UBB_RAT - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: UBB_RAT
• UniProt AC: P0CG51
• Protein Name: Polyubiquitin-B
• Gene Name: Ubb
• Organism: Rattus norvegicus (Rat).
• 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

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
7	Phosphorylation	-MQIFVKTLTGKTIT -CEEEEEECCCCEEE	25.01	25575281
9	Phosphorylation	QIFVKTLTGKTITLE EEEEEECCCCEEEEE	41.69	25575281
11	Acetylation	FVKTLTGKTITLEVE EEEECCCCEEEEEEC	31.36	22902405
12	Phosphorylation	VKTLTGKTITLEVEP EEECCCCEEEEEECC	22.12	22673903
14	Phosphorylation	TLTGKTITLEVEPSD ECCCCEEEEEECCCC	23.30	23984901
20	Phosphorylation	ITLEVEPSDTIENVK EEEEECCCCHHHHHH	33.60	22673903
22	Phosphorylation	LEVEPSDTIENVKAK EEECCCCHHHHHHHH	34.23	25575281
27	Acetylation	SDTIENVKAKIQDKE CCHHHHHHHHHCCCC	56.39	22902405
33	Succinylation	VKAKIQDKEGIPPDQ HHHHHCCCCCCCHHH	41.27	26843850
33	Acetylation	VKAKIQDKEGIPPDQ HHHHHCCCCCCCHHH	41.27	22902405
48	Ubiquitination	QRLIFAGKQLEDGRT HEEEEEEEECCCCCC	48.56	-
48	Acetylation	QRLIFAGKQLEDGRT HEEEEEEEECCCCCC	48.56	22902405
55	Phosphorylation	KQLEDGRTLSDYNIQ EECCCCCCCCCCCCC	35.82	27097102
57	Phosphorylation	LEDGRTLSDYNIQKE CCCCCCCCCCCCCCH	37.12	29779826
59	Phosphorylation	DGRTLSDYNIQKEST CCCCCCCCCCCCHHE	15.70	27097102
63	Acetylation	LSDYNIQKESTLHLV CCCCCCCCHHEEEEE	50.24	22902405
65	Phosphorylation	DYNIQKESTLHLVLR CCCCCCHHEEEEEEE	43.22	28432305
66	Phosphorylation	YNIQKESTLHLVLRL CCCCCHHEEEEEEEE	21.20	28432305
76	ADP-ribosylation	LVLRLRGGMQIFVKT EEEEECCCEEEEEEE	9.82	-
83	Phosphorylation	GMQIFVKTLTGKTIT CEEEEEEECCCCEEE	25.01	25575281
85	Phosphorylation	QIFVKTLTGKTITLE EEEEEECCCCEEEEE	41.69	25575281
87	Acetylation	FVKTLTGKTITLEVE EEEECCCCEEEEEEC	31.36	-
88	Phosphorylation	VKTLTGKTITLEVEP EEECCCCEEEEEECC	22.12	22673903
90	Phosphorylation	TLTGKTITLEVEPSD ECCCCEEEEEECCCC	23.30	23984901
96	Phosphorylation	ITLEVEPSDTIENVK EEEEECCCCHHHHHH	33.60	22673903
98	Phosphorylation	LEVEPSDTIENVKAK EEECCCCHHHHHHHH	34.23	25575281
103	Acetylation	SDTIENVKAKIQDKE CCHHHHHHHHHCCCC	56.39	-
109	Acetylation	VKAKIQDKEGIPPDQ HHHHHCCCCCCCHHH	41.27	-
109	Succinylation	VKAKIQDKEGIPPDQ HHHHHCCCCCCCHHH	41.27	26843850
124	Acetylation	QRLIFAGKQLEDGRT HEEEEEEEECCCCCC	48.56	-
131	Phosphorylation	KQLEDGRTLSDYNIQ EECCCCCCCCCCCCC	35.82	27097102
133	Phosphorylation	LEDGRTLSDYNIQKE CCCCCCCCCCCCCCH	37.12	29779826
135	Phosphorylation	DGRTLSDYNIQKEST CCCCCCCCCCCCHHE	15.70	27097102
139	Acetylation	LSDYNIQKESTLHLV CCCCCCCCHHEEEEE	50.24	-
141	Phosphorylation	DYNIQKESTLHLVLR CCCCCCHHEEEEEEE	43.22	28432305
142	Phosphorylation	YNIQKESTLHLVLRL CCCCCHHEEEEEEEE	21.20	28432305
159	Phosphorylation	GMQIFVKTLTGKTIT CEEEEEEECCCCEEE	25.01	25575281
161	Phosphorylation	QIFVKTLTGKTITLE EEEEEECCCCEEEEE	41.69	25575281
163	Acetylation	FVKTLTGKTITLEVE EEEECCCCEEEEEEC	31.36	-
164	Phosphorylation	VKTLTGKTITLEVEP EEECCCCEEEEEECC	22.12	22673903
166	Phosphorylation	TLTGKTITLEVEPSD ECCCCEEEEEECCCC	23.30	23984901
172	Phosphorylation	ITLEVEPSDTIENVK EEEEECCCCHHHHHH	33.60	22673903
174	Phosphorylation	LEVEPSDTIENVKAK EEECCCCHHHHHHHH	34.23	25575281
179	Acetylation	SDTIENVKAKIQDKE CCHHHHHHHHHCCCC	56.39	-
185	Succinylation	VKAKIQDKEGIPPDQ HHHHHCCCCCCCHHH	41.27	26843850
185	Acetylation	VKAKIQDKEGIPPDQ HHHHHCCCCCCCHHH	41.27	-
200	Acetylation	QRLIFAGKQLEDGRT HEEEEEEEECCCCCC	48.56	-
207	Phosphorylation	KQLEDGRTLSDYNIQ EECCCCCCCCCCCCC	35.82	27097102
209	Phosphorylation	LEDGRTLSDYNIQKE CCCCCCCCCCCCCCH	37.12	29779826
211	Phosphorylation	DGRTLSDYNIQKEST CCCCCCCCCCCCHHE	15.70	27097102
215	Acetylation	LSDYNIQKESTLHLV CCCCCCCCHHEEEEE	50.24	-
217	Phosphorylation	DYNIQKESTLHLVLR CCCCCCHHEEEEEEE	43.22	28432305
218	Phosphorylation	YNIQKESTLHLVLRL CCCCCHHEEEEEEEE	21.20	28432305
235	Phosphorylation	GMQIFVKTLTGKTIT CEEEEEEECCCCEEE	25.01	25575281
237	Phosphorylation	QIFVKTLTGKTITLE EEEEEECCCCEEEEE	41.69	25575281
239	Acetylation	FVKTLTGKTITLEVE EEEECCCCEEEEEEC	31.36	-
240	Phosphorylation	VKTLTGKTITLEVEP EEECCCCEEEEEECC	22.12	22673903
242	Phosphorylation	TLTGKTITLEVEPSD ECCCCEEEEEECCCC	23.30	23984901
248	Phosphorylation	ITLEVEPSDTIENVK EEEEECCCCHHHHHH	33.60	22673903
250	Phosphorylation	LEVEPSDTIENVKAK EEECCCCHHHHHHHH	34.23	25575281
255	Acetylation	SDTIENVKAKIQDKE CCHHHHHHHHHCCCC	56.39	-
261	Acetylation	VKAKIQDKEGIPPDQ HHHHHCCCCCCCHHH	41.27	-
261	Succinylation	VKAKIQDKEGIPPDQ HHHHHCCCCCCCHHH	41.27	26843850
276	Acetylation	QRLIFAGKQLEDGRT HEEEEEEEECCCCCC	48.56	-
283	Phosphorylation	KQLEDGRTLSDYNIQ EECCCCCCCCCCCCC	35.82	27097102
285	Phosphorylation	LEDGRTLSDYNIQKE CCCCCCCCCCCCCCH	37.12	29779826
287	Phosphorylation	DGRTLSDYNIQKEST CCCCCCCCCCCCHHE	15.70	27097102
291	Acetylation	LSDYNIQKESTLHLV CCCCCCCCHHEEEHH	50.24	-
293	Phosphorylation	DYNIQKESTLHLVLR CCCCCCHHEEEHHHE	43.22	28432305
294	Phosphorylation	YNIQKESTLHLVLRL CCCCCHHEEEHHHEE	21.20	28432305

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	B5DFG1	Uniprot

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	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.

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

Protein-Protein Interaction

Oops, there are no PPI records of UBB_RAT !!

Drug and Disease Associations

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