dbPTM

NEMO_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	NEMO_HUMAN
UniProt AC	Q9Y6K9
Protein Name	NF-kappa-B essential modulator
Gene Name	IKBKG
Organism	Homo sapiens (Human).
Sequence Length	419
Subcellular Localization	Cytoplasm . Nucleus . Sumoylated NEMO accumulates in the nucleus in response to genotoxic stress.
Protein Description	Regulatory subunit of the IKK core complex which phosphorylates inhibitors of NF-kappa-B thus leading to the dissociation of the inhibitor/NF-kappa-B complex and ultimately the degradation of the inhibitor. Its binding to scaffolding polyubiquitin seems to play a role in IKK activation by multiple signaling receptor pathways. However, the specific type of polyubiquitin recognized upon cell stimulation (either 'Lys-63'-linked or linear polyubiquitin) and its functional importance is reported conflictingly. Also considered to be a mediator for TAX activation of NF-kappa-B. Could be implicated in NF-kappa-B-mediated protection from cytokine toxicity. Essential for viral activation of IRF3. Involved in TLR3- and IFIH1-mediated antiviral innate response; this function requires 'Lys-27'-linked polyubiquitination..
Protein Sequence	MNRHLWKSQLCEMVQPSGGPAADQDVLGEESPLGKPAMLHLPSEQGAPETLQRCLEENQELRDAIRQSNQILRERCEELLHFQASQREEKEFLMCKFQEARKLVERLGLEKLDLKRQKEQALREVEHLKRCQQQMAEDKASVKAQVTSLLGELQESQSRLEAATKECQALEGRARAASEQARQLESEREALQQQHSVQVDQLRMQGQSVEAALRMERQAASEEKRKLAQLQVAYHQLFQEYDNHIKSSVVGSERKRGMQLEDLKQQLQQAEEALVAKQEVIDKLKEEAEQHKIVMETVPVLKAQADIYKADFQAERQAREKLAEKKELLQEQLEQLQREYSKLKASCQESARIEDMRKRHVEVSQAPLPPAPAYLSSPLALPSQRRSPPEEPPDFCCPKCQYQAPDMDTLQIHVMECIE

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
8	Phosphorylation	MNRHLWKSQLCEMVQ CCCCHHHHHHHHHHC	19.46	-
17	Phosphorylation	LCEMVQPSGGPAADQ HHHHHCCCCCCCCCC	39.01	-
31	Phosphorylation	QDVLGEESPLGKPAM CCCCCCCCCCCCCCH	22.56	12657630
43	Phosphorylation	PAMLHLPSEQGAPET CCHHCCCCCCCCHHH	49.24	12657630
50	Phosphorylation	SEQGAPETLQRCLEE CCCCCHHHHHHHHHH	27.42	23312004
68	Phosphorylation	LRDAIRQSNQILRER HHHHHHHHHHHHHHH	22.36	17977820
85	Phosphorylation	ELLHFQASQREEKEF HHHCHHHCHHHHHHH	20.98	17977820
96	Acetylation	EKEFLMCKFQEARKL HHHHHHHHHHHHHHH	35.80	25953088
111	Ubiquitination	VERLGLEKLDLKRQK HHHHCHHHHHHHHHH	52.95	21906983
111	Phosphorylation	VERLGLEKLDLKRQK HHHHCHHHHHHHHHH	52.95	27251275
115	Ubiquitination	GLEKLDLKRQKEQAL CHHHHHHHHHHHHHH	53.07	PubMed
118	Ubiquitination	KLDLKRQKEQALREV HHHHHHHHHHHHHHH	56.69	-
139	Ubiquitination	QQQMAEDKASVKAQV HHHHHHCHHHHHHHH	33.78	21906983
143	Ubiquitination	AEDKASVKAQVTSLL HHCHHHHHHHHHHHH	30.52	21906983
147	Phosphorylation	ASVKAQVTSLLGELQ HHHHHHHHHHHHHHH	11.11	27050516
148	Phosphorylation	SVKAQVTSLLGELQE HHHHHHHHHHHHHHH	23.81	27050516
165	Ubiquitination	SRLEAATKECQALEG HHHHHHHHHHHHHHH	52.33	-
178	Phosphorylation	EGRARAASEQARQLE HHHHHHHHHHHHHHH	29.29	23663014
179 (in isoform 2)	Ubiquitination	-	43.46	-
186	Phosphorylation	EQARQLESEREALQQ HHHHHHHHHHHHHHH	51.01	23663014
196	Phosphorylation	EALQQQHSVQVDQLR HHHHHHHCHHHHHHH	15.20	30108239
208	Phosphorylation	QLRMQGQSVEAALRM HHHHHCCHHHHHHHH	28.84	28555341
216	Phosphorylation	VEAALRMERQAASEE HHHHHHHHHHHCCHH	34.90	27251275
224	Ubiquitination	RQAASEEKRKLAQLQ HHHCCHHHHHHHHHH	51.27	PubMed
226	Ubiquitination	AASEEKRKLAQLQVA HCCHHHHHHHHHHHH	60.28	21906983
233 (in isoform 2)	Ubiquitination	-	5.32	-
246	Ubiquitination	QEYDNHIKSSVVGSE HHHHHHHCHHHHCCH	29.18	21906983
252	Phosphorylation	IKSSVVGSERKRGMQ HCHHHHCCHHHCCCC	23.71	28857561
255	Acetylation	SVVGSERKRGMQLED HHHCCHHHCCCCHHH	49.61	30589477
255	Ubiquitination	SVVGSERKRGMQLED HHHCCHHHCCCCHHH	49.61	-
264	Ubiquitination	GMQLEDLKQQLQQAE CCCHHHHHHHHHHHH	48.60	21906983
264	Phosphorylation	GMQLEDLKQQLQQAE CCCHHHHHHHHHHHH	48.60	27251275
277	Sumoylation	AEEALVAKQEVIDKL HHHHHHHHHHHHHHH	39.24	-
277	Sumoylation	AEEALVAKQEVIDKL HHHHHHHHHHHHHHH	39.24	14651848
277	Ubiquitination	AEEALVAKQEVIDKL HHHHHHHHHHHHHHH	39.24	14651848
283	Ubiquitination	AKQEVIDKLKEEAEQ HHHHHHHHHHHHHHH	50.78	21906983
285	Ubiquitination	QEVIDKLKEEAEQHK HHHHHHHHHHHHHHC	60.28	15620648
292	Ubiquitination	KEEAEQHKIVMETVP HHHHHHHCCHHHHHH	36.37	21906983
297	Phosphorylation	QHKIVMETVPVLKAQ HHCCHHHHHHHHHHH	16.41	20068231
300	Ubiquitination	IVMETVPVLKAQADI CHHHHHHHHHHHHHH	8.12	17363905
302	Phosphorylation	METVPVLKAQADIYK HHHHHHHHHHHHHHH	38.39	27642862
302	Ubiquitination	METVPVLKAQADIYK HHHHHHHHHHHHHHH	38.39	21906983
308	Phosphorylation	LKAQADIYKADFQAE HHHHHHHHHHHHHHH	10.73	29083192
309	Ubiquitination	KAQADIYKADFQAER HHHHHHHHHHHHHHH	41.64	21890473
309	Ubiquitination	KAQADIYKADFQAER HHHHHHHHHHHHHHH	41.64	14651848
309	Sumoylation	KAQADIYKADFQAER HHHHHHHHHHHHHHH	41.64	14651848
309	Phosphorylation	KAQADIYKADFQAER HHHHHHHHHHHHHHH	41.64	27642862
309	Sumoylation	KAQADIYKADFQAER HHHHHHHHHHHHHHH	41.64	-
320	Phosphorylation	QAERQAREKLAEKKE HHHHHHHHHHHHHHH	56.27	27251275
321	Ubiquitination	AERQAREKLAEKKEL HHHHHHHHHHHHHHH	47.66	20010814
323 (in isoform 2)	Ubiquitination	-	37.32	-
325	Ubiquitination	AREKLAEKKELLQEQ HHHHHHHHHHHHHHH	46.04	17728323
326	Ubiquitination	REKLAEKKELLQEQL HHHHHHHHHHHHHHH	45.13	17728323
342	Ubiquitination	QLQREYSKLKASCQE HHHHHHHHHHHHHHH	53.78	-
344	Ubiquitination	QREYSKLKASCQESA HHHHHHHHHHHHHHH	41.83	21906983
353 (in isoform 2)	Ubiquitination	-	5.42	-
358	Ubiquitination	ARIEDMRKRHVEVSQ HHHHHHHHHHCCHHC	39.97	-
364	Phosphorylation	RKRHVEVSQAPLPPA HHHHCCHHCCCCCCC	13.71	26074081
374	Phosphorylation	PLPPAPAYLSSPLAL CCCCCCCCCCCCCCC	13.17	25159151
376	Phosphorylation	PPAPAYLSSPLALPS CCCCCCCCCCCCCCC	19.75	23401153
377	Phosphorylation	PAPAYLSSPLALPSQ CCCCCCCCCCCCCCC	22.72	25159151
377 (in isoform 2)	Ubiquitination	-	22.72	-
377	Ubiquitination	PAPAYLSSPLALPSQ CCCCCCCCCCCCCCC	22.72	21890473
383	Phosphorylation	SSPLALPSQRRSPPE CCCCCCCCCCCCCCC	36.85	27794612
387	Phosphorylation	ALPSQRRSPPEEPPD CCCCCCCCCCCCCCC	47.17	29255136
399	Ubiquitination	PPDFCCPKCQYQAPD CCCCCCCCCCCCCCC	21.76	14695475
442	Phosphorylation	------------------------------ ------------------------------		27642862
445	Phosphorylation	--------------------------------- ---------------------------------		27642862
455	Phosphorylation	------------------------------------------- -------------------------------------------		24719451
467	Ubiquitination	------------------------------------------------------- -------------------------------------------------------		17363905

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
8	S	Phosphorylation	Kinase	GSK3B	P49841	PSP
17	S	Phosphorylation	Kinase	GSK3B	P49841	PSP
31	S	Phosphorylation	Kinase	GSK3B	P49841	PSP
31	S	Phosphorylation	Kinase	IKBKB	O14920	GPS
43	S	Phosphorylation	Kinase	DNAPK	P78527	PSP
43	S	Phosphorylation	Kinase	GSK3B	P49841	PSP
43	S	Phosphorylation	Kinase	IKBKB	O14920	GPS
68	S	Phosphorylation	Kinase	IKBKB	O14920	GPS
85	S	Phosphorylation	Kinase	ATM	Q62388	PSP
85	S	Phosphorylation	Kinase	PRKCA	P17252	GPS
85	S	Phosphorylation	Kinase	IKBKB	O14920	GPS
85	S	Phosphorylation	Kinase	ATM	Q13315	Uniprot
141	S	Phosphorylation	Kinase	PRKCA	P17252	GPS
374	Y	Phosphorylation	Kinase	FYN	P06241	PSP
374	Y	Phosphorylation	Kinase	FGR	P09769	PSP
374	Y	Phosphorylation	Kinase	LYN	P07948	PSP
374	Y	Phosphorylation	Kinase	SRC	P12931	PSP
376	S	Phosphorylation	Kinase	IKBKB	O14920	GPS
-	K	Ubiquitination	E3 ubiquitin ligase	RBCK1	Q9BYM8	PMID:19675569
-	K	Ubiquitination	E3 ubiquitin ligase	PRKN	O60260	PMID:19880420
-	K	Ubiquitination	E3 ubiquitin ligase	RNF31	Q96EP0	PMID:24469399
-	K	Ubiquitination	E3 ubiquitin ligase	TRAF6	Q9Y4K3	PMID:15125833
-	K	Ubiquitination	E3 ubiquitin ligase	BIRC2	Q13490	PMID:12867425
-	K	Ubiquitination	E3 ubiquitin ligase	MALT1	Q9UDY8	PMID:14695475
-	K	Ubiquitination	E3 ubiquitin ligase	MIB2	Q96AX9	PMID:21896478
-	K	Ubiquitination	E3 ubiquitin ligase	TRIM23	P36406	PMID:32296023
-	K	Ubiquitination	E3 ubiquitin ligase	ipaH9.8	Q8VSC3	PMID:32296023

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Reference
27	K	ubiquitylation	14651848
Polyubiquitinated through 'Lys-27' by TRIM23; involved in antiviral innate and inflammatory responses.
63	K	ubiquitylation	14695475
Polyubiquitinated on Lys-399 through 'Lys-63'; the ubiquitination is mediated by BCL10, MALT1 and TRAF6 and probably plays a role in signaling by facilitating interactions with ubiquitin domain-containing proteins and activates the NF-kappa-B pathway.
63	K	ubiquitylation	14695475
Polyubiquitinated on Lys-285 through 'Lys-63'; the ubiquitination is mediated by NOD2 and RIPK2 and probably plays a role in signaling by facilitating interactions with ubiquitin domain-containing proteins and activates the NF-kappa-B pathway.
68	S	Phosphorylation	17977820
Phosphorylation at Ser-68 attenuates aminoterminal homodimerization.
85	S	ubiquitylation	16497931
Sumoylated on Lys-277 and Lys-309 with SUMO1; the modification results in phosphorylation of Ser-85 by ATM leading to a replacement of the sumoylation by mono-ubiquitination on these residues.
85	S	Sumoylation	16497931
Sumoylated on Lys-277 and Lys-309 with SUMO1; the modification results in phosphorylation of Ser-85 by ATM leading to a replacement of the sumoylation by mono-ubiquitination on these residues.
85	S	Phosphorylation	16497931
Sumoylated on Lys-277 and Lys-309 with SUMO1; the modification results in phosphorylation of Ser-85 by ATM leading to a replacement of the sumoylation by mono-ubiquitination on these residues.
111	K	ubiquitylation	21455181
Linear polyubiquitinated on Lys-111, Lys-143, Lys-226, Lys-246, Lys-264, Lys-277, Lys-285, Lys-292, Lys-302, Lys-309 and Lys-326; the head-to-tail polyubiquitination is mediated by the LUBAC complex and plays a key role in NF-kappa-B activation.
143	K	ubiquitylation	21455181
Linear polyubiquitinated on Lys-111, Lys-143, Lys-226, Lys-246, Lys-264, Lys-277, Lys-285, Lys-292, Lys-302, Lys-309 and Lys-326; the head-to-tail polyubiquitination is mediated by the LUBAC complex and plays a key role in NF-kappa-B activation.
226	K	ubiquitylation	21455181
Linear polyubiquitinated on Lys-111, Lys-143, Lys-226, Lys-246, Lys-264, Lys-277, Lys-285, Lys-292, Lys-302, Lys-309 and Lys-326; the head-to-tail polyubiquitination is mediated by the LUBAC complex and plays a key role in NF-kappa-B activation.
246	K	ubiquitylation	21455181
Linear polyubiquitinated on Lys-111, Lys-143, Lys-226, Lys-246, Lys-264, Lys-277, Lys-285, Lys-292, Lys-302, Lys-309 and Lys-326; the head-to-tail polyubiquitination is mediated by the LUBAC complex and plays a key role in NF-kappa-B activation.
264	K	ubiquitylation	21455181
Linear polyubiquitinated on Lys-111, Lys-143, Lys-226, Lys-246, Lys-264, Lys-277, Lys-285, Lys-292, Lys-302, Lys-309 and Lys-326; the head-to-tail polyubiquitination is mediated by the LUBAC complex and plays a key role in NF-kappa-B activation.
277	K	ubiquitylation	14651848
Sumoylated on Lys-277 and Lys-309 with SUMO1; the modification results in phosphorylation of Ser-85 by ATM leading to a replacement of the sumoylation by mono-ubiquitination on these residues.
277	K	Phosphorylation	14651848
Sumoylated on Lys-277 and Lys-309 with SUMO1; the modification results in phosphorylation of Ser-85 by ATM leading to a replacement of the sumoylation by mono-ubiquitination on these residues.
277	K	Sumoylation	14651848
Sumoylated on Lys-277 and Lys-309 with SUMO1; the modification results in phosphorylation of Ser-85 by ATM leading to a replacement of the sumoylation by mono-ubiquitination on these residues.
277	K	ubiquitylation	14651848
Linear polyubiquitinated on Lys-111, Lys-143, Lys-226, Lys-246, Lys-264, Lys-277, Lys-285, Lys-292, Lys-302, Lys-309 and Lys-326; the head-to-tail polyubiquitination is mediated by the LUBAC complex and plays a key role in NF-kappa-B activation.
277	K	ubiquitylation	14651848
Monoubiquitinated on Lys-277 and Lys-309; promotes nuclear export.
285	K	ubiquitylation	15620648
Polyubiquitinated on Lys-285 through 'Lys-63'; the ubiquitination is mediated by NOD2 and RIPK2 and probably plays a role in signaling by facilitating interactions with ubiquitin domain-containing proteins and activates the NF-kappa-B pathway.
285	K	ubiquitylation	15620648
Linear polyubiquitinated on Lys-111, Lys-143, Lys-226, Lys-246, Lys-264, Lys-277, Lys-285, Lys-292, Lys-302, Lys-309 and Lys-326; the head-to-tail polyubiquitination is mediated by the LUBAC complex and plays a key role in NF-kappa-B activation.
292	K	ubiquitylation	21455181
Linear polyubiquitinated on Lys-111, Lys-143, Lys-226, Lys-246, Lys-264, Lys-277, Lys-285, Lys-292, Lys-302, Lys-309 and Lys-326; the head-to-tail polyubiquitination is mediated by the LUBAC complex and plays a key role in NF-kappa-B activation.
302	K	ubiquitylation	21455181
Linear polyubiquitinated on Lys-111, Lys-143, Lys-226, Lys-246, Lys-264, Lys-277, Lys-285, Lys-292, Lys-302, Lys-309 and Lys-326; the head-to-tail polyubiquitination is mediated by the LUBAC complex and plays a key role in NF-kappa-B activation.
309	K	Sumoylation	14651848
Sumoylated on Lys-277 and Lys-309 with SUMO1; the modification results in phosphorylation of Ser-85 by ATM leading to a replacement of the sumoylation by mono-ubiquitination on these residues.
309	K	ubiquitylation	14651848
(Microbial infection) Polyubiquitinated on Lys-309 and Lys-321 via 'Lys-27'-linked ubiquitin by Shigella flexneri E3 ubiquitin-protein ligase ipah9.8, leading to its degradation by the proteasome.
309	K	ubiquitylation	14651848
Linear polyubiquitinated on Lys-111, Lys-143, Lys-226, Lys-246, Lys-264, Lys-277, Lys-285, Lys-292, Lys-302, Lys-309 and Lys-326; the head-to-tail polyubiquitination is mediated by the LUBAC complex and plays a key role in NF-kappa-B activation.
309	K	ubiquitylation	14651848
Monoubiquitinated on Lys-277 and Lys-309; promotes nuclear export.
309	K	ubiquitylation	14651848
Sumoylated on Lys-277 and Lys-309 with SUMO1; the modification results in phosphorylation of Ser-85 by ATM leading to a replacement of the sumoylation by mono-ubiquitination on these residues.
309	K	Phosphorylation	14651848
Sumoylated on Lys-277 and Lys-309 with SUMO1; the modification results in phosphorylation of Ser-85 by ATM leading to a replacement of the sumoylation by mono-ubiquitination on these residues.
321	K	ubiquitylation	20010814
(Microbial infection) Polyubiquitinated on Lys-309 and Lys-321 via 'Lys-27'-linked ubiquitin by Shigella flexneri E3 ubiquitin-protein ligase ipah9.8, leading to its degradation by the proteasome.
326	K	ubiquitylation	21455181
Linear polyubiquitinated on Lys-111, Lys-143, Lys-226, Lys-246, Lys-264, Lys-277, Lys-285, Lys-292, Lys-302, Lys-309 and Lys-326; the head-to-tail polyubiquitination is mediated by the LUBAC complex and plays a key role in NF-kappa-B activation.
399	K	ubiquitylation	15620648
Polyubiquitinated on Lys-399 through 'Lys-63'; the ubiquitination is mediated by BCL10, MALT1 and TRAF6 and probably plays a role in signaling by facilitating interactions with ubiquitin domain-containing proteins and activates the NF-kappa-B pathway.

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 NEMO_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
CDC37_HUMAN	CDC37	physical	14743216
A16L1_HUMAN	ATG16L1	physical	14743216
TBK1_HUMAN	TBK1	physical	14743216
PPM1B_HUMAN	PPM1B	physical	14585847
IKKA_HUMAN	CHUK	physical	11877453
CSN3_HUMAN	COPS3	physical	11418127
CDC37_HUMAN	CDC37	physical	11864612
IKKB_HUMAN	IKBKB	physical	11864612
IKKA_HUMAN	CHUK	physical	11864612
M3K14_HUMAN	MAP3K14	physical	9927690
TNAP3_HUMAN	TNFAIP3	physical	10755617
TANK_HUMAN	TANK	physical	12133833
IKKB_HUMAN	IKBKB	physical	12133833
NCOA3_HUMAN	NCOA3	physical	11971985
CIKS_HUMAN	TRAF3IP2	physical	10962033
CIKS_HUMAN	TRAF3IP2	physical	10962024
TRAF6_HUMAN	TRAF6	physical	18617513
IRAK1_HUMAN	IRAK1	physical	18347055
BCL10_HUMAN	BCL10	physical	18287044
IKKA_HUMAN	CHUK	physical	18207244
IKKB_HUMAN	IKBKB	physical	18207244
IRAK1_HUMAN	IRAK1	physical	18180283
TRAF6_HUMAN	TRAF6	physical	18180283
TBG1_HUMAN	TUBG1	physical	17891179
CETN3_HUMAN	CETN3	physical	20098747
SYT1_HUMAN	SYT1	physical	20098747
CPNE2_HUMAN	CPNE2	physical	20098747
HPCL1_HUMAN	HPCAL1	physical	20098747
MYL5_HUMAN	MYL5	physical	20098747
CALB1_HUMAN	CALB1	physical	20098747
TTYH2_HUMAN	TTYH2	physical	20098747
TCTP_HUMAN	TPT1	physical	20098747
H10_HUMAN	H1F0	physical	20098747
MCM7_HUMAN	MCM7	physical	20098747
CNOT7_HUMAN	CNOT7	physical	20098747
ADAP2_HUMAN	ADAP2	physical	20098747
TBCD7_HUMAN	TBC1D7	physical	20098747
GBG1_HUMAN	GNGT1	physical	20098747
SEPT9_HUMAN	SEPT9	physical	20098747
IKKB_HUMAN	IKBKB	physical	20098747
KPCB_HUMAN	PRKCB	physical	20098747
TBK1_HUMAN	TBK1	physical	20098747
IKKA_HUMAN	CHUK	physical	20098747
LCK_HUMAN	LCK	physical	20098747
CDK2_HUMAN	CDK2	physical	20098747
FLT3_HUMAN	FLT3	physical	20098747
FGR_HUMAN	FGR	physical	20098747
STK25_HUMAN	STK25	physical	20098747
PIM2_HUMAN	PIM2	physical	20098747
EPHA4_HUMAN	EPHA4	physical	20098747
TIE2_HUMAN	TEK	physical	20098747
JAK2_HUMAN	JAK2	physical	20098747
TEC_HUMAN	TEC	physical	20098747
VGFR3_HUMAN	FLT4	physical	20098747
KS6B2_HUMAN	RPS6KB2	physical	20098747
GRK4_HUMAN	GRK4	physical	20098747
KPCD3_HUMAN	PRKD3	physical	20098747
M3K2_HUMAN	MAP3K2	physical	20098747
AKT1_HUMAN	AKT1	physical	20098747
SGK1_HUMAN	SGK1	physical	20098747
ITK_HUMAN	ITK	physical	20098747
TYRO3_HUMAN	TYRO3	physical	20098747
MERTK_HUMAN	MERTK	physical	20098747
ALK_HUMAN	ALK	physical	20098747
JAK3_HUMAN	JAK3	physical	20098747
RET_HUMAN	RET	physical	20098747
ROR2_HUMAN	ROR2	physical	20098747
SRPK1_HUMAN	SRPK1	physical	20098747
PCKGC_HUMAN	PCK1	physical	20098747
ROS1_HUMAN	ROS1	physical	20098747
DAPK1_HUMAN	DAPK1	physical	20098747
CUED1_HUMAN	CUEDC1	physical	20098747
RBX2_HUMAN	RNF7	physical	20098747
HOIL1_HUMAN	RBCK1	physical	20098747
PSA3_HUMAN	PSMA3	physical	20098747
WDR5_HUMAN	WDR5	physical	20098747
LZIC_HUMAN	LZIC	physical	20098747
AR6P4_HUMAN	ARL6IP4	physical	20098747
PHLP_HUMAN	PDCL	physical	20098747
PFD5_HUMAN	PFDN5	physical	20098747
LPXN_HUMAN	LPXN	physical	20098747
NTM1A_HUMAN	NTMT1	physical	20098747
GA45G_HUMAN	GADD45G	physical	20098747
LC7L2_HUMAN	LUC7L2	physical	20098747
G45IP_HUMAN	GADD45GIP1	physical	20098747
PHF7_HUMAN	PHF7	physical	20098747
SCLT1_HUMAN	SCLT1	physical	20098747
NP1L5_HUMAN	NAP1L5	physical	20098747
TRI41_HUMAN	TRIM41	physical	20098747
APT_HUMAN	APRT	physical	20098747
K2C8_HUMAN	KRT8	physical	20098747
CS057_HUMAN	C19orf57	physical	20098747
NECA3_HUMAN	NECAB3	physical	20098747
MCM10_HUMAN	MCM10	physical	20098747
RPAP3_HUMAN	RPAP3	physical	20098747
RBM34_HUMAN	RBM34	physical	20098747
NHP2_HUMAN	NHP2	physical	20098747
IF1AX_HUMAN	EIF1AX	physical	20098747
DD19B_HUMAN	DDX19B	physical	20098747
RBM8A_HUMAN	RBM8A	physical	20098747
RS12_HUMAN	RPS12	physical	20098747
RL41_HUMAN	RPL41	physical	20098747
GEMI2_HUMAN	GEMIN2	physical	20098747
AF17_HUMAN	MLLT6	physical	20098747
TEANC_HUMAN	TCEANC	physical	20098747
TCP1L_HUMAN	TCP10L	physical	20098747
CU077_HUMAN	TCP10L	physical	20098747
T11L1_HUMAN	TCP11L1	physical	20098747
LMCD1_HUMAN	LMCD1	physical	20098747
NRBF2_HUMAN	NRBF2	physical	20098747
MZT2A_HUMAN	MZT2A	physical	20098747
TSLP_HUMAN	TSLP	physical	20098747
DNJC8_HUMAN	DNAJC8	physical	20098747
FRMD8_HUMAN	FRMD8	physical	20098747
CS012_HUMAN	C19orf12	physical	20098747
TCP11_HUMAN	TCP11	physical	20098747
HBAZ_HUMAN	HBZ	physical	20098747
TMA16_HUMAN	TMA16	physical	20098747
VAMP3_HUMAN	VAMP3	physical	20098747
ARGL1_HUMAN	ARGLU1	physical	20098747
GLYG2_HUMAN	GYG2	physical	20098747
PNM8A_HUMAN	PNMAL1	physical	20098747
LEG2_HUMAN	LGALS2	physical	20098747
ODAM_HUMAN	ODAM	physical	20098747
AMERL_HUMAN	AMMECR1L	physical	20098747
PKHJ1_HUMAN	PLEKHJ1	physical	20098747
AVPI1_HUMAN	AVPI1	physical	20098747
SENP2_HUMAN	SENP2	physical	20098747
ACBD6_HUMAN	ACBD6	physical	20098747
SHOT1_HUMAN	KIAA1598	physical	20098747
NRARP_HUMAN	NRARP	physical	20098747
ARP19_HUMAN	ARPP19	physical	20098747
IKKB_HUMAN	IKBKB	physical	15802604
AIP_HUMAN	AIP	physical	20211142
MED7_HUMAN	MED7	physical	20211142
WWP1_HUMAN	WWP1	physical	20211142
TRI31_HUMAN	TRIM31	physical	20211142
RPC1_HUMAN	POLR3A	physical	20211142
SNW1_HUMAN	SNW1	physical	20211142
TRI29_HUMAN	TRIM29	physical	20211142
ZZZ3_HUMAN	ZZZ3	physical	20211142
ZBTB3_HUMAN	ZBTB3	physical	20211142
CYLD_HUMAN	CYLD	physical	12917691
CYLD_HUMAN	CYLD	physical	12917690
CYLD_HUMAN	CYLD	physical	12917689
TANK_HUMAN	TANK	physical	20484576
PLK1_HUMAN	PLK1	physical	20484576
IKKB_HUMAN	IKBKB	physical	9751060
IKKA_HUMAN	CHUK	physical	9751060
IRAK1_HUMAN	IRAK1	physical	17997719
IKKB_HUMAN	IKBKB	physical	16603398
RIPK1_HUMAN	RIPK1	physical	16603398
BCL10_HUMAN	BCL10	physical	19897484
PRKN_HUMAN	PARK2	physical	17314283
UBC_HUMAN	UBC	physical	21113135
RIPK1_HUMAN	RIPK1	physical	21113135
TNIP1_HUMAN	TNIP1	physical	20010814
CUL1_HUMAN	CUL1	physical	19656241
FBW1A_HUMAN	BTRC	physical	19656241
IKKB_HUMAN	IKBKB	physical	19656241
IKKA_HUMAN	CHUK	physical	18079694
IKBA_HUMAN	NFKBIA	physical	21896478
IRAK1_HUMAN	IRAK1	physical	21220427
RUSC1_HUMAN	RUSC1	physical	19365808
IKKB_HUMAN	IKBKB	physical	19365808
CNTN2_HUMAN	CNTN2	physical	19064727
TRAF6_HUMAN	TRAF6	physical	20529958
BIRC2_HUMAN	BIRC2	physical	20932475
TRAF6_HUMAN	TRAF6	physical	20932475
MALT1_HUMAN	MALT1	physical	19494296
MYC_HUMAN	MYC	physical	20970423
TRI40_HUMAN	TRIM40	physical	21474709
IKKB_HUMAN	IKBKB	physical	22099304
RIPK1_HUMAN	RIPK1	physical	22099304
TNAP3_HUMAN	TNFAIP3	physical	22099304
MAVS_HUMAN	MAVS	physical	21903422
TBK1_HUMAN	TBK1	physical	21903422
IKKA_HUMAN	CHUK	physical	21903422
IKKB_HUMAN	IKBKB	physical	21903422
AKT1_HUMAN	AKT1	physical	20837477
UBP7_HUMAN	USP7	physical	18952891
NLRX1_HUMAN	NLRX1	physical	21703539
IKKA_HUMAN	CHUK	physical	21703539
IKKA_HUMAN	CHUK	physical	22605335
IKKB_HUMAN	IKBKB	physical	22605335
IKKB_HUMAN	IKBKB	physical	21803029
NEMO_HUMAN	IKBKG	physical	21803029
UBC_HUMAN	UBC	physical	21803029
TNIP1_HUMAN	TNIP1	physical	18212736
RIPK1_HUMAN	RIPK1	physical	18212736
IKKA_HUMAN	CHUK	physical	12244103
IKBA_HUMAN	NFKBIA	physical	16547522
IKKB_HUMAN	IKBKB	physical	16547522
RIPK1_HUMAN	RIPK1	physical	16547522
UBC_HUMAN	UBC	physical	21622647
ATM_HUMAN	ATM	physical	16497931
IKKA_HUMAN	CHUK	physical	16497931
IKKB_HUMAN	IKBKB	physical	16497931
IKBA_HUMAN	NFKBIA	physical	18957422
TRI23_HUMAN	TRIM23	physical	20724660
SENP2_HUMAN	SENP2	physical	21777808
MUC1_HUMAN	MUC1	physical	18037881
NEMO_HUMAN	IKBKG	physical	18037881
RB6I2_HUMAN	ERC1	physical	15218148
IKBA_HUMAN	NFKBIA	physical	15218148
UBC_HUMAN	UBC	physical	19185524
IKKA_HUMAN	CHUK	physical	17977820
IKKB_HUMAN	IKBKB	physical	17977820
IKKE_HUMAN	IKBKE	physical	17468758
TANK_HUMAN	TANK	physical	17468758
IKKA_HUMAN	CHUK	physical	11485410
IKBB_HUMAN	NFKBIB	physical	11485410
IKKB_HUMAN	IKBKB	physical	18266324
UBC_HUMAN	UBC	physical	21153314
RIPK1_HUMAN	RIPK1	physical	19373245
UBC_HUMAN	UBC	physical	19033441
PIAS4_HUMAN	PIAS4	physical	16906147
IKBA_HUMAN	NFKBIA	physical	21862596
IKBB_HUMAN	NFKBIB	physical	21862596
IKKA_HUMAN	CHUK	physical	12138192
IKKB_HUMAN	IKBKB	physical	20167598
TNIP2_HUMAN	TNIP2	physical	14653779
RIPK1_HUMAN	RIPK1	physical	18029035
IKKA_HUMAN	CHUK	physical	17728323
TRAF6_HUMAN	TRAF6	physical	17728323
RGAP1_HUMAN	RACGAP1	physical	18511905
KIF23_HUMAN	KIF23	physical	18511905
NEMO_HUMAN	IKBKG	physical	12612076
IKKB_HUMAN	IKBKB	physical	12612076
IKKA_HUMAN	CHUK	physical	12612076
NEMO_HUMAN	IKBKG	physical	16611882
IKKB_HUMAN	IKBKB	physical	16611882
IKKA_HUMAN	CHUK	physical	16611882
CNTN2_HUMAN	CNTN2	physical	16611882
HSP74_HUMAN	HSPA4	physical	20368414
IKKB_HUMAN	IKBKB	physical	20368414
IKKA_HUMAN	CHUK	physical	20368414
NALP2_HUMAN	NLRP2	physical	15456791
IKKA_HUMAN	CHUK	physical	10733566
ATM_HUMAN	ATM	physical	20065354
IKKA_HUMAN	CHUK	physical	17244613
PP2AA_HUMAN	PPP2CA	physical	16126728
VFLIP_HHV8P	HHV8GK18_gp80	physical	16311516
DC1L1_HUMAN	DYNC1LI1	physical	20026645
IKBA_HUMAN	NFKBIA	physical	11830587
CBP_HUMAN	CREBBP	physical	14597638
IKBA_HUMAN	NFKBIA	physical	11064457
TBK1_HUMAN	TBK1	physical	23028469
MAVS_HUMAN	MAVS	physical	23028469
ANXA1_HUMAN	ANXA1	physical	21383699
IKKA_HUMAN	CHUK	physical	12459277
IKKB_HUMAN	IKBKB	physical	12459277
IKKA_HUMAN	CHUK	physical	10980203
TRAF2_HUMAN	TRAF2	physical	10980203
IKKB_HUMAN	IKBKB	physical	10980203
CAR10_HUMAN	CARD10	physical	15184390
BCL10_HUMAN	BCL10	physical	15184390
IKKB_HUMAN	IKBKB	physical	15184390
IKKA_HUMAN	CHUK	physical	15184390
CAR11_HUMAN	CARD11	physical	15184390
BCL10_HUMAN	BCL10	physical	11113112
NEMO_HUMAN	IKBKG	physical	12435599
CIKS_HUMAN	TRAF3IP2	physical	12943667
IKKA_HUMAN	CHUK	physical	17000764
NEMO_HUMAN	IKBKG	physical	17000764
IKBA_HUMAN	NFKBIA	physical	15670770
TNAP3_HUMAN	TNFAIP3	physical	23032186
HOIL1_HUMAN	RBCK1	physical	23032186
RNF31_HUMAN	RNF31	physical	23032186
SHRPN_HUMAN	SHARPIN	physical	23032186
IKKA_HUMAN	CHUK	physical	16583354
IKKB_HUMAN	IKBKB	physical	16583354
SHRPN_HUMAN	SHARPIN	physical	21709223
HOIL1_HUMAN	RBCK1	physical	21709223
RIPK1_HUMAN	RIPK1	physical	21458669
FADD_HUMAN	FADD	physical	21458669
IKBA_HUMAN	NFKBIA	physical	15749833
SRC_HUMAN	SRC	physical	15749833
IKKA_HUMAN	CHUK	physical	15749833
IKKB_HUMAN	IKBKB	physical	15749833
NEMO_HUMAN	IKBKG	physical	19422324
UBC_HUMAN	UBC	physical	19303852
UBC_HUMAN	UBC	physical	17702576
RIPK1_HUMAN	RIPK1	physical	17702576
CAR11_HUMAN	CARD11	physical	18625728
SLD5_HUMAN	GINS4	physical	22939629
KPCE_HUMAN	PRKCE	physical	23123196
MALT1_HUMAN	MALT1	physical	17948050
NSF1C_HUMAN	NSFL1C	physical	22990857
IKKB_HUMAN	IKBKB	physical	22990857
IKKA_HUMAN	CHUK	physical	22990857
CYLD_HUMAN	CYLD	physical	22990857
SQSTM_HUMAN	SQSTM1	physical	16874300
IKBA_HUMAN	NFKBIA	physical	17363973
IKKB_HUMAN	IKBKB	physical	17363973
IKKA_HUMAN	CHUK	physical	17363973
M3K7_HUMAN	MAP3K7	physical	17363973
IKBA_HUMAN	NFKBIA	physical	18429822
IKKA_HUMAN	CHUK	physical	17568778
IKKB_HUMAN	IKBKB	physical	17568778
CAR11_HUMAN	CARD11	physical	17363905
BCL2_HUMAN	BCL2	physical	17363905
IKKA_HUMAN	CHUK	physical	18266467
IKKB_HUMAN	IKBKB	physical	18266467
UBC_HUMAN	UBC	physical	21811235
RNF31_HUMAN	RNF31	physical	21811235
HOIL1_HUMAN	RBCK1	physical	21811235
IKBA_HUMAN	NFKBIA	physical	21811235
IKBA_HUMAN	NFKBIA	physical	21217772
ATM_HUMAN	ATM	physical	18583959
IKKB_HUMAN	IKBKB	physical	18583959
PIAS4_HUMAN	PIAS4	physical	18583959
ATR_HUMAN	ATR	physical	18583959
ATRIP_HUMAN	ATRIP	physical	18583959
PAR10_HUMAN	PARP10	physical	23575687
PAR14_HUMAN	PARP14	physical	23575687
IKKA_HUMAN	CHUK	physical	18949366
IKKB_HUMAN	IKBKB	physical	18949366
RIPK1_HUMAN	RIPK1	physical	23746843
UBC_HUMAN	UBC	physical	23746843
IKBA_HUMAN	NFKBIA	physical	23746843
SASH1_HUMAN	SASH1	physical	23776175
EGLN3_HUMAN	EGLN3	physical	23732909
BIRC2_HUMAN	BIRC2	physical	23732909
HOIL1_HUMAN	RBCK1	physical	23732909
IKBA_HUMAN	NFKBIA	physical	23732909
UBC_HUMAN	UBC	physical	23807287
K2C8_HUMAN	KRT8	physical	21988832
K1C18_HUMAN	KRT18	physical	21988832
TNIP2_HUMAN	TNIP2	physical	21988832
TNAP3_HUMAN	TNFAIP3	physical	21988832
TAXB1_HUMAN	TAX1BP1	physical	21988832
TARA_HUMAN	TRIOBP	physical	21988832
KPCI_HUMAN	PRKCI	physical	21988832
CTIP_HUMAN	RBBP8	physical	21988832
RET1_HUMAN	RBP1	physical	21988832
NEMO_HUMAN	IKBKG	physical	21988832
STX11_HUMAN	STX11	physical	21988832
TANK_HUMAN	TANK	physical	21988832
TNIP1_HUMAN	TNIP1	physical	21988832
TAB2_HUMAN	TAB2	physical	21988832
MPRIP_HUMAN	MPRIP	physical	21988832
MYO5C_HUMAN	MYO5C	physical	21988832
OSB10_HUMAN	OSBPL10	physical	21988832
ADIP_HUMAN	SSX2IP	physical	21988832
IN80E_HUMAN	INO80E	physical	21988832
TRAF3_HUMAN	TRAF3	physical	22901541
K1C17_HUMAN	KRT17	physical	22863883
PSB8_HUMAN	PSMB8	physical	22863883
ZC12A_HUMAN	ZC3H12A	physical	24270572
SQSTM_HUMAN	SQSTM1	physical	24270048
IKKA_HUMAN	CHUK	physical	24469399
IKKB_HUMAN	IKBKB	physical	24469399
UBP10_HUMAN	USP10	physical	24270572
IRAK1_HUMAN	IRAK1	physical	24735611
RIPK1_HUMAN	RIPK1	physical	24735611
NMRL1_HUMAN	NMRAL1	physical	24832601
UBP7_HUMAN	USP7	physical	24832601
IKKA_HUMAN	CHUK	physical	23131831
IKKB_HUMAN	IKBKB	physical	23131831
NEMO_HUMAN	IKBKG	physical	23131831
PP4C_HUMAN	PPP4C	physical	24109239
2AAB_HUMAN	PPP2R1B	physical	24109239
IKKB_HUMAN	IKBKB	physical	24266532
NEMO_HUMAN	IKBKG	physical	24266532
IKKB_MOUSE	Ikbkb	physical	24266532
RHOA_HUMAN	RHOA	physical	24240172
IKKB_HUMAN	IKBKB	physical	24240172
GDIR1_HUMAN	ARHGDIA	physical	24240172
IKBA_HUMAN	NFKBIA	physical	18519641
TF65_HUMAN	RELA	physical	18519641
TRI13_HUMAN	TRIM13	physical	25152375
ATM_HUMAN	ATM	physical	24457965
PIAS4_HUMAN	PIAS4	physical	24457965
UBC_HUMAN	UBC	physical	25296760
IKKA_HUMAN	CHUK	physical	25304104
IKKB_HUMAN	IKBKB	physical	25304104
IKKB_HUMAN	IKBKB	physical	18450452
VFLIP_HHV8P	HHV8GK18_gp80	physical	24672029
RNF31_HUMAN	RNF31	physical	21455180
HOIL1_HUMAN	RBCK1	physical	21455180
SHRPN_HUMAN	SHARPIN	physical	21455180
IKBA_HUMAN	NFKBIA	physical	19959994
IKKA_HUMAN	CHUK	physical	19959994
IKKB_HUMAN	IKBKB	physical	19959994
UBC_HUMAN	UBC	physical	21862579
UBC_HUMAN	UBC	physical	19373254
UBC_HUMAN	UBC	physical	22605335
UBC_HUMAN	UBC	physical	22099304
UBC_HUMAN	UBC	physical	16603398
UBC_HUMAN	UBC	physical	19763089
RNF31_HUMAN	RNF31	physical	23732909
TRAF6_HUMAN	TRAF6	physical	23986494
SHRPN_HUMAN	SHARPIN	physical	23986494
MYD88_HUMAN	MYD88	physical	23986494
IRAK4_HUMAN	IRAK4	physical	23986494
IRAK1_HUMAN	IRAK1	physical	23986494
RNF31_HUMAN	RNF31	physical	23986494
HOIL1_HUMAN	RBCK1	physical	23986494
IKKB_HUMAN	IKBKB	physical	23986494
IKKA_HUMAN	CHUK	physical	23986494
TAB1_HUMAN	TAB1	physical	23986494
TAB2_HUMAN	TAB2	physical	23986494
TAB3_HUMAN	TAB3	physical	23986494
M3K7_HUMAN	MAP3K7	physical	23986494
UBC_HUMAN	UBC	physical	23986494
CDC37_HUMAN	CDC37	physical	24618592
IKKA_HUMAN	CHUK	physical	24618592
IKKB_HUMAN	IKBKB	physical	24618592
ENPL_HUMAN	HSP90B1	physical	24618592
IKKB_HUMAN	IKBKB	physical	25286246
IKKB_HUMAN	IKBKB	physical	25400026
TRAF6_HUMAN	TRAF6	physical	25400026
UBC_HUMAN	UBC	physical	25736758
IKKA_HUMAN	CHUK	physical	26496610
HS90A_HUMAN	HSP90AA1	physical	26496610
HS90B_HUMAN	HSP90AB1	physical	26496610
IKKB_HUMAN	IKBKB	physical	26496610
MSH3_HUMAN	MSH3	physical	26496610
CDK13_HUMAN	CDK13	physical	26496610
RB11B_HUMAN	RAB11B	physical	26496610
CDC37_HUMAN	CDC37	physical	26496610
MUC13_HUMAN	MUC13	physical	26496610
RBM26_HUMAN	RBM26	physical	26496610
RPA49_HUMAN	POLR1E	physical	26496610
CAAP1_HUMAN	CAAP1	physical	26496610
RFIP1_HUMAN	RAB11FIP1	physical	26496610
UBC_HUMAN	UBC	physical	25736757
UBC_HUMAN	UBC	physical	26740240
RIPK1_HUMAN	RIPK1	physical	26740240
COMD7_HUMAN	COMMD7	physical	26060140
MACD1_HUMAN	MACROD1	physical	25735744
PARP1_HUMAN	PARP1	physical	25735744
PIAS4_HUMAN	PIAS4	physical	25735744
RNF31_HUMAN	RNF31	physical	26577923
IKBA_HUMAN	NFKBIA	physical	26865630
VFLIP_HHV8P	HHV8GK18_gp80	physical	26865630
RIPK1_HUMAN	RIPK1	physical	26865630
TRI26_HUMAN	TRIM26	physical	26611359
TBK1_HUMAN	TBK1	physical	26611359
TRAF1_HUMAN	TRAF1	physical	25996949
TNAP3_HUMAN	TNFAIP3	physical	26802121
NEMO_HUMAN	IKBKG	physical	26802121
RIPK1_HUMAN	RIPK1	physical	26802121
CYLD_HUMAN	CYLD	physical	26802121
UBP18_HUMAN	USP18	physical	26240016
UBP10_HUMAN	USP10	physical	25861989
ZC12A_HUMAN	ZC3H12A	physical	25861989
VFLIP_HHV8P	HHV8GK18_gp80	physical	25979343
IKKB_HUMAN	IKBKB	physical	25979343
IMA5_HUMAN	KPNA1	physical	26060253
IMA7_HUMAN	KPNA6	physical	26060253
IMA8_HUMAN	KPNA7	physical	26060253
TNPO2_HUMAN	TNPO2	physical	26060253
TRI14_HUMAN	TRIM14	physical	24379373
PBIP1_HUMAN	PBXIP1	physical	24488098
BCL10_HUMAN	BCL10	physical	27777308
KLH21_HUMAN	KLHL21	physical	27387502
GSK3B_HUMAN	GSK3B	physical	27929056
NSF1C_HUMAN	NSFL1C	physical	27929056
RIPK1_HUMAN	RIPK1	physical	27929056
TRAF6_HUMAN	TRAF6	physical	27929056
IKKB_HUMAN	IKBKB	physical	27929056
IKKA_HUMAN	CHUK	physical	27929056
SHRPN_HUMAN	SHARPIN	physical	27893701
HOIL1_HUMAN	RBCK1	physical	27893701
IKKB_HUMAN	IKBKB	physical	28514442
SDCG8_HUMAN	SDCCAG8	physical	28514442
IKKA_HUMAN	CHUK	physical	28514442
CENPF_HUMAN	CENPF	physical	28514442
TANK_HUMAN	TANK	physical	28514442
TBK1_HUMAN	TBK1	physical	28514442
NFM_HUMAN	NEFM	physical	28514442
UBB_HUMAN	UBB	physical	28514442
CCAR1_HUMAN	CCAR1	physical	28514442
ZPR1_HUMAN	ZPR1	physical	28514442
TRI29_HUMAN	TRIM29	physical	27695001
UBC_HUMAN	UBC	physical	28939760
UBC_HUMAN	UBC	physical	28319114
HIF1A_HUMAN	HIF1A	physical	26500060
EPAS1_HUMAN	EPAS1	physical	26500060
UBC_HUMAN	UBC	physical	27669734
IKKB_HUMAN	IKBKB	physical	18462684
IKKA_HUMAN	CHUK	physical	18462684
NEMO_HUMAN	IKBKG	physical	18462684
UBC_HUMAN	UBC	physical	29125880
NEMO_HUMAN	IKBKG	physical	29111346
IKKB_HUMAN	IKBKB	physical	29111346
UBC_HUMAN	UBC	physical	29111346
VFLIP_HHV8P	HHV8GK18_gp80	physical	29111346

Drug and Disease Associations

Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
300291	Ectodermal dysplasia, anhidrotic, with immunodeficiency X-linked (EDAID)
300301	Ectodermal dysplasia, anhidrotic, with immunodeficiency, osteopetrosis and lymphedema (OLEDAID)
300584	Immunodeficiency, NEMO-related, without anhidrotic ectodermal dysplasia (NEMOID)
300636	Immunodeficiency 33 (IMD33)
300640	Recurrent isolated invasive pneumococcal disease 2 (IPD2)
308300	Incontinentia pigmenti (IP)
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.

Regulatory Network of NEMO_HUMAN

Related Literatures of Post-Translational Modification

Phosphorylation
Reference	PubMed
"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 TYR-374 AND SER-387, ANDMASS SPECTROMETRY.	19369195 [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-377 AND SER-387, ANDMASS SPECTROMETRY.	18669648 [Abstract]
"Phosphorylation of serine 68 in the IkappaB kinase (IKK)-bindingdomain of NEMO interferes with the structure of the IKK complex andtumor necrosis factor-alpha-induced NF-kappaB activity."; Palkowitsch L., Leidner J., Ghosh S., Marienfeld R.B.; J. Biol. Chem. 283:76-86(2008). Cited for: INTERACTION WITH IKBKB, PHOSPHORYLATION AT SER-68, AND MUTAGENESIS OFSER-68.	17977820 [Abstract]
"Molecular linkage between the kinase ATM and NF-kappaB signaling inresponse to genotoxic stimuli."; Wu Z.H., Shi Y., Tibbetts R.S., Miyamoto S.; Science 311:1141-1146(2006). Cited for: INTERACTION WITH ATM, PHOSPHORYLATION AT SER-85, AND MUTAGENESIS OFSER-85.	16497931 [Abstract]
"In vivo identification of inducible phosphoacceptors in theIKKgamma/NEMO subunit of human IkappaB kinase."; Carter R.S., Pennington K.N., Ungurait B.J., Ballard D.W.; J. Biol. Chem. 278:19642-19648(2003). Cited for: PHOSPHORYLATION AT SER-31; SER-43 AND SER-376.	12657630 [Abstract]
Sumoylation
Reference	PubMed
"SHARPIN forms a linear ubiquitin ligase complex regulating NF-kappaBactivity and apoptosis."; Ikeda F., Deribe Y.L., Skanland S.S., Stieglitz B., Grabbe C.,Franz-Wachtel M., van Wijk S.J., Goswami P., Nagy V., Terzic J.,Tokunaga F., Androulidaki A., Nakagawa T., Pasparakis M., Iwai K.,Sundberg J.P., Schaefer L., Rittinger K., Macek B., Dikic I.; Nature 471:637-641(2011). Cited for: UBIQUITINATION AT LYS-277; LYS-285; LYS-309; LYS-326; LYS-111;LYS-143; LYS-226; LYS-246; LYS-264; LYS-292 AND LYS-302 BY THE LUBACCOMPLEX, AND UBIQUITINATION AT LYS-139 AND LYS-283.	21455181 [Abstract]
"A bacterial E3 ubiquitin ligase IpaH9.8 targets NEMO/IKKgamma todampen the host NF-kappaB-mediated inflammatory response."; Ashida H., Kim M., Schmidt-Supprian M., Ma A., Ogawa M., Sasakawa C.; Nat. Cell Biol. 12:66-73(2010). Cited for: INTERACTION WITH SHIGELLA FLEXNERI IPAH9.8, AND UBIQUITINATION ATLYS-309 AND LYS-321.	20010814 [Abstract]
"Involvement of linear polyubiquitylation of NEMO in NF-kappaBactivation."; Tokunaga F., Sakata S., Saeki Y., Satomi Y., Kirisako T., Kamei K.,Nakagawa T., Kato M., Murata S., Yamaoka S., Yamamoto M., Akira S.,Takao T., Tanaka K., Iwai K.; Nat. Cell Biol. 11:123-132(2009). Cited for: UBIQUITINATION AT LYS-285 AND LYS-309.	19136968 [Abstract]
"Sequential modification of NEMO/IKKgamma by SUMO-1 and ubiquitinmediates NF-kappaB activation by genotoxic stress."; Huang T.T., Wuerzberger-Davis S.M., Wu Z.H., Miyamoto S.; Cell 115:565-576(2003). Cited for: SUMOYLATION AT LYS-277 AND LYS-309, UBIQUITINATION AT LYS-277 ANDLYS-309, MUTAGENESIS OF LYS-277 AND LYS-309, SUBCELLULAR LOCATION, ANDCHARACTERIZATION OF VARIANT EDAID ARG-417.	14651848 [Abstract]
Ubiquitylation
Reference	PubMed
"SHARPIN forms a linear ubiquitin ligase complex regulating NF-kappaBactivity and apoptosis."; Ikeda F., Deribe Y.L., Skanland S.S., Stieglitz B., Grabbe C.,Franz-Wachtel M., van Wijk S.J., Goswami P., Nagy V., Terzic J.,Tokunaga F., Androulidaki A., Nakagawa T., Pasparakis M., Iwai K.,Sundberg J.P., Schaefer L., Rittinger K., Macek B., Dikic I.; Nature 471:637-641(2011). Cited for: UBIQUITINATION AT LYS-277; LYS-285; LYS-309; LYS-326; LYS-111;LYS-143; LYS-226; LYS-246; LYS-264; LYS-292 AND LYS-302 BY THE LUBACCOMPLEX, AND UBIQUITINATION AT LYS-139 AND LYS-283.	21455181 [Abstract]
"A bacterial E3 ubiquitin ligase IpaH9.8 targets NEMO/IKKgamma todampen the host NF-kappaB-mediated inflammatory response."; Ashida H., Kim M., Schmidt-Supprian M., Ma A., Ogawa M., Sasakawa C.; Nat. Cell Biol. 12:66-73(2010). Cited for: INTERACTION WITH SHIGELLA FLEXNERI IPAH9.8, AND UBIQUITINATION ATLYS-309 AND LYS-321.	20010814 [Abstract]
"Involvement of linear polyubiquitylation of NEMO in NF-kappaBactivation."; Tokunaga F., Sakata S., Saeki Y., Satomi Y., Kirisako T., Kamei K.,Nakagawa T., Kato M., Murata S., Yamaoka S., Yamamoto M., Akira S.,Takao T., Tanaka K., Iwai K.; Nat. Cell Biol. 11:123-132(2009). Cited for: UBIQUITINATION AT LYS-285 AND LYS-309.	19136968 [Abstract]
"Bcl10 activates the NF-kappaB pathway through ubiquitination ofNEMO."; Zhou H., Wertz I., O'Rourke K., Ultsch M., Seshagiri S., Eby M.,Xiao W., Dixit V.M.; Nature 427:167-171(2004). Cited for: FUNCTION, UBIQUITINATION AT LYS-399, AND MUTAGENESIS OF LYS-399.	14695475 [Abstract]
"The Crohn's disease protein, NOD2, requires RIP2 in order to induceubiquitinylation of a novel site on NEMO."; Abbott D.W., Wilkins A., Asara J.M., Cantley L.C.; Curr. Biol. 14:2217-2227(2004). Cited for: UBIQUITINATION AT LYS-285, AND MUTAGENESIS OF LYS-115; LYS-224;LYS-285 AND LYS-399.	15620648 [Abstract]

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