dbPTM

EMAL4_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	EMAL4_HUMAN
UniProt AC	Q9HC35
Protein Name	Echinoderm microtubule-associated protein-like 4
Gene Name	EML4
Organism	Homo sapiens (Human).
Sequence Length	981
Subcellular Localization	Cytoplasm, cytoskeleton .
Protein Description	May modify the assembly dynamics of microtubules, such that microtubules are slightly longer, but more dynamic..
Protein Sequence	MDGFAGSLDDSISAASTSDVQDRLSALESRVQQQEDEITVLKAALADVLRRLAISEDHVASVKKSVSSKGQPSPRAVIPMSCITNGSGANRKPSHTSAVSIAGKETLSSAAKSGTEKKKEKPQGQREKKEESHSNDQSPQIRASPSPQPSSQPLQIHRQTPESKNATPTKSIKRPSPAEKSHNSWENSDDSRNKLSKIPSTPKLIPKVTKTADKHKDVIINQEGEYIKMFMRGRPITMFIPSDVDNYDDIRTELPPEKLKLEWAYGYRGKDCRANVYLLPTGKIVYFIASVVVLFNYEERTQRHYLGHTDCVKCLAIHPDKIRIATGQIAGVDKDGRPLQPHVRVWDSVTLSTLQIIGLGTFERGVGCLDFSKADSGVHLCIIDDSNEHMLTVWDWQKKAKGAEIKTTNEVVLAVEFHPTDANTIITCGKSHIFFWTWSGNSLTRKQGIFGKYEKPKFVQCLAFLGNGDVLTGDSGGVMLIWSKTTVEPTPGKGPKGVYQISKQIKAHDGSVFTLCQMRNGMLLTGGGKDRKIILWDHDLNPEREIEVPDQYGTIRAVAEGKADQFLVGTSRNFILRGTFNDGFQIEVQGHTDELWGLATHPFKDLLLTCAQDRQVCLWNSMEHRLEWTRLVDEPGHCADFHPSGTVVAIGTHSGRWFVLDAETRDLVSIHTDGNEQLSVMRYSIDGTFLAVGSHDNFIYLYVVSENGRKYSRYGRCTGHSSYITHLDWSPDNKYIMSNSGDYEILYWDIPNGCKLIRNRSDCKDIDWTTYTCVLGFQVFGVWPEGSDGTDINALVRSHNRKVIAVADDFCKVHLFQYPCSKAKAPSHKYSAHSSHVTNVSFTHNDSHLISTGGKDMSIIQWKLVEKLSLPQNETVADTTLTKAPVSSTESVIQSNTPTPPPSQPLNETAEEESRISSSPTLLENSLEQTVEPSEDHSEEESEEGSGDLGEPLYEEPCNEISKEQAKATLLEDQQDPSPSS

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
1	Acetylation	-------MDGFAGSL -------CCCCCCCC	11.67	22814378
7	Phosphorylation	-MDGFAGSLDDSISA -CCCCCCCCCCCCCC	25.79	25159151
11	Phosphorylation	FAGSLDDSISAASTS CCCCCCCCCCCCCCH	20.36	25159151
13	Phosphorylation	GSLDDSISAASTSDV CCCCCCCCCCCCHHH	23.02	22617229
16	Phosphorylation	DDSISAASTSDVQDR CCCCCCCCCHHHHHH	28.32	25159151
17	Phosphorylation	DSISAASTSDVQDRL CCCCCCCCHHHHHHH	24.99	24043423
18	Phosphorylation	SISAASTSDVQDRLS CCCCCCCHHHHHHHH	33.03	24043423
25	Phosphorylation	SDVQDRLSALESRVQ HHHHHHHHHHHHHHH	31.53	22199227
29	Phosphorylation	DRLSALESRVQQQED HHHHHHHHHHHHCHH	38.30	22199227
39	Phosphorylation	QQQEDEITVLKAALA HHCHHHHHHHHHHHH	20.10	22210691
42	Ubiquitination	EDEITVLKAALADVL HHHHHHHHHHHHHHH	27.55	-
50	Methylation	AALADVLRRLAISED HHHHHHHHHHCCCHH	31.26	-
61	Phosphorylation	ISEDHVASVKKSVSS CCHHHHHHHHHHHCC	33.12	25159151
63	2-Hydroxyisobutyrylation	EDHVASVKKSVSSKG HHHHHHHHHHHCCCC	36.51	-
63	Ubiquitination	EDHVASVKKSVSSKG HHHHHHHHHHHCCCC	36.51	-
65	Phosphorylation	HVASVKKSVSSKGQP HHHHHHHHHCCCCCC	22.86	-
68	Phosphorylation	SVKKSVSSKGQPSPR HHHHHHCCCCCCCCC	38.35	24719451
69	Ubiquitination	VKKSVSSKGQPSPRA HHHHHCCCCCCCCCE	54.80	-
73	Phosphorylation	VSSKGQPSPRAVIPM HCCCCCCCCCEEEEH	21.09	27174698
81	Phosphorylation	PRAVIPMSCITNGSG CCEEEEHHHEECCCC	9.30	28258704
84	Phosphorylation	VIPMSCITNGSGANR EEEHHHEECCCCCCC	37.54	23882029
87	Phosphorylation	MSCITNGSGANRKPS HHHEECCCCCCCCCC	36.48	29978859
92	Ubiquitination	NGSGANRKPSHTSAV CCCCCCCCCCCCCCE	51.16	-
94	Phosphorylation	SGANRKPSHTSAVSI CCCCCCCCCCCCEEC	42.29	25159151
94 (in isoform 2)	Phosphorylation	-	42.29	24719451
96	Phosphorylation	ANRKPSHTSAVSIAG CCCCCCCCCCEECCC	23.79	27273156
97	Phosphorylation	NRKPSHTSAVSIAGK CCCCCCCCCEECCCH	22.65	30206219
100	Phosphorylation	PSHTSAVSIAGKETL CCCCCCEECCCHHHH	13.36	29978859
106	Phosphorylation	VSIAGKETLSSAAKS EECCCHHHHHHHHHH	35.11	27251275
108	Phosphorylation	IAGKETLSSAAKSGT CCCHHHHHHHHHHCC	25.92	29396449
109	Phosphorylation	AGKETLSSAAKSGTE CCHHHHHHHHHHCCH	35.04	25159151
113	Phosphorylation	TLSSAAKSGTEKKKE HHHHHHHHCCHHHCC	46.34	24719451
113 (in isoform 2)	Phosphorylation	-	46.34	24719451
132	Phosphorylation	QREKKEESHSNDQSP HHHHHHHCCCCCCCC	33.05	25159151
134	Phosphorylation	EKKEESHSNDQSPQI HHHHHCCCCCCCCCC	51.92	25159151
138	Phosphorylation	ESHSNDQSPQIRASP HCCCCCCCCCCCCCC	22.95	29255136
144	Phosphorylation	QSPQIRASPSPQPSS CCCCCCCCCCCCCCC	18.96	29255136
146	Phosphorylation	PQIRASPSPQPSSQP CCCCCCCCCCCCCCC	33.40	29255136
150	O-linked_Glycosylation	ASPSPQPSSQPLQIH CCCCCCCCCCCCEEE	36.04	OGP
150	Phosphorylation	ASPSPQPSSQPLQIH CCCCCCCCCCCCEEE	36.04	22167270
151	Phosphorylation	SPSPQPSSQPLQIHR CCCCCCCCCCCEEEC	42.36	30266825
160	Phosphorylation	PLQIHRQTPESKNAT CCEEECCCCCCCCCC	29.04	30266825
163	Phosphorylation	IHRQTPESKNATPTK EECCCCCCCCCCCCC	32.20	30266825
167	Phosphorylation	TPESKNATPTKSIKR CCCCCCCCCCCCCCC	40.67	26425664
170	Acetylation	SKNATPTKSIKRPSP CCCCCCCCCCCCCCC	51.92	25953088
171	Phosphorylation	KNATPTKSIKRPSPA CCCCCCCCCCCCCCC	35.50	23401153
173	Acetylation	ATPTKSIKRPSPAEK CCCCCCCCCCCCCCC	66.40	7664663
176	Phosphorylation	TKSIKRPSPAEKSHN CCCCCCCCCCCCCCC	40.55	23401153
181	Phosphorylation	RPSPAEKSHNSWENS CCCCCCCCCCCCCCC	21.29	23312004
184	Phosphorylation	PAEKSHNSWENSDDS CCCCCCCCCCCCHHH	30.28	30576142
188	Phosphorylation	SHNSWENSDDSRNKL CCCCCCCCHHHHHHH	31.14	30576142
191	Phosphorylation	SWENSDDSRNKLSKI CCCCCHHHHHHHHCC	42.62	25159151
196	Phosphorylation	DDSRNKLSKIPSTPK HHHHHHHHCCCCCCC	30.10	23403867
200	Phosphorylation	NKLSKIPSTPKLIPK HHHHCCCCCCCCCCC	61.90	26055452
201	Phosphorylation	KLSKIPSTPKLIPKV HHHCCCCCCCCCCCC	21.06	26055452
209	Phosphorylation	PKLIPKVTKTADKHK CCCCCCCCCCCHHHC	28.89	23403867
211	Phosphorylation	LIPKVTKTADKHKDV CCCCCCCCCHHHCCE	30.62	-
216	Ubiquitination	TKTADKHKDVIINQE CCCCHHHCCEEECCC	60.47	-
226	Phosphorylation	IINQEGEYIKMFMRG EECCCCCEEEEEECC	19.39	27273156
237	Phosphorylation	FMRGRPITMFIPSDV EECCCCEEEEECCCC	14.54	22199227
242	Phosphorylation	PITMFIPSDVDNYDD CEEEEECCCCCCHHH	45.51	22199227
247	Phosphorylation	IPSDVDNYDDIRTEL ECCCCCCHHHHHHCC	15.55	22199227
252	Phosphorylation	DNYDDIRTELPPEKL CCHHHHHHCCCHHHC	42.06	22199227
265	Phosphorylation	KLKLEWAYGYRGKDC HCCEEEEECCCCCCC	18.76	26657352
267	Phosphorylation	KLEWAYGYRGKDCRA CEEEEECCCCCCCCC	11.97	26657352
277	Phosphorylation	KDCRANVYLLPTGKI CCCCCCEEEECCCCE	11.43	26657352
297	Phosphorylation	SVVVLFNYEERTQRH EEHHHCCCHHHHCHH	16.31	-
305	Phosphorylation	EERTQRHYLGHTDCV HHHHCHHCCCCCCHH	19.30	-
313	Acetylation	LGHTDCVKCLAIHPD CCCCCHHHHEEECCC	29.84	26051181
326	Phosphorylation	PDKIRIATGQIAGVD CCCEEEEECCCCCCC	27.52	20068231
348	Phosphorylation	PHVRVWDSVTLSTLQ CCEEEEECEEEHHEE	10.99	20860994
350	Phosphorylation	VRVWDSVTLSTLQII EEEEECEEEHHEEEE	20.95	20860994
437	Phosphorylation	KSHIFFWTWSGNSLT CCEEEEEECCCCCCC	12.47	-
446	Malonylation	SGNSLTRKQGIFGKY CCCCCCHHCCCCCCC	47.87	26320211
453	Phosphorylation	KQGIFGKYEKPKFVQ HCCCCCCCCCCCHHE	29.57	23898821
486	Phosphorylation	MLIWSKTTVEPTPGK EEEEEEEEECCCCCC	26.97	28787133
490	Phosphorylation	SKTTVEPTPGKGPKG EEEEECCCCCCCCCC	31.03	23403867
493	Ubiquitination	TVEPTPGKGPKGVYQ EECCCCCCCCCCEEE	73.56	-
499	Phosphorylation	GKGPKGVYQISKQIK CCCCCCEEEECCEEE	14.59	22817900
502	Phosphorylation	PKGVYQISKQIKAHD CCCEEEECCEEECCC	11.72	22817900
525	Phosphorylation	MRNGMLLTGGGKDRK EECCEEEECCCCCCE	29.80	23612710
532	Ubiquitination	TGGGKDRKIILWDHD ECCCCCCEEEEECCC	44.20	-
562	Ubiquitination	IRAVAEGKADQFLVG EEEEEECCCCEEEEE	40.05	-
609	Phosphorylation	PFKDLLLTCAQDRQV CHHHHHHHHHCCCEE	13.03	31409757
743	Phosphorylation	IMSNSGDYEILYWDI ECCCCCCEEEEEEEC	14.37	27811184
867	Ubiquitination	IQWKLVEKLSLPQNE EEHEEHHHCCCCCCC	35.58	-
869	Phosphorylation	WKLVEKLSLPQNETV HEEHHHCCCCCCCEE	49.42	27050516
875	Phosphorylation	LSLPQNETVADTTLT CCCCCCCEECCCCCE	28.66	25159151
879	Phosphorylation	QNETVADTTLTKAPV CCCEECCCCCEECCC	17.61	28348404
880	Phosphorylation	NETVADTTLTKAPVS CCEECCCCCEECCCC	32.74	25159151
882	O-linked_Glycosylation	TVADTTLTKAPVSST EECCCCCEECCCCCC	24.06	23301498
887	Phosphorylation	TLTKAPVSSTESVIQ CCEECCCCCCCHHHH	30.40	23927012
888	Phosphorylation	LTKAPVSSTESVIQS CEECCCCCCCHHHHC	36.11	30278072
889	Phosphorylation	TKAPVSSTESVIQSN EECCCCCCCHHHHCC	25.44	29255136
891	Phosphorylation	APVSSTESVIQSNTP CCCCCCCHHHHCCCC	25.30	29255136
895	Phosphorylation	STESVIQSNTPTPPP CCCHHHHCCCCCCCC	31.39	29255136
897	Phosphorylation	ESVIQSNTPTPPPSQ CHHHHCCCCCCCCCC	33.51	29255136
899	Phosphorylation	VIQSNTPTPPPSQPL HHHCCCCCCCCCCCC	46.52	29255136
903	Phosphorylation	NTPTPPPSQPLNETA CCCCCCCCCCCCCCH	50.64	29255136
909	Phosphorylation	PSQPLNETAEEESRI CCCCCCCCHHHHHHC	37.99	23927012
914	Phosphorylation	NETAEEESRISSSPT CCCHHHHHHCCCCCC	37.89	23927012
917	Phosphorylation	AEEESRISSSPTLLE HHHHHHCCCCCCHHH	24.53	26074081
918	Phosphorylation	EEESRISSSPTLLEN HHHHHCCCCCCHHHH	37.66	26074081
919	Phosphorylation	EESRISSSPTLLENS HHHHCCCCCCHHHHH	18.34	27362937
921	Phosphorylation	SRISSSPTLLENSLE HHCCCCCCHHHHHHH	46.02	25137130
926	Phosphorylation	SPTLLENSLEQTVEP CCCHHHHHHHHCCCC	24.73	25921289
930	Phosphorylation	LENSLEQTVEPSEDH HHHHHHHCCCCCCCC	19.91	29496963
934	Phosphorylation	LEQTVEPSEDHSEEE HHHCCCCCCCCCHHH	41.99	28348404
938	Phosphorylation	VEPSEDHSEEESEEG CCCCCCCCHHHCCCC	60.05	18669648
942	Phosphorylation	EDHSEEESEEGSGDL CCCCHHHCCCCCCCC	44.20	28348404
946	Phosphorylation	EEESEEGSGDLGEPL HHHCCCCCCCCCCCC	32.20	28348404
954	Phosphorylation	GDLGEPLYEEPCNEI CCCCCCCCCCCCCCC	29.03	22817900
978	Phosphorylation	LEDQQDPSPSS---- HHHCCCCCCCC----	45.78	30266825
980	Phosphorylation	DQQDPSPSS------ HCCCCCCCC------	100.00	30266825
981	Phosphorylation	QQDPSPSS------- CCCCCCCC-------	0.00	30266825

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 EMAL4_HUMAN !!

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Reference
144	S	Phosphorylation	18669648
Phosphorylation at Ser-144 and Ser-146 promotes its dissociation from microtubules during mitosis which is required for efficient chromosome congression.
146	S	Phosphorylation	18669648
Phosphorylation at Ser-144 and Ser-146 promotes its dissociation from microtubules during mitosis which is required for efficient chromosome congression.

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 EMAL4_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference	Domain-Domain Interactions
EMAL4_HUMAN	EML4	physical	16890222
NUDC_HUMAN	NUDC	physical	25789526

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 EMAL4_HUMAN

Related Literatures of Post-Translational Modification

Phosphorylation
Reference	PubMed
"Lys-N and trypsin cover complementary parts of the phosphoproteome ina refined SCX-based approach."; Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,Mohammed S.; Anal. Chem. 81:4493-4501(2009). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-201; SER-895; THR-897;THR-899 AND SER-978, AND MASS SPECTROMETRY.	19413330 [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-144; SER-146; SER-895;THR-897; THR-899; SER-903; THR-909; THR-921; SER-934; SER-942 ANDSER-946, AND MASS SPECTROMETRY.	18669648 [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 SER-144; SER-146 ANDTHR-899, AND MASS SPECTROMETRY.	18220336 [Abstract]
"Evaluation of the low-specificity protease elastase for large-scalephosphoproteome analysis."; Wang B., Malik R., Nigg E.A., Korner R.; Anal. Chem. 80:9526-9533(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-16 AND SER-138, AND MASSSPECTROMETRY.	19007248 [Abstract]
"Global, in vivo, and site-specific phosphorylation dynamics insignaling networks."; Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,Mann M.; Cell 127:635-648(2006). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-87; SER-144; SER-146;TYR-499 AND SER-502, AND MASS SPECTROMETRY.	17081983 [Abstract]
"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 THR-897 AND THR-899, ANDMASS SPECTROMETRY.	19690332 [Abstract]
"Large-scale characterization of HeLa cell nuclear phosphoproteins."; Beausoleil S.A., Jedrychowski M., Schwartz D., Elias J.E., Villen J.,Li J., Cohn M.A., Cantley L.C., Gygi S.P.; Proc. Natl. Acad. Sci. U.S.A. 101:12130-12135(2004). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-899, AND MASSSPECTROMETRY.	15302935 [Abstract]
"Global survey of phosphotyrosine signaling identifies oncogenickinases in lung cancer."; Rikova K., Guo A., Zeng Q., Possemato A., Yu J., Haack H., Nardone J.,Lee K., Reeves C., Li Y., Hu Y., Tan Z., Stokes M., Sullivan L.,Mitchell J., Wetzel R., Macneill J., Ren J.M., Yuan J.,Bakalarski C.E., Villen J., Kornhauser J.M., Smith B., Li D., Zhou X.,Gygi S.P., Gu T.-L., Polakiewicz R.D., Rush J., Comb M.J.; Cell 131:1190-1203(2007). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-226, AND MASSSPECTROMETRY.	18083107 [Abstract]
"Immunoaffinity profiling of tyrosine phosphorylation in cancercells."; Rush J., Moritz A., Lee K.A., Guo A., Goss V.L., Spek E.J., Zhang H.,Zha X.-M., Polakiewicz R.D., Comb M.J.; Nat. Biotechnol. 23:94-101(2005). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-226, AND MASSSPECTROMETRY.	15592455 [Abstract]

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