UHRF2
E3 ubiquitin-protein ligase UHRF2
Also known as: MGC33463, NIRF, RNF107, TDRD23, UHRF2_HUMAN, URF2
Cross-references: UniProt · Ensembl · Human Protein Atlas · GeneCards · NCBI Gene
Protein identityUniProt · HPA
- UniProt accession
- Q96PU4
- Gene
- UHRF2
- Ensembl
- ENSG00000147854
- Chromosome
- 9
- Canonical length
- 802 aa
- Protein class
- Disease related genes, Enzymes, Metabolic proteins, Potential drug targets, Predicted intracellular proteins
- Subcellular location
- Nucleoplasm
- Quaternary structure
- Homodimer
OverviewNCBI Gene
This gene encodes a nuclear protein which is involved in cell-cycle regulation. The encoded protein is a ubiquitin-ligase capable of ubiquinating PCNP (PEST-containing nuclear protein), and together they may play a role in tumorigenesis. The encoded protein contains an NIRF_N domain, a PHD finger, a set- and ring-associated (SRA) domain, and a RING finger domain and several of these domains have been shown to be essential for the regulation of cell proliferation. This protein may also have a role in intranuclear degradation of polyglutamine aggregates. Alternative splicing results in multiple transcript variants some of which are non-protein coding. [provided by RefSeq, Feb 2012]
Canonical amino-acid sequenceUniProt
802 residues, UniProt reviewed canonical sequence.
>Q96PU4|UHRF2
1 MWIQVRTIDG SKTCTIEDVS RKATIEELRE RVWALFDVRP ECQRLFYRGK QLENGYTLFD
61 YDVGLNDIIQ LLVRPDPDHL PGTSTQIEAK PCSNSPPKVK KAPRVGPSNQ PSTSARARLI
121 DPGFGIYKVN ELVDARDVGL GAWFEAHIHS VTRASDGQSR GKTPLKNGSS CKRTNGNIKH
181 KSKENTNKLD SVPSTSNSDC VAADEDVIYH IQYDEYPESG TLEMNVKDLR PRARTILKWN
241 ELNVGDVVMV NYNVESPGQR GFWFDAEITT LKTISRTKKE LRVKIFLGGS EGTLNDCKII
301 SVDEIFKIER PGAHPLSFAD GKFLRRNDPE CDLCGGDPEK KCHSCSCRVC GGKHEPNMQL
361 LCDECNVAYH IYCLNPPLDK VPEEEYWYCP SCKTDSSEVV KAGERLKMSK KKAKMPSAST
421 ESRRDWGRGM ACVGRTRECT IVPSNHYGPI PGIPVGSTWR FRVQVSEAGV HRPHVGGIHG
481 RSNDGAYSLV LAGGFADEVD RGDEFTYTGS GGKNLAGNKR IGAPSADQTL TNMNRALALN
541 CDAPLDDKIG AESRNWRAGK PVRVIRSFKG RKISKYAPEE GNRYDGIYKV VKYWPEISSS
601 HGFLVWRYLL RRDDVEPAPW TSEGIERSRR LCLRLQYPAG YPSDKEGKKP KGQSKKQPSG
661 TTKRPISDDD CPSASKVYKA SDSAEAIEAF QLTPQQQHLI REDCQNQKLW DEVLSHLVEG
721 PNFLKKLEQS FMCVCCQELV YQPVTTECFH NVCKDCLQRS FKAQVFSCPA CRHDLGQNYI
781 MIPNEILQTL LDLFFPGYSK GRLocalizationUniProt · AlphaFold · HPA
Whether an antibody against UHRF2 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
- Intracellular
- Secreted
- No
- Transmembrane segments
- 0
- Mean surface accessibility (rSASA)
- 0.37
- Highest tissue expression
- 42 nTPM
Expression across tissuesHPA
Tissue
- bone marrow: 42 nTPM
- thymus: 20 nTPM
- lymph node: 16 nTPM
- tonsil: 16 nTPM
- prostate: 14 nTPM
- smooth muscle: 13 nTPM
Single-cell type
- neutrophil progenitors: 376 nCPM
- monocyte progenitors: 161 nCPM
- lymphatic endothelial cells: 140 nCPM
- b-cells: 136 nCPM
- t-cells: 132 nCPM
- prostatic glandular cells: 124 nCPM
Immune cell
- basophil: 4 nTPM
- naive B-cell: 2.9 nTPM
- eosinophil: 2.7 nTPM
- T-reg: 1.9 nTPM
- memory B-cell: 1.8 nTPM
- memory CD4 T-cell: 1.8 nTPM
Brain region
- cerebellum: 33 nTPM
- white matter: 31 nTPM
- choroid plexus: 24 nTPM
- thalamus: 24 nTPM
- basal ganglia: 23 nTPM
- cerebral cortex: 22 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)
- 0.25
- gnomAD pLI
- 1
- gnomAD missense Z
- 3.32
- DepMap mean gene effect
- -0.01
- DepMap dependency class
- none
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
- cell differentiation
- negative regulation of gene expression via chromosomal CpG island methylation
- protein autoubiquitination
- protein sumoylation
- protein ubiquitination
- regulation of cell cycle
- regulation of transcription by RNA polymerase II
Molecular functions
- DNA binding
- histone binding
- histone H3K9me2/3 reader activity
- RNA polymerase II-specific DNA-binding transcription factor binding
- SUMO transferase activity
- ubiquitin protein ligase activity
- ubiquitin-protein transferase activity
- zinc ion binding
Cellular components
Protein domainsUniProt · Pfam · InterPro
- Ubiquitin-like domain
- Zinc finger, RING-type
- Zinc finger, PHD-type
- SRA-YDG
- Zinc finger, FYVE/PHD-type
- Zinc finger, RING/FYVE/PHD-type
- PUA-like superfamily
- Zinc finger, RING-type, conserved site
- Zinc finger, PHD-finger
- UHRF1, tandem tudor domain
- Ubiquitin-like domain superfamily
- SRA-YDG superfamily
- UHRF1/2-like
- Ubiquitin family
- PHD-finger
- SAD/SRA domain
- Tandem tudor domain within UHRF1
- E3 ubiquitin-protein ligase UHRF2, first Tudor domain
- E3 ubiquitin-protein ligase UHRF2, RING finger, HC subclass
- E3 ubiquitin-protein ligase UHRF2, PHD finger
- E3 ubiquitin-protein ligase UHRF2, ubiquitin-like domain
KeywordsUniProt
InteractionsUniProt · HPA
Protein binding partners of UHRF2 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 UHRF2 as an antibody target. Whether an autoantibody or antibody against UHRF2 could matter depends on whether native UHRF2 is physically reachable, whether the body needs it intact, and whether it acts in a disease-relevant tissue.
UHRF2 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 UHRF2 as an autoantigen. Seroatlas presents hypothesis context only and does not manufacture a known-serology claim.
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