COP1_ARATH - dbPTM
COP1_ARATH - PTM Information in dbPTM
Basic Information of Protein
UniProt ID COP1_ARATH
UniProt AC P43254
Protein Name E3 ubiquitin-protein ligase COP1 {ECO:0000303|PubMed:1423630}
Gene Name COP1 {ECO:0000303|PubMed:1423630}
Organism Arabidopsis thaliana (Mouse-ear cress).
Sequence Length 675
Subcellular Localization Nucleus . Cytoplasm . Localizes to the nucleus in darkness but is gradually relocated to the cytoplasm upon illumination. Localizes to subnuclear foci (speckle) and in dispersed nuclear localization in the dark.
Protein Description E3 ubiquitin-protein ligase that acts as a repressor of photomorphogenesis and as an activator of etiolation in darkness. E3 ubiquitin ligases accept ubiquitin from an E2 ubiquitin-conjugating enzyme in the form of a thioester and then directly transfers the ubiquitin to targeted substrates. Represses photomorphogenesis in darkness by mediating ubiquitination and subsequent proteasomal degradation of light-induced transcription factors such as HY5, HYH and LAF1. Down-regulates MYB21, probably via ubiquitination process. Light stimuli abrogate the repression of photomorphogenesis, possibly due to its localization to the cytoplasm. Could play a role in switching between skotomorphogenetic and photomorphogenetic pathways. Mediates the ubiquitination-dependent degradation of HY5 in the darkness during seedling development (e.g. hypocotyl growth). [PubMed: 26474641 Represses CIP7 in darkness]
Protein Sequence MEEISTDPVVPAVKPDPRTSSVGEGANRHENDDGGSGGSEIGAPDLDKDLLCPICMQIIKDAFLTACGHSFCYMCIITHLRNKSDCPCCSQHLTNNQLYPNFLLDKLLKKTSARHVSKTASPLDQFREALQRGCDVSIKEVDNLLTLLAERKRKMEQEEAERNMQILLDFLHCLRKQKVDELNEVQTDLQYIKEDINAVERHRIDLYRARDRYSVKLRMLGDDPSTRNAWPHEKNQIGFNSNSLSIRGGNFVGNYQNKKVEGKAQGSSHGLPKKDALSGSDSQSLNQSTVSMARKKRIHAQFNDLQECYLQKRRQLADQPNSKQENDKSVVRREGYSNGLADFQSVLTTFTRYSRLRVIAEIRHGDIFHSANIVSSIEFDRDDELFATAGVSRCIKVFDFSSVVNEPADMQCPIVEMSTRSKLSCLSWNKHEKNHIASSDYEGIVTVWDVTTRQSLMEYEEHEKRAWSVDFSRTEPSMLVSGSDDCKVKVWCTRQEASVINIDMKANICCVKYNPGSSNYIAVGSADHHIHYYDLRNISQPLHVFSGHKKAVSYVKFLSNNELASASTDSTLRLWDVKDNLPVRTFRGHTNEKNFVGLTVNSEYLACGSETNEVYVYHKEITRPVTSHRFGSPDMDDAEEEAGSYFISAVCWKSDSPTMLTANSQGTIKVLVLAA
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
20PhosphorylationVKPDPRTSSVGEGAN
CCCCCCCCCCCCCCC
25.0625561503
21PhosphorylationKPDPRTSSVGEGANR
CCCCCCCCCCCCCCC
33.2625561503
36PhosphorylationHENDDGGSGGSEIGA
CCCCCCCCCCCCCCC
45.5730407730
39PhosphorylationDDGGSGGSEIGAPDL
CCCCCCCCCCCCCCC
29.5730407730
559PhosphorylationVSYVKFLSNNELASA
EEEEEECCCCCCCCC
40.5223776212
565PhosphorylationLSNNELASASTDSTL
CCCCCCCCCCCCCCE
35.0623776212
567PhosphorylationNNELASASTDSTLRL
CCCCCCCCCCCCEEE
30.1923776212
568PhosphorylationNELASASTDSTLRLW
CCCCCCCCCCCEEEE
33.4123776212
570PhosphorylationLASASTDSTLRLWDV
CCCCCCCCCEEEEEC
29.4523776212
571PhosphorylationASASTDSTLRLWDVK
CCCCCCCCEEEEECC
20.7823776212

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 COP1_ARATH !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of COP1_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 COP1_ARATH !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
HFR1_ARATHHFR1physical
17699755
HFR1_ARATHHFR1physical
15741320
HFR1_ARATHHFR1physical
15620659
PHYA_ARATHPHYAphysical
15031264
HY5_ARATHHY5physical
14597662
CIP8_ARATHCIP8physical
12827204
LAF1_ARATHMYB18physical
12827204
SPA1_ARATHSPA1physical
11461903
CIP8_ARATHCIP8physical
10488108
CONS_ARATHCOphysical
18296627
CRY1_ARATHCRY1physical
18252844
BBX25_ARATHSTHphysical
18796637
SPA1_ARATHSPA1physical
18722184
PHYA_ARATHPHYAphysical
18722184
SPA1_ARATHSPA1physical
18812498
SPA2_ARATHSPA2physical
18812498
SPA3_ARATHSPA3physical
18812498
SPA4_ARATHSPA4physical
18812498
ELF3_ARATHELF3physical
19061637
GIGAN_ARATHGIphysical
19061637
CRY2_ARATHCRY2physical
11509693
COP1_ARATHCOP1physical
11080276
COP1_ARATHCOP1physical
15084749
COP1_ARATHCOP1physical
9755158
COP1_ARATHCOP1physical
8837504
HY5_ARATHHY5physical
11226162
BBX24_ARATHSTOphysical
11226162
BBX25_ARATHSTHphysical
11226162
HYH_ARATHHYHphysical
12023303
CIP8_ARATHCIP8physical
12028569
HFR1_ARATHHFR1physical
15705947
COL3_ARATHCOL3physical
16339850
PHYB_ARATHPHYBphysical
20605855
PHYC_ARATHPHYCphysical
20605855
PHYD_ARATHPHYDphysical
20605855
PHYE_ARATHPHYEphysical
20605855
SCAR1_ARATHWAVE1physical
21972261
BBX20_ARATHAT4G39070physical
22535582
HY5_ARATHHY5physical
22692212
RPP8_ARATHRPP8physical
20624951
PHOT2_ARATHPHOT2physical
20624951
UVR8_ARATHUVR8physical
19165148
HY5_ARATHHY5physical
23425305
BIN4_ARATHBIN4physical
23573936
SPA1_ARATHSPA1physical
24067658
SPA3_ARATHSPA3physical
24067658
HY5_ARATHHY5genetic
24838976
CRY1_ARATHCRY1physical
24554768
CRY2_ARATHCRY2physical
24554768
UVR8_ARATHUVR8physical
24554768
CONS_ARATHCOphysical
24554768
HFR1_ARATHHFR1physical
24554768
COP1_ARATHCOP1physical
24554768
HFR1_ARATHHFR1physical
19802365
COP1_ARATHCOP1physical
19802365
HYH_ARATHHYHphysical
19802365
SPA1_ARATHSPA1physical
19802365
COP1_ARATHCOP1physical
21153370
PHYA_ARATHPHYAphysical
25627066
SPA1_ARATHSPA1physical
25744387
HY5_ARATHHY5physical
24610722
HY5_ARATHHY5physical
24858936
COP1_ARATHCOP1physical
24858936
COP1_ARATHCOP1physical
25817546
CSN1_ARATHFUS6physical
19175768
CSN4_ARATHCOP8physical
19175768
CSN5A_ARATHCSN5Aphysical
19175768
RAX2_ARATHRAX2physical
18397371
TRIB1_HUMANTRIB1physical
27041596
SUMO1_ARATHSUMO1physical
27128446

Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of COP1_ARATH

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Related Literatures of Post-Translational Modification

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