RELB_HUMAN - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: RELB_HUMAN
• UniProt AC: Q01201
• Protein Name: Transcription factor RelB
• Gene Name: RELB
• Organism: Homo sapiens (Human).
• Sequence Length: 579
• Subcellular Localization: Nucleus . Cytoplasm, cytoskeleton, microtubule organizing center, centrosome . Colocalizes with NEK6 in the centrosome.
• Protein Description: NF-kappa-B is a pleiotropic transcription factor which is present in almost all cell types and is involved in many biological processed 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. NF-kappa-B heterodimeric RelB-p50 and RelB-p52 complexes are transcriptional activators. RELB neither associates with DNA nor with RELA/p65 or REL. Stimulates promoter activity in the presence of NFKB2/p49. As a member of the NUPR1/RELB/IER3 survival pathway, may provide pancreatic ductal adenocarcinoma with remarkable resistance to cell stress, such as starvation or gemcitabine treatment. Regulates the circadian clock by repressing the transcriptional activator activity of the CLOCK-ARNTL/BMAL1 heterodimer in a CRY1/CRY2 independent manner. Increased repression of the heterodimer is seen in the presence of NFKB2/p52. Is required for both T and B lymphocyte maturation and function. [PubMed: 26385063]
• Protein Sequence: MLRSGPASGPSVPTGRAMPSRRVARPPAAPELGALGSPDLSSLSLAVSRSTDELEIIDEYIKENGFGLDGGQPGPGEGLPRLVSRGAASLSTVTLGPVAPPATPPPWGCPLGRLVSPAPGPGPQPHLVITEQPKQRGMRFRYECEGRSAGSILGESSTEASKTLPAIELRDCGGLREVEVTACLVWKDWPHRVHPHSLVGKDCTDGICRVRLRPHVSPRHSFNNLGIQCVRKKEIEAAIERKIQLGIDPYNAGSLKNHQEVDMNVVRICFQASYRDQQGQMRRMDPVLSEPVYDKKSTNTSELRICRINKESGPCTGGEELYLLCDKVQKEDISVVFSRASWEGRADFSQADVHRQIAIVFKTPPYEDLEIVEPVTVNVFLQRLTDGVCSEPLPFTYLPRDHDSYGVDKKRKRGMPDVLGELNSSDPHGIESKRRKKKPAILDHFLPNHGSGPFLPPSALLPDPDFFSGTVSLPGLEPPGGPDLLDDGFAYDPTAPTLFTMLDLLPPAPPHASAVVCSGGAGAVVGETPGPEPLTLDSYQAPGPGDGGTASLVGSNMFPNHYREAAFGGGLLSPGPEAT

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
8	Phosphorylation	MLRSGPASGPSVPTG CCCCCCCCCCCCCCC	55.13	28555341
11	Phosphorylation	SGPASGPSVPTGRAM CCCCCCCCCCCCCCC	44.23	22210691
14	Phosphorylation	ASGPSVPTGRAMPSR CCCCCCCCCCCCCCC	36.82	22210691
16	Methylation	GPSVPTGRAMPSRRV CCCCCCCCCCCCCCC	30.14	24129315
20	Phosphorylation	PTGRAMPSRRVARPP CCCCCCCCCCCCCCC	21.45	22210691
37	Phosphorylation	PELGALGSPDLSSLS CCCCCCCCCCHHHHH	18.98	29255136
41	Phosphorylation	ALGSPDLSSLSLAVS CCCCCCHHHHHHEEC	36.29	30108239
42	Phosphorylation	LGSPDLSSLSLAVSR CCCCCHHHHHHEECC	29.31	30108239
44	Phosphorylation	SPDLSSLSLAVSRST CCCHHHHHHEECCCC	19.07	27794612
48	Phosphorylation	SSLSLAVSRSTDELE HHHHHEECCCCCHHH	18.20	27080861
50	Phosphorylation	LSLAVSRSTDELEII HHHEECCCCCHHHHH	32.48	30108239
51	Phosphorylation	SLAVSRSTDELEIID HHEECCCCCHHHHHH	32.17	25954137
103	Phosphorylation	GPVAPPATPPPWGCP CCCCCCCCCCCCCCC	41.94	24719451
116	Phosphorylation	CPLGRLVSPAPGPGP CCCCCEECCCCCCCC	21.67	25159151
151	Phosphorylation	CEGRSAGSILGESST ECCCCCCCCCCCCCC	17.85	27067055
163	O-linked_Glycosylation	SSTEASKTLPAIELR CCCCHHHCCCEEEEE	35.16	30379171
217	Phosphorylation	VRLRPHVSPRHSFNN EEECCCCCCCCCCCC	17.12	26270265
221	Phosphorylation	PHVSPRHSFNNLGIQ CCCCCCCCCCCCCCE	30.83	30108239
254	Phosphorylation	IDPYNAGSLKNHQEV CCCCCCCCCCCCCEE	33.49	27067055
293	Phosphorylation	PVLSEPVYDKKSTNT CCCCCCCCCCCCCCC	32.53	28064214
425	Phosphorylation	VLGELNSSDPHGIES HHHHCCCCCCCCHHC	54.83	21712546
472	Phosphorylation	DFFSGTVSLPGLEPP CCCCCCEECCCCCCC	28.78	-
573	Phosphorylation	AFGGGLLSPGPEAT- HHCCCCCCCCCCCC-	32.62	25159151
579	Phosphorylation	LSPGPEAT------- CCCCCCCC-------	37.16	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
472	S	Phosphorylation	Kinase	CHUK	O15111	GPS
472	S	Phosphorylation	Kinase	IKBKB	O14920	GPS
573	S	Phosphorylation	Kinase	GSK3B	P49841	PSP

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
103	T	Phosphorylation	Phosphorylation at 'Thr-103' and 'Ser-573' is followed by proteasomal degradation.	-
573	S	Phosphorylation	Phosphorylation at 'Thr-103' and 'Ser-573' is followed by proteasomal degradation.	18669648

Disease-associated PTM Sites based on SAP

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

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

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
ACL6A_HUMAN	ACTL6A	physical	14743216
BCL7A_HUMAN	BCL7A	physical	14743216
HDAC6_HUMAN	HDAC6	physical	14743216
IMA1_HUMAN	KPNA2	physical	14743216
IMA7_HUMAN	KPNA6	physical	14743216
NFKB1_HUMAN	NFKB1	physical	14743216
NFKB2_HUMAN	NFKB2	physical	14743216
TF65_HUMAN	RELA	physical	14743216
REQU_HUMAN	DPF2	physical	14743216
SMCA4_HUMAN	SMARCA4	physical	14743216
SMRC1_HUMAN	SMARCC1	physical	14743216
SMRC2_HUMAN	SMARCC2	physical	14743216
SMCE1_HUMAN	SMARCE1	physical	14743216
SNF5_HUMAN	SMARCB1	physical	14743216
UBP11_HUMAN	USP11	physical	14743216
TF65_HUMAN	RELA	physical	21884980
EZH2_HUMAN	EZH2	physical	21884980
SUZ12_HUMAN	SUZ12	physical	21884980
NFKB2_HUMAN	NFKB2	physical	22388891
NFKB2_HUMAN	NFKB2	physical	22864569
GSK3B_HUMAN	GSK3B	physical	21217772
DNMT1_HUMAN	DNMT1	physical	23548901
UCRI_HUMAN	UQCRFS1	physical	21988832
TF65_HUMAN	RELA	physical	25241761
REL_HUMAN	REL	physical	28514442
NFKB2_HUMAN	NFKB2	physical	28514442
TF65_HUMAN	RELA	physical	28514442
NFKB1_HUMAN	NFKB1	physical	28514442
IKBE_HUMAN	NFKBIE	physical	28514442
TNIP2_HUMAN	TNIP2	physical	28514442
DIAC_HUMAN	CTBS	physical	28514442
SMRD2_HUMAN	SMARCD2	physical	28514442
SMRD1_HUMAN	SMARCD1	physical	28514442
SMCA2_HUMAN	SMARCA2	physical	28514442
KLH20_HUMAN	KLHL20	physical	28514442
SMRD3_HUMAN	SMARCD3	physical	28514442
SMRC2_HUMAN	SMARCC2	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

"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-573, AND MASSSPECTROMETRY.
PubMed: 19690332

"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-37 AND SER-573, AND MASSSPECTROMETRY.
PubMed: 18669648