RELB_MOUSE - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: RELB_MOUSE
• UniProt AC: Q04863
• Protein Name: Transcription factor RelB
• Gene Name: Relb
• Organism: Mus musculus (Mouse).
• Sequence Length: 558
• 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 (By similarity). As a member of the NUPR1/RELB/IER3 survival pathway, may allow the development of pancreatic intraepithelial neoplasias. 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 (By similarity)..
• Protein Sequence: MPSRRAARESAPELGALGSSDLSSLSLTVSRTTDELEIIDEYIKENGFGLDGTQLSEMPRLVPRGPASLSSVTLGPAAPPPPATPSWSCTLGRLVSPGPCPRPYLVITEQPKQRGMRFRYECEGRSAGSILGESSTEASKTLPAIELRDCGGLREVEVTACLVWKDWPHRVHPHSLVGKDCTDGVCRVRLRPHVSPRHSFNNLGIQCVRKKEIEAAIERKIQLGIDPYNAGSLKNHQEVDMNVVRICFQASYRDQQGHLHRMDPILSEPVYDKKSTNTSELRICRINKESGPCTGGEELYLLCDKVQKEDISVVFSTASWEGRADFSQADVHRQIAIVFKTPPYEDLEISEPVTVNVFLQRLTDGVCSEPLPFTYLPRDHDSYGVDKKRKRGLPDVLGELSSSDPHGIESKRRKKKPVFLDHFLPGHSSGLFLPPSALQPADSDFFPASISLPGLEPPGGPDLLDDGFAYDPSAPTLFTMLDLLPPAPPLASAVVGSGGAGATVVESSGPEPLSLDSFAAPGPGDVGTASLVGSNMFPNQYREAAFGGGLLSPGPEAT

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
3	Phosphorylation	-----MPSRRAARES -----CCCHHHHHHH	32.85	-
19	Phosphorylation	PELGALGSSDLSSLS CCHHCCCCCCHHHCE	22.87	-
84	Phosphorylation	AAPPPPATPSWSCTL CCCCCCCCCCCEEEC	24.51	22817900
96	Phosphorylation	CTLGRLVSPGPCPRP EECCCEECCCCCCCC	28.82	26824392
139	Phosphorylation	GESSTEASKTLPAIE CCCCCCHHHCCCEEE	21.68	-
195	Phosphorylation	VRLRPHVSPRHSFNN EEECCCCCCCCCCCC	17.12	29176673
199	Phosphorylation	PHVSPRHSFNNLGIQ CCCCCCCCCCCCCCE	30.83	26370283
273	Ubiquitination	LSEPVYDKKSTNTSE CCCCCCCCCCCCCCE	30.82	-
274	Ubiquitination	SEPVYDKKSTNTSEL CCCCCCCCCCCCCEE	60.66	-
305	Ubiquitination	ELYLLCDKVQKEDIS HHEEEECCCCHHCCE	45.64	-
308	Ubiquitination	LLCDKVQKEDISVVF EEECCCCHHCCEEEE	61.41	-
368	Phosphorylation	RLTDGVCSEPLPFTY HCCCCCCCCCCCCCC	39.58	12874295
552	Phosphorylation	AFGGGLLSPGPEAT- HHCCCCCCCCCCCC-	32.62	27087446
558	Phosphorylation	LSPGPEAT------- CCCCCCCC-------	37.16	25619855

Upstream regulatory proteins (kinases for phosphorylation sites, E3 ubiquitin ligases of ubiquitination sites, ...)

Oops, there are no upstream regulatory protein records of RELB_MOUSE !!

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.	11781828
573	S	Phosphorylation	Phosphorylation at 'Thr-103' and 'Ser-573' is followed by proteasomal degradation.	11781828

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_MOUSE !!

Protein-Protein Interaction

Oops, there are no PPI records of RELB_MOUSE !!

Drug and Disease Associations

• Kegg Drug
• DrugBank
• There are no disease associations of PTM sites.

Related Literatures of Post-Translational Modification

Phosphorylation

"Signal-specific and phosphorylation-dependent RelB degradation: apotential mechanism of NF-kappaB control.";
Marienfeld R., Berberich-Siebelt F., Berberich I., Denk A.,Serfling E., Neumann M.;
Oncogene 20:8142-8147(2001).
Cited for: PHOSPHORYLATION AT THR-84 AND SER-552.
PubMed: 11781828