Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

E3 ubiquitin-protein ligase COP1

Gene

COP1

Organism
Arabidopsis thaliana (Mouse-ear cress)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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.2 Publications

Pathwayi: protein ubiquitination

This protein is involved in the pathway protein ubiquitination, which is part of Protein modification.
View all proteins of this organism that are known to be involved in the pathway protein ubiquitination and in Protein modification.

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri52 – 9039RING-typePROSITE-ProRule annotationAdd
BLAST

GO - Molecular functioni

  • identical protein binding Source: IntAct
  • ligase activity Source: UniProtKB-KW
  • ubiquitin protein ligase activity Source: GO_Central
  • ubiquitin-protein transferase activity Source: TAIR
  • zinc ion binding Source: InterPro

GO - Biological processi

  • anthocyanin-containing compound metabolic process Source: TAIR
  • DNA repair Source: TAIR
  • entrainment of circadian clock Source: TAIR
  • photomorphogenesis Source: TAIR
  • photoperiodism, flowering Source: TAIR
  • positive regulation of proteasomal ubiquitin-dependent protein catabolic process Source: GO_Central
  • red, far-red light phototransduction Source: UniProtKB-KW
  • regulation of stomatal movement Source: TAIR
  • shade avoidance Source: TAIR
  • skotomorphogenesis Source: TAIR
Complete GO annotation...

Keywords - Molecular functioni

Ligase

Keywords - Biological processi

Phytochrome signaling pathway, Ubl conjugation pathway

Keywords - Ligandi

Metal-binding, Zinc

Enzyme and pathway databases

ReactomeiR-ATH-349425. Autodegradation of the E3 ubiquitin ligase COP1.
UniPathwayiUPA00143.

Names & Taxonomyi

Protein namesi
Recommended name:
E3 ubiquitin-protein ligase COP1 (EC:6.3.2.-)
Alternative name(s):
Constitutive photomorphogenesis protein 1
Gene namesi
Name:COP1
Ordered Locus Names:At2g32950
ORF Names:T21L14.11
OrganismiArabidopsis thaliana (Mouse-ear cress)
Taxonomic identifieri3702 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis
Proteomesi
  • UP000006548 Componenti: Chromosome 2

Organism-specific databases

TAIRiAT2G32950.

Subcellular locationi

  • Nucleus
  • Cytoplasm

  • Note: 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.

GO - Cellular componenti

  • Cul4-RING E3 ubiquitin ligase complex Source: TAIR
  • cytoplasm Source: UniProtKB-SubCell
  • nuclear body Source: TAIR
  • nuclear ubiquitin ligase complex Source: TAIR
  • nucleus Source: TAIR
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi52 – 521C → S: Abolishes LAF1 ubiquitination and degradation; when associated with S-55. 1 Publication
Mutagenesisi55 – 551C → S: Abolishes LAF1 ubiquitination and degradation; when associated with S-52. 1 Publication
Mutagenesisi294 – 2963RKK → SKT: Abolishes localization to the nucleus. 1 Publication
Mutagenesisi312 – 3143KRR → TRS: Abolishes localization to the nucleus. 1 Publication
Mutagenesisi422 – 4221K → E: 5-fold increase in interaction with HY5, weak interaction with BBX24/STO and BBX25/STH, and at low light intensity shorter hypocotyl. 1 Publication
Mutagenesisi465 – 4651R → E: No interaction with BBX24/STO and BBX25/STH, and at low light intensity shorter hypocotyl. 1 Publication
Mutagenesisi467 – 4671W → A: No interaction with HY5, BBX24/STO and BBX25/STH and at low light intensity shorter hypocotyl. 1 Publication
Mutagenesisi523 – 58462Missing in COP1-8; no interaction with SPA1 and lethal. Add
BLAST
Mutagenesisi524 – 5241G → E in COP1-9; no interaction with HY5, SPA1, BBX25/STH or BBX24/STO and lethal.
Mutagenesisi550 – 5501K → E: No interaction with HY5, BBX24/STO and BBX25/STH and at low light intensity shorter hypocotyl. 1 Publication
Mutagenesisi592 – 5921E → R: Better interaction with HY5, BBX24/STO and BBX25/STH and slightly longer hypocotyls. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 675675E3 ubiquitin-protein ligase COP1PRO_0000055881Add
BLAST

Post-translational modificationi

Autoubiquitinated.4 Publications

Keywords - PTMi

Ubl conjugation

Proteomic databases

PaxDbiP43254.
PRIDEiP43254.

PTM databases

iPTMnetiP43254.

Expressioni

Gene expression databases

GenevisibleiP43254. AT.

Interactioni

Subunit structurei

Homodimer. Interacts with HY5, HYH, BBX24/STO, BBX25/STH, CIP8, COP10, SPA1, SPA2, SPA3, SPA4 and UVR8 and phosphorylated PHYA. Light induces dissociation of the SPA1/COP1 complex. Interacts with HRT/RPP8 and triggers it to the 26s proteasome. Binds to CRY2; this competitive interaction prevents triggering to proteasome of other binding proteins (PubMed:20624951).12 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
itself5EBI-301649,EBI-301649
Q388433EBI-301649,EBI-2119970
BBX25Q9SID13EBI-301649,EBI-631960
CIP8Q9SPL26EBI-301649,EBI-301644
COQ390578EBI-301649,EBI-1639724
COL3Q9SK533EBI-301649,EBI-1995108
COP10Q9LJD73EBI-301649,EBI-2429853
CRY1Q431254EBI-301649,EBI-300703
CRY2Q965242EBI-301649,EBI-531555
HFR1Q9FE226EBI-301649,EBI-626001
HY5O246468EBI-301649,EBI-301660
HYHQ8W191-13EBI-301649,EBI-11463635
LAF1Q9M0K43EBI-301649,EBI-1543309
RAX2Q9SJL73EBI-301649,EBI-2292310
SPA1Q9SYX217EBI-301649,EBI-626992
SPA3Q9LJR37EBI-301649,EBI-626921
SPA4Q94BM714EBI-301649,EBI-626943
UVR8Q9FN033EBI-301649,EBI-2407499

GO - Molecular functioni

  • identical protein binding Source: IntAct

Protein-protein interaction databases

BioGridi3204. 53 interactions.
DIPiDIP-32850N.
IntActiP43254. 28 interactions.
MINTiMINT-189205.
STRINGi3702.AT2G32950.1.

Structurei

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
5IGOX-ray1.60A/B/C/D349-675[»]
ProteinModelPortaliP43254.
SMRiP43254. Positions 52-101, 335-673.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Repeati369 – 40840WD 1Add
BLAST
Repeati418 – 45841WD 2Add
BLAST
Repeati461 – 50141WD 3Add
BLAST
Repeati503 – 54341WD 4Add
BLAST
Repeati547 – 58539WD 5Add
BLAST
Repeati588 – 62740WD 6Add
BLAST
Repeati642 – 67433WD 7Add
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni67 – 177111CLS (cytoplasmic localization signal)Add
BLAST
Regioni120 – 17758SNLS (subnuclear localization signal)Add
BLAST

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili134 – 20168Sequence analysisAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi294 – 31724Bipartite nuclear localization signalAdd
BLAST
Motifi522 – 53615DWD box 1Add
BLAST
Motifi563 – 57816DWD box 2Add
BLAST

Domaini

The coiled-coil domain (134-201) is necessary for SPA1, SPA3 or SPA4 binding. The DWD box is required for interaction with DDB1A (By similarity).By similarity

Sequence similaritiesi

Contains 1 RING-type zinc finger.PROSITE-ProRule annotation
Contains 7 WD repeats.PROSITE-ProRule annotation

Zinc finger

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri52 – 9039RING-typePROSITE-ProRule annotationAdd
BLAST

Keywords - Domaini

Coiled coil, Repeat, WD repeat, Zinc-finger

Phylogenomic databases

eggNOGiENOG410ISDP. Eukaryota.
ENOG410XNTU. LUCA.
HOGENOMiHOG000006123.
InParanoidiP43254.
KOiK10143.
OMAiFSTRMTR.
PhylomeDBiP43254.

Family and domain databases

Gene3Di2.130.10.10. 1 hit.
3.30.40.10. 1 hit.
InterProiIPR033313. RFWD2/COP1.
IPR015943. WD40/YVTN_repeat-like_dom.
IPR001680. WD40_repeat.
IPR019775. WD40_repeat_CS.
IPR017986. WD40_repeat_dom.
IPR001841. Znf_RING.
IPR013083. Znf_RING/FYVE/PHD.
IPR017907. Znf_RING_CS.
[Graphical view]
PANTHERiPTHR22847:SF451. PTHR22847:SF451. 2 hits.
PfamiPF00400. WD40. 2 hits.
[Graphical view]
SMARTiSM00184. RING. 1 hit.
SM00320. WD40. 7 hits.
[Graphical view]
SUPFAMiSSF50978. SSF50978. 1 hit.
PROSITEiPS00678. WD_REPEATS_1. 1 hit.
PS50082. WD_REPEATS_2. 2 hits.
PS50294. WD_REPEATS_REGION. 1 hit.
PS00518. ZF_RING_1. 1 hit.
PS50089. ZF_RING_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P43254-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MEEISTDPVV PAVKPDPRTS SVGEGANRHE NDDGGSGGSE IGAPDLDKDL
60 70 80 90 100
LCPICMQIIK DAFLTACGHS FCYMCIITHL RNKSDCPCCS QHLTNNQLYP
110 120 130 140 150
NFLLDKLLKK TSARHVSKTA SPLDQFREAL QRGCDVSIKE VDNLLTLLAE
160 170 180 190 200
RKRKMEQEEA ERNMQILLDF LHCLRKQKVD ELNEVQTDLQ YIKEDINAVE
210 220 230 240 250
RHRIDLYRAR DRYSVKLRML GDDPSTRNAW PHEKNQIGFN SNSLSIRGGN
260 270 280 290 300
FVGNYQNKKV EGKAQGSSHG LPKKDALSGS DSQSLNQSTV SMARKKRIHA
310 320 330 340 350
QFNDLQECYL QKRRQLADQP NSKQENDKSV VRREGYSNGL ADFQSVLTTF
360 370 380 390 400
TRYSRLRVIA EIRHGDIFHS ANIVSSIEFD RDDELFATAG VSRCIKVFDF
410 420 430 440 450
SSVVNEPADM QCPIVEMSTR SKLSCLSWNK HEKNHIASSD YEGIVTVWDV
460 470 480 490 500
TTRQSLMEYE EHEKRAWSVD FSRTEPSMLV SGSDDCKVKV WCTRQEASVI
510 520 530 540 550
NIDMKANICC VKYNPGSSNY IAVGSADHHI HYYDLRNISQ PLHVFSGHKK
560 570 580 590 600
AVSYVKFLSN NELASASTDS TLRLWDVKDN LPVRTFRGHT NEKNFVGLTV
610 620 630 640 650
NSEYLACGSE TNEVYVYHKE ITRPVTSHRF GSPDMDDAEE EAGSYFISAV
660 670
CWKSDSPTML TANSQGTIKV LVLAA
Length:675
Mass (Da):76,188
Last modified:January 23, 2002 - v2
Checksum:iE6D9A1B702EAE8F0
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti292 – 2921M → I in AAA32772 (PubMed:1423630).Curated
Sequence conflicti361 – 3611E → Q in CAA04168 (PubMed:9744100).Curated
Sequence conflicti381 – 3811R → P in CAA04168 (PubMed:9744100).Curated
Sequence conflicti403 – 4031V → F in AAA32772 (PubMed:1423630).Curated
Sequence conflicti456 – 4561L → R in AAA32772 (PubMed:1423630).Curated
Sequence conflicti515 – 5151P → R in CAA04169 (PubMed:9744100).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L24437 mRNA. Translation: AAA32772.1.
AC003033 Genomic DNA. Translation: AAB91983.1.
CP002685 Genomic DNA. Translation: AEC08766.1.
BT025337 mRNA. Translation: ABF57293.1.
AJ000535 Genomic DNA. Translation: CAA04168.1.
AJ000536 Genomic DNA. Translation: CAA04169.1.
PIRiT01112.
RefSeqiNP_180854.1. NM_128855.3.
UniGeneiAt.298.

Genome annotation databases

EnsemblPlantsiAT2G32950.1; AT2G32950.1; AT2G32950.
GeneIDi817857.
GrameneiAT2G32950.1; AT2G32950.1; AT2G32950.
KEGGiath:AT2G32950.

Cross-referencesi

Web resourcesi

PlantsUBQ

A functional genomics database for the ubiquitin/26S proteasome proteolytic pathway in plants

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L24437 mRNA. Translation: AAA32772.1.
AC003033 Genomic DNA. Translation: AAB91983.1.
CP002685 Genomic DNA. Translation: AEC08766.1.
BT025337 mRNA. Translation: ABF57293.1.
AJ000535 Genomic DNA. Translation: CAA04168.1.
AJ000536 Genomic DNA. Translation: CAA04169.1.
PIRiT01112.
RefSeqiNP_180854.1. NM_128855.3.
UniGeneiAt.298.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
5IGOX-ray1.60A/B/C/D349-675[»]
ProteinModelPortaliP43254.
SMRiP43254. Positions 52-101, 335-673.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi3204. 53 interactions.
DIPiDIP-32850N.
IntActiP43254. 28 interactions.
MINTiMINT-189205.
STRINGi3702.AT2G32950.1.

PTM databases

iPTMnetiP43254.

Proteomic databases

PaxDbiP43254.
PRIDEiP43254.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblPlantsiAT2G32950.1; AT2G32950.1; AT2G32950.
GeneIDi817857.
GrameneiAT2G32950.1; AT2G32950.1; AT2G32950.
KEGGiath:AT2G32950.

Organism-specific databases

TAIRiAT2G32950.

Phylogenomic databases

eggNOGiENOG410ISDP. Eukaryota.
ENOG410XNTU. LUCA.
HOGENOMiHOG000006123.
InParanoidiP43254.
KOiK10143.
OMAiFSTRMTR.
PhylomeDBiP43254.

Enzyme and pathway databases

UniPathwayiUPA00143.
ReactomeiR-ATH-349425. Autodegradation of the E3 ubiquitin ligase COP1.

Miscellaneous databases

PROiP43254.

Gene expression databases

GenevisibleiP43254. AT.

Family and domain databases

Gene3Di2.130.10.10. 1 hit.
3.30.40.10. 1 hit.
InterProiIPR033313. RFWD2/COP1.
IPR015943. WD40/YVTN_repeat-like_dom.
IPR001680. WD40_repeat.
IPR019775. WD40_repeat_CS.
IPR017986. WD40_repeat_dom.
IPR001841. Znf_RING.
IPR013083. Znf_RING/FYVE/PHD.
IPR017907. Znf_RING_CS.
[Graphical view]
PANTHERiPTHR22847:SF451. PTHR22847:SF451. 2 hits.
PfamiPF00400. WD40. 2 hits.
[Graphical view]
SMARTiSM00184. RING. 1 hit.
SM00320. WD40. 7 hits.
[Graphical view]
SUPFAMiSSF50978. SSF50978. 1 hit.
PROSITEiPS00678. WD_REPEATS_1. 1 hit.
PS50082. WD_REPEATS_2. 2 hits.
PS50294. WD_REPEATS_REGION. 1 hit.
PS00518. ZF_RING_1. 1 hit.
PS50089. ZF_RING_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "COP1, an Arabidopsis regulatory gene, encodes a protein with both a zinc-binding motif and a G beta homologous domain."
    Deng X.-W., Matsui M., Wei N., Wagner D., Chu A.M., Feldmann K.A., Quail P.H.
    Cell 71:791-801(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Strain: cv. Columbia.
    Tissue: Seedling.
  2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: cv. Columbia.
  3. The Arabidopsis Information Resource (TAIR)
    Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases
    Cited for: GENOME REANNOTATION.
    Strain: cv. Columbia.
  4. "Arabidopsis ORF clones."
    Shinn P., Chen H., Kim C.J., Quinitio C., Ecker J.R.
    Submitted (MAY-2006) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: cv. Columbia.
  5. "Characterisation of exon skipping mutants of the COP1 gene from Arabidopsis."
    Simpson C.G., Mcquade C., Lyon J., Brown J.W.S.
    Plant J. 15:125-131(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 339-387 AND 506-594.
  6. "Genetic and molecular analysis of an allelic series of cop1 mutants suggests functional roles for the multiple protein domains."
    McNellis T.W., von Arnim A.G., Araki T., Komeda Y., Misera S., Deng X.-W.
    Plant Cell 6:487-500(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: CHARACTERIZATION, MUTANTS COP1-8 AND COP1-9.
  7. "A novel motif mediates the targeting of the Arabidopsis COP1 protein to subnuclear foci."
    Stacey M.G., von Arnim A.G.
    J. Biol. Chem. 274:27231-27236(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION.
  8. "Functional dissection of Arabidopsis COP1 reveals specific roles of its three structural modules in light control of seedling development."
    Torii K.U., McNellis T.W., Deng X.-W.
    EMBO J. 17:5577-5587(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION.
  9. "The RING finger motif of photomorphogenic repressor COP1 specifically interacts with the RING-H2 motif of a novel Arabidopsis protein."
    Torii K.U., Stoop-Myer C.D., Okamoto H., Coleman J.E., Matsui M., Deng X.-W.
    J. Biol. Chem. 274:27674-27681(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH CIP8.
    Tissue: Seedling.
  10. "Discrete domains mediate the light-responsive nuclear and cytoplasmic localization of Arabidopsis COP1."
    Stacey M.G., Hicks S.N., von Arnim A.G.
    Plant Cell 11:349-364(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION, MUTAGENESIS OF 294-ARG--LYS-296 AND 312-LYS--ARG-314.
  11. "The phytochrome A-specific signaling intermediate SPA1 interacts directly with COP1, a constitutive repressor of light signaling in Arabidopsis."
    Hoecker U., Quail P.H.
    J. Biol. Chem. 276:38173-38178(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: CHARACTERIZATION, INTERACTION WITH SPA1.
  12. "Identification of a structural motif that confers specific interaction with the WD40 repeat domain of Arabidopsis COP1."
    Holm M., Hardtke C.S., Gaudet R., Deng X.-W.
    EMBO J. 20:118-127(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH BBX24/STO AND BBX25/STH, MUTANTS COP1-4; COP1-8 AND COP1-9, MUTAGENESIS OF LYS-422; ARG-465; TRP-467; LYS-550 AND GLU-592.
    Tissue: Etiolated seedling.
  13. "Targeted destabilization of HY5 during light-regulated development of Arabidopsis."
    Osterlund M.T., Hardtke C.S., Wei N., Deng X.-W.
    Nature 405:462-466(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: UBIQUITINATION OF HY5.
  14. "Two interacting bZIP proteins are direct targets of COP1-mediated control of light-dependent gene expression in Arabidopsis."
    Holm M., Ma L.-G., Qu L.-J., Deng X.-W.
    Genes Dev. 16:1247-1259(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN DEGRADATION OF HYH.
  15. "AtMYB21, a gene encoding a flower-specific transcription factor, is regulated by COP1."
    Shin B., Choi G., Yi H., Yang S., Cho I., Kim J., Lee S., Paek N.-C., Kim J.-H., Song P.S., Choi G.
    Plant J. 30:23-32(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  16. "The COP1-SPA1 interaction defines a critical step in phytochrome A-mediated regulation of HY5 activity."
    Saijo Y., Sullivan J.A., Wang H., Yang J., Shen Y., Rubio V., Ma L., Hoecker U., Deng X.W.
    Genes Dev. 17:2642-2647(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH SPA1, UBIQUITINATION.
  17. "The SPA1-like proteins SPA3 and SPA4 repress photomorphogenesis in the light."
    Laubinger S., Hoecker U.
    Plant J. 35:373-385(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH SPA3 AND SPA4.
  18. "LAF1 ubiquitination by COP1 controls photomorphogenesis and is stimulated by SPA1."
    Seo H.S., Yang J.-Y., Ishikawa M., Bolle C., Ballesteros M.L., Chua N.-H.
    Nature 423:995-999(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: UBIQUITINATION, UBIQUITINATION OF LAF1, MUTAGENESIS OF CYS-52 AND CYS-55.
  19. "The SPA quartet: a family of WD-repeat proteins with a central role in suppression of photomorphogenesis in Arabidopsis."
    Laubinger S., Fittinghoff K., Hoecker U.
    Plant Cell 16:2293-2306(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH SPA2.
  20. "Arabidopsis COP10 forms a complex with DDB1 and DET1 in vivo and enhances the activity of ubiquitin conjugating enzymes."
    Yanagawa Y., Sullivan J.A., Komatsu S., Gusmaroli G., Suzuki G., Yin J., Ishibashi T., Saijo Y., Rubio V., Kimura S., Wang J., Deng X.-W.
    Genes Dev. 18:2172-2181(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH COP10.
  21. "Arabidopsis COP1/SPA1 complex and FHY1/FHY3 associate with distinct phosphorylated forms of phytochrome A in balancing light signaling."
    Saijo Y., Zhu D., Li J., Rubio V., Zhou Z., Shen Y., Hoecker U., Wang H., Deng X.W.
    Mol. Cell 31:607-613(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH SPA1 AND PHYA, UBIQUITINATION OF PHYA.
  22. "Characterization of Arabidopsis and rice DWD proteins and their roles as substrate receptors for CUL4-RING E3 ubiquitin ligases."
    Lee J.H., Terzaghi W., Gusmaroli G., Charron J.B., Yoon H.J., Chen H., He Y.J., Xiong Y., Deng X.W.
    Plant Cell 20:152-167(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: DWD MOTIF.
  23. "Interaction of COP1 and UVR8 regulates UV-B-induced photomorphogenesis and stress acclimation in Arabidopsis."
    Favory J.J., Stec A., Gruber H., Rizzini L., Oravecz A., Funk M., Albert A., Cloix C., Jenkins G.I., Oakeley E.J., Seidlitz H.K., Nagy F., Ulm R.
    EMBO J. 28:591-601(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH UVR8.
    Strain: cv. Wassilewskija.
  24. "Cryptochrome 2 and phototropin 2 regulate resistance protein-mediated viral defense by negatively regulating an E3 ubiquitin ligase."
    Jeong R.-D., Chandra-Shekara A.C., Barman S.R., Navarre D., Klessig D.F., Kachroo A., Kachroo P.
    Proc. Natl. Acad. Sci. U.S.A. 107:13538-13543(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH HRT/RPP8 AND CRY2.
  25. Cited for: INTERACTION WITH UVR8.

Entry informationi

Entry nameiCOP1_ARATH
AccessioniPrimary (citable) accession number: P43254
Secondary accession number(s): O23974
, O23975, O48770, Q1JPL6
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1995
Last sequence update: January 23, 2002
Last modified: June 8, 2016
This is version 158 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Miscellaneousi

Miscellaneous

Plants lacking COP1 are not viable.

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Arabidopsis thaliana
    Arabidopsis thaliana: entries and gene names
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.