dbPTM

UBX3_SCHPO - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	UBX3_SCHPO
UniProt AC	Q9UT81
Protein Name	UBX domain-containing protein 3
Gene Name	ubx3
Organism	Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
Sequence Length	410
Subcellular Localization
Protein Description	Involved in CDC48-dependent protein degradation through the ubiquitin/proteasome pathway. Involved in delivery of substrates to the 26S proteasome. Also required for membrane fusion and sporulation..
Protein Sequence	MDREDILKEFCNRNNIDVSQGRFFLESTNWNYELATALLHEVIPPEEDHGLQPSSDVSKVPEVTGSSSGISGGDQQPPRPLQRQQNTQGQGMKSGTASKKFATLRDLEGNDESAEEKSHLFTGGEKSGLSVEDGDPDPKKQLVRDILEKARQHTISPLDEQDSGPSSLASSWASVGQRLGTENEASGSTTPVTQSGPPRENPPTESQPEKPLRRTLYFWRNGFSVDDGPIYTYDDPANQEMLRYINSGRAPLHLLGVSMNQPIDVVVQHRMDEDYVAPFKPFSGKGQRLGSTYMQPRMSQMPGGLYTDTSTSSSVPINVKPNSTTPHASLQIDENKPTTRIQVRLSNGGRTVLTVNLSHTLHDIYEAVRAVSPGNFILSVPFPAKTLEDDPSVTVEAASLKNASLVQKSL

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
66	Phosphorylation	KVPEVTGSSSGISGG CCCCCCCCCCCCCCC	16.38	28889911
103	Phosphorylation	TASKKFATLRDLEGN CCCHHHEEHHHCCCC	26.01	21712547
113	Phosphorylation	DLEGNDESAEEKSHL HCCCCCCCHHHHHCE	43.79	24763107
118	Phosphorylation	DESAEEKSHLFTGGE CCCHHHHHCEECCCC	28.80	24763107
127	Phosphorylation	LFTGGEKSGLSVEDG EECCCCCCCCCCCCC	40.44	24763107
130	Phosphorylation	GGEKSGLSVEDGDPD CCCCCCCCCCCCCCC	27.30	25720772
154	Phosphorylation	LEKARQHTISPLDEQ HHHHHHCCCCCCCCC	18.14	29996109
156	Phosphorylation	KARQHTISPLDEQDS HHHHCCCCCCCCCCC	22.14	28889911
163	Phosphorylation	SPLDEQDSGPSSLAS CCCCCCCCCCCCHHH	52.91	29996109
167	Phosphorylation	EQDSGPSSLASSWAS CCCCCCCCHHHHHHH	30.96	28889911
171	Phosphorylation	GPSSLASSWASVGQR CCCCHHHHHHHHHHH	22.51	28889911
181	Phosphorylation	SVGQRLGTENEASGS HHHHHHCCCCCCCCC	39.98	29996109
186	Phosphorylation	LGTENEASGSTTPVT HCCCCCCCCCCCCCC	27.39	28889911
188	Phosphorylation	TENEASGSTTPVTQS CCCCCCCCCCCCCCC	26.98	28889911
189	Phosphorylation	ENEASGSTTPVTQSG CCCCCCCCCCCCCCC	38.35	25720772
190	Phosphorylation	NEASGSTTPVTQSGP CCCCCCCCCCCCCCC	19.91	28889911
193	Phosphorylation	SGSTTPVTQSGPPRE CCCCCCCCCCCCCCC	20.44	28889911
291	Phosphorylation	GKGQRLGSTYMQPRM CCCCCCCCCCCCCCH	22.43	25720772

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 UBX3_SCHPO !!

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of UBX3_SCHPO !!

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 UBX3_SCHPO !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
RPN10_SCHPO	rpn10	genetic	15120077
CDC48_SCHPO	cdc48	physical	15120077
ASSY_SCHPO	arg12	physical	23695164
ASSY_SCHPO	arg12	physical	26771498

Drug and Disease Associations

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

Regulatory Network of UBX3_SCHPO

Related Literatures of Post-Translational Modification

Phosphorylation
Reference	PubMed
"Phosphoproteome analysis of fission yeast."; Wilson-Grady J.T., Villen J., Gygi S.P.; J. Proteome Res. 7:1088-1097(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-156; SER-167; SER-186AND THR-190, AND MASS SPECTROMETRY.	18257517 [Abstract]