Curated Information
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Home > Curated Information Page > PubMed Id: 15905169
F├╝rst J, et al. (2005) ICln159 folds into a pleckstrin homology domain-like structure. Interaction with kinases and the splicing factor LSm4. J Biol Chem 280, 31276-82 15905169
This page summarizes selected information from the record referenced above and curated into PhosphoSitePlus®, a comprehensive online resource for the study of protein post-translational modifications (NAR, 2015, 43:D512-20). To learn more about the scope of PhosphoSitePlus®, click here.
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S2-p - ICLN (dog)
Modsite: ______MsFLKSFPP SwissProt Entrez-Gene
Orthologous residues
ICLN (human): S2‑p, ICLN (mouse): S2‑p, ICLN iso2 (mouse): S7‑p, ICLN (rat): S2‑p, ICLN (dog): S2‑p
Characterization
Enzymes shown to modify site in vitro
Type Enzyme
KINASE PKG2 (human)

S45-p - ICLN (dog)
Modsite: YIAESRLsWLDGSGL SwissProt Entrez-Gene
Orthologous residues
ICLN (human): S45‑p, ICLN (mouse): S45‑p, ICLN iso2 (mouse): S50‑p, ICLN (rat): S45‑p, ICLN (dog): S45‑p
Characterization
Enzymes shown to modify site in vitro
Type Enzyme
KINASE PKG2 (human)
KINASE PKACA (human)
KINASE PKCA (human)

S93-p - ICLN (dog)
Modsite: FGEESKEsVAEEEDS SwissProt Entrez-Gene
Orthologous residues
ICLN (human): P93‑p, ICLN (mouse): P93‑p, ICLN iso2 (mouse): P98‑p, ICLN (rat): P93‑p, ICLN (dog): S93‑p
Characterization
Enzymes shown to modify site in vitro
Type Enzyme
KINASE PKG2 (human)