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Protein Page:
hnRNP P2 (human)
p Phosphorylation
a Acetylation
m Methylation
m1 Mono-methylation
m2 Di-methylation
m3 Tri-methylation
u Ubiquitination
s Sumoylation
n Neddylation
g O-GlcNAc
h Palmitoylation
ad Adenylylation
sn S-Nitrosylation
ca Caspase cleavage

Overview
hnRNP P2 Binds both single-stranded and double-stranded DNA and promotes ATP-independent annealing of complementary single- stranded DNAs and D-loop formation in superhelical double-stranded DNA. May play a role in maintenance of genomic integrity. Component of nuclear riboprotein complexes. Interacts with ILF3, TDRD3 and SF1. Interacts through its C-terminus with SFRS13A. Interacts with OTUB1 and SARNP. Ubiquitous. Belongs to the RRM TET family. 2 isoforms of the human protein are produced by alternative splicing. Note: This description may include information from UniProtKB.
Protein type: Nuclear receptor co-regulator; RNA binding protein; RNA splicing; DNA binding protein
Cellular Component: nucleoplasm; cytoplasm; nucleolus; nucleus
Molecular Function: protein binding; DNA binding; zinc ion binding; RNA binding; nucleotide binding
Biological Process: nuclear mRNA splicing, via spliceosome; cell death; RNA splicing; gene expression
Reference #:  P35637 (UniProtKB)
Alt. Names/Synonyms: 75 kDa DNA-pairing protein; ALS6; FUS; fus-like protein; FUS1; fused in sarcoma; fusion gene in myxoid liposarcoma; heterogeneous nuclear ribonucleoprotein P2; HNRNPP2; Oncogene FUS; Oncogene TLS; POMp75; RNA-binding protein FUS; TLS; Translocated in liposarcoma protein
Gene Symbols: FUS
Molecular weight: 53,426 Da
Basal Isoelectric point: 9.4  Predict pI for various phosphorylation states
Protein-Specific Antibodies or siRNAs from Cell Signaling Technology® Total Proteins
Select Structure to View Below

hnRNP P2
Protein Structure Not Found.


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Sites Implicated In
protein stabilization: S257‑p

Modification Sites and Domains Show Modification Legend
Click here to view phosphorylation modifications only

Modification Sites in Parent Protein, Orthologs, and Isoforms Show Modification Legend
 

Show Multiple Sequence Alignment


 SS 

SS: The number of records in which this modification site was determined using site-specific methods. SS methods include amino acid sequencing, site-directed mutagenesis, modification site-specific antibodies, specific MS strategies, etc.


  MS 

MS: The number of records in which this modification site was assigned using ONLY proteomic discovery-mode mass spectrometry.


        human

 
2 0 S26-p TQPGQGYsQQSSQPY
2 0 S42-p QQSYSGYsQSTDTSG
2 0 S61-p SYSSYGQsQNTGYGT
2 0 S84-p STGGYGSsQSSQSSY
1 0 S131-p QPQSGSYsQQPSYGG
0 5 R216-m1 GQQDRGGrGrGGsGG
0 20 R216-m2 GQQDRGGrGrGGsGG
0 6 R218-m1 QDRGGrGrGGsGGGG
0 20 R218-m2 QDRGGrGrGGsGGGG
0 4 S221-p GGrGrGGsGGGGGGG
0 3 Y232-p GGGGGGGyNRSSGGY
0 1 R234 GGGGGyNRSSGGYEP
0 2 R242-m1 SSGGYEPrGRGGGRG
1 0 S257-p GRGGMGGsDrGGFNK
0 2 R259-m1 GGMGGsDrGGFNKFG
0 1 S273-p GGPRDQGsRHDsEQD
0 4 S277-p DQGsRHDsEQDNSDN
0 2 T286-p QDNSDNNtIFVQGLG
0 7 K316-u GIIKTNKkTGQPMIN
0 1 Y325-p GQPMINLyTDRETGK
0 1 K334 DRETGKLKGEATVSF
0 2 K348-u FDDPPSAkAAIDWFd
0 1 D355-ca kAAIDWFdGkEFSGN
0 7 K357-a AIDWFdGkEFSGNPI
0 1 K357 AIDWFdGKEFSGNPI
0 2 K365-u EFSGNPIkVSFATRR
0 11 R394-m1 GRGGPMGrGGYGGGG
0 3 R394-m2 GRGGPMGrGGYGGGG
0 9 R407-m1 GGSGGGGrGGFPSGG
0 3 R407-m2 GGSGGGGrGGFPSGG
0 2 S462-p PGGGPGGsHMGGNyG
0 62 Y468-p GsHMGGNyGDDRRGG
0 1 R473 GNyGDDRRGGRGGYD
0 2 R481-m1 GGRGGYDrGGYrGRG
0 1 R485-m1 GYDrGGYrGRGGDRG
0 16 R503-m1 GGRGGGDrGGFGPGK
  mouse

 
S26 TQPGQGYSQQSSQPY
G42 QQSYSGYGQSADTSG
T62 YGSSYGQTQNTGYGT
S85 STGGYGSSQSSQSSY
G132 QPQSGGYGQQSGYGG
R217 GQQDRGGRGRGGGGG
R217 GQQDRGGRGRGGGGG
R219 QDRGGRGRGGGGGYN
R219 QDRGGRGRGGGGGYN
- gap
Y225 GRGGGGGYNrSSGGY
R227-m1 GGGGGYNrSSGGYEP
R235-m1 SSGGYEPrGRGGGRG
S250 GRGGMGGSDRGGFNK
R252 GGMGGSDRGGFNKFG
S266 GGPRDQGSRHDsEQD
S270-p DQGSRHDsEQDNSDN
T279 QDNSDNNTIFVQGLG
K309-u GIIKTNKkTGQPMIN
Y318 GQPMINLYTDRETGK
K327-u DRETGKLkGEATVSF
K341-u FDDPPSAkAAIDWFD
D348 kAAIDWFDGkEFSGN
K350 AIDWFDGKEFSGNPI
K350-u AIDWFDGkEFSGNPI
K358-u EFSGNPIkVSFATRR
R387-m1 GRGGPMGrGGYGGGG
R387 GRGGPMGRGGYGGGG
R400-m1 GGSGGGGrGGFPSGG
R400 GGSGGGGRGGFPSGG
S455 PGGGPGGSHMGGNyG
Y461-p GSHMGGNyGDDRRGR
R466 GNyGDDRRGRGGYDR
R473 RGRGGYDRGGYRGRG
R477 GYDRGGYRGRGGDRG
R495-m1 GGRGGGDrGGFGPGK
  rat

 
S26 TQPGQGYSQQSNQPY
G42 QQSYSGYGQSADTSG
T62 YGSSYGQTQNTGYGT
S85 STGGYGSSQSSQSSY
G132 QPQSGGYGQQSGYGG
R217 GQQDRGGRGRGGGGG
R217 GQQDRGGRGRGGGGG
R219 QDRGGRGRGGGGGYN
R219 QDRGGRGRGGGGGYN
- gap
Y225 GRGGGGGYNRSSGGY
R227 GGGGGYNRSSGGYEP
R235 SSGGYEPRGRGGGRG
S250 GRGGMGGSDRGGFNK
R252 GGMGGSDRGGFNKFG
S266 GGPRDQGSRHDSEQD
S270 DQGSRHDSEQDNSDN
T279 QDNSDNNTIFVQGLG
K309 GIIKTNKKTGQPMIN
Y318 GQPMINLYTDRETGK
K327 DRETGKLKGEATVSF
K341 FDDPPSAKAAIDWFD
D348 KAAIDWFDGKEFSGN
K350 AIDWFDGKEFSGNPI
K350 AIDWFDGKEFSGNPI
K358 EFSGNPIKVSFATRR
R387-m1 GRGGPMGrGGYGGGG
R387 GRGGPMGRGGYGGGG
R400 GGSGGGGRGGFPSGG
R400 GGSGGGGRGGFPSGG
S455 PGGGPGGSHMGGNYG
Y461 GSHMGGNYGDDRrGR
R466-m1 GNYGDDRrGRGGYDR
R473 rGRGGYDRGGYRGRG
R477 GYDRGGYRGRGGDRG
R495-m1 GGRGGGDrGGFGPGK
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