AFfirm™ TLS/FUS Mouse Monoclonal Antibody - #BF8048
Product Info
*The optimal dilutions should be determined by the end user.
*Tips:
WB: For western blot detection of denatured protein samples. IHC: For immunohistochemical detection of paraffin sections (IHC-p) or frozen sections (IHC-f) of tissue samples. IF/ICC: For immunofluorescence detection of cell samples. ELISA(peptide): For ELISA detection of antigenic peptide.
Fold/Unfold
75 kDa DNA pairing protein; 75 kDa DNA-pairing protein; ALS6; Amyotrophic lateral sclerosis 6; fus; FUS CHOP; Fus like protein; FUS_HUMAN; FUS1; Fused in sarcoma; Fusion (involved in t(12;16) in malignant liposarcoma); Fusion derived from t(12;16) malignant liposarcoma; Fusion gene in myxoid liposarcoma; Heterogeneous nuclear ribonucleoprotein P2; hnRNP P2; hnRNPP2; Oncogene FUS; Oncogene TLS; POMp75; RNA binding protein FUS; RNA-binding protein FUS; TLS; TLS CHOP; Translocated in liposarcoma; Translocated in liposarcoma protein;
Immunogens
A synthesized peptide derived from human TLS/FUS, corresponding to a region within C-terminal amino acids.
- P35637 FUS_HUMAN:
- Protein BLAST With
- NCBI/
- ExPASy/
- Uniprot
MASNDYTQQATQSYGAYPTQPGQGYSQQSSQPYGQQSYSGYSQSTDTSGYGQSSYSSYGQSQNTGYGTQSTPQGYGSTGGYGSSQSSQSSYGQQSSYPGYGQQPAPSSTSGSYGSSSQSSSYGQPQSGSYSQQPSYGGQQQSYGQQQSYNPPQGYGQQNQYNSSSGGGGGGGGGGNYGQDQSSMSSGGGSGGGYGNQDQSGGGGSGGYGQQDRGGRGRGGSGGGGGGGGGGYNRSSGGYEPRGRGGGRGGRGGMGGSDRGGFNKFGGPRDQGSRHDSEQDNSDNNTIFVQGLGENVTIESVADYFKQIGIIKTNKKTGQPMINLYTDRETGKLKGEATVSFDDPPSAKAAIDWFDGKEFSGNPIKVSFATRRADFNRGGGNGRGGRGRGGPMGRGGYGGGGSGGGGRGGFPSGGGGGGGQQRAGDWKCPNPTCENMNFSWRNECNQCKAPKPDGPGGGPGGSHMGGNYGDDRRGGRGGYDRGGYRGRGGDRGGFRGGRGGGDRGGFGPGKMDSRGEHRQDRRERPY
PTMs - P35637 As Substrate
Site | PTM Type | Enzyme | Source |
---|---|---|---|
T7 | Phosphorylation | Uniprot | |
T11 | Phosphorylation | Uniprot | |
T19 | O-Glycosylation | Uniprot | |
T19 | Phosphorylation | Uniprot | |
S26 | Phosphorylation | P78527 (PRKDC) | Uniprot |
S30 | Phosphorylation | Uniprot | |
S42 | Phosphorylation | P78527 (PRKDC) , Q13315 (ATM) | Uniprot |
S54 | Phosphorylation | Uniprot | |
S61 | Phosphorylation | P78527 (PRKDC) | Uniprot |
T68 | Phosphorylation | Uniprot | |
S84 | Phosphorylation | P78527 (PRKDC) | Uniprot |
S87 | Phosphorylation | Uniprot | |
S112 | Phosphorylation | Uniprot | |
S117 | Phosphorylation | Uniprot | |
S131 | Phosphorylation | P78527 (PRKDC) | Uniprot |
S142 | Phosphorylation | Uniprot | |
R213 | Methylation | Uniprot | |
R216 | Methylation | Uniprot | |
R218 | Methylation | Uniprot | |
S221 | Phosphorylation | Uniprot | |
Y232 | Phosphorylation | Uniprot | |
R234 | Methylation | Uniprot | |
R242 | Methylation | Uniprot | |
R244 | Methylation | Uniprot | |
R248 | Methylation | Uniprot | |
R251 | Methylation | Uniprot | |
S257 | Phosphorylation | P05771-2 (PRKCB) | Uniprot |
R259 | Methylation | Uniprot | |
K264 | Ubiquitination | Uniprot | |
R269 | Methylation | Uniprot | |
S273 | Phosphorylation | Uniprot | |
S277 | Phosphorylation | Uniprot | |
T286 | Phosphorylation | Uniprot | |
K312 | Ubiquitination | Uniprot | |
K316 | Ubiquitination | Uniprot | |
T317 | Phosphorylation | Uniprot | |
Y325 | Phosphorylation | Uniprot | |
T326 | Phosphorylation | Uniprot | |
K332 | Acetylation | Uniprot | |
K334 | Ubiquitination | Uniprot | |
S340 | Phosphorylation | Uniprot | |
S346 | Phosphorylation | Uniprot | |
K348 | Sumoylation | Uniprot | |
K348 | Ubiquitination | Uniprot | |
K357 | Acetylation | Uniprot | |
K357 | Sumoylation | Uniprot | |
K357 | Ubiquitination | Uniprot | |
S360 | Phosphorylation | Uniprot | |
K365 | Methylation | Uniprot | |
K365 | Sumoylation | Uniprot | |
K365 | Ubiquitination | Uniprot | |
R371 | Methylation | Uniprot | |
R372 | Methylation | Uniprot | |
R377 | Methylation | Uniprot | |
R383 | Methylation | Uniprot | |
R386 | Methylation | Uniprot | |
R388 | Methylation | Uniprot | |
R394 | Methylation | Uniprot | |
Y397 | Phosphorylation | Uniprot | |
R407 | Methylation | Uniprot | |
S439 | Phosphorylation | Uniprot | |
K448 | Ubiquitination | Uniprot | |
S462 | Phosphorylation | Uniprot | |
Y468 | Phosphorylation | Uniprot | |
R473 | Methylation | Uniprot | |
R476 | Methylation | Uniprot | |
R481 | Methylation | Uniprot | |
R485 | Methylation | Uniprot | |
R487 | Methylation | Uniprot | |
R491 | Methylation | Uniprot | |
R495 | Methylation | Uniprot | |
R498 | Methylation | Uniprot | |
R503 | Methylation | Uniprot | |
R514 | Methylation | Uniprot | |
Y526 | Phosphorylation | P12931 (SRC) , P06241 (FYN) | Uniprot |
Research Backgrounds
DNA/RNA-binding protein that plays a role in various cellular processes such as transcription regulation, RNA splicing, RNA transport, DNA repair and damage response. Binds to nascent pre-mRNAs and acts as a molecular mediator between RNA polymerase II and U1 small nuclear ribonucleoprotein thereby coupling transcription and splicing. Binds also its own pre-mRNA and autoregulates its expression; this autoregulation mechanism is mediated by non-sense-mediated decay. Plays a role in DNA repair mechanisms by promoting D-loop formation and homologous recombination during DNA double-strand break repair. In neuronal cells, plays crucial roles in dendritic spine formation and stability, RNA transport, mRNA stability and synaptic homeostasis (By similarity).
Arg-216 and Arg-218 are dimethylated, probably to asymmetric dimethylarginine.
Phosphorylated in its N-terminal serine residues upon induced DNA damage. ATM and DNA-PK are able to phosphorylate FUS N-terminal region.
Nucleus.
Note: Displays a punctate pattern inside the nucleus and is excluded from nucleoli.
Ubiquitous.
Self-oligomerizes (via N-terminal region). Oligomerization is essential for chromatin binding. Component of nuclear riboprotein complexes. Interacts with ILF3, TDRD3 and SF1. Interacts through its C-terminus with SFRS13A. Interacts with OTUB1 and SARNP. Interacts with LRSAM1. Interacts with SAFB1 in a DNA-dependent manner; this interaction tethers FUS to chromatin. Interacts with MATR3. Interacts with SNRNP70 and POLR2A; these interactions couple RNA transcription and splicing. Interacts (through its RNA-binding domain) with RALY (through its RNA-binding domain); both are components of the same RNPs.
Belongs to the RRM TET family.
Research Fields
· Human Diseases > Cancers: Overview > Transcriptional misregulation in cancer.
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