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Q05823

- RN5A_HUMAN

UniProt

Q05823 - RN5A_HUMAN

Protein

2-5A-dependent ribonuclease

Gene

RNASEL

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 144 (01 Oct 2014)
      Sequence version 2 (01 Feb 1996)
      Previous versions | rss
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    Functioni

    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.1 Publication

    Catalytic activityi

    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.

    Cofactori

    Manganese or magnesium. Required for optimal RNA cleavage rates.

    Enzyme regulationi

    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.

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Zinc fingeri395 – 44450C6-type; atypicalAdd
    BLAST

    GO - Molecular functioni

    1. ATP binding Source: UniProtKB-KW
    2. endoribonuclease activity Source: UniProtKB
    3. metal ion binding Source: UniProtKB-KW
    4. protein binding Source: IntAct
    5. protein kinase activity Source: InterPro
    6. RNA binding Source: UniProtKB
    7. rRNA binding Source: Ensembl

    GO - Biological processi

    1. cytokine-mediated signaling pathway Source: Reactome
    2. defense response to virus Source: UniProtKB
    3. mRNA processing Source: InterPro
    4. negative regulation of viral genome replication Source: UniProtKB
    5. positive regulation of transcription from RNA polymerase II promoter Source: UniProtKB
    6. protein phosphorylation Source: UniProtKB
    7. RNA phosphodiester bond hydrolysis, endonucleolytic Source: GOC
    8. rRNA processing Source: Ensembl
    9. type I interferon signaling pathway Source: Reactome

    Keywords - Molecular functioni

    Endonuclease, Hydrolase, Nuclease

    Keywords - Biological processi

    Antiviral defense

    Keywords - Ligandi

    ATP-binding, Metal-binding, Nucleotide-binding, RNA-binding, Zinc

    Enzyme and pathway databases

    BioCyciMetaCyc:HS06069-MONOMER.
    ReactomeiREACT_25162. Interferon alpha/beta signaling.
    SignaLinkiQ05823.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    2-5A-dependent ribonuclease (EC:3.1.26.-)
    Short name:
    2-5A-dependent RNase
    Alternative name(s):
    Ribonuclease 4
    Ribonuclease L
    Short name:
    RNase L
    Gene namesi
    Name:RNASEL
    Synonyms:RNS4
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 1

    Organism-specific databases

    HGNCiHGNC:10050. RNASEL.

    Subcellular locationi

    Cytoplasm 1 Publication. Mitochondrion 1 Publication

    GO - Cellular componenti

    1. cytosol Source: Reactome
    2. mitochondrion Source: UniProtKB-SubCell
    3. nuclear matrix Source: Ensembl

    Keywords - Cellular componenti

    Cytoplasm, Mitochondrion

    Pathology & Biotechi

    Involvement in diseasei

    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.

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi240 – 2401K → N: Reduced 2-5A binding activity; almost complete loss of 2-5A binding activity; when associated with N-274. 1 Publication
    Mutagenesisi274 – 2741K → N: Reduced 2-5A binding activity; almost complete loss of 2-5A binding activity; when associated with N-240. 1 Publication
    Mutagenesisi392 – 3921K → R: Complete loss of enzymatic activity and enzyme dimerization. No change in binding to 2-5A and RNA. 1 Publication
    Mutagenesisi583 – 5831H → A: No change in enzymatic activity. 1 Publication
    Mutagenesisi584 – 5841P → A: No change in enzymatic activity. 1 Publication
    Mutagenesisi632 – 6321W → A: No change in enzymatic activity. 1 Publication
    Mutagenesisi661 – 6611D → A: Complete loss of enzymatic activity. 1 Publication
    Mutagenesisi667 – 6671R → A: Complete loss of enzymatic activity. No change in 2-5A binding and enzyme dimerization. 1 Publication
    Mutagenesisi672 – 6721H → A: Complete loss of enzymatic activity. No change in 2-5A binding activity and enzyme dimerization. 1 Publication

    Organism-specific databases

    MIMi176807. phenotype.
    601518. phenotype.
    Orphaneti1331. Familial prostate cancer.
    PharmGKBiPA34418.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 7417412-5A-dependent ribonucleasePRO_0000067051Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei684 – 6841N6-acetyllysine1 Publication

    Keywords - PTMi

    Acetylation

    Proteomic databases

    MaxQBiQ05823.
    PaxDbiQ05823.
    PeptideAtlasiQ05823.
    PRIDEiQ05823.

    PTM databases

    PhosphoSiteiQ05823.

    Miscellaneous databases

    PMAP-CutDBQ05823.

    Expressioni

    Tissue specificityi

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

    Inductioni

    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.

    Gene expression databases

    ArrayExpressiQ05823.
    BgeeiQ05823.
    CleanExiHS_RNASEL.
    GenevestigatoriQ05823.

    Organism-specific databases

    HPAiCAB010906.
    HPA002633.

    Interactioni

    Subunit structurei

    Monomer (inactive form) or homodimer. Interacts with ABCE1; this interaction inhibits the RNASEL.2 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    IQGAP1P469402EBI-8390477,EBI-297509

    Protein-protein interaction databases

    BioGridi111969. 2 interactions.
    IntActiQ05823. 2 interactions.
    MINTiMINT-7990548.
    STRINGi9606.ENSP00000356530.

    Structurei

    Secondary structure

    1
    741
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi22 – 3413
    Helixi38 – 469
    Turni56 – 583
    Helixi62 – 687
    Helixi72 – 809
    Helixi95 – 1028
    Helixi105 – 1139
    Helixi128 – 1347
    Helixi138 – 1469
    Helixi159 – 1635
    Helixi171 – 1788
    Helixi181 – 1899
    Helixi205 – 2117
    Turni215 – 2173
    Helixi218 – 22710
    Helixi237 – 2393
    Helixi242 – 2487
    Helixi252 – 2609
    Beta strandi261 – 2633
    Helixi276 – 2827
    Helixi286 – 29510
    Beta strandi301 – 3033
    Helixi304 – 3107
    Helixi314 – 3229
    Beta strandi341 – 3444
    Helixi345 – 3528
    Beta strandi361 – 3633
    Helixi367 – 3693
    Beta strandi370 – 3745
    Beta strandi377 – 39519
    Helixi399 – 40911
    Beta strandi420 – 4256
    Beta strandi427 – 4359
    Beta strandi438 – 4403
    Helixi441 – 4455
    Helixi459 – 47719
    Helixi488 – 4903
    Beta strandi491 – 4933
    Beta strandi495 – 4973
    Beta strandi499 – 5013
    Helixi514 – 53219
    Turni533 – 5353
    Helixi539 – 5446
    Helixi547 – 5515
    Helixi557 – 56711
    Helixi576 – 5805
    Helixi584 – 5863
    Helixi589 – 60012
    Helixi603 – 6064
    Helixi613 – 6186
    Turni628 – 6314
    Helixi632 – 6343
    Helixi638 – 6458
    Helixi646 – 6483
    Turni649 – 6524
    Helixi659 – 67214
    Helixi681 – 6855
    Helixi688 – 6958
    Helixi699 – 7079
    Helixi711 – 7155

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1WDYX-ray1.80A21-305[»]
    4G8KX-ray2.40A/B1-337[»]
    4G8LX-ray2.80A/B/C/D1-337[»]
    4OAUX-ray2.60C21-719[»]
    4OAVX-ray2.10B/D21-719[»]
    ProteinModelPortaliQ05823.
    SMRiQ05823. Positions 21-719.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ05823.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Repeati24 – 5330ANK 1Add
    BLAST
    Repeati58 – 8730ANK 2Add
    BLAST
    Repeati91 – 12030ANK 3Add
    BLAST
    Repeati124 – 15330ANK 4Add
    BLAST
    Repeati167 – 19731ANK 5Add
    BLAST
    Repeati201 – 23434ANK 6Add
    BLAST
    Repeati238 – 26831ANK 7Add
    BLAST
    Repeati272 – 30130ANK 8Add
    BLAST
    Repeati303 – 32927ANK 9Add
    BLAST
    Domaini365 – 586222Protein kinasePROSITE-ProRule annotationAdd
    BLAST
    Domaini589 – 723135KENPROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni229 – 242142-5A binding (P-loop) 1Add
    BLAST
    Regioni253 – 275232-5A binding (P-loop) 2Add
    BLAST

    Domaini

    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.By similarity

    Sequence similaritiesi

    Belongs to the protein kinase superfamily.Curated
    Contains 9 ANK repeats.PROSITE-ProRule annotation
    Contains 1 KEN domain.PROSITE-ProRule annotation
    Contains 1 protein kinase domain.PROSITE-ProRule annotation

    Zinc finger

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Zinc fingeri395 – 44450C6-type; atypicalAdd
    BLAST

    Keywords - Domaini

    ANK repeat, Repeat, Zinc-finger

    Phylogenomic databases

    eggNOGiCOG0666.
    HOGENOMiHOG000276879.
    HOVERGENiHBG012673.
    InParanoidiQ05823.
    KOiK01165.
    OMAiDCGDLVM.
    OrthoDBiEOG7VDXNN.
    PhylomeDBiQ05823.
    TreeFamiTF344032.

    Family and domain databases

    Gene3Di1.25.40.20. 3 hits.
    InterProiIPR002110. Ankyrin_rpt.
    IPR020683. Ankyrin_rpt-contain_dom.
    IPR010513. KEN_dom.
    IPR011009. Kinase-like_dom.
    IPR000719. Prot_kinase_dom.
    IPR006567. PUG-dom.
    [Graphical view]
    PfamiPF00023. Ank. 5 hits.
    PF00069. Pkinase. 1 hit.
    PF06479. Ribonuc_2-5A. 1 hit.
    [Graphical view]
    PRINTSiPR01415. ANKYRIN.
    SMARTiSM00248. ANK. 8 hits.
    SM00580. PUG. 1 hit.
    [Graphical view]
    SUPFAMiSSF48403. SSF48403. 1 hit.
    SSF56112. SSF56112. 1 hit.
    PROSITEiPS50297. ANK_REP_REGION. 1 hit.
    PS50088. ANK_REPEAT. 6 hits.
    PS51392. KEN. 1 hit.
    PS50011. PROTEIN_KINASE_DOM. 1 hit.
    [Graphical view]

    Sequences (2)i

    Sequence statusi: Complete.

    This entry describes 2 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: Q05823-1) [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

    MESRDHNNPQ EGPTSSSGRR AAVEDNHLLI KAVQNEDVDL VQQLLEGGAN    50
    VNFQEEEGGW TPLHNAVQMS REDIVELLLR HGADPVLRKK NGATPFILAA 100
    IAGSVKLLKL FLSKGADVNE CDFYGFTAFM EAAVYGKVKA LKFLYKRGAN 150
    VNLRRKTKED QERLRKGGAT ALMDAAEKGH VEVLKILLDE MGADVNACDN 200
    MGRNALIHAL LSSDDSDVEA ITHLLLDHGA DVNVRGERGK TPLILAVEKK 250
    HLGLVQRLLE QEHIEINDTD SDGKTALLLA VELKLKKIAE LLCKRGASTD 300
    CGDLVMTARR NYDHSLVKVL LSHGAKEDFH PPAEDWKPQS SHWGAALKDL 350
    HRIYRPMIGK LKFFIDEKYK IADTSEGGIY LGFYEKQEVA VKTFCEGSPR 400
    AQREVSCLQS SRENSHLVTF YGSESHRGHL FVCVTLCEQT LEACLDVHRG 450
    EDVENEEDEF ARNVLSSIFK AVQELHLSCG YTHQDLQPQN ILIDSKKAAH 500
    LADFDKSIKW AGDPQEVKRD LEDLGRLVLY VVKKGSISFE DLKAQSNEEV 550
    VQLSPDEETK DLIHRLFHPG EHVRDCLSDL LGHPFFWTWE SRYRTLRNVG 600
    NESDIKTRKS ESEILRLLQP GPSEHSKSFD KWTTKINECV MKKMNKFYEK 650
    RGNFYQNTVG DLLKFIRNLG EHIDEEKHKK MKLKIGDPSL YFQKTFPDLV 700
    IYVYTKLQNT EYRKHFPQTH SPNKPQCDGA GGASGLASPG C 741
    Length:741
    Mass (Da):83,533
    Last modified:February 1, 1996 - v2
    Checksum:i91385EA307E3CE1D
    GO
    Isoform 2 (identifier: Q05823-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         636-652: INECVMKKMNKFYEKRG → MSKLRHRQIIFPTTQNQ
         653-741: Missing.

    Show »
    Length:652
    Mass (Da):73,416
    Checksum:i4F39B25B82F07216
    GO

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti59 – 591G → S.2 Publications
    Corresponds to variant rs151296858 [ dbSNP | Ensembl ].
    VAR_013509
    Natural varianti97 – 971I → L.1 Publication
    Corresponds to variant rs56250729 [ dbSNP | Ensembl ].
    VAR_042358
    Natural varianti289 – 2891A → T.1 Publication
    Corresponds to variant rs35553278 [ dbSNP | Ensembl ].
    VAR_042359
    Natural varianti406 – 4061S → F.1 Publication
    Corresponds to variant rs145787003 [ dbSNP | Ensembl ].
    VAR_013510
    Natural varianti462 – 4621R → Q Risk factor for prostate cancer; reduced enzymatic activity. 3 Publications
    Corresponds to variant rs486907 [ dbSNP | Ensembl ].
    VAR_012056
    Natural varianti541 – 5411D → E No change in enzymatic activity. 3 Publications
    Corresponds to variant rs627928 [ dbSNP | Ensembl ].
    VAR_012057
    Natural varianti592 – 5921R → H.1 Publication
    Corresponds to variant rs35896902 [ dbSNP | Ensembl ].
    VAR_042360

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei636 – 65217INECV…YEKRG → MSKLRHRQIIFPTTQNQ in isoform 2. 2 PublicationsVSP_056272Add
    BLAST
    Alternative sequencei653 – 74189Missing in isoform 2. 2 PublicationsVSP_056273Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    L10381 Genomic DNA. Translation: AAA18032.1.
    CR627369 mRNA. Translation: CAH10468.1.
    AL138776 Genomic DNA. Translation: CAH71322.1.
    CH471067 Genomic DNA. Translation: EAW91128.1.
    BC090934 mRNA. Translation: AAH90934.1.
    BC114433 mRNA. Translation: AAI14434.1.
    CCDSiCCDS1347.1.
    PIRiA45771.
    RefSeqiNP_066956.1. NM_021133.3.
    XP_005245468.1. XM_005245411.1.
    UniGeneiHs.518545.

    Genome annotation databases

    EnsembliENST00000367559; ENSP00000356530; ENSG00000135828.
    ENST00000539397; ENSP00000440844; ENSG00000135828.
    GeneIDi6041.
    KEGGihsa:6041.
    UCSCiuc009wxz.2. human.

    Polymorphism databases

    DMDMi1350802.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    L10381 Genomic DNA. Translation: AAA18032.1 .
    CR627369 mRNA. Translation: CAH10468.1 .
    AL138776 Genomic DNA. Translation: CAH71322.1 .
    CH471067 Genomic DNA. Translation: EAW91128.1 .
    BC090934 mRNA. Translation: AAH90934.1 .
    BC114433 mRNA. Translation: AAI14434.1 .
    CCDSi CCDS1347.1.
    PIRi A45771.
    RefSeqi NP_066956.1. NM_021133.3.
    XP_005245468.1. XM_005245411.1.
    UniGenei Hs.518545.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1WDY X-ray 1.80 A 21-305 [» ]
    4G8K X-ray 2.40 A/B 1-337 [» ]
    4G8L X-ray 2.80 A/B/C/D 1-337 [» ]
    4OAU X-ray 2.60 C 21-719 [» ]
    4OAV X-ray 2.10 B/D 21-719 [» ]
    ProteinModelPortali Q05823.
    SMRi Q05823. Positions 21-719.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 111969. 2 interactions.
    IntActi Q05823. 2 interactions.
    MINTi MINT-7990548.
    STRINGi 9606.ENSP00000356530.

    Chemistry

    BindingDBi Q05823.
    ChEMBLi CHEMBL3575.

    PTM databases

    PhosphoSitei Q05823.

    Polymorphism databases

    DMDMi 1350802.

    Proteomic databases

    MaxQBi Q05823.
    PaxDbi Q05823.
    PeptideAtlasi Q05823.
    PRIDEi Q05823.

    Protocols and materials databases

    DNASUi 6041.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000367559 ; ENSP00000356530 ; ENSG00000135828 .
    ENST00000539397 ; ENSP00000440844 ; ENSG00000135828 .
    GeneIDi 6041.
    KEGGi hsa:6041.
    UCSCi uc009wxz.2. human.

    Organism-specific databases

    CTDi 6041.
    GeneCardsi GC01M182542.
    HGNCi HGNC:10050. RNASEL.
    HPAi CAB010906.
    HPA002633.
    MIMi 176807. phenotype.
    180435. gene.
    601518. phenotype.
    neXtProti NX_Q05823.
    Orphaneti 1331. Familial prostate cancer.
    PharmGKBi PA34418.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG0666.
    HOGENOMi HOG000276879.
    HOVERGENi HBG012673.
    InParanoidi Q05823.
    KOi K01165.
    OMAi DCGDLVM.
    OrthoDBi EOG7VDXNN.
    PhylomeDBi Q05823.
    TreeFami TF344032.

    Enzyme and pathway databases

    BioCyci MetaCyc:HS06069-MONOMER.
    Reactomei REACT_25162. Interferon alpha/beta signaling.
    SignaLinki Q05823.

    Miscellaneous databases

    EvolutionaryTracei Q05823.
    GeneWikii Ribonuclease_L.
    RNASEL.
    GenomeRNAii 6041.
    NextBioi 23543.
    PMAP-CutDB Q05823.
    PROi Q05823.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q05823.
    Bgeei Q05823.
    CleanExi HS_RNASEL.
    Genevestigatori Q05823.

    Family and domain databases

    Gene3Di 1.25.40.20. 3 hits.
    InterProi IPR002110. Ankyrin_rpt.
    IPR020683. Ankyrin_rpt-contain_dom.
    IPR010513. KEN_dom.
    IPR011009. Kinase-like_dom.
    IPR000719. Prot_kinase_dom.
    IPR006567. PUG-dom.
    [Graphical view ]
    Pfami PF00023. Ank. 5 hits.
    PF00069. Pkinase. 1 hit.
    PF06479. Ribonuc_2-5A. 1 hit.
    [Graphical view ]
    PRINTSi PR01415. ANKYRIN.
    SMARTi SM00248. ANK. 8 hits.
    SM00580. PUG. 1 hit.
    [Graphical view ]
    SUPFAMi SSF48403. SSF48403. 1 hit.
    SSF56112. SSF56112. 1 hit.
    PROSITEi PS50297. ANK_REP_REGION. 1 hit.
    PS50088. ANK_REPEAT. 6 hits.
    PS51392. KEN. 1 hit.
    PS50011. PROTEIN_KINASE_DOM. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    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. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
      Tissue: Colon carcinoma.
    4. "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.
      , 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].
    5. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    6. "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 1 AND 2).
      Tissue: Lymph.
    7. "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.
    8. "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.
    9. "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.
    10. Erratum
      Le Roy F., Bisbal C., Silhol M., Martinand C., Lebleu B., Salehzada T.
      J. Biol. Chem. 277:13354-13354(2002)
    11. "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.
    12. "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.
    13. "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.
    14. "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].
    15. "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.
    16. "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.
    17. Cited for: VARIANTS SER-59; GLN-462 AND GLU-541.
    18. Cited for: CHARACTERIZATION OF VARIANTS GLN-462 AND GLU-541.
    19. "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.
      , 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.

    Entry informationi

    Entry nameiRN5A_HUMAN
    AccessioniPrimary (citable) accession number: Q05823
    Secondary accession number(s): Q5W0L2, Q6AI46
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 1, 1995
    Last sequence update: February 1, 1996
    Last modified: October 1, 2014
    This is version 144 of the entry and version 2 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 1
      Human chromosome 1: 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

    External Data

    Dasty 3