dbPTM

NELFE_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	NELFE_HUMAN
UniProt AC	P18615
Protein Name	Negative elongation factor E
Gene Name	NELFE
Organism	Homo sapiens (Human).
Sequence Length	380
Subcellular Localization	Nucleus.
Protein Description	Essential component of the NELF complex, a complex that negatively regulates the elongation of transcription by RNA polymerase II. The NELF complex, which acts via an association with the DSIF complex and causes transcriptional pausing, is counteracted by the P-TEFb kinase complex. The NELF complex is involved in HIV-1 latency possibly involving recruitment of PCF11 to paused RNA polymerase II. Provides the strongest RNA binding activity of the NELF complex and may initially recruit the NELF complex to RNA. Binds to the HIV-1 TAR RNA which is located in the long terminal repeat (LTR) of HIV-1..
Protein Sequence	MLVIPPGLSEEEEALQKKFNKLKKKKKALLALKKQSSSSTTSQGGVKRSLSEQPVMDTATATEQAKQLVKSGAISAIKAETKNSGFKRSRTLEGKLKDPEKGPVPTFQPFQRSISADDDLQESSRRPQRKSLYESFVSSSDRLRELGPDGEEAEGPGAGDGPPRSFDWGYEERSGAHSSASPPRSRSRDRSHERNRDRDRDRERDRDRDRDRDRERDRDRDRDRDRDRERDRDRERDRDRDREGPFRRSDSFPERRAPRKGNTLYVYGEDMTPTLLRGAFSPFGNIIDLSMDPPRNCAFVTYEKMESADQAVAELNGTQVESVQLKVNIARKQPMLDAATGKSVWGSLAVQNSPKGCHRDKRTQIVYSDDVYKENLVDGF

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
9	Phosphorylation	LVIPPGLSEEEEALQ CCCCCCCCHHHHHHH	49.21	28122231
33	2-Hydroxyisobutyrylation	KKALLALKKQSSSST HHHHHHHHHHCCCCC	43.06	-
33	Acetylation	KKALLALKKQSSSST HHHHHHHHHHCCCCC	43.06	25953088
36	Phosphorylation	LLALKKQSSSSTTSQ HHHHHHHCCCCCCCC	40.86	28348404
37	Phosphorylation	LALKKQSSSSTTSQG HHHHHHCCCCCCCCC	26.30	22496350
38	Phosphorylation	ALKKQSSSSTTSQGG HHHHHCCCCCCCCCC	36.63	28348404
39	Phosphorylation	LKKQSSSSTTSQGGV HHHHCCCCCCCCCCC	37.34	28348404
40	Phosphorylation	KKQSSSSTTSQGGVK HHHCCCCCCCCCCCC	32.20	28348404
41	Phosphorylation	KQSSSSTTSQGGVKR HHCCCCCCCCCCCCC	22.47	24114839
42	Phosphorylation	QSSSSTTSQGGVKRS HCCCCCCCCCCCCCC	27.24	24114839
47	Sumoylation	TTSQGGVKRSLSEQP CCCCCCCCCCCCCCC	39.27	-
47	Sumoylation	TTSQGGVKRSLSEQP CCCCCCCCCCCCCCC	39.27	-
49	Phosphorylation	SQGGVKRSLSEQPVM CCCCCCCCCCCCCCC	30.45	29255136
51	Phosphorylation	GGVKRSLSEQPVMDT CCCCCCCCCCCCCCC	35.12	29255136
56	Sulfoxidation	SLSEQPVMDTATATE CCCCCCCCCCHHHHH	4.89	21406390
58	Phosphorylation	SEQPVMDTATATEQA CCCCCCCCHHHHHHH	14.07	30266825
60	Phosphorylation	QPVMDTATATEQAKQ CCCCCCHHHHHHHHH	35.88	30266825
62	Phosphorylation	VMDTATATEQAKQLV CCCCHHHHHHHHHHH	25.03	23927012
71	Phosphorylation	QAKQLVKSGAISAIK HHHHHHHHCCHHHHE	26.44	25159151
75	Phosphorylation	LVKSGAISAIKAETK HHHHCCHHHHEEHHC	24.33	25159151
78	Sumoylation	SGAISAIKAETKNSG HCCHHHHEEHHCCCC	39.63	-
78	Sumoylation	SGAISAIKAETKNSG HCCHHHHEEHHCCCC	39.63	25114211
78	Acetylation	SGAISAIKAETKNSG HCCHHHHEEHHCCCC	39.63	25953088
82	Sumoylation	SAIKAETKNSGFKRS HHHEEHHCCCCCCCC	40.39	28112733
84	Phosphorylation	IKAETKNSGFKRSRT HEEHHCCCCCCCCEE	47.35	21857030
89	Phosphorylation	KNSGFKRSRTLEGKL CCCCCCCCEEECCCC	30.15	22817900
91	Phosphorylation	SGFKRSRTLEGKLKD CCCCCCEEECCCCCC	30.33	29900121
95	Ubiquitination	RSRTLEGKLKDPEKG CCEEECCCCCCCCCC	42.88	-
97	Acetylation	RTLEGKLKDPEKGPV EEECCCCCCCCCCCC	74.79	25953088
101	Acetylation	GKLKDPEKGPVPTFQ CCCCCCCCCCCCCCC	74.11	25953088
106	Phosphorylation	PEKGPVPTFQPFQRS CCCCCCCCCCCCCCC	34.83	26074081
113	Phosphorylation	TFQPFQRSISADDDL CCCCCCCCCCCCCCH	15.31	22167270
115	Phosphorylation	QPFQRSISADDDLQE CCCCCCCCCCCCHHH	27.22	19664994
123	Phosphorylation	ADDDLQESSRRPQRK CCCCHHHHCCCHHHH	19.04	25159151
124	Phosphorylation	DDDLQESSRRPQRKS CCCHHHHCCCHHHHH	31.40	23927012
130	Ubiquitination	SSRRPQRKSLYESFV HCCCHHHHHHHHHHH	39.30	21890473
130	Ubiquitination	SSRRPQRKSLYESFV HCCCHHHHHHHHHHH	39.30	21890473
131	Phosphorylation	SRRPQRKSLYESFVS CCCHHHHHHHHHHHC	38.07	25159151
133	Phosphorylation	RPQRKSLYESFVSSS CHHHHHHHHHHHCCH	19.33	22167270
135	Phosphorylation	QRKSLYESFVSSSDR HHHHHHHHHHCCHHH	19.86	23927012
138	Phosphorylation	SLYESFVSSSDRLRE HHHHHHHCCHHHHHH	23.32	23927012
139	Phosphorylation	LYESFVSSSDRLREL HHHHHHCCHHHHHHH	30.84	23927012
140	Phosphorylation	YESFVSSSDRLRELG HHHHHCCHHHHHHHC	21.17	23927012
142	Methylation	SFVSSSDRLRELGPD HHHCCHHHHHHHCCC	37.28	115490999
165	Phosphorylation	AGDGPPRSFDWGYEE CCCCCCCCCCCCCCC	33.07	22115753
170	Phosphorylation	PRSFDWGYEERSGAH CCCCCCCCCCCCCCC	15.46	28796482
174	Phosphorylation	DWGYEERSGAHSSAS CCCCCCCCCCCCCCC	43.54	30266825
178	Phosphorylation	EERSGAHSSASPPRS CCCCCCCCCCCCCCC	27.37	30266825
179	Phosphorylation	ERSGAHSSASPPRSR CCCCCCCCCCCCCCC	23.93	23927012
181	Phosphorylation	SGAHSSASPPRSRSR CCCCCCCCCCCCCCC	37.07	23927012
185	Phosphorylation	SSASPPRSRSRDRSH CCCCCCCCCCCCCCH	40.14	26055452
187	Phosphorylation	ASPPRSRSRDRSHER CCCCCCCCCCCCHHH	39.52	28464451
191	Phosphorylation	RSRSRDRSHERNRDR CCCCCCCCHHHHHHH	33.71	20068231
249	Phosphorylation	REGPFRRSDSFPERR CCCCCCCCCCCCCCC	33.09	30266825
251	Phosphorylation	GPFRRSDSFPERRAP CCCCCCCCCCCCCCC	43.90	25159151
263	Phosphorylation	RAPRKGNTLYVYGED CCCCCCCEEEEECCC	28.30	29978859
265	Phosphorylation	PRKGNTLYVYGEDMT CCCCCEEEEECCCCC	6.92	18669648
267	Phosphorylation	KGNTLYVYGEDMTPT CCCEEEEECCCCCHH	10.97	18669648
272	Phosphorylation	YVYGEDMTPTLLRGA EEECCCCCHHHHCCC	25.99	25159151
274	Phosphorylation	YGEDMTPTLLRGAFS ECCCCCHHHHCCCCC	29.29	21082442
281	Phosphorylation	TLLRGAFSPFGNIID HHHCCCCCCCCCEEE	20.84	25159151
332	Ubiquitination	LKVNIARKQPMLDAA EEEEHHHHCCCCHHH	50.13	-
340	Phosphorylation	QPMLDAATGKSVWGS CCCCHHHCCCCHHHH	47.03	20044836
343	Phosphorylation	LDAATGKSVWGSLAV CHHHCCCCHHHHHHH	25.17	26074081
347	Phosphorylation	TGKSVWGSLAVQNSP CCCCHHHHHHHCCCC	9.46	20044836
353	Phosphorylation	GSLAVQNSPKGCHRD HHHHHCCCCCCCCCC	15.76	19664994
363	Phosphorylation	GCHRDKRTQIVYSDD CCCCCCCCEEEECCC	28.52	22210691
367	Phosphorylation	DKRTQIVYSDDVYKE CCCCEEEECCCHHHH	14.17	25159151
368	Phosphorylation	KRTQIVYSDDVYKEN CCCEEEECCCHHHHH	19.21	28387310
372	Phosphorylation	IVYSDDVYKENLVDG EEECCCHHHHHCCCC	21.41	22210691

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
51	S	Phosphorylation	Kinase	MAPKAPK2	P49137	PSP
115	S	Phosphorylation	Kinase	MAPKAPK2	P49137	PSP
131	S	Phosphorylation	Kinase	AURKB	Q96GD4	GPS
251	S	Phosphorylation	Kinase	MAPKAPK2	P49137	PSP

Functions of PTM Sites

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

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
NELFB_HUMAN	NELFB	physical	14667819
NCOR1_HUMAN	NCOR1	physical	14667819
CATIN_HUMAN	CACTIN	physical	14667819
NELFA_HUMAN	NELFA	physical	12612062
NELFB_HUMAN	NELFB	physical	12612062
NELFD_HUMAN	NELFCD	physical	12612062
RPB1_HUMAN	POLR2A	physical	12612062
VAMP3_HUMAN	VAMP3	physical	16169070
NELFB_HUMAN	NELFB	physical	20305087
SF3B1_HUMAN	SF3B1	physical	20305087
NELFD_HUMAN	NELFCD	physical	20305087
TM141_HUMAN	TMEM141	physical	20305087
NELFA_HUMAN	NELFA	physical	20305087
MTUS2_HUMAN	MTUS2	physical	25416956
CCD57_HUMAN	CCDC57	physical	25416956
NELFA_HUMAN	NELFA	physical	26186194
NELFD_HUMAN	NELFCD	physical	26186194
NELFB_HUMAN	NELFB	physical	26186194
SMBP2_HUMAN	IGHMBP2	physical	26186194
RRP44_HUMAN	DIS3	physical	26186194
NELFA_HUMAN	NELFA	physical	26496610
NELFB_HUMAN	NELFB	physical	26496610
RSRC1_HUMAN	RSRC1	physical	26496610
NELFD_HUMAN	NELFCD	physical	26496610
NELFA_HUMAN	NELFA	physical	28514442
NELFD_HUMAN	NELFCD	physical	28514442
NELFB_HUMAN	NELFB	physical	28514442
SMBP2_HUMAN	IGHMBP2	physical	28514442
RRP44_HUMAN	DIS3	physical	28514442

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 NELFE_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-51; SER-131 AND SER-353,AND MASS SPECTROMETRY.	19690332 [Abstract]
"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-115, AND MASSSPECTROMETRY.	19369195 [Abstract]
"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 SER-115 AND SER-353, ANDMASS 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-113; SER-131; SER-251;TYR-265; TYR-267; THR-272; THR-274; SER-281 AND SER-353, 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-115, AND MASSSPECTROMETRY.	18691976 [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-131 AND SER-281, ANDMASS SPECTROMETRY.	18220336 [Abstract]
"Automated phosphoproteome analysis for cultured cancer cells by two-dimensional nanoLC-MS using a calcined titania/C18 biphasic column."; Imami K., Sugiyama N., Kyono Y., Tomita M., Ishihama Y.; Anal. Sci. 24:161-166(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-51, AND MASSSPECTROMETRY.	18187866 [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-115, AND MASSSPECTROMETRY.	19007248 [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-181, AND MASSSPECTROMETRY.	17924679 [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-115 AND SER-353, ANDMASS SPECTROMETRY.	16964243 [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-115 AND SER-191, ANDMASS SPECTROMETRY.	17081983 [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 SER-115, AND MASSSPECTROMETRY.	15302935 [Abstract]