RPC2_YEAST - dbPTM
RPC2_YEAST - PTM Information in dbPTM
Basic Information of Protein
UniProt ID RPC2_YEAST
UniProt AC P22276
Protein Name DNA-directed RNA polymerase III subunit RPC2
Gene Name RET1
Organism Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
Sequence Length 1149
Subcellular Localization Nucleus .
Protein Description DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates. Second largest core component of RNA polymerase III which synthesizes small RNAs, such as 5S rRNA and tRNAs. Proposed to contribute to the polymerase catalytic activity and forms the polymerase active center together with the largest subunit. Pol III is composed of mobile elements and RPC2 is part of the core element with the central large cleft and probably a clamp element that moves to open and close the cleft (By similarity)..
Protein Sequence MVAATKRRKTHIHKHVKDEAFDDLLKPVYKGKKLTDEINTAQDKWHLLPAFLKVKGLVKQHLDSFNYFVDTDLKKIIKANQLILSDVDPEFYLKYVDIRVGKKSSSSTKDYLTPPHECRLRDMTYSAPIYVDIEYTRGRNIIMHKDVEIGRMPIMLRSNKCILYDADESKMAKLNECPLDPGGYFIVNGTEKVILVQEQLSKNRIIVEADEKKGIVQASVTSSTHERKSKTYVITKNGKIYLKHNSIAEEIPIAIVLKACGILSDLEIMQLVCGNDSSYQDIFAVNLEESSKLDIYTQQQALEYIGAKVKTMRRQKLTILQEGIEAIATTVIAHLTVEALDFREKALYIAMMTRRVVMAMYNPKMIDDRDYVGNKRLELAGQLISLLFEDLFKKFNNDFKLSIDKVLKKPNRAMEYDALLSINVHSNNITSGLNRAISTGNWSLKRFKMERAGVTHVLSRLSYISALGMMTRISSQFEKSRKVSGPRALQPSQFGMLCTADTPEGEACGLVKNLALMTHITTDDEEEPIKKLCYVLGVEDITLIDSASLHLNYGVYLNGTLIGSIRFPTKFVTQFRHLRRTGKVSEFISIYSNSHQMAVHIATDGGRICRPLIIVSDGQSRVKDIHLRKLLDGELDFDDFLKLGLVEYLDVNEENDSYIALYEKDIVPSMTHLEIEPFTILGAVAGLIPYPHHNQSPRNTYQCAMGKQAIGAIAYNQFKRIDTLLYLMTYPQQPMVKTKTIELIDYDKLPAGQNATVAVMSYSGYDIEDALVLNKSSIDRGFGRCETRRKTTTVLKRYANHTQDIIGGMRVDENGDPIWQHQSLGPDGLGEVGMKVQSGQIYINKSVPTNSADAPNPNNVNVQTQYREAPVIYRGPEPSHIDQVMMSVSDNDQALIKVLLRQNRRPELGDKFSSRHGQKGVCGIIVKQEDMPFNDQGIVPDIIMNPHGFPSRMTVGKMIELISGKAGVLNGTLEYGTCFGGSKLEDMSKILVDQGFNYSGKDMLYSGITGECLQAYIFFGPIYYQKLKHMVLDKMHARARGPRAVLTRQPTEGRSRDGGLRLGEMERDCVIAYGASQLLLERLMISSDAFEVDVCDKCGLMGYSGWCTTCKSAENIIKMTIPYAAKLLFQELLSMNIAPRLRLEDIFQQ
Overview of Protein Modification Sites with Functional and Structural Information
Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations Modification Substrate Peptides
&
Secondary Structure
ASA (%) Reference Orthologous
Protein Cluster
17AcetylationTHIHKHVKDEAFDDL
CCHHHHHCHHHHHHH
49.9624489116
32UbiquitinationLKPVYKGKKLTDEIN
HHHHHCCCCCHHHCC
40.2217644757
33UbiquitinationKPVYKGKKLTDEINT
HHHHCCCCCHHHCCH
66.3517644757
35PhosphorylationVYKGKKLTDEINTAQ
HHCCCCCHHHCCHHH
40.2322369663
40PhosphorylationKLTDEINTAQDKWHL
CCHHHCCHHHHHHHH
31.2122369663
44UbiquitinationEINTAQDKWHLLPAF
HCCHHHHHHHHHHHH
25.1617644757
53UbiquitinationHLLPAFLKVKGLVKQ
HHHHHHHHHHHHHHH
35.1317644757
74AcetylationYFVDTDLKKIIKANQ
EEECCCHHHHHHHHH
44.7424489116
78UbiquitinationTDLKKIIKANQLILS
CCHHHHHHHHHHHHC
44.7715699485
94UbiquitinationVDPEFYLKYVDIRVG
CCHHHHHEEEEEEEC
31.6715699485
103UbiquitinationVDIRVGKKSSSSTKD
EEEEECCCCCCCCCC
50.0317644757
109UbiquitinationKKSSSSTKDYLTPPH
CCCCCCCCCCCCCCH
46.4517644757
124PhosphorylationECRLRDMTYSAPIYV
HCCCCCCCCCCCEEE
20.7228889911
125PhosphorylationCRLRDMTYSAPIYVD
CCCCCCCCCCCEEEE
9.0128889911
130PhosphorylationMTYSAPIYVDIEYTR
CCCCCCEEEEEEEEC
7.3328889911
135PhosphorylationPIYVDIEYTRGRNII
CEEEEEEEECCCEEE
11.3228889911
136PhosphorylationIYVDIEYTRGRNIIM
EEEEEEEECCCEEEE
17.5428889911
173UbiquitinationADESKMAKLNECPLD
CCHHHCHHHCCCCCC
48.6317644757
192UbiquitinationFIVNGTEKVILVQEQ
EEECCCCEEEEEEEH
34.1217644757
202UbiquitinationLVQEQLSKNRIIVEA
EEEEHHHCCCEEEEE
59.8617644757
212UbiquitinationIIVEADEKKGIVQAS
EEEEECCCCCEEEEE
57.7717644757
213UbiquitinationIVEADEKKGIVQASV
EEEECCCCCEEEEEE
52.3917644757
219PhosphorylationKKGIVQASVTSSTHE
CCCEEEEEECCCCCC
14.6127017623
228UbiquitinationTSSTHERKSKTYVIT
CCCCCCCCCCEEEEE
54.0117644757
229PhosphorylationSSTHERKSKTYVITK
CCCCCCCCCEEEEEC
36.1328889911
231PhosphorylationTHERKSKTYVITKNG
CCCCCCCEEEEECCC
30.0628889911
232PhosphorylationHERKSKTYVITKNGK
CCCCCCEEEEECCCE
8.1325371407
235PhosphorylationKSKTYVITKNGKIYL
CCCEEEEECCCEEEE
14.3828889911
243UbiquitinationKNGKIYLKHNSIAEE
CCCEEEECCCCCCCC
24.6217644757
258UbiquitinationIPIAIVLKACGILSD
CCHHHHHHHCCCCCC
30.6417644757
405AcetylationDFKLSIDKVLKKPNR
CCCCCHHHHHCCCCC
48.0424489116
570AcetylationGSIRFPTKFVTQFRH
EEEECCHHHHHHHHH
37.7724489116
707UbiquitinationTYQCAMGKQAIGAIA
CCHHHHCHHHHHHHH
24.3815699485
719UbiquitinationAIAYNQFKRIDTLLY
HHHHHHHCCCCHHHH
38.3815699485
737UbiquitinationYPQQPMVKTKTIELI
CCCCCCCCCEEEEEE
37.7415699485
845UbiquitinationSGQIYINKSVPTNSA
CCCEEEECCCCCCCC
43.1815699485
879PhosphorylationIYRGPEPSHIDQVMM
EEECCCCHHCCEEEE
31.2627017623
887PhosphorylationHIDQVMMSVSDNDQA
HCCEEEECCCCCHHH
10.6027017623
889PhosphorylationDQVMMSVSDNDQALI
CEEEECCCCCHHHHH
24.3227017623
957UbiquitinationPSRMTVGKMIELISG
CCCCCHHHHHHHHHC
32.1622106047
965UbiquitinationMIELISGKAGVLNGT
HHHHHHCCCCCCCCE
34.8715699485
972PhosphorylationKAGVLNGTLEYGTCF
CCCCCCCEEEECCCC
18.4919779198
975PhosphorylationVLNGTLEYGTCFGGS
CCCCEEEECCCCCCC
22.3519779198
1126UbiquitinationMTIPYAAKLLFQELL
CHHHHHHHHHHHHHH
37.2417644757

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 RPC2_YEAST !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of RPC2_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 RPC2_YEAST !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
RPAB1_YEASTRPB5physical
16554755
RPC10_YEASTRPC11physical
16554755
RPAC2_YEASTRPC19physical
16554755
RPC6_YEASTRPC34physical
16554755
RPC1_YEASTRPO31physical
16554755
RPAB5_YEASTRPB10physical
16554755
RPAB3_YEASTRPB8physical
16554755
RPAC1_YEASTRPC40physical
16554755
RPAB2_YEASTRPO26physical
16554755
RPC3_YEASTRPC82physical
16554755
RPC9_YEASTRPC17physical
16429126
RPAC2_YEASTRPC19physical
16429126
RPC8_YEASTRPC25physical
16429126
RPC6_YEASTRPC34physical
16429126
RPC5_YEASTRPC37physical
16429126
RPC4_YEASTRPC53physical
16429126
RPAB1_YEASTRPB5physical
16429126
RPC7_YEASTRPC31physical
16429126
RPAC1_YEASTRPC40physical
16429126
RPC3_YEASTRPC82physical
16429126
RPAB2_YEASTRPO26physical
16429126
RPC1_YEASTRPO31physical
16429126
PSP1_YEASTPSP1genetic
17314980
HSL1_YEASTHSL1genetic
17314980
GET1_YEASTGET1genetic
17314980
IES1_YEASTIES1genetic
17314980
CSK21_YEASTCKA1genetic
17314980
RAD16_YEASTRAD16genetic
17314980
YRM1_YEASTYRM1genetic
17314980
MCK1_YEASTMCK1genetic
17314980
H2AZ_YEASTHTZ1genetic
17314980
CSM3_YEASTCSM3genetic
17314980
DEP1_YEASTDEP1genetic
17314980
SSB1_YEASTSSB1physical
19536198
RPC1_YEASTRPO31physical
21048197
RPAC1_YEASTRPC40physical
21048197
RPC9_YEASTRPC17physical
21048197
RPAB1_YEASTRPB5physical
21048197
RPAB2_YEASTRPO26physical
21048197
RPC8_YEASTRPC25physical
21048197
RPAB3_YEASTRPB8physical
21048197
RPC10_YEASTRPC11physical
21048197
RPAB5_YEASTRPB10physical
21048197
RPAC2_YEASTRPC19physical
21048197
RPAB4_YEASTRPC10physical
21048197
RPC7_YEASTRPC31physical
21048197
RPC6_YEASTRPC34physical
21048197
RPC5_YEASTRPC37physical
21048197
RPC4_YEASTRPC53physical
21048197
RPC3_YEASTRPC82physical
21048197
RPAB5_YEASTRPB10physical
20887893
RPAB1_YEASTRPB5physical
20887893
RPAB3_YEASTRPB8physical
20887893
RPAB4_YEASTRPC10physical
20887893
RPC10_YEASTRPC11physical
20887893
RPC9_YEASTRPC17physical
20887893
RPAC2_YEASTRPC19physical
20887893
RPC8_YEASTRPC25physical
20887893
RPC7_YEASTRPC31physical
20887893
RPC6_YEASTRPC34physical
20887893
RPC5_YEASTRPC37physical
20887893
RPAC1_YEASTRPC40physical
20887893
RPC4_YEASTRPC53physical
20887893
RPC3_YEASTRPC82physical
20887893
RPAB2_YEASTRPO26physical
20887893
RPC1_YEASTRPO31physical
20887893
RPC5_YEASTRPC37physical
21536656
RPC4_YEASTRPC53physical
21536656
MNN11_YEASTMNN11genetic
23891562
GET2_YEASTGET2genetic
23891562
FEN1_YEASTRAD27genetic
23891562
RBS1_YEASTRBS1genetic
25605335
ALF_YEASTFBA1genetic
25605335
FOB1_YEASTFOB1genetic
25605335
EIF3B_YEASTPRT1genetic
25605335
RPAB5_YEASTRPB10genetic
25605335
ALF_YEASTFBA1genetic
24576411
RPC1_YEASTRPO31physical
26423792
RPC3_YEASTRPC82physical
26423792
RPC4_YEASTRPC53physical
26423792
RPAC1_YEASTRPC40physical
26423792
RPC6_YEASTRPC34physical
26423792
RPC7_YEASTRPC31physical
26423792
RPAC2_YEASTRPC19physical
26423792

Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of RPC2_YEAST

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Related Literatures of Post-Translational Modification

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