Basic Information | Overview of PTM Sites | Experimental PTM Sites | Protein-Protein Interactions | Drug and Disease Associations | Related Literatures
Basic Information
Protein Name :  Pre-mRNA-splicing factor RBM22  

UniProtKB / Swiss-Prot ID :  RBM22_HUMAN

Gene Name (Synonyms) : 
RBM22, ZC3H16 199G4  

Species :  Homo sapiens (Human). 

Subcellular Localization :  Nucleus. Cytoplasm. Note=Mainly located in the nucleus. Translocated from the nucleus to the cytoplasm after heat shock cell treatment. May be shuttling between the nucleus and the cytosol. 

Protein Function :  Involved in the first step of pre-mRNA splicing. Binds directly to the internal stem-loop (ISL) domain of the U6 snRNA and to the pre-mRNA intron near the 5' splice site during the activation and catalytic phases of the spliceosome cycle. Involved in both translocations of the nuclear SLU7 to the cytoplasm and the cytosolic calcium-binding protein PDCD6 to the nucleus upon cellular stress responses. 

Protein Sequence MATSLGSNTYNRQNWEDADFPILCQTCLGENPYIRMTKEKYGKECKICARPFTVFRWCPGVRMRFKKTEV...
Predicted Secondary Structure CCCCCCCCCCCCCCCCCCCCHHHHHHCCCCCCCEEECCCCCCCCCCEECCCCEEEEEECCCCCCCCEEEE...
Protein Variant -
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Overview of Protein Modification Sites with Functional and Structural Information
Accessible Surface Area (ASA)
Pred. Secondary
Real Secondary
Disorder Prediction
Protein Domain
&
Experimental PTM Sites
Predicted PTM Sites
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Experimental Post-Translational Modification Sites Download
Locations
Modification
Substrate Sites
&
Secondary Structure
Accessible Surface Area (%)
Resource
Reference
Structural Characterization
Orthologous
Protein Cluster
2N-acetylalanine.---MATSLG
---CCCCCC
13.09UniProtKB
Link-
3Phosphothreonine--MATSLGS
--CCCCCCC
24.16HPRD
Link-
4Phosphoserine-MATSLGSN
-CCCCCCCC
22.61HPRD
Link-
114Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)SDVNKEYYT
CCCCHHHHH
47.11Phosphositeplus
Link-
116PhosphotyrosineVNKEYYTQN
CCHHHHHHH
17.27Phosphositeplus
Link-
117PhosphotyrosineNKEYYTQNM
CHHHHHHHH
11.71Phosphositeplus
Link-
126PhosphoserineEREISNSDG
HHHHHHCCC
26.06HPRD
Link-
131PhosphothreonineNSDGTRPVG
HCCCCCCHH
36.47HPRD
Link-
142PhosphoserineGKATSTSDM
HHHHHHHHH
30.67Phosphositeplus
Link-
212N6-acetyllysinePVADKLLKR
CCCCCCCCC
46.08HPRD
Link-
212N6-acetyllysinePVADKLLKR
CCCCCCCCC
46.08Phosphositeplus
Link-
212N6-acetyllysine.PVADKLLKR
CCCCCCCCC
46.08UniProtKB
Link-
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Protein-Protein Interactions
      Interacting Protein      
Interaction type
Source ID
      Resource      
      Pubmed ID      
Domain-Domain Interactions
There are no Protein-Protein Interactions.
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Disease Reference
Kegg disease
There are no disease associations of PTM sites.
Drug Reference
There are no disease associations of PTM sites.
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Related Literatures of Post-Translational Modification
Acetylation
ReferencePubMed
"Lysine acetylation targets protein complexes and co-regulates majorcellular functions.";
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.,Olsen J.V., Mann M.;
Science 325:834-840(2009).
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-212, AND MASS SPECTROMETRY.
"Lys-N and trypsin cover complementary parts of the phosphoproteome ina refined SCX-based approach.";
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,Mohammed S.;
Anal. Chem. 81:4493-4501(2009).
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, AND MASS SPECTROMETRY.
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Basic Information | Overview of PTM Sites | Experimental PTM Sites | Protein-Protein Interactions | Drug and Disease Associations | Related Literatures