dbPTM

NELFB_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	NELFB_HUMAN
UniProt AC	Q8WX92
Protein Name	Negative elongation factor B
Gene Name	NELFB
Organism	Homo sapiens (Human).
Sequence Length	580
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. Binds RNA which may help to stabilize the NELF complex on nucleic acid. In vitro, binds weakly to the HIV-1 TAR RNA which is located in the long terminal repeat (LTR) of HIV-1. May be able to induce chromatin unfolding..
Protein Sequence	MFAGLQDLGVANGEDLKETLTNCTEPLKAIEQFQTENGVLLPSLQSALPFLDLHGTPRLEFHQSVFDELRDKLLERVSAIASEGKAEERYKKLEDLLEKSFSLVKMPSLQPVVMCVMKHLPKVPEKKLKLVMADKELYRACAVEVKRQIWQDNQALFGDEVSPLLKQYILEKESALFSTELSVLHNFFSPSPKTRRQGEVVQRLTRMVGKNVKLYDMVLQFLRTLFLRTRNVHYCTLRAELLMSLHDLDVGEICTVDPCHKFTWCLDACIRERFVDSKRARELQGFLDGVKKGQEQVLGDLSMILCDPFAINTLALSTVRHLQELVGQETLPRDSPDLLLLLRLLALGQGAWDMIDSQVFKEPKMEVELITRFLPMLMSFLVDDYTFNVDQKLPAEEKAPVSYPNTLPESFTKFLQEQRMACEVGLYYVLHITKQRNKNALLRLLPGLVETFGDLAFGDIFLHLLTGNLALLADEFALEDFCSSLFDGFFLTASPRKENVHRHALRLLIHLHPRVAPSKLEALQKALEPTGQSGEAVKELYSQLGEKLEQLDHRKPSPAQAAETPALELPLPSVPAPAPL

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
56	Phosphorylation	PFLDLHGTPRLEFHQ CCCCCCCCCCHHHCH	8.42	25159151
78	Phosphorylation	DKLLERVSAIASEGK HHHHHHHHHHHHCCC	21.85	21406692
82	Phosphorylation	ERVSAIASEGKAEER HHHHHHHHCCCHHHH	40.54	21406692
85	Ubiquitination	SAIASEGKAEERYKK HHHHHCCCHHHHHHH	48.88	21890473
85	Acetylation	SAIASEGKAEERYKK HHHHHCCCHHHHHHH	48.88	26051181
90	Phosphorylation	EGKAEERYKKLEDLL CCCHHHHHHHHHHHH	18.76	29083192
99	Ubiquitination	KLEDLLEKSFSLVKM HHHHHHHHHCHHCCC	57.69	21890473
100	Phosphorylation	LEDLLEKSFSLVKMP HHHHHHHHCHHCCCC	15.64	21712546
102	Phosphorylation	DLLEKSFSLVKMPSL HHHHHHCHHCCCCCC	39.07	20860994
108	Phosphorylation	FSLVKMPSLQPVVMC CHHCCCCCCHHHHHH	35.82	20860994
133	Ubiquitination	KKLKLVMADKELYRA HHHHHHCCCHHHHHH	19.76	33845483
135	2-Hydroxyisobutyrylation	LKLVMADKELYRACA HHHHCCCHHHHHHHH	39.83	-
135	Ubiquitination	LKLVMADKELYRACA HHHHCCCHHHHHHHH	39.83	21890473
135	Acetylation	LKLVMADKELYRACA HHHHCCCHHHHHHHH	39.83	23954790
140	Ubiquitination	ADKELYRACAVEVKR CCHHHHHHHHHHHHH	3.37	29967540
146	Ubiquitination	RACAVEVKRQIWQDN HHHHHHHHHHHHHCC	25.69	-
146	Acetylation	RACAVEVKRQIWQDN HHHHHHHHHHHHHCC	25.69	25953088
146	2-Hydroxyisobutyrylation	RACAVEVKRQIWQDN HHHHHHHHHHHHHCC	25.69	-
147	Ubiquitination	ACAVEVKRQIWQDNQ HHHHHHHHHHHHCCH	38.09	21890473
162	Phosphorylation	ALFGDEVSPLLKQYI HHHCCCCHHHHHHHH	14.05	24719451
166	Ubiquitination	DEVSPLLKQYILEKE CCCHHHHHHHHHHHH	49.06	-
183	Ubiquitination	LFSTELSVLHNFFSP HHHCHHHHHHHHCCC	11.16	21890473
189	Phosphorylation	SVLHNFFSPSPKTRR HHHHHHCCCCCCCCC	21.96	25159151
191	Phosphorylation	LHNFFSPSPKTRRQG HHHHCCCCCCCCCHH	37.52	25159151
194	Ubiquitination	FFSPSPKTRRQGEVV HCCCCCCCCCHHHHH	34.17	24816145
205	Phosphorylation	GEVVQRLTRMVGKNV HHHHHHHHHHHCCCC	20.93	24719451
213	Ubiquitination	RMVGKNVKLYDMVLQ HHHCCCCHHHHHHHH	51.20	-
214	Ubiquitination	MVGKNVKLYDMVLQF HHCCCCHHHHHHHHH	3.69	29967540
291	Ubiquitination	QGFLDGVKKGQEQVL HHHHHHHHHCHHHHH	57.63	21890473
330	Phosphorylation	QELVGQETLPRDSPD HHHHCCCCCCCCCHH	33.89	-
335	Phosphorylation	QETLPRDSPDLLLLL CCCCCCCCHHHHHHH	22.92	21712546
339	Ubiquitination	PRDSPDLLLLLRLLA CCCCHHHHHHHHHHH	4.06	22817900
340	Ubiquitination	RDSPDLLLLLRLLAL CCCHHHHHHHHHHHH	5.71	22817900
357	Phosphorylation	GAWDMIDSQVFKEPK CHHHHHCCHHHCCCC	19.81	20068231
361	Ubiquitination	MIDSQVFKEPKMEVE HHCCHHHCCCCHHHH	74.40	21890473
398	Ubiquitination	QKLPAEEKAPVSYPN CCCCHHHCCCCCCCC	49.88	21890473
402	Phosphorylation	AEEKAPVSYPNTLPE HHHCCCCCCCCCCCH	33.54	20068231
403	Phosphorylation	EEKAPVSYPNTLPES HHCCCCCCCCCCCHH	10.75	30576142
406	Phosphorylation	APVSYPNTLPESFTK CCCCCCCCCCHHHHH	38.90	30576142
409	Ubiquitination	SYPNTLPESFTKFLQ CCCCCCCHHHHHHHH	62.69	22817900
410	Phosphorylation	YPNTLPESFTKFLQE CCCCCCHHHHHHHHH	35.95	24719451
412	Ubiquitination	NTLPESFTKFLQEQR CCCCHHHHHHHHHHH	30.11	22817900
412	Phosphorylation	NTLPESFTKFLQEQR CCCCHHHHHHHHHHH	30.11	20068231
413	Ubiquitination	TLPESFTKFLQEQRM CCCHHHHHHHHHHHH	41.91	21890473
413	Acetylation	TLPESFTKFLQEQRM CCCHHHHHHHHHHHH	41.91	26051181
440	Ubiquitination	TKQRNKNALLRLLPG HHHCCHHHHHHHHHH	15.02	23503661
446	Ubiquitination	NALLRLLPGLVETFG HHHHHHHHHHHHHHH	38.37	22817900
454	Phosphorylation	GLVETFGDLAFGDIF HHHHHHHHHHHHHHH	30.54	20068231
461	Ubiquitination	DLAFGDIFLHLLTGN HHHHHHHHHHHHHCC	4.12	21963094
518	Phosphorylation	LHPRVAPSKLEALQK HCCCCCHHHHHHHHH	39.89	22210691
519	Ubiquitination	HPRVAPSKLEALQKA CCCCCHHHHHHHHHH	49.65	21890473
519	Acetylation	HPRVAPSKLEALQKA CCCCCHHHHHHHHHH	49.65	19608861
525	Ubiquitination	SKLEALQKALEPTGQ HHHHHHHHHHCCCCC	56.65	-
533	Phosphorylation	ALEPTGQSGEAVKEL HHCCCCCCHHHHHHH	39.69	-
538	Ubiquitination	GQSGEAVKELYSQLG CCCHHHHHHHHHHHH	49.39	21890473
541	Phosphorylation	GEAVKELYSQLGEKL HHHHHHHHHHHHHHH	8.75	-
555	Ubiquitination	LEQLDHRKPSPAQAA HHHCCCCCCCHHHHC	46.56	-
557	Phosphorylation	QLDHRKPSPAQAAET HCCCCCCCHHHHCCC	35.58	29255136
564	Phosphorylation	SPAQAAETPALELPL CHHHHCCCCCCCCCC	14.77	29255136
567	Ubiquitination	QAAETPALELPLPSV HHCCCCCCCCCCCCC	7.96	22817900
567	Acetylation	QAAETPALELPLPSV HHCCCCCCCCCCCCC	7.96	19608861
573	Ubiquitination	ALELPLPSVPAPAPL CCCCCCCCCCCCCCC	48.71	29967540
573	Phosphorylation	ALELPLPSVPAPAPL CCCCCCCCCCCCCCC	48.71	23927012
586	Ubiquitination	PL------------- CC-------------		22817900
595	Ubiquitination	---------------------- ----------------------		29967540
603	Ubiquitination	------------------------------ ------------------------------		23503661
605	Phosphorylation	-------------------------------- --------------------------------		19664995
612	Phosphorylation	--------------------------------------- ---------------------------------------		20068231
621	Phosphorylation	------------------------------------------------ ------------------------------------------------		17081983

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 NELFB_HUMAN !!

Functions of PTM Sites

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

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
JUN_HUMAN	JUN	physical	15530430
FOS_HUMAN	FOS	physical	15530430
ESR1_HUMAN	ESR1	physical	15342491
AL3A2_HUMAN	ALDH3A2	physical	20305087
AT1A1_HUMAN	ATP1A1	physical	20305087
TCPQ_HUMAN	CCT8	physical	20305087
MSH2_HUMAN	MSH2	physical	20305087
NELFE_HUMAN	NELFE	physical	20305087
RPN1_HUMAN	RPN1	physical	20305087
NELFB_HUMAN	NELFB	physical	11940650
SPT5H_HUMAN	SUPT5H	physical	11940650
RPB1_HUMAN	POLR2A	physical	11940650
GRP75_HUMAN	HSPA9	physical	20195357
KHDR3_HUMAN	KHDRBS3	physical	20195357
MGST1_HUMAN	MGST1	physical	20195357
DENR_HUMAN	DENR	physical	20195357
ABCF1_HUMAN	ABCF1	physical	22863883
HNRPU_HUMAN	HNRNPU	physical	22863883
IF2B3_HUMAN	IGF2BP3	physical	22863883
ILF2_HUMAN	ILF2	physical	22863883
MRE11_HUMAN	MRE11A	physical	22863883
NMT1_HUMAN	NMT1	physical	22863883
PTBP1_HUMAN	PTBP1	physical	22863883
RFC4_HUMAN	RFC4	physical	22863883
RL23A_HUMAN	RPL23A	physical	22863883
HNRPQ_HUMAN	SYNCRIP	physical	22863883
YBOX1_HUMAN	YBX1	physical	22863883

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 NELFB_HUMAN

Related Literatures of Post-Translational Modification

Acetylation
Reference	PubMed
"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-519, AND MASS SPECTROMETRY.	19608861 [Abstract]
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-557, 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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-557, AND MASSSPECTROMETRY.	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-557, AND MASSSPECTROMETRY.	18669648 [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-557, AND MASSSPECTROMETRY.	16964243 [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-557, AND MASSSPECTROMETRY.	15302935 [Abstract]