dbPTM

NTC20_YEAST - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	NTC20_YEAST
UniProt AC	P38302
Protein Name	Pre-mRNA-splicing factor NTC20
Gene Name	NTC20
Organism	Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
Sequence Length	140
Subcellular Localization	Nucleus .
Protein Description	Involved in pre-mRNA splicing. As a component of the NTC complex, associates to the spliceosome to mediate conformational rearrangement or to stabilize the structure of the spliceosome after U4 snRNA dissociation, which leads to spliceosome maturation..
Protein Sequence	MPSLRDLSLERDQELNQLRARINQLGKTGKEEANDFVGLNISNEPVYDTVIQTGQSSNATNSFVQETIQKTKQKESGQPYIIPQKNEHQRYIDKVCETSDLKAKLAPIMEVLEKKTNEKIKGIIRKRVLQEPDRDNDDSG

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference	Orthologous Protein Cluster
27	Acetylation	ARINQLGKTGKEEAN HHHHHHHHCCHHHHH	63.80	25381059
139	Phosphorylation	PDRDNDDSG------ CCCCCCCCC------	49.63	22369663

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 NTC20_YEAST !!

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of NTC20_YEAST !!

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 NTC20_YEAST !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
ISY1_YEAST	ISY1	physical	11842115
PRP19_YEAST	PRP19	physical	11842115
SN309_YEAST	SNT309	physical	11842115
SYF1_YEAST	SYF1	physical	11842115
SYF2_YEAST	SYF2	physical	11842115
CLF1_YEAST	CLF1	physical	11842115
ISY1_YEAST	ISY1	physical	10318896
PRP19_YEAST	PRP19	physical	10318896
SN309_YEAST	SNT309	physical	10318896
SYF1_YEAST	SYF1	physical	11102353
CLF1_YEAST	CLF1	physical	11102353
PRP19_YEAST	PRP19	physical	10092627
SYF1_YEAST	SYF1	genetic	11842115
ISY1_YEAST	ISY1	genetic	11018040
PRP19_YEAST	PRP19	physical	16554755
CLF1_YEAST	CLF1	physical	16554755
SYF1_YEAST	SYF1	physical	11283351
PRP19_YEAST	PRP19	genetic	19061648
ISY1_YEAST	ISY1	genetic	19061648
IST3_YEAST	IST3	genetic	19061648
MAK11_YEAST	MAK11	genetic	19061648
YM11_YEAST	EPO1	physical	18719252
SYF1_YEAST	SYF1	physical	18719252
CLF1_YEAST	CLF1	physical	18719252
DAL80_YEAST	DAL80	physical	18719252
SYF2_YEAST	SYF2	genetic	11842115
KPC1_YEAST	PKC1	genetic	27708008
UAP1_YEAST	QRI1	genetic	27708008
DBF4_YEAST	DBF4	genetic	27708008
SLU7_YEAST	SLU7	genetic	27708008
RIFK_YEAST	FMN1	genetic	27708008
SYF1_YEAST	SYF1	genetic	27708008
SMC1_YEAST	SMC1	genetic	27708008
STT3_YEAST	STT3	genetic	27708008
HSF_YEAST	HSF1	genetic	27708008
PRP18_YEAST	PRP18	genetic	27708008
PAN1_YEAST	PAN1	genetic	27708008
STS1_YEAST	STS1	genetic	27708008
ARP4_YEAST	ARP4	genetic	27708008
DPB11_YEAST	DPB11	genetic	27708008
KRE9_YEAST	KRE9	genetic	27708008
CWC16_YEAST	YJU2	genetic	27708008
MED14_YEAST	RGR1	genetic	27708008
CLF1_YEAST	CLF1	genetic	27708008
RSE1_YEAST	RSE1	genetic	27708008
MCM1_YEAST	MCM1	genetic	27708008
CEF1_YEAST	CEF1	genetic	27708008
PRP24_YEAST	PRP24	genetic	27708008
CAP_YEAST	SRV2	genetic	27708008
CH10_YEAST	HSP10	genetic	27708008
BUR1_YEAST	SGV1	genetic	27708008
MED10_YEAST	NUT2	genetic	27708008
PRCC_HUMAN	PRCC	physical	27107014
MAGAC_HUMAN	MAGEA12	physical	27107014

Drug and Disease Associations

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

Regulatory Network of NTC20_YEAST

Related Literatures of Post-Translational Modification

Phosphorylation
Reference	PubMed
"A multidimensional chromatography technology for in-depthphosphoproteome analysis."; Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.; Mol. Cell. Proteomics 7:1389-1396(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-139, AND MASSSPECTROMETRY.	18407956 [Abstract]