EMAL4_MOUSE - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: EMAL4_MOUSE
• UniProt AC: Q3UMY5
• Protein Name: Echinoderm microtubule-associated protein-like 4
• Gene Name: Eml4
• Organism: Mus musculus (Mouse).
• Sequence Length: 988
• Subcellular Localization: Cytoplasm, cytoskeleton .
• Protein Description: May modify the assembly dynamics of microtubules, such that microtubules are slightly longer, but more dynamic..
• Protein Sequence: MDGFAGSLDDSISAASTSDVQDRLSALESRVQQQEDEITVLKAALADVLRRLAISEDHVASVKKSMPSKGQPSLREAISMSCITNGSGISRKQNHTSSVSIARKETLSSAAKSGTEKKKEKPQGQREKKEDSHSNDQSPQIRASPSPQPSSQPLQINRQTPESKSSAPIKSIKRPPTAEKSHNSWENSDDSRNKLMKTVSTSKLISKVIKNADKHKDVIVNQAKMSTREKNSQEGEYIKMFMRGRPITMFIPSDVDNYDDIRTELPPEKLKLEWVYGYRGKDCRANVYLLPTGEIVYFIASVVVLFNYEERTQRHYLGHTDCVRCLAVHPDKIRIATGQIAGVDKDGRPLQPHVRVWDSVSLTTLHVIGLGTFERGVGCLDFSKADSGVHLCVIDDSNEHMLTVWDWQKKSKIAEIKTTNEVVLAVEFHPTDANTIITCGKSHIFFWTWSGNSLTRKQGIFGKYEKPKFVQCLAFLGNGDVLTGDSGGVMLIWSKTMVEPPPGKGPKGVYQINRQIKAHDGSVFTLCQMRNGMLLTGGGKDRKIILWDHDLNLEREIEVPDQYGTIRAVAEGRAEQFLVGTSRNFILRGTFNDGFQIEVQGHRDELWGLATHPFKDLLLTCAQDRQVCMWNSVEHRLEWTRLVDEPGHCADFHPSGTVVAIGTHSGRWFVLDAETRDLVSIHTDGNEQLSVMRYSVDGTLLAVGSHDNFIYLYTVLENGRKYSRYGKCTGHSSYITHLDWSPDNKHIMSNSGDYEILYWDIENGCKLIRNRSDCKDIDWTTYTCVLGFQVFGVWPEGSDGTDINALVRSHNRRVIAVADDFCKVHLFQYPCSKAKAPSHKYSAHSSHVTNVSFTHNDSHLISTGGKDMSIIQWKLVEKLPVPQNEVITDASVTKTPASSSETARPSNSPPLPPSLPLTGTAEEESRMGSSPTLVENSLEQIAEPSEEQSEWGSEDLGVVIDEEPASELSETQGATELPEEERGITPLC

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
1	Acetylation	-------MDGFAGSL -------CCCCCCCC	11.67	-
7	Phosphorylation	-MDGFAGSLDDSISA -CCCCCCCCCCCCCC	25.79	30635358
11	Phosphorylation	FAGSLDDSISAASTS CCCCCCCCCCCCCCH	20.36	30635358
13	Phosphorylation	GSLDDSISAASTSDV CCCCCCCCCCCCHHH	23.02	30635358
16	Phosphorylation	DDSISAASTSDVQDR CCCCCCCCCHHHHHH	28.32	29514104
17	Phosphorylation	DSISAASTSDVQDRL CCCCCCCCHHHHHHH	24.99	30635358
18	Phosphorylation	SISAASTSDVQDRLS CCCCCCCHHHHHHHH	33.03	30635358
61	Phosphorylation	ISEDHVASVKKSMPS CCHHHHHHHHHHCCC	33.12	-
79	Phosphorylation	PSLREAISMSCITNG CCHHHHHHHHHHCCC	16.22	25521595
81	Phosphorylation	LREAISMSCITNGSG HHHHHHHHHHCCCCC	8.79	28066266
84	Phosphorylation	AISMSCITNGSGISR HHHHHHHCCCCCCCC	37.54	23140645
96	Phosphorylation	ISRKQNHTSSVSIAR CCCCCCCCCCCEEEH	30.19	18846507
97	Phosphorylation	SRKQNHTSSVSIARK CCCCCCCCCCEEEHH	22.61	18846507
98	Phosphorylation	RKQNHTSSVSIARKE CCCCCCCCCEEEHHH	22.50	18846507
100 (in isoform 2)	Phosphorylation	-	16.69	29514104
100	Phosphorylation	QNHTSSVSIARKETL CCCCCCCEEEHHHHH	16.69	22817900
104 (in isoform 3)	Phosphorylation	-	46.13	29514104
132	Phosphorylation	QREKKEDSHSNDQSP HHHHCCCCCCCCCCC	29.88	26824392
134	Phosphorylation	EKKEDSHSNDQSPQI HHCCCCCCCCCCCCC	46.16	25521595
138	Phosphorylation	DSHSNDQSPQIRASP CCCCCCCCCCCCCCC	22.95	25521595
144	Phosphorylation	QSPQIRASPSPQPSS CCCCCCCCCCCCCCC	18.96	25521595
146	Phosphorylation	PQIRASPSPQPSSQP CCCCCCCCCCCCCCC	33.40	27087446
150	Phosphorylation	ASPSPQPSSQPLQIN CCCCCCCCCCCCEEC	36.04	22942356
151	Phosphorylation	SPSPQPSSQPLQINR CCCCCCCCCCCEECC	42.36	25619855
160	Phosphorylation	PLQINRQTPESKSSA CCEECCCCCCCCCCC	26.28	25266776
163	Phosphorylation	INRQTPESKSSAPIK ECCCCCCCCCCCCCC	38.76	26745281
171	Phosphorylation	KSSAPIKSIKRPPTA CCCCCCCCCCCCCCC	33.78	22817900
181	Phosphorylation	RPPTAEKSHNSWENS CCCCCCCCCCCCCCC	21.29	29550500
184	Phosphorylation	TAEKSHNSWENSDDS CCCCCCCCCCCCHHH	30.28	23684622
200	Phosphorylation	NKLMKTVSTSKLISK HHHHHHHHHHHHHHH	31.99	22942356
201	Phosphorylation	KLMKTVSTSKLISKV HHHHHHHHHHHHHHH	26.08	-
232	Phosphorylation	MSTREKNSQEGEYIK CCCCCCCCCCCHHHH	40.45	25367039
237	Phosphorylation	KNSQEGEYIKMFMRG CCCCCCHHHHHHCCC	19.39	25367039
248	Phosphorylation	FMRGRPITMFIPSDV HCCCCCEEEEECCCC	14.54	25338131
337	Phosphorylation	PDKIRIATGQIAGVD CCCEEEEECCCCCCC	27.52	-
620	Phosphorylation	PFKDLLLTCAQDRQV CHHHHHHHHHCCCCE	13.03	-
694	Phosphorylation	EQLSVMRYSVDGTLL CEEEEEEEEECCEEE	8.58	22871156
713	Phosphorylation	HDNFIYLYTVLENGR CCCEEEEEEEECCCE	4.28	22871156
714	Phosphorylation	DNFIYLYTVLENGRK CCEEEEEEEECCCEE	18.93	22871156
895	Phosphorylation	TDASVTKTPASSSET CCCCCCCCCCCCCCC	18.09	26239621
898	Phosphorylation	SVTKTPASSSETARP CCCCCCCCCCCCCCC	35.28	26239621
899	Phosphorylation	VTKTPASSSETARPS CCCCCCCCCCCCCCC	34.01	26239621
900	Phosphorylation	TKTPASSSETARPSN CCCCCCCCCCCCCCC	36.15	26239621
902	Phosphorylation	TPASSSETARPSNSP CCCCCCCCCCCCCCC	29.89	26239621
906	Phosphorylation	SSETARPSNSPPLPP CCCCCCCCCCCCCCC	44.37	26824392
908	Phosphorylation	ETARPSNSPPLPPSL CCCCCCCCCCCCCCC	32.03	25521595
914	Phosphorylation	NSPPLPPSLPLTGTA CCCCCCCCCCCCCCH	40.45	28609623
918	Phosphorylation	LPPSLPLTGTAEEES CCCCCCCCCCHHHHH	30.46	28609623
920	Phosphorylation	PSLPLTGTAEEESRM CCCCCCCCHHHHHHC	26.17	28609623
985	Phosphorylation	PEEERGITPLC---- CHHHCCCCCCC----	17.03	25521595

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

Oops, there are no upstream regulatory protein records of EMAL4_MOUSE !!

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
144	S	Phosphorylation	Phosphorylation at Ser-144 and Ser-146 promotes its dissociation from microtubules during mitosis which is required for efficient chromosome congression (By similarity).	21183079
146	S	Phosphorylation	Phosphorylation at Ser-144 and Ser-146 promotes its dissociation from microtubules during mitosis which is required for efficient chromosome congression (By similarity).	21183079

Disease-associated PTM Sites based on SAP

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

Oops, there are no SNP-PTM records of EMAL4_MOUSE !!

Protein-Protein Interaction

Oops, there are no PPI records of EMAL4_MOUSE !!

Drug and Disease Associations

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

Related Literatures of Post-Translational Modification

Phosphorylation

"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-144, AND MASSSPECTROMETRY.
PubMed: 17242355