RPB7_HUMAN - dbPTM
RPB7_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID RPB7_HUMAN
UniProt AC P62487
Protein Name DNA-directed RNA polymerase II subunit RPB7
Gene Name POLR2G
Organism Homo sapiens (Human).
Sequence Length 172
Subcellular Localization Nucleus .
Protein Description DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates. Component of RNA polymerase II which synthesizes mRNA precursors and many functional non-coding RNAs. Pol II is the central component of the basal RNA polymerase II transcription machinery. It is composed of mobile elements that move relative to each other. RPB7 is part of a subcomplex with RPB4 that binds to a pocket formed by RPB1, RPB2 and RPB6 at the base of the clamp element. The RBP4-RPB7 subcomplex seems to lock the clamp via RPB7 in the closed conformation thus preventing double-stranded DNA to enter the active site cleft. The RPB4-RPB7 subcomplex binds single-stranded DNA and RNA (By similarity). Binds RNA..
Protein Sequence MFYHISLEHEILLHPRYFGPNLLNTVKQKLFTEVEGTCTGKYGFVIAVTTIDNIGAGVIQPGRGFVLYPVKYKAIVFRPFKGEVVDAVVTQVNKVGLFTEIGPMSCFISRHSIPSEMEFDPNSNPPCYKTMDEDIVIQQDDEIRLKIVGTRVDKNDIFAIGSLMDDYLGLVS
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
3Phosphorylation-----MFYHISLEHE
-----CCEEEEEEEE
9.2824719451
6Phosphorylation--MFYHISLEHEILL
--CCEEEEEEEEEEC
17.8824719451
17PhosphorylationEILLHPRYFGPNLLN
EEECCHHHCCHHHHH
19.8328152594
27UbiquitinationPNLLNTVKQKLFTEV
HHHHHHHHHHHCCEE
39.4121906983
29UbiquitinationLLNTVKQKLFTEVEG
HHHHHHHHHCCEECC
39.5922817900
29AcetylationLLNTVKQKLFTEVEG
HHHHHHHHHCCEECC
39.5925953088
71UbiquitinationGFVLYPVKYKAIVFR
CEEEEEECEEEEEEE
36.2121906983
73UbiquitinationVLYPVKYKAIVFRPF
EEEEECEEEEEEECC
26.3922817900
81UbiquitinationAIVFRPFKGEVVDAV
EEEEECCCCCEEEEE
57.7723000965
81AcetylationAIVFRPFKGEVVDAV
EEEEECCCCCEEEEE
57.7726051181
129UbiquitinationNSNPPCYKTMDEDIV
CCCCCCCCCCCCCEE
44.0521963094
131SulfoxidationNPPCYKTMDEDIVIQ
CCCCCCCCCCCEEEE
4.6721406390
146UbiquitinationQDDEIRLKIVGTRVD
CCCEEEEEEEEEECC
26.0421906983
1462-HydroxyisobutyrylationQDDEIRLKIVGTRVD
CCCEEEEEEEEEECC
26.04-
154UbiquitinationIVGTRVDKNDIFAIG
EEEEECCHHCEEEEH
54.3722817900

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
-KUbiquitinationE3 ubiquitin ligaseVHLP40337
PMID:12912922

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of RPB7_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 RPB7_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
RPB3_HUMANPOLR2Cphysical
9201987
RPAB1_HUMANPOLR2Ephysical
9201987
RPAB2_HUMANPOLR2Fphysical
9201987
RPB7_HUMANPOLR2Gphysical
9201987
RPAB3_HUMANPOLR2Hphysical
9201987
MCAF1_MOUSEAtf7ipphysical
10777215
PRKRA_HUMANPRKRAphysical
21988832
TNNC1_HUMANTNNC1physical
21988832
ESR1_HUMANESR1physical
16957778
SRC_HUMANSRCphysical
16957778
PSB9_HUMANPSMB9physical
16957778
ELOA1_HUMANTCEB3physical
16957778
RPAP2_HUMANRPAP2physical
26186194
RPB1_HUMANPOLR2Aphysical
26186194
RPB4_HUMANPOLR2Dphysical
26186194
RPR1A_HUMANRPRD1Aphysical
26186194
SFR19_HUMANSCAF1physical
26186194
RPRD2_HUMANRPRD2physical
26186194
RECQ5_HUMANRECQL5physical
26186194
RPB2_HUMANPOLR2Bphysical
26186194
GPN1_HUMANGPN1physical
26186194
RPB11_HUMANPOLR2Jphysical
26186194
RPB9_HUMANPOLR2Iphysical
26186194
MED17_HUMANMED17physical
26186194
RPAB5_HUMANPOLR2Lphysical
26186194
RPAB2_HUMANPOLR2Fphysical
26186194
MED26_HUMANMED26physical
26186194
CTDP1_HUMANCTDP1physical
26186194
MED30_HUMANMED30physical
26186194
RPB1_HUMANPOLR2Aphysical
26344197
RPAB5_HUMANPOLR2Lphysical
26344197
IPP2_HUMANPPP1R2physical
26344197
CX6B1_HUMANCOX6B1physical
26496610
TF2B_HUMANGTF2Bphysical
26496610
T2FA_HUMANGTF2F1physical
26496610
T2FB_HUMANGTF2F2physical
26496610
NASP_HUMANNASPphysical
26496610
RPB1_HUMANPOLR2Aphysical
26496610
RPB2_HUMANPOLR2Bphysical
26496610
RPB3_HUMANPOLR2Cphysical
26496610
RPB4_HUMANPOLR2Dphysical
26496610
RPAB1_HUMANPOLR2Ephysical
26496610
RPAB3_HUMANPOLR2Hphysical
26496610
RPB9_HUMANPOLR2Iphysical
26496610
RPB11_HUMANPOLR2Jphysical
26496610
MED1_HUMANMED1physical
26496610
SPT5H_HUMANSUPT5Hphysical
26496610
TCEA1_HUMANTCEA1physical
26496610
MOGS_HUMANMOGSphysical
26496610
CTDP1_HUMANCTDP1physical
26496610
MED14_HUMANMED14physical
26496610
RECQ5_HUMANRECQL5physical
26496610
MED21_HUMANMED21physical
26496610
MED17_HUMANMED17physical
26496610
MED26_HUMANMED26physical
26496610
MED6_HUMANMED6physical
26496610
MED16_HUMANMED16physical
26496610
PUR6_HUMANPAICSphysical
26496610
GPN1_HUMANGPN1physical
26496610
SETX_HUMANSETXphysical
26496610
RPRD2_HUMANRPRD2physical
26496610
MED4_HUMANMED4physical
26496610
MED31_HUMANMED31physical
26496610
GPN3_HUMANGPN3physical
26496610
MED15_HUMANMED15physical
26496610
PAF1_HUMANPAF1physical
26496610
MED18_HUMANMED18physical
26496610
MCM10_HUMANMCM10physical
26496610
MED29_HUMANMED29physical
26496610
CDC73_HUMANCDC73physical
26496610
RPAP2_HUMANRPAP2physical
26496610
MYZAP_HUMANPOLR2Mphysical
26496610
GRL1A_HUMANPOLR2Mphysical
26496610
GL1AD_HUMANPOLR2Mphysical
26496610
RECQ5_HUMANRECQL5physical
28514442
RPAP2_HUMANRPAP2physical
28514442
RPR1A_HUMANRPRD1Aphysical
28514442
CTDP1_HUMANCTDP1physical
28514442
RPRD2_HUMANRPRD2physical
28514442
RPB9_HUMANPOLR2Iphysical
28514442
RPB1_HUMANPOLR2Aphysical
28514442
RPAB5_HUMANPOLR2Lphysical
28514442
RPB11_HUMANPOLR2Jphysical
28514442
MED26_HUMANMED26physical
28514442
RPB2_HUMANPOLR2Bphysical
28514442
GPN1_HUMANGPN1physical
28514442
MED30_HUMANMED30physical
28514442
RPB3_HUMANPOLR2Cphysical
28514442
RPAB3_HUMANPOLR2Hphysical
28514442
SFR19_HUMANSCAF1physical
28514442

Drug and Disease Associations
Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
There are no disease associations of PTM sites.
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of RPB7_HUMAN

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Related Literatures of Post-Translational Modification

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