dbPTM

UBE4B_MOUSE - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	UBE4B_MOUSE
UniProt AC	Q9ES00
Protein Name	Ubiquitin conjugation factor E4 B {ECO:0000305}
Gene Name	Ube4b {ECO:0000312\|MGI:MGI:1927086}
Organism	Mus musculus (Mouse).
Sequence Length	1173
Subcellular Localization	Cytoplasm . Nucleus .
Protein Description	Ubiquitin-protein ligase that probably functions as an E3 ligase in conjunction with specific E1 and E2 ligases. May also function as an E4 ligase mediating the assembly of polyubiquitin chains on substrates ubiquitinated by another E3 ubiquitin ligase..
Protein Sequence	MEELSADEIRRRRLARLAGGQTSQPTTPLTSPQRENPPGPPIAASAPGPSQSLGLNVHNMTPATSPIGAAGVAHRSQSSEGVSSLSSSPSNSLETQSQSLSRSQSMDIDGVSCEKSMSQVDVDSGIENMEVDENDRREKRSLSDKEPSSGPEVSEEQALQLVCKIFRVSWKDRDRDVIFLSSLSAQFKQNPKEVFSDFKDLIGQILMEVLMMSTQTRDENPFASLTATSQPIATAARSPDRNLMLNTGSSSGTSPMFCNMGSFSTSSLSSLGASGGASNWDSYSDHFTIETCKETDMLNYLIECFDRVGIEEKKAPKMCSQPAVSQLLSNIRSQCISHTALVLQGSLTQPRSLQQPSFLVPYMLCRNLPYGFIQELVRTTHQDEEVFKQIFIPILQGLALAAKECSLESDYFKYPLMALGELCETKFGKTHPMCNLVASLPLWLPKSLSPGSGRELQRLSYLGAFFSFSVFAEDDAKVVEKYFSGPAITLENTRVVSQSLQHYLELGRQELFKILHSILLNGETREAALSYMAALVNANMKKAQMQADDRLVSTDGFMLNLLWVLQQLSTKIKLETVDPTYIFHPRCRITLPNDETRINATMEDVNERLTELYGDQPPFSEPKFPTECFFLTLHAHHLSILPSCRRYIRRLRAIRELNRTVEDLKNNESQWKDSPLATRHREMLKRCKTQLKKLVRCKACADAGLLDESFLRRCLNFYGLLIQLMLRILDPAYPDVTLPLNSEVPKVFAALPEFYVEDVAEFLFFIVQYSPQVLYEPCTQDIVMFLVVMLCNQNYIRNPYLVAKLVEVMFMTNPSVQPRTQKFFEMIENHPLSTKLLVPSLMKFYTDVEHTGATSEFYDKFTIRYHISTIFKSLWQNIAHHGTFMEEFNSGKQFVRYINMLINDTTFLLDESLESLKRIHEVQEEMKNKEQWDQLPRDQQQARQSQLAQDERVSRSYLALATETVDMFHLLTKQVQKPFLRPELGPRLAAMLNFNLQQLCGPKCRDLKVENPEKYGFEPKKLLDQLTDIYLQLDCARFAKAIADDQRSYSKELFEEVISKMRKAGIKSTIAIEKFKLLAEKVEEIVAKNARAEIDYSDAPDEFRDPLMDTLMTDPVRLPSGTVMDRSIILRHLLNSPTDPFNRQMLTESMLEPVPELKEQIQAWMREKQSSDH

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
1	Acetylation	-------MEELSADE -------CCCCCHHH	40.22	-
5	Phosphorylation	---MEELSADEIRRR ---CCCCCHHHHHHH	36.63	25338131
22	Phosphorylation	ARLAGGQTSQPTTPL HHHHCCCCCCCCCCC	32.38	25619855
23	Phosphorylation	RLAGGQTSQPTTPLT HHHCCCCCCCCCCCC	26.69	25293948
26	Phosphorylation	GGQTSQPTTPLTSPQ CCCCCCCCCCCCCCC	33.15	20469934
27	Phosphorylation	GQTSQPTTPLTSPQR CCCCCCCCCCCCCCC	24.00	21082442
30	Phosphorylation	SQPTTPLTSPQRENP CCCCCCCCCCCCCCC	39.29	28725479
31	Phosphorylation	QPTTPLTSPQRENPP CCCCCCCCCCCCCCC	27.07	25521595
45	Phosphorylation	PGPPIAASAPGPSQS CCCCCCCCCCCCCCC	26.44	25293948
50	Phosphorylation	AASAPGPSQSLGLNV CCCCCCCCCCCCCCC	38.01	25293948
52	Phosphorylation	SAPGPSQSLGLNVHN CCCCCCCCCCCCCCC	28.83	25293948
61	Phosphorylation	GLNVHNMTPATSPIG CCCCCCCCCCCCCCC	18.32	26643407
64	Phosphorylation	VHNMTPATSPIGAAG CCCCCCCCCCCCCCC	35.92	26643407
65	Phosphorylation	HNMTPATSPIGAAGV CCCCCCCCCCCCCCC	19.34	26643407
76	Phosphorylation	AAGVAHRSQSSEGVS CCCCCCCCCCCCCCC	25.25	24925903
78	Phosphorylation	GVAHRSQSSEGVSSL CCCCCCCCCCCCCCC	31.44	25521595
79	Phosphorylation	VAHRSQSSEGVSSLS CCCCCCCCCCCCCCC	30.63	25521595
83	Phosphorylation	SQSSEGVSSLSSSPS CCCCCCCCCCCCCCC	36.10	24925903
84	Phosphorylation	QSSEGVSSLSSSPSN CCCCCCCCCCCCCCC	29.84	25521595
86	Phosphorylation	SEGVSSLSSSPSNSL CCCCCCCCCCCCCCH	30.62	24925903
87	Phosphorylation	EGVSSLSSSPSNSLE CCCCCCCCCCCCCHH	52.11	24925903
88	Phosphorylation	GVSSLSSSPSNSLET CCCCCCCCCCCCHHH	29.04	25521595
90	Phosphorylation	SSLSSSPSNSLETQS CCCCCCCCCCHHHHH	40.78	24925903
92	Phosphorylation	LSSSPSNSLETQSQS CCCCCCCCHHHHHHH	31.74	24925903
95	Phosphorylation	SPSNSLETQSQSLSR CCCCCHHHHHHHCHH	38.52	25619855
97	Phosphorylation	SNSLETQSQSLSRSQ CCCHHHHHHHCHHHH	29.20	25619855
99	Phosphorylation	SLETQSQSLSRSQSM CHHHHHHHCHHHHCC	33.29	24925903
101	Phosphorylation	ETQSQSLSRSQSMDI HHHHHHCHHHHCCCC	34.82	25521595
103	Phosphorylation	QSQSLSRSQSMDIDG HHHHCHHHHCCCCCC	24.19	25521595
105	Phosphorylation	QSLSRSQSMDIDGVS HHCHHHHCCCCCCCC	21.48	24925903
106	Oxidation	SLSRSQSMDIDGVSC HCHHHHCCCCCCCCC	3.98	17242355
112	Phosphorylation	SMDIDGVSCEKSMSQ CCCCCCCCCCCCCCC	23.30	24759943
116	Phosphorylation	DGVSCEKSMSQVDVD CCCCCCCCCCCCCCC	11.02	25619855
118	Phosphorylation	VSCEKSMSQVDVDSG CCCCCCCCCCCCCCC	33.86	25619855
124	Phosphorylation	MSQVDVDSGIENMEV CCCCCCCCCCCCCCC	41.33	27742792
141	Phosphorylation	NDRREKRSLSDKEPS CCHHHHHCCCCCCCC	43.20	25293948
143	Phosphorylation	RREKRSLSDKEPSSG HHHHHCCCCCCCCCC	48.13	25293948
148	Phosphorylation	SLSDKEPSSGPEVSE CCCCCCCCCCCCCCH	49.36	25293948
149	Phosphorylation	LSDKEPSSGPEVSEE CCCCCCCCCCCCCHH	69.91	25293948
154	Phosphorylation	PSSGPEVSEEQALQL CCCCCCCCHHHHHHH	33.48	25293948
224	Phosphorylation	RDENPFASLTATSQP CCCCCCCCCEECCCC	26.99	25619855
226	Phosphorylation	ENPFASLTATSQPIA CCCCCCCEECCCCCC	25.95	25619855
228	Phosphorylation	PFASLTATSQPIATA CCCCCEECCCCCCCC	23.74	25619855
229	Phosphorylation	FASLTATSQPIATAA CCCCEECCCCCCCCC	31.34	25619855
234	Phosphorylation	ATSQPIATAARSPDR ECCCCCCCCCCCCCC	22.90	25521595
238	Phosphorylation	PIATAARSPDRNLML CCCCCCCCCCCCEEE	26.82	25521595
333	Phosphorylation	QLLSNIRSQCISHTA HHHHHHHHHHHHHHH	26.13	26745281
337	Phosphorylation	NIRSQCISHTALVLQ HHHHHHHHHHHHHHC	23.55	26745281
339	Phosphorylation	RSQCISHTALVLQGS HHHHHHHHHHHHCCC	18.20	26745281
426	Acetylation	LGELCETKFGKTHPM HHHHHHHHCCCCCCC	29.81	22826441
481	Ubiquitination	DDAKVVEKYFSGPAI CHHHHHHHHHCCCEE	39.73	-
665	Acetylation	NRTVEDLKNNESQWK HCHHHHHHCCHHHHC	70.78	23954790
665	Ubiquitination	NRTVEDLKNNESQWK HCHHHHHHCCHHHHC	70.78	-
669	Phosphorylation	EDLKNNESQWKDSPL HHHHCCHHHHCCCHH	43.39	20415495
672	Ubiquitination	KNNESQWKDSPLATR HCCHHHHCCCHHHHH	40.46	-
674	Phosphorylation	NESQWKDSPLATRHR CHHHHCCCHHHHHHH	20.34	25521595
678	Phosphorylation	WKDSPLATRHREMLK HCCCHHHHHHHHHHH	34.39	22817900
833	Phosphorylation	MIENHPLSTKLLVPS HHHCCCCCHHHHHHH	28.13	21183079
840	Phosphorylation	STKLLVPSLMKFYTD CHHHHHHHHHHHHCC	33.35	22817900
929	Ubiquitination	VQEEMKNKEQWDQLP HHHHHCCHHHHHHCC	45.85	-
1040	Ubiquitination	LDCARFAKAIADDQR HHHHHHHHHHHCCHH	37.30	-
1060	Ubiquitination	LFEEVISKMRKAGIK HHHHHHHHHHHCCCC	31.44	-
1074	Ubiquitination	KSTIAIEKFKLLAEK CHHHHHHHHHHHHHH	41.51	-
1136	Phosphorylation	ILRHLLNSPTDPFNR HHHHHHCCCCCHHHH	29.19	25521595
1138	Phosphorylation	RHLLNSPTDPFNRQM HHHHCCCCCHHHHHH	57.01	25521595
1149	Phosphorylation	NRQMLTESMLEPVPE HHHHHCHHHHCCCHH	24.35	25338131

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
Oops, there are no upstream regulatory protein records of UBE4B_MOUSE !!

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of UBE4B_MOUSE !!

Disease-associated PTM Sites based on SAP

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

Modified Location	Modification	Variant Position (Distance <= 10)	Residue Change	SAP	Related Disease	Reference
Oops, there are no SNP-PTM records of UBE4B_MOUSE !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
TERA_MOUSE	Vcp	physical	15189447
TERA_MOUSE	Vcp	physical	12504083
UBE4B_MOUSE	Ube4b	physical	11435423
TERA_MOUSE	Vcp	physical	22174917
UBE4B_MOUSE	Ube4b	physical	23509263
UB2D3_HUMAN	UBE2D3	physical	23509263
UBE2W_HUMAN	UBE2W	physical	23509263
UB2D3_HUMAN	UBE2D3	physical	11435423

Drug and Disease Associations

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

Regulatory Network of UBE4B_MOUSE

Related Literatures of Post-Translational Modification

Phosphorylation
Reference	PubMed
"Large-scale phosphorylation analysis of mouse liver."; Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.; Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-105, AND MASSSPECTROMETRY.	17242355 [Abstract]
"Phosphoproteomic analysis of the developing mouse brain."; Ballif B.A., Villen J., Beausoleil S.A., Schwartz D., Gygi S.P.; Mol. Cell. Proteomics 3:1093-1101(2004). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-31 AND SER-101, AND MASSSPECTROMETRY.	15345747 [Abstract]