dbPTM

NELFA_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	NELFA_HUMAN
UniProt AC	Q9H3P2
Protein Name	Negative elongation factor A
Gene Name	NELFA
Organism	Homo sapiens (Human).
Sequence Length	528
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. In vitro, the NELFA:NELFCD subcomplex binds to ssDNA and ssRNA in a sequence- and structure-dependent manner. Probably required to interact with the RNA polymerase II complex..
Protein Sequence	MASMRESDTGLWLHNKLGATDELWAPPSIASLLTAAVIDNIRLCFHGLSSAVKLKLLLGTLHLPRRTVDEMKGALMEIIQLASLDSDPWVLMVADILKSFPDTGSLNLELEEQNPNVQDILGELREKVGECEASAMLPLECQYLNKNALTTLAGPLTPPVKHFQLKRKPKSATLRAELLQKSTETAQQLKRSAGVPFHAKGRGLLRKMDTTTPLKGIPKQAPFRSPTAPSVFSPTGNRTPIPPSRTLLRKERGVKLLDISELDMVGAGREAKRRRKTLDAEVVEKPAKEETVVENATPDYAAGLVSTQKLGSLNNEPALPSTSYLPSTPSVVPASSYIPSSETPPAPSSREASRPPEEPSAPSPTLPAQFKQRAPMYNSGLSPATPTPAAPTSPLTPTTPPAVAPTTQTPPVAMVAPQTQAPAQQQPKKNLSLTREQMFAAQEMFKTANKVTRPEKALILGFMAGSRENPCQEQGDVIQIKLSEHTEDLPKADGQGSTTMLVDTVFEMNYATGQWTRFKKYKPMTNVS

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
2	Acetylation	------MASMRESDT ------CCCCCCCCC	16.43	-
7	Phosphorylation	-MASMRESDTGLWLH -CCCCCCCCCCCCCC	30.06	25159151
9	Phosphorylation	ASMRESDTGLWLHNK CCCCCCCCCCCCCCC	43.37	24719451
14 (in isoform 7)	Phosphorylation	-	20.14	29507054
60	Phosphorylation	KLKLLLGTLHLPRRT HHHHHHCCCCCCCCC	15.80	-
83	Phosphorylation	MEIIQLASLDSDPWV HHHHHHHCCCCCCCH	41.10	25599653
108 (in isoform 7)	Ubiquitination	-	10.89	21890473
127	Ubiquitination	ILGELREKVGECEAS HHHHHHHHHCCCHHH	49.45	-
138	Ubiquitination	CEASAMLPLECQYLN CHHHHCCEEEHHHCC	17.02	-
150	Phosphorylation	YLNKNALTTLAGPLT HCCCCCCHHHCCCCC	19.84	23403867
151	Phosphorylation	LNKNALTTLAGPLTP CCCCCCHHHCCCCCC	18.56	23403867
157	Phosphorylation	TTLAGPLTPPVKHFQ HHHCCCCCCCCCCEE	28.78	27273156
161	Acetylation	GPLTPPVKHFQLKRK CCCCCCCCCEECCCC	44.46	25953088
161	Ubiquitination	GPLTPPVKHFQLKRK CCCCCCCCCEECCCC	44.46	-
168	Phosphorylation	KHFQLKRKPKSATLR CCEECCCCCCCHHHH	56.03	19664995
172	Ubiquitination	LKRKPKSATLRAELL CCCCCCCHHHHHHHH	19.44	-
178	Phosphorylation	SATLRAELLQKSTET CHHHHHHHHHHHHHH	6.31	16964243
190	2-Hydroxyisobutyrylation	TETAQQLKRSAGVPF HHHHHHHHHHCCCCC	39.71	-
190	Methylation	TETAQQLKRSAGVPF HHHHHHHHHHCCCCC	39.71	115978531
190	Ubiquitination	TETAQQLKRSAGVPF HHHHHHHHHHCCCCC	39.71	-
192	Phosphorylation	TAQQLKRSAGVPFHA HHHHHHHHCCCCCCC	27.99	25159151
192	Ubiquitination	TAQQLKRSAGVPFHA HHHHHHHHCCCCCCC	27.99	-
200	Methylation	AGVPFHAKGRGLLRK CCCCCCCCCCHHHHC	40.34	115978539
201	Methylation	GVPFHAKGRGLLRKM CCCCCCCCCHHHHCC	29.67	-
201	Ubiquitination	GVPFHAKGRGLLRKM CCCCCCCCCHHHHCC	29.67	-
202	Methylation	VPFHAKGRGLLRKMD CCCCCCCCHHHHCCC	31.70	115388697
203	Phosphorylation	PFHAKGRGLLRKMDT CCCCCCCHHHHCCCC	37.42	-
210	Phosphorylation	GLLRKMDTTTPLKGI HHHHCCCCCCCCCCC	29.13	29396449
211	Methylation	LLRKMDTTTPLKGIP HHHCCCCCCCCCCCC	23.35	-
211	Phosphorylation	LLRKMDTTTPLKGIP HHHCCCCCCCCCCCC	23.35	21815630
212	Phosphorylation	LRKMDTTTPLKGIPK HHCCCCCCCCCCCCC	28.81	21815630
213	Methylation	RKMDTTTPLKGIPKQ HCCCCCCCCCCCCCC	29.95	-
215	Acetylation	MDTTTPLKGIPKQAP CCCCCCCCCCCCCCC	56.87	25953088
222	Phosphorylation	KGIPKQAPFRSPTAP CCCCCCCCCCCCCCC	23.77	27251275
225	Phosphorylation	PKQAPFRSPTAPSVF CCCCCCCCCCCCCCC	27.29	23401153
227	Phosphorylation	QAPFRSPTAPSVFSP CCCCCCCCCCCCCCC	53.07	30266825
230	Phosphorylation	FRSPTAPSVFSPTGN CCCCCCCCCCCCCCC	33.07	30266825
233	Phosphorylation	PTAPSVFSPTGNRTP CCCCCCCCCCCCCCC	21.28	25159151
235	Phosphorylation	APSVFSPTGNRTPIP CCCCCCCCCCCCCCC	45.98	23927012
236	Phosphorylation	PSVFSPTGNRTPIPP CCCCCCCCCCCCCCC	25.63	24719451
238	Methylation	VFSPTGNRTPIPPSR CCCCCCCCCCCCCCH	43.13	115368673
238	Phosphorylation	VFSPTGNRTPIPPSR CCCCCCCCCCCCCCH	43.13	24719451
239	Phosphorylation	FSPTGNRTPIPPSRT CCCCCCCCCCCCCHH	29.57	22199227
241	Phosphorylation	PTGNRTPIPPSRTLL CCCCCCCCCCCHHHC	8.50	20068231
244	Phosphorylation	NRTPIPPSRTLLRKE CCCCCCCCHHHCHHH	32.32	22199227
246	Phosphorylation	TPIPPSRTLLRKERG CCCCCCHHHCHHHCC	34.19	20068231
249	Methylation	PPSRTLLRKERGVKL CCCHHHCHHHCCCEE	41.73	-
250	Phosphorylation	PSRTLLRKERGVKLL CCHHHCHHHCCCEEE	52.30	-
254	Phosphorylation	LLRKERGVKLLDISE HCHHHCCCEEEEHHH	5.03	15302935
255	Acetylation	LRKERGVKLLDISEL CHHHCCCEEEEHHHH	46.27	25953088
257	Phosphorylation	KERGVKLLDISELDM HHCCCEEEEHHHHCC	4.56	-
260	Phosphorylation	GVKLLDISELDMVGA CCEEEEHHHHCCCCC	31.60	29214152
264	Sulfoxidation	LDISELDMVGAGREA EEHHHHCCCCCCHHH	4.72	21406390
271	Phosphorylation	MVGAGREAKRRRKTL CCCCCHHHHHHHHCC	14.86	-
277	Phosphorylation	EAKRRRKTLDAEVVE HHHHHHHCCCHHHHC	28.23	27273156
285	Acetylation	LDAEVVEKPAKEETV CCHHHHCCCCCCCCE	38.37	23954790
288	Sumoylation	EVVEKPAKEETVVEN HHHCCCCCCCCEECC	65.69	-
288	Phosphorylation	EVVEKPAKEETVVEN HHHCCCCCCCCEECC	65.69	20068231
291	Phosphorylation	EKPAKEETVVENATP CCCCCCCCEECCCCC	30.83	21815630
296	Acetylation	EETVVENATPDYAAG CCCEECCCCCCCHHH	13.65	-
297	Phosphorylation	ETVVENATPDYAAGL CCEECCCCCCCHHHH	28.42	21815630
299	Sumoylation	VVENATPDYAAGLVS EECCCCCCCHHHHHC	41.15	-
300	Phosphorylation	VENATPDYAAGLVST ECCCCCCCHHHHHCC	10.27	29978859
306	Phosphorylation	DYAAGLVSTQKLGSL CCHHHHHCCCHHCCC	30.11	28555341
308	Phosphorylation	AAGLVSTQKLGSLNN HHHHHCCCHHCCCCC	31.32	27251275
312	Phosphorylation	VSTQKLGSLNNEPAL HCCCHHCCCCCCCCC	38.06	22199227
321	Phosphorylation	NNEPALPSTSYLPST CCCCCCCCCCCCCCC	30.73	22199227
322	Phosphorylation	NEPALPSTSYLPSTP CCCCCCCCCCCCCCC	21.32	22199227
323	Phosphorylation	EPALPSTSYLPSTPS CCCCCCCCCCCCCCC	29.07	22199227
324	Phosphorylation	PALPSTSYLPSTPSV CCCCCCCCCCCCCCC	23.79	22199227
327	Phosphorylation	PSTSYLPSTPSVVPA CCCCCCCCCCCCCCH	50.81	22199227
328	Phosphorylation	STSYLPSTPSVVPAS CCCCCCCCCCCCCHH	20.04	22199227
330	Phosphorylation	SYLPSTPSVVPASSY CCCCCCCCCCCHHHC	35.52	22199227
335	Phosphorylation	TPSVVPASSYIPSSE CCCCCCHHHCCCCCC	20.01	22199227
336	Phosphorylation	PSVVPASSYIPSSET CCCCCHHHCCCCCCC	29.23	22199227
337	Phosphorylation	SVVPASSYIPSSETP CCCCHHHCCCCCCCC	17.85	22199227
339	Phosphorylation	VPASSYIPSSETPPA CCHHHCCCCCCCCCC	24.46	27251275
340	Phosphorylation	PASSYIPSSETPPAP CHHHCCCCCCCCCCC	31.11	26074081
341	Phosphorylation	ASSYIPSSETPPAPS HHHCCCCCCCCCCCC	39.89	26074081
343	Phosphorylation	SYIPSSETPPAPSSR HCCCCCCCCCCCCCC	36.20	29496963
348	Phosphorylation	SETPPAPSSREASRP CCCCCCCCCCCCCCC	44.10	22199227
349	Phosphorylation	ETPPAPSSREASRPP CCCCCCCCCCCCCCC	32.83	22199227
351	Phosphorylation	PPAPSSREASRPPEE CCCCCCCCCCCCCCC	53.60	27251275
353	Phosphorylation	APSSREASRPPEEPS CCCCCCCCCCCCCCC	40.33	23927012
360	Phosphorylation	SRPPEEPSAPSPTLP CCCCCCCCCCCCCCC	56.97	30266825
363	Phosphorylation	PEEPSAPSPTLPAQF CCCCCCCCCCCCHHH	30.18	29255136
364	Phosphorylation	EEPSAPSPTLPAQFK CCCCCCCCCCCHHHH	36.57	-
365	Phosphorylation	EPSAPSPTLPAQFKQ CCCCCCCCCCHHHHH	50.11	29255136
371	Phosphorylation	PTLPAQFKQRAPMYN CCCCHHHHHHCCCCC	27.13	18669648
371	Ubiquitination	PTLPAQFKQRAPMYN CCCCHHHHHHCCCCC	27.13	2189047
371 (in isoform 1)	Ubiquitination	-	27.13	21890473
374	Phosphorylation	PAQFKQRAPMYNSGL CHHHHHHCCCCCCCC	7.24	18669648
376	Phosphorylation	QFKQRAPMYNSGLSP HHHHHCCCCCCCCCC	4.89	17081983
382	Ubiquitination	PMYNSGLSPATPTPA CCCCCCCCCCCCCCC	18.93	-
382 (in isoform 7)	Ubiquitination	-	18.93	21890473
385	Phosphorylation	NSGLSPATPTPAAPT CCCCCCCCCCCCCCC	30.95	26074081
387	Phosphorylation	GLSPATPTPAAPTSP CCCCCCCCCCCCCCC	22.62	26074081
392	Phosphorylation	TPTPAAPTSPLTPTT CCCCCCCCCCCCCCC	37.95	26074081
393	Phosphorylation	PTPAAPTSPLTPTTP CCCCCCCCCCCCCCC	19.49	26074081
396	Phosphorylation	AAPTSPLTPTTPPAV CCCCCCCCCCCCCCC	23.21	26074081
398	Phosphorylation	PTSPLTPTTPPAVAP CCCCCCCCCCCCCCC	46.85	22210691
399	Phosphorylation	TSPLTPTTPPAVAPT CCCCCCCCCCCCCCC	28.60	26074081
406	Phosphorylation	TPPAVAPTTQTPPVA CCCCCCCCCCCCCEE	23.07	28348404
407	O-linked_Glycosylation	PPAVAPTTQTPPVAM CCCCCCCCCCCCEEE	29.41	OGP
407	Phosphorylation	PPAVAPTTQTPPVAM CCCCCCCCCCCCEEE	29.41	28348404
409	Phosphorylation	AVAPTTQTPPVAMVA CCCCCCCCCCEEEEC	27.71	28348404
432	Phosphorylation	QQPKKNLSLTREQMF HCCCCCCCCCHHHHH	36.77	24719451
440	Ubiquitination	LTREQMFAAQEMFKT CCHHHHHHHHHHHHH	11.68	-
446	Methylation	FAAQEMFKTANKVTR HHHHHHHHHHCCCCC	45.47	115978547
446	Ubiquitination	FAAQEMFKTANKVTR HHHHHHHHHHCCCCC	45.47	-
457	Methylation	KVTRPEKALILGFMA CCCCHHHHHHHHHHH	9.73	-
457	Ubiquitination	KVTRPEKALILGFMA CCCCHHHHHHHHHHH	9.73	-
521	Phosphorylation	QWTRFKKYKPMTNVS CCCCCEECCCCCCCC	22.40	-
528	Phosphorylation	YKPMTNVS------- CCCCCCCC-------	36.25	25159151
539	Phosphorylation	------------------ ------------------		27251275

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
157	T	Phosphorylation	Kinase	CDK2	P24941	PSP

Functions of PTM Sites

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

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
NELFB_HUMAN	NELFB	physical	12612062
NELFD_HUMAN	NELFCD	physical	12612062
NELFE_HUMAN	NELFE	physical	12612062
RPB1_HUMAN	POLR2A	physical	12612062
AT1A1_HUMAN	ATP1A1	physical	20305087
NELFB_HUMAN	NELFB	physical	20305087
NELFE_HUMAN	NELFE	physical	20305087
NELFD_HUMAN	NELFCD	physical	20305087
A4_HUMAN	APP	physical	21832049
NELFD_HUMAN	NELFCD	physical	25416956
PRR22_HUMAN	PRR22	physical	25416956
RPB1_HUMAN	POLR2A	physical	26496610
RPB2_HUMAN	POLR2B	physical	26496610
RPB3_HUMAN	POLR2C	physical	26496610
SPT5H_HUMAN	SUPT5H	physical	26496610
NELFE_HUMAN	NELFE	physical	26496610
NELFB_HUMAN	NELFB	physical	26496610
NELFD_HUMAN	NELFCD	physical	26496610
INT12_HUMAN	INTS12	physical	26496610
PYM1_HUMAN	WIBG	physical	26496610
NELFD_HUMAN	NELFCD	physical	28514442
NELFB_HUMAN	NELFB	physical	28514442
MCM9_HUMAN	MCM9	physical	28514442
SMBP2_HUMAN	IGHMBP2	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 NELFA_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 ALA-2, PHOSPHORYLATION [LARGESCALE ANALYSIS] AT THR-157 AND THR-277, AND MASS SPECTROMETRY.	19413330 [Abstract]
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-363, AND MASSSPECTROMETRY.	18669648 [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-157 AND SER-233, ANDMASS SPECTROMETRY.	15302935 [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-157, AND MASSSPECTROMETRY.	19690332 [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: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, PHOSPHORYLATION [LARGESCALE ANALYSIS] AT THR-157 AND THR-277, AND MASS SPECTROMETRY.	19413330 [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-157, AND MASSSPECTROMETRY.	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 THR-365, AND MASSSPECTROMETRY.	17081983 [Abstract]