PASK
entrez
23178
canonical
uniprot
Q96RG2
canonical
ensembl
ENSG00000115687
resolver
ensp
ENSP00000234040
resolver
ensp
ENSP00000351475
resolver
ensp
ENSP00000384438
resolver
ensp
ENSP00000441374
resolver
ensp
ENSP00000600324
resolver
genesymbol
PASK
resolver
genesymbol_syn
KIAA0135
resolver
hgnc
HGNC:17270
resolver
uniprot
B7Z7R6
resolver
uniprot
G5E9F1
resolver
uniprot
Q05BE4
resolver
uniprot
Q68DY3
resolver
uniprot
Q6GSJ5
resolver
uniprot
Q86XH6
resolver
uniprot
Q99763
resolver
uniprot
Q9UFR7
resolver
uniprot_entry
B7Z7R6_HUMAN
resolver
uniprot_entry
PASK_HUMAN
resolver
uniprot_sec
G5E9F1
resolver
uniprot_sec
Q05BE4
resolver
uniprot_sec
Q68DY3
resolver
uniprot_sec
Q6GSJ5
resolver
uniprot_sec
Q86XH6
resolver
uniprot_sec
Q99763
resolver
uniprot_sec
Q9UFR7
resolver
activity_regulation
ACTIVITY REGULATION: Protein kinase activity is inhibited by the first PAS domain: binding of an unidentified ligand desinhibits the protein kinase activity. May be activated by autophosphorylation on Thr-1161 and Thr-1165 (PubMed:11459942). The activating role of autophosphorylation at Thr-1161 is unclear: according to a report, autophosphorylation at Thr-1161 does not play a major role in activation (PubMed:20943661). Autophosphorylation is enhanced upon phosphatidylinositol monophosphate (phosphatidylinositol 4-phosphate) binding and inhibited upon phosphatidylinositol bi- and tri-phosphate binding. In contrast, phosphorylation of target proteins is inhibited upon all phosphatidylinositol-binding (phosphatidylinositol mono- bi- and tri-phosphate). {ECO:0000269|PubMed:11459942, ECO:0000269|PubMed:20943661, ECO:0000269|PubMed:21418524}.
uniprot
proteins
amino_acid_sequence
MEDGGLTAFEEDQRCLSQSLPLPVSAEGPAAQTTAEPSRSFSSAHRHLSRRNGLSRLCQSRTALSEDRWSSYCLSSLAAQNICTSKLHCPAAPEHTDPSEPRGSVSCCSLLRGLSSGWSSPLLPAPVCNPNKAIFTVDAKTTEILVANDKACGLLGYSSQDLIGQKLTQFFLRSDSDVVEALSEEHMEADGHAAVVFGTVVDIISRSGEKIPVSVWMKRMRQERRLCCVVVLEPVERVSTWVAFQSDGTVTSCDSLFAHLHGYVSGEDVAGQHITDLIPSVQLPPSGQHIPKNLKIQRSVGRARDGTTFPLSLKLKSQPSSEEATTGEAAPVSGYRASVWVFCTISGLITLLPDGTIHGINHSFALTLFGYGKTELLGKNITFLIPGFYSYMDLAYNSSLQLPDLASCLDVGNESGCGERTLDPWQGQDPAEGGQDPRINVVLAGGHVVPRDEIRKLMESQDIFTGTQTELIAGGQLLSCLSPQPAPGVDNVPEGSLPVHGEQALPKDQQITALGREEPVAIESPGQDLLGESRSEPVDVKPFASCEDSEAPVPAEDGGSDAGMCGLCQKAQLERMGVSGPSGSDLWAGAAVAKPQAKGQLAGGSLLMHCPCYGSEWGLWWRSQDLAPSPSGMAGLSFGTPTLDEPWLGVENDREELQTCLIKEQLSQLSLAGALDVPHAELVPTECQAVTAPVSSCDLGGRDLCGGCTGSSSACYALATDLPGGLEAVEAQEVDVNSFSWNLKELFFSDQTDQTSSNCSCATSELRETPSSLAVGSDPDVGSLQEQGSCVLDDRELLLLTGTCVDLGQGRRFRESCVGHDPTEPLEVCLVSSEHYAASDRESPGHVPSTLDAGPEDTCPSAEEPRLNVQVTSTPVIVMRGAAGLQREIQEGAYSGSCYHRDGLRLSIQFEVRRVELQGPTPLFCCWLVKDLLHSQRDSAARTRLFLASLPGSTHSTAAELTGPSLVEVLRARPWFEEPPKAVELEGLAACEGEYSQKYSTMSPLGSGAFGFVWTAVDKEKNKEVVVKFIKKEKVLEDCWIEDPKLGKVTLEIAILSRVEHANIIKVLDIFENQGFFQLVMEKHGSGLDLFAFIDRHPRLDEPLASYIFRQLVSAVGYLRLKDIIHRDIKDENIVIAEDFTIKLIDFGSAAYLERGKLFYTFCGTIEYCAPEVLMGNPYRGPELEMWSLGVTLYTLVFEENPFCELEETVEAAIHPPYLVSKELMSLVSGLLQPVPERRTTLEKLVTDPWVTQPVNLADYTWEEVFRVNKPESGVLSAASLEMGNRSLSDVAQAQELCGGPVPGEAPNGQGCLHPGDPRLLTS
uniprot
proteins
ec_number
2.7.11.1
uniprot
proteins
function
FUNCTION: Serine/threonine-protein kinase involved in energy homeostasis and protein translation. Phosphorylates EEF1A1, GYS1, PDX1 and RPS6. Probably plays a role under changing environmental conditions (oxygen, glucose, nutrition), rather than under standard conditions. Acts as a sensor involved in energy homeostasis: regulates glycogen synthase synthesis by mediating phosphorylation of GYS1, leading to GYS1 inactivation. May be involved in glucose-stimulated insulin production in pancreas and regulation of glucagon secretion by glucose in alpha cells; however such data require additional evidence. May play a role in regulation of protein translation by phosphorylating EEF1A1, leading to increase translation efficiency. May also participate in respiratory regulation. {ECO:0000269|PubMed:16275910, ECO:0000269|PubMed:17052199, ECO:0000269|PubMed:17595531, ECO:0000269|PubMed:20943661, ECO:0000269|PubMed:21181396, ECO:0000269|PubMed:21418524}.
uniprot
proteins
mass_dalton
142929
uniprot
proteins
mutagenesis
MUTAGEN 1028; /note="K->R: Loss of autophosphorylating activity."; /evidence="ECO:0000269|PubMed:11459942, ECO:0000269|PubMed:20943661"; MUTAGEN 1058; /note="R->A: Induces lower protein kinase activity."; /evidence="ECO:0000269|PubMed:20943661"; MUTAGEN 1058; /note="R->K: Does not affect protein kinase activity."; /evidence="ECO:0000269|PubMed:20943661"; MUTAGEN 1151; /note="A->K: Induces lower protein kinase activity and ability to autophosphorylate."; /evidence="ECO:0000269|PubMed:20943661"; MUTAGEN 1152; /note="Y->F: Induces lower protein kinase activity."; /evidence="ECO:0000269|PubMed:20943661"; MUTAGEN 1161; /note="T->A: Loss of catalytic activity (PubMed:11459942). According to another report, does not affect the protein kinase activity (PubMed:20943661). Does not affect protein translation."; /evidence="ECO:0000269|PubMed:11459942, ECO:0000269|PubMed:17595531, ECO:0000269|PubMed:20943661"; MUTAGEN 1165; /note="T->A: Loss of catalytic activity. Does not affect protein translation."; /evidence="ECO:0000269|PubMed:11459942, ECO:0000269|PubMed:17595531
uniprot
proteins
post_translational_modification
PTM: Autophosphorylated on Thr-1161 and Thr-1165. Autophosphorylation is activated by phospholipids. {ECO:0000269|PubMed:11459942}.
uniprot
proteins
protein_family
CAMK Ser/Thr protein kinase family
uniprot
proteins
protein_family
Protein kinase superfamily
uniprot
proteins
pubmed
11459942
uniprot
proteins
pubmed
12168954
uniprot
proteins
pubmed
12377121
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
15815621
uniprot
proteins
pubmed
16275910
uniprot
proteins
pubmed
17052199
uniprot
proteins
pubmed
17344846
uniprot
proteins
pubmed
17595531
uniprot
proteins
pubmed
17974005
uniprot
proteins
pubmed
18669648
uniprot
proteins
pubmed
19189049
uniprot
proteins
pubmed
19690332
uniprot
proteins
pubmed
20943661
uniprot
proteins
pubmed
21181396
uniprot
proteins
pubmed
21418524
uniprot
proteins
pubmed
22814378
uniprot
proteins
pubmed
23186163
uniprot
proteins
pubmed
8590280
uniprot
proteins
pubmed
9110174
uniprot
proteins
sequence_length
1323
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:17595531}. Nucleus {ECO:0000269|PubMed:17595531}. Note=Localizes in the nucleus of testis germ cells and in the midpiece of sperm tails.
uniprot
proteins