CPL3_ARATH - dbPTM
CPL3_ARATH - PTM Information in dbPTM
Basic Information of Protein
UniProt ID CPL3_ARATH
UniProt AC Q8LL04
Protein Name RNA polymerase II C-terminal domain phosphatase-like 3
Gene Name CPL3
Organism Arabidopsis thaliana (Mouse-ear cress).
Sequence Length 1241
Subcellular Localization Nucleus .
Protein Description Processively dephosphorylates 'Ser-2' and/or 'Ser-5' 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 (By similarity). Negative regulator of stress gene transcription involved in abscisic acid (ABA) mediated signaling pathway and cold resistance..
Protein Sequence MLVARSGCSRTLIRMGNDENLMVMVDVEEGEIPDSVNTEIEVKHKSTTTTADVGGDVDVGVVAGGRGGGGGGSNGNSRVWTMEELISQYPAYRPYANSGLSNLAWARAVQNKPFNEGLVMDYEPRESDKIVIEDSDDEKEEGELEEGEIDLVDNASDDNLVEKDTESVVLISADKVEDDRILKERDLEKKVKLIRGVLESTSLVEAQTGFEGVCSRILGALESLRELVSDNDDFPKRDTLVQLSFASLQTINYVFCSMNNISKERNKETMSRLLTLVNDHFSQFLSFNQKNEIETMNQDLSRSAIAVFAGTSSEENVNQMTQPSNGDSFLAKKLTSESTHRGAAYLRSRLPMLPLLDLHKDHDADSLPSPTRETTPSLPVNGRHTMVRPGFPVGRESQTTEGAKVYSYESDARKAVSTYQQKFGLNSVFKTDDLPSPTPSGEPNDGNGDVGGEVSSSVVKSSNPGSHLIYGQDVPLPSNFNSRSMPVANSVSSTVPPHHLSIHAISAPTASDQTVKPSAKSRDPRLRLAKPDAANVTIYSYSSGDARNLSKVELSADLVNPRKQKAADEFLIDGPAWKRQKSDTDAPKAAGTGGWLEDTESSGLLKLESKPRLIENGVTSMTSSVMPTSAVSVSQKVRTASTDTASLQSLLKDIAVNPTMLLNLLKMGERQKVPEKAIQKPMDPRRAAQLPGSSVQPGVSTPLSIPASNALAANSLNSGVLQDSSQNAPAAESGSIRMKPRDPRRILHGSTLQRTDSSMEKQTKVNDPSTLGTLTMKGKAEDLETPPQLDPRQNISQNGTSKMKISGELLSGKTPDFSTQFTKNLKSIADMVVVSQQLGNPPASMHSVQLKTERDVKHNPSNPNAQDEDVSVSAASVTAAAGPTRSMNSWGDVEHLFEGYDDIQRVAIQRERVRRLEEQNKMFASQKLSLVLDIDHTLLNSAKFNEVESRHEEILRKKEEQDREKPYRHLFRFLHMGMWTKLRPGIWNFLEKASKLYELHLYTMGNKLYATEMAKLLDPKGVLFNGRVISKGDDGDPLDGDERVPKSKDLEGVMGMESSVVIIDDSVRVWPQHKMNLIAVERYLYFPCSRRQFGLLGPSLLELDRDEVPEEGTLASSLAVIEKIHQNFFSHTSLDEVDVRNILASEQRKILAGCRIVFSRIIPVGEAKPHLHPLWQTAEQFGAVCTTQVDEHVTHVVTNSLGTDKVNWALTRGRFVVHPGWVEASAFLYQRANENLYAINP
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
135PhosphorylationDKIVIEDSDDEKEEG
CCEEEECCCCCCCCC
33.8823776212
366PhosphorylationHKDHDADSLPSPTRE
CCCCCCCCCCCCCCC
43.8519376835
369PhosphorylationHDADSLPSPTRETTP
CCCCCCCCCCCCCCC
44.1730291188
371PhosphorylationADSLPSPTRETTPSL
CCCCCCCCCCCCCCC
45.5419376835
431PhosphorylationGLNSVFKTDDLPSPT
CCCCCEECCCCCCCC
24.2330407730
436PhosphorylationFKTDDLPSPTPSGEP
EECCCCCCCCCCCCC
49.0230407730
438PhosphorylationTDDLPSPTPSGEPND
CCCCCCCCCCCCCCC
34.1330407730
440PhosphorylationDLPSPTPSGEPNDGN
CCCCCCCCCCCCCCC
59.2630407730
490PhosphorylationRSMPVANSVSSTVPP
CCCCCCCCCCCCCCC
17.4025368622
492PhosphorylationMPVANSVSSTVPPHH
CCCCCCCCCCCCCCC
21.8025368622
493PhosphorylationPVANSVSSTVPPHHL
CCCCCCCCCCCCCCC
31.1325368622
494PhosphorylationVANSVSSTVPPHHLS
CCCCCCCCCCCCCCE
29.5325368622
501PhosphorylationTVPPHHLSIHAISAP
CCCCCCCEEEEEECC
14.1525368622

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 CPL3_ARATH !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of CPL3_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 CPL3_ARATH !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
NRPB1_ARATHNRPB1physical
25464831

Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of CPL3_ARATH

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Related Literatures of Post-Translational Modification

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