UBE3B_HUMAN - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: UBE3B_HUMAN
• UniProt AC: Q7Z3V4
• Protein Name: Ubiquitin-protein ligase E3B
• Gene Name: UBE3B
• Organism: Homo sapiens (Human).
• Sequence Length: 1068
• Protein Description: E3 ubiquitin-protein ligase which accepts ubiquitin from an E2 ubiquitin-conjugating enzyme in the form of a thioester and then directly transfers the ubiquitin to targeted substrates..
• Protein Sequence: MFTLSQTSRAWFIDRARQAREERLVQKERERAAVVIQAHVRSFLCRSRLQRDIRREIDDFFKADDPESTKRSALCIFKIARKLLFLFRIKEDNERFEKLCRSILSSMDAENEPKVWYVSLACSKDLTLLWIQQIKNILWYCCDFLKQLKPEILQDSRLITLYLTMLVTFTDTSTWKILRGKGESLRPAMNHICANIMGHLNQHGFYSVLQILLTRGLARPRPCLSKGTLTAAFSLALRPVIAAQFSDNLIRPFLIHIMSVPALVTHLSTVTPERLTVLESHDMLRKFIIFLRDQDRCRDVCESLEGCHTLCLMGNLLHLGSLSPRVLEEETDGFVSLLTQTLCYCRKYVSQKKSNLTHWHPVLGWFSQSVDYGLNESMHLITKQLQFLWGVPLIRIFFCDILSKKLLESQEPAHAQPASPQNVLPVKSLLKRAFQKSASVRNILRPVGGKRVDSAEVQKVCNICVLYQTSLTTLTQIRLQILTGLTYLDDLLPKLWAFICELGPHGGLKLFLECLNNDTEESKQLLAMLMLFCDCSRHLITILDDIEVYEEQISFKLEELVTISSFLNSFVFKMIWDGIVENAKGETLELFQSVHGWLMVLYERDCRRRFTPEDHWLRKDLKPSVLFQELDRDRKRAQLILQYIPHVIPHKNRVLLFRTMVTKEKEKLGLVETSSASPHVTHITIRRSRMLEDGYEQLRQLSQHAMKGVIRVKFVNDLGVDEAGIDQDGVFKEFLEEIIKRVFDPALNLFKTTSGDERLYPSPTSYIHENYLQLFEFVGKMLGKAVYEGIVVDVPFASFFLSQLLGHHHSVFYSSVDELPSLDSEFYKNLTSIKRYDGDITDLGLTLSYDEDVMGQLVCHELIPGGKTIPVTNENKISYIHLMAHFRMHTQIKNQTAALISGFRSIIKPEWIRMFSTPELQRLISGDNAEIDLEDLKKHTVYYGGFHGSHRVIIWLWDILASDFTPDERAMFLKFVTSCSRPPLLGFAYLKPPFSIRCVEVSDDQDTGDTLGSVLRGFFTIRKREPGGRLPTSSTCFNLLKLPNYSKKSVLREKLRYAISMNTGFELS

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
1	Acetylation	-------MFTLSQTS -------CCCCCCCC	27.85	22814378
42	Phosphorylation	VIQAHVRSFLCRSRL HHHHHHHHHHHHHHH	22.83	24719451
102	Phosphorylation	RFEKLCRSILSSMDA HHHHHHHHHHHCCCC	27.21	-
105	Phosphorylation	KLCRSILSSMDAENE HHHHHHHHCCCCCCC	23.19	29116813
106	Phosphorylation	LCRSILSSMDAENEP HHHHHHHCCCCCCCC	19.75	29116813
149	Ubiquitination	CDFLKQLKPEILQDS HHHHHHHCHHHHHCH	37.80	-
160	Phosphorylation	LQDSRLITLYLTMLV HHCHHHHHHHHHHHH	17.59	26356563
162	Phosphorylation	DSRLITLYLTMLVTF CHHHHHHHHHHHHHC	7.47	26356563
164	Phosphorylation	RLITLYLTMLVTFTD HHHHHHHHHHHHCCC	8.56	26356563
170	Phosphorylation	LTMLVTFTDTSTWKI HHHHHHCCCCCCHHH	29.06	26356563
184	Phosphorylation	ILRGKGESLRPAMNH HHCCCCCCHHHHHHH	38.04	22210691
206	Phosphorylation	HLNQHGFYSVLQILL HHHHCCHHHHHHHHH	11.49	22210691
321	Phosphorylation	GNLLHLGSLSPRVLE HHHHHHHCCCHHHHC	31.84	24719451
323	Phosphorylation	LLHLGSLSPRVLEEE HHHHHCCCHHHHCCC	16.62	24719451
409	Phosphorylation	LSKKLLESQEPAHAQ HHHHHHHCCCCCCCC	39.55	30108239
419	Phosphorylation	PAHAQPASPQNVLPV CCCCCCCCCCCCCCH	33.43	25159151
427	Ubiquitination	PQNVLPVKSLLKRAF CCCCCCHHHHHHHHH	33.18	-
428	Phosphorylation	QNVLPVKSLLKRAFQ CCCCCHHHHHHHHHH	38.89	24719451
436	Ubiquitination	LLKRAFQKSASVRNI HHHHHHHHCCCHHHH	41.35	-
450	Acetylation	ILRPVGGKRVDSAEV HHHCCCCCCCCHHHH	43.23	30593215
454	Phosphorylation	VGGKRVDSAEVQKVC CCCCCCCHHHHHHHH	24.38	30622161
554	Phosphorylation	EVYEEQISFKLEELV HHHHHHHCCCHHHHH	18.94	24719451
564	Phosphorylation	LEELVTISSFLNSFV HHHHHHHHHHHHHHH	12.98	25627689
565	Phosphorylation	EELVTISSFLNSFVF HHHHHHHHHHHHHHH	29.87	25627689
593	Phosphorylation	ETLELFQSVHGWLMV CHHHHHHHHHHHHHH	14.56	24972180
602	Phosphorylation	HGWLMVLYERDCRRR HHHHHHHHHHHHHHC	9.48	24972180
622	Ubiquitination	HWLRKDLKPSVLFQE CHHCCCCCHHHHHHH	45.43	-
643	Phosphorylation	RAQLILQYIPHVIPH HHHHHHHHCCCCCCC	16.99	-
673	Phosphorylation	EKLGLVETSSASPHV HHHCCEECCCCCCCC	22.09	29255136
674	Phosphorylation	KLGLVETSSASPHVT HHCCEECCCCCCCCE	15.48	29255136
675	Phosphorylation	LGLVETSSASPHVTH HCCEECCCCCCCCEE	39.94	29255136
677	Phosphorylation	LVETSSASPHVTHIT CEECCCCCCCCEEEE	19.93	29255136
681	Phosphorylation	SSASPHVTHITIRRS CCCCCCCEEEEEEHH	12.43	29255136
684	Phosphorylation	SPHVTHITIRRSRML CCCCEEEEEEHHHHH	10.79	25850435
695	Phosphorylation	SRMLEDGYEQLRQLS HHHHHHHHHHHHHHH	16.90	-
751	Ubiquitination	DPALNLFKTTSGDER CHHHHHHCCCCCCCC	54.80	21906983
751 (in isoform 1)	Ubiquitination	-	54.80	21906983
787	Phosphorylation	KMLGKAVYEGIVVDV HHHCHHHHCCCEEEC	17.19	-
901	Phosphorylation	NQTAALISGFRSIIK HHHHHHHHHHHHHCC	32.50	-
905	Phosphorylation	ALISGFRSIIKPEWI HHHHHHHHHCCHHHH	26.80	24719451
925	Phosphorylation	PELQRLISGDNAEID HHHHHHHCCCCCEEC	44.69	-
940	Phosphorylation	LEDLKKHTVYYGGFH HHHHHHCEEEECCCC	21.05	-
1020	Phosphorylation	SVLRGFFTIRKREPG HHHHHEEEEEECCCC	20.01	24719451

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

Oops, there are no upstream regulatory protein records of UBE3B_HUMAN !!

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of UBE3B_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 UBE3B_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
UBE3B_HUMAN	UBE3B	physical	28003368

Drug and Disease Associations

• Kegg Disease
• There are no disease associations of PTM sites.
• OMIM Disease
• 244450: Kaufman oculocerebrofacial syndrome (KOS)
• 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

"Kinase-selective enrichment enables quantitative phosphoproteomics ofthe kinome across the cell cycle.";
Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,Greff Z., Keri G., Stemmann O., Mann M.;
Mol. Cell 31:438-448(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-419, AND MASSSPECTROMETRY.
PubMed: 18691976