Pip5k1b
entrez
18719
canonical
uniprot
P70181
canonical
ensembl
ENSMUSG00000024867
resolver
ensp
ENSMUSP00000025800
resolver
genesymbol
Pip5k1b
resolver
uniprot
O70335
resolver
uniprot
Q8JZY6
resolver
uniprot_entry
PI51B_MOUSE
resolver
uniprot_sec
O70335
resolver
uniprot_sec
Q8JZY6
resolver
activity_regulation
ACTIVITY REGULATION: Activated by phosphatidic acid. {ECO:0000269|PubMed:8798574, ECO:0000269|PubMed:9535851}.
uniprot
proteins
amino_acid_sequence
MSSTAENGDAVPGKQNEEKTYKKTASSAIKGAIQLGIGYTVGNLTSKPERDVLMQDFYVVESVFLPSEGSNLTPAHHYPDFRFKTYAPLAFRYFRELFGIKPDDYLYSICSEPLIELSNPGASGSLFFLTSDDEFIIKTVQHKEAEFLQKLLPGYYMNLNQNPRTLLPKFYGLYCMQSGGINIRIVVMNNVLPRAMRMHLTYDLKGSTYKRRASRKEREKPNPTFKDLDFLQDMHEGLYFDTETYNALMKTLQRDCRVLESFKIMDYSLLLGIHILDHSLKDKEEEPLQNVPDAKRPGMQKVLYSTAMESIQGPGKSADGIIAENPDTMGGIPAKSHKGEKLLLFMGIIDILQSYRLMKKLEHSWKALVYDGDTVSVHRPSFYADRFLKFMNSRVFKKIQALKASPSKKRCNSIAALKATSQEIVSSISQEWKDEKRDLLTEGQSFSSLDEEALGSRHRPDLVPSTPSLFEAASLATTISSSSLYVGEHYPHDRTTLYSNSKGLPSSSTFTLEEGTIYLTAEPNTLDLQDDASVLDVYL
uniprot
proteins
ec_number
2.7.1.68
uniprot
proteins
function
FUNCTION: Catalyzes the phosphorylation of phosphatidylinositol 4-phosphate (PtdIns(4)P/PI4P) to form phosphatidylinositol 4,5-bisphosphate (PtdIns(4,5)P2/PIP2), a lipid second messenger that regulates several cellular processes such as signal transduction, vesicle trafficking, actin cytoskeleton dynamics, cell adhesion, and cell motility (PubMed:22942276, PubMed:8798574, PubMed:9367159, PubMed:9535851). PtdIns(4,5)P2 can directly act as a second messenger or can be utilized as a precursor to generate other second messengers: inositol 1,4,5-trisphosphate (IP3), diacylglycerol (DAG) or phosphatidylinositol-3,4,5-trisphosphate (PtdIns(3,4,5)P3/PIP3) (By similarity). Mediates RAC1-dependent reorganization of actin filaments (PubMed:10679324). Contributes to the activation of phospholipase PLD2 (PubMed:11032811). Together with PIP5K1A, is required, after stimulation by G protein-coupled receptors, for the synthesis of IP3 that will induce stable platelet adhesion (PubMed:18772378). {ECO:0000250|UniProtKB:Q99755, ECO:0000269|PubMed:10679324, ECO:0000269|PubMed:11032811, ECO:0000269|PubMed:18772378, ECO:0000269|PubMed:22942276, ECO:0000269|PubMed:8798574, ECO:0000269|PubMed:9367159, ECO:0000269|PubMed:9535851}.
uniprot
proteins
mass_dalton
60803
uniprot
proteins
mutagenesis
MUTAGEN 138; /note="K->A: Almost complete loss of 1-phosphatidylinositol-4-phosphate 5-kinase activity."; /evidence="ECO:0000269|PubMed:9535851"; MUTAGEN 227; /note="D->A: Reduced 1-phosphatidylinositol-4-phosphate 5-kinase activity by 98%. Loss of actin-remodeling activity."; /evidence="ECO:0000269|PubMed:10679324
uniprot
proteins
pubmed
10679324
uniprot
proteins
pubmed
10747863
uniprot
proteins
pubmed
11032811
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
15870270
uniprot
proteins
pubmed
16141072
uniprot
proteins
pubmed
18772378
uniprot
proteins
pubmed
21183079
uniprot
proteins
pubmed
22942276
uniprot
proteins
pubmed
8798574
uniprot
proteins
pubmed
9367159
uniprot
proteins
pubmed
9535851
uniprot
proteins
sequence_length
539
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000269|PubMed:11032811}. Cell membrane {ECO:0000269|PubMed:11032811}. Endomembrane system {ECO:0000250}. Note=Associated with membranes. {ECO:0000250}.
uniprot
proteins