CPL1_ARATH - dbPTM
CPL1_ARATH - PTM Information in dbPTM
Basic Information of Protein
UniProt ID CPL1_ARATH
UniProt AC Q5YDB6
Protein Name RNA polymerase II C-terminal domain phosphatase-like 1 {ECO:0000305}
Gene Name CPL1 {ECO:0000303|PubMed:15388846}
Organism Arabidopsis thaliana (Mouse-ear cress).
Sequence Length 967
Subcellular Localization Nucleus . Nucleus speckle .
Protein Description Processively dephosphorylates 'Ser-5' but not 'Ser-2' of the heptad repeats YSPTSPS in the C-terminal domain of the largest RNA polymerase II subunit (RPB1). This promotes the activity of RNA polymerase II. Together with CPL2, required for male gametes fertility. Multifunctional regulator that modulates plant growth, stress, and phytohormones responses. Negative regulator of stress gene transcription involved in abscisic acid (ABA) mediated and jasmonic acid (JA) mediated signaling pathways, NaCl, osmotic stress, wounding, and cold resistance. Regulates negatively the expression of jasmonic acid (JA) biosynthetic genes in response to wounding. [PubMed: 11874572]
Protein Sequence MYSNNRVEVFHGDGRLGELEIYPSRELNQQQDDVMKQRKKKQREVMELAKMGIRISHFSQSGERCPPLAILTTISSCGLCFKLEASPSPAQESLSLFYSSCLRDNKTAVMLLGGEELHLVAMYSENIKNDRPCFWAFSVAPGIYDSCLVMLNLRCLGIVFDLDETLVVANTMRSFEDKIDGFQRRINNEMDPQRLAVIVAEMKRYQDDKNLLKQYIESDQVVENGEVIKVQSEIVPALSDNHQPLVRPLIRLQEKNIILTRINPMIRDTSVLVRMRPSWEELRSYLTAKGRKRFEVYVCTMAERDYALEMWRLLDPEGNLINTNDLLARIVCVKSGFKKSLFNVFLDGTCHPKMALVIDDRLKVWDEKDQPRVHVVPAFAPYYSPQAEAAATPVLCVARNVACGVRGGFFRDFDDSLLPRIAEISYENDAEDIPSPPDVSHYLVSEDDTSGLNGNKDPLSFDGMADTEVERRLKEAISASSAVLPAANIDPRIAAPVQFPMASASSVSVPVPVQVVQQAIQPSAMAFPSIPFQQPQQPTSIAKHLVPSEPSLQSSPAREEGEVPESELDPDTRRRLLILQHGQDTRDPAPSEPSFPQRPPVQAPPSHVQSRNGWFPVEEEMDPAQIRRAVSKEYPLDSEMIHMEKHRPRHPSFFSKIDNSTQSDRMLHENRRPPKESLRRDEQLRSNNNLPDSHPFYGEDASWNQSSSRNSDLDFLPERSVSATETSADVLHGIAIKCGAKVEYKPSLVSSTDLRFSVEAWLSNQKIGEGIGKSRREALHKAAEASIQNLADGYMRANGDPGPSHRDATPFTNENISMGNANALNNQPFARDETALPVSSRPTDPRLEGSMRHTGSITALRELCASEGLEMAFQSQRQLPSDMVHRDELHAQVEIDGRVVGEGVGSTWDEARMQAAERALSSVRSMLGQPLHKRQGSPRSFGGMSNKRLKPDFQRSLQRMPSSGRYS
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
269PhosphorylationINPMIRDTSVLVRMR
ECHHHCCCEEEEEEC
15.7524894044
270PhosphorylationNPMIRDTSVLVRMRP
CHHHCCCEEEEEECC
20.1024894044
278PhosphorylationVLVRMRPSWEELRSY
EEEEECCCHHHHHHH
36.4324894044
506PhosphorylationFPMASASSVSVPVPV
CCCCCCCCCCCCCCH
20.3728011693
508PhosphorylationMASASSVSVPVPVQV
CCCCCCCCCCCCHHH
23.7428011693
548PhosphorylationIAKHLVPSEPSLQSS
HHHHCCCCCCCCCCC
55.4423776212
551PhosphorylationHLVPSEPSLQSSPAR
HCCCCCCCCCCCCCC
34.6823776212
554PhosphorylationPSEPSLQSSPAREEG
CCCCCCCCCCCCCCC
43.5123776212
555PhosphorylationSEPSLQSSPAREEGE
CCCCCCCCCCCCCCC
15.0423776212
566PhosphorylationEEGEVPESELDPDTR
CCCCCCHHHCCHHHH
37.0723776212
572PhosphorylationESELDPDTRRRLLIL
HHHCCHHHHHHEHHH
31.3123776212
856PhosphorylationGSMRHTGSITALREL
CCCCCCCHHHHHHHH
20.2325561503

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 CPL1_ARATH !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of CPL1_ARATH !!

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 CPL1_ARATH !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
DMS3_ARATHDMS3physical
18541146
XB31_ARATHXBAT31physical
18541146
MYB3_ARATHMYB3physical
18541146
NAC19_ARATHNAC019physical
18541146
NRPB1_ARATHNRPB1physical
15388846
SRRT_ARATHSEphysical
23141542
DRB1_ARATHHYL1physical
23141542

Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of CPL1_ARATH

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Related Literatures of Post-Translational Modification

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