NRPB1_ARATH - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: NRPB1_ARATH
• UniProt AC: P18616
• Protein Name: DNA-directed RNA polymerase II subunit 1
• Gene Name: NRPB1
• Organism: Arabidopsis thaliana (Mouse-ear cress).
• Sequence Length: 1839
• Subcellular Localization: Nucleus . Peri-nucleolar.
• 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. NRPB1 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 NRPB1 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 (NRPB1), which serves as a platform for assembly of factors that regulate transcription initiation, elongation, termination and mRNA processing..
• Protein Sequence: MDTRFPFSPAEVSKVRVVQFGILSPDEIRQMSVIHVEHSETTEKGKPKVGGLSDTRLGTIDRKVKCETCMANMAECPGHFGYLELAKPMYHVGFMKTVLSIMRCVCFNCSKILADEEEHKFKQAMKIKNPKNRLKKILDACKNKTKCDGGDDIDDVQSHSTDEPVKKSRGGCGAQQPKLTIEGMKMIAEYKIQRKKNDEPDQLPEPAERKQTLGADRVLSVLKRISDADCQLLGFNPKFARPDWMILEVLPIPPPPVRPSVMMDATSRSEDDLTHQLAMIIRHNENLKRQEKNGAPAHIISEFTQLLQFHIATYFDNELPGQPRATQKSGRPIKSICSRLKAKEGRIRGNLMGKRVDFSARTVITPDPTINIDELGVPWSIALNLTYPETVTPYNIERLKELVDYGPHPPPGKTGAKYIIRDDGQRLDLRYLKKSSDQHLELGYKVERHLQDGDFVLFNRQPSLHKMSIMGHRIRIMPYSTFRLNLSVTSPYNADFDGDEMNMHVPQSFETRAEVLELMMVPKCIVSPQANRPVMGIVQDTLLGCRKITKRDTFIEKDVFMNTLMWWEDFDGKVPAPAILKPRPLWTGKQVFNLIIPKQINLLRYSAWHADTETGFITPGDTQVRIERGELLAGTLCKKTLGTSNGSLVHVIWEEVGPDAARKFLGHTQWLVNYWLLQNGFTIGIGDTIADSSTMEKINETISNAKTAVKDLIRQFQGKELDPEPGRTMRDTFENRVNQVLNKARDDAGSSAQKSLAETNNLKAMVTAGSKGSFINISQMTACVGQQNVEGKRIPFGFDGRTLPHFTKDDYGPESRGFVENSYLRGLTPQEFFFHAMGGREGLIDTAVKTSETGYIQRRLVKAMEDIMVKYDGTVRNSLGDVIQFLYGEDGMDAVWIESQKLDSLKMKKSEFDRTFKYEIDDENWNPTYLSDEHLEDLKGIRELRDVFDAEYSKLETDRFQLGTEIATNGDSTWPLPVNIKRHIWNAQKTFKIDLRKISDMHPVEIVDAVDKLQERLLVVPGDDALSVEAQKNATLFFNILLRSTLASKRVLEEYKLSREAFEWVIGEIESRFLQSLVAPGEMIGCVAAQSIGEPATQMTLNTFHYAGVSAKNVTLGVPRLREIINVAKRIKTPSLSVYLTPEASKSKEGAKTVQCALEYTTLRSVTQATEVWYDPDPMSTIIEEDFEFVRSYYEMPDEDVSPDKISPWLLRIELNREMMVDKKLSMADIAEKINLEFDDDLTCIFNDDNAQKLILRIRIMNDEGPKGELQDESAEDDVFLKKIESNMLTEMALRGIPDINKVFIKQVRKSRFDEEGGFKTSEEWMLDTEGVNLLAVMCHEDVDPKRTTSNHLIEIIEVLGIEAVRRALLDELRVVISFDGSYVNYRHLAILCDTMTYRGHLMAITRHGINRNDTGPLMRCSFEETVDILLDAAAYAETDCLRGVTENIMLGQLAPIGTGDCELYLNDEMLKNAIELQLPSYMDGLEFGMTPARSPVSGTPYHEGMMSPNYLLSPNMRLSPMSDAQFSPYVGGMAFSPSSSPGYSPSSPGYSPTSPGYSPTSPGYSPTSPGYSPTSPTYSPSSPGYSPTSPAYSPTSPSYSPTSPSYSPTSPSYSPTSPSYSPTSPSYSPTSPSYSPTSPAYSPTSPAYSPTSPAYSPTSPSYSPTSPSYSPTSPSYSPTSPSYSPTSPSYSPTSPAYSPTSPGYSPTSPSYSPTSPSYGPTSPSYNPQSAKYSPSIAYSPSNARLSPASPYSPTSPNYSPTSPSYSPTSPSYSPSSPTYSPSSPYSSGASPDYSPSAGYSPTLPGYSPSSTGQYTPHEGDKKDKTGKKDASKDDKGNP

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
1514	Phosphorylation	MSPNYLLSPNMRLSP CCCCCCCCCCCCCCC		29654922
1733	Phosphorylation	YNPQSAKYSPSIAYS CCCCCCCCCCCCCCC		23776212
1734	Phosphorylation	NPQSAKYSPSIAYSP CCCCCCCCCCCCCCC		23776212
1736	Phosphorylation	QSAKYSPSIAYSPSN CCCCCCCCCCCCCCC		23776212
1739	Phosphorylation	KYSPSIAYSPSNARL CCCCCCCCCCCCCCC		23776212
1740	Phosphorylation	YSPSIAYSPSNARLS CCCCCCCCCCCCCCC		30291188
1742	Phosphorylation	PSIAYSPSNARLSPA CCCCCCCCCCCCCCC		23776212

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

Oops, there are no upstream regulatory protein records of NRPB1_ARATH !!

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
2	S	Phosphorylation	'Ser-2' and 'Ser-5' phosphorylation are repressed by flavopiridol (Flap) and seliciclib (Selic), inhibitors of CDK7 and CDK9.	21266657
2	S	Phosphorylation	Phosphorylation occurs mainly at residues 'Ser-2' and 'Ser-5' of the heptapeptide repeat.	21266657
5	S	Phosphorylation	'Ser-2' and 'Ser-5' phosphorylation are repressed by flavopiridol (Flap) and seliciclib (Selic), inhibitors of CDK7 and CDK9.	21266657
5	S	Phosphorylation	Phosphorylation occurs mainly at residues 'Ser-2' and 'Ser-5' of the heptapeptide repeat.	21266657

Disease-associated PTM Sites based on SAP

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

Oops, there are no SNP-PTM records of NRPB1_ARATH !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
CYP59_ARATH	CYP59	physical	16497658
RDM1_ARATH	RDM1	physical	20410883
CPL4_ARATH	CPL4	physical	25041272
CPL3_ARATH	CPL3	physical	25464831
PR35B_ARATH	PRP40B	physical	19467629

Drug and Disease Associations

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