Ddrgk1
entrez
77006
canonical
uniprot
Q80WW9
canonical
ensembl
ENSMUSG00000068290
resolver
ensp
ENSMUSP00000086988
resolver
enst
ENSMUST00000089559
resolver
genesymbol
Ddrgk1
resolver
genesymbol_syn
Ufbp1
resolver
uniprot
Q14BT4
resolver
uniprot
Q9CT52
resolver
uniprot_entry
DDRGK_MOUSE
resolver
uniprot_sec
Q14BT4
resolver
uniprot_sec
Q9CT52
resolver
amino_acid_sequence
MVGPWVYLVAAVLLIGLILFLTRSRGRAAAADGEPLHNEEERAGAGQVGRSLPQESEEQRTGSRPRRRRDLGSRLQAQRRAQRVAWEDGDENVGQTVIPAQEEEGIEKPAEVHPTGKIGAKKLRKLEEKQARKAQREAEEAEREERKRLESQREAEWKKEEERLRLKEEQKEEEERKAQEEQARREHEEYLKLKEAFVVEEEGVSETMTEEQSHSFLTEFINYIKKSKVVLLEDLAFQMGLRTQDAINRIQDLLTEGTLTGVIDDRGKFIYITPEELAAVANFIRQRGRVSITELAQASNSLISWGQDLPAQASA
uniprot
proteins
function
FUNCTION: Component of the UFM1 ribosome E3 ligase (UREL) complex, a multiprotein complex that catalyzes ufmylation of endoplasmic reticulum-docked proteins (PubMed:30701081, PubMed:37795761). The UREL complex plays a key role in ribosome recycling by mediating mono-ufmylation of the RPL26/uL24 subunit of the 60S ribosome following ribosome dissociation: ufmylation weakens the junction between post-termination 60S subunits and SEC61 translocons, promoting release and recycling of the large ribosomal subunit from the endoplasmic reticulum membrane (By similarity). Ufmylation of RPL26/uL24 and subsequent 60S ribosome recycling either take place after normal termination of translation or after ribosome stalling during cotranslational translocation at the endoplasmic reticulum (By similarity). Within the UREL complex, DDRGK1 tethers the complex to the endoplasmic reticulum membrane to restrict its activity to endoplasmic reticulum-docked ribosomes and acts as an ufmylation 'reader': following RPL26/uL24 ufmylation, DDRGK1 specifically binds to ufmylated RPL26/uL24 via its UFIM motif, resulting in stable association between the 60S ribosome and the UREL complex, followed by dissociation of the 60S ribosome subunit from the endoplasmic reticulum membrane (By similarity). The UREL complex is also involved in reticulophagy in response to endoplasmic reticulum stress by promoting ufmylation of proteins such as CYB5R3 and RPN1, thereby promoting lysosomal degradation of ufmylated proteins (By similarity). Ufmylation-dependent reticulophagy inhibits the unfolded protein response (UPR) by regulating ERN1/IRE1-alpha stability (PubMed:28128204). Acts as a regulator of immunity by promoting differentiation of B-cells into plasma cells: acts by promoting expansion of the endoplasmic reticulum and regulating the unfolded protein response (UPR) (PubMed:30842412). May also be required for TRIP4 ufmylation (By similarity). May play a role in NF-kappa-B-mediated transcription through regulation of the phosphorylation and the degradation of NFKBIA, the inhibitor of NF-kappa-B (PubMed:28263186). Plays a role in cartilage development through SOX9, inhibiting the ubiquitin-mediated proteasomal degradation of this transcriptional regulator (PubMed:28263186). Required for stabilization and ufmylation of ATG9A (PubMed:37086384). {ECO:0000250|UniProtKB:Q96HY6, ECO:0000269|PubMed:28128204, ECO:0000269|PubMed:28263186, ECO:0000269|PubMed:30701081, ECO:0000269|PubMed:30842412, ECO:0000269|PubMed:37086384, ECO:0000269|PubMed:37795761}.
uniprot
proteins
mass_dalton
35977
uniprot
proteins
post_translational_modification
PTM: Ufmylated; conjugated to ubiquitin-like protein UFM1, probably at Lys-268 by UFL1 (PubMed:21494687). The relevance of ufmylation is however unclear: as DDRGK1 acts as a substrate adapter for ufmylation, it is uncertain whether ufmylation is a collateral effect of the ufmylation process or whether it is required to regulate its activity (By similarity). {ECO:0000250|UniProtKB:Q96HY6, ECO:0000269|PubMed:21494687}.; PTM: Ubiquitinated. Ubiquitination probably triggers proteasomal degradation and is negatively regulated by UFL1, the enzyme involved in the ufmylation of DDRGK1. {ECO:0000250|UniProtKB:Q96HY6}.
uniprot
proteins
protein_family
DDRGK1 family
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
16141072
uniprot
proteins
pubmed
19468303
uniprot
proteins
pubmed
20228063
uniprot
proteins
pubmed
21183079
uniprot
proteins
pubmed
21494687
uniprot
proteins
pubmed
26544067
uniprot
proteins
pubmed
28128204
uniprot
proteins
pubmed
28263186
uniprot
proteins
pubmed
30701081
uniprot
proteins
pubmed
30842412
uniprot
proteins
pubmed
37086384
uniprot
proteins
pubmed
37795761
uniprot
proteins
sequence_length
315
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000269|PubMed:37795761}; Single-pass membrane protein {ECO:0000250|UniProtKB:Q96HY6}.
uniprot
proteins
transmembrane_region
TRANSMEM 1..28; /note="Helical"; /evidence="ECO:0000250|UniProtKB:Q96HY6
uniprot
proteins