dbPTM

ENL_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	ENL_HUMAN
UniProt AC	Q03111
Protein Name	Protein ENL
Gene Name	MLLT1
Organism	Homo sapiens (Human).
Sequence Length	559
Subcellular Localization	Nucleus.
Protein Description	Component of the super elongation complex (SEC), a complex required to increase the catalytic rate of RNA polymerase II transcription by suppressing transient pausing by the polymerase at multiple sites along the DNA..
Protein Sequence	MDNQCTVQVRLELGHRAQLRKKPTTEGFTHDWMVFVRGPEQCDIQHFVEKVVFWLHDSFPKPRRVCKEPPYKVEESGYAGFIMPIEVHFKNKEEPRKVCFTYDLFLNLEGNPPVNHLRCEKLTFNNPTTEFRYKLLRAGGVMVMPEGADTVSRPSPDYPMLPTIPLSAFSDPKKTKPSHGSKDANKESSKTSKPHKVTKEHRERPRKDSESKSSSKELEREQAKSSKDTSRKLGEGRLPKEEKAPPPKAAFKEPKMALKETKLESTSPKGGPPPPPPPPPRASSKRPATADSPKPSAKKQKKSSSKGSRSAPGTSPRTSSSSSFSDKKPAKDKSSTRGEKVKAESEPREAKKALEVEESNSEDEASFKSESAQSSPSNSSSSSDSSSDSDFEPSQNHSQGPLRSMVEDLQSEESDEDDSSSGEEAAGKTNPGRDSRLSFSDSESDNSADSSLPSREPPPPQKPPPPNSKVSGRRSPESCSKPEKILKKGTYDKAYTDELVELHRRLMALRERNVLQQIVNLIEETGHFNVTNTTFDFDLFSLDETTVRKLQSCLEAVAT

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
1	Acetylation	-------MDNQCTVQ -------CCCCEEEE	11.16	22814378
121	Acetylation	VNHLRCEKLTFNNPT CCEEEEEECCCCCCC	57.35	25953088
121	Ubiquitination	VNHLRCEKLTFNNPT CCEEEEEECCCCCCC	57.35	-
123	Phosphorylation	HLRCEKLTFNNPTTE EEEEEECCCCCCCHH	35.07	21406692
128	Phosphorylation	KLTFNNPTTEFRYKL ECCCCCCCHHHHHHH	40.87	21406692
129	Phosphorylation	LTFNNPTTEFRYKLL CCCCCCCHHHHHHHH	34.09	21406692
150	Phosphorylation	VMPEGADTVSRPSPD ECCCCCCCCCCCCCC	21.61	22199227
150	Ubiquitination	VMPEGADTVSRPSPD ECCCCCCCCCCCCCC	21.61	25015289
152	Phosphorylation	PEGADTVSRPSPDYP CCCCCCCCCCCCCCC	40.33	22199227
154	Ubiquitination	GADTVSRPSPDYPML CCCCCCCCCCCCCCC	42.58	25015289
155	Phosphorylation	ADTVSRPSPDYPMLP CCCCCCCCCCCCCCC	29.32	19369195
158	Phosphorylation	VSRPSPDYPMLPTIP CCCCCCCCCCCCCCC	8.23	28122231
158	Ubiquitination	VSRPSPDYPMLPTIP CCCCCCCCCCCCCCC	8.23	25015289
163	Phosphorylation	PDYPMLPTIPLSAFS CCCCCCCCCCHHHCC	31.12	23403867
167	Phosphorylation	MLPTIPLSAFSDPKK CCCCCCHHHCCCCCC	23.16	22199227
170	Phosphorylation	TIPLSAFSDPKKTKP CCCHHHCCCCCCCCC	53.36	22199227
175	Phosphorylation	AFSDPKKTKPSHGSK HCCCCCCCCCCCCCC	55.07	26699800
178	Phosphorylation	DPKKTKPSHGSKDAN CCCCCCCCCCCCCCC	41.87	26699800
180	Ubiquitination	KKTKPSHGSKDANKE CCCCCCCCCCCCCHH	40.50	24816145
182	Ubiquitination	TKPSHGSKDANKESS CCCCCCCCCCCHHHC	66.51	25015289
184	Ubiquitination	PSHGSKDANKESSKT CCCCCCCCCHHHCCC	32.50	25015289
186	Ubiquitination	HGSKDANKESSKTSK CCCCCCCHHHCCCCC	61.77	25015289
188	Phosphorylation	SKDANKESSKTSKPH CCCCCHHHCCCCCCC	38.45	28302921
188	Ubiquitination	SKDANKESSKTSKPH CCCCCHHHCCCCCCC	38.45	25015289
189	Phosphorylation	KDANKESSKTSKPHK CCCCHHHCCCCCCCC	40.83	28302921
190	Ubiquitination	DANKESSKTSKPHKV CCCHHHCCCCCCCCC	67.12	25015289
191	Phosphorylation	ANKESSKTSKPHKVT CCHHHCCCCCCCCCC	43.88	28302921
192	Phosphorylation	NKESSKTSKPHKVTK CHHHCCCCCCCCCCH	48.18	28302921
192	Ubiquitination	NKESSKTSKPHKVTK CHHHCCCCCCCCCCH	48.18	25015289
209	Phosphorylation	RERPRKDSESKSSSK HHCCCCCCCCCHHHH	46.97	22817900
211	Phosphorylation	RPRKDSESKSSSKEL CCCCCCCCCHHHHHH	41.61	23312004
211	Ubiquitination	RPRKDSESKSSSKEL CCCCCCCCCHHHHHH	41.61	24816145
212	Ubiquitination	PRKDSESKSSSKELE CCCCCCCCHHHHHHH	50.75	24816145
213	Phosphorylation	RKDSESKSSSKELER CCCCCCCHHHHHHHH	49.47	23312004
214	Phosphorylation	KDSESKSSSKELERE CCCCCCHHHHHHHHH	49.52	23312004
214	Ubiquitination	KDSESKSSSKELERE CCCCCCHHHHHHHHH	49.52	24816145
223	Ubiquitination	KELEREQAKSSKDTS HHHHHHHHHCCHHHH	14.67	25015289
227	Ubiquitination	REQAKSSKDTSRKLG HHHHHCCHHHHHHHC	72.60	25015289
231	Ubiquitination	KSSKDTSRKLGEGRL HCCHHHHHHHCCCCC	40.07	25015289
240	Sumoylation	LGEGRLPKEEKAPPP HCCCCCCHHHCCCCC	81.00	-
240	Sumoylation	LGEGRLPKEEKAPPP HCCCCCCHHHCCCCC	81.00	28112733
252	Acetylation	PPPKAAFKEPKMALK CCCCHHCCCCHHHHH	69.27	21466224
253	Ubiquitination	PPKAAFKEPKMALKE CCCHHCCCCHHHHHH	43.64	24816145
259	Acetylation	KEPKMALKETKLEST CCCHHHHHHHCCCCC	54.52	25953088
261	Phosphorylation	PKMALKETKLESTSP CHHHHHHHCCCCCCC	39.06	28464451
262	Sumoylation	KMALKETKLESTSPK HHHHHHHCCCCCCCC	51.88	-
262	Acetylation	KMALKETKLESTSPK HHHHHHHCCCCCCCC	51.88	25953088
262	Sumoylation	KMALKETKLESTSPK HHHHHHHCCCCCCCC	51.88	28112733
265	Phosphorylation	LKETKLESTSPKGGP HHHHCCCCCCCCCCC	44.62	23401153
266	Phosphorylation	KETKLESTSPKGGPP HHHCCCCCCCCCCCC	39.41	30266825
267	Phosphorylation	ETKLESTSPKGGPPP HHCCCCCCCCCCCCC	33.62	30266825
283	Phosphorylation	PPPPPRASSKRPATA CCCCCCCCCCCCCCC	37.36	26074081
284	Phosphorylation	PPPPRASSKRPATAD CCCCCCCCCCCCCCC	31.53	26074081
285	Acetylation	PPPRASSKRPATADS CCCCCCCCCCCCCCC	60.96	25953088
289	Phosphorylation	ASSKRPATADSPKPS CCCCCCCCCCCCCCC	33.41	23927012
292	Phosphorylation	KRPATADSPKPSAKK CCCCCCCCCCCCHHH	32.15	29255136
296	Phosphorylation	TADSPKPSAKKQKKS CCCCCCCCHHHHCCC	59.87	23927012
298	Acetylation	DSPKPSAKKQKKSSS CCCCCCHHHHCCCCC	61.14	155585
299	Ubiquitination	SPKPSAKKQKKSSSK CCCCCHHHHCCCCCC	68.04	24816145
308	Phosphorylation	KKSSSKGSRSAPGTS CCCCCCCCCCCCCCC	27.14	28102081
310	Phosphorylation	SSSKGSRSAPGTSPR CCCCCCCCCCCCCCC	40.28	22199227
310	Ubiquitination	SSSKGSRSAPGTSPR CCCCCCCCCCCCCCC	40.28	24816145
314	Phosphorylation	GSRSAPGTSPRTSSS CCCCCCCCCCCCCCC	34.20	30266825
315	Phosphorylation	SRSAPGTSPRTSSSS CCCCCCCCCCCCCCC	20.49	30266825
318	Phosphorylation	APGTSPRTSSSSSFS CCCCCCCCCCCCCCC	36.02	22199227
319	Phosphorylation	PGTSPRTSSSSSFSD CCCCCCCCCCCCCCC	29.51	22199227
320	Phosphorylation	GTSPRTSSSSSFSDK CCCCCCCCCCCCCCC	33.36	22199227
321	Phosphorylation	TSPRTSSSSSFSDKK CCCCCCCCCCCCCCC	29.75	22199227
322	Phosphorylation	SPRTSSSSSFSDKKP CCCCCCCCCCCCCCC	37.03	30576142
323	Phosphorylation	PRTSSSSSFSDKKPA CCCCCCCCCCCCCCC	30.62	30576142
325	Phosphorylation	TSSSSSFSDKKPAKD CCCCCCCCCCCCCCC	50.93	21815630
327	Acetylation	SSSSFSDKKPAKDKS CCCCCCCCCCCCCCC	60.50	23954790
330	Ubiquitination	SFSDKKPAKDKSSTR CCCCCCCCCCCCCCC	41.37	24816145
331	Ubiquitination	FSDKKPAKDKSSTRG CCCCCCCCCCCCCCC	74.37	24816145
333	Acetylation	DKKPAKDKSSTRGEK CCCCCCCCCCCCCCH	45.67	19608861
333	Ubiquitination	DKKPAKDKSSTRGEK CCCCCCCCCCCCCCH	45.67	24816145
334	O-linked_Glycosylation	KKPAKDKSSTRGEKV CCCCCCCCCCCCCHH	47.26	30059200
341	Ubiquitination	SSTRGEKVKAESEPR CCCCCCHHCCCCCCH	6.55	24816145
342	Sumoylation	STRGEKVKAESEPRE CCCCCHHCCCCCCHH	58.46	-
342	Sumoylation	STRGEKVKAESEPRE CCCCCHHCCCCCCHH	58.46	28112733
342	Ubiquitination	STRGEKVKAESEPRE CCCCCHHCCCCCCHH	58.46	24816145
344	Ubiquitination	RGEKVKAESEPREAK CCCHHCCCCCCHHHH	50.33	24816145
345	Phosphorylation	GEKVKAESEPREAKK CCHHCCCCCCHHHHH	58.73	28985074
359	Phosphorylation	KALEVEESNSEDEAS HHHHHHHCCCCCHHH	31.95	29255136
361	Phosphorylation	LEVEESNSEDEASFK HHHHHCCCCCHHHHC	56.56	29255136
366	Phosphorylation	SNSEDEASFKSESAQ CCCCCHHHHCCCCCC	31.03	22167270
369	Phosphorylation	EDEASFKSESAQSSP CCHHHHCCCCCCCCC	34.47	21955146
371	Phosphorylation	EASFKSESAQSSPSN HHHHCCCCCCCCCCC	38.40	21955146
372	Ubiquitination	ASFKSESAQSSPSNS HHHCCCCCCCCCCCC	14.82	24816145
374	Phosphorylation	FKSESAQSSPSNSSS HCCCCCCCCCCCCCC	43.89	21955146
375	Phosphorylation	KSESAQSSPSNSSSS CCCCCCCCCCCCCCC	21.92	21955146
377	Phosphorylation	ESAQSSPSNSSSSSD CCCCCCCCCCCCCCC	51.82	21955146
379	Phosphorylation	AQSSPSNSSSSSDSS CCCCCCCCCCCCCCC	35.61	21955146
380	Phosphorylation	QSSPSNSSSSSDSSS CCCCCCCCCCCCCCC	38.19	21955146
381	Phosphorylation	SSPSNSSSSSDSSSD CCCCCCCCCCCCCCC	33.41	21955146
382	Phosphorylation	SPSNSSSSSDSSSDS CCCCCCCCCCCCCCC	39.86	21955146
383	Phosphorylation	PSNSSSSSDSSSDSD CCCCCCCCCCCCCCC	43.38	21955146
383	Ubiquitination	PSNSSSSSDSSSDSD CCCCCCCCCCCCCCC	43.38	24816145
385	Phosphorylation	NSSSSSDSSSDSDFE CCCCCCCCCCCCCCC	33.42	21955146
386	Phosphorylation	SSSSSDSSSDSDFEP CCCCCCCCCCCCCCC	43.06	21955146
387	Phosphorylation	SSSSDSSSDSDFEPS CCCCCCCCCCCCCCC	45.12	21955146
389	Phosphorylation	SSDSSSDSDFEPSQN CCCCCCCCCCCCCCC	46.26	21955146
394	Phosphorylation	SDSDFEPSQNHSQGP CCCCCCCCCCCCCCC	36.09	21955146
398	Phosphorylation	FEPSQNHSQGPLRSM CCCCCCCCCCCHHHH	44.36	30576142
404	Phosphorylation	HSQGPLRSMVEDLQS CCCCCHHHHHHHHHH	34.56	18691976
411	Phosphorylation	SMVEDLQSEESDEDD HHHHHHHHCCCCCCC	51.10	25137130
414	Phosphorylation	EDLQSEESDEDDSSS HHHHHCCCCCCCCCC	42.10	25072903
419	Phosphorylation	EESDEDDSSSGEEAA CCCCCCCCCCHHHHC	38.43	25072903
420	Phosphorylation	ESDEDDSSSGEEAAG CCCCCCCCCHHHHCC	49.73	25072903
421	Phosphorylation	SDEDDSSSGEEAAGK CCCCCCCCHHHHCCC	54.93	25072903
435	Phosphorylation	KTNPGRDSRLSFSDS CCCCCCCCCCCCCCC	33.49	23663014
438	Phosphorylation	PGRDSRLSFSDSESD CCCCCCCCCCCCCCC	22.92	30266825
440	Phosphorylation	RDSRLSFSDSESDNS CCCCCCCCCCCCCCC	36.53	30266825
442	Phosphorylation	SRLSFSDSESDNSAD CCCCCCCCCCCCCCC	37.49	30266825
444	Phosphorylation	LSFSDSESDNSADSS CCCCCCCCCCCCCCC	46.15	30266825
447	Phosphorylation	SDSESDNSADSSLPS CCCCCCCCCCCCCCC	38.14	30266825
450	Phosphorylation	ESDNSADSSLPSREP CCCCCCCCCCCCCCC	33.23	29888752
451	Phosphorylation	SDNSADSSLPSREPP CCCCCCCCCCCCCCC	44.86	29888752
454	Phosphorylation	SADSSLPSREPPPPQ CCCCCCCCCCCCCCC	55.35	24144214
468	Phosphorylation	QKPPPPNSKVSGRRS CCCCCCCCCCCCCCC	39.96	24144214
471	Phosphorylation	PPPNSKVSGRRSPES CCCCCCCCCCCCHHH	30.25	23403867
475	Phosphorylation	SKVSGRRSPESCSKP CCCCCCCCHHHCCCH	31.49	20164059
478	Phosphorylation	SGRRSPESCSKPEKI CCCCCHHHCCCHHHH	27.37	23927012
480	Phosphorylation	RRSPESCSKPEKILK CCCHHHCCCHHHHHH	61.60	23927012
490	Phosphorylation	EKILKKGTYDKAYTD HHHHHCCCCCHHHHH	37.11	-
491	Phosphorylation	KILKKGTYDKAYTDE HHHHCCCCCHHHHHH	24.90	-

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
394	S	Phosphorylation	Kinase	ATM	Q13315	PSP
398	S	Phosphorylation	Kinase	ATM	Q13315	PSP

Functions of PTM Sites

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

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 ENL_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
CBX8_HUMAN	CBX8	physical	11313972
AFF1_HUMAN	AFF1	physical	19956800
CDK9_HUMAN	CDK9	physical	19956800
RFX5_HUMAN	RFX5	physical	20431927
AFF1_HUMAN	AFF1	physical	20431927
AFF4_HUMAN	AFF4	physical	20431927
CSK21_HUMAN	CSNK2A1	physical	20431927
CDK9_HUMAN	CDK9	physical	20431927
DOT1L_HUMAN	DOT1L	physical	20431927
BCOR_HUMAN	BCOR	physical	20431927
CBX8_HUMAN	CBX8	physical	20431927
RFXAP_HUMAN	RFXAP	physical	20431927
AF10_HUMAN	MLLT10	physical	20431927
ACACA_HUMAN	ACACA	physical	20431927
CHD1_HUMAN	CHD1	physical	20431927
ELL_HUMAN	ELL	physical	20431927
SIR1_HUMAN	SIRT1	physical	20431927
AF17_HUMAN	MLLT6	physical	20431927
AFF4_HUMAN	AFF4	physical	20153263
CCNT1_HUMAN	CCNT1	physical	20153263
CDK9_HUMAN	CDK9	physical	20153263
AFF1_HUMAN	AFF1	physical	20153263
DOT1L_HUMAN	DOT1L	physical	20153263
KMT2A_HUMAN	KMT2A	physical	20153263
BRD4_HUMAN	BRD4	physical	21964340
AFF4_HUMAN	AFF4	physical	21873227
AF9_HUMAN	MLLT3	physical	21873227
CDK9_HUMAN	CDK9	physical	21873227
ELL2_HUMAN	ELL2	physical	21873227
DOT1L_HUMAN	DOT1L	physical	21873227
PAF1_HUMAN	PAF1	physical	21873227
RPB1_HUMAN	POLR2A	physical	21873227
AFF1_HUMAN	AFF1	physical	15856011
AFF4_HUMAN	AFF4	physical	15856011
AF10_HUMAN	MLLT10	physical	15856011
CBX8_HUMAN	CBX8	physical	15856011
H31T_HUMAN	HIST3H3	physical	15856011
H15_HUMAN	HIST1H1B	physical	15856011
AFF1_HUMAN	AFF1	physical	25921070
CDK9_HUMAN	CDK9	physical	25921070
RING2_HUMAN	RNF2	physical	25921070
RL12_HUMAN	RPL12	physical	25921070
RM12_HUMAN	MRPL12	physical	25921070
H2A2C_HUMAN	HIST2H2AC	physical	25921070
H2AX_HUMAN	H2AFX	physical	25921070
H2B2E_HUMAN	HIST2H2BE	physical	25921070
BMI1_HUMAN	BMI1	physical	25921070
PAF1_HUMAN	PAF1	physical	25921070
AFF4_HUMAN	AFF4	physical	25921070

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 ENL_HUMAN

Related Literatures of Post-Translational Modification

Acetylation
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: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND MASS SPECTROMETRY.	19413330 [Abstract]
"Lysine acetylation targets protein complexes and co-regulates majorcellular functions."; Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.,Olsen J.V., Mann M.; Science 325:834-840(2009). Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-252, AND MASS SPECTROMETRY.	19608861 [Abstract]
Phosphorylation
Reference	PubMed
"Large-scale proteomics analysis of the human kinome."; Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G.,Mann M., Daub H.; Mol. Cell. Proteomics 8:1751-1764(2009). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-155; THR-289; SER-292AND THR-314, AND MASS SPECTROMETRY.	19369195 [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-155, AND MASSSPECTROMETRY.	18669648 [Abstract]
"Kinase-selective enrichment enables quantitative phosphoproteomics ofthe kinome across the cell cycle."; Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,Greff Z., Keri G., Stemmann O., Mann M.; Mol. Cell 31:438-448(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-292; SER-296 ANDSER-315, AND MASS SPECTROMETRY.	18691976 [Abstract]
"Improved titanium dioxide enrichment of phosphopeptides from HeLacells and high confident phosphopeptide identification by cross-validation of MS/MS and MS/MS/MS spectra."; Yu L.-R., Zhu Z., Chan K.C., Issaq H.J., Dimitrov D.S., Veenstra T.D.; J. Proteome Res. 6:4150-4162(2007). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-292, AND MASSSPECTROMETRY.	17924679 [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-209; SER-359; SER-361;SER-366 AND SER-475, AND MASS SPECTROMETRY.	17081983 [Abstract]