IKBA_HUMAN - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: IKBA_HUMAN
• UniProt AC: P25963
• Protein Name: NF-kappa-B inhibitor alpha
• Gene Name: NFKBIA
• Organism: Homo sapiens (Human).
• Sequence Length: 317
• Subcellular Localization: Cytoplasm. Nucleus. Shuttles between the nucleus and the cytoplasm by a nuclear localization signal (NLS) and a CRM1-dependent nuclear export..
• Protein Description: Inhibits the activity of dimeric NF-kappa-B/REL complexes by trapping REL dimers in the cytoplasm through masking of their nuclear localization signals. On cellular stimulation by immune and proinflammatory responses, becomes phosphorylated promoting ubiquitination and degradation, enabling the dimeric RELA to translocate to the nucleus and activate transcription..
• Protein Sequence: MFQAAERPQEWAMEGPRDGLKKERLLDDRHDSGLDSMKDEEYEQMVKELQEIRLEPQEVPRGSEPWKQQLTEDGDSFLHLAIIHEEKALTMEVIRQVKGDLAFLNFQNNLQQTPLHLAVITNQPEIAEALLGAGCDPELRDFRGNTPLHLACEQGCLASVGVLTQSCTTPHLHSILKATNYNGHTCLHLASIHGYLGIVELLVSLGADVNAQEPCNGRTALHLAVDLQNPDLVSLLLKCGADVNRVTYQGYSPYQLTWGRPSTRIQQQLGQLTLENLQMLPESEDEESYDTESEFTEFTEDELPYDDCVFGGQRLTL

Overview of Protein Modification Sites with Functional and Structural Information

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
21	Ubiquitination	EGPRDGLKKERLLDD CCCCCCCCHHHHHCC	59.11	7479976
21	Sumoylation	EGPRDGLKKERLLDD CCCCCCCCHHHHHCC	59.11	7479976
21	Sumoylation	EGPRDGLKKERLLDD CCCCCCCCHHHHHCC	59.11	-
22	Ubiquitination	GPRDGLKKERLLDDR CCCCCCCHHHHHCCC	53.78	7479976
22	Sumoylation	GPRDGLKKERLLDDR CCCCCCCHHHHHCCC	53.78	-
22	Sumoylation	GPRDGLKKERLLDDR CCCCCCCHHHHHCCC	53.78	-
32	Phosphorylation	LLDDRHDSGLDSMKD HHCCCCCCCHHHHCH	34.82	11266466
36	Phosphorylation	RHDSGLDSMKDEEYE CCCCCHHHHCHHHHH	32.54	22322096
38	Ubiquitination	DSGLDSMKDEEYEQM CCCHHHHCHHHHHHH	66.97	22817900
42	Phosphorylation	DSMKDEEYEQMVKEL HHHCHHHHHHHHHHH	14.93	11266466
42	Dephosphorylation	DSMKDEEYEQMVKEL HHHCHHHHHHHHHHH	14.93	11106428
45	Sulfoxidation	KDEEYEQMVKELQEI CHHHHHHHHHHHHHH	2.88	11983684
47	Ubiquitination	EEYEQMVKELQEIRL HHHHHHHHHHHHHCC	47.57	22817900
67	Ubiquitination	PRGSEPWKQQLTEDG CCCCCCHHHHCCCCC	38.59	29967540
87	Ubiquitination	LAIIHEEKALTMEVI EEEECHHHCCHHHHH	45.79	-
90	Phosphorylation	IHEEKALTMEVIRQV ECHHHCCHHHHHHHH	19.02	20068231
98	Ubiquitination	MEVIRQVKGDLAFLN HHHHHHHCCCCEEEE	38.07	-
166	Phosphorylation	SVGVLTQSCTTPHLH HHHHHCCCCCCCCHH	14.27	-
174	Phosphorylation	CTTPHLHSILKATNY CCCCCHHHHHHHCCC	35.66	24719451
181	Nitration	SILKATNYNGHTCLH HHHHHCCCCCCCCEE	20.40	-
186	Glutathionylation	TNYNGHTCLHLASIH CCCCCCCCEEHHHHH	1.55	22833525
210	Hydroxylation	VSLGADVNAQEPCNG HHCCCCCCCCCCCCC	36.13	17003112
238	Ubiquitination	DLVSLLLKCGADVNR CHHHHHHHCCCCCCC	30.50	21963094
244	Hydroxylation	LKCGADVNRVTYQGY HHCCCCCCCEEECCC	33.00	17003112
283	Phosphorylation	NLQMLPESEDEESYD HHCCCCCCCCCCCCC	48.70	22817900
288	Phosphorylation	PESEDEESYDTESEF CCCCCCCCCCCCCCC	26.68	22817900
289	Phosphorylation	ESEDEESYDTESEFT CCCCCCCCCCCCCCC	30.11	-
291	Phosphorylation	EDEESYDTESEFTEF CCCCCCCCCCCCCCC	32.93	22817900
293	Phosphorylation	EESYDTESEFTEFTE CCCCCCCCCCCCCCC	39.85	22817900
299	Phosphorylation	ESEFTEFTEDELPYD CCCCCCCCCCCCCCC	35.97	8797825
305	Phosphorylation	FTEDELPYDDCVFGG CCCCCCCCCCCCCCC	36.72	14757045
305	Nitration	FTEDELPYDDCVFGG CCCCCCCCCCCCCCC	36.72	-

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
32	S	Phosphorylation	Kinase	CK2-FAMILY	-	GPS
32	S	Phosphorylation	Kinase	MAP3K14	Q99558	GPS
32	S	Phosphorylation	Kinase	RPS6KA3	P51812	GPS
32	S	Phosphorylation	Kinase	RPS6KA1	Q15418	GPS
32	S	Phosphorylation	Kinase	IKBKE	Q14164	GPS
32	S	Phosphorylation	Kinase	MAPK15	Q8TD08	GPS
32	S	Phosphorylation	Kinase	IKBKB	O14920	GPS
32	S	Phosphorylation	Kinase	SGK1	O00141	PSP
32	S	Phosphorylation	Kinase	CHUK	O15111	GPS
32	S	Phosphorylation	Kinase	CSNK2A1	P68400	GPS
32	S	Phosphorylation	Kinase	IKK-FAMILY	-	GPS
32	S	Phosphorylation	Kinase	CK2_GROUP	-	PhosphoELM
32	S	Phosphorylation	Kinase	IKK_GROUP	-	PhosphoELM
32	S	Phosphorylation	Kinase	AURKC	Q9UQB9	GPS
32	S	Phosphorylation	Kinase	AURKA	O14965	GPS
36	S	Phosphorylation	Kinase	CK2-FAMILY	-	GPS
36	S	Phosphorylation	Kinase	AURKA	O14965	GPS
36	S	Phosphorylation	Kinase	TBK1	Q9UHD2	Uniprot
36	S	Phosphorylation	Kinase	IKK-FAMILY	-	GPS
36	S	Phosphorylation	Kinase	CK2_GROUP	-	PhosphoELM
36	S	Phosphorylation	Kinase	MAPK15	Q8TD08	GPS
36	S	Phosphorylation	Kinase	MAP3K14	Q99558	GPS
36	S	Phosphorylation	Kinase	IKK_GROUP	-	PhosphoELM
36	S	Phosphorylation	Kinase	IKBKE	Q14164	GPS
36	S	Phosphorylation	Kinase	IKBKB	O14920	GPS
36	S	Phosphorylation	Kinase	CHUK	O15111	GPS
36	S	Phosphorylation	Kinase	CSNK2A1	P68400	GPS
42	Y	Phosphorylation	Kinase	INSR	P06213	PSP
42	Y	Phosphorylation	Kinase	SRC64	-	PhosphoELM
42	Y	Phosphorylation	Kinase	TYR-KINASES	-	Uniprot
42	Y	Phosphorylation	Kinase	LCK	P06239	PSP
42	Y	Phosphorylation	Kinase	SRC	P05480	PSP
283	S	Phosphorylation	Kinase	CK2	-	Uniprot
283	S	Phosphorylation	Kinase	CK2_GROUP	-	PhosphoELM
283	S	Phosphorylation	Kinase	CSNK2A1	P68400	GPS
283	S	Phosphorylation	Kinase	CK2-FAMILY	-	GPS
288	S	Phosphorylation	Kinase	CSNK2A1	P68400	GPS
288	S	Phosphorylation	Kinase	CK2-FAMILY	-	GPS
288	S	Phosphorylation	Kinase	CK2	-	Uniprot
289	Y	Phosphorylation	Kinase	BTK	Q06187	PSP
291	T	Phosphorylation	Kinase	CK2-FAMILY	-	GPS
291	T	Phosphorylation	Kinase	CSNK2A1	P68400	GPS
291	T	Phosphorylation	Kinase	CK2_GROUP	-	PhosphoELM
291	T	Phosphorylation	Kinase	CK2	-	Uniprot
293	S	Phosphorylation	Kinase	CK2	-	Uniprot
293	S	Phosphorylation	Kinase	CSNK2A1	P68400	GPS
293	S	Phosphorylation	Kinase	CK2-FAMILY	-	GPS
299	T	Phosphorylation	Kinase	CK2	-	Uniprot
299	T	Phosphorylation	Kinase	CK2-FAMILY	-	GPS
299	T	Phosphorylation	Kinase	CSNK2A1	P68400	GPS
305	Y	Phosphorylation	Kinase	ABL-FAMILY	-	GPS
305	Y	Phosphorylation	Kinase	BTK	Q06187	PSP
305	Y	Phosphorylation	Kinase	ABL1	P00519	PhosphoELM
-	K	Ubiquitination	E3 ubiquitin ligase	FBXW11	Q9UKB1	PMID:10748083
-	K	Ubiquitination	E3 ubiquitin ligase	BTRC	Q9Y297	PMID:10066435
-	K	Ubiquitination	E3 ubiquitin ligase	SKP2	Q13309	PMID:22199232
-	K	Ubiquitination	E3 ubiquitin ligase	CDC34	P49427	PMID:22199232
-	K	Ubiquitination	E3 ubiquitin ligase	SAG	P10523	PMID:23136067
-	K	Ubiquitination	E3 ubiquitin ligase	TRIM63	Q969Q1	PMID:23535871

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
21	K	ubiquitylation	Monoubiquitinated at Lys-21 and/or Lys-22 by UBE2D3.	7479976
22	K	ubiquitylation	Monoubiquitinated at Lys-21 and/or Lys-22 by UBE2D3.	7479976
32	S	Phosphorylation	Also ubiquitinated by SCF(BTRC) following stimulus-dependent phosphorylation at Ser-32 and Ser-36.	8657102
32	S	ubiquitylation	Also ubiquitinated by SCF(BTRC) following stimulus-dependent phosphorylation at Ser-32 and Ser-36.	8657102
36	S	Phosphorylation	Also ubiquitinated by SCF(BTRC) following stimulus-dependent phosphorylation at Ser-32 and Ser-36.	8657102
36	S	ubiquitylation	Also ubiquitinated by SCF(BTRC) following stimulus-dependent phosphorylation at Ser-32 and Ser-36.	8657102

Disease-associated PTM Sites based on SAP

* Distance = the distance between SAP position and PTM sites.

Oops, there are no SNP-PTM records of IKBA_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
P121A_HUMAN	POM121	physical	16189514
PIR_HUMAN	PIR	physical	10362352
BARD1_HUMAN	BARD1	physical	10362352
TF65_HUMAN	RELA	physical	11533489
TF65_HUMAN	RELA	physical	12419806
FBW1A_HUMAN	BTRC	physical	9990853
TF65_HUMAN	RELA	physical	9990853
TF65_HUMAN	RELA	physical	11313474
NFKB1_HUMAN	NFKB1	physical	11313474
ROA1_HUMAN	HNRNPA1	physical	11313474
DYL1_HUMAN	DYNLL1	physical	9372968
KS6A1_HUMAN	RPS6KA1	physical	9214631
G3BP2_HUMAN	G3BP2	physical	10969074
CAN1_HUMAN	CAPN1	physical	10521480
IKKB_HUMAN	IKBKB	physical	9751059
IKKA_HUMAN	CHUK	physical	9751059
M3K14_HUMAN	MAP3K14	physical	9751059
TF65_HUMAN	RELA	physical	9751059
ELP1_HUMAN	IKBKAP	physical	9751059
IKKA_HUMAN	CHUK	physical	10094049
HXB7_HUMAN	HOXB7	physical	10026139
UB2D1_HUMAN	UBE2D1	physical	9409737
AURKA_HUMAN	AURKA	physical	17060341
RELB_HUMAN	RELB	physical	19219072
TF65_HUMAN	RELA	physical	19219072
PSA2_HUMAN	PSMA2	physical	16098527
TF65_HUMAN	RELA	physical	16105840
NFKB1_HUMAN	NFKB1	physical	20980497
TF65_HUMAN	RELA	physical	20980497
NCOR1_HUMAN	NCOR1	physical	15536134
NCOR2_HUMAN	NCOR2	physical	15536134
CUL1_HUMAN	CUL1	physical	11483504
TF65_HUMAN	RELA	physical	11231305
CUL1_HUMAN	CUL1	physical	10713156
SKP1_HUMAN	SKP1	physical	10230406
FBW1B_HUMAN	FBXW11	physical	10230406
FBW1A_HUMAN	BTRC	physical	10066435
FBW1B_HUMAN	FBXW11	physical	10066435
SKP1_HUMAN	SKP1	physical	10066435
CUL1_HUMAN	CUL1	physical	10066435
ADT1_HUMAN	SLC25A4	physical	11287411
TF65_HUMAN	RELA	physical	11287411
KS6A1_HUMAN	RPS6KA1	physical	9261139
FBW1A_HUMAN	BTRC	physical	9859996
FBW1B_HUMAN	FBXW11	physical	12165731
SKP1_HUMAN	SKP1	physical	9990852
TF65_HUMAN	RELA	physical	8657102
CLUS_HUMAN	CLU	physical	20068069
MALT1_HUMAN	MALT1	physical	20551178
BCL10_HUMAN	BCL10	physical	20551178
TF65_HUMAN	RELA	physical	20551178
KC1A_HUMAN	CSNK1A1	physical	20551178
TF65_HUMAN	RELA	physical	10066434
FBW1A_HUMAN	BTRC	physical	19933270
IKKB_HUMAN	IKBKB	physical	20797629
TF65_HUMAN	RELA	physical	20797629
TF65_HUMAN	RELA	physical	22022389
FBW1A_HUMAN	BTRC	physical	20797629
MK14_HUMAN	MAPK14	physical	20797629
IKBB_HUMAN	NFKBIB	physical	22081069
TF65_HUMAN	RELA	physical	22081069
NEMO_HUMAN	IKBKG	physical	22081069
CSN2_HUMAN	COPS2	physical	17318178
NFKB1_HUMAN	NFKB1	physical	20558726
FBW1A_HUMAN	BTRC	physical	20558726
FBXW8_HUMAN	FBXW8	physical	20558726
FBW1A_HUMAN	BTRC	physical	9990852
TERA_HUMAN	VCP	physical	10930447
SKP1_HUMAN	SKP1	physical	22590978
CUL1_HUMAN	CUL1	physical	22590978
PSA4_HUMAN	PSMA4	physical	9875328
TF65_HUMAN	RELA	physical	14690596
PIN1_HUMAN	PIN1	physical	14690596
NFKB1_HUMAN	NFKB1	physical	11020244
TF65_HUMAN	RELA	physical	11020244
CUL1_HUMAN	CUL1	physical	11027288
DNJA3_HUMAN	DNAJA3	physical	15601829
SOCS3_HUMAN	SOCS3	physical	21451109
ATF4_HUMAN	ATF4	physical	18255255
ARRB1_HUMAN	ARRB1	physical	15173580
ARRB2_HUMAN	ARRB2	physical	15173580
PSA1_HUMAN	PSMA1	physical	23393163
TERA_HUMAN	VCP	physical	23393163
REL_HUMAN	REL	physical	8887627
TF65_HUMAN	RELA	physical	8887627
ARRB2_HUMAN	ARRB2	physical	15125834
ARRB1_HUMAN	ARRB1	physical	15125834
CSK2B_HUMAN	CSNK2B	physical	10398585
CSN1_HUMAN	GPS1	physical	23818606
CSN3_HUMAN	COPS3	physical	23818606
RPB3_HUMAN	POLR2C	physical	21988832
TF65_HUMAN	RELA	physical	21988832
ST7_HUMAN	ST7	physical	21988832
TF65_HUMAN	RELA	physical	9057089
NFKB1_HUMAN	NFKB1	physical	17003112
TF65_HUMAN	RELA	physical	17003112
TF65_HUMAN	RELA	physical	24248593
TERA_HUMAN	VCP	physical	24248593
FBW1A_HUMAN	BTRC	physical	10497169
CYTSA_HUMAN	SPECC1L	physical	26186194
SPDLY_HUMAN	SPDL1	physical	26186194
NFKB2_HUMAN	NFKB2	physical	26186194
REL_HUMAN	REL	physical	26186194
RPB1_HUMAN	POLR2A	physical	26186194
DCAF6_HUMAN	DCAF6	physical	26186194
NFKB1_HUMAN	NFKB1	physical	26186194
NEB1_HUMAN	PPP1R9A	physical	26186194
TF65_HUMAN	RELA	physical	26186194
AIDA_HUMAN	AIDA	physical	26186194
RPB11_HUMAN	POLR2J	physical	26186194
ANR27_HUMAN	ANKRD27	physical	26186194
RPOM_HUMAN	POLRMT	physical	26186194
YES_HUMAN	YES1	physical	26186194
SRC_HUMAN	SRC	physical	26186194
RELB_HUMAN	RELB	physical	26186194
SCRN2_HUMAN	SCRN2	physical	26186194
CTU2_HUMAN	CTU2	physical	26186194
OGDHL_HUMAN	OGDHL	physical	26186194
OTUB1_HUMAN	OTUB1	physical	26186194
HIF1N_HUMAN	HIF1AN	physical	26186194
TLDC1_HUMAN	TLDC1	physical	26186194
PRDC1_HUMAN	PRTFDC1	physical	26186194
FBW1B_HUMAN	FBXW11	physical	26186194
UBFD1_HUMAN	UBFD1	physical	26186194
IKKA_HUMAN	CHUK	physical	26186194
IKBB_HUMAN	NFKBIB	physical	26186194
TBC24_HUMAN	TBC1D24	physical	26186194
RHOA_HUMAN	RHOA	physical	26186194
TCEA1_HUMAN	TCEA1	physical	26186194
DENR_HUMAN	DENR	physical	26186194
BIRC2_HUMAN	BIRC2	physical	26186194
TBCE_HUMAN	TBCE	physical	26186194
GBG5_HUMAN	GNG5	physical	26186194
CUED1_HUMAN	CUEDC1	physical	26186194
ARMT1_HUMAN	C6orf211	physical	26186194
CHAC2_HUMAN	CHAC2	physical	26186194
MAVS_HUMAN	MAVS	physical	25636800
UBC9_HUMAN	UBE2I	physical	9409737
CENPF_HUMAN	CENPF	physical	26496610
CO7A1_HUMAN	COL7A1	physical	26496610
ATX3_HUMAN	ATXN3	physical	26496610
NFKB1_HUMAN	NFKB1	physical	26496610
NFKB2_HUMAN	NFKB2	physical	26496610
IKBE_HUMAN	NFKBIE	physical	26496610
REL_HUMAN	REL	physical	26496610
TF65_HUMAN	RELA	physical	26496610
NEMO_HUMAN	IKBKG	physical	26496610
AVL9_HUMAN	AVL9	physical	26496610
MED31_HUMAN	MED31	physical	26496610
RHG39_HUMAN	ARHGAP39	physical	26496610
TF65_HUMAN	RELA	physical	26463447
FBW1A_HUMAN	BTRC	physical	20851351
REL_HUMAN	REL	physical	28514442
RELB_HUMAN	RELB	physical	28514442
TF65_HUMAN	RELA	physical	28514442
NFKB2_HUMAN	NFKB2	physical	28514442
NFKB1_HUMAN	NFKB1	physical	28514442
ANR27_HUMAN	ANKRD27	physical	28514442
IKBB_HUMAN	NFKBIB	physical	28514442
OGDHL_HUMAN	OGDHL	physical	28514442
IKKA_HUMAN	CHUK	physical	28514442
TBC24_HUMAN	TBC1D24	physical	28514442
HIF1N_HUMAN	HIF1AN	physical	28514442
AIDA_HUMAN	AIDA	physical	28514442
TBCE_HUMAN	TBCE	physical	28514442
SPDLY_HUMAN	SPDL1	physical	28514442
NEB1_HUMAN	PPP1R9A	physical	28514442
SRC_HUMAN	SRC	physical	28514442
SCRN2_HUMAN	SCRN2	physical	28514442
PRDC1_HUMAN	PRTFDC1	physical	28514442
CUED1_HUMAN	CUEDC1	physical	28514442
CYTSA_HUMAN	SPECC1L	physical	28514442
TCEA1_HUMAN	TCEA1	physical	28514442
FBW1B_HUMAN	FBXW11	physical	28514442
RPB1_HUMAN	POLR2A	physical	28514442
MCTS1_HUMAN	MCTS1	physical	28514442
DENR_HUMAN	DENR	physical	28514442
ARMT1_HUMAN	C6orf211	physical	28514442
GNA1_HUMAN	GNPNAT1	physical	28514442
RPOM_HUMAN	POLRMT	physical	28514442
RHOA_HUMAN	RHOA	physical	28514442
GBG5_HUMAN	GNG5	physical	28514442
PLSI_HUMAN	PLS1	physical	28514442

Drug and Disease Associations

• Kegg Disease
• There are no disease associations of PTM sites.
• OMIM Disease
• 612132: Ectodermal dysplasia, anhidrotic, with T-cell immunodeficiency autosomal dominant (ADEDAID)
• Kegg Drug
• There are no disease associations of PTM sites.
• DrugBank
• DB00945: Acetylsalicylic acid

Related Literatures of Post-Translational Modification

Hydroxylation

"Posttranslational hydroxylation of ankyrin repeats in IkappaBproteins by the hypoxia-inducible factor (HIF) asparaginylhydroxylase, factor inhibiting HIF (FIH).";
Cockman M.E., Lancaster D.E., Stolze I.P., Hewitson K.S.,McDonough M.A., Coleman M.L., Coles C.H., Yu X., Hay R.T., Ley S.C.,Pugh C.W., Oldham N.J., Masson N., Schofield C.J., Ratcliffe P.J.;
Proc. Natl. Acad. Sci. U.S.A. 103:14767-14772(2006).
Cited for: INTERACTION WITH HIF1AN, HYDROXYLATION AT ASN-210 AND ASN-244, ANDMUTAGENESIS OF ASN-210 AND ASN-244.
PubMed: 17003112

Phosphorylation

"IKK epsilon is part of a novel PMA-inducible IkappaB kinasecomplex.";
Peters R.T., Liao S.-M., Maniatis T.;
Mol. Cell 5:513-522(2000).
Cited for: PHOSPHORYLATION AT SER-32 AND SER-36.
PubMed: 10882136

"Identification of the ubiquitin carrier proteins, E2s, involved insignal-induced conjugation and subsequent degradation ofIkappaBalpha.";
Gonen H., Bercovich B., Orian A., Carrano A., Takizawa C.,Yamanaka K., Pagano M., Iwai K., Ciechanover A.;
J. Biol. Chem. 274:14823-14830(1999).
Cited for: PHOSPHORYLATION AT SER-32 AND SER-36, MUTAGENESIS OF SER-32 ANDSER-36, AND UBIQUITINATION BY UBE2D2 AND UBE2D3.
PubMed: 10329681

"Phosphorylation of IkappaBalpha in the C-terminal PEST domain bycasein kinase II affects intrinsic protein stability.";
Lin R., Beauparlant P., Makris C., Meloche S., Hiscott J.;
Mol. Cell. Biol. 16:1401-1409(1996).
Cited for: PHOSPHORYLATION AT THR-291; SER-283 AND THR-299.
PubMed: 8657113

"Casein kinase II phosphorylates I kappa B alpha at S-283, S-289, S-293, and T-291 and is required for its degradation.";
McElhinny J.A., Trushin S.A., Bren G.D., Chester N., Paya C.V.;
Mol. Cell. Biol. 16:899-906(1996).
Cited for: PHOSPHORYLATION AT SER-283; SER-288; SER-293 AND THR-291.
PubMed: 8622692

"Tyrosine phosphorylation of IkappaB-alpha activates NF-kappaB withoutproteolytic degradation of IkappaB-alpha.";
Imbert V., Rupec R.A., Livolsi A., Pahl H.L., Traenckner E.B.-M.,Mueller-Dieckmann C., Farahifar D., Rossi B., Auberger P.,Baeuerle P.A., Peyron J.-F.;
Cell 86:787-798(1996).
Cited for: PHOSPHORYLATION AT TYR-42, AND MUTAGENESIS OF TYR-42.
PubMed: 8797825

Ubiquitylation

"Priming and extending: a UbcH5/Cdc34 E2 handoff mechanism forpolyubiquitination on a SCF substrate.";
Wu K., Kovacev J., Pan Z.Q.;
Mol. Cell 37:784-796(2010).
Cited for: UBIQUITINATION AT LYS-21 AND LYS-22.
PubMed: 20347421

"Signal-induced degradation of IkappaB alpha requires site-specificubiquitination.";
Scherer D.C., Brockman J.A., Chen Z., Maniatis T., Ballard D.W.;
Proc. Natl. Acad. Sci. U.S.A. 92:11259-11263(1995).
Cited for: UBIQUITINATION AT LYS-21 AND LYS-22, FUNCTION, AND MUTAGENESIS OFLYS-21; LYS-22; LYS-38 AND LYS-47.
PubMed: 7479976