ERI1_HUMAN - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: ERI1_HUMAN
• UniProt AC: Q8IV48
• Protein Name: 3'-5' exoribonuclease 1
• Gene Name: ERI1
• Organism: Homo sapiens (Human).
• Sequence Length: 349
• Subcellular Localization: Cytoplasm . Nucleus . Nucleus, nucleolus .
• Protein Description: RNA exonuclease that binds to the 3'-end of histone mRNAs and degrades them, suggesting that it plays an essential role in histone mRNA decay after replication. A 2' and 3'-hydroxyl groups at the last nucleotide of the histone 3'-end is required for efficient degradation of RNA substrates. Also able to degrade the 3'-overhangs of short interfering RNAs (siRNAs) in vitro, suggesting a possible role as regulator of RNA interference (RNAi). Requires for binding the 5'-ACCCA-3' sequence present in stem-loop structure. Able to bind other mRNAs. Required for 5.8S rRNA 3'-end processing. Also binds to 5.8s ribosomal RNA. Binds with high affinity to the stem-loop structure of replication-dependent histone pre-mRNAs..
• Protein Sequence: MEDPQSKEPAGEAVALALLESPRPEGGEEPPRPSPEETQQCKFDGQETKGSKFITSSASDFSDPVYKEIAITNGCINRMSKEELRAKLSEFKLETRGVKDVLKKRLKNYYKKQKLMLKESNFADSYYDYICIIDFEATCEEGNPPEFVHEIIEFPVVLLNTHTLEIEDTFQQYVRPEINTQLSDFCISLTGITQDQVDRADTFPQVLKKVIDWMKLKELGTKYKYSLLTDGSWDMSKFLNIQCQLSRLKYPPFAKKWINIRKSYGNFYKVPRSQTKLTIMLEKLGMDYDGRPHCGLDDSKNIARIAVRMLQDGCELRINEKMHAGQLMSVSSSLPIEGTPPPQMPHFRK

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
21	Phosphorylation	VALALLESPRPEGGE HHHHHHCCCCCCCCC	26.61	26657352
34	Phosphorylation	GEEPPRPSPEETQQC CCCCCCCCHHHHHCC	46.34	29116813
38	Phosphorylation	PRPSPEETQQCKFDG CCCCHHHHHCCCCCC	23.44	26074081
49	Sumoylation	KFDGQETKGSKFITS CCCCCCCCCCCEECC	61.51	-
49	Sumoylation	KFDGQETKGSKFITS CCCCCCCCCCCEECC	61.51	-
49	Ubiquitination	KFDGQETKGSKFITS CCCCCCCCCCCEECC	61.51	-
52	Ubiquitination	GQETKGSKFITSSAS CCCCCCCCEECCCHH	49.83	21890473
52	Acetylation	GQETKGSKFITSSAS CCCCCCCCEECCCHH	49.83	25953088
52	Sumoylation	GQETKGSKFITSSAS CCCCCCCCEECCCHH	49.83	-
52	Sumoylation	GQETKGSKFITSSAS CCCCCCCCEECCCHH	49.83	-
55	Phosphorylation	TKGSKFITSSASDFS CCCCCEECCCHHHCC	21.55	21945579
56	Phosphorylation	KGSKFITSSASDFSD CCCCEECCCHHHCCC	21.06	21945579
57	Phosphorylation	GSKFITSSASDFSDP CCCEECCCHHHCCCC	24.12	21945579
59	Phosphorylation	KFITSSASDFSDPVY CEECCCHHHCCCCCH	40.93	21945579
62	Phosphorylation	TSSASDFSDPVYKEI CCCHHHCCCCCHHHH	46.09	21945579
66	Phosphorylation	SDFSDPVYKEIAITN HHCCCCCHHHHHHHC	14.32	21945579
67	Acetylation	DFSDPVYKEIAITNG HCCCCCHHHHHHHCC	42.76	30592947
67	Ubiquitination	DFSDPVYKEIAITNG HCCCCCHHHHHHHCC	42.76	-
72	Phosphorylation	VYKEIAITNGCINRM CHHHHHHHCCHHHHC	19.28	22210691
81	Sumoylation	GCINRMSKEELRAKL CHHHHCCHHHHHHHH	45.95	-
81	Ubiquitination	GCINRMSKEELRAKL CHHHHCCHHHHHHHH	45.95	-
81	Sumoylation	GCINRMSKEELRAKL CHHHHCCHHHHHHHH	45.95	-
87	Ubiquitination	SKEELRAKLSEFKLE CHHHHHHHHHHHHHH	46.22	-
89	Phosphorylation	EELRAKLSEFKLETR HHHHHHHHHHHHHHH	40.04	28555341
92	Ubiquitination	RAKLSEFKLETRGVK HHHHHHHHHHHHCHH	41.17	-
99	Acetylation	KLETRGVKDVLKKRL HHHHHCHHHHHHHHH	44.97	70817
103	Ubiquitination	RGVKDVLKKRLKNYY HCHHHHHHHHHHHHH	35.38	-
217	2-Hydroxyisobutyrylation	VIDWMKLKELGTKYK HHHHHHHHHHCCCCC	45.43	-
217	Ubiquitination	VIDWMKLKELGTKYK HHHHHHHHHHCCCCC	45.43	-
222	Ubiquitination	KLKELGTKYKYSLLT HHHHHCCCCCEEEEC	37.64	-
249	Acetylation	QCQLSRLKYPPFAKK HHHHHCCCCCCHHHH	55.38	25953088
249	Malonylation	QCQLSRLKYPPFAKK HHHHHCCCCCCHHHH	55.38	26320211
249	Ubiquitination	QCQLSRLKYPPFAKK HHHHHCCCCCCHHHH	55.38	-
262	Ubiquitination	KKWINIRKSYGNFYK HHHHEEEHHHCCCCC	44.20	-
269	Ubiquitination	KSYGNFYKVPRSQTK HHHCCCCCCCHHHCH	41.44	21890473
273	Phosphorylation	NFYKVPRSQTKLTIM CCCCCCHHHCHHHHH	35.81	27067055
275	Phosphorylation	YKVPRSQTKLTIMLE CCCCHHHCHHHHHHH	29.30	27067055
276	Ubiquitination	KVPRSQTKLTIMLEK CCCHHHCHHHHHHHH	35.68	-
300	Ubiquitination	HCGLDDSKNIARIAV CCCCCCCHHHHHHHH	60.41	-
339	Phosphorylation	SSLPIEGTPPPQMPH CCCCCCCCCCCCCCC	21.60	28555341

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

Oops, there are no upstream regulatory protein records of ERI1_HUMAN !!

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of ERI1_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 ERI1_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
HNRPD_HUMAN	HNRNPD	physical	22863883

Drug and Disease Associations

• Kegg Disease
• There are no disease associations of PTM sites.
• OMIM Disease
• There are no disease associations of PTM sites.
• 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

Phosphorylation

"Quantitative phosphoproteomic analysis of T cell receptor signalingreveals system-wide modulation of protein-protein interactions.";
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,Rodionov V., Han D.K.;
Sci. Signal. 2:RA46-RA46(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-62, AND MASSSPECTROMETRY.
PubMed: 19690332