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Protein

Endonuclease V

Gene

ENDOV

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

Functioni

Endoribonuclease that specifically cleaves inosine-containing RNAs: cleaves RNA at the second phosphodiester bond 3' to inosine. Has strong preference for single-stranded RNAs (ssRNAs) toward double-stranded RNAs (dsRNAs). Cleaves mRNAs and tRNAs containing inosine. Also able to cleave structure-specific dsRNA substrates containing the specific sites 5'-IIUI-3' and 5'-UIUU-3'. Inosine is present in a number of RNAs following editing; the function of inosine-specific endoribonuclease is still unclear: it could either play a regulatory role in edited RNAs, or be involved in antiviral response by removing the hyperedited long viral dsRNA genome that has undergone A-to-I editing. Binds branched DNA structures.3 Publications

Cofactori

Mg2+1 Publication

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi52 – 521MagnesiumCurated
Metal bindingi126 – 1261MagnesiumBy similarity

GO - Molecular functioni

  • endodeoxyribonuclease activity, producing 5'-phosphomonoesters Source: UniProtKB
  • endoribonuclease activity, producing 5'-phosphomonoesters Source: UniProtKB
  • magnesium ion binding Source: UniProtKB
  • single-stranded RNA binding Source: UniProtKB
  • structure-specific DNA binding Source: UniProtKB

GO - Biological processi

  • DNA repair Source: UniProtKB
  • RNA phosphodiester bond hydrolysis, endonucleolytic Source: GOC
Complete GO annotation...

Keywords - Molecular functioni

Endonuclease, Hydrolase, Nuclease

Keywords - Ligandi

DNA-binding, Magnesium, Metal-binding, RNA-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Endonuclease V (EC:3.1.26.-)
Short name:
hEndoV
Alternative name(s):
Inosine-specific endoribonuclease
Gene namesi
Name:ENDOV
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 17

Organism-specific databases

HGNCiHGNC:26640. ENDOV.

Subcellular locationi

GO - Cellular componenti

  • cytoplasm Source: UniProtKB
  • nucleolus Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi52 – 521D → A: Abolishes ribonuclease activity. 2 Publications
Mutagenesisi90 – 934PYVS → GGGG: Abolishes ability to bind branched DNA and RNA. 1 Publication
Mutagenesisi91 – 911Y → A: Abolishes ribonuclease activity without affecting ability to bind branched DNA. 2 Publications
Mutagenesisi100 – 1001E → A: Abolishes ribonuclease activity. 1 Publication
Mutagenesisi248 – 2492RK → AA: Abolishes ability to bind branched DNA and RNA. 1 Publication

Polymorphism and mutation databases

BioMutaiENDOV.
DMDMi74729504.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 282282Endonuclease VPRO_0000349223Add
BLAST

Proteomic databases

MaxQBiQ8N8Q3.
PaxDbiQ8N8Q3.
PRIDEiQ8N8Q3.

PTM databases

iPTMnetiQ8N8Q3.
PhosphoSiteiQ8N8Q3.

Expressioni

Gene expression databases

BgeeiQ8N8Q3.
ExpressionAtlasiQ8N8Q3. baseline and differential.
GenevisibleiQ8N8Q3. HS.

Interactioni

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sitei91 – 911Interaction with target RNACurated

Protein-protein interaction databases

BioGridi129772. 10 interactions.
IntActiQ8N8Q3. 2 interactions.
MINTiMINT-1385974.
STRINGi9606.ENSP00000429190.

Structurei

Secondary structure

1
282
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi15 – 2511Combined sources
Helixi35 – 384Combined sources
Beta strandi47 – 559Combined sources
Beta strandi61 – 7111Combined sources
Turni72 – 743Combined sources
Beta strandi77 – 8610Combined sources
Helixi97 – 11418Combined sources
Helixi116 – 1183Combined sources
Beta strandi121 – 1277Combined sources
Beta strandi129 – 1324Combined sources
Helixi138 – 1469Combined sources
Beta strandi150 – 1567Combined sources
Helixi167 – 1759Combined sources
Beta strandi182 – 1865Combined sources
Beta strandi192 – 1976Combined sources
Beta strandi207 – 2159Combined sources
Helixi217 – 22610Combined sources
Beta strandi229 – 2324Combined sources
Helixi234 – 25017Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4NSPX-ray2.30A13-250[»]
ProteinModelPortaliQ8N8Q3.
SMRiQ8N8Q3. Positions 13-250.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi225 – 2284Poly-Cys

Sequence similaritiesi

Belongs to the endonuclease V family.Curated

Phylogenomic databases

eggNOGiKOG4417. Eukaryota.
COG1515. LUCA.
GeneTreeiENSGT00390000011880.
HOVERGENiHBG062398.
InParanoidiQ8N8Q3.
OMAiREAPFLV.
PhylomeDBiQ8N8Q3.
TreeFamiTF300065.

Family and domain databases

HAMAPiMF_00801. Endonuclease_5.
InterProiIPR007581. Endonuclease-V.
[Graphical view]
PfamiPF04493. Endonuclease_5. 1 hit.
[Graphical view]

Sequences (5)i

Sequence statusi: Complete.

This entry describes 5 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q8N8Q3-1) [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
MALEAAGGPP EETLSLWKRE QARLKAHVVD RDTEAWQRDP AFSGLQRVGG
60 70 80 90 100
VDVSFVKGDS VRACASLVVL SFPELEVVYE ESRMVSLTAP YVSGFLAFRE
110 120 130 140 150
VPFLLELVQQ LREKEPGLMP QVLLVDGNGV LHHRGFGVAC HLGVLTDLPC
160 170 180 190 200
VGVAKKLLQV DGLENNALHK EKIRLLQTRG DSFPLLGDSG TVLGMALRSH
210 220 230 240 250
DRSTRPLYIS VGHRMSLEAA VRLTCCCCRF RIPEPVRQAD ICSREHIRKS
260 270 280
LGLPGPPTPR SPKAQRPVAC PKGDSGESSA LC
Length:282
Mass (Da):30,792
Last modified:October 1, 2002 - v1
Checksum:iEDB10210FB508A51
GO
Isoform 2 (identifier: Q8N8Q3-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     77-121: Missing.

Show »
Length:237
Mass (Da):25,612
Checksum:iA89BC40B3E5E0D22
GO
Isoform 3 (identifier: Q8N8Q3-3) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     77-121: Missing.
     280-282: ALC → GEGQPPQDHSPGPRTAPRPGSQEQAGKDWQ

Show »
Length:264
Mass (Da):28,503
Checksum:iEA8145ACC6AB8CF9
GO
Isoform 4 (identifier: Q8N8Q3-4) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-194: Missing.
     239-282: ADICSREHIRKSLGLPGPPTPRSPKAQRPVACPKGDSGESSALC → HFVERGGESTRPRLIPDRTRW

Show »
Length:65
Mass (Da):7,665
Checksum:iE75AB2F40226FC4E
GO
Isoform 5 (identifier: Q8N8Q3-5) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-194: Missing.

Show »
Length:88
Mass (Da):9,670
Checksum:i77BE0951D5518E2F
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti19 – 191R → W in BAC03912 (PubMed:14702039).Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti29 – 291V → I.1 Publication
Corresponds to variant rs35549084 [ dbSNP | Ensembl ].
VAR_046285
Natural varianti112 – 1121R → Q.1 Publication
Corresponds to variant rs34933300 [ dbSNP | Ensembl ].
VAR_046286
Natural varianti114 – 1141K → R.1 Publication
Corresponds to variant rs41298706 [ dbSNP | Ensembl ].
VAR_046287
Natural varianti141 – 1411H → Y.1 Publication
VAR_046288
Natural varianti201 – 2011D → N.1 Publication
Corresponds to variant rs35929621 [ dbSNP | Ensembl ].
VAR_046289

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 194194Missing in isoform 4 and isoform 5. 2 PublicationsVSP_035228Add
BLAST
Alternative sequencei77 – 12145Missing in isoform 2 and isoform 3. 2 PublicationsVSP_035229Add
BLAST
Alternative sequencei239 – 28244ADICS…SSALC → HFVERGGESTRPRLIPDRTR W in isoform 4. 1 PublicationVSP_035230Add
BLAST
Alternative sequencei280 – 2823ALC → GEGQPPQDHSPGPRTAPRPG SQEQAGKDWQ in isoform 3. 1 PublicationVSP_035231

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK092539 mRNA. Translation: BAC03912.1.
AK096344 mRNA. Translation: BAC04765.1.
AK096802 mRNA. No translation available.
DQ500957 Genomic DNA. Translation: ABF47100.1.
AC120024 Genomic DNA. No translation available.
CH471099 Genomic DNA. Translation: EAW89607.1.
CH471099 Genomic DNA. Translation: EAW89605.1.
CH471099 Genomic DNA. Translation: EAW89615.1.
BC037889 mRNA. Translation: AAH37889.1.
BC045824 mRNA. Translation: AAH45824.1.
BC064545 mRNA. Translation: AAH64545.1.
CCDSiCCDS54172.1. [Q8N8Q3-1]
CCDS54173.1. [Q8N8Q3-2]
CCDS54174.1. [Q8N8Q3-3]
RefSeqiNP_001158109.1. NM_001164637.2. [Q8N8Q3-2]
NP_001158110.1. NM_001164638.1. [Q8N8Q3-3]
NP_775898.2. NM_173627.4. [Q8N8Q3-1]
UniGeneiHs.389678.
Hs.728933.

Genome annotation databases

EnsembliENST00000323854; ENSP00000317810; ENSG00000173818. [Q8N8Q3-3]
ENST00000517795; ENSP00000461577; ENSG00000173818. [Q8N8Q3-5]
ENST00000518137; ENSP00000429190; ENSG00000173818. [Q8N8Q3-1]
ENST00000518901; ENSP00000460685; ENSG00000173818. [Q8N8Q3-5]
ENST00000518907; ENSP00000458361; ENSG00000173818. [Q8N8Q3-4]
ENST00000520284; ENSP00000458391; ENSG00000173818. [Q8N8Q3-4]
ENST00000520367; ENSP00000431036; ENSG00000173818. [Q8N8Q3-2]
GeneIDi284131.
KEGGihsa:284131.
UCSCiuc002jyk.4. human. [Q8N8Q3-1]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Web resourcesi

NIEHS-SNPs

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK092539 mRNA. Translation: BAC03912.1.
AK096344 mRNA. Translation: BAC04765.1.
AK096802 mRNA. No translation available.
DQ500957 Genomic DNA. Translation: ABF47100.1.
AC120024 Genomic DNA. No translation available.
CH471099 Genomic DNA. Translation: EAW89607.1.
CH471099 Genomic DNA. Translation: EAW89605.1.
CH471099 Genomic DNA. Translation: EAW89615.1.
BC037889 mRNA. Translation: AAH37889.1.
BC045824 mRNA. Translation: AAH45824.1.
BC064545 mRNA. Translation: AAH64545.1.
CCDSiCCDS54172.1. [Q8N8Q3-1]
CCDS54173.1. [Q8N8Q3-2]
CCDS54174.1. [Q8N8Q3-3]
RefSeqiNP_001158109.1. NM_001164637.2. [Q8N8Q3-2]
NP_001158110.1. NM_001164638.1. [Q8N8Q3-3]
NP_775898.2. NM_173627.4. [Q8N8Q3-1]
UniGeneiHs.389678.
Hs.728933.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4NSPX-ray2.30A13-250[»]
ProteinModelPortaliQ8N8Q3.
SMRiQ8N8Q3. Positions 13-250.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi129772. 10 interactions.
IntActiQ8N8Q3. 2 interactions.
MINTiMINT-1385974.
STRINGi9606.ENSP00000429190.

PTM databases

iPTMnetiQ8N8Q3.
PhosphoSiteiQ8N8Q3.

Polymorphism and mutation databases

BioMutaiENDOV.
DMDMi74729504.

Proteomic databases

MaxQBiQ8N8Q3.
PaxDbiQ8N8Q3.
PRIDEiQ8N8Q3.

Protocols and materials databases

DNASUi284131.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000323854; ENSP00000317810; ENSG00000173818. [Q8N8Q3-3]
ENST00000517795; ENSP00000461577; ENSG00000173818. [Q8N8Q3-5]
ENST00000518137; ENSP00000429190; ENSG00000173818. [Q8N8Q3-1]
ENST00000518901; ENSP00000460685; ENSG00000173818. [Q8N8Q3-5]
ENST00000518907; ENSP00000458361; ENSG00000173818. [Q8N8Q3-4]
ENST00000520284; ENSP00000458391; ENSG00000173818. [Q8N8Q3-4]
ENST00000520367; ENSP00000431036; ENSG00000173818. [Q8N8Q3-2]
GeneIDi284131.
KEGGihsa:284131.
UCSCiuc002jyk.4. human. [Q8N8Q3-1]

Organism-specific databases

CTDi284131.
GeneCardsiENDOV.
HGNCiHGNC:26640. ENDOV.
neXtProtiNX_Q8N8Q3.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG4417. Eukaryota.
COG1515. LUCA.
GeneTreeiENSGT00390000011880.
HOVERGENiHBG062398.
InParanoidiQ8N8Q3.
OMAiREAPFLV.
PhylomeDBiQ8N8Q3.
TreeFamiTF300065.

Miscellaneous databases

GenomeRNAii284131.
NextBioi35533104.
PROiQ8N8Q3.

Gene expression databases

BgeeiQ8N8Q3.
ExpressionAtlasiQ8N8Q3. baseline and differential.
GenevisibleiQ8N8Q3. HS.

Family and domain databases

HAMAPiMF_00801. Endonuclease_5.
InterProiIPR007581. Endonuclease-V.
[Graphical view]
PfamiPF04493. Endonuclease_5. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "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.
    , 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] (ISOFORMS 1; 2 AND 5).
    Tissue: Prostate.
  2. NIEHS SNPs program
    Submitted (JUN-2006) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANTS ILE-29; GLN-112; ARG-114; TYR-141 AND ASN-201.
  3. "DNA sequence of human chromosome 17 and analysis of rearrangement in the human lineage."
    Zody M.C., Garber M., Adams D.J., Sharpe T., Harrow J., Lupski J.R., Nicholson C., Searle S.M., Wilming L., Young S.K., Abouelleil A., Allen N.R., Bi W., Bloom T., Borowsky M.L., Bugalter B.E., Butler J., Chang J.L.
    , Chen C.-K., Cook A., Corum B., Cuomo C.A., de Jong P.J., DeCaprio D., Dewar K., FitzGerald M., Gilbert J., Gibson R., Gnerre S., Goldstein S., Grafham D.V., Grocock R., Hafez N., Hagopian D.S., Hart E., Norman C.H., Humphray S., Jaffe D.B., Jones M., Kamal M., Khodiyar V.K., LaButti K., Laird G., Lehoczky J., Liu X., Lokyitsang T., Loveland J., Lui A., Macdonald P., Major J.E., Matthews L., Mauceli E., McCarroll S.A., Mihalev A.H., Mudge J., Nguyen C., Nicol R., O'Leary S.B., Osoegawa K., Schwartz D.C., Shaw-Smith C., Stankiewicz P., Steward C., Swarbreck D., Venkataraman V., Whittaker C.A., Yang X., Zimmer A.R., Bradley A., Hubbard T., Birren B.W., Rogers J., Lander E.S., Nusbaum C.
    Nature 440:1045-1049(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  5. "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] (ISOFORMS 3 AND 4).
    Tissue: Brain and Duodenum.
  6. "Human endonuclease V as a repair enzyme for DNA deamination."
    Mi R., Alford-Zappala M., Kow Y.W., Cunningham R.P., Cao W.
    Mutat. Res. 735:12-18(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: PRELIMINARY ACTIVITY.
  7. "The human homolog of Escherichia coli endonuclease V is a nucleolar protein with affinity for branched DNA structures."
    Fladeby C., Vik E.S., Laerdahl J.K., Gran Neurauter C., Heggelund J.E., Thorgaard E., Strom-Andersen P., Bjoras M., Dalhus B., Alseth I.
    PLoS ONE 7:E47466-E47466(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION.
  8. Cited for: FUNCTION, CATALYTIC ACTIVITY, COFACTOR, MUTAGENESIS OF ASP-52; 90-PRO--SER-93; TYR-91 AND 248-ARG-LYS-249.
  9. "Human endonuclease V is a ribonuclease specific for inosine-containing RNA."
    Morita Y., Shibutani T., Nakanishi N., Nishikura K., Iwai S., Kuraoka I.
    Nat. Commun. 4:2273-2273(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, CATALYTIC ACTIVITY, SUBCELLULAR LOCATION, MUTAGENESIS OF ASP-52; TYR-91 AND GLU-100.

Entry informationi

Entry nameiENDOV_HUMAN
AccessioniPrimary (citable) accession number: Q8N8Q3
Secondary accession number(s): I3L3S4
, Q6P2G2, Q86X99, Q8NAK0
Entry historyi
Integrated into UniProtKB/Swiss-Prot: September 2, 2008
Last sequence update: October 1, 2002
Last modified: April 13, 2016
This is version 101 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

Miscellaneous

Was initially characterized as an endodeoxyribonuclease involved in DNA repair (PubMed:22664237). While it shows some weak endodeoxyribonuclease activity in vitro, such activity probably does not exist in vivo.1 Publication

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 17
    Human chromosome 17: 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. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  5. 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.