CUL4B_MOUSE - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: CUL4B_MOUSE
• UniProt AC: A2A432
• Protein Name: Cullin-4B {ECO:0000312|EMBL:CAM17145.1}
• Gene Name: Cul4b {ECO:0000312|MGI:MGI:1919834}
• Organism: Mus musculus (Mouse).
• Sequence Length: 970
• Subcellular Localization: Nucleus .
• Protein Description: Core component of multiple cullin-RING-based E3 ubiquitin-protein ligase complexes which mediate the ubiquitination and subsequent proteasomal degradation of target proteins. The functional specificity of the E3 ubiquitin-protein ligase complex depends on the variable substrate recognition subunit. CUL4B may act within the complex as a scaffold protein, contributing to catalysis through positioning of the substrate and the ubiquitin-conjugating enzyme. Plays a role as part of the E3 ubiquitin-protein ligase complex in polyubiquitination of CDT1, histone H2A, histone H3 and histone H4 in response to radiation-induced DNA damage. Targeted to UV damaged chromatin by DDB2 and may be important for DNA repair and DNA replication. Required for ubiquitination of cyclin E, and consequently, normal G1 cell cycle progression. Regulates the mammalian target-of-rapamycin (mTOR) pathway involved in control of cell growth, size and metabolism. Specific CUL4B regulation of the mTORC1-mediated pathway is dependent upon 26S proteasome function and requires interaction between CUL4B and MLST8 (By similarity)..
• Protein Sequence: MSRSTRSKERRENDTDSEDNSSETSNQERRRCRQGPPRPPYPPLLPPVFPPPTPPPQVRRTRGLQDLGAMKSVCPGTSGFSSPNPSAASAAAQEVRSATDGNTSTTPPTSAKKRKLNSSSSSSNSSNEREDFDSTSSSSTPPQPRDSASPSTSSFCLGVPVATSSHVPIQKKLRFEDTLEFVGIDTKMAEESSSSSSSSSPTAATSQQQQQQQLKTKSILISSVASVHHANGLAKSSTAVSSFANSKPGSAKKLVIKNFKDKPKLPENYTDETWQKLKEAVEAIQNSTSIKYNLEELYQAVENLCSHKISANLYKQLRQICEDHIKAQIHQFREDSLDSVLFLKKIDRCWQNHCRQMIMIRSIFLFLDRTYVLQNSMLPSIWDMGLELFRAHIISDQKVQTKTIDGILLLIERERNGEAIDRSLLRSLLSMLSDLQIYQDSFEQQFLQETNRLYAAEGQKLMQEREVPEYLHHVNKRLEEEADRLITYLDQTTQKSLIASVEKQLLGEHLTAILQKGLNSLLDENRIQDLSLLYQLFSRVRGGVQVLLQQWIEYIKAFGSTIVINPEKDKTMVQELLDFKDKVDHIIDTCFLKNEKFINAMKEAFETFINKRPNKPAELIAKYVDSKLRAGNKEATDEELEKMLDKIMIIFRFIYGKDVFEAFYKKDLAKRLLVGKSASVDAEKSMLSKLKHECGAAFTSKLEGMFKDMELSKDIMIQFKQYMQNQNVPGNIELTVNILTMGYWPTYVPMEVHLPPEMVKLQEIFKTFYLGKHSGRKLQWQSTLGHCVLKAEFKEGKKELQVSLFQTMVLLMFNEGEEFSLEEIKHATGIEDGELRRTLQSLACGKARVLAKNPKGKDIEDGDKFICNDDFKHKLFRIKINQIQMKETVEEQASTTERVFQDRQYQIDAAIVRIMKMRKTLSHNLLVSEVYNQLKFPVKPADLKKRIESLIDRDYMERDKENPNQYNYIA

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
15	Phosphorylation	KERRENDTDSEDNSS HHHHCCCCCCCCCCC	53.67	26824392
17	Phosphorylation	RRENDTDSEDNSSET HHCCCCCCCCCCCCH	49.28	21149613
21	Phosphorylation	DTDSEDNSSETSNQE CCCCCCCCCCHHHHH	41.70	29550500
22	Phosphorylation	TDSEDNSSETSNQER CCCCCCCCCHHHHHH	51.66	29550500
53	Phosphorylation	PPVFPPPTPPPQVRR CCCCCCCCCCCCCCC	54.95	26643407
72	Phosphorylation	QDLGAMKSVCPGTSG HHHHCCCCCCCCCCC	18.83	25619855
77	Phosphorylation	MKSVCPGTSGFSSPN CCCCCCCCCCCCCCC	15.72	25619855
78	Phosphorylation	KSVCPGTSGFSSPNP CCCCCCCCCCCCCCH	43.70	25619855
81	Phosphorylation	CPGTSGFSSPNPSAA CCCCCCCCCCCHHHH	48.70	25619855
82	Phosphorylation	PGTSGFSSPNPSAAS CCCCCCCCCCHHHHH	26.83	25521595
86	Phosphorylation	GFSSPNPSAASAAAQ CCCCCCHHHHHHHHH	43.01	25619855
89	Phosphorylation	SPNPSAASAAAQEVR CCCHHHHHHHHHHHH	20.39	25619855
97	Phosphorylation	AAAQEVRSATDGNTS HHHHHHHHCCCCCCC	40.47	25619855
99	Phosphorylation	AQEVRSATDGNTSTT HHHHHHCCCCCCCCC	45.76	25619855
103	Phosphorylation	RSATDGNTSTTPPTS HHCCCCCCCCCCCCH	32.74	23984901
104	Phosphorylation	SATDGNTSTTPPTSA HCCCCCCCCCCCCHH	33.99	27087446
105	Phosphorylation	ATDGNTSTTPPTSAK CCCCCCCCCCCCHHH	41.08	25521595
106	Phosphorylation	TDGNTSTTPPTSAKK CCCCCCCCCCCHHHC	27.34	27087446
109	Phosphorylation	NTSTTPPTSAKKRKL CCCCCCCCHHHCCCC	42.38	21082442
110	Phosphorylation	TSTTPPTSAKKRKLN CCCCCCCHHHCCCCC	43.81	27149854
112	Acetylation	TTPPTSAKKRKLNSS CCCCCHHHCCCCCCC	53.53	156683
118	Phosphorylation	AKKRKLNSSSSSSNS HHCCCCCCCCCCCCC	41.87	25777480
119	Phosphorylation	KKRKLNSSSSSSNSS HCCCCCCCCCCCCCC	32.92	25777480
120	Phosphorylation	KRKLNSSSSSSNSSN CCCCCCCCCCCCCCC	33.78	25777480
121	Phosphorylation	RKLNSSSSSSNSSNE CCCCCCCCCCCCCCC	39.47	25777480
122	Phosphorylation	KLNSSSSSSNSSNER CCCCCCCCCCCCCCC	35.17	25777480
123	Phosphorylation	LNSSSSSSNSSNERE CCCCCCCCCCCCCCC	42.55	25777480
125	Phosphorylation	SSSSSSNSSNEREDF CCCCCCCCCCCCCCC	36.17	25777480
126	Phosphorylation	SSSSSNSSNEREDFD CCCCCCCCCCCCCCC	47.13	25777480
134	Phosphorylation	NEREDFDSTSSSSTP CCCCCCCCCCCCCCC	30.13	25619855
135	Phosphorylation	EREDFDSTSSSSTPP CCCCCCCCCCCCCCC	34.18	25619855
136	Phosphorylation	REDFDSTSSSSTPPQ CCCCCCCCCCCCCCC	31.98	25619855
137	Phosphorylation	EDFDSTSSSSTPPQP CCCCCCCCCCCCCCC	28.53	25619855
138	Phosphorylation	DFDSTSSSSTPPQPR CCCCCCCCCCCCCCC	37.69	25619855
139	Phosphorylation	FDSTSSSSTPPQPRD CCCCCCCCCCCCCCC	47.05	25619855
140	Phosphorylation	DSTSSSSTPPQPRDS CCCCCCCCCCCCCCC	40.72	27087446
147	Phosphorylation	TPPQPRDSASPSTSS CCCCCCCCCCCCCCC	31.74	24925903
149	Phosphorylation	PQPRDSASPSTSSFC CCCCCCCCCCCCCEE	24.28	25521595
151	Phosphorylation	PRDSASPSTSSFCLG CCCCCCCCCCCEECC	38.12	24925903
152	Phosphorylation	RDSASPSTSSFCLGV CCCCCCCCCCEECCC	31.60	28833060
153	Phosphorylation	DSASPSTSSFCLGVP CCCCCCCCCEECCCC	26.25	28833060
154	Phosphorylation	SASPSTSSFCLGVPV CCCCCCCCEECCCCE	21.77	25521595
163	Phosphorylation	CLGVPVATSSHVPIQ ECCCCEECCCCCCCC	30.88	28833060
164	Phosphorylation	LGVPVATSSHVPIQK CCCCEECCCCCCCCC	14.54	28833060
165	Phosphorylation	GVPVATSSHVPIQKK CCCEECCCCCCCCCC	24.93	28833060
192	Phosphorylation	DTKMAEESSSSSSSS CHHHCCCCCCCCCCC	27.33	25619855
193	Phosphorylation	TKMAEESSSSSSSSS HHHCCCCCCCCCCCC	37.20	25619855
194	Phosphorylation	KMAEESSSSSSSSSP HHCCCCCCCCCCCCC	43.44	25619855
195	Phosphorylation	MAEESSSSSSSSSPT HCCCCCCCCCCCCCC	35.87	25619855
196	Phosphorylation	AEESSSSSSSSSPTA CCCCCCCCCCCCCCH	35.87	27087446
197	Phosphorylation	EESSSSSSSSSPTAA CCCCCCCCCCCCCHH	35.87	27087446
198	Phosphorylation	ESSSSSSSSSPTAAT CCCCCCCCCCCCHHC	36.46	27087446
199	Phosphorylation	SSSSSSSSSPTAATS CCCCCCCCCCCHHCH	42.14	27087446
200	Phosphorylation	SSSSSSSSPTAATSQ CCCCCCCCCCHHCHH	28.37	27087446
202	Phosphorylation	SSSSSSPTAATSQQQ CCCCCCCCHHCHHHH	30.76	25521595
205	Phosphorylation	SSSPTAATSQQQQQQ CCCCCHHCHHHHHHH	25.30	25619855
206	Phosphorylation	SSPTAATSQQQQQQQ CCCCHHCHHHHHHHH	22.67	25619855
250	Phosphorylation	FANSKPGSAKKLVIK HCCCCCCCCCEEEEC	45.50	25619855
315	Ubiquitination	KISANLYKQLRQICE CCHHHHHHHHHHHHH	46.12	22790023
336	Phosphorylation	IHQFREDSLDSVLFL HHHHHHCCCHHHHHH	29.35	-
646	Acetylation	ELEKMLDKIMIIFRF HHHHHHHHHHHHHHH	30.16	30985589
657	Acetylation	IFRFIYGKDVFEAFY HHHHHHCHHHHHHHH	33.47	30985595
665	Ubiquitination	DVFEAFYKKDLAKRL HHHHHHHHHHHHHHH	33.10	-
676	Malonylation	AKRLLVGKSASVDAE HHHHHCCCCCCCHHH	35.06	26320211
676	Ubiquitination	AKRLLVGKSASVDAE HHHHHCCCCCCCHHH	35.06	-
691	Acetylation	KSMLSKLKHECGAAF HHHHHHHHHHHCHHH	40.88	-
694	S-nitrosocysteine	LSKLKHECGAAFTSK HHHHHHHHCHHHHHH	4.49	-
694	S-nitrosylation	LSKLKHECGAAFTSK HHHHHHHHCHHHHHH	4.49	20925432
707	Ubiquitination	SKLEGMFKDMELSKD HHHHHHHCCCHHCHH	47.47	-
846	Malonylation	LQSLACGKARVLAKN HHHHHHCCHHHHCCC	32.67	26320211
846	Ubiquitination	LQSLACGKARVLAKN HHHHHHCCHHHHCCC	32.67	-
916	Ubiquitination	AAIVRIMKMRKTLSH HHHHHHHHHHHHHCC	32.93	-
920	Phosphorylation	RIMKMRKTLSHNLLV HHHHHHHHHCCHHHH	24.11	29899451
949	Phosphorylation	DLKKRIESLIDRDYM HHHHHHHHHHCHHHH	28.40	28066266
960	Ubiquitination	RDYMERDKENPNQYN HHHHHHHCCCCCCCC	66.66	-

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

Oops, there are no upstream regulatory protein records of CUL4B_MOUSE !!

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of CUL4B_MOUSE !!

Disease-associated PTM Sites based on SAP

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

Oops, there are no SNP-PTM records of CUL4B_MOUSE !!

Protein-Protein Interaction

Oops, there are no PPI records of CUL4B_MOUSE !!

Drug and Disease Associations

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