dbPTM

NFKB1_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	NFKB1_HUMAN
UniProt AC	P19838
Protein Name	Nuclear factor NF-kappa-B p105 subunit
Gene Name	NFKB1
Organism	Homo sapiens (Human).
Sequence Length	968
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 and the heterodimeric p65-p50 complex appears to be most abundant one. 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. NF-kappa-B heterodimeric p65-p50 and RelB-p50 complexes are transcriptional activators. The NF-kappa-B p50-p50 homodimer is a transcriptional repressor, but can act as a transcriptional activator when associated with BCL3. NFKB1 appears to have dual functions such as cytoplasmic retention of attached NF-kappa-B proteins by p105 and generation of p50 by a cotranslational processing. The proteasome-mediated process ensures the production of both p50 and p105 and preserves their independent function, although processing of NFKB1/p105 also appears to occur post-translationally. p50 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. In a complex with MAP3K8, NFKB1/p105 represses MAP3K8-induced MAPK signaling; active MAP3K8 is released by proteasome-dependent degradation of NFKB1/p105..
Protein Sequence	MAEDDPYLGRPEQMFHLDPSLTHTIFNPEVFQPQMALPTDGPYLQILEQPKQRGFRFRYVCEGPSHGGLPGASSEKNKKSYPQVKICNYVGPAKVIVQLVTNGKNIHLHAHSLVGKHCEDGICTVTAGPKDMVVGFANLGILHVTKKKVFETLEARMTEACIRGYNPGLLVHPDLAYLQAEGGGDRQLGDREKELIRQAALQQTKEMDLSVVRLMFTAFLPDSTGSFTRRLEPVVSDAIYDSKAPNASNLKIVRMDRTAGCVTGGEEIYLLCDKVQKDDIQIRFYEEEENGGVWEGFGDFSPTDVHRQFAIVFKTPKYKDINITKPASVFVQLRRKSDLETSEPKPFLYYPEIKDKEEVQRKRQKLMPNFSDSFGGGSGAGAGGGGMFGSGGGGGGTGSTGPGYSFPHYGFPTYGGITFHPGTTKSNAGMKHGTMDTESKKDPEGCDKSDDKNTVNLFGKVIETTEQDQEPSEATVGNGEVTLTYATGTKEESAGVQDNLFLEKAMQLAKRHANALFDYAVTGDVKMLLAVQRHLTAVQDENGDSVLHLAIIHLHSQLVRDLLEVTSGLISDDIINMRNDLYQTPLHLAVITKQEDVVEDLLRAGADLSLLDRLGNSVLHLAAKEGHDKVLSILLKHKKAALLLDHPNGDGLNAIHLAMMSNSLPCLLLLVAAGADVNAQEQKSGRTALHLAVEHDNISLAGCLLLEGDAHVDSTTYDGTTPLHIAAGRGSTRLAALLKAAGADPLVENFEPLYDLDDSWENAGEDEGVVPGTTPLDMATSWQVFDILNGKPYEPEFTSDDLLAQGDMKQLAEDVKLQLYKLLEIPDPDKNWATLAQKLGLGILNNAFRLSPAPSKTLMDNYEVSGGTVRELVEALRQMGYTEAIEVIQAASSPVKTTSQAHSLPLSPASTRQQIDELRDSDSVCDSGVETSFRKLSFTESLTSGASLLTLNKMPHDYGQEGPLEGKI

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
20	Phosphorylation	QMFHLDPSLTHTIFN HHCCCCCCCCCEECC	45.63	20966071
59	Phosphorylation	QRGFRFRYVCEGPSH HCCCCEEEEECCCCC	13.52	18083107
61	S-nitrosocysteine	GFRFRYVCEGPSHGG CCCEEEEECCCCCCC	3.57	-
61	Glutathionylation	GFRFRYVCEGPSHGG CCCEEEEECCCCCCC	3.57	22833525
61	Other	GFRFRYVCEGPSHGG CCCEEEEECCCCCCC	3.57	11466314
61	S-nitrosylation	GFRFRYVCEGPSHGG CCCEEEEECCCCCCC	3.57	8710491
73	Phosphorylation	HGGLPGASSEKNKKS CCCCCCCCCCCCCCC	44.97	28348404
74	Phosphorylation	GGLPGASSEKNKKSY CCCCCCCCCCCCCCC	52.64	28857561
80	Phosphorylation	SSEKNKKSYPQVKIC CCCCCCCCCCCEEEC	43.59	24905233
81	Phosphorylation	SEKNKKSYPQVKICN CCCCCCCCCCEEECC	13.43	24905233
116	Acetylation	HAHSLVGKHCEDGIC EEHHHHCCCCCCCEE	37.29	26051181
147	Ubiquitination	GILHVTKKKVFETLE EEEEECHHHHHHHHH	44.82	29967540
148	Ubiquitination	ILHVTKKKVFETLEA EEEECHHHHHHHHHH	54.43	29967540
149	Ubiquitination	LHVTKKKVFETLEAR EEECHHHHHHHHHHH	7.81	29967540
165	Phosphorylation	TEACIRGYNPGLLVH HHHHHHCCCCCCEEC	14.34	-
205	Ubiquitination	QAALQQTKEMDLSVV HHHHHHHHHCCHHHH	46.86	24816145
206	Ubiquitination	AALQQTKEMDLSVVR HHHHHHHHCCHHHHH	41.12	24816145
213	Ubiquitination	EMDLSVVRLMFTAFL HCCHHHHHHHHHHHC	20.48	24816145
223	Phosphorylation	FTAFLPDSTGSFTRR HHHHCCCCCCCCCCC	32.50	-
228	Phosphorylation	PDSTGSFTRRLEPVV CCCCCCCCCCCCCCC	19.31	-
240	Phosphorylation	PVVSDAIYDSKAPNA CCCCCHHCCCCCCCC	18.84	20090780
241	Phosphorylation	VVSDAIYDSKAPNAS CCCCHHCCCCCCCCC	37.23	25147952
242	Phosphorylation	VSDAIYDSKAPNASN CCCHHCCCCCCCCCC	17.47	-
243	Ubiquitination	SDAIYDSKAPNASNL CCHHCCCCCCCCCCC	66.03	29967540
244	Ubiquitination	DAIYDSKAPNASNLK CHHCCCCCCCCCCCE	13.41	29967540
251	Acetylation	APNASNLKIVRMDRT CCCCCCCEEEEECCC	43.32	25953088
251	Malonylation	APNASNLKIVRMDRT CCCCCCCEEEEECCC	43.32	26320211
251	Ubiquitination	APNASNLKIVRMDRT CCCCCCCEEEEECCC	43.32	29967540
252	Ubiquitination	PNASNLKIVRMDRTA CCCCCCEEEEECCCC	2.40	29967540
252 (in isoform 2)	Ubiquitination	-	2.40	-
277	Malonylation	LLCDKVQKDDIQIRF EEECCCCCCCCEEEE	61.43	26320211
301	Phosphorylation	WEGFGDFSPTDVHRQ CCCCCCCCCCHHHHC	31.46	28348404
302	Phosphorylation	EGFGDFSPTDVHRQF CCCCCCCCCHHHHCE	32.39	27251275
304	Ubiquitination	FGDFSPTDVHRQFAI CCCCCCCHHHHCEEE	37.29	24816145
324	Phosphorylation	KYKDINITKPASVFV CCCCCCCCCCHHHEE	26.87	-
325	Sumoylation	YKDINITKPASVFVQ CCCCCCCCCHHHEEE	34.49	-
325	Sumoylation	YKDINITKPASVFVQ CCCCCCCCCHHHEEE	34.49	28112733
328	Phosphorylation	INITKPASVFVQLRR CCCCCCHHHEEEEEE	25.31	22152481
337	Phosphorylation	FVQLRRKSDLETSEP EEEEEEHHCCCCCCC	45.69	12947093
345	Ubiquitination	DLETSEPKPFLYYPE CCCCCCCCCCCCCCC	44.33	29967540
346	Ubiquitination	LETSEPKPFLYYPEI CCCCCCCCCCCCCCC	34.88	29967540
356	Ubiquitination	YYPEIKDKEEVQRKR CCCCCCCHHHHHHHH	51.26	24816145
357	Ubiquitination	YPEIKDKEEVQRKRQ CCCCCCHHHHHHHHH	73.80	24816145
364	Ubiquitination	EEVQRKRQKLMPNFS HHHHHHHHHHCCCCC	46.39	24816145
371	Phosphorylation	QKLMPNFSDSFGGGS HHHCCCCCCCCCCCC	38.70	28348404
373	Phosphorylation	LMPNFSDSFGGGSGA HCCCCCCCCCCCCCC	25.29	28348404
378	Phosphorylation	SDSFGGGSGAGAGGG CCCCCCCCCCCCCCC	28.83	28348404
379	Phosphorylation	DSFGGGSGAGAGGGG CCCCCCCCCCCCCCC	31.16	27251275
390	Phosphorylation	GGGGMFGSGGGGGGT CCCCCCCCCCCCCCC	24.01	28348404
397	Phosphorylation	SGGGGGGTGSTGPGY CCCCCCCCCCCCCCC	31.10	28348404
399	O-linked_Glycosylation	GGGGGTGSTGPGYSF CCCCCCCCCCCCCCC	29.99	23301498
399	Phosphorylation	GGGGGTGSTGPGYSF CCCCCCCCCCCCCCC	29.99	28348404
400	Phosphorylation	GGGGTGSTGPGYSFP CCCCCCCCCCCCCCC	49.06	28348404
409	Phosphorylation	PGYSFPHYGFPTYGG CCCCCCCCCCCCCCC	22.24	-
413	Phosphorylation	FPHYGFPTYGGITFH CCCCCCCCCCCEEEC	32.32	-
423	O-linked_Glycosylation	GITFHPGTTKSNAGM CEEECCCCCCCCCCC	35.19	23301498
431	Acetylation	TKSNAGMKHGTMDTE CCCCCCCCCCCCCCC	37.66	11739381
435	Sulfoxidation	AGMKHGTMDTESKKD CCCCCCCCCCCCCCC	7.70	30846556
440	Acetylation	GTMDTESKKDPEGCD CCCCCCCCCCCCCCC	55.77	11739381
440	Ubiquitination	GTMDTESKKDPEGCD CCCCCCCCCCCCCCC	55.77	10207090
441	Acetylation	TMDTESKKDPEGCDK CCCCCCCCCCCCCCC	83.93	11739381
441	Ubiquitination	TMDTESKKDPEGCDK CCCCCCCCCCCCCCC	83.93	10207090
449	Phosphorylation	DPEGCDKSDDKNTVN CCCCCCCCCCCCCEE	37.48	-
452	Ubiquitination	GCDKSDDKNTVNLFG CCCCCCCCCCEECCC	60.55	22817900
485	Phosphorylation	NGEVTLTYATGTKEE CCEEEEEEEECCCCC	12.79	-
504	Ubiquitination	QDNLFLEKAMQLAKR CCCHHHHHHHHHHHH	51.83	21906983
504 (in isoform 1)	Ubiquitination	-	51.83	21906983
505	Ubiquitination	DNLFLEKAMQLAKRH CCHHHHHHHHHHHHH	4.99	22817900
505 (in isoform 2)	Ubiquitination	-	4.99	21906983
512	Ubiquitination	AMQLAKRHANALFDY HHHHHHHHHHHHHHH	23.72	22817900
519	Phosphorylation	HANALFDYAVTGDVK HHHHHHHHHHHHCHH	8.81	28796482
520	Phosphorylation	ANALFDYAVTGDVKM HHHHHHHHHHHCHHH	8.34	27642862
582	Phosphorylation	INMRNDLYQTPLHLA HHCCCCCCCCCCEEE	17.13	-
584	Phosphorylation	MRNDLYQTPLHLAVI CCCCCCCCCCEEEEE	17.79	-
624	Ubiquitination	SVLHLAAKEGHDKVL HHHHHHHHCCCHHHH	59.63	29967540
625	Ubiquitination	VLHLAAKEGHDKVLS HHHHHHHCCCHHHHH	57.97	29967540
625 (in isoform 2)	Ubiquitination	-	57.97	-
678	Hydroxylation	VAAGADVNAQEQKSG HHHCCCCCHHHHHHC	36.13	17003112
759	Phosphorylation	PLYDLDDSWENAGED CCCCCCCHHHHCCCC	35.64	-
764	Ubiquitination	DDSWENAGEDEGVVP CCHHHHCCCCCCCCC	55.24	22817900
769	Ubiquitination	NAGEDEGVVPGTTPL HCCCCCCCCCCCCCC	4.40	22817900
804	Ubiquitination	FTSDDLLAQGDMKQL CCHHHHHHCCCHHHH	20.71	21963094
816	Ubiquitination	KQLAEDVKLQLYKLL HHHHHHHHHHHHHHH	42.72	22817900
817	Ubiquitination	QLAEDVKLQLYKLLE HHHHHHHHHHHHHHC	4.21	22817900
817 (in isoform 2)	Ubiquitination	-	4.21	-
821	Ubiquitination	DVKLQLYKLLEIPDP HHHHHHHHHHCCCCC	56.01	21906983
821 (in isoform 1)	Ubiquitination	-	56.01	21906983
822	Ubiquitination	VKLQLYKLLEIPDPD HHHHHHHHHCCCCCC	3.07	22817900
822 (in isoform 2)	Ubiquitination	-	3.07	21906983
824	Ubiquitination	LQLYKLLEIPDPDKN HHHHHHHCCCCCCCC	64.01	22817900
829	Ubiquitination	LLEIPDPDKNWATLA HHCCCCCCCCHHHHH	65.39	22817900
830	Ubiquitination	LEIPDPDKNWATLAQ HCCCCCCCCHHHHHH	60.83	29967540
831	Ubiquitination	EIPDPDKNWATLAQK CCCCCCCCHHHHHHH	40.78	29967540
831 (in isoform 2)	Ubiquitination	-	40.78	-
851	Phosphorylation	LNNAFRLSPAPSKTL HCCCHHCCCCCCCCC	18.11	25159151
852	Phosphorylation	NNAFRLSPAPSKTLM CCCHHCCCCCCCCCC	53.43	24719451
855	Phosphorylation	FRLSPAPSKTLMDNY HHCCCCCCCCCCCCE	40.14	23403867
856	Ubiquitination	RLSPAPSKTLMDNYE HCCCCCCCCCCCCEE	44.62	27667366
856 (in isoform 1)	Ubiquitination	-	44.62	21906983
857	Phosphorylation	LSPAPSKTLMDNYEV CCCCCCCCCCCCEEE	31.49	28796482
857	Ubiquitination	LSPAPSKTLMDNYEV CCCCCCCCCCCCEEE	31.49	27667366
857 (in isoform 2)	Ubiquitination	-	31.49	21906983
862	Phosphorylation	SKTLMDNYEVSGGTV CCCCCCCEEECCHHH	17.28	28796482
863	Phosphorylation	KTLMDNYEVSGGTVR CCCCCCEEECCHHHH	36.14	27642862
864	Ubiquitination	TLMDNYEVSGGTVRE CCCCCEEECCHHHHH	4.55	21963094
865	Phosphorylation	LMDNYEVSGGTVREL CCCCEEECCHHHHHH	21.40	28796482
868	Phosphorylation	NYEVSGGTVRELVEA CEEECCHHHHHHHHH	21.66	28796482
882	Phosphorylation	ALRQMGYTEAIEVIQ HHHHCCCHHHHHHHH	17.14	22617229
892	Phosphorylation	IEVIQAASSPVKTTS HHHHHHCCCCCCCCC	37.88	29255136
893	Phosphorylation	EVIQAASSPVKTTSQ HHHHHCCCCCCCCCC	29.05	29255136
897	Phosphorylation	AASSPVKTTSQAHSL HCCCCCCCCCCCCCC	31.73	23927012
898	Phosphorylation	ASSPVKTTSQAHSLP CCCCCCCCCCCCCCC	17.08	23927012
899	Phosphorylation	SSPVKTTSQAHSLPL CCCCCCCCCCCCCCC	30.51	23927012
903	Phosphorylation	KTTSQAHSLPLSPAS CCCCCCCCCCCCCCC	34.40	25159151
904	Phosphorylation	TTSQAHSLPLSPAST CCCCCCCCCCCCCCH	3.38	24719451
907	Phosphorylation	QAHSLPLSPASTRQQ CCCCCCCCCCCHHHH	19.24	22322096
908	Phosphorylation	AHSLPLSPASTRQQI CCCCCCCCCCHHHHH	37.60	24719451
910	Phosphorylation	SLPLSPASTRQQIDE CCCCCCCCHHHHHHH	27.75	23927012
911	Phosphorylation	LPLSPASTRQQIDEL CCCCCCCHHHHHHHH	34.30	23927012
921	Phosphorylation	QIDELRDSDSVCDSG HHHHHHHCCCCCCCC	25.92	28985074
923	Phosphorylation	DELRDSDSVCDSGVE HHHHHCCCCCCCCCH	28.70	10469655
924	Phosphorylation	ELRDSDSVCDSGVET HHHHCCCCCCCCCHH	5.16	24719451
927	Phosphorylation	DSDSVCDSGVETSFR HCCCCCCCCCHHCCC	39.34	25849741
931	Phosphorylation	VCDSGVETSFRKLSF CCCCCCHHCCCHHCC	30.66	29978859
932	Phosphorylation	CDSGVETSFRKLSFT CCCCCHHCCCHHCCC	15.00	29978859
933	Phosphorylation	DSGVETSFRKLSFTE CCCCHHCCCHHCCCC	11.88	27251275
937	Phosphorylation	ETSFRKLSFTESLTS HHCCCHHCCCCCCCC	32.91	29255136
938	Phosphorylation	TSFRKLSFTESLTSG HCCCHHCCCCCCCCC	14.75	24719451
939	Phosphorylation	SFRKLSFTESLTSGA CCCHHCCCCCCCCCC	22.68	25159151
940	Phosphorylation	FRKLSFTESLTSGAS CCHHCCCCCCCCCCE	41.56	27251275
941	Phosphorylation	RKLSFTESLTSGASL CHHCCCCCCCCCCEE	33.61	22617229
942	Phosphorylation	KLSFTESLTSGASLL HHCCCCCCCCCCEEE	3.44	27251275
943	Phosphorylation	LSFTESLTSGASLLT HCCCCCCCCCCEEEE	34.10	28102081
944	Phosphorylation	SFTESLTSGASLLTL CCCCCCCCCCEEEEC	37.34	23403867
945	Phosphorylation	FTESLTSGASLLTLN CCCCCCCCCEEEECC	17.60	27251275
947	Phosphorylation	ESLTSGASLLTLNKM CCCCCCCEEEECCCC	27.69	23403867
950	Phosphorylation	TSGASLLTLNKMPHD CCCCEEEECCCCCCC	33.31	23403867

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
20	S	Phosphorylation	Kinase	PRKDC	P78527	GPS
328	S	Phosphorylation	Kinase	CHEK1	O14757	GPS
337	S	Phosphorylation	Kinase	PKA_GROUP	-	PhosphoELM
337	S	Phosphorylation	Kinase	PKA	-	Uniprot
337	S	Phosphorylation	Kinase	PKA-FAMILY	-	GPS
337	S	Phosphorylation	Kinase	PRKACA	P17612	GPS
903	S	Phosphorylation	Kinase	GSK3B	P49841	PhosphoELM
903	S	Phosphorylation	Kinase	GSK3B	Q9WV60	PSP
907	S	Phosphorylation	Kinase	GSK3B	P49841	PhosphoELM
907	S	Phosphorylation	Kinase	GSK3B	Q9WV60	PSP
921	S	Phosphorylation	Kinase	IKK-FAMILY	-	GPS
923	S	Phosphorylation	Kinase	IKBKB	O14920	GPS
923	S	Phosphorylation	Kinase	IKK-FAMILY	-	GPS
923	S	Phosphorylation	Kinase	CHUK	O15111	GPS
923	S	Phosphorylation	Kinase	IKK_GROUP	-	PhosphoELM
927	S	Phosphorylation	Kinase	IKBKB	O14920	GPS
927	S	Phosphorylation	Kinase	CHUK	O15111	GPS
927	S	Phosphorylation	Kinase	IKK-FAMILY	-	GPS
927	S	Phosphorylation	Kinase	IKK_GROUP	-	PhosphoELM
932	S	Phosphorylation	Kinase	IKBKB	O14920	GPS
932	S	Phosphorylation	Kinase	IKK-FAMILY	-	GPS
932	S	Phosphorylation	Kinase	CHUK	O15111	GPS
-	K	Ubiquitination	E3 ubiquitin ligase	RNF123	Q5XPI4	PMID:25860612
-	K	Ubiquitination	E3 ubiquitin ligase	BTRC	Q9Y297	PMID:10835356
-	K	Ubiquitination	E3 ubiquitin ligase	FBXW11	Q9UKB1	PMID:25503564

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Reference
61	C	S-nitrosylation	8710491
S-nitrosylation of Cys-61 affects DNA binding.
903	S	Phosphorylation	12871932
Phosphorylation at 'Ser-903' and 'Ser-907' primes p105 for proteolytic processing in response to TNF-alpha stimulation.
907	S	Phosphorylation	12871932
Phosphorylation at 'Ser-903' and 'Ser-907' primes p105 for proteolytic processing in response to TNF-alpha stimulation.
927	S	Phosphorylation	11297557
Phosphorylation at 'Ser-927' and 'Ser-932' are required for BTRC/BTRCP-mediated proteolysis.
932	S	Phosphorylation	10469655
Phosphorylation at 'Ser-927' and 'Ser-932' are required for BTRC/BTRCP-mediated proteolysis.

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 NFKB1_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
LYL1_HUMAN	LYL1	physical	10023675
COPB2_HUMAN	COPB2	physical	14743216
REL_HUMAN	REL	physical	14743216
JIP4_HUMAN	SPAG9	physical	14743216
NFKB2_HUMAN	NFKB2	physical	14743216
TF65_HUMAN	RELA	physical	14743216
IMA4_HUMAN	KPNA3	physical	14743216
NFKB1_HUMAN	NFKB1	physical	14743216
RELB_HUMAN	RELB	physical	14743216
NFKB1_HUMAN	NFKB1	physical	8428580
TP53B_HUMAN	TP53BP1	physical	10646849
NEMO_HUMAN	IKBKG	physical	14743216
TBK1_HUMAN	TBK1	physical	14743216
TNIP2_HUMAN	TNIP2	physical	14743216
TNIP3_HUMAN	TNIP3	physical	14743216
RSF1_HUMAN	RSF1	physical	15242768
KLF5_HUMAN	KLF5	physical	14573617
HMGB1_HUMAN	HMGB1	physical	12604365
TAB2_HUMAN	TAB2	physical	12150997
HDAC1_HUMAN	HDAC1	physical	11931769
TF65_HUMAN	RELA	physical	8798655
FBW1A_HUMAN	BTRC	physical	11158290
MEN1_HUMAN	MEN1	physical	11526476
NOTC1_HUMAN	NOTCH1	physical	8642313
CENPR_HUMAN	ITGB3BP	physical	12244126
IKKA_HUMAN	CHUK	physical	10469655
IKKB_HUMAN	IKBKB	physical	10469655
NCOA1_HUMAN	NCOA1	physical	9556555
RXRA_HUMAN	RXRA	physical	10075655
IKBA_HUMAN	NFKBIA	physical	9738011
PP4C_HUMAN	PPP4C	physical	9837938
IRF8_HUMAN	IRF8	physical	8550813
IRF2_HUMAN	IRF2	physical	8550813
IRF9_HUMAN	IRF9	physical	8550813
TTP_HUMAN	ZFP36	physical	19738286
PHS_HUMAN	PCBD1	physical	20211142
ZBTB9_HUMAN	ZBTB9	physical	20211142
BRMS1_HUMAN	BRMS1	physical	17000776
TF65_HUMAN	RELA	physical	16740634
SP1_HUMAN	SP1	physical	16740634
MEN1_HUMAN	MEN1	physical	16651450
EP300_HUMAN	EP300	physical	14662860
TF65_HUMAN	RELA	physical	16319923
HDAC1_HUMAN	HDAC1	physical	16319923
RPB1_HUMAN	POLR2A	physical	16319923
PARP1_HUMAN	PARP1	physical	16204234
TF65_HUMAN	RELA	physical	16204234
TF65_HUMAN	RELA	physical	16105840
FBW1A_HUMAN	BTRC	physical	12482991
ANXA4_HUMAN	ANXA4	physical	20237821
TF65_HUMAN	RELA	physical	20237821
IKBA_HUMAN	NFKBIA	physical	20237821
HDAC3_HUMAN	HDAC3	physical	15494311
NCOR2_HUMAN	NCOR2	physical	15494311
RS3_HUMAN	RPS3	physical	18045535
PSD10_HUMAN	PSMD10	physical	17904523
HDAC1_HUMAN	HDAC1	physical	17827154
HDAC2_HUMAN	HDAC2	physical	17827154
IKBA_HUMAN	NFKBIA	physical	8631829
EP300_HUMAN	EP300	physical	20065107
SP1_HUMAN	SP1	physical	18083845
CLUS_HUMAN	CLU	physical	20068069
TF65_HUMAN	RELA	physical	2050119
SF01_HUMAN	SF1	physical	12917325
HDAC5_HUMAN	HDAC5	physical	12917325
KAT5_HUMAN	KAT5	physical	15829968
CTNB1_HUMAN	CTNNB1	physical	15829968
RUVB2_HUMAN	RUVBL2	physical	15829968
BCL3_HUMAN	BCL3	physical	15829968
EP300_HUMAN	EP300	physical	22013068
PSA4_HUMAN	PSMA4	physical	8692272
TNIP1_HUMAN	TNIP1	physical	19695220
TNIP2_HUMAN	TNIP2	physical	15169888
M3K8_HUMAN	MAP3K8	physical	15169888
STA5A_HUMAN	STAT5A	physical	21763497
SOCS3_HUMAN	SOCS3	physical	21451109
IKKA_HUMAN	CHUK	physical	11976329
IKKB_HUMAN	IKBKB	physical	11976329
TF65_HUMAN	RELA	physical	11976329
PARP1_HUMAN	PARP1	physical	16799643
TF65_HUMAN	RELA	physical	20547752
M3K8_HUMAN	MAP3K8	physical	16291755
NFKB1_HUMAN	NFKB1	physical	11880271
TF65_HUMAN	RELA	physical	11880271
NFKB1_HUMAN	NFKB1	physical	14645533
TF65_HUMAN	RELA	physical	14645533
TNIP2_HUMAN	TNIP2	physical	21988832
SPP2A_HUMAN	SPPL2A	physical	21988832
AACT_HUMAN	SERPINA3	physical	21988832
NR4A1_HUMAN	NR4A1	physical	21988832
NFKB1_HUMAN	NFKB1	physical	21988832
NFKB2_HUMAN	NFKB2	physical	21988832
IKBA_HUMAN	NFKBIA	physical	21988832
PML_HUMAN	PML	physical	21988832
TF65_HUMAN	RELA	physical	21988832
RELB_HUMAN	RELB	physical	21988832
TYY1_HUMAN	YY1	physical	21988832
TNIP1_HUMAN	TNIP1	physical	21988832
RGS14_HUMAN	RGS14	physical	21988832
1433T_HUMAN	YWHAQ	physical	21988832
IKBZ_HUMAN	NFKBIZ	physical	21988832
NFKB1_HUMAN	NFKB1	physical	1508666
IKBA_HUMAN	NFKBIA	physical	7739549
IKBA_HUMAN	NFKBIA	physical	7891711
IKBA_HUMAN	NFKBIA	physical	9572494
NFKB1_HUMAN	NFKB1	physical	15043934
NEMO_HUMAN	IKBKG	physical	15043934
MAD3_HUMAN	MXD3	physical	8255759
TF65_HUMAN	RELA	physical	8255759
NFKB1_HUMAN	NFKB1	physical	8887676
IKBA_HUMAN	NFKBIA	physical	8887676
HIF1N_HUMAN	HIF1AN	physical	17003112
PELP1_HUMAN	PELP1	physical	20195357
PLD3_HUMAN	PLD3	physical	20195357
MPP6_HUMAN	MPP6	physical	20195357
IKBA_HUMAN	NFKBIA	physical	16210649
NFKB1_HUMAN	NFKB1	physical	9722548
TF65_HUMAN	RELA	physical	9722548
TF65_HUMAN	RELA	physical	24175631
NFKB1_HUMAN	NFKB1	physical	12414801
TF65_HUMAN	RELA	physical	12414801
TF65_HUMAN	RELA	physical	21544861
TF65_HUMAN	RELA	physical	17982102
ECSIT_HUMAN	ECSIT	physical	25355951
TF65_HUMAN	RELA	physical	25355951
PPARG_HUMAN	PPARG	physical	18556801
TRIP4_HUMAN	TRIP4	physical	12077347
ELF3_HUMAN	ELF3	physical	23687337
TF65_HUMAN	RELA	physical	23687337
HDAC1_HUMAN	HDAC1	physical	25241761
CD82_HUMAN	CD82	physical	25241761
CTNB1_HUMAN	CTNNB1	physical	25241761
STAT3_HUMAN	STAT3	physical	25241761
HS71L_HUMAN	HSPA1L	physical	25241761
KLF5_HUMAN	KLF5	physical	16102021
NFKB2_HUMAN	NFKB2	physical	25609649
TNIP2_HUMAN	TNIP2	physical	25609649
REL_HUMAN	REL	physical	25609649
TF65_HUMAN	RELA	physical	25609649
TNIP1_HUMAN	TNIP1	physical	25609649
IKBA_HUMAN	NFKBIA	physical	25609649
TERA_HUMAN	VCP	physical	26112410
FBW1A_HUMAN	BTRC	physical	26112410
RN123_HUMAN	RNF123	physical	25860612
CDX2_HUMAN	CDX2	physical	17876541
EP300_HUMAN	EP300	physical	12471036
CNOT2_HUMAN	CNOT2	physical	27173435
CNOT6_HUMAN	CNOT6	physical	27173435
CNO6L_HUMAN	CNOT6L	physical	27173435
CNO11_HUMAN	CNOT11	physical	27173435
TB182_HUMAN	TNKS1BP1	physical	27173435
CNOT7_HUMAN	CNOT7	physical	27173435
RN123_HUMAN	RNF123	physical	28923245
TNAP3_HUMAN	TNFAIP3	physical	28923245

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 NFKB1_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-893; SER-903; SER-907AND SER-937, AND MASS SPECTROMETRY.	19690332 [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-907, AND MASSSPECTROMETRY.	18220336 [Abstract]
"betaTrCP-mediated proteolysis of NF-kappaB1 p105 requiresphosphorylation of p105 serines 927 and 932."; Lang V., Janzen J., Fischer G.Z., Soneji Y., Beinke S., Salmeron A.,Allen H., Hay R.T., Ben-Neriah Y., Ley S.C.; Mol. Cell. Biol. 23:402-413(2003). Cited for: PHOSPHORYLATION AT SER-927 AND SER-932.	12482991 [Abstract]
"Glycogen synthase kinase-3 beta regulates NF-kappa B1/p105stability."; Demarchi F., Bertoli C., Sandy P., Schneider C.; J. Biol. Chem. 278:39583-39590(2003). Cited for: INTERACTION WITH GSK3B, PHOSPHORYLATION AT SER-903 AND SER-907, ANDMUTAGENESIS OF SER-903 AND SER-907.	12871932 [Abstract]
"Direct phosphorylation of NF-kappa B1 p105 by the Ikappa B kinasecomplex on serine 927 is essential for signal-induced p105proteolysis."; Salmeron A., Janzen J., Soneji Y., Bump N., Kamens J., Allen H.,Ley S.C.; J. Biol. Chem. 276:22215-22222(2001). Cited for: PHOSPHORYLATION AT SER-927.	11297557 [Abstract]
S-nitrosylation
Reference	PubMed
"Inhibition of NF-kappaB DNA binding by nitric oxide."; Matthews J.R., Botting C.H., Panico M., Morris H.R., Hay R.T.; Nucleic Acids Res. 24:2236-2242(1996). Cited for: S-NITROSYLATION AT CYS-61, MUTAGENESIS OF CYS-61, AND MASSSPECTROMETRY.	8710491 [Abstract]

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