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Q8TDP1 (RNH2C_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 89. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Ribonuclease H2 subunit C

Short name=RNase H2 subunit C
Alternative name(s):
Aicardi-Goutieres syndrome 3 protein
Short name=AGS3
RNase H1 small subunit
Ribonuclease HI subunit C
Gene names
Name:RNASEH2C
Synonyms:AYP1
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length164 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. Ref.9 Ref.11

Subunit structure

The RNase H2 complex is a heterotrimer composed of the catalytic subunit RNASEH2A and the non-catalytic subunits RNASEH2B and RNASEH2C. Ref.9

Subcellular location

Nucleus Probable.

Tissue specificity

Widely expressed. Ref.11

Involvement in disease

Aicardi-Goutieres syndrome 3 (AGS3) [MIM:610329]: A 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.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.10 Ref.11 Ref.12

Miscellaneous

The T6 pseudogene located upstream of SRY on chromosome Y is derived from the transcript of this gene.

Sequence similarities

Belongs to the RNase H2 subunit C family.

Ontologies

Keywords
   Cellular componentNucleus
   Coding sequence diversityAlternative splicing
   DiseaseAicardi-Goutieres syndrome
Disease mutation
   PTMAcetylation
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processRNA catabolic process

Inferred from direct assay Ref.9. Source: UniProtKB

   Cellular_componentnucleus

Inferred from electronic annotation. Source: UniProtKB-SubCell

ribonuclease H2 complex

Inferred from direct assay Ref.9. Source: UniProtKB

Complete GO annotation...

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q8TDP1-1)

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.
Isoform 2 (identifier: Q8TDP1-2)

The sequence of this isoform differs from the canonical sequence as follows:
     89-89: Missing.
Note: No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 164164Ribonuclease H2 subunit C
PRO_0000248385

Amino acid modifications

Modified residue11N-acetylmethionine Ref.5 Ref.7 Ref.8

Natural variations

Alternative sequence891Missing in isoform 2.
VSP_020258
Natural variant131R → H in AGS3. Ref.10
VAR_070618
Natural variant391D → Y in AGS3. Ref.12
VAR_070619
Natural variant691R → W in AGS3. Ref.10 Ref.11 Ref.12
VAR_027287
Natural variant761P → L in AGS3. Ref.10
VAR_070620
Natural variant1381P → L in AGS3. Ref.10
VAR_070621
Natural variant1431K → I in AGS3. Ref.10 Ref.11
VAR_027288
Natural variant1511P → S in AGS3. Ref.10
VAR_070622

Secondary structure

.............................. 164
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified June 1, 2002. Version 1.
Checksum: 13D0F1D039963671

FASTA16417,840
        10         20         30         40         50         60 
MESGDEAAIE RHRVHLRSAT LRDAVPATLH LLPCEVAVDG PAPVGRFFTP AIRQGPEGLE 

        70         80         90        100        110        120 
VSFRGRCLRG EEVAVPPGLV GYVMVTEEKK VSMGKPDPLR DSGTDDQEEE PLERDFDRFI 

       130        140        150        160 
GATANFSRFT LWGLETIPGP DAKVRGALTW PSLAAAIHAQ VPED 

« Hide

Isoform 2 [UniParc].

Checksum: 7CD8D8306DE81EDC
Show »

FASTA16317,712

References

« Hide 'large scale' references
[1]"Cloning of the cDNA encoding the small subunit of human RNase HI."
Frank P., Bogusch A., Grimm R., Wintersberger U.
Submitted (OCT-2000) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
[2]"Evidence that the T6 pseudogene upstream of human SRY is derived from the transcript of a novel autosomal gene, AYP1."
Lim H.N., Oakenfull E.A., Hawkins J.R.
Submitted (FEB-2001) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORM 1).
[3]"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. expand/collapse author list , 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] (ISOFORM 2).
Tissue: Adipose tissue.
[4]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
Tissue: B-cell.
[5]"Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[6]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[7]"Comparative large-scale characterisation of plant vs. mammal proteins reveals similar and idiosyncratic N-alpha acetylation features."
Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T., Giglione C.
Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[8]"N-terminal acetylome analyses and functional insights of the N-terminal acetyltransferase NatB."
Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A., Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[9]"The structural and biochemical characterization of human RNase H2 complex reveals the molecular basis for substrate recognition and Aicardi-Goutieres syndrome defects."
Figiel M., Chon H., Cerritelli S.M., Cybulska M., Crouch R.J., Nowotny M.
J. Biol. Chem. 286:10540-10550(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (3.1 ANGSTROMS), FUNCTION, SUBUNIT.
[10]"Clinical and molecular phenotype of Aicardi-Goutieres syndrome."
Rice G., Patrick T., Parmar R., Taylor C.F., Aeby A., Aicardi J., Artuch R., Montalto S.A., Bacino C.A., Barroso B., Baxter P., Benko W.S., Bergmann C., Bertini E., Biancheri R., Blair E.M., Blau N., Bonthron D.T. expand/collapse author list , Briggs T., Brueton L.A., Brunner H.G., Burke C.J., Carr I.M., Carvalho D.R., Chandler K.E., Christen H.J., Corry P.C., Cowan F.M., Cox H., D'Arrigo S., Dean J., De Laet C., De Praeter C., Dery C., Ferrie C.D., Flintoff K., Frints S.G., Garcia-Cazorla A., Gener B., Goizet C., Goutieres F., Green A.J., Guet A., Hamel B.C., Hayward B.E., Heiberg A., Hennekam R.C., Husson M., Jackson A.P., Jayatunga R., Jiang Y.H., Kant S.G., Kao A., King M.D., Kingston H.M., Klepper J., van der Knaap M.S., Kornberg A.J., Kotzot D., Kratzer W., Lacombe D., Lagae L., Landrieu P.G., Lanzi G., Leitch A., Lim M.J., Livingston J.H., Lourenco C.M., Lyall E.G., Lynch S.A., Lyons M.J., Marom D., McClure J.P., McWilliam R., Melancon S.B., Mewasingh L.D., Moutard M.L., Nischal K.K., Ostergaard J.R., Prendiville J., Rasmussen M., Rogers R.C., Roland D., Rosser E.M., Rostasy K., Roubertie A., Sanchis A., Schiffmann R., Scholl-Burgi S., Seal S., Shalev S.A., Corcoles C.S., Sinha G.P., Soler D., Spiegel R., Stephenson J.B., Tacke U., Tan T.Y., Till M., Tolmie J.L., Tomlin P., Vagnarelli F., Valente E.M., Van Coster R.N., Van der Aa N., Vanderver A., Vles J.S., Voit T., Wassmer E., Weschke B., Whiteford M.L., Willemsen M.A., Zankl A., Zuberi S.M., Orcesi S., Fazzi E., Lebon P., Crow Y.J.
Am. J. Hum. Genet. 81:713-725(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS AGS3 HIS-13; TRP-69; LEU-76; LEU-138; ILE-143 AND SER-151.
[11]"Mutations in genes encoding ribonuclease H2 subunits cause Aicardi-Goutieres syndrome and mimic congenital viral brain infection."
Crow Y.J., Leitch A., Hayward B.E., Garner A., Parmar R., Griffith E., Ali M., Semple C., Aicardi J., Babul-Hirji R., Baumann C., Baxter P., Bertini E., Chandler K.E., Chitayat D., Cau D., Dery C., Fazzi E. expand/collapse author list , Goizet C., King M.D., Klepper J., Lacombe D., Lanzi G., Lyall H., Martinez-Frias M.L., Mathieu M., McKeown C., Monier A., Oade Y., Quarrell O.W., Rittey C.D., Rogers R.C., Sanchis A., Stephenson J.B.P., Tacke U., Till M., Tolmie J.L., Tomlin P., Voit T., Weschke B., Woods C.G., Lebon P., Bonthron D.T., Ponting C.P., Jackson A.P.
Nat. Genet. 38:910-916(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS AGS3 TRP-69 AND ILE-143, FUNCTION, TISSUE SPECIFICITY, INTERACTION WITH RNASEH2A AND RNASEH2B.
[12]"Expanding the phenotypic spectrum of lupus erythematosus in Aicardi-Goutieres syndrome."
Ramantani G., Kohlhase J., Hertzberg C., Innes A.M., Engel K., Hunger S., Borozdin W., Mah J.K., Ungerath K., Walkenhorst H., Richardt H.H., Buckard J., Bevot A., Siegel C., von Stuelpnagel C., Ikonomidou C., Thomas K., Proud V. expand/collapse author list , Niemann F., Wieczorek D., Haeusler M., Niggemann P., Baltaci V., Conrad K., Lebon P., Lee-Kirsch M.A.
Arthritis Rheum. 62:1469-1477(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS AGS3 TYR-39 AND TRP-69.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF312034 mRNA. Translation: AAL87739.1.
AF346605 Genomic DNA. Translation: AAO49176.1.
AF346606 mRNA. Translation: AAO49177.1.
AK024627 mRNA. Translation: BAB14937.1.
BC023588 mRNA. Translation: AAH23588.1.
CCDSCCDS8111.1. [Q8TDP1-1]
RefSeqNP_115569.2. NM_032193.3. [Q8TDP1-1]
UniGeneHs.718438.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
3P56X-ray4.06C/F1-164[»]
3PUFX-ray3.10C/F/I/L/O/R1-164[»]
ProteinModelPortalQ8TDP1.
SMRQ8TDP1. Positions 7-162.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid123916. 4 interactions.
STRING9606.ENSP00000308193.

PTM databases

PhosphoSiteQ8TDP1.

Polymorphism databases

DMDM74730607.

Proteomic databases

MaxQBQ8TDP1.
PaxDbQ8TDP1.
PRIDEQ8TDP1.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000308418; ENSP00000308193; ENSG00000172922. [Q8TDP1-1]
GeneID84153.
KEGGhsa:84153.
UCSCuc001ofn.3. human. [Q8TDP1-1]

Organism-specific databases

CTD84153.
GeneCardsGC11M065485.
GeneReviewsRNASEH2C.
HGNCHGNC:24116. RNASEH2C.
HPAHPA059703.
MIM610329. phenotype.
610330. gene.
neXtProtNX_Q8TDP1.
Orphanet51. Aicardi-Goutieres syndrome.
PharmGKBPA162401445.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG72919.
HOGENOMHOG000230780.
HOVERGENHBG093917.
InParanoidQ8TDP1.
KOK10745.
PhylomeDBQ8TDP1.
TreeFamTF324370.

Gene expression databases

ArrayExpressQ8TDP1.
BgeeQ8TDP1.
CleanExHS_RNASEH2C.
GenevestigatorQ8TDP1.

Family and domain databases

InterProIPR013924. RNase_H2_suC.
[Graphical view]
PfamPF08615. RNase_H2_suC. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSRNASEH2C. human.
EvolutionaryTraceQ8TDP1.
GenomeRNAi84153.
NextBio73488.
PROQ8TDP1.
SOURCESearch...

Entry information

Entry nameRNH2C_HUMAN
AccessionPrimary (citable) accession number: Q8TDP1
Secondary accession number(s): Q9H7F5
Entry history
Integrated into UniProtKB/Swiss-Prot: September 5, 2006
Last sequence update: June 1, 2002
Last modified: July 9, 2014
This is version 89 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 11

Human chromosome 11: entries, gene names and cross-references to MIM