SDCBP2
entrez
27111
canonical
uniprot
Q9H190
canonical
ensembl
ENSG00000125775
resolver
ensp
ENSP00000342935
resolver
ensp
ENSP00000354013
resolver
ensp
ENSP00000371229
resolver
genesymbol
SDCBP2
resolver
genesymbol_syn
SITAC18
resolver
hgnc
HGNC:15756
resolver
uniprot
O95892
resolver
uniprot
Q5W0X1
resolver
uniprot
Q9BZ42
resolver
uniprot
Q9H567
resolver
uniprot
Q9NRY8
resolver
uniprot_entry
SDCB2_HUMAN
resolver
uniprot_sec
O95892
resolver
uniprot_sec
Q5W0X1
resolver
uniprot_sec
Q9BZ42
resolver
uniprot_sec
Q9H567
resolver
uniprot_sec
Q9NRY8
resolver
amino_acid_sequence
MSSLYPSLEDLKVDQAIQAQVRASPKMPALPVQATAISPPPVLYPNLAELENYMGLSLSSQEVQESLLQIPEGDSTAVSGPGPGQMVAPVTGYSLGVRRAEIKPGVREIHLCKDERGKTGLRLRKVDQGLFVQLVQANTPASLVGLRFGDQLLQIDGRDCAGWSSHKAHQVVKKASGDKIVVVVRDRPFQRTVTMHKDSMGHVGFVIKKGKIVSLVKGSSAARNGLLTNHYVCEVDGQNVIGLKDKKIMEILATAGNVVTLTIIPSVIYEHMVKKLPPVLLHHTMDHSIPDA
uniprot
proteins
function
FUNCTION: Binds phosphatidylinositol 4,5-bisphosphate (PIP2). May play a role in the organization of nuclear PIP2, cell division and cell survival (PubMed:15961997). {ECO:0000269|PubMed:15961997}.
uniprot
proteins
mass_dalton
31594
uniprot
proteins
mutagenesis
MUTAGEN 113; /note="K->A: Abolishes phosphatidylinositol 4,5-bisphosphate binding and targeting to plasma membrane, speckles and nucleoli; when associated with A-167; A-197 and A-244. Reduces phosphatidylinositol 4,5-bisphosphate binding and does not change subcellular localization; when associated with A-167."; /evidence="ECO:0000269|PubMed:15961997"; MUTAGEN 167; /note="K->A: Abolishes phosphatidylinositol 4,5-bisphosphate binding and targeting to plasma membrane, speckles and nucleoli; when associated with A-113; A-197 and A-244. Reduces phosphatidylinositol 4,5-bisphosphate binding and does not change subcellular localization; when associated with A-113."; /evidence="ECO:0000269|PubMed:15961997"; MUTAGEN 197; /note="K->A: Abolishes phosphatidylinositol 4,5-bisphosphate binding and targeting to plasma membrane, speckles and nucleoli; when associated with A-113; A-167 and A-244. Reduces phosphatidylinositol 4,5-bisphosphate binding and does not change subcellular localization; when associated with A-244."; /evidence="ECO:0000269|PubMed:15961997"; MUTAGEN 244; /note="K->A: Abolishes phosphatidylinositol 4,5-bisphosphate binding and targeting to plasma membrane, speckles and nucleoli; when associated with A-113; A-167 and A-197. Reduces phosphatidylinositol 4,5-bisphosphate binding and does not change subcellular localization; when associated with A-197."; /evidence="ECO:0000269|PubMed:15961997
uniprot
proteins
pubmed
11102519
uniprot
proteins
pubmed
11152476
uniprot
proteins
pubmed
11780052
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
15961997
uniprot
proteins
pubmed
16959974
uniprot
proteins
pubmed
22623796
uniprot
proteins
pubmed
23300061
uniprot
proteins
sequence_length
292
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:15961997}. Nucleus, nucleolus {ECO:0000269|PubMed:15961997, ECO:0000269|PubMed:23300061}. Nucleus, nucleoplasm {ECO:0000269|PubMed:23300061}. Cell membrane {ECO:0000269|PubMed:15961997}. Nucleus speckle {ECO:0000269|PubMed:15961997}. Note=Associates with intracellular membranes and enriched in the apical region of the cell and in intracellular compartments (PubMed:11102519). Colocalizes with TM4SF1 in the apical region of the cell (PubMed:11102519). Predominantly targeted to nuclear PIP2 pools. Shuttles between several subcellular compartments (PubMed:15961997). PIP2 plays an important role in the distribution of SDCBP2 (PubMed:23300061). {ECO:0000269|PubMed:11102519, ECO:0000269|PubMed:15961997, ECO:0000269|PubMed:23300061}.
uniprot
proteins