RN5A_HUMAN - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: RN5A_HUMAN
• UniProt AC: Q05823
• Protein Name: 2-5A-dependent ribonuclease
• Gene Name: RNASEL
• Organism: Homo sapiens (Human).
• Sequence Length: 741
• Subcellular Localization: Cytoplasm . Mitochondrion .
• Protein 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. In the crosstalk between autophagy and apoptosis proposed to induce autophagy as an early stress response to small double-stranded RNA and at later stages of prolonged stress to activate caspase-dependent proteolytic cleavage of BECN1 to terminate autophagy and promote apoptosis. [PubMed: 26263979 Might play a central role in the regulation of mRNA turnover]
• Protein Sequence: MESRDHNNPQEGPTSSSGRRAAVEDNHLLIKAVQNEDVDLVQQLLEGGANVNFQEEEGGWTPLHNAVQMSREDIVELLLRHGADPVLRKKNGATPFILAAIAGSVKLLKLFLSKGADVNECDFYGFTAFMEAAVYGKVKALKFLYKRGANVNLRRKTKEDQERLRKGGATALMDAAEKGHVEVLKILLDEMGADVNACDNMGRNALIHALLSSDDSDVEAITHLLLDHGADVNVRGERGKTPLILAVEKKHLGLVQRLLEQEHIEINDTDSDGKTALLLAVELKLKKIAELLCKRGASTDCGDLVMTARRNYDHSLVKVLLSHGAKEDFHPPAEDWKPQSSHWGAALKDLHRIYRPMIGKLKFFIDEKYKIADTSEGGIYLGFYEKQEVAVKTFCEGSPRAQREVSCLQSSRENSHLVTFYGSESHRGHLFVCVTLCEQTLEACLDVHRGEDVENEEDEFARNVLSSIFKAVQELHLSCGYTHQDLQPQNILIDSKKAAHLADFDKSIKWAGDPQEVKRDLEDLGRLVLYVVKKGSISFEDLKAQSNEEVVQLSPDEETKDLIHRLFHPGEHVRDCLSDLLGHPFFWTWESRYRTLRNVGNESDIKTRKSESEILRLLQPGPSEHSKSFDKWTTKINECVMKKMNKFYEKRGNFYQNTVGDLLKFIRNLGEHIDEEKHKKMKLKIGDPSLYFQKTFPDLVIYVYTKLQNTEYRKHFPQTHSPNKPQCDGAGGASGLASPGC

Overview of Protein Modification Sites with Functional and Structural Information

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
15	Phosphorylation	NPQEGPTSSSGRRAA CCCCCCCCCHHCCCE	26.16	-
16	Phosphorylation	PQEGPTSSSGRRAAV CCCCCCCCHHCCCEE	39.01	-
17	Phosphorylation	QEGPTSSSGRRAAVE CCCCCCCHHCCCEEE	35.77	-
109	Acetylation	AGSVKLLKLFLSKGA HHHHHHHHHHHHCCC	47.86	25953088
166	Ubiquitination	EDQERLRKGGATALM HHHHHHHHCCHHHHH	67.31	29967540
250	Ubiquitination	LILAVEKKHLGLVQR EEEEEHHHHHHHHHH	30.47	29967540
287	Ubiquitination	AVELKLKKIAELLCK HHHHHHHHHHHHHHH	58.55	-
294	Ubiquitination	KIAELLCKRGASTDC HHHHHHHHCCCCCCH	54.56	29967540
315	Phosphorylation	ARRNYDHSLVKVLLS HHHCCCHHHHHHHHH	31.77	27251275
337	Ubiquitination	HPPAEDWKPQSSHWG CCCHHHCCCCCCCHH	45.56	29967540
406	Phosphorylation	PRAQREVSCLQSSRE HHHHHHHHHHHCCCC	12.35	28857561
467	Phosphorylation	FARNVLSSIFKAVQE HHHHHHHHHHHHHHH	28.08	24719451
496	Ubiquitination	QNILIDSKKAAHLAD CEEEECCCHHHHHHC	42.56	29967540
506	Ubiquitination	AHLADFDKSIKWAGD HHHHCHHHCCCCCCC	54.82	29967540
507	Phosphorylation	HLADFDKSIKWAGDP HHHCHHHCCCCCCCH	31.11	24719451
509	Ubiquitination	ADFDKSIKWAGDPQE HCHHHCCCCCCCHHH	37.77	29967540
536	Phosphorylation	LYVVKKGSISFEDLK EEEECCCCCCHHHHH	24.76	19690332
554	Phosphorylation	NEEVVQLSPDEETKD CCCCEECCCCHHHHH	17.14	27732954
559	Phosphorylation	QLSPDEETKDLIHRL ECCCCHHHHHHHHHH	28.01	27732954
607	O-linked_Glycosylation	GNESDIKTRKSESEI CCHHHHCCCCCHHHH	43.60	30379171
607	Phosphorylation	GNESDIKTRKSESEI CCHHHHCCCCCHHHH	43.60	28270605
609	Ubiquitination	ESDIKTRKSESEILR HHHHCCCCCHHHHHH	64.90	29967540
610	Phosphorylation	SDIKTRKSESEILRL HHHCCCCCHHHHHHH	42.96	28270605
612	Phosphorylation	IKTRKSESEILRLLQ HCCCCCHHHHHHHHC	36.71	28270605
623	Phosphorylation	RLLQPGPSEHSKSFD HHHCCCCCCCCCCHH	54.58	28857561
627	Ubiquitination	PGPSEHSKSFDKWTT CCCCCCCCCHHHHHH	57.98	29967540
628	Phosphorylation	GPSEHSKSFDKWTTK CCCCCCCCHHHHHHH	41.51	24719451
642	Acetylation	KINECVMKKMNKFYE HHHHHHHHHHHHHHH	28.59	23749302
684	Acetylation	KHKKMKLKIGDPSLY HHHHCCCCCCCHHHH	38.84	19608861
684	Malonylation	KHKKMKLKIGDPSLY HHHHCCCCCCCHHHH	38.84	26320211
689	Phosphorylation	KLKIGDPSLYFQKTF CCCCCCHHHHCCCCC	40.20	28857561
691	Phosphorylation	KIGDPSLYFQKTFPD CCCCHHHHCCCCCCC	14.33	28152594
719	Phosphorylation	YRKHFPQTHSPNKPQ HHHHCCCCCCCCCCC	25.26	27080861
721	Phosphorylation	KHFPQTHSPNKPQCD HHCCCCCCCCCCCCC	33.29	27080861
734	Phosphorylation	CDGAGGASGLASPGC CCCCCCCCCCCCCCC	37.30	27080861
738	Phosphorylation	GGASGLASPGC---- CCCCCCCCCCC----	27.20	27080861

Upstream regulatory proteins (kinases for phosphorylation sites, E3 ubiquitin ligases of ubiquitination sites, ...)

Oops, there are no upstream regulatory protein records of RN5A_HUMAN !!

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of RN5A_HUMAN !!

Disease-associated PTM Sites based on SAP

* Distance = the distance between SAP position and PTM sites.

Oops, there are no SNP-PTM records of RN5A_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
HTF4_HUMAN	TCF12	physical	25416956

Drug and Disease Associations

• Kegg Disease
• There are no disease associations of PTM sites.
• OMIM Disease
• 601518: Prostate cancer, hereditary, 1 (HPC1)
• Kegg Drug
• There are no disease associations of PTM sites.
• DrugBank
• There are no disease associations of PTM sites.

Related Literatures of Post-Translational Modification

Acetylation

"Lysine acetylation targets protein complexes and co-regulates majorcellular functions.";
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.,Olsen J.V., Mann M.;
Science 325:834-840(2009).
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-684, AND MASS SPECTROMETRY.
PubMed: 19608861