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Protein Page:
PASK (human)
p Phosphorylation
ac Acetylation
me Methylation
m1 Mono-methylation
m2 Di-methylation
m3 Tri-methylation
ub Ubiquitination
sm Sumoylation
ne Neddylation
gl O-GlcNAc
ga O-GalNAc
pa Palmitoylation
ad Adenylylation
sn S-Nitrosylation
ca Caspase cleavage
sc Succinylation

Overview
PASK 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 evidences. May play a role in regulation of protein translation by phosphorylating EEF1A1, leading to increase translation efficiency. May also participate to respiratory regulation. Ubiquitously expressed, with slightly higher expression in brain, prostate and testis. Reduced expression was found in placenta. Present in germ cells of testis and in the midpiece of sperm tails. 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). Belongs to the protein kinase superfamily. CAMK Ser/Thr protein kinase family. 2 isoforms of the human protein are produced by alternative splicing. Note: This description may include information from UniProtKB.
Protein type: Protein kinase, CAMK; EC 2.7.11.1; Protein kinase, Ser/Thr (non-receptor); Kinase, protein; CAMK group; CAMKL family; PASK subfamily
Cellular Component: Golgi apparatus; cytoplasm; nucleus
Molecular Function: protein serine/threonine kinase activity; protein binding; signal transducer activity; phosphoinositide binding; ATP binding
Biological Process: regulation of respiratory gaseous exchange; positive regulation of translation; protein amino acid autophosphorylation; signal transduction; protein amino acid phosphorylation; negative regulation of glycogen biosynthetic process
Reference #:  Q96RG2 (UniProtKB)
Alt. Names/Synonyms: DKFZp434O051; DKFZp686P2031; hPASK; KIAA0135; PAS domain containing serine/threonine kinase; PAS domain-containing serine/threonine-protein kinase; PAS-kinase; PAS-serine/threonine kinase; PASK; PASKIN; STK37
Gene Symbols: PASK
Molecular weight: 142,929 Da
Basal Isoelectric point: 4.75  Predict pI for various phosphorylation states
Protein-Specific Antibodies or siRNAs from Cell Signaling Technology® Total Proteins
Select Structure to View Below

PASK

Protein Structure Not Found.


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Modification Sites and Domains Show Modification Legend
Click here to view phosphorylation modifications only

Modification Sites in Parent Protein, Orthologs, and Isoforms Show Modification Legend
 

Show Multiple Sequence Alignment


 SS 

SS: The number of records in which this modification site was determined using site-specific methods. SS methods include amino acid sequencing, site-directed mutagenesis, modification site-specific antibodies, specific MS strategies, etc.


 MS 

MS: The number of records in which this modification site was assigned using ONLY proteomic discovery-mode mass spectrometry.


       human

 
0 3 S19-p DQRCLSQsLPLPVSA
0 1 T34 EGPAAQTTAEPSRsF
0 1 S40-p TTAEPSRsFSSAHRH
0 2 S55-p LSRRNGLsRLCQsRT
0 2 S60-p GLsRLCQsRTALSED
0 2 S104-p DPSEPRGsVsCCsLL
0 4 S106-p SEPRGsVsCCsLLRG
0 5 S109-p RGsVsCCsLLRGLSs
0 1 S116-p sLLRGLSsGWSSPLL
0 1 T142 FTVDAKTTEILVAND
0 1 K218-ac IPVSVWMkRMRQERR
0 1 K316-ub FPLSLKLkSQPSSEE
0 1 Y389-p TFLIPGFysYMDLAY
0 1 S390-p FLIPGFysYMDLAYN
0 1 N491 QPAPGVDNVPEGSLP
0 2 S524-p EEPVAIEsPGQDLLG
0 2 S533-p GQDLLGEsRSEPVDV
0 1 S579-p QLERMGVsGPsGSDL
0 2 S582-p RMGVsGPsGSDLWAG
0 1 K594-ub WAGAAVAkPQAKGQL
0 9 S667-p CLIKEQLsQLsLAGA
0 3 S670-p KEQLsQLsLAGALDV
0 1 G788 VGSLQEQGSCVLDDR
0 3 S789 GSLQEQGSCVLDDRE
0 1 G808 TGTCVDLGQGRRFRE
0 3 T874-p LNVQVTStPVIVMRG
0 1 S935 LVKDLLHSQRDsAAR
0 3 S939-p LLHSQRDsAARTRLF
0 3 S949-p RTRLFLAsLPGStHS
0 1 T954-p LAsLPGStHSTAAEL
0 1 Y999-p EGEYSQKystMsPLG
0 1 S1000-p GEYSQKystMsPLGS
0 1 T1001-p EYSQKystMsPLGSG
0 1 S1003-p SQKystMsPLGSGAF
1 0 T1161-p ERGKLFYtFCGtIEY
1 0 T1165-p LFYtFCGtIEYCAPE
0 1 S1273-p FRVNKPEsGVLsAAs
0 4 S1277-p KPEsGVLsAAsLEMG
0 4 S1280-p sGVLsAAsLEMGNRS
0 1 N1285 AAsLEMGNRSLSDVA
0 1 S1287 sLEMGNRSLSDVAQA
0 3 T1322-p PGDPRLLts______
0 1 S1323-p GDPRLLts_______
  mouse

 
S19-p DWKCLSEsPPVQEGP
T31-p EGPAAQAtFEPSKPL
P37 AtFEPSKPLSIAHKH
S52 LSRKNGLSRLCQSRM
S57 GLSRLCQSRMALSED
S102-p PTAGPLGsTsCCsLL
S104-p AGPLGsTsCCsLLRG
S107-p LGsTsCCsLLRGLAS
S114 sLLRGLASGCSGSLL
T140-p FTVDAKTtEILVAND
K216 IPVSVWIKRLQQDRG
K314 FPLSLKLKSKPSGRA
Y387 TFLIPGFYHYMDLTY
H388 FLIPGFYHYMDLTYD
S488-p QPSLGVDsNPEDGEQ
S591 EDPSAAESYRESLLE
S600 RESLLEESKSKPVDA
S646 QLELMGVSSPNPWAD
- gap
- gap
S730 CLIKEQLSKSSCEGN
S733 KEQLSKSSCEGNLGI
T851-p VGILHRQtsDILVDR
S852-p GILHRQtsDILVDRE
S871-p TGTYFDLsEGQRFQE
T937 PSAQITSTPVARGAT
S996-p LVKDLFHsHRDSATR
S1000 LFHsHRDSATRTRLF
S1010-p RTRLFLAsLPSSTHS
T1015 LAsLPSSTHSMPELS
Y1059 EGEYDYKYNTISPLG
N1060 GEYDYKYNTISPLGS
T1061 EYDYKYNTISPLGSG
S1063 DYKYNTISPLGSGAF
T1221 ERGKLFYTFCGTIEY
T1225 LFYTFCGTIEYCAPE
S1333 CRTNQPESGLLsAAs
S1337-p QPESGLLsAAsLEIG
S1340-p SGLLsAAsLEIGsRs
S1345-p AAsLEIGsRsPSEMA
S1347-p sLEIGsRsPSEMAQR
V1382 LKDPSLPVS______
S1383 KDPSLPVS_______
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