dbPTM

EMD_MOUSE - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	EMD_MOUSE
UniProt AC	O08579
Protein Name	Emerin
Gene Name	Emd
Organism	Mus musculus (Mouse).
Sequence Length	259
Subcellular Localization	Nucleus inner membrane Single-pass membrane protein Nucleoplasmic side . Nucleus outer membrane. Colocalized with BANF1 at the central region of the assembling nuclear rim, near spindle-attachment sites. The accumulation of different intermediates
Protein Description	Stabilizes and promotes the formation of a nuclear actin cortical network. Stimulates actin polymerization in vitro by binding and stabilizing the pointed end of growing filaments. Inhibits beta-catenin activity by preventing its accumulation in the nucleus. Acts by influencing the nuclear accumulation of beta-catenin through a CRM1-dependent export pathway. Links centrosomes to the nuclear envelope via a microtubule association. Required for proper localization of non-farnesylated prelamin-A/C (By similarity)..
Protein Sequence	MDDYAVLSDTELAAVLRQYNIPHGPIVGSTRKLYEKKIFEYETQRRRLLPPNSSSSSFSYQFSDLDSAAVDSDMYDLPKKEDALLYQSKDYNDDYYEESYLTTKTYGEPESVGMSKSFRQPGTSLVDADTFHHQVRDDIFSSLEEEGKDRERLIYGQDSAYQSIAHYRPISNVSRSSLGLSYYPTSSTSSVSSSSSSPSSWLTRRAIRPEKQAPAAALGQDRQVPLWGQLLLFLVFAAFLLFVYYSIQAEEGNPFWMDP

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
1	Acetylation	-------MDDYAVLS -------CCCEEECC	8.80	-
8	Phosphorylation	MDDYAVLSDTELAAV CCCEEECCHHHHHHH	35.57	28066266
10	Phosphorylation	DYAVLSDTELAAVLR CEEECCHHHHHHHHH	29.53	28066266
29	Phosphorylation	PHGPIVGSTRKLYEK CCCCCCCCCHHHHHH	17.72	25266776
30	Phosphorylation	HGPIVGSTRKLYEKK CCCCCCCCHHHHHHH	26.37	28066266
37	Malonylation	TRKLYEKKIFEYETQ CHHHHHHHHHHHHHH	40.46	26320211
37	Ubiquitination	TRKLYEKKIFEYETQ CHHHHHHHHHHHHHH	40.46	-
41	Phosphorylation	YEKKIFEYETQRRRL HHHHHHHHHHHHCCC	17.33	25159016
43	Phosphorylation	KKIFEYETQRRRLLP HHHHHHHHHHCCCCC	26.86	25159016
53	Phosphorylation	RRLLPPNSSSSSFSY CCCCCCCCCCCCCEE	37.05	23984901
54	Phosphorylation	RLLPPNSSSSSFSYQ CCCCCCCCCCCCEEE	40.66	23984901
55	Phosphorylation	LLPPNSSSSSFSYQF CCCCCCCCCCCEEEC	29.80	23984901
56	Phosphorylation	LPPNSSSSSFSYQFS CCCCCCCCCCEEECC	37.03	23984901
57	Phosphorylation	PPNSSSSSFSYQFSD CCCCCCCCCEEECCC	21.84	23984901
59	Phosphorylation	NSSSSSFSYQFSDLD CCCCCCCEEECCCCC	21.70	23984901
60	Phosphorylation	SSSSSFSYQFSDLDS CCCCCCEEECCCCCC	16.15	23984901
63	Phosphorylation	SSFSYQFSDLDSAAV CCCEEECCCCCCCCC	23.03	23984901
67	Phosphorylation	YQFSDLDSAAVDSDM EECCCCCCCCCCCCC	25.98	23984901
72	Phosphorylation	LDSAAVDSDMYDLPK CCCCCCCCCCCCCCC	20.06	23984901
75	Phosphorylation	AAVDSDMYDLPKKED CCCCCCCCCCCCHHC	21.22	16857009
80	Ubiquitination	DMYDLPKKEDALLYQ CCCCCCCHHCCEEEC	59.91	22790023
86	Phosphorylation	KKEDALLYQSKDYND CHHCCEEECCCCCCC	16.16	25159016
88	Phosphorylation	EDALLYQSKDYNDDY HCCEEECCCCCCCCC	17.59	26824392
89	Ubiquitination	DALLYQSKDYNDDYY CCEEECCCCCCCCCC	49.02	-
91	Phosphorylation	LLYQSKDYNDDYYEE EEECCCCCCCCCCCC	24.99	27149854
95	Phosphorylation	SKDYNDDYYEESYLT CCCCCCCCCCCHHEE	18.68	16857009
96	Phosphorylation	KDYNDDYYEESYLTT CCCCCCCCCCHHEEE	21.88	22817900
99	Phosphorylation	NDDYYEESYLTTKTY CCCCCCCHHEEEEEC	17.32	27149854
100	Phosphorylation	DDYYEESYLTTKTYG CCCCCCHHEEEEECC	16.02	27149854
102	Phosphorylation	YYEESYLTTKTYGEP CCCCHHEEEEECCCC	20.29	27149854
103	Phosphorylation	YEESYLTTKTYGEPE CCCHHEEEEECCCCC	20.85	27149854
104	Ubiquitination	EESYLTTKTYGEPES CCHHEEEEECCCCCC	34.22	-
105	Phosphorylation	ESYLTTKTYGEPESV CHHEEEEECCCCCCC	34.37	25159016
106	Phosphorylation	SYLTTKTYGEPESVG HHEEEEECCCCCCCC	22.50	25159016
111	Phosphorylation	KTYGEPESVGMSKSF EECCCCCCCCCCCCC	34.39	29514104
116	Ubiquitination	PESVGMSKSFRQPGT CCCCCCCCCCCCCCC	44.73	22790023
117	Phosphorylation	ESVGMSKSFRQPGTS CCCCCCCCCCCCCCC	20.53	25266776
123	Phosphorylation	KSFRQPGTSLVDADT CCCCCCCCCCEECCC	26.10	28833060
124	Phosphorylation	SFRQPGTSLVDADTF CCCCCCCCCEECCCC	32.10	28833060
130	Phosphorylation	TSLVDADTFHHQVRD CCCEECCCCHHHHHH	26.96	28066266
141	Phosphorylation	QVRDDIFSSLEEEGK HHHHHHHHHHHHCCC	34.06	21082442
142	Phosphorylation	VRDDIFSSLEEEGKD HHHHHHHHHHHCCCC	29.11	25521595
148	Ubiquitination	SSLEEEGKDRERLIY HHHHHCCCCHHHEEE	57.82	-
155	Phosphorylation	KDRERLIYGQDSAYQ CCHHHEEECCCCHHH	17.21	25159016
159	Phosphorylation	RLIYGQDSAYQSIAH HEEECCCCHHHHHCC	22.46	25159016
161	Phosphorylation	IYGQDSAYQSIAHYR EECCCCHHHHHCCCC	13.52	25159016
163	Phosphorylation	GQDSAYQSIAHYRPI CCCCHHHHHCCCCCC	14.74	25367039
167	Phosphorylation	AYQSIAHYRPISNVS HHHHHCCCCCCCCCC	14.73	25159016
171	Phosphorylation	IAHYRPISNVSRSSL HCCCCCCCCCCHHHC	33.58	25159016
174	Phosphorylation	YRPISNVSRSSLGLS CCCCCCCCHHHCCCE	30.60	25159016
176	Phosphorylation	PISNVSRSSLGLSYY CCCCCCHHHCCCEEC	23.55	26643407
177	Phosphorylation	ISNVSRSSLGLSYYP CCCCCHHHCCCEECC	25.91	26643407
181	Phosphorylation	SRSSLGLSYYPTSST CHHHCCCEECCCCCC	22.33	26643407
185	Phosphorylation	LGLSYYPTSSTSSVS CCCEECCCCCCCCCC	21.13	23984901
186	Phosphorylation	GLSYYPTSSTSSVSS CCEECCCCCCCCCCC	27.41	23984901
187	Phosphorylation	LSYYPTSSTSSVSSS CEECCCCCCCCCCCC	34.48	23984901
188	Phosphorylation	SYYPTSSTSSVSSSS EECCCCCCCCCCCCC	25.45	23984901
189	Phosphorylation	YYPTSSTSSVSSSSS ECCCCCCCCCCCCCC	30.59	23984901
190	Phosphorylation	YPTSSTSSVSSSSSS CCCCCCCCCCCCCCC	26.55	23649490
192	Phosphorylation	TSSTSSVSSSSSSPS CCCCCCCCCCCCCCC	26.84	23984901
193	Phosphorylation	SSTSSVSSSSSSPSS CCCCCCCCCCCCCCC	31.89	23984901
194	Phosphorylation	STSSVSSSSSSPSSW CCCCCCCCCCCCCCH	27.08	23984901
195	Phosphorylation	TSSVSSSSSSPSSWL CCCCCCCCCCCCCHH	36.46	23984901
196	Phosphorylation	SSVSSSSSSPSSWLT CCCCCCCCCCCCHHH	48.49	23984901
197	Phosphorylation	SVSSSSSSPSSWLTR CCCCCCCCCCCHHHH	30.65	23984901
199	Phosphorylation	SSSSSSPSSWLTRRA CCCCCCCCCHHHHHH	35.77	23984901
200	Phosphorylation	SSSSSPSSWLTRRAI CCCCCCCCHHHHHHC	29.50	23984901
203	Phosphorylation	SSPSSWLTRRAIRPE CCCCCHHHHHHCCHH	16.32	23984901

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
75	Y	Phosphorylation	Kinase	SRC	P05480	PSP
96	Y	Phosphorylation	Kinase	SRC	P05480	PSP

Functions of PTM Sites

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

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference	Domain-Domain Interactions
Oops, there are no PPI records of EMD_MOUSE !!

Drug and Disease Associations

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

Regulatory Network of EMD_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 TYR-161, AND MASSSPECTROMETRY.	19131326 [Abstract]