dbPTM

DRN1_YEAST - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	DRN1_YEAST
UniProt AC	P53255
Protein Name	CWF19-like protein DRN1
Gene Name	DRN1
Organism	Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
Sequence Length	507
Subcellular Localization	Nucleus. Cytoplasm. Relocalizes to the cytoplasm in response to hypoxia.
Protein Description	Involved in branched RNA metabolism, modulating the turnover of lariat-intron pre-mRNAs by the lariat-debranching enzyme DBR1. Enhances the debranching activity of DBR1 in vitro..
Protein Sequence	MTNAKILVAHISESDADEAIRKIKKVNEKSGPFDLIIIFSNSYDENFELNTDGLPQLILLSCDKANNSKSKKINENVTLLHNMGTYKLANGITLSYFIYPDDTLQGEKKSILDEFGKSEDQVDILLTKEWGLSISERCGRLSGSEVVDELAKKLQARYHFAFSDEINFYELEPFQWERERLSRFLNIPKYGSGKKWAYAFNMPIGDNELKDEPEPPNLIANPYNSVVTNSNKRPLETETENSFDGDKQVLANREKNENKKIRTILPSSCHFCFSNPNLEDHMIISIGKLVYLTTAKGPLSVPKGDMDISGHCLIIPIEHIPKLDPSKNAELTQSILAYEASLVKMNYIKFDMCTIVFEIQSERSIHFHKQVIPVPKYLVLKFCSALDRQVHFNNEKFTRNAKLEFQCYDSHSSKQYVDVINNQSNNYLQFTVYETPEADPKIYLATFNASETIDLQFGRRVLAFLLNLPRRVKWNSSTCLQTKQQETIEAEKFQKAYRTYDISLTEN

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
237	Phosphorylation	SNKRPLETETENSFD CCCCCCCCCCCCCCC	56.76	19779198
239	Phosphorylation	KRPLETETENSFDGD CCCCCCCCCCCCCCC	48.13	24603354
242	Phosphorylation	LETETENSFDGDKQV CCCCCCCCCCCCHHH	20.62	25521595
300	Phosphorylation	TTAKGPLSVPKGDMD EECCCCCCCCCCCCC	39.23	28889911
473	Acetylation	LNLPRRVKWNSSTCL HCCCCCCCCCCCHHC	38.55	25381059

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 DRN1_YEAST !!

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of DRN1_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 DRN1_YEAST !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
SRO9_YEAST	SRO9	genetic	19061648
NUP57_YEAST	NUP57	genetic	19061648
YL287_YEAST	YLR287C	genetic	19061648
AIR2_YEAST	AIR2	genetic	19061648
LHP1_YEAST	LHP1	genetic	19061648
NSI1_YEAST	NSI1	genetic	19061648
RKM2_YEAST	RKM2	genetic	19061648
NCL1_YEAST	NCL1	genetic	19061648
RU1A_YEAST	MUD1	genetic	19061648
SHE3_YEAST	SHE3	genetic	19061648
KA122_YEAST	KAP122	genetic	19061648
REXO1_YEAST	RNH70	genetic	19061648
CSK22_YEAST	CKA2	genetic	19061648
AIR1_YEAST	AIR1	genetic	19061648
YME2_YEAST	YME2	genetic	19061648
NAM8_YEAST	NAM8	genetic	19061648
LSM12_YEAST	LSM12	genetic	19061648
DBR1_YEAST	DBR1	physical	24919400
SYF1_YEAST	SYF1	physical	24919400
ACT_YEAST	ACT1	physical	24919400
RS17B_YEAST	RPS17B	physical	24919400
RLA3_YEAST	RPP1B	physical	24919400
MCM1_YEAST	MCM1	genetic	27708008
YRA2_YEAST	YRA2	genetic	27708008
FAD1_YEAST	FAD1	genetic	27708008
RPB1_YEAST	RPO21	genetic	27708008
SYF1_YEAST	SYF1	genetic	27708008
PRP43_YEAST	PRP43	genetic	27708008
DPOD2_YEAST	POL31	genetic	27708008
SMC4_YEAST	SMC4	genetic	27708008
SEC22_YEAST	SEC22	genetic	27708008
TAF4_YEAST	TAF4	genetic	27708008
CEF1_YEAST	CEF1	genetic	27708008
NIP7_YEAST	NIP7	genetic	27708008
DIM1_YEAST	DIM1	genetic	27708008
TF2B_YEAST	SUA7	genetic	27708008
BUD31_YEAST	BUD31	genetic	27708008
ELM1_YEAST	ELM1	genetic	27708008
SFL1_YEAST	SFL1	genetic	27708008
GGPPS_YEAST	BTS1	genetic	27708008
CCD57_HUMAN	CCDC57	physical	27107014

Drug and Disease Associations

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

Regulatory Network of DRN1_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-242, AND MASSSPECTROMETRY.	18407956 [Abstract]
"Proteome-wide identification of in vivo targets of DNA damagecheckpoint kinases."; Smolka M.B., Albuquerque C.P., Chen S.H., Zhou H.; Proc. Natl. Acad. Sci. U.S.A. 104:10364-10369(2007). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-242, AND MASSSPECTROMETRY.	17563356 [Abstract]