ERI1_MOUSE - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: ERI1_MOUSE
• UniProt AC: Q7TMF2
• Protein Name: 3'-5' exoribonuclease 1
• Gene Name: Eri1
• Organism: Mus musculus (Mouse).
• Sequence Length: 345
• 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). Binds with high affinity to the 3' side of the stem-loop structure and to the downstream cleavage product (DCP) of histone pre-mRNAs. Requires for binding the 5'-ACCCA-3' sequence present in stem-loop structure. Able to bind other mRNAs (By similarity). Required for 5.8S rRNA 3'-end processing. Also binds to 5.8s ribosomal RNA..
• Protein Sequence: MEDERGRERGGDAAQQKTPRPECEESRPLSVEKKQRCRLDGKETDGSKFISSNGSDFSDPVYKEIAMTNGCINRMSKEELRAKLSEFKLETRGVKDVLKKRLKNYYKKQKLMLKESSAGDSYYDYICIIDFEATCEEGNPAEFLHEIIEFPVVLLNTHTLEIEDTFQQYVRPEVNAQLSEFCIGLTGITQDQVDRADAFPQVLKKVIEWMKSKELGTKYKYCILTDGSWDMSKFLSIQCRLSRLKHPAFAKKWINIRKSYGNFYKVPRSQTKLTIMLEKLGMDYDGRPHSGLDDSKNIARIAVRMLQDGCELRINEKILGGQLMSVSSSLPVEGAPAPQMPHSRK

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
18	Phosphorylation	GDAAQQKTPRPECEE CCHHHCCCCCCCCCC	21.86	27149854
26	Phosphorylation	PRPECEESRPLSVEK CCCCCCCCCCCCHHH	19.53	25159016
30	Phosphorylation	CEESRPLSVEKKQRC CCCCCCCCHHHHHCC	30.80	26824392
47	Phosphorylation	DGKETDGSKFISSNG CCCCCCCCCCCCCCC	27.48	28059163
51	Phosphorylation	TDGSKFISSNGSDFS CCCCCCCCCCCCCCC	22.38	26643407
52	Phosphorylation	DGSKFISSNGSDFSD CCCCCCCCCCCCCCC	40.15	26643407
55	Phosphorylation	KFISSNGSDFSDPVY CCCCCCCCCCCCHHH	39.47	26745281
58	Phosphorylation	SSNGSDFSDPVYKEI CCCCCCCCCHHHHHH	46.09	26745281
62	Phosphorylation	SDFSDPVYKEIAMTN CCCCCHHHHHHHHHC	14.32	22817900
85	Phosphorylation	EELRAKLSEFKLETR HHHHHHHHHHHHHHH	40.04	29514104
99	Ubiquitination	RGVKDVLKKRLKNYY HCHHHHHHHHHHHHH	35.38	-
100	Ubiquitination	GVKDVLKKRLKNYYK CHHHHHHHHHHHHHH	59.82	-
116	Phosphorylation	QKLMLKESSAGDSYY HCEECCCCCCCCCCC	24.73	-
117	Phosphorylation	KLMLKESSAGDSYYD CEECCCCCCCCCCCE	37.04	-
245	Ubiquitination	QCRLSRLKHPAFAKK HHHHHHCCCHHHHHH	46.57	22790023
252	Acetylation	KHPAFAKKWINIRKS CCHHHHHHHHHHHHH	50.29	22826441

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

Oops, there are no upstream regulatory protein records of ERI1_MOUSE !!

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of ERI1_MOUSE !!

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_MOUSE !!

Protein-Protein Interaction

Oops, there are no PPI records of ERI1_MOUSE !!

Drug and Disease Associations

• Kegg Drug
• DrugBank
• There are no disease associations of PTM sites.