dbPTM

RPA12_YEAST - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	RPA12_YEAST
UniProt AC	P32529
Protein Name	DNA-directed RNA polymerase I subunit RPA12
Gene Name	RPA12
Organism	Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
Sequence Length	125
Subcellular Localization	Nucleus, nucleolus .
Protein Description	DNA-dependent RNA polymerases catalyze the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates. Component of RNA polymerase I (Pol I) which synthesizes ribosomal RNA precursors. Besides, RNA polymerase I has intrinsic RNA cleavage activity. Proposed to contribute to the polymerase catalytic activity and form the polymerase active center together with the two largest subunits. Subunit RPA12 contributes a catalytic zinc ribbon that is required for RNA cleavage by Pol I. Involved in transcriptional termination..
Protein Sequence	MSVVGSLIFCLDCGDLLENPNAVLGSNVECSQCKAIYPKSQFSNLKVVTTTADDAFPSSLRAKKSVVKTSLKKNELKDGATIKEKCPQCGNEEMNYHTLQLRSADEGATVFYTCTSCGYKFRTNN

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
46	Acetylation	KSQFSNLKVVTTTAD HHHCCCCEEEEEECC	38.62	24489116
58	Phosphorylation	TADDAFPSSLRAKKS ECCCCCCHHHHHCHH	35.23	27017623
59	Phosphorylation	ADDAFPSSLRAKKSV CCCCCCHHHHHCHHH	23.32	21440633
103	Phosphorylation	YHTLQLRSADEGATV EEEEEEEECCCCCEE	48.98	21440633

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 RPA12_YEAST !!

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of RPA12_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 RPA12_YEAST !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
CDC14_YEAST	CDC14	physical	11805826
RPA2_YEAST	RPA135	physical	11805826
RPA1_YEAST	RPA190	physical	11805826
RPA43_YEAST	RPA43	physical	11805826
RPAB5_YEAST	RPB10	physical	11805826
RPAB1_YEAST	RPB5	physical	11805826
RPAB3_YEAST	RPB8	physical	11805826
RPAC1_YEAST	RPC40	physical	11805826
RPAB2_YEAST	RPO26	physical	11805826
RPA2_YEAST	RPA135	physical	11918799
RPA2_YEAST	RPA135	physical	10393904
GCN5_YEAST	GCN5	genetic	11779853
RPAB1_YEAST	RPB5	physical	16554755
RPA14_YEAST	RPA14	physical	16554755
RPAC2_YEAST	RPC19	physical	16554755
RPA49_YEAST	RPA49	physical	16554755
RPAB5_YEAST	RPB10	physical	16554755
RPA43_YEAST	RPA43	physical	16554755
RPA1_YEAST	RPA190	physical	16554755
RPA2_YEAST	RPA135	physical	16554755
RPAC1_YEAST	RPC40	physical	16554755
RPAB2_YEAST	RPO26	physical	16554755
CDC14_YEAST	CDC14	physical	16429126
RPA2_YEAST	RPA135	physical	16429126
RPA1_YEAST	RPA190	physical	16429126
RPA43_YEAST	RPA43	physical	16429126
RPAB5_YEAST	RPB10	physical	16429126
RPAB1_YEAST	RPB5	physical	16429126
RPAB3_YEAST	RPB8	physical	16429126
RPAC1_YEAST	RPC40	physical	16429126
RPAB2_YEAST	RPO26	physical	16429126
RPA14_YEAST	RPA14	genetic	18086878
RPA1_YEAST	RPA190	genetic	8417319
RPA1_YEAST	RPA190	physical	24153184
RPA2_YEAST	RPA135	physical	24153184
RPA34_YEAST	RPA34	physical	24153184
RPA49_YEAST	RPA49	physical	24153184
MSN4_YEAST	MSN4	physical	27637775
IKZF1_HUMAN	IKZF1	physical	27107014
GOGA2_HUMAN	GOLGA2	physical	27107014

Drug and Disease Associations

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

Regulatory Network of RPA12_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-59, AND MASSSPECTROMETRY.	18407956 [Abstract]