UFL1
E3 UFM1-protein ligase 1
Also known as: KIAA0776, Maxer, NLBP, RCAD, UFL1_HUMAN
Cross-references: UniProt · Ensembl · Human Protein Atlas · GeneCards · NCBI Gene
Protein identityUniProt · HPA
- UniProt accession
- O94874
- Gene
- UFL1
- Ensembl
- ENSG00000014123
- Chromosome
- 6
- Canonical length
- 794 aa
- Protein class
- Predicted intracellular proteins
- Subcellular location
- Endoplasmic reticulum
OverviewNCBI Gene
Enables UFM1 ligase activity and protein kinase binding activity. Involved in several processes, including positive regulation of reticulophagy; regulation of intracellular signal transduction; and regulation of primary metabolic process. Acts upstream of or within several processes, including positive regulation of cell population proliferation; regulation of proteasomal ubiquitin-dependent protein catabolic process; and response to endoplasmic reticulum stress. Located in cytoplasm; nucleus; and site of double-strand break. Part of protein-containing complex. Is active in endoplasmic reticulum membrane and mitochondrial outer membrane. [provided by Alliance of Genome Resources, Jul 2025]
Canonical amino-acid sequenceUniProt
794 residues, UniProt reviewed canonical sequence.
>O94874|UFL1
1 MADAWEEIRR LAADFQRAQF AEATQRLSER NCIEIVNKLI AQKQLEVVHT LDGKEYITPA
61 QISKEMRDEL HVRGGRVNIV DLQQVINVDL IHIENRIGDI IKSEKHVQLV LGQLIDENYL
121 DRLAEEVNDK LQESGQVTIS ELCKTYDLPG NFLTQALTQR LGRIISGHID LDNRGVIFTE
181 AFVARHKARI RGLFSAITRP TAVNSLISKY GFQEQLLYSV LEELVNSGRL RGTVVGGRQD
241 KAVFVPDIYS RTQSTWVDSF FRQNGYLEFD ALSRLGIPDA VSYIKKRYKT TQLLFLKAAC
301 VGQGLVDQVE ASVEEAISSG TWVDIAPLLP TSLSVEDAAI LLQQVMRAFS KQASTVVFSD
361 TVVVSEKFIN DCTELFRELM HQKAEKEMKN NPVHLITEED LKQISTLESV STSKKDKKDE
421 RRRKATEGSG SMRGGGGGNA REYKIKKVKK KGRKDDDSDD ESQSSHTGKK KPEISFMFQD
481 EIEDFLRKHI QDAPEEFISE LAEYLIKPLN KTYLEVVRSV FMSSTTSASG TGRKRTIKDL
541 QEEVSNLYNN IRLFEKGMKF FADDTQAALT KHLLKSVCTD ITNLIFNFLA SDLMMAVDDP
601 AAITSEIRKK ILSKLSEETK VALTKLHNSL NEKSIEDFIS CLDSAAEACD IMVKRGDKKR
661 ERQILFQHRQ ALAEQLKVTE DPALILHLTS VLLFQFSTHS MLHAPGRCVP QIIAFLNSKI
721 PEDQHALLVK YQGLVVKQLV SQSKKTGQGD YPLNNELDKE QEDVASTTRK ELQELSSSIK
781 DLVLKSRKSS VTEELocalizationUniProt · AlphaFold · HPA
Whether an antibody against UFL1 can act on the native protein depends on physical access: surface and secreted proteins are reachable by circulating antibodies, intracellular proteins usually are not.
- Antibody reachability
- Other membrane
- Secreted
- No
- Transmembrane segments
- 0
- Mean surface accessibility (rSASA)
- 0.35
- Highest tissue expression
- 29 nTPM
Expression across tissuesHPA
Tissue
- retina: 29 nTPM
- liver: 28 nTPM
- thyroid gland: 26 nTPM
- pancreas: 24 nTPM
- parathyroid gland: 24 nTPM
- prostate: 23 nTPM
Single-cell type
- corticotrophs: 144 nCPM
- syncytiotrophoblasts: 144 nCPM
- pancreatic acinar cells: 135 nCPM
- esophageal apical cells: 130 nCPM
- plasma cells: 126 nCPM
- epididymal principal cells: 121 nCPM
Immune cell
- NK-cell: 13 nTPM
- naive CD4 T-cell: 11 nTPM
- T-reg: 11 nTPM
- plasmacytoid DC: 11 nTPM
- non-classical monocyte: 10 nTPM
- myeloid DC: 10 nTPM
Brain region
- white matter: 40 nTPM
- medulla oblongata: 32 nTPM
- basal ganglia: 27 nTPM
- spinal cord: 26 nTPM
- hypothalamus: 26 nTPM
- cerebellum: 25 nTPM
Genetic constraint and essentialitygnomAD · DepMap
Does the body need this protein intact? Low LOEUF or a strong DepMap dependency means loss or blockade of the protein is likely to be felt.
- gnomAD LOEUF (loss-of-function intolerance)
- 0.84
- gnomAD pLI
- 0
- gnomAD missense Z
- 0.19
- DepMap mean gene effect
- -0.37
- DepMap dependency class
- selective
Cancer expressionTCGA
Across TCGA tumor cohorts, this protein is over-expressed in roughly 3% of surveyed tumor types (aggregate summary; per-cohort expression, alteration, and survival load in the interactive view).
OntologyGO
Biological processes
- DNA damage checkpoint signaling
- DNA damage response
- DNA repair
- erythrocyte differentiation
- hematopoietic stem cell differentiation
- negative regulation of IRE1-mediated unfolded protein response
- negative regulation of NF-kappaB transcription factor activity
- negative regulation of protein ubiquitination
- negative regulation of T cell activation
- negative regulation of T cell mediated immune response to tumor cell
- osteoblast differentiation
- positive regulation of autophagy
- positive regulation of cell population proliferation
- positive regulation of glial cell proliferation
- positive regulation of proteolysis involved in protein catabolic process
- positive regulation of reticulophagy
- protein K69-linked ufmylation
- protein stabilization
- protein ufmylation
- regulation of canonical NF-kappaB signal transduction
- regulation of inflammatory response
- regulation of intracellular estrogen receptor signaling pathway
- regulation of proteasomal ubiquitin-dependent protein catabolic process
- regulation of protein localization
- rescue of stalled ribosome
- response to endoplasmic reticulum stress
- response to L-glutamate
- reticulophagy
- ribosome disassembly
Molecular functions
- protein kinase binding
- UFM1 transferase activity
- UFM1 ligase activity
Cellular components
Protein domainsUniProt · Pfam · InterPro
- E3 UFM1-protein ligase 1
- E3 UFM1-protein ligase 1-like, N-terminal
- E3 UFM1-protein ligase 1-like domain
- E3 UFM1-protein ligase-like, C-terminal domain
- E3 UFM1-protein ligase 1
- E3 UFM1-protein ligase 1-like domain
- E3 UFM1-protein ligase 1 C-terminal domain
- Winged helix-turn-helix domain 5 in UFL1 protein
KeywordsUniProt
InteractionsUniProt · HPA
Protein binding partners of UFL1 in the human serome: UniProt-annotated complex subunits plus reported interactors. Each links to its own Seroatlas record.
Antibody and autoantibody relevanceSeroatlas analysis
Seroatlas reads UFL1 as an antibody target. Whether an autoantibody or antibody against UFL1 could matter depends on whether native UFL1 is physically reachable, whether the body needs it intact, and whether it acts in a disease-relevant tissue.
UFL1 is annotated as predominantly intracellular. Intracellular proteins are common autoantibody markers, becoming visible to the immune system after cell injury or altered processing, but are usually markers of disease rather than direct drivers.
Annotation status
The present source text does not explicitly label UFL1 as an autoantigen. Seroatlas presents hypothesis context only and does not manufacture a known-serology claim.
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