Structure of PDB 8oj8 Chain A
Receptor sequence
>8oj8A (length=474) Species:
9606
(Homo sapiens) [
Search protein sequence
]
DIYSRTQSTWVDSFFRQNGYLEFDALSRLGIPDAVSYIKKRYKTTQLLFL
KAACVGQGLVDQVEASVEEAISSGTWVDIAPLLPTSLSVEDAAILLQQVM
RAFSKQASTVVFSDTVVVSEKFINDCTELFRELMHQKAEKEMKDKKDERR
RKATEGSGSMRGGGGGNAREYKIKKVQDEIEDFLRKHIQDAPEEFISELA
EYLIKPLNKTYLEVVRSVFMSSTTSASGTGRKRTIKDLQEEVSNLYNNIR
LFEKGMKFFADDTQAALTKHLLKSVCTDITNLIFNFLASDLMMAVDDPAA
ITSEIRKKILSKLSEETKVALTKLHNSLNEKSIEDFISCLDSAAEACDIM
VKRGDKKRERQILFQHRQALAEQLKVTEDPALILHLTSVLLFQFSTHSML
HAPGRCVPQIIAFLNSKIPEDQHALLVKYQGLVVKQLVSQSKKTGLDKEQ
EDVASTTRKELQELSSSIKDLVLK
3D structure
PDB
8oj8
UFM1 E3 ligase promotes recycling of 60S ribosomal subunits from the ER
Chain
A
Resolution
3.3 Å
3D
structure
[
Spin on
]
[
Spin off
]
[
Reset orientation
]
[
High quality
]
[
Low quality
]
[
White background
]
[
Black background
]
[
Download
]
[
Download structure with residue number starting from 1
]
Enzymatic activity
Enzyme Commision number
2.3.2.-
Interaction with ligand
Site
#
Ligand
Ligand
chain
Binding residues on receptor
(original residue number in PDB)
Binding residues on receptor
(residue number reindexed from 1)
Binding affinity
BS01
rna
A
K417 K418 R421 R422 K424 G428 G430 R433 G434 G436 G437 G438 N439 A440 R441 E442 Y443 K444 I445 K446 K447 K534 K575 D657 K658 K659 R662 Q663 F666 Q667
K145 K146 R149 R150 K152 G156 G158 R161 G162 G164 G165 G166 N167 A168 R169 E170 Y171 K172 I173 K174 K175 K232 K273 D355 K356 K357 R360 Q361 F364 Q365
Gene Ontology
Molecular Function
GO:0005515
protein binding
GO:0016740
transferase activity
GO:0019901
protein kinase binding
GO:0061666
UFM1 ligase activity
GO:0071568
UFM1 transferase activity
Biological Process
GO:0000077
DNA damage checkpoint signaling
GO:0001649
osteoblast differentiation
GO:0002841
negative regulation of T cell mediated immune response to tumor cell
GO:0006281
DNA repair
GO:0006974
DNA damage response
GO:0008284
positive regulation of cell population proliferation
GO:0010468
regulation of gene expression
GO:0010508
positive regulation of autophagy
GO:0030218
erythrocyte differentiation
GO:0031397
negative regulation of protein ubiquitination
GO:0032088
negative regulation of NF-kappaB transcription factor activity
GO:0032434
regulation of proteasomal ubiquitin-dependent protein catabolic process
GO:0032790
ribosome disassembly
GO:0032880
regulation of protein localization
GO:0033146
regulation of intracellular estrogen receptor signaling pathway
GO:0034976
response to endoplasmic reticulum stress
GO:0043066
negative regulation of apoptotic process
GO:0043122
regulation of canonical NF-kappaB signal transduction
GO:0050727
regulation of inflammatory response
GO:0050821
protein stabilization
GO:0050868
negative regulation of T cell activation
GO:0060218
hematopoietic stem cell differentiation
GO:0060252
positive regulation of glial cell proliferation
GO:0061709
reticulophagy
GO:0071569
protein ufmylation
GO:0072344
rescue of stalled ribosome
GO:0140501
positive regulation of reticulophagy
GO:1902065
response to L-glutamate
GO:1903052
positive regulation of proteolysis involved in protein catabolic process
GO:1903895
negative regulation of IRE1-mediated unfolded protein response
GO:1990592
protein K69-linked ufmylation
Cellular Component
GO:0005634
nucleus
GO:0005694
chromosome
GO:0005737
cytoplasm
GO:0005741
mitochondrial outer membrane
GO:0005783
endoplasmic reticulum
GO:0005789
endoplasmic reticulum membrane
GO:0005829
cytosol
GO:0016020
membrane
GO:0032991
protein-containing complex
GO:0035861
site of double-strand break
GO:0043005
neuron projection
View graph for
Molecular Function
View graph for
Biological Process
View graph for
Cellular Component
External links
PDB
RCSB:8oj8
,
PDBe:8oj8
,
PDBj:8oj8
PDBsum
8oj8
PubMed
38383785
UniProt
O94874
|UFL1_HUMAN E3 UFM1-protein ligase 1 (Gene Name=UFL1)
[
Back to BioLiP
]