RPB1_DROME - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: RPB1_DROME
• UniProt AC: P04052
• Protein Name: DNA-directed RNA polymerase II subunit RPB1
• Gene Name: RpII215
• Organism: Drosophila melanogaster (Fruit fly).
• Sequence Length: 1887
• Subcellular Localization: Nucleus.
• Protein Description: DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates. Largest and catalytic component of RNA polymerase II which synthesizes mRNA precursors and many functional non-coding RNAs. Forms the polymerase active center together with the second largest subunit. 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. RPB1 is part of the core element with the central large cleft, the clamp element that moves to open and close the cleft and the jaws that are thought to grab the incoming DNA template. At the start of transcription, a single-stranded DNA template strand of the promoter is positioned within the central active site cleft of Pol II. A bridging helix emanates from RPB1 and crosses the cleft near the catalytic site and is thought to promote translocation of Pol II 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. During transcription elongation, Pol II moves on the template as the transcript elongates. Elongation is influenced by the phosphorylation status of the C-terminal domain (CTD) of Pol II largest subunit (RPB1), which serves as a platform for assembly of factors that regulate transcription initiation, elongation, termination and mRNA processing (By similarity)..
• Protein Sequence: MSTPTDSKAPLRQVKRVQFGILSPDEIRRMSVTEGGVQFAETMEGGRPKLGGLMDPRQGVIDRTSRCQTCAGNMTECPGHFGHIDLAKPVFHIGFITKTIKILRCVCFYCSKMLVSPHNPKIKEIVMKSRGQPRKRLAYVYDLCKGKTICEGGEDMDLTKENQQPDPNKKPGHGGCGHYQPSIRRTGLDLTAEWKHQNEDSQEKKIVVSAERVWEILKHITDEECFILGMDPKYARPDWMIVTVLPVPPLAVRPAVVMFGAAKNQDDLTHKLSDIIKANNELRKNEASGAAAHVIQENIKMLQFHVATLVDNDMPGMPRAMQKSGKPLKAIKARLKGKEGRIRGNLMGKRVDFSARTVITPDPNLRIDQVGVPRSIAQNLTFPELVTPFNIDRMQELVRRGNSQYPGAKYIVRDNGERIDLRFHPKSSDLHLQCGYKVERHLRDDDLVIFNRQPTLHKMSMMGHRVKVLPWSTFRMNLSCTSPYNADFDGDEMNLHVPQSMETRAEVENIHITPRQIITPQANKPVMGIVQDTLTAVRKMTKRDVFITREQVMNLLMFLPTWDAKMPQPCILKPRPLWTGKQIFSLIIPGNVNMIRTHSTHPDEEDEGPYKWISPGDTKVMVEHGELIMGILCKKSLGTSAGSLLHICFLELGHDIAGRFYGNIQTVINNWLLFEGHSIGIGDTIADPQTYNEIQQAIKKAKDDVINVIQKAHNMELEPTPGNTLRQTFENKVNRILNDARDKTGGSAKKSLTEYNNLKAMVVSGSKGSNINISQVIACVGQQNVEGKRIPYGFRKRTLPHFIKDDYGPESRGFVENSYLAGLTPSEFYFHAMGGREGLIDTAVKTAETGYIQRRLIKAMESVMVNYDGTVRNSVGQLIQLRYGEDGLCGELVEFQNMPTVKLSNKSFEKRFKFDWSNERLMKKVFTDDVIKEMTDSSEAIQELEAEWDRLVSDRDSLRQIFPNGESKVVLPCNLQRMIWNVQKIFHINKRLPTDLSPIRVIKGVKTLLERCVIVTGNDRISKQANENATLLFQCLIRSTLCTKYVSEEFRLSTEAFEWLVGEIETRFQQAQANPGEMVGALAAQSLGEPATQMTLNTFHFAGVSSKNVTLGVPRLKEIINISKKPKAPSLTVFLTGGAARDAEKAKNVLCRLEHTTLRKVTANTAIYYDPDPQRTVISEDQEFVNVYYEMPDFDPTRISPWLLRIELDRKRMTDKKLTMEQIAEKINVGFGEDLNCIFNDDNADKLVLRIRIMNNEENKFQDEDEAVDKMEDDMFLRCIEANMLSDMTLQGIEAIGKVYMHLPQTDSKKRIVITETGEFKAIGEWLLETDGTSMMKVLSERDVDPIRTSSNDICEIFQVLGIEAVRKSVEKEMNAVLQFYGLYVNYRHLALLCDVMTAKGHLMAITRHGINRQDTGALMRCSFEETVDVLMDAAAHAETDPMRGVSENIIMGQLPKMGTGCFDLLLDAEKCRFGIEIPNTLGNSMLGGAAMFIGGGSTPSMTPPMTPWANCNTPRYFSPPGHVSAMTPGGPSFSPSAASDASGMSPSWSPAHPGSSPSSPGPSMSPYFPASPSVSPSYSPTSPNYTASSPGGASPNYSPSSPNYSPTSPLYASPRYASTTPNFNPQSTGYSPSSSGYSPTSPVYSPTVQFQSSPSFAGSGSNIYSPGNAYSPSSSNYSPNSPSYSPTSPSYSPSSPSYSPTSPCYSPTSPSYSPTSPNYTPVTPSYSPTSPNYSASPQYSPASPAYSQTGVKYSPTSPTYSPPSPSYDGSPGSPQYTPGSPQYSPASPKYSPTSPLYSPSSPQHSPSNQYSPTGSTYSATSPRYSPNMSIYSPSSTKYSPTSPTYTPTARNYSPTSPMYSPTAPSHYSPTSPAYSPSSPTFEESED

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
2	Phosphorylation	------MSTPTDSKA ------CCCCCCCCC	55.16	18200011
31	Phosphorylation	PDEIRRMSVTEGGVQ HHHHHCCEECCCCCE	24.87	21082442
1802	Phosphorylation	SPLYSPSSPQHSPSN CCCCCCCCCCCCCCC	31.78	21082442
1822	Phosphorylation	GSTYSATSPRYSPNM CCCCCCCCCCCCCCC	13.70	21082442
1825	Phosphorylation	YSATSPRYSPNMSIY CCCCCCCCCCCCEEE	31.68	19429919
1826	Phosphorylation	SATSPRYSPNMSIYS CCCCCCCCCCCEEEC	15.86	19429919
1832	Phosphorylation	YSPNMSIYSPSSTKY CCCCCEEECCCCCCC	13.76	27626673
1833	Phosphorylation	SPNMSIYSPSSTKYS CCCCEEECCCCCCCC	19.35	19429919
1835	Phosphorylation	NMSIYSPSSTKYSPT CCEEECCCCCCCCCC	44.70	19429919
1836	Phosphorylation	MSIYSPSSTKYSPTS CEEECCCCCCCCCCC	32.10	19429919
1837	Phosphorylation	SIYSPSSTKYSPTSP EEECCCCCCCCCCCC	38.04	19429919
1839	Phosphorylation	YSPSSTKYSPTSPTY ECCCCCCCCCCCCCC	21.70	27626673
1842	Phosphorylation	SSTKYSPTSPTYTPT CCCCCCCCCCCCCCC	41.20	29892262
1843	Phosphorylation	STKYSPTSPTYTPTA CCCCCCCCCCCCCCC	20.73	22668510

Upstream regulatory proteins (kinases for phosphorylation sites, E3 ubiquitin ligases of ubiquitination sites, ...)

Oops, there are no upstream regulatory protein records of RPB1_DROME !!

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of RPB1_DROME !!

Disease-associated PTM Sites based on SAP

* Distance = the distance between SAP position and PTM sites.

Oops, there are no SNP-PTM records of RPB1_DROME !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
RPB2_DROME	RpII140	genetic	9669327
RPB2_DROME	RpII140	genetic	2352953
RPB2_DROME	RpII140	genetic	7966318
RPB4_DROME	Rpb4	physical	25242320
HSP83_DROME	Hsp83	physical	24394412
NELFE_DROME	Nelf-E	physical	22056986
AGO2_DROME	AGO2	physical	22056986
BRM_DROME	brm	physical	27687497
T2FB_DROME	TfIIFbeta	physical	25242320
TCTP_DROME	Tctp	physical	27687497
RPB2_DROME	RpII140	physical	24394412
SPT6H_DROME	Spt6	physical	27879206

Drug and Disease Associations

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