dbPTM

EMAL3_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	EMAL3_HUMAN
UniProt AC	Q32P44
Protein Name	Echinoderm microtubule-associated protein-like 3
Gene Name	EML3
Organism	Homo sapiens (Human).
Sequence Length	896
Subcellular Localization	Cytoplasm, cytoskeleton .
Protein Description	May modify the assembly dynamics of microtubules, such that microtubules are slightly longer, but more dynamic..
Protein Sequence	MDGAAGPGDGPAREALQSLSQRLRVQEQEMELVKAALAEALRLLRLQVPPSSLQGSGTPAPPGDSLAAPPGLPPTCTPSLVSRGTQTETEVELKSSPGPPGLSNGPPAPQGASEEPSGTQSEGGGSSSSGAGSPGPPGILRPLQPPQRADTPRRNSSSSSSPSERPRQKLSRKAISSANLLVRSGSTESRGGKDPLSSPGGPGSRRSNYNLEGISVKMFLRGRPITMYIPSGIRSLEELPSGPPPETLSLDWVYGYRGRDSRSNLFVLRSGEVVYFIACVVVLYRPGGGPGGPGGGGQRHYRGHTDCVRCLAVHPDGVRVASGQTAGVDKDGKPLQPVVHIWDSETLLKLQEIGLGAFERGVGALAFSAADQGAFLCVVDDSNEHMLSVWDCSRGMKLAEIKSTNDSVLAVGFNPRDSSCIVTSGKSHVHFWNWSGGVGVPGNGTLTRKQGVFGKYKKPKFIPCFVFLPDGDILTGDSEGNILTWGRSPSDSKTPGRGGAKETYGIVAQAHAHEGSIFALCLRRDGTVLSGGGRDRRLVQWGPGLVALQEAEIPEHFGAVRAIAEGLGSELLVGTTKNALLRGDLAQGFSPVIQGHTDELWGLCTHPSQNRFLTCGHDRQLCLWDGESHALAWSIDLKETGLCADFHPSGAVVAVGLNTGRWLVLDTETREIVSDVIDGNEQLSVVRYSPDGLYLAIGSHDNVIYIYSVSSDGAKSSRFGRCMGHSSFITHLDWSKDGNFIMSNSGDYEILYWDVAGGCKQLKNRYESRDREWATYTCVLGFHVYGVWPDGSDGTDINSLCRSHNERVVAVADDFCKVHLFQYPCARAKAPSRMYGGHGSHVTSVRFTHDDSHLVSLGGKDASIFQWRVLGAGGAGPAPATPSRTPSLSPASSLDV

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
1	Acetylation	-------MDGAAGPG -------CCCCCCCC	10.94	22814378
13	Methylation	GPGDGPAREALQSLS CCCCCHHHHHHHHHH	32.62	-
126	Phosphorylation	TQSEGGGSSSSGAGS CCCCCCCCCCCCCCC	30.26	27251275
127	Phosphorylation	QSEGGGSSSSGAGSP CCCCCCCCCCCCCCC	31.62	27251275
128	Phosphorylation	SEGGGSSSSGAGSPG CCCCCCCCCCCCCCC	34.19	22468782
129	Phosphorylation	EGGGSSSSGAGSPGP CCCCCCCCCCCCCCC	34.31	27251275
133	Phosphorylation	SSSSGAGSPGPPGIL CCCCCCCCCCCCCCC	26.58	27251275
156 (in isoform 2)	Phosphorylation	-	29.77	21406692
156	Phosphorylation	ADTPRRNSSSSSSPS CCCCCCCCCCCCCCC	29.77	28355574
157	Phosphorylation	DTPRRNSSSSSSPSE CCCCCCCCCCCCCCC	37.48	27461979
158	Phosphorylation	TPRRNSSSSSSPSER CCCCCCCCCCCCCCC	33.78	27461979
159 (in isoform 2)	Phosphorylation	-	36.46	21406692
159	Phosphorylation	PRRNSSSSSSPSERP CCCCCCCCCCCCCCH	36.46	25159151
160	Phosphorylation	RRNSSSSSSPSERPR CCCCCCCCCCCCCHH	48.49	25159151
161	Phosphorylation	RNSSSSSSPSERPRQ CCCCCCCCCCCCHHH	34.10	25159151
163	Phosphorylation	SSSSSSPSERPRQKL CCCCCCCCCCHHHHH	48.46	23663014
173	Ubiquitination	PRQKLSRKAISSANL HHHHHHHHHHHHCCE	46.85	-
173	Acetylation	PRQKLSRKAISSANL HHHHHHHHHHHHCCE	46.85	7674097
173 (in isoform 2)	Ubiquitination	-	46.85	-
176 (in isoform 2)	Phosphorylation	-	28.40	21406692
176	Phosphorylation	KLSRKAISSANLLVR HHHHHHHHHCCEEEE	28.40	29255136
177	Phosphorylation	LSRKAISSANLLVRS HHHHHHHHCCEEEEC	18.31	22167270
179 (in isoform 3)	Phosphorylation	-	35.54	29052541
184	Phosphorylation	SANLLVRSGSTESRG HCCEEEECCCCCCCC	29.62	29514088
186	Phosphorylation	NLLVRSGSTESRGGK CEEEECCCCCCCCCC	30.19	29514088
187	Phosphorylation	LLVRSGSTESRGGKD EEEECCCCCCCCCCC	41.32	29514088
189	Phosphorylation	VRSGSTESRGGKDPL EECCCCCCCCCCCCC	35.99	29514088
190	Methylation	RSGSTESRGGKDPLS ECCCCCCCCCCCCCC	52.21	-
193 (in isoform 2)	Ubiquitination	-	60.02	-
193	Ubiquitination	STESRGGKDPLSSPG CCCCCCCCCCCCCCC	60.02	-
193	Malonylation	STESRGGKDPLSSPG CCCCCCCCCCCCCCC	60.02	26320211
193 (in isoform 2)	Malonylation	-	60.02	26320211
197	Phosphorylation	RGGKDPLSSPGGPGS CCCCCCCCCCCCCCC	39.62	23401153
198	Phosphorylation	GGKDPLSSPGGPGSR CCCCCCCCCCCCCCC	34.94	23401153
204	Phosphorylation	SSPGGPGSRRSNYNL CCCCCCCCCCCCCCC	27.88	25159151
207	Phosphorylation	GGPGSRRSNYNLEGI CCCCCCCCCCCCCCC	42.42	25159151
209	Phosphorylation	PGSRRSNYNLEGISV CCCCCCCCCCCCCEE	23.52	26852163
231	Phosphorylation	PITMYIPSGIRSLEE EEEEEECCCCCCHHH	36.98	30631047
445	O-linked_Glycosylation	VGVPGNGTLTRKQGV CCCCCCCCEEEECCC	29.02	29351928
445	Phosphorylation	VGVPGNGTLTRKQGV CCCCCCCCEEEECCC	29.02	-
447	Phosphorylation	VPGNGTLTRKQGVFG CCCCCCEEEECCCCC	35.34	-
456	Phosphorylation	KQGVFGKYKKPKFIP ECCCCCCCCCCCEEC	25.32	-
462 (in isoform 3)	Ubiquitination	-	3.47	21890473
488	Phosphorylation	NILTWGRSPSDSKTP CEEEECCCCCCCCCC	25.47	20068231
490	Phosphorylation	LTWGRSPSDSKTPGR EEECCCCCCCCCCCC	56.62	20068231
492	Phosphorylation	WGRSPSDSKTPGRGG ECCCCCCCCCCCCCC	42.65	20068231
494	Phosphorylation	RSPSDSKTPGRGGAK CCCCCCCCCCCCCCC	34.62	20068231
575	O-linked_Glycosylation	GSELLVGTTKNALLR CCEEEEECCCCHHHC	27.41	29351928
577 (in isoform 2)	Ubiquitination	-	39.81	21890473
577 (in isoform 1)	Ubiquitination	-	39.81	21890473
577	Ubiquitination	ELLVGTTKNALLRGD EEEEECCCCHHHCCC	39.81	22053931
634	Phosphorylation	ESHALAWSIDLKETG CCCEEEEEEECHHHC	10.70	24961811
640	Phosphorylation	WSIDLKETGLCADFH EEEECHHHCCCCCCC	33.59	28464451
688	Phosphorylation	EQLSVVRYSPDGLYL CCEEEEEECCCCEEE	16.97	25002506
689	Phosphorylation	QLSVVRYSPDGLYLA CEEEEEECCCCEEEE	13.12	25002506
694	Phosphorylation	RYSPDGLYLAIGSHD EECCCCEEEEECCCC	10.30	25002506
699	Phosphorylation	GLYLAIGSHDNVIYI CEEEEECCCCCEEEE	22.89	25002506
705	Phosphorylation	GSHDNVIYIYSVSSD CCCCCEEEEEEECCC	6.90	25002506
707	Phosphorylation	HDNVIYIYSVSSDGA CCCEEEEEEECCCCC	6.00	25002506
708	Phosphorylation	DNVIYIYSVSSDGAK CCEEEEEEECCCCCC	13.13	25002506
710	Phosphorylation	VIYIYSVSSDGAKSS EEEEEEECCCCCCCC	19.44	25002506
711	Phosphorylation	IYIYSVSSDGAKSSR EEEEEECCCCCCCCC	37.60	25002506
716	Phosphorylation	VSSDGAKSSRFGRCM ECCCCCCCCCCCCCC	26.64	25002506
717	Phosphorylation	SSDGAKSSRFGRCMG CCCCCCCCCCCCCCC	30.81	25002506
817	Acetylation	AVADDFCKVHLFQYP EEECCCCEEEEEECC	32.46	26051181
817	Ubiquitination	AVADDFCKVHLFQYP EEECCCCEEEEEECC	32.46	-
840	Phosphorylation	RMYGGHGSHVTSVRF CCCCCCCCCEEEEEE	14.76	-
843	Phosphorylation	GGHGSHVTSVRFTHD CCCCCCEEEEEECCC	18.97	28857561
844	Phosphorylation	GHGSHVTSVRFTHDD CCCCCEEEEEECCCC	15.37	28857561
847 (in isoform 2)	Phosphorylation	-	7.15	22210691
881	Phosphorylation	GAGPAPATPSRTPSL CCCCCCCCCCCCCCC	22.27	29255136
881	O-linked_Glycosylation	GAGPAPATPSRTPSL CCCCCCCCCCCCCCC	22.27	29351928
883	Phosphorylation	GPAPATPSRTPSLSP CCCCCCCCCCCCCCC	44.42	29255136
883	O-linked_Glycosylation	GPAPATPSRTPSLSP CCCCCCCCCCCCCCC	44.42	29351928
885	Phosphorylation	APATPSRTPSLSPAS CCCCCCCCCCCCCCH	22.90	25159151
887	Phosphorylation	ATPSRTPSLSPASSL CCCCCCCCCCCCHHC	40.65	25159151
889	Phosphorylation	PSRTPSLSPASSLDV CCCCCCCCCCHHCCC	23.82	25159151
892	Phosphorylation	TPSLSPASSLDV--- CCCCCCCHHCCC---	34.51	22617229
893	Phosphorylation	PSLSPASSLDV---- CCCCCCHHCCC----	30.60	22617229
900 (in isoform 2)	Phosphorylation	-		-

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
176	S	Phosphorylation	Kinase	CHEK1	O14757	GPS
881	T	Phosphorylation	Kinase	CDK1	P06493	PSP

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
881	T	Phosphorylation		16964243
Phosphorylation at Thr-881 during mitosis is required for interaction with TUBG1, HAUS1, HAUS2, HAUS3, HAUS4, HAUS5, HAUS6, HAUS7 and HAUS8 and their recruitement to spindle microtubules.

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 EMAL3_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference	Domain-Domain Interactions
EMAL3_HUMAN	EML3	physical	25740311

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.

Regulatory Network of EMAL3_HUMAN

Related Literatures of Post-Translational Modification

Phosphorylation
Reference	PubMed
"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-176, AND MASSSPECTROMETRY.	19690332 [Abstract]
"A quantitative atlas of mitotic phosphorylation."; Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,Elledge S.J., Gygi S.P.; Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-176 AND THR-881, ANDMASS SPECTROMETRY.	18669648 [Abstract]
"A probability-based approach for high-throughput proteinphosphorylation analysis and site localization."; Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.; Nat. Biotechnol. 24:1285-1292(2006). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-176 AND THR-881, ANDMASS SPECTROMETRY.	16964243 [Abstract]
"Combining protein-based IMAC, peptide-based IMAC, and MudPIT forefficient phosphoproteomic analysis."; Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D.,Yates J.R. III; J. Proteome Res. 7:1346-1351(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-881, AND MASSSPECTROMETRY.	18220336 [Abstract]

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