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Protein

Ribonuclease H2 subunit C

Gene

Rnaseh2c

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 3 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.1 Publication

GO - Biological processi

Complete GO annotation...

Names & Taxonomyi

Protein namesi
Recommended name:
Ribonuclease H2 subunit C
Short name:
RNase H2 subunit C
Alternative name(s):
Ribonuclease HI subunit C
Gene namesi
Name:Rnaseh2c
Synonyms:Ayp1
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 19

Organism-specific databases

MGIiMGI:1915459. Rnaseh2c.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 166166Ribonuclease H2 subunit CPRO_0000248386Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei1 – 11N-acetylmethionineBy similarity

Keywords - PTMi

Acetylation

Proteomic databases

EPDiQ9CQ18.
MaxQBiQ9CQ18.
PaxDbiQ9CQ18.
PRIDEiQ9CQ18.

PTM databases

iPTMnetiQ9CQ18.
PhosphoSiteiQ9CQ18.

Expressioni

Gene expression databases

BgeeiQ9CQ18.
CleanExiMM_RNASEH2C.
ExpressionAtlasiQ9CQ18. baseline and differential.
GenevisibleiQ9CQ18. MM.

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

STRINGi10090.ENSMUSP00000025864.

Structurei

Secondary structure

1
166
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi14 – 163Combined sources
Turni18 – 236Combined sources
Beta strandi29 – 3810Combined sources
Helixi44 – 474Combined sources
Helixi49 – 513Combined sources
Beta strandi56 – 583Combined sources
Beta strandi60 – 634Combined sources
Beta strandi66 – 749Combined sources
Beta strandi79 – 868Combined sources
Turni87 – 893Combined sources
Beta strandi92 – 10615Combined sources
Helixi113 – 1153Combined sources
Beta strandi123 – 13816Combined sources
Helixi145 – 1495Combined sources
Helixi152 – 1598Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3KIOX-ray2.90C1-166[»]
3P5JX-ray2.90C1-166[»]
ProteinModelPortaliQ9CQ18.
SMRiQ9CQ18. Positions 13-141.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ9CQ18.

Family & Domainsi

Sequence similaritiesi

Belongs to the RNase H2 subunit C family.Curated

Phylogenomic databases

eggNOGiENOG410J0SE. Eukaryota.
ENOG41126TY. LUCA.
GeneTreeiENSGT00390000001568.
HOGENOMiHOG000230780.
HOVERGENiHBG093917.
InParanoidiQ9CQ18.
KOiK10745.
OMAiHLLPCDV.
OrthoDBiEOG779P0Q.
PhylomeDBiQ9CQ18.
TreeFamiTF324370.

Family and domain databases

InterProiIPR013924. RNase_H2_suC.
[Graphical view]
PfamiPF08615. RNase_H2_suC. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q9CQ18-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MKNPEEAADG KQRIHLRPGS LRGAAPAKLH LLPCDVLVSR PAPVDRFFTP
60 70 80 90 100
AVRHDADGLQ ASFRGRGLRG EEVAVPPGFA GFVMVTEEKG EGLIGKLNFS
110 120 130 140 150
GDAEDKADEA QEPLERDFDR LIGATGSFSH FTLWGLETVP GPDAKVHRAL
160
GWPSLAAAIH AQVPED
Length:166
Mass (Da):17,823
Last modified:June 1, 2001 - v1
Checksum:iD631CFE252040417
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti9 – 91D → E in AAH24333 (PubMed:15489334).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF346604 mRNA. Translation: AAO49175.1.
AK018776 mRNA. Translation: BAB31401.1.
AK011556 mRNA. Translation: BAB27694.1.
BC024333 mRNA. Translation: AAH24333.1.
CCDSiCCDS29471.1.
RefSeqiNP_080892.1. NM_026616.2.
UniGeneiMm.246200.

Genome annotation databases

EnsembliENSMUST00000025864; ENSMUSP00000025864; ENSMUSG00000024925.
GeneIDi68209.
KEGGimmu:68209.
UCSCiuc008gdx.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF346604 mRNA. Translation: AAO49175.1.
AK018776 mRNA. Translation: BAB31401.1.
AK011556 mRNA. Translation: BAB27694.1.
BC024333 mRNA. Translation: AAH24333.1.
CCDSiCCDS29471.1.
RefSeqiNP_080892.1. NM_026616.2.
UniGeneiMm.246200.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3KIOX-ray2.90C1-166[»]
3P5JX-ray2.90C1-166[»]
ProteinModelPortaliQ9CQ18.
SMRiQ9CQ18. Positions 13-141.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000025864.

PTM databases

iPTMnetiQ9CQ18.
PhosphoSiteiQ9CQ18.

Proteomic databases

EPDiQ9CQ18.
MaxQBiQ9CQ18.
PaxDbiQ9CQ18.
PRIDEiQ9CQ18.

Protocols and materials databases

DNASUi68209.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000025864; ENSMUSP00000025864; ENSMUSG00000024925.
GeneIDi68209.
KEGGimmu:68209.
UCSCiuc008gdx.1. mouse.

Organism-specific databases

CTDi84153.
MGIiMGI:1915459. Rnaseh2c.

Phylogenomic databases

eggNOGiENOG410J0SE. Eukaryota.
ENOG41126TY. LUCA.
GeneTreeiENSGT00390000001568.
HOGENOMiHOG000230780.
HOVERGENiHBG093917.
InParanoidiQ9CQ18.
KOiK10745.
OMAiHLLPCDV.
OrthoDBiEOG779P0Q.
PhylomeDBiQ9CQ18.
TreeFamiTF324370.

Miscellaneous databases

EvolutionaryTraceiQ9CQ18.
PROiQ9CQ18.
SOURCEiSearch...

Gene expression databases

BgeeiQ9CQ18.
CleanExiMM_RNASEH2C.
ExpressionAtlasiQ9CQ18. baseline and differential.
GenevisibleiQ9CQ18. MM.

Family and domain databases

InterProiIPR013924. RNase_H2_suC.
[Graphical view]
PfamiPF08615. RNase_H2_suC. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "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 [MRNA].
  2. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: C57BL/6J.
    Tissue: Cerebellum.
  3. "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].
    Strain: FVB/N.
    Tissue: Kidney.
  4. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Kidney, Liver, Lung, Spleen and Testis.
  5. "The structure of the mammalian RNase H2 complex provides insight into RNA.NA hybrid processing to prevent immune dysfunction."
    Shaban N.M., Harvey S., Perrino F.W., Hollis T.
    J. Biol. Chem. 285:3617-3624(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.9 ANGSTROMS), FUNCTION, SUBUNIT.

Entry informationi

Entry nameiRNH2C_MOUSE
AccessioniPrimary (citable) accession number: Q9CQ18
Secondary accession number(s): Q8R1N2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: September 5, 2006
Last sequence update: June 1, 2001
Last modified: June 8, 2016
This is version 95 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. 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.