dbPTM

LS14A_MOUSE - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	LS14A_MOUSE
UniProt AC	Q8K2F8
Protein Name	Protein LSM14 homolog A
Gene Name	Lsm14a
Organism	Mus musculus (Mouse).
Sequence Length	462
Subcellular Localization	Cytoplasm, P-body . Cytoplasm, Stress granule .
Protein Description	Essential for formation of P-bodies, cytoplasmic structures that provide storage sites for non-translating mRNAs..
Protein Sequence	MSGGTPYIGSKISLISKAEIRYEGILYTIDTENSTVALAKVRSFGTEDRPTDRPIPPRDEVFEYIIFRGSDIKDLTVCEPPKPQCSLPQDPAIVQSSLGSSSSSFQSVGSYGPFGRMPAYSQFSPSTLVGQQFGAVGVAGNSLTSFGTEASNSGTLSQSNAVGSAFTQDTRSVKPQLAQGRSSPQLDPLRKSPTMEQAVQTASAHLPAPAPVGRRSPVPARPLPPTSQKAIDNQEHRRAEVHKVPRPENEQLRNDKRQVVPGVPSAPRRGRGGHRGGRGRFGIRRDGPMKFEKDFDFESANAQFNKEEIDREFHNKLKLKEDKLEKQEKPVNGEDKGDSGVDTQNSEGNADEEDPLGPNCYYDKTKSFFDNISCDDNRERRPTWAEERRLNAETFGIPLRPNRGRGGYRGRGGLGFRGGRGRGSGRGGTFTAPRGFRAGFRGARGGREFADFEYRKTTAFGP

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
2	Acetylation	------MSGGTPYIG ------CCCCCCCCC	46.02	-
5	Phosphorylation	---MSGGTPYIGSKI ---CCCCCCCCCCEE	19.22	29233185
7	Phosphorylation	-MSGGTPYIGSKISL -CCCCCCCCCCEEEE	20.11	29233185
11	Acetylation	GTPYIGSKISLISKA CCCCCCCEEEEEEEC	30.97	22826441
17	Acetylation	SKISLISKAEIRYEG CEEEEEEECEEEECE	42.94	22826441
182	Phosphorylation	PQLAQGRSSPQLDPL HHHHCCCCCCCCCCC	53.87	27087446
183	Phosphorylation	QLAQGRSSPQLDPLR HHHCCCCCCCCCCCC	18.46	27087446
192	Phosphorylation	QLDPLRKSPTMEQAV CCCCCCCCCHHHHHH	21.11	27087446
194	Phosphorylation	DPLRKSPTMEQAVQT CCCCCCCHHHHHHHH	40.19	25521595
201	Phosphorylation	TMEQAVQTASAHLPA HHHHHHHHHHHCCCC	18.91	27742792
203	Phosphorylation	EQAVQTASAHLPAPA HHHHHHHHHCCCCCC	21.43	27742792
216	Phosphorylation	PAPVGRRSPVPARPL CCCCCCCCCCCCCCC	28.96	27087446
226	Phosphorylation	PARPLPPTSQKAIDN CCCCCCCCCHHHCCC	41.68	20531401
227	Phosphorylation	ARPLPPTSQKAIDNQ CCCCCCCCHHHCCCH	35.14	25619855
326	Acetylation	LKEDKLEKQEKPVNG CCHHHHHHCCCCCCC	74.35	7625371
336	Acetylation	KPVNGEDKGDSGVDT CCCCCCCCCCCCCCC	61.38	7625383
339	Phosphorylation	NGEDKGDSGVDTQNS CCCCCCCCCCCCCCC	49.76	23984901
343	Phosphorylation	KGDSGVDTQNSEGNA CCCCCCCCCCCCCCC	27.52	25168779
346	Phosphorylation	SGVDTQNSEGNADEE CCCCCCCCCCCCCCC	36.74	25521595
361	Phosphorylation	DPLGPNCYYDKTKSF CCCCCCCCCCCCHHH	22.72	25168779
362	Phosphorylation	PLGPNCYYDKTKSFF CCCCCCCCCCCHHHH	17.11	25168779
367	Phosphorylation	CYYDKTKSFFDNISC CCCCCCHHHHHCCCC	36.06	22324799
373	Phosphorylation	KSFFDNISCDDNRER HHHHHCCCCCCCCCC	20.11	21884089
383	Phosphorylation	DNRERRPTWAEERRL CCCCCCCCHHHHHHH	35.18	11939611
400	Asymmetric dimethylarginine	ETFGIPLRPNRGRGG HHHCCCCCCCCCCCC	22.54	-
400	Methylation	ETFGIPLRPNRGRGG HHHCCCCCCCCCCCC	22.54	24129315
454	Phosphorylation	REFADFEYRKTTAFG CCCCCCEEEECCCCC	19.87	22374951

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

Modified Location	Modified Residue	Modification	Type of Upstream Proteins	Gene Name of Upstream Proteins	UniProt AC of Upstream Proteins	Sources
Oops, there are no upstream regulatory protein records of LS14A_MOUSE !!

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of LS14A_MOUSE !!

Disease-associated PTM Sites based on SAP

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

Modified Location	Modification	Variant Position (Distance <= 10)	Residue Change	SAP	Related Disease	Reference
Oops, there are no SNP-PTM records of LS14A_MOUSE !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
DDX6_HUMAN	DDX6	physical	20360068
ANM1_HUMAN	PRMT1	physical	20360068
LS14A_HUMAN	LSM14A	physical	20360068
C1QBP_HUMAN	C1QBP	physical	20360068

Drug and Disease Associations

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

Regulatory Network of LS14A_MOUSE

Related Literatures of Post-Translational Modification

Phosphorylation
Reference	PubMed
"Large scale localization of protein phosphorylation by use ofelectron capture dissociation mass spectrometry."; Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.; Mol. Cell. Proteomics 8:904-912(2009). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-216, AND MASSSPECTROMETRY.	19131326 [Abstract]
"The phagosomal proteome in interferon-gamma-activated macrophages."; Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,Thibault P.; Immunity 30:143-154(2009). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-216, AND MASSSPECTROMETRY.	19144319 [Abstract]
"Large-scale phosphorylation analysis of mouse liver."; Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.; Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-183, AND MASSSPECTROMETRY.	17242355 [Abstract]