Q9R1A8

PR
Gene name
Cop1
Protein name
E3 ubiquitin-protein ligase COP1
Names
Constitutive photomorphogenesis protein 1 homolog, mCOP1, RING finger and WD repeat domain protein 2, RING-type E3 ubiquitin transferase RFWD2
Species
Mus musculus (Mouse)
KEGG Pathway
mmu:26374
EC number
2.3.2.27: Aminoacyltransferases
Protein Class

Descriptions

The autoinhibited protein was predicted that may have potential autoinhibitory elements via cis-regPred.

Autoinhibitory domains (AIDs)

1-147 (Predicted disordered autoinhibitory region) PR

Target domain

Relief mechanism

Assay

cis-regPred

Accessory elements

No accessory elements

References

Autoinhibited structure

Activated structure

1 structures for Q9R1A8

Entry ID Method Resolution Chain Position Source
AF-Q9R1A8-F1 Predicted AlphaFoldDB

17 variants for Q9R1A8

Variant ID(s) Position Change Description Diseaes Association Provenance
rs229564281 84 V>A No EVA
rs229564281 84 V>G No EVA
rs581952882 90 R>W No EVA
rs3388509479 234 N>S No EVA
rs3388509478 332 E>* No EVA
rs3390714484 337 P>A No EVA
rs3390872240 337 P>R No EVA
rs3390796873 340 S>N No EVA
rs3388511644 441 A>D No EVA
rs3388508674 491 S>R No EVA
rs3388508678 502 G>V No EVA
rs3388510789 536 D>A No EVA
rs3390875861 580 H>Q No EVA
rs218422157 598 K>R No EVA
rs3388508665 626 L>M No EVA
rs3388507570 700 E>V No EVA
rs3388510786 715 S>P No EVA

No associated diseases with Q9R1A8

21 regional properties for Q9R1A8

Type Name Position InterPro Accession
repeat Leucine-rich repeat 81 - 148 IPR001611-1
repeat Leucine-rich repeat 150 - 172 IPR001611-2
repeat Leucine-rich repeat 173 - 195 IPR001611-3
repeat Leucine-rich repeat 196 - 263 IPR001611-4
repeat Leucine-rich repeat 264 - 333 IPR001611-5
repeat Leucine-rich repeat 449 - 506 IPR001611-6
repeat Leucine-rich repeat 517 - 575 IPR001611-7
repeat Leucine-rich repeat, typical subtype 80 - 101 IPR003591-1
repeat Leucine-rich repeat, typical subtype 102 - 124 IPR003591-2
repeat Leucine-rich repeat, typical subtype 125 - 147 IPR003591-3
repeat Leucine-rich repeat, typical subtype 148 - 170 IPR003591-4
repeat Leucine-rich repeat, typical subtype 171 - 193 IPR003591-5
repeat Leucine-rich repeat, typical subtype 194 - 217 IPR003591-6
repeat Leucine-rich repeat, typical subtype 240 - 262 IPR003591-7
repeat Leucine-rich repeat, typical subtype 286 - 308 IPR003591-8
repeat Leucine-rich repeat, typical subtype 309 - 330 IPR003591-9
repeat Leucine-rich repeat, typical subtype 332 - 355 IPR003591-10
repeat Leucine-rich repeat, typical subtype 449 - 469 IPR003591-11
repeat Leucine-rich repeat, typical subtype 470 - 492 IPR003591-12
repeat Leucine-rich repeat, typical subtype 493 - 516 IPR003591-13
repeat Leucine-rich repeat, typical subtype 540 - 563 IPR003591-14

Functions

Description
EC Number 2.3.2.27 Aminoacyltransferases
Subcellular Localization
  • Nucleus speckle
  • Cytoplasm
  • In the nucleus, it forms nuclear speckles
PANTHER Family
PANTHER Subfamily
PANTHER Protein Class
PANTHER Pathway Category No pathway information available

3 GO annotations of cellular component

Name Definition
Cul4A-RING E3 ubiquitin ligase complex A ubiquitin ligase complex in which a cullin from the Cul4A subfamily and a RING domain protein form the catalytic core; substrate specificity is conferred by an adaptor protein.
Golgi membrane The lipid bilayer surrounding any of the compartments of the Golgi apparatus.
nuclear speck A discrete extra-nucleolar subnuclear domain, 20-50 in number, in which splicing factors are seen to be localized by immunofluorescence microscopy.

2 GO annotations of molecular function

Name Definition
metal ion binding Binding to a metal ion.
ubiquitin protein ligase activity Catalysis of the transfer of ubiquitin to a substrate protein via the reaction X-ubiquitin + S -> X + S-ubiquitin, where X is either an E2 or E3 enzyme, the X-ubiquitin linkage is a thioester bond, and the S-ubiquitin linkage is an amide bond: an isopeptide bond between the C-terminal glycine of ubiquitin and the epsilon-amino group of lysine residues in the substrate or, in the linear extension of ubiquitin chains, a peptide bond the between the C-terminal glycine and N-terminal methionine of ubiquitin residues.

3 GO annotations of biological process

Name Definition
positive regulation of proteasomal ubiquitin-dependent protein catabolic process Any process that activates or increases the frequency, rate or extent of the breakdown of a protein or peptide by hydrolysis of its peptide bonds, initiated by the covalent attachment of ubiquitin, and mediated by the proteasome.
proteasome-mediated ubiquitin-dependent protein catabolic process The chemical reactions and pathways resulting in the breakdown of a protein or peptide by hydrolysis of its peptide bonds, initiated by the covalent attachment of ubiquitin, and mediated by the proteasome.
response to ionizing radiation Any process that results in a change in state or activity of a cell or an organism (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of a ionizing radiation stimulus. Ionizing radiation is radiation with sufficient energy to remove electrons from atoms and may arise from spontaneous decay of unstable isotopes, resulting in alpha and beta particles and gamma rays. Ionizing radiation also includes X-rays.

2 homologous proteins in AiPD

UniProt AC Gene Name Protein Name Species Evidence Code
Q8NHY2 COP1 E3 ubiquitin-protein ligase COP1 Homo sapiens (Human) PR
Q9T014 SPA2 Protein SPA1-RELATED 2 Arabidopsis thaliana (Mouse-ear cress) PR
10 20 30 40 50 60
MSGSRQAGSG SAGTSPGSSA ASSVTSASSS LSSSPSPPSV AASAATLVSG GVAPAAGSGG
70 80 90 100 110 120
LGGPGRPVLV AAAVSGSASA GGAVSAGQSR LSCAARPSAG VGGSSSSLGS SSRKRPLLVP
130 140 150 160 170 180
LCNGLLNSYE DKSNDFVCPI CFDMIEEAYM TKCGHSFCYK CIHQSLEDNN RCPKCNYVVD
190 200 210 220 230 240
NIDHLYPNFL VNELILKQKQ RFEEKRFKLD HSVSSTNGHR WQIFQDLLGT DQDNLDLANV
250 260 270 280 290 300
NLMLELLVQK KKQLEAESHA AQLQILMEFL KVARRNKREQ LEQIQKELSV LEEDIKRVEE
310 320 330 340 350 360
MSGLYSPVSE DSTVPQFEAP SPSHSSIIDS TEYSQPPGFS GTSQTKKQPW YNSTLASRRK
370 380 390 400 410 420
RLTAHFEDLE QCYFSTRMSR ISDDSRTASQ LDEFQECLSK FTRYNSVRPL ATLSYASDLY
430 440 450 460 470 480
NGSSIVSSIE FDRDCDYFAI AGVTKKIKVY EYGTVIQDAV DIHYPENEMT CNSKISCISW
490 500 510 520 530 540
SSYHKNLLAS SDYEGTVILW DGFTGQRSKV YQEHEKRCWS VDFNLMDPKL LASGSDDAKV
550 560 570 580 590 600
KLWSTNLDNS VASIEAKANV CCVKFSPSSR YHLAFGCADH CVHYYDLRNT KQPIMVFKGH
610 620 630 640 650 660
RKAVSYAKFV SGEEIVSAST DSQLKLWNVG KPYCLRSFKG HINEKNFVGL ASNGDYIACG
670 680 690 700 710 720
SENNSLYLYY KGLSKTLLTF KFDTVKSVLD KDRKEDDTNE FVSAVCWRAL SDGESNVLIA
730
ANSQGTIKVL ELV