Basic Information | Overview of PTM Sites | Experimental PTM Sites | Protein-Protein Interactions | Drug and Disease Associations | Related Literatures
Basic Information
Protein Name :  Heterogeneous nuclear ribonucleoproteins C1/C2  

UniProtKB / Swiss-Prot ID :  HNRPC_MOUSE

Gene Name (Synonyms) : 
Hnrnpc, Hnrpc  

Species :  Mus musculus (Mouse). 

Subcellular Localization :  Nucleus (By similarity). Note=Component of ribonucleosomes (By similarity). 

Protein Function :  Binds pre-mRNA and nucleates the assembly of 40S hnRNP particles. Single HNRNPC tetramers bind 230-240 nucleotides. Trimers of HNRNPC tetramers bind 700 nucleotides. May play a role in the early steps of spliceosome assembly and pre-mRNA splicing. Interacts with poly-U tracts in the 3'-UTR or 5'-UTR of mRNA and modulates the stability and the level of translation of bound mRNA molecules (By similarity). 

Protein Sequence MASNVTNKTDPRSMNSRVFIGNLNTLVVKKSDVEAIFSKYGKIVGCSVHKGFAFVQYVNERNARAAVAGE...
Predicted Secondary Structure CCCCCCCCCCCCCCCCEEEEECCCCCCCCHHHHHHHHHCCCCEEEEEEEECEEEEEECCHHHHHHHHHHH...
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
121PhosphoserineLLSSSFDLD
CCCCCCCCC
21.28Phosphositeplus
Link-
138PhosphoserineDRMYSYPAR
CCCCCCCCC
18.46Phosphositeplus
Link-
162PhosphoserineRQRVSGNTS
CCCCCCCCC
28.63Phosphositeplus
Link-
229PhosphoserineQADLSFSSP
CCCCCCCCC
24.51Phosphositeplus
Link-
231PhosphoserineDLSFSSPVE
CCCCCCCCC
30.29Phosphositeplus
Link-
232PhosphoserineLSFSSPVEM
CCCCCCCCC
30.84PhosphoELM
Link-
232PhosphoserineLSFSSPVEM
CCCCCCCCC
30.84Phosphositeplus
Link-
232Phosphoserine.LSFSSPVEM
CCCCCCCCC
30.84UniProtKB
Link-
241PhosphoserineKNEKSEEEQ
CCCCCHHHH
44.02Phosphositeplus
Link-
241Phosphoserine.KNEKSEEEQ
CCCCCHHHH
44.02UniProtKB
Link-
246PhosphoserineEEEQSSASV
HHHHHHHHH
31.02Phosphositeplus
Link-
249PhosphoserineQSSASVKKD
HHHHHHHCC
36.10Phosphositeplus
Link-
249Phosphoserine.QSSASVKKD
HHHHHHHCC
36.10UniProtKB
Link-
261PhosphoserineVKMESEAGA
CEEHHHCCC
29.28Phosphositeplus
Link-
268PhosphoserineGADDSAEEG
CCCCCHHCC
37.82PhosphoELM
Link-
268PhosphoserineGADDSAEEG
CCCCCHHCC
37.82Phosphositeplus
Link-
268PhosphoserineGADDSAEEG
CCCCCHHCC
37.82SysPTM
Link-
268Phosphoserine.GADDSAEEG
CCCCCHHCC
37.82UniProtKB
Link-
306PhosphoserineDDRDSANGE
CCCCCCCCC
25.24Phosphositeplus
Link-
313PhosphoserineGEDDS
CCCCC
55.21Phosphositeplus
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
Drug Reference
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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Identification of phosphoproteins and their phosphorylation sites inthe WEHI-231 B lymphoma cell line.";
Shu H., Chen S., Bi Q., Mumby M., Brekken D.L.;
Mol. Cell. Proteomics 3:279-286(2004).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-232, AND MASSSPECTROMETRY.
"Large-scale phosphorylation analysis of mouse liver.";
Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-232, AND MASSSPECTROMETRY.
"Solid tumor proteome and phosphoproteome analysis by high resolutionmass spectrometry.";
Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J.,Faessler R., Mann M.;
J. Proteome Res. 7:5314-5326(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-241 AND SER-249, ANDMASS SPECTROMETRY.
"The phagosomal proteome in interferon-gamma-activated macrophages.";
Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,Thibault P.;
Immunity 30:143-154(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-241 AND SER-268, ANDMASS SPECTROMETRY.
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Basic Information | Overview of PTM Sites | Experimental PTM Sites | Protein-Protein Interactions | Drug and Disease Associations | Related Literatures