nuclear pore membrane glycoprotein 210 (POM210, nuclear pore protein gp210, NUP210, KIAA0906, PSEC0245)

Function: - nucleoporin - phosphorylated at Ser-1881 in mitosis - not phosphorylated in interphase Structure: - forms dimers & possibly higher-order oligomers - N-glycosylated - contains high-mannose type oligosaccharides Compartment: - nuclear pore complex, endoplasmic reticulum membrane Alternative splicing: named isoforms=2 Expression: - ubiquitous expression - expressed in lung, liver, pancreas, testis, ovary > brain, kidney, spleen > heart, skeletal muscle Pathology: - recognized by antinuclear autoantibodies in primary biliary cirrhosis - knockdown of NUP210 causes nuclear membranes to accumulate aberrant structures & nuclear pore complex to cluster, induces cell death & chromatin disruptions

General

glycoprotein membrane protein phosphoprotein

Properties

SIZE: MW = 205 kD entity length = 1887 aa COMPARTMENT: cell nucleus endoplasmic reticulum MOTIF: signal sequence {1-26} N-glycosylation site {N44} N-glycosylation site {N337} N-glycosylation site {N405} N-glycosylation site {N484} serine-rich region {486-491} MOTIF: serine residue (SEVERAL) N-glycosylation site {N681} N-glycosylation site {N801} N-glycosylation site {N926} N-glycosylation site {N1039} N-glycosylation site {N1116} N-glycosylation site {N1135} N-glycosylation site {N1362} N-glycosylation site {N1441} transmembrane domain {1809-1829} Thr phosphorylation site {T1844} Ser phosphorylation site {S1881}

Database Correlations

OMIM 607703 UniProt Q8TEM1

References

UniProt :accession Q8TEM1