dbPTM

NFKB2_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	NFKB2_HUMAN
UniProt AC	Q00653
Protein Name	Nuclear factor NF-kappa-B p100 subunit
Gene Name	NFKB2
Organism	Homo sapiens (Human).
Sequence Length	900
Subcellular Localization	Nucleus. Cytoplasm. Nuclear, but also found in the cytoplasm in an inactive form complexed to an inhibitor (I-kappa-B).
Protein Description	NF-kappa-B is a pleiotropic transcription factor present in almost all cell types and is the endpoint of a series of signal transduction events that are initiated by a vast array of stimuli related to many biological processes such as inflammation, immunity, differentiation, cell growth, tumorigenesis and apoptosis. NF-kappa-B is a homo- or heterodimeric complex formed by the Rel-like domain-containing proteins RELA/p65, RELB, NFKB1/p105, NFKB1/p50, REL and NFKB2/p52. The dimers bind at kappa-B sites in the DNA of their target genes and the individual dimers have distinct preferences for different kappa-B sites that they can bind with distinguishable affinity and specificity. Different dimer combinations act as transcriptional activators or repressors, respectively. NF-kappa-B is controlled by various mechanisms of post-translational modification and subcellular compartmentalization as well as by interactions with other cofactors or corepressors. NF-kappa-B complexes are held in the cytoplasm in an inactive state complexed with members of the NF-kappa-B inhibitor (I-kappa-B) family. In a conventional activation pathway, I-kappa-B is phosphorylated by I-kappa-B kinases (IKKs) in response to different activators, subsequently degraded thus liberating the active NF-kappa-B complex which translocates to the nucleus. In a non-canonical activation pathway, the MAP3K14-activated CHUK/IKKA homodimer phosphorylates NFKB2/p100 associated with RelB, inducing its proteolytic processing to NFKB2/p52 and the formation of NF-kappa-B RelB-p52 complexes. The NF-kappa-B heterodimeric RelB-p52 complex is a transcriptional activator. The NF-kappa-B p52-p52 homodimer is a transcriptional repressor. NFKB2 appears to have dual functions such as cytoplasmic retention of attached NF-kappa-B proteins by p100 and generation of p52 by a cotranslational processing. The proteasome-mediated process ensures the production of both p52 and p100 and preserves their independent function. p52 binds to the kappa-B consensus sequence 5'-GGRNNYYCC-3', located in the enhancer region of genes involved in immune response and acute phase reactions. p52 and p100 are respectively the minor and major form; the processing of p100 being relatively poor. Isoform p49 is a subunit of the NF-kappa-B protein complex, which stimulates the HIV enhancer in synergy with p65. In concert with RELB, regulates the circadian clock by repressing the transcriptional activator activity of the CLOCK-ARNTL/BMAL1 heterodimer..
Protein Sequence	MESCYNPGLDGIIEYDDFKLNSSIVEPKEPAPETADGPYLVIVEQPKQRGFRFRYGCEGPSHGGLPGASSEKGRKTYPTVKICNYEGPAKIEVDLVTHSDPPRAHAHSLVGKQCSELGICAVSVGPKDMTAQFNNLGVLHVTKKNMMGTMIQKLQRQRLRSRPQGLTEAEQRELEQEAKELKKVMDLSIVRLRFSAFLRASDGSFSLPLKPVISQPIHDSKSPGASNLKISRMDKTAGSVRGGDEVYLLCDKVQKDDIEVRFYEDDENGWQAFGDFSPTDVHKQYAIVFRTPPYHKMKIERPVTVFLQLKRKRGGDVSDSKQFTYYPLVEDKEEVQRKRRKALPTFSQPFGGGSHMGGGSGGAAGGYGGAGGGGSLGFFPSSLAYSPYQSGAGPMGCYPGGGGGAQMAATVPSRDSGEEAAEPSAPSRTPQCEPQAPEMLQRAREYNARLFGLAQRSARALLDYGVTADARALLAGQRHLLTAQDENGDTPLHLAIIHGQTSVIEQIVYVIHHAQDLGVVNLTNHLHQTPLHLAVITGQTSVVSFLLRVGADPALLDRHGDSAMHLALRAGAGAPELLRALLQSGAPAVPQLLHMPDFEGLYPVHLAVRARSPECLDLLVDSGAEVEATERQGGRTALHLATEMEELGLVTHLVTKLRANVNARTFAGNTPLHLAAGLGYPTLTRLLLKAGADIHAENEEPLCPLPSPPTSDSDSDSEGPEKDTRSSFRGHTPLDLTCSTKVKTLLLNAAQNTMEPPLTPPSPAGPGLSLGDTALQNLEQLLDGPEAQGSWAELAERLGLRSLVDTYRQTTSPSGSLLRSYELAGGDLAGLLEALSDMGLEEGVRLLRGPETRDKLPSTAEVKEDSAYGSQSVEQEAEKLGPPPEPPGGLCHGHPQPQVH

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
3	Phosphorylation	-----MESCYNPGLD -----CCCCCCCCCC	22.17	27642862
5	Phosphorylation	---MESCYNPGLDGI ---CCCCCCCCCCCE	33.40	26552605
15	Phosphorylation	GLDGIIEYDDFKLNS CCCCEEEECCCEECC	15.48	27642862
19	Sumoylation	IIEYDDFKLNSSIVE EEEECCCEECCCCCC	54.47	-
22	Phosphorylation	YDDFKLNSSIVEPKE ECCCEECCCCCCCCC	31.70	25159151
23	Phosphorylation	DDFKLNSSIVEPKEP CCCEECCCCCCCCCC	29.58	25159151
28	Ubiquitination	NSSIVEPKEPAPETA CCCCCCCCCCCCCCC	63.92	29967540
34	Phosphorylation	PKEPAPETADGPYLV CCCCCCCCCCCCEEE	29.05	30576142
39	Phosphorylation	PETADGPYLVIVEQP CCCCCCCEEEEEECC	21.09	27642862
47	Ubiquitination	LVIVEQPKQRGFRFR EEEEECCCCCCCCCC	52.93	29967540
55	Phosphorylation	QRGFRFRYGCEGPSH CCCCCCCCCCCCCCC	24.34	20090780
69	Phosphorylation	HGGLPGASSEKGRKT CCCCCCCCCCCCCCC	44.97	27251275
70	Phosphorylation	GGLPGASSEKGRKTY CCCCCCCCCCCCCCC	42.67	27251275
72	Ubiquitination	LPGASSEKGRKTYPT CCCCCCCCCCCCCCE	67.00	21963094
90	Sumoylation	CNYEGPAKIEVDLVT CCCCCCCEEEEEEEE	42.40	-
90	Sumoylation	CNYEGPAKIEVDLVT CCCCCCCEEEEEEEE	42.40	18617892
97	Phosphorylation	KIEVDLVTHSDPPRA EEEEEEEECCCCCCH	23.98	-
99	Phosphorylation	EVDLVTHSDPPRAHA EEEEEECCCCCCHHH	42.31	22817900
108	Phosphorylation	PPRAHAHSLVGKQCS CCCHHHHHHHCCCCC	26.07	22817900
112	Ubiquitination	HAHSLVGKQCSELGI HHHHHHCCCCCCCCC	40.42	29967540
115	Phosphorylation	SLVGKQCSELGICAV HHHCCCCCCCCCEEE	33.10	28857561
123	Phosphorylation	ELGICAVSVGPKDMT CCCCEEEEECCCCCC	11.66	22817900
138	Ubiquitination	AQFNNLGVLHVTKKN HHHCCCCEEEEECHH	3.63	21963094
143	Ubiquitination	LGVLHVTKKNMMGTM CCEEEEECHHHHHHH	40.85	29967540
144	Ubiquitination	GVLHVTKKNMMGTMI CEEEEECHHHHHHHH	40.48	29967540
153	Ubiquitination	MMGTMIQKLQRQRLR HHHHHHHHHHHHHHH	35.35	29967540
161	Phosphorylation	LQRQRLRSRPQGLTE HHHHHHHCCCCCCHH	53.56	30108239
167	Phosphorylation	RSRPQGLTEAEQREL HCCCCCCHHHHHHHH	39.72	23312004
176	Ubiquitination	AEQRELEQEAKELKK HHHHHHHHHHHHHHH	69.44	21963094
179	Ubiquitination	RELEQEAKELKKVMD HHHHHHHHHHHHHHC	63.93	29967540
183	Malonylation	QEAKELKKVMDLSIV HHHHHHHHHHCHHHH	56.25	26320211
187	Ubiquitination	ELKKVMDLSIVRLRF HHHHHHCHHHHHHHH	1.71	21963094
188	Phosphorylation	LKKVMDLSIVRLRFS HHHHHCHHHHHHHHH	18.12	24719451
201	Phosphorylation	FSAFLRASDGSFSLP HHHHHCCCCCCEECC	35.75	30108239
204	Phosphorylation	FLRASDGSFSLPLKP HHCCCCCCEECCCCC	19.36	30108239
206	Phosphorylation	RASDGSFSLPLKPVI CCCCCCEECCCCCEE	30.67	30108239
214	Phosphorylation	LPLKPVISQPIHDSK CCCCCEECCCCCCCC	30.09	30108239
220	Phosphorylation	ISQPIHDSKSPGASN ECCCCCCCCCCCCCC	22.37	30108239
222	Phosphorylation	QPIHDSKSPGASNLK CCCCCCCCCCCCCCE	32.30	30266825
226	Phosphorylation	DSKSPGASNLKISRM CCCCCCCCCCEEEEE	48.92	30108239
229	Acetylation	SPGASNLKISRMDKT CCCCCCCEEEEECCC	42.77	25953088
229	Ubiquitination	SPGASNLKISRMDKT CCCCCCCEEEEECCC	42.77	29967540
231	Phosphorylation	GASNLKISRMDKTAG CCCCCEEEEECCCCC	21.69	24719451
235	Ubiquitination	LKISRMDKTAGSVRG CEEEEECCCCCCCCC	30.82	29967540
239	Phosphorylation	RMDKTAGSVRGGDEV EECCCCCCCCCCCEE	13.23	28555341
252	Ubiquitination	EVYLLCDKVQKDDIE EEEEEECCCCCCCCE	45.64	29967540
253	Ubiquitination	VYLLCDKVQKDDIEV EEEEECCCCCCCCEE	5.66	21963094
277	Phosphorylation	WQAFGDFSPTDVHKQ EEEECCCCCCCHHCC	31.46	20068231
279	Phosphorylation	AFGDFSPTDVHKQYA EECCCCCCCHHCCEE	49.83	20068231
283	Ubiquitination	FSPTDVHKQYAIVFR CCCCCHHCCEEEEEE	44.87	21963094
285	Phosphorylation	PTDVHKQYAIVFRTP CCCHHCCEEEEEECC	11.78	20090780
291	Phosphorylation	QYAIVFRTPPYHKMK CEEEEEECCCCCCCC	19.70	28555341
298	Sumoylation	TPPYHKMKIERPVTV CCCCCCCCCCCCEEE	46.34	-
298	Sumoylation	TPPYHKMKIERPVTV CCCCCCCCCCCCEEE	46.34	18617892
321	Ubiquitination	GGDVSDSKQFTYYPL CCCCCCCCCEEEEEC	55.19	21906983
321 (in isoform 1)	Ubiquitination	-	55.19	21906983
325	Phosphorylation	SDSKQFTYYPLVEDK CCCCCEEEEECCCCH	12.36	-
326	Phosphorylation	DSKQFTYYPLVEDKE CCCCEEEEECCCCHH	6.24	-
332	Ubiquitination	YYPLVEDKEEVQRKR EEECCCCHHHHHHHH	42.12	21963094
345 (in isoform 3)	Phosphorylation	-	36.45	25954137
347 (in isoform 3)	Phosphorylation	-	39.15	25954137
360 (in isoform 3)	Phosphorylation	-	37.01	22210691
367 (in isoform 3)	Phosphorylation	-	16.09	25954137
424	Phosphorylation	GEEAAEPSAPSRTPQ CCCCCCCCCCCCCCC	44.30	21857030
427	Phosphorylation	AAEPSAPSRTPQCEP CCCCCCCCCCCCCCC	48.80	28555341
429	Phosphorylation	EPSAPSRTPQCEPQA CCCCCCCCCCCCCCH	23.27	18669648
464	Phosphorylation	SARALLDYGVTADAR HHHHHHHHCCCHHHH	17.29	27642862
464	Ubiquitination	SARALLDYGVTADAR HHHHHHHHCCCHHHH	17.29	21963094
502	Ubiquitination	AIIHGQTSVIEQIVY EEECCCCHHHHHHHH	17.14	21963094
511	Ubiquitination	IEQIVYVIHHAQDLG HHHHHHHHHHHHHCC	0.78	21963094
513	Ubiquitination	QIVYVIHHAQDLGVV HHHHHHHHHHHCCCE	17.60	21963094
544	Phosphorylation	TGQTSVVSFLLRVGA ECCCHHHHHHHHCCC	14.18	24719451
596	Ubiquitination	VPQLLHMPDFEGLYP HHHHCCCCCCCCCCE	32.18	21963094
612	Phosphorylation	HLAVRARSPECLDLL EEEEECCCHHHHHHH	24.86	30624053
614	Ubiquitination	AVRARSPECLDLLVD EEECCCHHHHHHHCC	49.29	21963094
651	Phosphorylation	MEELGLVTHLVTKLR HHHHCHHHHHHHHHH	17.97	-
655	Phosphorylation	GLVTHLVTKLRANVN CHHHHHHHHHHHCCC	30.62	24719451
656	Ubiquitination	LVTHLVTKLRANVNA HHHHHHHHHHHCCCC	28.61	21963094
656 (in isoform 4)	Ubiquitination	-	28.61	-
680	Phosphorylation	HLAAGLGYPTLTRLL HHCCCCCHHHHHHHH	9.70	27080861
682	Phosphorylation	AAGLGYPTLTRLLLK CCCCCHHHHHHHHHH	32.07	27067055
684	Phosphorylation	GLGYPTLTRLLLKAG CCCHHHHHHHHHHHC	23.04	27080861
689	Sumoylation	TLTRLLLKAGADIHA HHHHHHHHHCCCCCC	44.75	-
689	Sumoylation	TLTRLLLKAGADIHA HHHHHHHHHCCCCCC	44.75	18617892
699	Ubiquitination	ADIHAENEEPLCPLP CCCCCCCCCCCCCCC	53.12	21963094
707	Phosphorylation	EPLCPLPSPPTSDSD CCCCCCCCCCCCCCC	51.71	23401153
710	Phosphorylation	CPLPSPPTSDSDSDS CCCCCCCCCCCCCCC	48.85	30108239
710	Ubiquitination	CPLPSPPTSDSDSDS CCCCCCCCCCCCCCC	48.85	22817900
711	Phosphorylation	PLPSPPTSDSDSDSE CCCCCCCCCCCCCCC	40.67	30108239
713	Phosphorylation	PSPPTSDSDSDSEGP CCCCCCCCCCCCCCC	38.49	30108239
715	Phosphorylation	PPTSDSDSDSEGPEK CCCCCCCCCCCCCCC	47.16	30576142
717	Phosphorylation	TSDSDSDSEGPEKDT CCCCCCCCCCCCCCC	48.70	30108239
724	Phosphorylation	SEGPEKDTRSSFRGH CCCCCCCCCHHCCCC	43.44	30108239
726	Phosphorylation	GPEKDTRSSFRGHTP CCCCCCCHHCCCCCC	35.60	23401153
727	Phosphorylation	PEKDTRSSFRGHTPL CCCCCCHHCCCCCCC	18.70	30108239
732	Phosphorylation	RSSFRGHTPLDLTCS CHHCCCCCCCCCCCC	28.50	30108239
737	Phosphorylation	GHTPLDLTCSTKVKT CCCCCCCCCCHHHHH	12.22	25627689
739	Phosphorylation	TPLDLTCSTKVKTLL CCCCCCCCHHHHHHH	26.48	25159151
740	Phosphorylation	PLDLTCSTKVKTLLL CCCCCCCHHHHHHHH	41.84	25627689
741	Acetylation	LDLTCSTKVKTLLLN CCCCCCHHHHHHHHH	25.99	25953088
741	Ubiquitination	LDLTCSTKVKTLLLN CCCCCCHHHHHHHHH	25.99	21906983
741 (in isoform 1)	Ubiquitination	-	25.99	21906983
743	Ubiquitination	LTCSTKVKTLLLNAA CCCCHHHHHHHHHHH	34.70	-
744	Phosphorylation	TCSTKVKTLLLNAAQ CCCHHHHHHHHHHHH	26.14	20068231
753	Phosphorylation	LLNAAQNTMEPPLTP HHHHHHCCCCCCCCC	15.72	20068231
759	Phosphorylation	NTMEPPLTPPSPAGP CCCCCCCCCCCCCCC	38.64	20068231
762	Phosphorylation	EPPLTPPSPAGPGLS CCCCCCCCCCCCCCC	28.69	28464451
769	Phosphorylation	SPAGPGLSLGDTALQ CCCCCCCCCCHHHHH	35.90	20068231
773	Phosphorylation	PGLSLGDTALQNLEQ CCCCCCHHHHHHHHH	27.71	28464451
790	Phosphorylation	DGPEAQGSWAELAER HCHHHCCCHHHHHHH	15.84	20068231
802	Phosphorylation	AERLGLRSLVDTYRQ HHHHCCHHHHHHHHH	37.47	22199227
806	Phosphorylation	GLRSLVDTYRQTTSP CCHHHHHHHHHCCCC	17.08	22199227
810	O-linked_Glycosylation	LVDTYRQTTSPSGSL HHHHHHHCCCCCCHH	21.90	23301498
810	Phosphorylation	LVDTYRQTTSPSGSL HHHHHHHCCCCCCHH	21.90	22199227
811	Phosphorylation	VDTYRQTTSPSGSLL HHHHHHCCCCCCHHH	30.24	21815630
812	Phosphorylation	DTYRQTTSPSGSLLR HHHHHCCCCCCHHHH	22.06	25159151
813	Ubiquitination	TYRQTTSPSGSLLRS HHHHCCCCCCHHHHE	40.39	22817900
814	Phosphorylation	YRQTTSPSGSLLRSY HHHCCCCCCHHHHEE	40.56	30108239
816	Phosphorylation	QTTSPSGSLLRSYEL HCCCCCCHHHHEEEE	28.68	30108239
837	Ubiquitination	GLLEALSDMGLEEGV HHHHHHHHCCCHHHH	35.70	21963094
852	Phosphorylation	RLLRGPETRDKLPST HHHCCCCCCCCCCCC	47.50	22210691
855	Ubiquitination	RGPETRDKLPSTAEV CCCCCCCCCCCCCCC	60.03	27667366
855 (in isoform 4)	Ubiquitination	-	60.03	-
858	Phosphorylation	ETRDKLPSTAEVKED CCCCCCCCCCCCCCC	51.16	29255136
858 (in isoform 4)	Phosphorylation	-	51.16	23663014
859	O-linked_Glycosylation	TRDKLPSTAEVKEDS CCCCCCCCCCCCCCC	25.54	23301498
859	Phosphorylation	TRDKLPSTAEVKEDS CCCCCCCCCCCCCCC	25.54	29255136
859 (in isoform 4)	Phosphorylation	-	25.54	23663014
863	Sumoylation	LPSTAEVKEDSAYGS CCCCCCCCCCCCCCC	47.51	-
863	Sumoylation	LPSTAEVKEDSAYGS CCCCCCCCCCCCCCC	47.51	-
865 (in isoform 4)	Phosphorylation	-	32.61	23663014
866	Phosphorylation	TAEVKEDSAYGSQSV CCCCCCCCCCCCHHH	25.20	21082442
867 (in isoform 4)	Phosphorylation	-	25.65	23663014
868	Phosphorylation	EVKEDSAYGSQSVEQ CCCCCCCCCCHHHHH	22.66	30108239
869 (in isoform 4)	Phosphorylation	-	20.94	30108239
870	Phosphorylation	KEDSAYGSQSVEQEA CCCCCCCCHHHHHHH	13.45	25159151
871 (in isoform 4)	Phosphorylation	-	47.32	25849741
872	Phosphorylation	DSAYGSQSVEQEAEK CCCCCCHHHHHHHHH	29.35	25159151
922	Ubiquitination	----------------------------- -----------------------------		21963094
1036	Ubiquitination	----------------------------------------------------------------------------------------------------------------------------------------------- -----------------------------------------------------------------------------------------------------------------------------------------------		22817900

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
99	S	Phosphorylation	Kinase	CHUK	O15111	GPS
108	S	Phosphorylation	Kinase	CHUK	O15111	GPS
115	S	Phosphorylation	Kinase	CHUK	O15111	GPS
123	S	Phosphorylation	Kinase	CHUK	O15111	GPS
222	S	Phosphorylation	Kinase	GSK3B	P49841	PSP
707	S	Phosphorylation	Kinase	GSK3B	P49841	PSP
711	S	Phosphorylation	Kinase	GSK3B	P49841	PSP
866	S	Phosphorylation	Kinase	IKKA	O15111	PSP
866	S	Phosphorylation	Kinase	M3K14	Q99558	PhosphoELM
870	S	Phosphorylation	Kinase	IKKA	O15111	PSP
870	S	Phosphorylation	Kinase	M3K14	Q99558	PhosphoELM
872	S	Phosphorylation	Kinase	CHUK	O15111	GPS
872	S	Phosphorylation	Kinase	IKK-FAMILY	-	GPS
-	K	Ubiquitination	E3 ubiquitin ligase	FBXW7	Q969H0	PMID:24658274
-	K	Ubiquitination	E3 ubiquitin ligase	BTRC	Q9Y297	PMID:11994270

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of NFKB2_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 NFKB2_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
FBXW7_HUMAN	FBXW7	physical	14743216
REL_HUMAN	REL	physical	14743216
SC16A_HUMAN	SEC16A	physical	14743216
TF65_HUMAN	RELA	physical	14743216
UBP2_HUMAN	USP2	physical	14743216
DDX3X_HUMAN	DDX3X	physical	14743216
GSLG1_HUMAN	GLG1	physical	14743216
NFKB1_HUMAN	NFKB1	physical	14743216
NFKB2_HUMAN	NFKB2	physical	14743216
RELB_HUMAN	RELB	physical	14743216
RL30_HUMAN	RPL30	physical	14743216
RL6_HUMAN	RPL6	physical	14743216
RS13_HUMAN	RPS13	physical	14743216
BCL3_HUMAN	BCL3	physical	14678988
RELB_HUMAN	RELB	physical	14678988
NEMO_HUMAN	IKBKG	physical	14743216
M3K8_HUMAN	MAP3K8	physical	14743216
TNIP2_HUMAN	TNIP2	physical	14743216
MEN1_HUMAN	MEN1	physical	11526476
FBW1A_HUMAN	BTRC	physical	11994270
TF65_HUMAN	RELA	physical	8413211
REL_HUMAN	REL	physical	8413211
BCL3_HUMAN	BCL3	physical	8453667
FBW1A_HUMAN	BTRC	physical	18617892
IKKA_HUMAN	CHUK	physical	16303288
FBW1A_HUMAN	BTRC	physical	16303288
IKBZ_HUMAN	NFKBIZ	physical	20211142
IKKA_HUMAN	CHUK	physical	15140882
FBW1A_HUMAN	BTRC	physical	15140882
PSD11_HUMAN	PSMD11	physical	12185077
M3K14_HUMAN	MAP3K14	physical	17563756
IKKA_HUMAN	CHUK	physical	17563756
FBXW7_HUMAN	FBXW7	physical	22388891
NFKB2_HUMAN	NFKB2	physical	22388891
RELB_HUMAN	RELB	physical	22388891
FBXW7_HUMAN	FBXW7	physical	22864569
TF65_HUMAN	RELA	physical	16940413

Drug and Disease Associations

Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
	Note=A chromosomal aberration involving NFKB2 is found in a case of B-cell non Hodgkin lymphoma (B-NHL). Translocation t(10
	14)(q24
	q32) with IGHA1. The resulting oncogene is also called Lyt-10C alpha variant.
615577
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
DB00945	Acetylsalicylic acid
DB01296	Glucosamine

Regulatory Network of NFKB2_HUMAN

Related Literatures of Post-Translational Modification

Phosphorylation
Reference	PubMed
"NF-kappaB-inducing kinase regulates the processing of NF-kappaB2p100."; Xiao G., Harhaj E.W., Sun S.-C.; Mol. Cell 7:401-409(2001). Cited for: PHOSPHORYLATION AT SER-866 AND SER-870, MUTAGENESIS OF SER-866 ANDSER-870, AND PROTEOLYTIC PROCESSING OF P100.	11239468 [Abstract]
"Differential regulation of NF-kappaB2(p100) processing and control byamino-terminal sequences."; Betts J.C., Nabel G.J.; Mol. Cell. Biol. 16:6363-6371(1996). Cited for: PHOSPHORYLATION AT SER-713; SER-715 AND SER-717, MUTAGENESIS,DIMERIZATION, AND PROTEOLYTIC PROCESSING OF P100.	8887665 [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 THR-429, AND MASSSPECTROMETRY.	18669648 [Abstract]
Ubiquitylation
Reference	PubMed
"Mechanism of processing of the NF-kappa B2 p100 precursor:identification of the specific polyubiquitin chain-anchoring lysineresidue and analysis of the role of NEDD8-modification on theSCF(beta-TrCP) ubiquitin ligase."; Amir R.E., Haecker H., Karin M., Ciechanover A.; Oncogene 23:2540-2547(2004). Cited for: UBIQUITINATION AT LYS-855.	14676825 [Abstract]