CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-011316
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 2-5A-dependent ribonuclease 
Protein Synonyms/Alias
 2-5A-dependent RNase; Ribonuclease 4; Ribonuclease L; RNase L 
Gene Name
 RNASEL 
Gene Synonyms/Alias
 RNS4 
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
642KINECVMKKMNKFYEacetylation[1]
684KHKKMKLKIGDPSLYacetylation[1, 2, 3]
Reference
 [1] Integrated proteomic analysis of post-translational modifications by serial enrichment.
 Mertins P, Qiao JW, Patel J, Udeshi ND, Clauser KR, Mani DR, Burgess MW, Gillette MA, Jaffe JD, Carr SA.
 Nat Methods. 2013 Jul;10(7):634-7. [PMID: 23749302]
 [2] Lysine acetylation targets protein complexes and co-regulates major cellular functions.
 Choudhary C, Kumar C, Gnad F, Nielsen ML, Rehman M, Walther TC, Olsen JV, Mann M.
 Science. 2009 Aug 14;325(5942):834-40. [PMID: 19608861]
 [3] Proteomic investigations of lysine acetylation identify diverse substrates of mitochondrial deacetylase sirt3.
 Sol EM, Wagner SA, Weinert BT, Kumar A, Kim HS, Deng CX, Choudhary C.
 PLoS One. 2012;7(12):e50545. [PMID: 23236377
Functional Description
 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. 
Sequence Annotation
 REPEAT 24 53 ANK 1.
 REPEAT 58 87 ANK 2.
 REPEAT 91 120 ANK 3.
 REPEAT 124 153 ANK 4.
 REPEAT 167 197 ANK 5.
 REPEAT 201 234 ANK 6.
 REPEAT 238 268 ANK 7.
 REPEAT 272 301 ANK 8.
 REPEAT 303 329 ANK 9.
 DOMAIN 365 586 Protein kinase.
 DOMAIN 589 723 KEN.
 ZN_FING 395 444 C6-type; atypical.
 REGION 229 242 2-5A binding (P-loop) 1.
 REGION 253 275 2-5A binding (P-loop) 2.
 MOD_RES 684 684 N6-acetyllysine.  
Keyword
 3D-structure; Acetylation; ANK repeat; Antiviral defense; ATP-binding; Complete proteome; Cytoplasm; Endonuclease; Hydrolase; Metal-binding; Mitochondrion; Nuclease; Nucleotide-binding; Polymorphism; Reference proteome; Repeat; RNA-binding; Zinc; Zinc-finger. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 741 AA 
Protein Sequence
MESRDHNNPQ EGPTSSSGRR AAVEDNHLLI KAVQNEDVDL VQQLLEGGAN VNFQEEEGGW 60
TPLHNAVQMS REDIVELLLR HGADPVLRKK NGATPFILAA IAGSVKLLKL FLSKGADVNE 120
CDFYGFTAFM EAAVYGKVKA LKFLYKRGAN VNLRRKTKED QERLRKGGAT ALMDAAEKGH 180
VEVLKILLDE MGADVNACDN MGRNALIHAL LSSDDSDVEA ITHLLLDHGA DVNVRGERGK 240
TPLILAVEKK HLGLVQRLLE QEHIEINDTD SDGKTALLLA VELKLKKIAE LLCKRGASTD 300
CGDLVMTARR NYDHSLVKVL LSHGAKEDFH PPAEDWKPQS SHWGAALKDL HRIYRPMIGK 360
LKFFIDEKYK IADTSEGGIY LGFYEKQEVA VKTFCEGSPR AQREVSCLQS SRENSHLVTF 420
YGSESHRGHL FVCVTLCEQT LEACLDVHRG EDVENEEDEF ARNVLSSIFK AVQELHLSCG 480
YTHQDLQPQN ILIDSKKAAH LADFDKSIKW AGDPQEVKRD LEDLGRLVLY VVKKGSISFE 540
DLKAQSNEEV VQLSPDEETK DLIHRLFHPG EHVRDCLSDL LGHPFFWTWE SRYRTLRNVG 600
NESDIKTRKS ESEILRLLQP GPSEHSKSFD KWTTKINECV MKKMNKFYEK RGNFYQNTVG 660
DLLKFIRNLG EHIDEEKHKK MKLKIGDPSL YFQKTFPDLV IYVYTKLQNT EYRKHFPQTH 720
SPNKPQCDGA GGASGLASPG C 741 
Gene Ontology
 GO:0005829; C:cytosol; TAS:Reactome.
 GO:0005739; C:mitochondrion; IEA:UniProtKB-SubCell.
 GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
 GO:0004521; F:endoribonuclease activity; NAS:UniProtKB.
 GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
 GO:0004672; F:protein kinase activity; IEA:InterPro.
 GO:0003723; F:RNA binding; IDA:UniProtKB.
 GO:0051607; P:defense response to virus; IDA:UniProtKB.
 GO:0006397; P:mRNA processing; IEA:InterPro.
 GO:0045071; P:negative regulation of viral genome replication; IDA:UniProtKB.
 GO:0045944; P:positive regulation of transcription from RNA polymerase II promoter; IDA:UniProtKB.
 GO:0006468; P:protein phosphorylation; NAS:UniProtKB.
 GO:0060337; P:type I interferon-mediated signaling pathway; TAS:Reactome. 
Interpro
 IPR002110; Ankyrin_rpt.
 IPR020683; Ankyrin_rpt-contain_dom.
 IPR010513; KEN_dom.
 IPR011009; Kinase-like_dom.
 IPR000719; Prot_kinase_cat_dom.
 IPR006567; PUG-dom. 
Pfam
 PF00023; Ank
 PF00069; Pkinase
 PF06479; Ribonuc_2-5A 
SMART
 SM00248; ANK
 SM00580; PUG 
PROSITE
 PS50297; ANK_REP_REGION
 PS50088; ANK_REPEAT
 PS51392; KEN
 PS00107; PROTEIN_KINASE_ATP
 PS50011; PROTEIN_KINASE_DOM 
PRINTS
 PR01415; ANKYRIN.