protein kinase C-binding protein NELL2; NEL-like protein 2; Nel-related protein 2 (NELL2 NRP2)

Function: - 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)

General

glycoprotein secreted protein

Properties

SIZE: entity length = 816 aa MW = 91 kD COMPARTMENT: extracellular compartment MOTIF: signal sequence {1-21} TSP N-terminal {30-258} MOTIF: N-glycosylation site {N53} N-glycosylation site {N225} VWFC domain {272-331} MOTIF: N-glycosylation site {N293} N-glycosylation site {N298} VWFC domain {332-396} EGF domain {397-439} MOTIF: cysteine residue {C401} MODIFICATION: cysteine residue {C413} cysteine residue {C407} MODIFICATION: cysteine residue {C422} cysteine residue {C413} MODIFICATION: cysteine residue {C401} cysteine residue {C422} MODIFICATION: cysteine residue {C407} cysteine residue {C424} MODIFICATION: cysteine residue {C438} cysteine residue {C438} MODIFICATION: cysteine residue {C424} EGF domain {440-481} MOTIF: cysteine residue {C444} MODIFICATION: cysteine residue {C457} cysteine residue {C451} MODIFICATION: cysteine residue {C466} cysteine residue {C457} MODIFICATION: cysteine residue {C444} cysteine residue {C466} MODIFICATION: cysteine residue {C451} cysteine residue {C468} MODIFICATION: cysteine residue {C480} cysteine residue {C480} MODIFICATION: cysteine residue {C468} EGF domain {482-522} MOTIF: cysteine residue {C486} MODIFICATION: cysteine residue {C499} cysteine residue {C493} MODIFICATION: cysteine residue {C508} cysteine residue {C499} MODIFICATION: cysteine residue {C486} cysteine residue {C508} MODIFICATION: cysteine residue {C493} cysteine residue {C510} MODIFICATION: cysteine residue {C521} N-glycosylation site {N517} EGF domain {521-553} MOTIF: cysteine residue {C521} MODIFICATION: cysteine residue {C510} cysteine residue {C525} MODIFICATION: cysteine residue {C535} cysteine residue {C529} MODIFICATION: cysteine residue {C541} cysteine residue {C535} MODIFICATION: cysteine residue {C525} cysteine residue {C541} MODIFICATION: cysteine residue {C529} cysteine residue {C543} MODIFICATION: cysteine residue {C552} cysteine residue {C552} MODIFICATION: cysteine residue {C543} EGF domain {555-601} MOTIF: cysteine residue {C559} MODIFICATION: cysteine residue {C572} cysteine residue {C566} MODIFICATION: cysteine residue {C581} cysteine residue {C572} MODIFICATION: cysteine residue {C559} cysteine residue {C581} MODIFICATION: cysteine residue {C566} cysteine residue {C583} MODIFICATION: cysteine residue {C600} cysteine residue {C600} MODIFICATION: cysteine residue {C583} EGF domain {602-637} MOTIF: cysteine residue {C606} MODIFICATION: cysteine residue {C619} cysteine residue {C613} MODIFICATION: cysteine residue {C628} N-glycosylation site {N615} cysteine residue {C619} MODIFICATION: cysteine residue {C606} cysteine residue {C628} MODIFICATION: cysteine residue {C613} cysteine residue {C630} MODIFICATION: cysteine residue {C636} N-glycosylation site {N635} cysteine residue {C636} MODIFICATION: cysteine residue {C630} VWFC domain {638-693} VWFC domain {698-756} VWFC domain {758-813}

Database Correlations

OMIM 602320 UniProt Q99435 PFAM correlations Entrez Gene 4753 Kegg hsa:4753

References

UniProt :accession Q99435