dbPTM

UBB_MOUSE - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	UBB_MOUSE
UniProt AC	P0CG49
Protein Name	Polyubiquitin-B
Gene Name	Ubb
Organism	Mus musculus (Mouse).
Sequence Length	305
Subcellular Localization	Cytoplasm. Nucleus.
Protein Description	Ubiquitin: Exists either covalently attached to another protein, or free (unanchored). When covalently bound, it is conjugated to target proteins via an isopeptide bond either as a monomer (monoubiquitin), a polymer linked via different Lys residues of the ubiquitin (polyubiquitin chains) or a linear polymer linked via the initiator Met of the ubiquitin (linear polyubiquitin chains). Polyubiquitin chains, when attached to a target protein, have different functions depending on the Lys residue of the ubiquitin that is linked: Lys-6-linked may be involved in DNA repair; Lys-11-linked is involved in ERAD (endoplasmic reticulum-associated degradation) and in cell-cycle regulation; Lys-29-linked is involved in lysosomal degradation; Lys-33-linked is involved in kinase modification; Lys-48-linked is involved in protein degradation via the proteasome; Lys-63-linked is involved in endocytosis, DNA-damage responses as well as in signaling processes leading to activation of the transcription factor NF-kappa-B. Linear polymer chains formed via attachment by the initiator Met lead to cell signaling. Ubiquitin is usually conjugated to Lys residues of target proteins, however, in rare cases, conjugation to Cys or Ser residues has been observed. When polyubiquitin is free (unanchored-polyubiquitin), it also has distinct roles, such as in activation of protein kinases, and in signaling..
Protein Sequence	MQIFVKTLTGKTITLEVEPSDTIENVKAKIQDKEGIPPDQQRLIFAGKQLEDGRTLSDYNIQKESTLHLVLRLRGGMQIFVKTLTGKTITLEVEPSDTIENVKAKIQDKEGIPPDQQRLIFAGKQLEDGRTLSDYNIQKESTLHLVLRLRGGMQIFVKTLTGKTITLEVEPSDTIENVKAKIQDKEGIPPDQQRLIFAGKQLEDGRTLSDYNIQKESTLHLVLRLRGGMQIFVKTLTGKTITLEVEPSDTIENVKAKIQDKEGIPPDQQRLIFAGKQLEDGRTLSDYNIQKESTLHLVLRLRGGY

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
6	Acetylation	--MQIFVKTLTGKTI --CEEEEEECCCCEE	27.37	-
6	Malonylation	--MQIFVKTLTGKTI --CEEEEEECCCCEE	27.37	26320211
6	Ubiquitination	--MQIFVKTLTGKTI --CEEEEEECCCCEE	27.37	-
7	Phosphorylation	-MQIFVKTLTGKTIT -CEEEEEECCCCEEE	25.01	27600695
9	Phosphorylation	QIFVKTLTGKTITLE EEEEEECCCCEEEEE	41.69	26643407
11	Acetylation	FVKTLTGKTITLEVE EEEECCCCEEEEEEC	31.36	23236377
11	Malonylation	FVKTLTGKTITLEVE EEEECCCCEEEEEEC	31.36	26320211
11	Ubiquitination	FVKTLTGKTITLEVE EEEECCCCEEEEEEC	31.36	-
12	Phosphorylation	VKTLTGKTITLEVEP EEECCCCEEEEEECC	22.12	27180971
14	Phosphorylation	TLTGKTITLEVEPSD ECCCCEEEEEECCCC	23.30	27742792
20	Phosphorylation	ITLEVEPSDTIENVK EEEEECCCCHHHHHH	33.60	26745281
22	Phosphorylation	LEVEPSDTIENVKAK EEECCCCHHHHHHHH	34.23	26745281
27	Acetylation	SDTIENVKAKIQDKE CCHHHHHHHHHCCCC	56.39	23806337
27	Succinylation	SDTIENVKAKIQDKE CCHHHHHHHHHCCCC	56.39	23806337
27	Ubiquitination	SDTIENVKAKIQDKE CCHHHHHHHHHCCCC	56.39	-
29	Ubiquitination	TIENVKAKIQDKEGI HHHHHHHHHCCCCCC	34.87	-
33	Acetylation	VKAKIQDKEGIPPDQ HHHHHCCCCCCCHHH	41.27	23806337
33	Ubiquitination	VKAKIQDKEGIPPDQ HHHHHCCCCCCCHHH	41.27	-
48	Acetylation	QRLIFAGKQLEDGRT HEEEEEEEECCCCCC	48.56	23864654
48	Malonylation	QRLIFAGKQLEDGRT HEEEEEEEECCCCCC	48.56	26320211
48	Succinylation	QRLIFAGKQLEDGRT HEEEEEEEECCCCCC	48.56	23806337
48	Ubiquitination	QRLIFAGKQLEDGRT HEEEEEEEECCCCCC	48.56	-
55	Phosphorylation	KQLEDGRTLSDYNIQ EECCCCCCCCCCCCC	35.82	24925903
57	Phosphorylation	LEDGRTLSDYNIQKE CCCCCCCCCCCCCCH	37.12	24925903
59	Phosphorylation	DGRTLSDYNIQKEST CCCCCCCCCCCCHHE	15.70	24925903
63	Acetylation	LSDYNIQKESTLHLV CCCCCCCCHHEEEEE	50.24	23236377
63	Malonylation	LSDYNIQKESTLHLV CCCCCCCCHHEEEEE	50.24	26320211
63	Ubiquitination	LSDYNIQKESTLHLV CCCCCCCCHHEEEEE	50.24	-
65	Phosphorylation	DYNIQKESTLHLVLR CCCCCCHHEEEEEEE	43.22	27742792
66	Phosphorylation	YNIQKESTLHLVLRL CCCCCHHEEEEEEEE	21.20	22324799
76	ADP-ribosylation	LVLRLRGGMQIFVKT EEEEECCCEEEEEEE	9.82	-
82	Acetylation	GGMQIFVKTLTGKTI CCEEEEEEECCCCEE	27.37	-
82	Malonylation	GGMQIFVKTLTGKTI CCEEEEEEECCCCEE	27.37	26320211
82	Ubiquitination	GGMQIFVKTLTGKTI CCEEEEEEECCCCEE	27.37	-
83	Phosphorylation	GMQIFVKTLTGKTIT CEEEEEEECCCCEEE	25.01	27600695
85	Phosphorylation	QIFVKTLTGKTITLE EEEEEECCCCEEEEE	41.69	26643407
87	Malonylation	FVKTLTGKTITLEVE EEEECCCCEEEEEEC	31.36	26320211
87	Ubiquitination	FVKTLTGKTITLEVE EEEECCCCEEEEEEC	31.36	-
88	Phosphorylation	VKTLTGKTITLEVEP EEECCCCEEEEEECC	22.12	27180971
90	Phosphorylation	TLTGKTITLEVEPSD ECCCCEEEEEECCCC	23.30	27742792
96	Phosphorylation	ITLEVEPSDTIENVK EEEEECCCCHHHHHH	33.60	26745281
98	Phosphorylation	LEVEPSDTIENVKAK EEECCCCHHHHHHHH	34.23	26745281
103	Ubiquitination	SDTIENVKAKIQDKE CCHHHHHHHHHCCCC	56.39	-
105	Ubiquitination	TIENVKAKIQDKEGI HHHHHHHHHCCCCCC	34.87	-
109	Acetylation	VKAKIQDKEGIPPDQ HHHHHCCCCCCCHHH	41.27	-
109	Ubiquitination	VKAKIQDKEGIPPDQ HHHHHCCCCCCCHHH	41.27	-
124	Acetylation	QRLIFAGKQLEDGRT HEEEEEEEECCCCCC	48.56	-
124	Malonylation	QRLIFAGKQLEDGRT HEEEEEEEECCCCCC	48.56	26320211
124	Ubiquitination	QRLIFAGKQLEDGRT HEEEEEEEECCCCCC	48.56	-
131	Phosphorylation	KQLEDGRTLSDYNIQ EECCCCCCCCCCCCC	35.82	24925903
133	Phosphorylation	LEDGRTLSDYNIQKE CCCCCCCCCCCCCCH	37.12	24925903
135	Phosphorylation	DGRTLSDYNIQKEST CCCCCCCCCCCCHHE	15.70	24925903
139	Acetylation	LSDYNIQKESTLHLV CCCCCCCCHHEEEEE	50.24	-
139	Malonylation	LSDYNIQKESTLHLV CCCCCCCCHHEEEEE	50.24	26320211
139	Ubiquitination	LSDYNIQKESTLHLV CCCCCCCCHHEEEEE	50.24	-
141	Phosphorylation	DYNIQKESTLHLVLR CCCCCCHHEEEEEEE	43.22	27742792
142	Phosphorylation	YNIQKESTLHLVLRL CCCCCHHEEEEEEEE	21.20	22324799
158	Acetylation	GGMQIFVKTLTGKTI CCEEEEEEECCCCEE	27.37	-
158	Malonylation	GGMQIFVKTLTGKTI CCEEEEEEECCCCEE	27.37	26320211
158	Ubiquitination	GGMQIFVKTLTGKTI CCEEEEEEECCCCEE	27.37	-
159	Phosphorylation	GMQIFVKTLTGKTIT CEEEEEEECCCCEEE	25.01	27600695
161	Phosphorylation	QIFVKTLTGKTITLE EEEEEECCCCEEEEE	41.69	26643407
163	Malonylation	FVKTLTGKTITLEVE EEEECCCCEEEEEEC	31.36	26320211
163	Ubiquitination	FVKTLTGKTITLEVE EEEECCCCEEEEEEC	31.36	-
164	Phosphorylation	VKTLTGKTITLEVEP EEECCCCEEEEEECC	22.12	27180971
166	Phosphorylation	TLTGKTITLEVEPSD ECCCCEEEEEECCCC	23.30	27742792
172	Phosphorylation	ITLEVEPSDTIENVK EEEEECCCCHHHHHH	33.60	26745281
174	Phosphorylation	LEVEPSDTIENVKAK EEECCCCHHHHHHHH	34.23	26745281
179	Ubiquitination	SDTIENVKAKIQDKE CCHHHHHHHHHCCCC	56.39	-
181	Ubiquitination	TIENVKAKIQDKEGI HHHHHHHHHCCCCCC	34.87	-
185	Acetylation	VKAKIQDKEGIPPDQ HHHHHCCCCCCCHHH	41.27	-
185	Ubiquitination	VKAKIQDKEGIPPDQ HHHHHCCCCCCCHHH	41.27	-
200	Acetylation	QRLIFAGKQLEDGRT HEEEEEEEECCCCCC	48.56	-
200	Malonylation	QRLIFAGKQLEDGRT HEEEEEEEECCCCCC	48.56	26320211
200	Ubiquitination	QRLIFAGKQLEDGRT HEEEEEEEECCCCCC	48.56	-
207	Phosphorylation	KQLEDGRTLSDYNIQ EECCCCCCCCCCCCC	35.82	24925903
209	Phosphorylation	LEDGRTLSDYNIQKE CCCCCCCCCCCCCCH	37.12	24925903
211	Phosphorylation	DGRTLSDYNIQKEST CCCCCCCCCCCCHHE	15.70	24925903
215	Acetylation	LSDYNIQKESTLHLV CCCCCCCCHHEEEEE	50.24	-
215	Malonylation	LSDYNIQKESTLHLV CCCCCCCCHHEEEEE	50.24	26320211
215	Ubiquitination	LSDYNIQKESTLHLV CCCCCCCCHHEEEEE	50.24	-
217	Phosphorylation	DYNIQKESTLHLVLR CCCCCCHHEEEEEEE	43.22	27742792
218	Phosphorylation	YNIQKESTLHLVLRL CCCCCHHEEEEEEEE	21.20	22324799
234	Acetylation	GGMQIFVKTLTGKTI CCEEEEEEECCCCEE	27.37	-
234	Malonylation	GGMQIFVKTLTGKTI CCEEEEEEECCCCEE	27.37	26320211
234	Ubiquitination	GGMQIFVKTLTGKTI CCEEEEEEECCCCEE	27.37	-
235	Phosphorylation	GMQIFVKTLTGKTIT CEEEEEEECCCCEEE	25.01	27600695
237	Phosphorylation	QIFVKTLTGKTITLE EEEEEECCCCEEEEE	41.69	26643407
239	Malonylation	FVKTLTGKTITLEVE EEEECCCCEEEEEEC	31.36	26320211
239	Ubiquitination	FVKTLTGKTITLEVE EEEECCCCEEEEEEC	31.36	-
240	Phosphorylation	VKTLTGKTITLEVEP EEECCCCEEEEEECC	22.12	27180971
242	Phosphorylation	TLTGKTITLEVEPSD ECCCCEEEEEECCCC	23.30	27742792
248	Phosphorylation	ITLEVEPSDTIENVK EEEEECCCCHHHHHH	33.60	26745281
250	Phosphorylation	LEVEPSDTIENVKAK EEECCCCHHHHHHHH	34.23	26745281
255	Ubiquitination	SDTIENVKAKIQDKE CCHHHHHHHHHCCCC	56.39	-
257	Ubiquitination	TIENVKAKIQDKEGI HHHHHHHHHCCCCCC	34.87	-
261	Acetylation	VKAKIQDKEGIPPDQ HHHHHCCCCCCCHHH	41.27	-
261	Ubiquitination	VKAKIQDKEGIPPDQ HHHHHCCCCCCCHHH	41.27	-
276	Acetylation	QRLIFAGKQLEDGRT HEEEEEEEECCCCCC	48.56	-
276	Malonylation	QRLIFAGKQLEDGRT HEEEEEEEECCCCCC	48.56	26320211
276	Ubiquitination	QRLIFAGKQLEDGRT HEEEEEEEECCCCCC	48.56	-
283	Phosphorylation	KQLEDGRTLSDYNIQ EECCCCCCCCCCCCC	35.82	24925903
285	Phosphorylation	LEDGRTLSDYNIQKE CCCCCCCCCCCCCCH	37.12	24925903
287	Phosphorylation	DGRTLSDYNIQKEST CCCCCCCCCCCCHHE	15.70	24925903
291	Acetylation	LSDYNIQKESTLHLV CCCCCCCCHHEEEHH	50.24	-
291	Malonylation	LSDYNIQKESTLHLV CCCCCCCCHHEEEHH	50.24	26320211
291	Ubiquitination	LSDYNIQKESTLHLV CCCCCCCCHHEEEHH	50.24	-
293	O-linked_Glycosylation	DYNIQKESTLHLVLR CCCCCCHHEEEHHHE	43.22	22645316
293	Phosphorylation	DYNIQKESTLHLVLR CCCCCCHHEEEHHHE	43.22	27180971
294	Phosphorylation	YNIQKESTLHLVLRL CCCCCHHEEEHHHEE	21.20	22324799

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
65	S	Phosphorylation	Kinase	PINK1	Q99MQ3	Uniprot

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Reference
65	S	Phosphorylation	-
[Ubiquitin]: Phosphorylated at Ser-65 by PINK1 during mitophagy.
65	S	ubiquitylation	-
[Ubiquitin]: Phosphorylated at Ser-65 by PINK1 during mitophagy.

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 UBB_MOUSE !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference	Domain-Domain Interactions
POLK_MOUSE	Polk	physical	18162470

Drug and Disease Associations

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

Regulatory Network of UBB_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-57, AND MASSSPECTROMETRY.	17242355 [Abstract]

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