Cyth3
entrez
19159
canonical
uniprot
O08967
canonical
ensembl
ENSMUSG00000018001
resolver
ensp
ENSMUSP00000106355
resolver
ensp
ENSMUSP00000112157
resolver
ensp
ENSMUSP00000239196
resolver
enst
ENSMUST00000110727
resolver
enst
ENSMUST00000116456
resolver
genesymbol
Cyth3
resolver
genesymbol_syn
Grp1
resolver
genesymbol_syn
Pscd3
resolver
uniprot
G5E8Q4
resolver
uniprot
Q3TXK1
resolver
uniprot
Q8CI93
resolver
uniprot_entry
CYH3_MOUSE
resolver
uniprot_entry
G5E8Q4_MOUSE
resolver
uniprot_entry
Q3TXK1_MOUSE
resolver
uniprot_sec
Q8CI93
resolver
amino_acid_sequence
MDEGGGGEGGSVPEDLSLEEREELLDIRRRKKELIDDIERLKYEIAEVMTEIDNLTSVEESKTTQRNKQIAMGRKKFNMDPKKGIQFLIENDLLQSSPEDVAQFLYKGEGLNKTVIGDYLGERDDFNIKVLQAFVELHEFADLNLVQALRQFLWSFRLPGEAQKIDRMMEAFASRYCLCNPGVFQSTDTCYVLSFAIIMLNTSLHNHNVRDKPTAERFITMNRGINEGGDLPEELLRNLYESIKNEPFKIPEDDGNDLTHTFFNPDREGWLLKLGGRVKTWKRRWFILTDNCLYYFEYTTDKEPRGIIPLENLSIREVEDPRKPNCFELYNPSHKGQVIKACKTEADGRVVEGNHVVYRISAPSPEEKEEWMKSIKASISRDPFYDMLATRKRRIANKK
uniprot
proteins
function
FUNCTION: Promotes guanine-nucleotide exchange on ARF1. Promotes the activation of ARF factors through replacement of GDP with GTP (PubMed:18042453). Plays a role in the epithelial polarization (PubMed:20080746). {ECO:0000269|PubMed:18042453, ECO:0000269|PubMed:20080746}.
uniprot
proteins
mass_dalton
46280
uniprot
proteins
mutagenesis
MUTAGEN 161; /note="E->K: Impairs epithelium polarization."; /evidence="ECO:0000269|PubMed:20080746"; MUTAGEN 273; /note="K->A: Abolishes phosphatidylinositol 3,4,5-trisphosphate binding."; /evidence="ECO:0000269|PubMed:15359279"; MUTAGEN 277; /note="R->A,G: Reduces phosphatidylinositol 3,4,5-trisphosphate binding."; /evidence="ECO:0000269|PubMed:15359279"; MUTAGEN 280; /note="T->A,G: Reduces phosphatidylinositol 3,4,5-trisphosphate binding."; /evidence="ECO:0000269|PubMed:15359279"; MUTAGEN 282; /note="K->A: Reduces phosphatidylinositol 3,4,5-trisphosphate binding."; /evidence="ECO:0000269|PubMed:15359279"; MUTAGEN 284; /note="R->A: Abolishes phosphatidylinositol 3,4,5-trisphosphate binding."; /evidence="ECO:0000269|PubMed:15359279"; MUTAGEN 295; /note="Y->F: Reduces phosphatidylinositol 3,4,5-trisphosphate binding."; /evidence="ECO:0000269|PubMed:15359279"; MUTAGEN 305; /note="R->A: Abolishes phosphatidylinositol 3,4,5-trisphosphate binding."; /evidence="ECO:0000269|PubMed:15359279"; MUTAGEN 343; /note="K->A: Abolishes phosphatidylinositol 3,4,5-trisphosphate binding."; /evidence="ECO:0000269|PubMed:15359279"; MUTAGEN 354; /note="N->A: Slightly reduces phosphatidylinositol 3,4,5-trisphosphate binding."; /evidence="ECO:0000269|PubMed:15359279"; MUTAGEN 355; /note="H->A: Abolishes phosphatidylinositol 3,4,5-trisphosphate binding."; /evidence="ECO:0000269|PubMed:15359279"; MUTAGEN 388; /note="L->A: Impairs autoinhibition; when associated with A-392."; /evidence="ECO:0000269|PubMed:18042453"; MUTAGEN 392; /note="K->A: Impairs autoinhibition; when associated with A-388."; /evidence="ECO:0000269|PubMed:18042453
uniprot
proteins
pubmed
10605025
uniprot
proteins
pubmed
10828067
uniprot
proteins
pubmed
10983984
uniprot
proteins
pubmed
10983985
uniprot
proteins
pubmed
15359279
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
18042453
uniprot
proteins
pubmed
20080746
uniprot
proteins
pubmed
21183079
uniprot
proteins
pubmed
9072969
uniprot
proteins
pubmed
9744817
uniprot
proteins
sequence_length
399
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000250}. Cell membrane {ECO:0000269|PubMed:18042453}; Peripheral membrane protein {ECO:0000269|PubMed:18042453}. Cell junction, adherens junction {ECO:0000269|PubMed:20080746}. Cell junction, tight junction {ECO:0000269|PubMed:20080746}. Note=Translocates from the cytosol to membranes enriched in phosphatidylinositol 3,4,5-trisphosphate.
uniprot
proteins