IKBB_HUMAN - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: IKBB_HUMAN
• UniProt AC: Q15653
• Protein Name: NF-kappa-B inhibitor beta
• Gene Name: NFKBIB
• Organism: Homo sapiens (Human).
• Sequence Length: 356
• Subcellular Localization: Cytoplasm. Nucleus.
• Protein Description: Inhibits NF-kappa-B by complexing with and trapping it in the cytoplasm. However, the unphosphorylated form resynthesized after cell stimulation is able to bind NF-kappa-B allowing its transport to the nucleus and protecting it to further NFKBIA-dependent inactivation. Association with inhibitor kappa B-interacting NKIRAS1 and NKIRAS2 prevent its phosphorylation rendering it more resistant to degradation, explaining its slower degradation..
• Protein Sequence: MAGVACLGKAADADEWCDSGLGSLGPDAAAPGGPGLGAELGPGLSWAPLVFGYVTEDGDTALHLAVIHQHEPFLDFLLGFSAGTEYMDLQNDLGQTALHLAAILGETSTVEKLYAAGAGLCVAERRGHTALHLACRVGAHACARALLQPRPRRPREAPDTYLAQGPDRTPDTNHTPVALYPDSDLEKEEEESEEDWKLQLEAENYEGHTPLHVAVIHKDVEMVRLLRDAGADLDKPEPTCGRSPLHLAVEAQAADVLELLLRAGANPAARMYGGRTPLGSAMLRPNPILARLLRAHGAPEPEGEDEKSGPCSSSSDSDSGDEGDEYDDIVVHSSRSQTRLPPTPASKPLPDDPRPV

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
19	Phosphorylation	DADEWCDSGLGSLGP CHHHHHHCCCHHCCC	32.55	16822942
23	Phosphorylation	WCDSGLGSLGPDAAA HHHCCCHHCCCCCCC	34.88	16822942
160	Phosphorylation	RPREAPDTYLAQGPD CCCCCCCCCCCCCCC	21.26	29978859
161	Phosphorylation	PREAPDTYLAQGPDR CCCCCCCCCCCCCCC	13.86	24927040
169	Phosphorylation	LAQGPDRTPDTNHTP CCCCCCCCCCCCCCC	32.66	26074081
172	Phosphorylation	GPDRTPDTNHTPVAL CCCCCCCCCCCCEEE	30.06	26074081
175	Phosphorylation	RTPDTNHTPVALYPD CCCCCCCCCEEECCC	22.87	26657352
180	Phosphorylation	NHTPVALYPDSDLEK CCCCEEECCCCHHHH	8.68	29978859
183	Phosphorylation	PVALYPDSDLEKEEE CEEECCCCHHHHHHH	39.32	21082442
192	Phosphorylation	LEKEEEESEEDWKLQ HHHHHHHCHHHHHHH	49.95	29978859
235	Acetylation	DAGADLDKPEPTCGR HCCCCCCCCCCCCCC	59.59	26051181
235	Ubiquitination	DAGADLDKPEPTCGR HCCCCCCCCCCCCCC	59.59	-
239	Phosphorylation	DLDKPEPTCGRSPLH CCCCCCCCCCCCHHH	26.40	20068231
276	Phosphorylation	ARMYGGRTPLGSAML HHHHCCCCCCCCCCC	26.58	-
280	Phosphorylation	GGRTPLGSAMLRPNP CCCCCCCCCCCCCCH	20.42	28857561
308	Phosphorylation	PEGEDEKSGPCSSSS CCCCCCCCCCCCCCC	46.01	-
312	Phosphorylation	DEKSGPCSSSSDSDS CCCCCCCCCCCCCCC	36.07	24461736
313	Phosphorylation	EKSGPCSSSSDSDSG CCCCCCCCCCCCCCC	40.35	12732617
314	Phosphorylation	KSGPCSSSSDSDSGD CCCCCCCCCCCCCCC	23.13	24461736
314 (in isoform 2)	Phosphorylation	-	23.13	24114839
315 (in isoform 2)	Phosphorylation	-	42.98	9278383
315	Phosphorylation	SGPCSSSSDSDSGDE CCCCCCCCCCCCCCC	42.98	12732617
317	Phosphorylation	PCSSSSDSDSGDEGD CCCCCCCCCCCCCCC	35.31	24461736
317 (in isoform 2)	Phosphorylation	-	35.31	24114839
319 (in isoform 2)	Phosphorylation	-	52.69	24114839
319	Phosphorylation	SSSSDSDSGDEGDEY CCCCCCCCCCCCCCC	52.69	24461736
325 (in isoform 2)	Phosphorylation	-	62.81	24114839
343	Phosphorylation	SQTRLPPTPASKPLP CCCCCCCCCCCCCCC	29.55	21857030
346	Phosphorylation	RLPPTPASKPLPDDP CCCCCCCCCCCCCCC	35.69	24719451
347	Acetylation	LPPTPASKPLPDDPR CCCCCCCCCCCCCCC	53.32	26051181

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
19	S	Phosphorylation	Kinase	KS6A1	Q15418	PhosphoELM
23	S	Phosphorylation	Kinase	KS6A1	Q15418	PhosphoELM
313	S	Phosphorylation	Kinase	CSNK2A1	P68400	GPS
313	S	Phosphorylation	Kinase	CK2-FAMILY	-	GPS
313	S	Phosphorylation	Kinase	CK2	-	Uniprot
315	S	Phosphorylation	Kinase	CSNK2A1	P68400	GPS
315	S	Phosphorylation	Kinase	CK2-FAMILY	-	GPS
315	S	Phosphorylation	Kinase	CK2	-	Uniprot
-	K	Ubiquitination	E3 ubiquitin ligase	BTRC	Q9Y297	PMID:10514424
-	K	Ubiquitination	E3 ubiquitin ligase	ARIH2	O95376	PMID:23179078

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of IKBB_HUMAN !!

Disease-associated PTM Sites based on SAP

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

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

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
TF65_HUMAN	RELA	physical	12672800
RXRA_HUMAN	RXRA	physical	9452433
TF65_HUMAN	RELA	physical	8816457
NCOR2_HUMAN	NCOR2	physical	15536134
TF65_HUMAN	RELA	physical	22081069
BRAP_HUMAN	BRAP	physical	21670849
DNJA3_HUMAN	DNAJA3	physical	15601829
A4_HUMAN	APP	physical	21832049
REL_HUMAN	REL	physical	8887627
TF65_HUMAN	RELA	physical	8887627
TF65_HUMAN	RELA	physical	21988832
TSN1_HUMAN	TSPAN1	physical	21988832
VPS52_HUMAN	VPS52	physical	25416956
FBW1A_HUMAN	BTRC	physical	10497169
RPA49_HUMAN	POLR1E	physical	26186194
REL_HUMAN	REL	physical	26186194
NFKB2_HUMAN	NFKB2	physical	26186194
NFKB1_HUMAN	NFKB1	physical	26186194
CRCM_HUMAN	MCC	physical	26186194
TF65_HUMAN	RELA	physical	26186194
HIF1N_HUMAN	HIF1AN	physical	26186194
TBP_HUMAN	TBP	physical	26186194
FBW1B_HUMAN	FBXW11	physical	25241761
REL_HUMAN	REL	physical	28514442
TF65_HUMAN	RELA	physical	28514442
CRCM_HUMAN	MCC	physical	28514442
NFKB1_HUMAN	NFKB1	physical	28514442
NFKB2_HUMAN	NFKB2	physical	28514442
RPA49_HUMAN	POLR1E	physical	28514442
TBP_HUMAN	TBP	physical	28514442

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.

Related Literatures of Post-Translational Modification

Phosphorylation

"Basal phosphorylation of the PEST domain in the I(kappa)B(beta)regulates its functional interaction with the c-rel proto-oncogeneproduct.";
Chu Z.L., McKinsey T.A., Liu L., Qi X., Ballard D.W.;
Mol. Cell. Biol. 16:5974-5984(1996).
Cited for: PHOSPHORYLATION AT SER-313 AND SER-315.
PubMed: 8887627