RPAC1_HUMAN - dbPTM
RPAC1_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID RPAC1_HUMAN
UniProt AC O15160
Protein Name DNA-directed RNA polymerases I and III subunit RPAC1
Gene Name POLR1C
Organism Homo sapiens (Human).
Sequence Length 346
Subcellular Localization Nucleus .
Protein Description DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates. Common component of RNA polymerases I and III which synthesize ribosomal RNA precursors and small RNAs, such as 5S rRNA and tRNAs, respectively. RPAC1 is part of the Pol core element with the central large cleft and probably a clamp element that moves to open and close the cleft (By similarity)..
Protein Sequence MAASQAVEEMRSRVVLGEFGVRNVHTTDFPGNYSGYDDAWDQDRFEKNFRVDVVHMDENSLEFDMVGIDAAIANAFRRILLAEVPTMAVEKVLVYNNTSIVQDEILAHRLGLIPIHADPRLFEYRNQGDEEGTEIDTLQFRLQVRCTRNPHAAKDSSDPNELYVNHKVYTRHMTWIPLGNQADLFPEGTIRPVHDDILIAQLRPGQEIDLLMHCVKGIGKDHAKFSPVATASYRLLPDITLLEPVEGEAAEELSRCFSPGVIEVQEVQGKKVARVANPRLDTFSREIFRNEKLKKVVRLARVRDHYIFSVESTGVLPPDVLVSEAIKVLMGKCRRFLDELDAVQMD
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
2Acetylation------MAASQAVEE
------CCHHHHHHH		18.8022223895
4Phosphorylation----MAASQAVEEMR
----CCHHHHHHHHH		14.7723663014
33PhosphorylationTTDFPGNYSGYDDAW
CCCCCCCCCCCCCCC		14.9128796482
33 (in isoform 2)Phosphorylation-14.91-
34PhosphorylationTDFPGNYSGYDDAWD
CCCCCCCCCCCCCCC		34.5728796482
36PhosphorylationFPGNYSGYDDAWDQD
CCCCCCCCCCCCCHH		12.5228796482
47UbiquitinationWDQDRFEKNFRVDVV
CCHHHHHHCCCEEEE		59.6921906983
47 (in isoform 2)Ubiquitination-59.6921890473
47 (in isoform 1)Ubiquitination-59.6921890473
86PhosphorylationILLAEVPTMAVEKVL
HHHHCCCCEEEEEEE		23.9629396449
91UbiquitinationVPTMAVEKVLVYNNT
CCCEEEEEEEEECCC		33.98-
95PhosphorylationAVEKVLVYNNTSIVQ
EEEEEEEECCCHHHH		9.8728152594
98PhosphorylationKVLVYNNTSIVQDEI
EEEEECCCHHHHHHH		19.0528152594
99PhosphorylationVLVYNNTSIVQDEIL
EEEECCCHHHHHHHH		23.9228152594
120MethylationIPIHADPRLFEYRNQ
CCCCCCHHHHCCCCC		53.18115491513
124PhosphorylationADPRLFEYRNQGDEE
CCHHHHCCCCCCCCC		13.9222817900
125MethylationDPRLFEYRNQGDEEG
CHHHHCCCCCCCCCC		23.07115491507
154UbiquitinationTRNPHAAKDSSDPNE
CCCCCCCCCCCCCCC		59.9521906983
154 (in isoform 1)Ubiquitination-59.9521890473
154 (in isoform 2)Ubiquitination-59.9521890473
157PhosphorylationPHAAKDSSDPNELYV
CCCCCCCCCCCCEEE		68.1925159151
163PhosphorylationSSDPNELYVNHKVYT
CCCCCCEEECCEEEE		7.9428152594
167UbiquitinationNELYVNHKVYTRHMT
CCEEECCEEEECEEE		31.5621906983
167 (in isoform 2)Ubiquitination-31.5621890473
167AcetylationNELYVNHKVYTRHMT
CCEEECCEEEECEEE		31.5623236377
167 (in isoform 1)Ubiquitination-31.5621890473
169PhosphorylationLYVNHKVYTRHMTWI
EEECCEEEECEEEEE		11.6728152594
170PhosphorylationYVNHKVYTRHMTWIP
EECCEEEECEEEEEE		19.6528152594
220UbiquitinationHCVKGIGKDHAKFSP
HHHHCCCCCCCCCCC		44.4122817900
224 (in isoform 2)Ubiquitination-42.8521890473
224AcetylationGIGKDHAKFSPVATA
CCCCCCCCCCCCCCE		42.8526051181
224 (in isoform 1)Ubiquitination-42.8521890473
224UbiquitinationGIGKDHAKFSPVATA
CCCCCCCCCCCCCCE		42.8527667366
226PhosphorylationGKDHAKFSPVATASY
CCCCCCCCCCCCEEE		20.1220068231
226 (in isoform 2)Phosphorylation-20.12-
230PhosphorylationAKFSPVATASYRLLP
CCCCCCCCEEEEECC		19.1721406692
232PhosphorylationFSPVATASYRLLPDI
CCCCCCEEEEECCCC		13.3621406692
233PhosphorylationSPVATASYRLLPDIT
CCCCCEEEEECCCCE		11.6521406692
240PhosphorylationYRLLPDITLLEPVEG
EEECCCCEEEECCCC		32.4420068231
254 (in isoform 2)Phosphorylation-30.22-
254PhosphorylationGEAAEELSRCFSPGV
CHHHHHHHHHCCCCE		30.2220068231
258PhosphorylationEELSRCFSPGVIEVQ
HHHHHHCCCCEEEEE		25.1121815630
270UbiquitinationEVQEVQGKKVARVAN
EEEEECCEEEEEECC		27.3021963094
270AcetylationEVQEVQGKKVARVAN
EEEEECCEEEEEECC		27.3026051181
271UbiquitinationVQEVQGKKVARVANP
EEEECCEEEEEECCC		48.2022817900
282PhosphorylationVANPRLDTFSREIFR
ECCCCCCHHHHHHHC		28.2721815630
284PhosphorylationNPRLDTFSREIFRNE
CCCCCHHHHHHHCCH		30.9722817900
294UbiquitinationIFRNEKLKKVVRLAR
HHCCHHHHHHHHHHH		55.3724816145
332UbiquitinationAIKVLMGKCRRFLDE
HHHHHHHHHHHHHHH		15.5929967540
3322-HydroxyisobutyrylationAIKVLMGKCRRFLDE
HHHHHHHHHHHHHHH		15.59-
345SulfoxidationDELDAVQMD------
HHHHHHCCC------		5.4721406390
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 RPAC1_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of RPAC1_HUMAN !!
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 RPAC1_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
WRN_HUMANWRNphysical
11971179
RPA49_HUMANPOLR1Ephysical
9254723
RPC1_HUMANPOLR3Aphysical
22939629
RPC8_HUMANPOLR3Hphysical
22939629
RPC2_HUMANPOLR3Bphysical
22939629
RPC9_HUMANCRCPphysical
22939629
TSR1_HUMANTSR1physical
22939629
RPC3_HUMANPOLR3Cphysical
22939629
VIME_HUMANVIMphysical
21988832
TARA_HUMANTRIOBPphysical
21988832
RPB11_HUMANPOLR2Jphysical
21988832
BACD2_HUMANTNFAIP1physical
21988832
NMT1_HUMANNMT1physical
22863883
IKZF3_HUMANIKZF3physical
25416956
MBIP1_HUMANMBIPphysical
25416956
F208B_HUMANFAM208Bphysical
25416956
P2R3C_HUMANPPP2R3Cphysical
25416956
BIRC7_HUMANBIRC7physical
25416956
CCD33_HUMANCCDC33physical
25416956
T22D4_HUMANTSC22D4physical
25416956
ATRIP_HUMANATRIPphysical
25416956
LZTS2_HUMANLZTS2physical
25416956
RIM3A_HUMANRIMBP3physical
25416956
SAXO1_HUMANFAM154Aphysical
25416956
KCTD1_HUMANKCTD1physical
25416956
IHO1_HUMANCCDC36physical
25416956
ABCF2_HUMANABCF2physical
26344197
RPC9_HUMANCRCPphysical
26344197
DCA13_HUMANDCAF13physical
26344197
DDX47_HUMANDDX47physical
26344197
GAR1_HUMANGAR1physical
26344197
NOG1_HUMANGTPBP4physical
26344197
NMD3_HUMANNMD3physical
26344197
NOP9_HUMANNOP9physical
26344197
RPA1_HUMANPOLR1Aphysical
26344197
RPAB1_HUMANPOLR2Ephysical
26344197
RPAB3_HUMANPOLR2Hphysical
26344197
RPAB5_HUMANPOLR2Lphysical
26344197
RPC6_HUMANPOLR3Fphysical
26344197
RPC7_HUMANPOLR3Gphysical
26344197
RPC8_HUMANPOLR3Hphysical
26344197
RUVB1_HUMANRUVBL1physical
26344197
RPA43_HUMANTWISTNBphysical
26344197
WDR36_HUMANWDR36physical
26344197
RPC4_HUMANPOLR3Dphysical
28514442
RPC7_HUMANPOLR3Gphysical
28514442
RPC9_HUMANCRCPphysical
28514442
RPC6_HUMANPOLR3Fphysical
28514442
RPC5_HUMANPOLR3Ephysical
28514442
RPC3_HUMANPOLR3Cphysical
28514442
RPC8_HUMANPOLR3Hphysical
28514442
RPA34_HUMANCD3EAPphysical
28514442
RPA49_HUMANPOLR1Ephysical
28514442
RRN3_HUMANRRN3physical
28514442
RPC10_HUMANPOLR3Kphysical
28514442
RPC2_HUMANPOLR3Bphysical
28514442
RPC1_HUMANPOLR3Aphysical
28514442
RPA1_HUMANPOLR1Aphysical
28514442
RPB11_HUMANPOLR2Jphysical
28514442
RPA2_HUMANPOLR1Bphysical
28514442
TR61B_HUMANTRMT61Bphysical
28514442
RPAB5_HUMANPOLR2Lphysical
28514442
RPAP1_HUMANRPAP1physical
28514442
Drug and Disease Associations
Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
248390Treacher Collins syndrome 3 (TCS3)
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of RPAC1_HUMAN

loading...

Related Literatures of Post-Translational Modification
Acetylation
ReferencePubMed
"Lys-N and trypsin cover complementary parts of the phosphoproteome ina refined SCX-based approach.";
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,Mohammed S.;
Anal. Chem. 81:4493-4501(2009).
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, AND MASS SPECTROMETRY.
Phosphorylation
ReferencePubMed
"Immunoaffinity profiling of tyrosine phosphorylation in cancercells.";
Rush J., Moritz A., Lee K.A., Guo A., Goss V.L., Spek E.J., Zhang H.,Zha X.-M., Polakiewicz R.D., Comb M.J.;
Nat. Biotechnol. 23:94-101(2005).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-33, AND MASSSPECTROMETRY.

TOP
© 2024 Institute of Bioinformatics and Systems Biology, NYCU | Designed by : BiOmics Laboratory