dbPTM

ECT2_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	ECT2_HUMAN
UniProt AC	Q9H8V3
Protein Name	Protein ECT2
Gene Name	ECT2
Organism	Homo sapiens (Human).
Sequence Length	914
Subcellular Localization	Nucleus. Cytoplasm. Cytoplasm, cytoskeleton, spindle. Cleavage furrow. Midbody. Cell junction. Cell junction, tight junction. Sequestered within the nucleus during interphase. Dispersed throughout the cytoplasm upon breakdown of the nuclear envelope
Protein Description	Guanine nucleotide exchange factor (GEF) that catalyzes the exchange of GDP for GTP. Promotes guanine nucleotide exchange on the Rho family members of small GTPases, like RHOA, RHOC, RAC1 and CDC42. Required for signal transduction pathways involved in the regulation of cytokinesis. Component of the centralspindlin complex that serves as a microtubule-dependent and Rho-mediated signaling required for the myosin contractile ring formation during the cell cycle cytokinesis. Regulates the translocation of RHOA from the central spindle to the equatorial region. Plays a role in the control of mitotic spindle assembly; regulates the activation of CDC42 in metaphase for the process of spindle fibers attachment to kinetochores before chromosome congression. Involved in the regulation of epithelial cell polarity; participates in the formation of epithelial tight junctions in a polarity complex PARD3-PARD6-protein kinase PRKCQ-dependent manner. Plays a role in the regulation of neurite outgrowth. Inhibits phenobarbital (PB)-induced NR1I3 nuclear translocation. Stimulates the activity of RAC1 through its association with the oncogenic PARD6A-PRKCI complex in cancer cells, thereby acting to coordinately drive tumor cell proliferation and invasion. Also stimulates genotoxic stress-induced RHOB activity in breast cancer cells leading to their cell death..
Protein Sequence	MAENSVLTSTTGRTSLADSSIFDSKVTEISKENLLIGSTSYVEEEMPQIETRVILVQEAGKQEELIKALKTIKIMEVPVIKIKESCPGKSDEKLIKSVINMDIKVGFVKMESVEEFEGLDSPEFENVFVVTDFQDSVFNDLYKADCRVIGPPVVLNCSQKGEPLPFSCRPLYCTSMMNLVLCFTGFRKKEELVRLVTLVHHMGGVIRKDFNSKVTHLVANCTQGEKFRVAVSLGTPIMKPEWIYKAWERRNEQDFYAAVDDFRNEFKVPPFQDCILSFLGFSDEEKTNMEEMTEMQGGKYLPLGDERCTHLVVEENIVKDLPFEPSKKLYVVKQEWFWGSIQMDARAGETMYLYEKANTPELKKSVSMLSLNTPNSNRKRRRLKETLAQLSRETDVSPFPPRKRPSAEHSLSIGSLLDISNTPESSINYGDTPKSCTKSSKSSTPVPSKQSARWQVAKELYQTESNYVNILATIIQLFQVPLEEEGQRGGPILAPEEIKTIFGSIPDIFDVHTKIKDDLEDLIVNWDESKSIGDIFLKYSKDLVKTYPPFVNFFEMSKETIIKCEKQKPRFHAFLKINQAKPECGRQSLVELLIRPVQRLPSVALLLNDLKKHTADENPDKSTLEKAIGSLKEVMTHINEDKRKTEAQKQIFDVVYEVDGCPANLLSSHRSLVQRVETISLGEHPCDRGEQVTLFLFNDCLEIARKRHKVIGTFRSPHGQTRPPASLKHIHLMPLSQIKKVLDIRETEDCHNAFALLVRPPTEQANVLLSFQMTSDELPKENWLKMLCRHVANTICKADAENLIYTADPESFEVNTKDMDSTLSRASRAIKKTSKKVTRAFSFSKTPKRALRRALMTSHGSVEGRSPSSNDKHVMSRLSSTSSLAGIPSPSLVSLPSFFERRSHTLSRSTTHLI

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
2	Acetylation	------MAENSVLTS ------CCCCCEEEC	25.36	22814378
5	Phosphorylation	---MAENSVLTSTTG ---CCCCCEEECCCC	15.26	22199227
8	Phosphorylation	MAENSVLTSTTGRTS CCCCCEEECCCCCCC	23.13	22199227
9	Phosphorylation	AENSVLTSTTGRTSL CCCCEEECCCCCCCC	21.58	22199227
10	Phosphorylation	ENSVLTSTTGRTSLA CCCEEECCCCCCCCC	28.21	22199227
11	Phosphorylation	NSVLTSTTGRTSLAD CCEEECCCCCCCCCC	25.16	22199227
13	Methylation	VLTSTTGRTSLADSS EEECCCCCCCCCCCC	21.03	-
14	Phosphorylation	LTSTTGRTSLADSSI EECCCCCCCCCCCCC	29.45	25850435
15	Phosphorylation	TSTTGRTSLADSSIF ECCCCCCCCCCCCCC	21.87	25159151
19	Phosphorylation	GRTSLADSSIFDSKV CCCCCCCCCCCCCCC	21.52	28985074
20	Phosphorylation	RTSLADSSIFDSKVT CCCCCCCCCCCCCCC	28.02	24173317
24	Phosphorylation	ADSSIFDSKVTEISK CCCCCCCCCCCEECC	20.48	-
25	Sumoylation	DSSIFDSKVTEISKE CCCCCCCCCCEECCC	55.83	-
25	Ubiquitination	DSSIFDSKVTEISKE CCCCCCCCCCEECCC	55.83	29967540
27	Phosphorylation	SIFDSKVTEISKENL CCCCCCCCEECCCCE	31.19	28464451
31	Ubiquitination	SKVTEISKENLLIGS CCCCEECCCCEEEEC	57.17	21906983
31 (in isoform 1)	Ubiquitination	-	57.17	21906983
31 (in isoform 2)	Ubiquitination	-	57.17	21906983
38	Phosphorylation	KENLLIGSTSYVEEE CCCEEEECCCCCCCC	13.74	30576142
39	Phosphorylation	ENLLIGSTSYVEEEM CCEEEECCCCCCCCC	20.90	30576142
40	Phosphorylation	NLLIGSTSYVEEEMP CEEEECCCCCCCCCC	28.95	30278072
41	Phosphorylation	LLIGSTSYVEEEMPQ EEEECCCCCCCCCCC	16.39	30278072
61	Ubiquitination	ILVQEAGKQEELIKA EEEECCCCHHHHHHH	62.68	-
61 (in isoform 3)	Ubiquitination	-	62.68	-
67	Ubiquitination	GKQEELIKALKTIKI CCHHHHHHHHHHCEE	61.36	-
73	Ubiquitination	IKALKTIKIMEVPVI HHHHHHCEEEECCEE	41.03	29967540
104	Ubiquitination	SVINMDIKVGFVKME HHHCCCEEEEEEECE	31.85	-
112	Phosphorylation	VGFVKMESVEEFEGL EEEEECEEHHHCCCC	31.19	24144214
121	Phosphorylation	EEFEGLDSPEFENVF HHCCCCCCCCCCCEE	31.22	24144214
131	Phosphorylation	FENVFVVTDFQDSVF CCCEEEEEECCCHHH	26.29	24144214
136	Phosphorylation	VVTDFQDSVFNDLYK EEEECCCHHHHHHHH	20.16	24144214
142	Phosphorylation	DSVFNDLYKADCRVI CHHHHHHHHCCCEEE	13.64	24144214
182	Ubiquitination	SMMNLVLCFTGFRKK HHHHHHHHHHCCCCH	1.93	29967540
195	Ubiquitination	KKEELVRLVTLVHHM CHHHHHHHHHHHHHC	2.42	29967540
212 (in isoform 2)	Phosphorylation	-	28.61	25147952
213	Ubiquitination	IRKDFNSKVTHLVAN HHHCCCCHHHHHEEE	52.86	29967540
226	Acetylation	ANCTQGEKFRVAVSL EECCCCCEEEEEEEC	45.34	23749302
226	Ubiquitination	ANCTQGEKFRVAVSL EECCCCCEEEEEEEC	45.34	29967540
239	Ubiquitination	SLGTPIMKPEWIYKA ECCCCCCCHHHHHHH	40.27	-
239 (in isoform 3)	Ubiquitination	-	40.27	-
244	Phosphorylation	IMKPEWIYKAWERRN CCCHHHHHHHHHHHC	8.84	-
268 (in isoform 1)	Ubiquitination	-	9.88	21906983
268 (in isoform 2)	Ubiquitination	-	9.88	21906983
287	Phosphorylation	GFSDEEKTNMEEMTE CCCHHHHCCHHHHHH	42.98	22210691
288	Ubiquitination	FSDEEKTNMEEMTEM CCHHHHCCHHHHHHH	47.11	29967540
296	Ubiquitination	MEEMTEMQGGKYLPL HHHHHHHCCCCEECC	51.78	29967540
299	Ubiquitination	MTEMQGGKYLPLGDE HHHHCCCCEECCCCC	50.90	21906983
319	Ubiquitination	VVEENIVKDLPFEPS EEECCCCCCCCCCCC	50.15	29967540
327	Phosphorylation	DLPFEPSKKLYVVKQ CCCCCCCCCEEEEEE	58.47	32645325
327	Ubiquitination	DLPFEPSKKLYVVKQ CCCCCCCCCEEEEEE	58.47	29967540
328	Phosphorylation	LPFEPSKKLYVVKQE CCCCCCCCEEEEEEE	49.76	24719451
333	Ubiquitination	SKKLYVVKQEWFWGS CCCEEEEEEEEECEE	32.24	29967540
334	Phosphorylation	KKLYVVKQEWFWGSI CCEEEEEEEEECEEE	41.36	18669648
336	Phosphorylation	LYVVKQEWFWGSIQM EEEEEEEEECEEEEC	7.56	24719451
338	Phosphorylation	VVKQEWFWGSIQMDA EEEEEEECEEEECCC	10.74	33259812
339	Phosphorylation	VKQEWFWGSIQMDAR EEEEEECEEEECCCC	12.85	24719451
342	Phosphorylation	EWFWGSIQMDARAGE EEECEEEECCCCCCC	25.96	24719451
345	Phosphorylation	WGSIQMDARAGETMY CEEEECCCCCCCEEE	9.62	18669648
350	Phosphorylation	MDARAGETMYLYEKA CCCCCCCEEEEEECC	15.36	27174698
352	Phosphorylation	ARAGETMYLYEKANT CCCCCEEEEEECCCC	17.35	28122231
352	Ubiquitination	ARAGETMYLYEKANT CCCCCEEEEEECCCC	17.35	33845483
353	Ubiquitination	RAGETMYLYEKANTP CCCCEEEEEECCCCH	2.86	33845483
354	Phosphorylation	AGETMYLYEKANTPE CCCEEEEEECCCCHH	9.63	27174698
358	Phosphorylation	MYLYEKANTPELKKS EEEEECCCCHHHHHH	68.20	32645325
359	Phosphorylation	YLYEKANTPELKKSV EEEECCCCHHHHHHH	24.01	23401153
360	Phosphorylation	LYEKANTPELKKSVS EEECCCCHHHHHHHH	44.74	24719451
364	Ubiquitination	ANTPELKKSVSMLSL CCCHHHHHHHHHHHC	69.57	29967540
365	Phosphorylation	NTPELKKSVSMLSLN CCHHHHHHHHHHHCC	20.17	22617229
366	Phosphorylation	TPELKKSVSMLSLNT CHHHHHHHHHHHCCC	5.53	24719451
367	Phosphorylation	PELKKSVSMLSLNTP HHHHHHHHHHHCCCC	22.54	23401153
368	Sulfoxidation	ELKKSVSMLSLNTPN HHHHHHHHHHCCCCC	2.49	21406390
369	Phosphorylation	LKKSVSMLSLNTPNS HHHHHHHHHCCCCCC	4.03	33259812
370	Phosphorylation	KKSVSMLSLNTPNSN HHHHHHHHCCCCCCH	15.78	22167270
372	Ubiquitination	SVSMLSLNTPNSNRK HHHHHHCCCCCCHHH	50.55	29967540
373	Phosphorylation	VSMLSLNTPNSNRKR HHHHHCCCCCCHHHH	29.19	22167270
375	Phosphorylation	MLSLNTPNSNRKRRR HHHCCCCCCHHHHHH	50.29	24719451
376	Phosphorylation	LSLNTPNSNRKRRRL HHCCCCCCHHHHHHH	38.93	22167270
383	Ubiquitination	SNRKRRRLKETLAQL CHHHHHHHHHHHHHH	5.80	33845483
384	Ubiquitination	NRKRRRLKETLAQLS HHHHHHHHHHHHHHH	47.01	33845483
384 (in isoform 3)	Ubiquitination	-	47.01	-
386	Phosphorylation	KRRRLKETLAQLSRE HHHHHHHHHHHHHHC	26.30	21712546
391	Phosphorylation	KETLAQLSRETDVSP HHHHHHHHHCCCCCC	18.91	25159151
394	Phosphorylation	LAQLSRETDVSPFPP HHHHHHCCCCCCCCC	40.36	30266825
397	Phosphorylation	LSRETDVSPFPPRKR HHHCCCCCCCCCCCC	24.51	30266825
403	Ubiquitination	VSPFPPRKRPSAEHS CCCCCCCCCCCCCCC	74.55	29967540
406	Phosphorylation	FPPRKRPSAEHSLSI CCCCCCCCCCCCCCH	50.77	25159151
410	Phosphorylation	KRPSAEHSLSIGSLL CCCCCCCCCCHHHHH	18.47	29496963
411	Phosphorylation	RPSAEHSLSIGSLLD CCCCCCCCCHHHHHC	4.70	15302935
412	Phosphorylation	PSAEHSLSIGSLLDI CCCCCCCCHHHHHCC	28.11	26471730
413	Phosphorylation	SAEHSLSIGSLLDIS CCCCCCCHHHHHCCC	5.43	24719451
415	Phosphorylation	EHSLSIGSLLDISNT CCCCCHHHHHCCCCC	24.88	27251275
417	Phosphorylation	SLSIGSLLDISNTPE CCCHHHHHCCCCCCH	6.18	15302935
418	Ubiquitination	LSIGSLLDISNTPES CCHHHHHCCCCCCHH	47.79	29967540
420	Phosphorylation	IGSLLDISNTPESSI HHHHHCCCCCCHHHC	34.03	29523821
422	Phosphorylation	SLLDISNTPESSINY HHHCCCCCCHHHCCC	22.95	29523821
425	Phosphorylation	DISNTPESSINYGDT CCCCCCHHHCCCCCC	37.41	22798277
429	Phosphorylation	TPESSINYGDTPKSC CCHHHCCCCCCCCCC	18.08	25627689
432	Phosphorylation	SSINYGDTPKSCTKS HHCCCCCCCCCCCCC	28.40	25627689
439	Ubiquitination	TPKSCTKSSKSSTPV CCCCCCCCCCCCCCC	25.50	33845483
442	Phosphorylation	SCTKSSKSSTPVPSK CCCCCCCCCCCCCCH	41.20	29396449
443	Phosphorylation	CTKSSKSSTPVPSKQ CCCCCCCCCCCCCHH	40.23	27794612
444	Phosphorylation	TKSSKSSTPVPSKQS CCCCCCCCCCCCHHH	35.08	25159151
448	Phosphorylation	KSSTPVPSKQSARWQ CCCCCCCCHHHHHHH	43.49	29396449
449	Ubiquitination	SSTPVPSKQSARWQV CCCCCCCHHHHHHHH	42.05	29967540
449 (in isoform 3)	Ubiquitination	-	42.05	-
467	Ubiquitination	LYQTESNYVNILATI HHHCCCHHHHHHHHH	12.26	33845483
468	Ubiquitination	YQTESNYVNILATII HHCCCHHHHHHHHHH	4.14	33845483
485	Ubiquitination	FQVPLEEEGQRGGPI HCCCCHHCCCCCCCC	51.78	29967540
498	Ubiquitination	PILAPEEIKTIFGSI CCCCHHHHHHHHCCC	4.56	33845483
499	Ubiquitination	ILAPEEIKTIFGSIP CCCHHHHHHHHCCCC	38.56	33845483
507	Ubiquitination	TIFGSIPDIFDVHTK HHHCCCCCCCCCCHH	53.14	29967540
516	Ubiquitination	FDVHTKIKDDLEDLI CCCCHHHCCCHHHHC	46.90	29967540
530	Ubiquitination	IVNWDESKSIGDIFL CCCCCCCCCHHHHHH	44.00	29967540
538	Ubiquitination	SIGDIFLKYSKDLVK CHHHHHHHHCHHHHH	36.41	29967540
539	Phosphorylation	IGDIFLKYSKDLVKT HHHHHHHHCHHHHHH	24.09	-
545	Ubiquitination	KYSKDLVKTYPPFVN HHCHHHHHHCCCCCC	50.03	-
546	Phosphorylation	YSKDLVKTYPPFVNF HCHHHHHHCCCCCCH	33.51	29083192
547	Phosphorylation	SKDLVKTYPPFVNFF CHHHHHHCCCCCCHH	11.82	29083192
563	Sumoylation	MSKETIIKCEKQKPR CCHHHHHEECCCCCC	32.27	-
563	Sumoylation	MSKETIIKCEKQKPR CCHHHHHEECCCCCC	32.27	-
566	Ubiquitination	ETIIKCEKQKPRFHA HHHHEECCCCCCEEE	73.43	33845483
580 (in isoform 1)	Ubiquitination	-	25.53	21906983
580 (in isoform 2)	Ubiquitination	-	25.53	21906983
594	Ubiquitination	QSLVELLIRPVQRLP HHHHHHHHHHHHHCC	7.96	33845483
595	Ubiquitination	SLVELLIRPVQRLPS HHHHHHHHHHHHCCH	25.88	33845483
601	Ubiquitination	IRPVQRLPSVALLLN HHHHHHCCHHHHHHH	29.01	29967540
602	Phosphorylation	RPVQRLPSVALLLND HHHHHCCHHHHHHHH	25.31	-
611	Sumoylation	ALLLNDLKKHTADEN HHHHHHHHHHCCCCC	45.43	28112733
611	Ubiquitination	ALLLNDLKKHTADEN HHHHHHHHHHCCCCC	45.43	21906983
611 (in isoform 3)	Ubiquitination	-	45.43	-
612 (in isoform 3)	Ubiquitination	-	54.18	-
621	Ubiquitination	TADENPDKSTLEKAI CCCCCCCHHHHHHHH	46.74	-
625	Ubiquitination	NPDKSTLEKAIGSLK CCCHHHHHHHHHHHH	40.30	33845483
626	Ubiquitination	PDKSTLEKAIGSLKE CCHHHHHHHHHHHHH	48.71	33845483
632	Ubiquitination	EKAIGSLKEVMTHIN HHHHHHHHHHHHHCC	50.38	29967540
636	Phosphorylation	GSLKEVMTHINEDKR HHHHHHHHHCCHHHH	25.44	30619164
685	Phosphorylation	TISLGEHPCDRGEQV EEECCCCCCCCCCCE	19.87	24719451
708	Ubiquitination	LEIARKRHKVIGTFR HHHHHHHCCEEEEEC	31.60	29967540
709	Ubiquitination	EIARKRHKVIGTFRS HHHHHHCCEEEEECC	39.31	-
709 (in isoform 3)	Ubiquitination	-	39.31	-
713	Phosphorylation	KRHKVIGTFRSPHGQ HHCCEEEEECCCCCC	12.54	25159151
716	Phosphorylation	KVIGTFRSPHGQTRP CEEEEECCCCCCCCC	19.63	25159151
721	Phosphorylation	FRSPHGQTRPPASLK ECCCCCCCCCCCCCC	50.14	23186163
726	Phosphorylation	GQTRPPASLKHIHLM CCCCCCCCCCEEEEE	43.66	23186163
736	Phosphorylation	HIHLMPLSQIKKVLD EEEEEEHHHHCHHHC	24.80	23025827
739	Ubiquitination	LMPLSQIKKVLDIRE EEEHHHHCHHHCCCC	29.23	29967540
757	Ubiquitination	CHNAFALLVRPPTEQ CCCEEEEEECCCCHH	2.48	21963094
766	Ubiquitination	RPPTEQANVLLSFQM CCCCHHCCEEEEEEC	25.35	29967540
786	Ubiquitination	PKENWLKMLCRHVAN CHHHHHHHHHHHHHH	3.91	21963094
786 (in isoform 1)	Ubiquitination	-	3.91	21906983
786 (in isoform 2)	Ubiquitination	-	3.91	21906983
788	Ubiquitination	ENWLKMLCRHVANTI HHHHHHHHHHHHHHH	2.24	21963094
797	Ubiquitination	HVANTICKADAENLI HHHHHHHHHCHHHCE	45.51	29967540
797 (in isoform 3)	Ubiquitination	-	45.51	-
805	Phosphorylation	ADAENLIYTADPESF HCHHHCEEECCHHHE	10.07	24275569
806	Phosphorylation	DAENLIYTADPESFE CHHHCEEECCHHHEE	20.00	24275569
811	Phosphorylation	IYTADPESFEVNTKD EEECCHHHEECCCHH	31.90	18669648
815	Phosphorylation	DPESFEVNTKDMDST CHHHEECCCHHHHHH	33.92	24719451
817	Ubiquitination	ESFEVNTKDMDSTLS HHEECCCHHHHHHHH	45.94	21963094
821	Phosphorylation	VNTKDMDSTLSRASR CCCHHHHHHHHHHHH	25.30	24275569
822	Phosphorylation	NTKDMDSTLSRASRA CCHHHHHHHHHHHHH	25.21	24275569
824	Phosphorylation	KDMDSTLSRASRAIK HHHHHHHHHHHHHHH	26.37	21964256
830	Phosphorylation	LSRASRAIKKTSKKV HHHHHHHHHHHCCHH	4.58	24719451
835	Phosphorylation	RAIKKTSKKVTRAFS HHHHHHCCHHHHHHC	57.40	24719451
838	Phosphorylation	KKTSKKVTRAFSFSK HHHCCHHHHHHCCCC	25.76	29514088
842	Phosphorylation	KKVTRAFSFSKTPKR CHHHHHHCCCCCHHH	27.85	22167270
844	Phosphorylation	VTRAFSFSKTPKRAL HHHHHCCCCCHHHHH	34.13	22167270
845	Ubiquitination	TRAFSFSKTPKRALR HHHHCCCCCHHHHHH	67.83	-
845 (in isoform 3)	Ubiquitination	-	67.83	-
846	Phosphorylation	RAFSFSKTPKRALRR HHHCCCCCHHHHHHH	32.61	26055452
848	Phosphorylation	FSFSKTPKRALRRAL HCCCCCHHHHHHHHH	56.38	24719451
851	Phosphorylation	SKTPKRALRRALMTS CCCHHHHHHHHHHHC	4.41	24719451
857	Phosphorylation	ALRRALMTSHGSVEG HHHHHHHHCCCCCCC	20.58	30183078
858	Phosphorylation	LRRALMTSHGSVEGR HHHHHHHCCCCCCCC	16.34	30183078
860	Phosphorylation	RALMTSHGSVEGRSP HHHHHCCCCCCCCCC	32.90	24719451
861	Phosphorylation	ALMTSHGSVEGRSPS HHHHCCCCCCCCCCC	16.15	28731282
866	Phosphorylation	HGSVEGRSPSSNDKH CCCCCCCCCCCCCHH	39.74	25159151
868	Phosphorylation	SVEGRSPSSNDKHVM CCCCCCCCCCCHHHH	42.91	30576142
869	Phosphorylation	VEGRSPSSNDKHVMS CCCCCCCCCCHHHHH	53.05	30576142
872	Phosphorylation	RSPSSNDKHVMSRLS CCCCCCCHHHHHHHH	42.20	24719451
874	Phosphorylation	PSSNDKHVMSRLSST CCCCCHHHHHHHHCC	4.61	24719451
878	Phosphorylation	DKHVMSRLSSTSSLA CHHHHHHHHCCHHHC	3.58	24719451
879	O-linked_Glycosylation	KHVMSRLSSTSSLAG HHHHHHHHCCHHHCC	30.38	30379171
879	Phosphorylation	KHVMSRLSSTSSLAG HHHHHHHHCCHHHCC	30.38	20068231
880	Phosphorylation	HVMSRLSSTSSLAGI HHHHHHHCCHHHCCC	36.58	27273156
881	Phosphorylation	VMSRLSSTSSLAGIP HHHHHHCCHHHCCCC	20.96	27273156
882	Phosphorylation	MSRLSSTSSLAGIPS HHHHHCCHHHCCCCC	25.88	29496963
883	Phosphorylation	SRLSSTSSLAGIPSP HHHHCCHHHCCCCCH	23.48	29496963
889	Phosphorylation	SSLAGIPSPSLVSLP HHHCCCCCHHHCCCC	25.79	25159151
891	Phosphorylation	LAGIPSPSLVSLPSF HCCCCCHHHCCCCCH	45.82	28387310
894	Phosphorylation	IPSPSLVSLPSFFER CCCHHHCCCCCHHHH	39.60	27732954
897	Phosphorylation	PSLVSLPSFFERRSH HHHCCCCCHHHHCCC	48.11	27732954
903	Phosphorylation	PSFFERRSHTLSRST CCHHHHCCCCCCCCC	27.35	24719451
905	Phosphorylation	FFERRSHTLSRSTTH HHHHCCCCCCCCCCC	27.89	24719451
907	Phosphorylation	ERRSHTLSRSTTHLI HHCCCCCCCCCCCCC	25.91	20736484
909	Phosphorylation	RSHTLSRSTTHLI-- CCCCCCCCCCCCC--	33.99	22210691
910	Phosphorylation	SHTLSRSTTHLI--- CCCCCCCCCCCC---	19.68	22210691
911	Phosphorylation	HTLSRSTTHLI---- CCCCCCCCCCC----	18.87	-

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
342	T	Phosphorylation	Kinase	CDK1	P06493	PhosphoELM
359	T	Phosphorylation	Kinase	PKCI	P41743	PSP
373	T	Phosphorylation	Kinase	CDK1	P06493	Uniprot
413	T	Phosphorylation	Kinase	CDK1	P06493	PhosphoELM
444	T	Phosphorylation	Kinase	CDK1	P06493	Uniprot
815	T	Phosphorylation	Kinase	CDK1	P06493	PhosphoELM
846	T	Phosphorylation	Kinase	CDK1	P06493	Uniprot

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Reference
359	T	Phosphorylation	21189248
Phosphorylation at Thr-359 is required for its transformation activity in cancer cells.
373	T	Phosphorylation	21189248
Phosphorylation at Thr-373 occurs during the G2/M phase, relieves its auto-inhibition status and stimulates its GEF activity.
444	T	Phosphorylation	21189248
Phosphorylation at Thr-444 in G2/M phase is required for subsequent binding with PLK1 and Rho exchange activation.

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 ECT2_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
PAR6A_HUMAN	PARD6A	physical	15254234
KLH20_HUMAN	KLHL20	physical	14668487
KPCZ_HUMAN	PRKCZ	physical	15254234
KLH20_HUMAN	KLHL20	physical	17395875
ABR_HUMAN	ABR	physical	22990118
CD19_HUMAN	CD19	physical	22990118
CYTB_HUMAN	CSTB	physical	22990118
IF4A2_HUMAN	EIF4A2	physical	22990118
MBD1_HUMAN	MBD1	physical	22990118
MT2_HUMAN	MT2A	physical	22990118
COX2_HUMAN	COX2	physical	22990118
PCOC1_HUMAN	PCOLCE	physical	22990118
PSA6_HUMAN	PSMA6	physical	22990118
RS20_HUMAN	RPS20	physical	22990118
ELOC_HUMAN	TCEB1	physical	22990118
UBB_HUMAN	UBB	physical	22990118
VDAC2_HUMAN	VDAC2	physical	22990118
CHSTA_HUMAN	CHST10	physical	22990118
IF2P_HUMAN	EIF5B	physical	22990118
NPC2_HUMAN	NPC2	physical	22990118
ILVBL_HUMAN	ILVBL	physical	22990118
U520_HUMAN	SNRNP200	physical	22990118
NOMO1_HUMAN	NOMO1	physical	22990118
ERAL1_HUMAN	ERAL1	physical	22990118
POMP_HUMAN	POMP	physical	22990118
CB042_HUMAN	C2orf42	physical	22990118
CCD91_HUMAN	CCDC91	physical	22990118
OTUB1_HUMAN	OTUB1	physical	22990118
THA11_HUMAN	THAP11	physical	22990118
FANCM_HUMAN	FANCM	physical	22990118
SPT22_HUMAN	SPATA22	physical	22990118
GGN_HUMAN	GGN	physical	22990118
OOSP2_HUMAN	OOSP2	physical	22990118
CRPAK_HUMAN	CRIPAK	physical	22990118
AL1B1_HUMAN	ALDH1B1	physical	22990118
AT2A2_HUMAN	ATP2A2	physical	22990118
CAN1_HUMAN	CAPN1	physical	22990118
CAN2_HUMAN	CAPN2	physical	22990118
CAZA1_HUMAN	CAPZA1	physical	22990118
CDK5_HUMAN	CDK5	physical	22990118
COF1_HUMAN	CFL1	physical	22990118
AP3S1_HUMAN	AP3S1	physical	22990118
DIC_HUMAN	SLC25A10	physical	22990118
CTBP1_HUMAN	CTBP1	physical	22990118
CTBP2_HUMAN	CTBP2	physical	22990118
CUX1_HUMAN	CUX1	physical	22990118
CASP_HUMAN	CUX1	physical	22990118
CY1_HUMAN	CYC1	physical	22990118
DC1I2_HUMAN	DYNC1I2	physical	22990118
ACSL1_HUMAN	ACSL1	physical	22990118
FHL3_HUMAN	FHL3	physical	22990118
FLNA_HUMAN	FLNA	physical	22990118
XRCC6_HUMAN	XRCC6	physical	22990118
GALK1_HUMAN	GALK1	physical	22990118
HNRPC_HUMAN	HNRNPC	physical	22990118
HXB9_HUMAN	HOXB9	physical	22990118
IF6_HUMAN	EIF6	physical	22990118
IMB1_HUMAN	KPNB1	physical	22990118
LDHA_HUMAN	LDHA	physical	22990118
LDHB_HUMAN	LDHB	physical	22990118
MCM6_HUMAN	MCM6	physical	22990118
MYO1D_HUMAN	MYO1D	physical	22990118
NUMA1_HUMAN	NUMA1	physical	22990118
NUP98_HUMAN	NUP98	physical	22990118
ODPB_HUMAN	PDHB	physical	22990118
PML_HUMAN	PML	physical	22990118
PPM1G_HUMAN	PPM1G	physical	22990118
PP1A_HUMAN	PPP1CA	physical	22990118
PP2AA_HUMAN	PPP2CA	physical	22990118
MK01_HUMAN	MAPK1	physical	22990118
PSMD4_HUMAN	PSMD4	physical	22990118
ABCD3_HUMAN	ABCD3	physical	22990118
RFC2_HUMAN	RFC2	physical	22990118
RFC5_HUMAN	RFC5	physical	22990118
RPN1_HUMAN	RPN1	physical	22990118
SRSF1_HUMAN	SRSF1	physical	22990118
AAAT_HUMAN	SLC1A5	physical	22990118
STRN_HUMAN	STRN	physical	22990118
ELOA1_HUMAN	TCEB3	physical	22990118
TCOF_HUMAN	TCOF1	physical	22990118
P53_HUMAN	TP53	physical	22990118
XRCC5_HUMAN	XRCC5	physical	22990118
1433B_HUMAN	YWHAB	physical	22990118
1433Z_HUMAN	YWHAZ	physical	22990118
UBP11_HUMAN	USP11	physical	22990118
USP9X_HUMAN	USP9X	physical	22990118
ARI1A_HUMAN	ARID1A	physical	22990118
M2OM_HUMAN	SLC25A11	physical	22990118
SUCB2_HUMAN	SUCLG2	physical	22990118
SUCA_HUMAN	SUCLG1	physical	22990118
PCH2_HUMAN	TRIP13	physical	22990118
TF3C5_HUMAN	GTF3C5	physical	22990118
PSA_HUMAN	NPEPPS	physical	22990118
RNF14_HUMAN	RNF14	physical	22990118
NUP93_HUMAN	NUP93	physical	22990118
UBE3C_HUMAN	UBE3C	physical	22990118
RACK1_HUMAN	GNB2L1	physical	22990118
UN13B_HUMAN	UNC13B	physical	22990118
ML12A_HUMAN	MYL12A	physical	22990118
SAHH2_HUMAN	AHCYL1	physical	22990118
CPSF4_HUMAN	CPSF4	physical	22990118
CKAP4_HUMAN	CKAP4	physical	22990118
MIC60_HUMAN	IMMT	physical	22990118
WDHD1_HUMAN	WDHD1	physical	22990118
STRAP_HUMAN	STRAP	physical	22990118
XPOT_HUMAN	XPOT	physical	22990118
COPE_HUMAN	COPE	physical	22990118
PHB2_HUMAN	PHB2	physical	22990118
KDM1A_HUMAN	KDM1A	physical	22990118
TBD2B_HUMAN	TBC1D2B	physical	22990118
LARP1_HUMAN	LARP1	physical	22990118
SIR1_HUMAN	SIRT1	physical	22990118
NU188_HUMAN	NUP188	physical	22990118
SERA_HUMAN	PHGDH	physical	22990118
COPG2_HUMAN	COPG2	physical	22990118
PELP1_HUMAN	PELP1	physical	22990118
STML2_HUMAN	STOML2	physical	22990118
NUB1_HUMAN	NUB1	physical	22990118
PELO_HUMAN	PELO	physical	22990118
CPSF2_HUMAN	CPSF2	physical	22990118
DCA16_HUMAN	DCAF16	physical	22990118
MIC19_HUMAN	CHCHD3	physical	22990118
AGGF1_HUMAN	AGGF1	physical	22990118
PP6R3_HUMAN	PPP6R3	physical	22990118
IPO9_HUMAN	IPO9	physical	22990118
CAND1_HUMAN	CAND1	physical	22990118
RAD18_HUMAN	RAD18	physical	22990118
CCD47_HUMAN	CCDC47	physical	22990118
ESYT2_HUMAN	ESYT2	physical	22990118
MICA3_HUMAN	MICAL3	physical	22990118
UBE2O_HUMAN	UBE2O	physical	22990118
PCAT1_HUMAN	LPCAT1	physical	22990118
TRUA_HUMAN	PUS1	physical	22990118
LAS1L_HUMAN	LAS1L	physical	22990118
SLN11_HUMAN	SLFN11	physical	22990118
PPR18_HUMAN	PPP1R18	physical	22990118
PGAM5_HUMAN	PGAM5	physical	22990118
FTM_HUMAN	RPGRIP1L	physical	27173435

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 ECT2_HUMAN

Related Literatures of Post-Translational Modification

Phosphorylation
Reference	PubMed
"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-367; SER-370; THR-373;SER-376; SER-842 AND THR-846, 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-40 AND SER-889, AND MASSSPECTROMETRY.	18220336 [Abstract]
"Oncogenic activity of Ect2 is regulated through protein kinase Ciota-mediated phosphorylation."; Justilien V., Jameison L., Der C.J., Rossman K.L., Fields A.P.; J. Biol. Chem. 286:8149-8157(2011). Cited for: FUNCTION, PHOSPHORYLATION AT THR-359, MUTAGENESIS OF THR-359, ANDIDENTIFICATION BY MASS SPECTROMETRY.	21189248 [Abstract]
"Cytokinesis regulator ECT2 changes its conformation throughphosphorylation at Thr-341 in G2/M phase."; Hara T., Abe M., Inoue H., Yu L.R., Veenstra T.D., Kang Y.H.,Lee K.S., Miki T.; Oncogene 25:566-578(2006). Cited for: FUNCTION, HOMODIMERIZATION, PHOSPHORYLATION AT THR-373, ANDMUTAGENESIS OF THR-373.	16170345 [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 THR-359, AND MASSSPECTROMETRY.	16964243 [Abstract]

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