STAU2
Double-stranded RNA-binding protein Staufen homolog 2
Also known as: 39K2, STAU2_HUMAN
Cross-references: UniProt · Ensembl · Human Protein Atlas · GeneCards · NCBI Gene
Protein identityUniProt · HPA
- UniProt accession
- Q9NUL3
- Gene
- STAU2
- Ensembl
- ENSG00000040341
- Chromosome
- 8
- Canonical length
- 570 aa
- Protein class
- Predicted intracellular proteins
- Subcellular location
- Nucleoplasm,Cytosol
OverviewNCBI Gene
Staufen homolog 2 is a member of the family of double-stranded RNA (dsRNA)-binding proteins involved in the transport and/or localization of mRNAs to different subcellular compartments and/or organelles. These proteins are characterized by the presence of multiple dsRNA-binding domains which are required to bind RNAs having double-stranded secondary structures. Staufen homolog 2 shares 48.5% and 59.9% similarity with drosophila and human staufen, respectively. The exact function of Staufen homolog 2 is not known, but since it contains 3 copies of conserved dsRNA binding domain, it could be involved in double-stranded RNA binding events. Several transcript variants encoding different isoforms have been found for this gene. [provided by RefSeq, Aug 2009]
Canonical amino-acid sequenceUniProt
570 residues, UniProt reviewed canonical sequence.
>Q9NUL3|STAU2
1 MANPKEKTAM CLVNELARFN RVQPQYKLLN ERGPAHSKMF SVQLSLGEQT WESEGSSIKK
61 AQQAVANKAL TESTLPKPVQ KPPKSNVNNN PGSITPTVEL NGLAMKRGEP AIYRPLDPKP
121 FPNYRANYNF RGMYNQRYHC PVPKIFYVQL TVGNNEFFGE GKTRQAARHN AAMKALQALQ
181 NEPIPERSPQ NGESGKDVDD DKDANKSEIS LVFEIALKRN MPVSFEVIKE SGPPHMKSFV
241 TRVSVGEFSA EGEGNSKKLS KKRAATTVLQ ELKKLPPLPV VEKPKLFFKK RPKTIVKAGP
301 EYGQGMNPIS RLAQIQQAKK EKEPDYVLLS ERGMPRRREF VMQVKVGNEV ATGTGPNKKI
361 AKKNAAEAML LQLGYKASTN LQDQLEKTGE NKGWSGPKPG FPEPTNNTPK GILHLSPDVY
421 QEMEASRHKV ISGTTLGYLS PKDMNQPSSS FFSISPTSNS SATIARELLM NGTSSTAEAI
481 GLKGSSPTPP CSPVQPSKQL EYLARIQGFQ AALSALKQFS EQGLDPIDGA MNIEKGSLEK
541 QAKHLREKAD NNQAPPGSIA QDCKKSNSAVLocalizationUniProt · AlphaFold · HPA
Whether an antibody against STAU2 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)
- 0.49
- Highest tissue expression
- 104 nTPM
Expression across tissuesHPA
Tissue
- skeletal muscle: 104 nTPM
- tongue: 103 nTPM
- heart muscle: 66 nTPM
- cerebral cortex: 54 nTPM
- esophagus: 33 nTPM
- thymus: 33 nTPM
Single-cell type
- choroid plexus epithelial cells: 374 nCPM
- brain excitatory neurons: 344 nCPM
- myonuclei: 319 nCPM
- brain inhibitory neurons: 312 nCPM
- other brain neurons: 287 nCPM
- neutrophil progenitors: 285 nCPM
Immune cell
- NK-cell: 45 nTPM
- eosinophil: 43 nTPM
- neutrophil: 31 nTPM
- gdT-cell: 29 nTPM
- T-reg: 26 nTPM
- plasmacytoid DC: 25 nTPM
Brain region
- cerebral cortex: 129 nTPM
- cerebellum: 122 nTPM
- white matter: 120 nTPM
- basal ganglia: 108 nTPM
- midbrain: 106 nTPM
- medulla oblongata: 103 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)
- 0.32
- gnomAD pLI
- 0.97
- gnomAD missense Z
- 1.42
- DepMap mean gene effect
- -0.05
- DepMap dependency class
- none
Cancer expressionTCGA
Across TCGA tumor cohorts, this protein is over-expressed in roughly 13% of surveyed tumor types (aggregate summary; per-cohort expression, alteration, and survival load in the interactive view).
OntologyGO
Biological processes
- anterograde dendritic transport of messenger ribonucleoprotein complex
- cellular response to oxidative stress
- eye morphogenesis
- germ cell development
- intracellular mRNA localization
- positive regulation of dendritic spine morphogenesis
- positive regulation of long-term synaptic depression
- positive regulation of synapse assembly
- protein localization to synapse
- regulation of actin cytoskeleton organization
- regulation of filopodium assembly
Molecular functions
- double-stranded RNA binding
- Hsp70 protein binding
- kinesin binding
- mitogen-activated protein kinase binding
- mRNA binding
- ribosome binding
- RNA binding
Cellular components
Protein domainsUniProt · Pfam · InterPro
- Double-stranded RNA-binding domain
- Staufen, C-terminal
- Double-stranded RNA-binding domain-containing protein
- Double-stranded RNA binding motif
- Staufen C-terminal domain
- Staufen 2, second double-stranded RNA binding domain
- Staufen 2, third double-stranded RNA binding domain
- Staufen 2, fourth double-stranded RNA binding domain
KeywordsUniProt
InteractionsUniProt · HPA
Protein binding partners of STAU2 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 STAU2 as an antibody target. Whether an autoantibody or antibody against STAU2 could matter depends on whether native STAU2 is physically reachable, whether the body needs it intact, and whether it acts in a disease-relevant tissue.
STAU2 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 STAU2 as an autoantigen. Seroatlas presents hypothesis context only and does not manufacture a known-serology claim.
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