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protein kinase C-binding protein NELL1; NEL-like protein 1; Nel-related protein 1 (NELL1 NRP1)

Function: - role in the control of cell growth & differentiation (putative) - binds to PKC beta-1 (putative) Structure: - homotrimer - contains 6 EGF-like domains - contains 1 TSP N-terminal (TSPN) domain - contains 5 VWFC domains Compartment: secreted (putative)

Related

protein kinase C (PKC)

General

glycoprotein secreted protein

Properties

SIZE: entity length = 810 aa MW = 90 kD COMPARTMENT: extracellular compartment MOTIF: signal sequence {1-16} N-glycosylation site {N40} N-glycosylation site {N53} TSP N-terminal {81-230} MOTIF: N-glycosylation site {N83} N-glycosylation site {N224} VWFC domain {271-332} MOTIF: N-glycosylation site {N294} VWFC domain {335-390} MOTIF: N-glycosylation site {N372} EGF domain {391-433} MOTIF: cysteine residue {C395} MODIFICATION: cysteine residue {C407} cysteine residue {C401} MODIFICATION: cysteine residue {C416} cysteine residue {C407} MODIFICATION: cysteine residue {C395} cysteine residue {C416} MODIFICATION: cysteine residue {C401} cysteine residue {C418} MODIFICATION: cysteine residue {C432} cysteine residue {C432} MODIFICATION: cysteine residue {C418} EGF domain {434-475} MOTIF: cysteine residue {C438} MODIFICATION: cysteine residue {C451} cysteine residue {C445} MODIFICATION: cysteine residue {C460} cysteine residue {C451} MODIFICATION: cysteine residue {C438} cysteine residue {C460} MODIFICATION: cysteine residue {C445} cysteine residue {C462} MODIFICATION: cysteine residue {C474} cysteine residue {C474} MODIFICATION: cysteine residue {C462} EGF domain {476-516} MOTIF: cysteine residue {C480} MODIFICATION: cysteine residue {C493} cysteine residue {C487} MODIFICATION: cysteine residue {C502} cysteine residue {C493} MODIFICATION: cysteine residue {C480} cysteine residue {C502} MODIFICATION: cysteine residue {C487} cysteine residue {C504} MODIFICATION: cysteine residue {C515} N-glycosylation site {N511} EGF domain {515-547} MOTIF: cysteine residue {C515} MODIFICATION: cysteine residue {C504} cysteine residue {C519} MODIFICATION: cysteine residue {C529} cysteine residue {C523} MODIFICATION: cysteine residue {C535} cysteine residue {C529} MODIFICATION: cysteine residue {C519} cysteine residue {C535} MODIFICATION: cysteine residue {C523} cysteine residue {C537} MODIFICATION: cysteine residue {C546} cysteine residue {C546} MODIFICATION: cysteine residue {C537} EGF domain {549-595} MOTIF: cysteine residue {C553} MODIFICATION: cysteine residue {C566} cysteine residue {C560} MODIFICATION: cysteine residue {C575} N-glycosylation site {N562} cysteine residue {C566} MODIFICATION: cysteine residue {C553} cysteine residue {C575} MODIFICATION: cysteine residue {C560} cysteine residue {C577} MODIFICATION: cysteine residue {C594} cysteine residue {C594} MODIFICATION: cysteine residue {C577} EGF domain {596-631} MOTIF: cysteine residue {C600} MODIFICATION: cysteine residue {C613} cysteine residue {C607} MODIFICATION: cysteine residue {C622} N-glycosylation site {N609} cysteine residue {C613} MODIFICATION: cysteine residue {C600} cysteine residue {C622} MODIFICATION: cysteine residue {C607} cysteine residue {C624} MODIFICATION: cysteine residue {C630} cysteine residue {C630} MODIFICATION: cysteine residue {C624} VWFC domain {632-687} VWFC domain {692-750} MOTIF: N-glycosylation site {N708} N-glycosylation site {N732} VWFC domain {752-807} MOTIF: N-glycosylation site {N758}

Database Correlations

OMIM 602319 UniProt Q92832 PFAM correlations Entrez Gene 4745 Kegg hsa:4745

References

UniProt :accession Q92832