO

Sequence cautioni

The sequence AAH01397 differs from that shown. Contaminating sequence. Potential poly-A sequence.Curated
The sequence AAH07332 differs from that shown. Contaminating sequence. Potential poly-A sequence.Curated
The sequence AAH10174 differs from that shown. Contaminating sequence. Potential poly-A sequence.Curated

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti61F → L in AAX13343 (Ref. 1) Curated1
Sequence conflicti61F → L in BAB13892 (PubMed:14702039).Curated1
Sequence conflicti305N → K in AAH05088 (PubMed:15489334).Curated1

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_07061143P → H in AGS2. 1 PublicationCorresponds to variant rs79564863dbSNPEnsembl.1
Natural variantiVAR_02728060L → R in AGS2; heterozygous compound with T-177. 2 PublicationsCorresponds to variant rs75325951dbSNPEnsembl.1
Natural variantiVAR_07061273W → L in AGS2; reduces stability of the RNase complex. 2 PublicationsCorresponds to variant rs78071087dbSNPEnsembl.1
Natural variantiVAR_07061383G → S in AGS2; reduces stability of the RNase complex. 2 PublicationsCorresponds to variant rs76158094dbSNPEnsembl.1
Natural variantiVAR_02728186H → R in AGS2; heterozygous compound with T-177; reduces stability of the RNase complex. 3 PublicationsCorresponds to variant rs77931005dbSNPEnsembl.1
Natural variantiVAR_070614138L → F in AGS2. 1 PublicationCorresponds to variant rs78705382dbSNPEnsembl.1
Natural variantiVAR_070615159S → I in AGS2. 1 PublicationCorresponds to variant rs76219783dbSNPEnsembl.1
Natural variantiVAR_027282162K → T in AGS2. 2 PublicationsCorresponds to variant rs75971463dbSNPEnsembl.1
Natural variantiVAR_027283163T → I in AGS2; heterozygous compound with T-177. 2 PublicationsCorresponds to variant rs79310911dbSNPEnsembl.1
Natural variantiVAR_027284177A → T in AGS2; frequent mutation. 2 PublicationsCorresponds to variant rs75184679dbSNPEnsembl.1
Natural variantiVAR_070616183V → M in AGS2. 1 PublicationCorresponds to variant rs77377571dbSNPEnsembl.1
Natural variantiVAR_027285185V → G in AGS2. 2 PublicationsCorresponds to variant rs74555752dbSNPEnsembl.1
Natural variantiVAR_027286219Y → H in AGS2; heterozygous compound with a nonsense mutation; reduces stability of the RNase complex. 3 PublicationsCorresponds to variant rs77391331dbSNPEnsembl.1
Natural variantiVAR_070617229S → P in AGS2. 1 PublicationCorresponds to variant rs768565639dbSNPEnsembl.1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_054039248 – 257KIKLSDEPVE → MAAQRQKRGK in isoform 2. Curated10
Alternative sequenceiVSP_054040258 – 312Missing in isoform 2. CuratedAdd BLAST55

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY764036 mRNA. Translation: AAX13343.1.
AK021774 mRNA. Translation: BAB13892.1.
AK223340 mRNA. Translation: BAD97060.1.
AL137881 Genomic DNA. No translation available.
CH471075 Genomic DNA. Translation: EAX08864.1.
BC001397 mRNA. Translation: AAH01397.1. Sequence problems.
BC005088 mRNA. Translation: AAH05088.1.
BC007332 mRNA. Translation: AAH07332.1. Sequence problems.
BC010174 mRNA. Translation: AAH10174.1. Sequence problems.
CCDSiCCDS45047.1. [Q5TBB1-2]
CCDS9425.1. [Q5TBB1-1]
RefSeqiNP_001135751.1. NM_001142279.2. [Q5TBB1-2]
NP_078846.2. NM_024570.3. [Q5TBB1-1]
UniGeneiHs.306291.

Genome annotation databases

EnsembliENST00000336617; ENSP00000337623; ENSG00000136104. [Q5TBB1-1]
ENST00000422660; ENSP00000389877; ENSG00000136104. [Q5TBB1-2]
GeneIDi79621.
KEGGihsa:79621.
UCSCiuc001vfa.4. human. [Q5TBB1-1]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY764036 mRNA. Translation: AAX13343.1.
AK021774 mRNA. Translation: BAB13892.1.
AK223340 mRNA. Translation: BAD97060.1.
AL137881 Genomic DNA. No translation available.
CH471075 Genomic DNA. Translation: EAX08864.1.
BC001397 mRNA. Translation: AAH01397.1. Sequence problems.
BC005088 mRNA. Translation: AAH05088.1.
BC007332 mRNA. Translation: AAH07332.1. Sequence problems.
BC010174 mRNA. Translation: AAH10174.1. Sequence problems.
CCDSiCCDS45047.1. [Q5TBB1-2]
CCDS9425.1. [Q5TBB1-1]
RefSeqiNP_001135751.1. NM_001142279.2. [Q5TBB1-2]
NP_078846.2. NM_024570.3. [Q5TBB1-1]
UniGeneiHs.306291.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
3P56X-ray4.06B/E2-226[»]
3P87X-ray2.99G/H/I/J/K/L290-312[»]
3PUFX-ray3.10B/E/H/K/N/Q14-233[»]
ProteinModelPortaliQ5TBB1.
SMRiQ5TBB1.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi122751. 39 interactors.
IntActiQ5TBB1. 30 interactors.
STRINGi9606.ENSP00000337623.

PTM databases

iPTMnetiQ5TBB1.
PhosphoSitePlusiQ5TBB1.

Polymorphism and mutation databases

BioMutaiRNASEH2B.
DMDMi74745929.

Proteomic databases

EPDiQ5TBB1.
MaxQBiQ5TBB1.
PaxDbiQ5TBB1.
PeptideAtlasiQ5TBB1.
PRIDEiQ5TBB1.

Protocols and materials databases

DNASUi79621.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000336617; ENSP00000337623; ENSG00000136104. [Q5TBB1-1]
ENST00000422660; ENSP00000389877; ENSG00000136104. [Q5TBB1-2]
GeneIDi79621.
KEGGihsa:79621.
UCSCiuc001vfa.4. human. [Q5TBB1-1]

Organism-specific databases

CTDi79621.
DisGeNETi79621.
GeneCardsiRNASEH2B.
GeneReviewsiRNASEH2B.
HGNCiHGNC:25671. RNASEH2B.
HPAiHPA040084.
HPA041469.
MalaCardsiRNASEH2B.
MIMi610181. phenotype.
610326. gene.
neXtProtiNX_Q5TBB1.
OpenTargetsiENSG00000136104.
Orphaneti51. Aicardi-Goutieres syndrome.
PharmGKBiPA162401418.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG4705. Eukaryota.
ENOG410YS7I. LUCA.
GeneTreeiENSGT00390000011439.
HOVERGENiHBG056010.
InParanoidiQ5TBB1.
KOiK10744.
PhylomeDBiQ5TBB1.
TreeFamiTF105250.

Enzyme and pathway databases

BioCyciZFISH:HS13612-MONOMER.
BRENDAi3.1.26.4. 2681.

Miscellaneous databases

ChiTaRSiRNASEH2B. human.
EvolutionaryTraceiQ5TBB1.
GenomeRNAii79621.
PROiQ5TBB1.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000136104.
CleanExiHS_RNASEH2B.
ExpressionAtlasiQ5TBB1. baseline and differential.
GenevisibleiQ5TBB1. HS.

Family and domain databases

CDDicd09270. RNase_H2-B. 1 hit.
InterProiIPR019024. RNase_H2_suB.
[Graphical view]
PfamiPF09468. RNase_H2-Ydr279. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiRNH2B_HUMAN
AccessioniPrimary (citable) accession number: Q5TBB1
Secondary accession number(s): G3XAJ1
, Q05DR2, Q6PK48, Q9HAF7
Entry historyi
Integrated into UniProtKB/Swiss-Prot: September 5, 2006
Last sequence update: April 12, 2005
Last modified: November 2, 2016
This is version 108 of the entry and version 1 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 13
    Human chromosome 13: 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.