UBIQP_DROME - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: UBIQP_DROME
• UniProt AC: P0CG69
• Protein Name: Polyubiquitin
• Gene Name: Ubi-p63E
• Organism: Drosophila melanogaster (Fruit fly).
• Sequence Length: 763
• Subcellular Localization: Ubiquitin: 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-48-linked is involved in protein degradation via the proteasome. 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 (By similarity)..
• Protein Sequence: MQIFVKTLTGKTITLEVEPSDTIENVKAKIQDKEGIPPDQQRLIFAGKQLEDGRTLSDYNIQKESTLHLVLRLRGGMQIFVKTLTGKTITLEVEPSDTIENVKAKIQDKEGIPPDQQRLIFAGKQLEDGRTLSDYNIQKESTLHLVLRLRGGMQIFVKTLTGKTITLEVEPSDTIENVKAKIQDKEGIPPDQQRLIFAGKQLEDGRTLSDYNIQKESTLHLVLRLRGGMQIFVKTLTGKTITLEVEPSDTIENVKAKIQDKEGIPPDQQRLIFAGKQLEDGRTLSDYNIQKESTLHLVLRLRGGMQIFVKTLTGKTITLEVEPSDTIENVKAKIQDKEGIPPDQQRLIFAGKQLEDGRTLSDYNIQKESTLHLVLRLRGGMQIFVKTLTGKTITLEVEPSDTIENVKAKIQDKEGIPPDQQRLIFAGKQLEDGRTLSDYNIQKESTLHLVLRLRGGMQIFVKTLTGKTITLEVEPSDTIENVKAKIQDKEGIPPDQQRLIFAGKQLEDGRTLSDYNIQKESTLHLVLRLRGGMQIFVKTLTGKTITLEVEPSDTIENVKAKIQDKEGIPPDQQRLIFAGKQLEDGRTLSDYNIQKESTLHLVLRLRGGMQIFVKTLTGKTITLEVEPSDTIENVKAKIQDKEGIPPDQQRLIFAGKQLEDGRTLSDYNIQKESTLHLVLRLRGGMQIFVKTLTGKTITLEVEPSDTIENVKAKIQDKEGIPPDQQRLIFAGKQLEDGRTLSDYNIQKESTLHLVLRLRGGIQA

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
6	Acetylation	--MQIFVKTLTGKTI --CEEEEEECCCCEE	27.37	21791702
22	Phosphorylation	LEVEPSDTIENVKAK EEECCCCCHHHHHHH	34.23	27794539
48	Acetylation	QRLIFAGKQLEDGRT HEEEEEECCCCCCCC	48.56	21791702
55	Phosphorylation	KQLEDGRTLSDYNIQ CCCCCCCCCCCCCCC	35.82	27794539
57	Phosphorylation	LEDGRTLSDYNIQKE CCCCCCCCCCCCCCH	37.12	22668510
65	Phosphorylation	DYNIQKESTLHLVLR CCCCCCHHEEEEEEE	43.22	19429919
66	Phosphorylation	YNIQKESTLHLVLRL CCCCCHHEEEEEEEE	21.20	19429919
98	Phosphorylation	LEVEPSDTIENVKAK EEECCCCCHHHHHHH	34.23	27794539
131	Phosphorylation	KQLEDGRTLSDYNIQ CCCCCCCCCCCCCCC	35.82	27794539
133	Phosphorylation	LEDGRTLSDYNIQKE CCCCCCCCCCCCCCH	37.12	22668510
141	Phosphorylation	DYNIQKESTLHLVLR CCCCCCHHEEEEEEE	43.22	19429919
142	Phosphorylation	YNIQKESTLHLVLRL CCCCCHHEEEEEEEE	21.20	19429919
174	Phosphorylation	LEVEPSDTIENVKAK EEECCCCCHHHHHHH	34.23	27794539
207	Phosphorylation	KQLEDGRTLSDYNIQ CCCCCCCCCCCCCCC	35.82	27794539
209	Phosphorylation	LEDGRTLSDYNIQKE CCCCCCCCCCCCCCH	37.12	22668510
217	Phosphorylation	DYNIQKESTLHLVLR CCCCCCHHEEEEEEE	43.22	19429919
218	Phosphorylation	YNIQKESTLHLVLRL CCCCCHHEEEEEEEE	21.20	19429919
250	Phosphorylation	LEVEPSDTIENVKAK EEECCCCCHHHHHHH	34.23	27794539
283	Phosphorylation	KQLEDGRTLSDYNIQ CCCCCCCCCCCCCCC	35.82	27794539
285	Phosphorylation	LEDGRTLSDYNIQKE CCCCCCCCCCCCCCH	37.12	22668510
293	Phosphorylation	DYNIQKESTLHLVLR CCCCCCHHEEEEEEE	43.22	19429919
294	Phosphorylation	YNIQKESTLHLVLRL CCCCCHHEEEEEEEE	21.20	19429919
326	Phosphorylation	LEVEPSDTIENVKAK EEECCCCCHHHHHHH	34.23	27794539
359	Phosphorylation	KQLEDGRTLSDYNIQ CCCCCCCCCCCCCCC	35.82	27794539
361	Phosphorylation	LEDGRTLSDYNIQKE CCCCCCCCCCCCCCH	37.12	22668510
369	Phosphorylation	DYNIQKESTLHLVLR CCCCCCHHEEEEEEE	43.22	19429919
370	Phosphorylation	YNIQKESTLHLVLRL CCCCCHHEEEEEEEE	21.20	19429919
402	Phosphorylation	LEVEPSDTIENVKAK EEECCCCCHHHHHHH	34.23	27794539
435	Phosphorylation	KQLEDGRTLSDYNIQ CCCCCCCCCCCCCCC	35.82	27794539
437	Phosphorylation	LEDGRTLSDYNIQKE CCCCCCCCCCCCCCH	37.12	22668510
445	Phosphorylation	DYNIQKESTLHLVLR CCCCCCHHEEEEEEE	43.22	19429919
446	Phosphorylation	YNIQKESTLHLVLRL CCCCCHHEEEEEEEE	21.20	19429919
478	Phosphorylation	LEVEPSDTIENVKAK EEECCCCCHHHHHHH	34.23	27794539
511	Phosphorylation	KQLEDGRTLSDYNIQ CCCCCCCCCCCCCCC	35.82	27794539
513	Phosphorylation	LEDGRTLSDYNIQKE CCCCCCCCCCCCCCH	37.12	22668510
521	Phosphorylation	DYNIQKESTLHLVLR CCCCCCHHEEEEEEE	43.22	19429919
522	Phosphorylation	YNIQKESTLHLVLRL CCCCCHHEEEEEEEE	21.20	19429919
554	Phosphorylation	LEVEPSDTIENVKAK EEECCCCCHHHHHHH	34.23	27794539
587	Phosphorylation	KQLEDGRTLSDYNIQ CCCCCCCCCCCCCCC	35.82	27794539
589	Phosphorylation	LEDGRTLSDYNIQKE CCCCCCCCCCCCCCH	37.12	22668510
597	Phosphorylation	DYNIQKESTLHLVLR CCCCCCHHEEEEEEE	43.22	19429919
598	Phosphorylation	YNIQKESTLHLVLRL CCCCCHHEEEEEEEE	21.20	19429919
630	Phosphorylation	LEVEPSDTIENVKAK EEECCCCCHHHHHHH	34.23	27794539
663	Phosphorylation	KQLEDGRTLSDYNIQ CCCCCCCCCCCCCCC	35.82	27794539
665	Phosphorylation	LEDGRTLSDYNIQKE CCCCCCCCCCCCCCH	37.12	22668510
673	Phosphorylation	DYNIQKESTLHLVLR CCCCCCHHEEEEEEE	43.22	19429919
674	Phosphorylation	YNIQKESTLHLVLRL CCCCCHHEEEEEEEE	21.20	19429919
706	Phosphorylation	LEVEPSDTIENVKAK EEECCCCCHHHHHHH	34.23	27794539
739	Phosphorylation	KQLEDGRTLSDYNIQ CCCCCCCCCCCCCCC	35.82	27794539
741	Phosphorylation	LEDGRTLSDYNIQKE CCCCCCCCCCCCCCH	37.12	22668510
749	Phosphorylation	DYNIQKESTLHLVLR CCCCCCHHHHHHHHH	43.22	19429919
750	Phosphorylation	YNIQKESTLHLVLRL CCCCCHHHHHHHHHH	21.20	19429919

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

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

Functions of PTM Sites

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

Disease-associated PTM Sites based on SAP

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

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

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
TTF2_DROME	lds	physical	14605208
GRIM_DROME	grim	physical	23940367

Drug and Disease Associations

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