dbPTM

RPA2_YEAST - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	RPA2_YEAST
UniProt AC	P22138
Protein Name	DNA-directed RNA polymerase I subunit RPA135
Gene Name	RPA135
Organism	Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
Sequence Length	1203
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. RPA190 and RPA135 both contribute to the polymerase catalytic activity and together form the Pol I active center. In addition, subunit RPA12 contributes a catalytic zinc ribbon that is required for RNA cleavage by Pol I. A single stranded DNA template strand of the promoter is positioned within the central active site cleft of Pol I. A bridging helix emanates from RPA190 and crosses the cleft near the catalytic site and is thought to promote translocation of Pol I by acting as a ratchet that moves the RNA-DNA hybrid through the active site by switching from straight to bent conformations at each step of nucleotide addition..
Protein Sequence	MSKVIKPPGQARTADFRTLERESRFINPPKDKSAFPLLQEAVQPHIGSFNALTEGPDGGLLNLGVKDIGEKVIFDGKPLNSEDEISNSGYLGNKLSVSVEQVSIAKPMSNDGVSSAVERKVYPSESRQRLTSYRGKLLLKLKWSVNNGEENLFEVRDCGGLPVMLQSNRCHLNKMSPYELVQHKEESDEIGGYFIVNGIEKLIRMLIVQRRNHPMAIIRPSFANRGASYSHYGIQIRSVRPDQTSQTNVLHYLNDGQVTFRFSWRKNEYLVPVVMILKALCHTSDREIFDGIIGNDVKDSFLTDRLELLLRGFKKRYPHLQNRTQVLQYLGDKFRVVFQASPDQSDLEVGQEVLDRIVLVHLGKDGSQDKFRMLLFMIRKLYSLVAGECSPDNPDATQHQEVLLGGFLYGMILKEKIDEYLQNIIAQVRMDINRGMAINFKDKRYMSRVLMRVNENIGSKMQYFLSTGNLVSQSGLDLQQVSGYTVVAEKINFYRFISHFRMVHRGSFFAQLKTTTVRKLLPESWGFLCPVHTPDGSPCGLLNHFAHKCRISTQQSDVSRIPSILYSLGVAPASHTFAAGPSLCCVQIDGKIIGWVSHEQGKIIADTLRYWKVEGKTPGLPIDLEIGYVPPSTRGQYPGLYLFGGHSRMLRPVRYLPLDKEDIVGPFEQVYMNIAVTPQEIQNNVHTHVEFTPTNILSILANLTPFSDFNQSPRNMYQCQMGKQTMGTPGVALCHRSDNKLYRLQTGQTPIVKANLYDDYGMDNFPNGFNAVVAVISYTGYDMDDAMIINKSADERGFGYGTMYKTEKVDLALNRNRGDPITQHFGFGNDEWPKEWLEKLDEDGLPYIGTYVEEGDPICAYFDDTLNKTKIKTYHSSEPAYIEEVNLIGDESNKFQELQTVSIKYRIRRTPQIGDKFSSRHGQKGVCSRKWPTIDMPFSETGIQPDIIINPHAFPSRMTIGMFVESLAGKAGALHGIAQDSTPWIFNEDDTPADYFGEQLAKAGYNYHGNEPMYSGATGEELRADIYVGVVYYQRLRHMVNDKFQVRSTGPVNSLTMQPVKGRKRHGGIRVGEMERDALIGHGTSFLLQDRLLNSSDYTQASVCRECGSILTTQQSVPRIGSISTVCCRRCSMRFEDAKKLLTKSEDGEKIFIDDSQIWEDGQGNKFVGGNETTTVAIPFVLKYLDSELSAMGIRLRYNVEPK

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
2	Acetylation	------MSKVIKPPG ------CCCCCCCCC	47.11	22814378
32	Ubiquitination	FINPPKDKSAFPLLQ CCCCCCCCCHHHHHH	50.22	17644757
66	Ubiquitination	GLLNLGVKDIGEKVI CCEECCCCCCCCEEE	41.66	17644757
71	Acetylation	GVKDIGEKVIFDGKP CCCCCCCEEEECCCC	35.10	24489116
71	Ubiquitination	GVKDIGEKVIFDGKP CCCCCCCEEEECCCC	35.10	17644757
77	Acetylation	EKVIFDGKPLNSEDE CEEEECCCCCCCCCC	48.45	24489116
77	Ubiquitination	EKVIFDGKPLNSEDE CEEEECCCCCCCCCC	48.45	17644757
81	Phosphorylation	FDGKPLNSEDEISNS ECCCCCCCCCCCCCC	54.85	22369663
86	Phosphorylation	LNSEDEISNSGYLGN CCCCCCCCCCCCCCC	23.93	22369663
88	Phosphorylation	SEDEISNSGYLGNKL CCCCCCCCCCCCCEE	23.25	22369663
90	Phosphorylation	DEISNSGYLGNKLSV CCCCCCCCCCCEEEE	15.97	22369663
94	Ubiquitination	NSGYLGNKLSVSVEQ CCCCCCCEEEEEEEE	40.10	17644757
106	Ubiquitination	VEQVSIAKPMSNDGV EEEEEECCCCCCCCC	39.31	15699485
109	Phosphorylation	VSIAKPMSNDGVSSA EEECCCCCCCCCCHH	40.05	19823750
114	Phosphorylation	PMSNDGVSSAVERKV CCCCCCCCHHHHCCC	20.36	21551504
115	Phosphorylation	MSNDGVSSAVERKVY CCCCCCCHHHHCCCC	33.65	19823750
120	Ubiquitination	VSSAVERKVYPSESR CCHHHHCCCCCCHHH	32.39	15699485
140	Ubiquitination	YRGKLLLKLKWSVNN HCCEEEEEEEEEECC	48.25	17644757
142	Acetylation	GKLLLKLKWSVNNGE CEEEEEEEEEECCCC	35.52	24489116
142	Ubiquitination	GKLLLKLKWSVNNGE CEEEEEEEEEECCCC	35.52	17644757
266	Ubiquitination	TFRFSWRKNEYLVPV EEEEEECCCCCHHHH	48.12	17644757
278	Ubiquitination	VPVVMILKALCHTSD HHHHHHHHHHHCCCC	28.52	17644757
333	Acetylation	VLQYLGDKFRVVFQA HHHHHHHHEEEEEEC	33.02	24489116
333	Ubiquitination	VLQYLGDKFRVVFQA HHHHHHHHEEEEEEC	33.02	17644757
364	Ubiquitination	IVLVHLGKDGSQDKF EEEEEECCCCCHHHH	66.34	17644757
370	Ubiquitination	GKDGSQDKFRMLLFM CCCCCHHHHHHHHHH	27.51	17644757
414	Ubiquitination	FLYGMILKEKIDEYL HHHHHHHHHHHHHHH	46.14	17644757
416	Ubiquitination	YGMILKEKIDEYLQN HHHHHHHHHHHHHHH	54.60	17644757
513	Methylation	GSFFAQLKTTTVRKL CCHHHHCCHHHHHHH	31.57	20137074
556	Phosphorylation	CRISTQQSDVSRIPS CCCCCCCCCHHHCCH	30.11	28889911
559	Phosphorylation	STQQSDVSRIPSILY CCCCCCHHHCCHHHH	29.50	28889911
591	Ubiquitination	CCVQIDGKIIGWVSH EEEEECCEEEEEEEH	27.66	17644757
602	Ubiquitination	WVSHEQGKIIADTLR EEEHHCCCEEEEHHH	30.54	17644757
612	Ubiquitination	ADTLRYWKVEGKTPG EEHHHHEEECCCCCC	22.83	15699485
616	Ubiquitination	RYWKVEGKTPGLPID HHEEECCCCCCCCEE	37.73	23749301
723	Ubiquitination	MYQCQMGKQTMGTPG CCCCCCCCCCCCCCC	36.93	23749301
740	Ubiquitination	LCHRSDNKLYRLQTG EEECCCCCEEEECCC	52.46	23749301
742	Phosphorylation	HRSDNKLYRLQTGQT ECCCCCEEEECCCCC	15.75	21440633
746	Phosphorylation	NKLYRLQTGQTPIVK CCEEEECCCCCCEEE	35.53	21440633
749	Phosphorylation	YRLQTGQTPIVKANL EEECCCCCCEEECCC	19.14	22369663
805	Acetylation	FGYGTMYKTEKVDLA CCCCCCCCCCEEEHH	39.11	24489116
805	Ubiquitination	FGYGTMYKTEKVDLA CCCCCCCCCCEEEHH	39.11	17644757
808	Ubiquitination	GTMYKTEKVDLALNR CCCCCCCEEEHHCCC	46.40	17644757
872	Ubiquitination	TLNKTKIKTYHSSEP CCCCCEEEEEECCCC	44.58	17644757
873	Phosphorylation	LNKTKIKTYHSSEPA CCCCEEEEEECCCCC	29.91	22369663
874	Phosphorylation	NKTKIKTYHSSEPAY CCCEEEEEECCCCCE	8.49	22369663
876	Phosphorylation	TKIKTYHSSEPAYIE CEEEEEECCCCCEEE	26.44	22369663
877	Phosphorylation	KIKTYHSSEPAYIEE EEEEEECCCCCEEEE	34.00	22369663
881	Phosphorylation	YHSSEPAYIEEVNLI EECCCCCEEEEEEEC	21.41	22369663
892	Phosphorylation	VNLIGDESNKFQELQ EEECCCCCCCCCCCC	50.49	22369663
894	Ubiquitination	LIGDESNKFQELQTV ECCCCCCCCCCCCEE	58.67	17644757
902	Phosphorylation	FQELQTVSIKYRIRR CCCCCEEEEEEEECC	19.42	27214570
904	Ubiquitination	ELQTVSIKYRIRRTP CCCEEEEEEEECCCC	22.44	17644757
916	Ubiquitination	RTPQIGDKFSSRHGQ CCCCCCHHHHHCCCC	41.77	17644757
916	Acetylation	RTPQIGDKFSSRHGQ CCCCCCHHHHHCCCC	41.77	24489116
930	Ubiquitination	QKGVCSRKWPTIDMP CCCCCCCCCCCCCCC	41.03	17644757
970	Ubiquitination	FVESLAGKAGALHGI HHHHHCHHHCHHHCC	37.73	17644757
1002	Ubiquitination	YFGEQLAKAGYNYHG HHHHHHHHCCCCCCC	51.44	17644757
1043	Ubiquitination	LRHMVNDKFQVRSTG HHHHHCCCCEEECCC	32.28	17644757
1061	Ubiquitination	SLTMQPVKGRKRHGG CEEEEECCCCCCCCC	60.73	23749301
1064	Ubiquitination	MQPVKGRKRHGGIRV EEECCCCCCCCCEEC	58.37	22817900
1084	Phosphorylation	DALIGHGTSFLLQDR HCCCCCCHHHHHHHH	15.61	30377154
1085	Phosphorylation	ALIGHGTSFLLQDRL CCCCCCHHHHHHHHH	20.63	23749301
1116	Phosphorylation	SILTTQQSVPRIGSI CEEEECCCCCCCCCH	25.03	28889911
1122	Phosphorylation	QSVPRIGSISTVCCR CCCCCCCCHHHHHHC	15.82	30377154
1144	Ubiquitination	DAKKLLTKSEDGEKI HHHHHHHCCCCCCEE	52.39	23749301
1150	Ubiquitination	TKSEDGEKIFIDDSQ HCCCCCCEEEECHHH	48.74	17644757
1156	Phosphorylation	EKIFIDDSQIWEDGQ CEEEECHHHHEECCC	21.59	28152593
1166	Ubiquitination	WEDGQGNKFVGGNET EECCCCCCCCCCCCC	48.53	17644757
1183	Ubiquitination	VAIPFVLKYLDSELS EEHHHHHHHHCHHHH	38.17	17644757

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 RPA2_YEAST !!

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of RPA2_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 RPA2_YEAST !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
SIR2_YEAST	SIR2	physical	12923057
RPA1_YEAST	RPA190	physical	15477604
RPA49_YEAST	RPA49	physical	15477604
RPA43_YEAST	RPA43	physical	15477604
RPA1_YEAST	RPA190	physical	11511359
NET1_YEAST	NET1	physical	11511359
RPAB4_YEAST	RPC10	physical	10393904
RPAB5_YEAST	RPB10	physical	10393904
RPAB1_YEAST	RPB5	physical	16554755
RPAC1_YEAST	RPC40	physical	16554755
RPAB2_YEAST	RPO26	physical	16554755
GFA1_YEAST	GFA1	physical	16429126
MET10_YEAST	MET10	physical	16429126
RPAC2_YEAST	RPC19	physical	16429126
TBB_YEAST	TUB2	physical	16429126
PYR1_YEAST	URA2	physical	16429126
EI2BE_YEAST	GCD6	physical	16429126
RPA1_YEAST	RPA190	physical	16429126
RPAB1_YEAST	RPB5	physical	16429126
RPAB3_YEAST	RPB8	physical	16429126
RPAC1_YEAST	RPC40	physical	16429126
KPYK1_YEAST	CDC19	physical	16429126
SYEC_YEAST	GUS1	physical	16429126
RPA12_YEAST	RPA12	physical	16908835
SPT4_YEAST	SPT4	physical	16908835
SPT5_YEAST	SPT5	physical	16908835
RRN3_YEAST	RRN3	physical	16908835
RPA49_YEAST	RPA49	genetic	18086878
HSP72_YEAST	SSA2	physical	19536198
SSB1_YEAST	SSB1	physical	19536198
RRN3_YEAST	RRN3	genetic	17466624
HSP72_YEAST	SSA2	physical	22940862
SSB1_YEAST	SSB1	physical	22940862
RPA1_YEAST	RPA190	physical	22940862
DED1_YEAST	DED1	physical	22940862
RPA2_YEAST	RPA135	physical	22940862
RPAC1_YEAST	RPC40	physical	22940862
RPAB1_YEAST	RPB5	physical	22940862
RPA49_YEAST	RPA49	physical	22940862
RPA43_YEAST	RPA43	physical	22940862
RS6A_YEAST	RPS6B	physical	22940862
RS6B_YEAST	RPS6B	physical	22940862
HSP71_YEAST	SSA1	physical	22940862
HMO1_YEAST	HMO1	physical	23209026
RPA2_YEAST	RPA135	physical	23209026
NOP56_YEAST	NOP56	physical	23209026
NOP58_YEAST	NOP58	physical	23209026
RPA1_YEAST	RPA190	physical	23209026
NOP6_YEAST	NOP6	physical	23209026
RPA43_YEAST	RPA43	physical	23209026
NOP10_YEAST	NOP10	physical	23209026
RPAC2_YEAST	RPC19	physical	23209026
RPA34_YEAST	RPA34	physical	23209026
RPAC1_YEAST	RPC40	physical	23209026
SNU13_YEAST	SNU13	physical	23209026
RPA49_YEAST	RPA49	physical	23209026
RPA12_YEAST	RPA12	physical	23209026
FKBP3_YEAST	FPR3	physical	23209026
CBF5_YEAST	CBF5	physical	23209026
PWP1_YEAST	PWP1	physical	23209026
NHP2_YEAST	NHP2	physical	23209026
FBRL_YEAST	NOP1	physical	23209026
PRP43_YEAST	PRP43	physical	23209026
BFR2_YEAST	BFR2	physical	23209026
NHP6A_YEAST	NHP6A	physical	23209026
NHP6B_YEAST	NHP6B	physical	23209026
ERB1_YEAST	ERB1	physical	23209026
MAK21_YEAST	MAK21	physical	23209026
DBP3_YEAST	DBP3	physical	23209026
PESC_YEAST	NOP7	physical	23209026
BRX1_YEAST	BRX1	physical	23209026
NOL10_YEAST	ENP2	physical	23209026
NSR1_YEAST	NSR1	physical	23209026
NIP7_YEAST	NIP7	physical	23209026
MRD1_YEAST	MRD1	physical	23209026
UTP14_YEAST	UTP14	physical	23209026
EBP2_YEAST	EBP2	physical	23209026
NOC3_YEAST	NOC3	physical	23209026
DRS1_YEAST	DRS1	physical	23209026
NOP2_YEAST	NOP2	physical	23209026
HAS1_YEAST	HAS1	physical	23209026
NAT10_YEAST	KRE33	physical	23209026
RRP5_YEAST	RRP5	physical	23209026
KRI1_YEAST	KRI1	physical	23209026
IF6_YEAST	TIF6	physical	23209026
TRM61_YEAST	GCD14	physical	23209026
RL18A_YEAST	RPL18A	physical	23209026
RL18B_YEAST	RPL18A	physical	23209026
RL15A_YEAST	RPL15A	physical	23209026
RL15B_YEAST	RPL15B	physical	23209026
RDH54_YEAST	RDH54	physical	23209026
NOP14_YEAST	NOP14	physical	23209026
FKBP4_YEAST	FPR4	physical	23209026
NOP4_YEAST	NOP4	physical	23209026
SAS10_YEAST	SAS10	physical	23209026
RRS1_YEAST	RRS1	physical	23209026
PMP1_YEAST	PMP1	physical	26404137

Drug and Disease Associations

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

Regulatory Network of RPA2_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-81; SER-1085 ANDSER-1116, AND MASS SPECTROMETRY.	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-81 AND SER-88, AND MASSSPECTROMETRY.	17563356 [Abstract]