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Q05823 (RN5A_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 139. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (7) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
2-5A-dependent ribonuclease

Short name=2-5A-dependent RNase
EC=3.1.26.-
Alternative name(s):
Ribonuclease 4
Ribonuclease L
Short name=RNase L
Gene names
Name:RNASEL
Synonyms:RNS4
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length741 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Endoribonuclease that functions in the interferon (IFN) antiviral response. In INF treated and virus infected cells, RNASEL probably mediates its antiviral effects through a combination of direct cleavage of single-stranded viral RNAs, inhibition of protein synthesis through the degradation of rRNA, induction of apoptosis, and induction of other antiviral genes. RNASEL mediated apoptosis is the result of a JNK-dependent stress-response pathway leading to cytochrome c release from mitochondria and caspase-dependent apoptosis. Therefore, activation of RNASEL could lead to elimination of virus infected cells under some circumstances. Might play a central role in the regulation of mRNA turnover. Ref.8

Catalytic activity

Cleaves 3' of UpNp dimers, with preference for UU and UA sequences, to sets of discrete products ranging from between 4 and 22 nucleotides in length.

Cofactor

Manganese or magnesium. Required for optimal RNA cleavage rates.

Enzyme regulation

After binding to 2-5A (5'-phosphorylated 2',5'-linked oligoadenylates) the homodimerization and subsequent activation occurs. Inhibited by RNASEL inhibitor ABCE1/RLI, a cytoplasmic member of the ATP-binding cassette (ABC) transporter family.

Subunit structure

Monomer (inactive form) or homodimer. Interacts with ABCE1; this interaction inhibits the RNASEL. Ref.7

Subcellular location

Cytoplasm. Mitochondrion Ref.8.

Tissue specificity

Highly expressed in spleen and thymus followed by prostate, testis, uterus, small intestine, colon and peripheral blood leukocytes.

Induction

By interferons. Virus replication in higher vertebrates is restrained by IFNs that cause cells to transcribe genes encoding antiviral proteins, such as 2'-5' oligoadenylate synthetases (OASs). oligoadenylate synthetase is stimulated by dsRNA to produce 5'-phosphorylated, 2'-5'-linked oligoadenylates (2-5A), whose function is to activate RNASEL.

Domain

The nine ankyrin repeats also called 2-5A sensor constitute the N-terminus 2-5A binding domain.

The protein kinase domain is predicted to be catalytically inactive. It allows the homodimerization.

The ribonuclease domain is located in the C-terminus. A single active nuclease domain in a dimer is sufficient for ribonuclease activity By similarity.

Involvement in disease

Prostate cancer, hereditary, 1 (HPC1) [MIM:601518]: A condition associated with familial predisposition to cancer of the prostate. Most prostate cancers are adenocarcinomas that develop in the acini of the prostatic ducts. Other rare histopathologic types of prostate cancer that occur in approximately 5% of patients include small cell carcinoma, mucinous carcinoma, prostatic ductal carcinoma, transitional cell carcinoma, squamous cell carcinoma, basal cell carcinoma, adenoid cystic carcinoma (basaloid), signet-ring cell carcinoma and neuroendocrine carcinoma.
Note: Disease susceptibility is associated with variations affecting the gene represented in this entry.

Sequence similarities

Belongs to the protein kinase superfamily.

Contains 9 ANK repeats.

Contains 1 KEN domain.

Contains 1 protein kinase domain.

Ontologies

Keywords
   Biological processAntiviral defense
   Cellular componentCytoplasm
Mitochondrion
   Coding sequence diversityPolymorphism
   DomainANK repeat
Repeat
Zinc-finger
   LigandATP-binding
Metal-binding
Nucleotide-binding
RNA-binding
Zinc
   Molecular functionEndonuclease
Hydrolase
Nuclease
   PTMAcetylation
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processRNA phosphodiester bond hydrolysis, endonucleolytic

Non-traceable author statement Ref.6. Source: GOC

cytokine-mediated signaling pathway

Traceable author statement. Source: Reactome

defense response to virus

Inferred from direct assay PubMed 19923450. Source: UniProtKB

mRNA processing

Inferred from electronic annotation. Source: InterPro

negative regulation of viral genome replication

Inferred from direct assay PubMed 19923450. Source: UniProtKB

positive regulation of transcription from RNA polymerase II promoter

Inferred from direct assay PubMed 19245366. Source: UniProtKB

protein phosphorylation

Non-traceable author statement Ref.6. Source: UniProtKB

rRNA processing

Inferred from electronic annotation. Source: Ensembl

type I interferon signaling pathway

Traceable author statement. Source: Reactome

   Cellular_componentcytosol

Traceable author statement. Source: Reactome

mitochondrion

Inferred from electronic annotation. Source: UniProtKB-SubCell

nuclear matrix

Inferred from electronic annotation. Source: Ensembl

   Molecular_functionATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

RNA binding

Inferred from direct assay Ref.6. Source: UniProtKB

endoribonuclease activity

Non-traceable author statement Ref.6. Source: UniProtKB

metal ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

protein kinase activity

Inferred from electronic annotation. Source: InterPro

rRNA binding

Inferred from electronic annotation. Source: Ensembl

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

IQGAP1P469402EBI-8390477,EBI-297509

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 7417412-5A-dependent ribonuclease
PRO_0000067051

Regions

Repeat24 – 5330ANK 1
Repeat58 – 8730ANK 2
Repeat91 – 12030ANK 3
Repeat124 – 15330ANK 4
Repeat167 – 19731ANK 5
Repeat201 – 23434ANK 6
Repeat238 – 26831ANK 7
Repeat272 – 30130ANK 8
Repeat303 – 32927ANK 9
Domain365 – 586222Protein kinase
Domain589 – 723135KEN
Zinc finger395 – 44450C6-type; atypical
Region229 – 242142-5A binding (P-loop) 1
Region253 – 275232-5A binding (P-loop) 2

Amino acid modifications

Modified residue6841N6-acetyllysine Ref.13

Natural variations

Natural variant591G → S. Ref.15 Ref.16
Corresponds to variant rs151296858 [ dbSNP | Ensembl ].
VAR_013509
Natural variant971I → L. Ref.18
Corresponds to variant rs56250729 [ dbSNP | Ensembl ].
VAR_042358
Natural variant2891A → T. Ref.18
Corresponds to variant rs35553278 [ dbSNP | Ensembl ].
VAR_042359
Natural variant4061S → F. Ref.15
Corresponds to variant rs145787003 [ dbSNP | Ensembl ].
VAR_013510
Natural variant4621R → Q Risk factor for prostate cancer; reduced enzymatic activity. Ref.15 Ref.16 Ref.17 Ref.18
Corresponds to variant rs486907 [ dbSNP | Ensembl ].
VAR_012056
Natural variant5411D → E No change in enzymatic activity. Ref.15 Ref.16 Ref.17 Ref.18
Corresponds to variant rs627928 [ dbSNP | Ensembl ].
VAR_012057
Natural variant5921R → H. Ref.18
Corresponds to variant rs35896902 [ dbSNP | Ensembl ].
VAR_042360

Experimental info

Mutagenesis2401K → N: Reduced 2-5A binding activity; almost complete loss of 2-5A binding activity; when associated with N-274. Ref.1
Mutagenesis2741K → N: Reduced 2-5A binding activity; almost complete loss of 2-5A binding activity; when associated with N-240. Ref.1
Mutagenesis3921K → R: Complete loss of enzymatic activity and enzyme dimerization. No change in binding to 2-5A and RNA. Ref.11
Mutagenesis5831H → A: No change in enzymatic activity. Ref.12
Mutagenesis5841P → A: No change in enzymatic activity. Ref.12
Mutagenesis6321W → A: No change in enzymatic activity. Ref.12
Mutagenesis6611D → A: Complete loss of enzymatic activity. Ref.12
Mutagenesis6671R → A: Complete loss of enzymatic activity. No change in 2-5A binding and enzyme dimerization. Ref.12
Mutagenesis6721H → A: Complete loss of enzymatic activity. No change in 2-5A binding activity and enzyme dimerization. Ref.12

Secondary structure

............................................. 741
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q05823 [UniParc].

Last modified February 1, 1996. Version 2.
Checksum: 91385EA307E3CE1D

FASTA74183,533
        10         20         30         40         50         60 
MESRDHNNPQ EGPTSSSGRR AAVEDNHLLI KAVQNEDVDL VQQLLEGGAN VNFQEEEGGW 

        70         80         90        100        110        120 
TPLHNAVQMS REDIVELLLR HGADPVLRKK NGATPFILAA IAGSVKLLKL FLSKGADVNE 

       130        140        150        160        170        180 
CDFYGFTAFM EAAVYGKVKA LKFLYKRGAN VNLRRKTKED QERLRKGGAT ALMDAAEKGH 

       190        200        210        220        230        240 
VEVLKILLDE MGADVNACDN MGRNALIHAL LSSDDSDVEA ITHLLLDHGA DVNVRGERGK 

       250        260        270        280        290        300 
TPLILAVEKK HLGLVQRLLE QEHIEINDTD SDGKTALLLA VELKLKKIAE LLCKRGASTD 

       310        320        330        340        350        360 
CGDLVMTARR NYDHSLVKVL LSHGAKEDFH PPAEDWKPQS SHWGAALKDL HRIYRPMIGK 

       370        380        390        400        410        420 
LKFFIDEKYK IADTSEGGIY LGFYEKQEVA VKTFCEGSPR AQREVSCLQS SRENSHLVTF 

       430        440        450        460        470        480 
YGSESHRGHL FVCVTLCEQT LEACLDVHRG EDVENEEDEF ARNVLSSIFK AVQELHLSCG 

       490        500        510        520        530        540 
YTHQDLQPQN ILIDSKKAAH LADFDKSIKW AGDPQEVKRD LEDLGRLVLY VVKKGSISFE 

       550        560        570        580        590        600 
DLKAQSNEEV VQLSPDEETK DLIHRLFHPG EHVRDCLSDL LGHPFFWTWE SRYRTLRNVG 

       610        620        630        640        650        660 
NESDIKTRKS ESEILRLLQP GPSEHSKSFD KWTTKINECV MKKMNKFYEK RGNFYQNTVG 

       670        680        690        700        710        720 
DLLKFIRNLG EHIDEEKHKK MKLKIGDPSL YFQKTFPDLV IYVYTKLQNT EYRKHFPQTH 

       730        740 
SPNKPQCDGA GGASGLASPG C 

« Hide

References

« Hide 'large scale' references
[1]"Expression cloning of 2-5A-dependent RNAase: a uniquely regulated mediator of interferon action."
Zhou A., Hassel B.A., Silverman R.H.
Cell 72:753-765(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], MUTAGENESIS OF LYS-240 AND LYS-274.
Tissue: Kidney.
[2]"Analysis and origins of the human and mouse RNase L genes: mediators of interferon action."
Zhou A., Nie H., Silverman R.H.
Mamm. Genome 11:989-992(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Tissue: Placenta.
[3]"The DNA sequence and biological annotation of human chromosome 1."
Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K. expand/collapse author list , Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.
Nature 441:315-321(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[4]Mural R.J., Istrail S., Sutton G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
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].
[6]"Intrinsic molecular activities of the interferon-induced 2-5A-dependent RNase."
Dong B., Xu L., Zhou A., Hassel B.A., Lee X., Torrence P.F., Silverman R.H.
J. Biol. Chem. 269:14153-14158(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: CHARACTERIZATION OF RNASEL ACTIVITY.
[7]"Cloning and characterization of a RNase L inhibitor. A new component of the interferon-regulated 2-5A pathway."
Bisbal C., Martinand C., Silhol M., Lebleu B., Salehzada T.
J. Biol. Chem. 270:13308-13317(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH ABCE1.
[8]"The 2-5A/RNase L/RNase L inhibitor (RNI) pathway regulates mitochondrial mRNAs stability in interferon alpha-treated H9 cells."
Le Roy F., Bisbal C., Silhol M., Martinand C., Lebleu B., Salehzada T.
J. Biol. Chem. 276:48473-48482(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, SUBCELLULAR LOCATION.
[9]Erratum
Le Roy F., Bisbal C., Silhol M., Martinand C., Lebleu B., Salehzada T.
J. Biol. Chem. 277:13354-13354(2002)
[10]"The 2-5A system in viral infection and apoptosis."
Castelli J., Wood K.A., Youle R.J.
Biomed. Pharmacother. 52:386-390(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: REVIEW.
[11]"Alternative function of a protein kinase homology domain in 2', 5'-oligoadenylate dependent RNase L."
Dong B., Silverman R.H.
Nucleic Acids Res. 27:439-445(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: MUTAGENESIS OF LYS-392.
[12]"Basis for regulated RNA cleavage by functional analysis of RNase L and Ire1p."
Dong B., Niwa M., Walter P., Silverman R.H.
RNA 7:361-373(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: MUTAGENESIS OF HIS-583; PRO-584; TRP-632; ASP-661; ARG-667 AND HIS-672.
[13]"Lysine acetylation targets protein complexes and co-regulates major cellular functions."
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M.
Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-684, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[14]"Structural basis for recognition of 2',5'-linked oligoadenylates by human ribonuclease L."
Tanaka N., Nakanishi M., Kusakabe Y., Goto Y., Kitade Y., Nakamura K.T.
EMBO J. 23:3929-3938(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 21-305 IN COMPLEX WITH THE ACTIVATOR 2-5A.
[15]"Germline alterations of the RNASEL gene, a candidate HPC1 gene at 1q25, in patients and families with prostate cancer."
Roekman A., Ikonen T., Seppaelae E.H., Nupponen N., Autio V., Mononen N., Bailey-Wilson J., Trent J., Carpten J., Matikainen M.P., Koivisto P.A., Tammela T.L.J., Kallioniemi O.-P., Schleutker J.
Am. J. Hum. Genet. 70:1299-1304(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS SER-59; PHE-406; GLN-462 AND GLU-541.
[16]"Germline mutations in the ribonuclease L gene in families showing linkage with HPC1."
Carpten J., Nupponen N., Isaacs S., Sood R., Robbins C., Xu J., Faruque M., Moses T., Ewing C., Gillanders E., Hu P., Bujnovszky P., Makalowska I., Baffoe-Bonnie A., Faith D., Smith J., Stephan D., Wiley K. expand/collapse author list , Brownstein M., Gildea D., Kelly B., Jenkins R., Hostetter G., Matikainen M., Schleutker J., Klinger K., Connors T., Xiang Y., Wang Z., De Marzo A., Papadopoulos N., Kallioniemi O.-P., Burk R., Meyers D., Groenberg H., Meltzer P., Silverman R., Bailey-Wilson J., Walsh P., Isaacs W., Trent J.
Nat. Genet. 30:181-184(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS SER-59; GLN-462 AND GLU-541.
[17]"RNASEL Arg462Gln variant is implicated in up to 13% of prostate cancer cases."
Casey G., Neville P.J., Plummer S.J., Xiang Y., Krumroy L.M., Klein E.A., Catalona W.J., Nupponen N., Carpten J.D., Trent J.M., Silverman R.H., Witte J.S.
Nat. Genet. 32:581-583(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: CHARACTERIZATION OF VARIANTS GLN-462 AND GLU-541.
[18]"Patterns of somatic mutation in human cancer genomes."
Greenman C., Stephens P., Smith R., Dalgliesh G.L., Hunter C., Bignell G., Davies H., Teague J., Butler A., Stevens C., Edkins S., O'Meara S., Vastrik I., Schmidt E.E., Avis T., Barthorpe S., Bhamra G., Buck G. expand/collapse author list , Choudhury B., Clements J., Cole J., Dicks E., Forbes S., Gray K., Halliday K., Harrison R., Hills K., Hinton J., Jenkinson A., Jones D., Menzies A., Mironenko T., Perry J., Raine K., Richardson D., Shepherd R., Small A., Tofts C., Varian J., Webb T., West S., Widaa S., Yates A., Cahill D.P., Louis D.N., Goldstraw P., Nicholson A.G., Brasseur F., Looijenga L., Weber B.L., Chiew Y.-E., DeFazio A., Greaves M.F., Green A.R., Campbell P., Birney E., Easton D.F., Chenevix-Trench G., Tan M.-H., Khoo S.K., Teh B.T., Yuen S.T., Leung S.Y., Wooster R., Futreal P.A., Stratton M.R.
Nature 446:153-158(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS [LARGE SCALE ANALYSIS] LEU-97; THR-289; GLN-462; GLU-541 AND HIS-592.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
L10381 Genomic DNA. Translation: AAA18032.1.
AL138776 Genomic DNA. Translation: CAH71322.1.
CH471067 Genomic DNA. Translation: EAW91128.1.
BC114433 mRNA. Translation: AAI14434.1.
PIRA45771.
RefSeqNP_066956.1. NM_021133.3.
UniGeneHs.518545.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1WDYX-ray1.80A21-305[»]
4G8KX-ray2.40A/B1-337[»]
4G8LX-ray2.80A/B/C/D1-337[»]
ProteinModelPortalQ05823.
SMRQ05823. Positions 21-346, 357-716.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid111969. 2 interactions.
IntActQ05823. 2 interactions.
MINTMINT-7990548.
STRING9606.ENSP00000356530.

Chemistry

BindingDBQ05823.
ChEMBLCHEMBL3575.

PTM databases

PhosphoSiteQ05823.

Polymorphism databases

DMDM1350802.

Proteomic databases

PaxDbQ05823.
PeptideAtlasQ05823.
PRIDEQ05823.

Protocols and materials databases

DNASU6041.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000367559; ENSP00000356530; ENSG00000135828.
ENST00000444138; ENSP00000411147; ENSG00000135828.
GeneID6041.
KEGGhsa:6041.
UCSCuc009wxz.2. human.

Organism-specific databases

CTD6041.
GeneCardsGC01M182542.
HGNCHGNC:10050. RNASEL.
HPACAB010906.
HPA002633.
MIM176807. phenotype.
180435. gene.
601518. phenotype.
neXtProtNX_Q05823.
Orphanet1331. Familial prostate cancer.
PharmGKBPA34418.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG0666.
HOGENOMHOG000276879.
HOVERGENHBG012673.
InParanoidQ05823.
KOK01165.
OMANMGRNAL.
OrthoDBEOG7VDXNN.
PhylomeDBQ05823.
TreeFamTF344032.

Enzyme and pathway databases

BioCycMetaCyc:HS06069-MONOMER.
ReactomeREACT_6900. Immune System.
SignaLinkQ05823.

Gene expression databases

ArrayExpressQ05823.
BgeeQ05823.
CleanExHS_RNASEL.
GenevestigatorQ05823.

Family and domain databases

Gene3D1.25.40.20. 3 hits.
InterProIPR002110. Ankyrin_rpt.
IPR020683. Ankyrin_rpt-contain_dom.
IPR010513. KEN_dom.
IPR011009. Kinase-like_dom.
IPR000719. Prot_kinase_dom.
IPR006567. PUG-dom.
[Graphical view]
PfamPF00023. Ank. 5 hits.
PF00069. Pkinase. 1 hit.
PF06479. Ribonuc_2-5A. 1 hit.
[Graphical view]
PRINTSPR01415. ANKYRIN.
SMARTSM00248. ANK. 8 hits.
SM00580. PUG. 1 hit.
[Graphical view]
SUPFAMSSF48403. SSF48403. 1 hit.
SSF56112. SSF56112. 1 hit.
PROSITEPS50297. ANK_REP_REGION. 1 hit.
PS50088. ANK_REPEAT. 6 hits.
PS51392. KEN. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceQ05823.
GeneWikiRibonuclease_L.
RNASEL.
GenomeRNAi6041.
NextBio23543.
PMAP-CutDBQ05823.
PROQ05823.
SOURCESearch...

Entry information

Entry nameRN5A_HUMAN
AccessionPrimary (citable) accession number: Q05823
Secondary accession number(s): Q5W0L2
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1995
Last sequence update: February 1, 1996
Last modified: April 16, 2014
This is version 139 of the entry and version 2 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

Human and mouse protein kinases

Human and mouse protein kinases: classification and index

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 1

Human chromosome 1: entries, gene names and cross-references to MIM