PASK_HUMAN - dbPTM
PASK_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID PASK_HUMAN
UniProt AC Q96RG2
Protein Name PAS domain-containing serine/threonine-protein kinase
Gene Name PASK
Organism Homo sapiens (Human).
Sequence Length 1323
Subcellular Localization Cytoplasm . Nucleus . Localizes in the nucleus of testis germ cells and in the midpiece of sperm tails.
Protein Description 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..
Protein Sequence MEDGGLTAFEEDQRCLSQSLPLPVSAEGPAAQTTAEPSRSFSSAHRHLSRRNGLSRLCQSRTALSEDRWSSYCLSSLAAQNICTSKLHCPAAPEHTDPSEPRGSVSCCSLLRGLSSGWSSPLLPAPVCNPNKAIFTVDAKTTEILVANDKACGLLGYSSQDLIGQKLTQFFLRSDSDVVEALSEEHMEADGHAAVVFGTVVDIISRSGEKIPVSVWMKRMRQERRLCCVVVLEPVERVSTWVAFQSDGTVTSCDSLFAHLHGYVSGEDVAGQHITDLIPSVQLPPSGQHIPKNLKIQRSVGRARDGTTFPLSLKLKSQPSSEEATTGEAAPVSGYRASVWVFCTISGLITLLPDGTIHGINHSFALTLFGYGKTELLGKNITFLIPGFYSYMDLAYNSSLQLPDLASCLDVGNESGCGERTLDPWQGQDPAEGGQDPRINVVLAGGHVVPRDEIRKLMESQDIFTGTQTELIAGGQLLSCLSPQPAPGVDNVPEGSLPVHGEQALPKDQQITALGREEPVAIESPGQDLLGESRSEPVDVKPFASCEDSEAPVPAEDGGSDAGMCGLCQKAQLERMGVSGPSGSDLWAGAAVAKPQAKGQLAGGSLLMHCPCYGSEWGLWWRSQDLAPSPSGMAGLSFGTPTLDEPWLGVENDREELQTCLIKEQLSQLSLAGALDVPHAELVPTECQAVTAPVSSCDLGGRDLCGGCTGSSSACYALATDLPGGLEAVEAQEVDVNSFSWNLKELFFSDQTDQTSSNCSCATSELRETPSSLAVGSDPDVGSLQEQGSCVLDDRELLLLTGTCVDLGQGRRFRESCVGHDPTEPLEVCLVSSEHYAASDRESPGHVPSTLDAGPEDTCPSAEEPRLNVQVTSTPVIVMRGAAGLQREIQEGAYSGSCYHRDGLRLSIQFEVRRVELQGPTPLFCCWLVKDLLHSQRDSAARTRLFLASLPGSTHSTAAELTGPSLVEVLRARPWFEEPPKAVELEGLAACEGEYSQKYSTMSPLGSGAFGFVWTAVDKEKNKEVVVKFIKKEKVLEDCWIEDPKLGKVTLEIAILSRVEHANIIKVLDIFENQGFFQLVMEKHGSGLDLFAFIDRHPRLDEPLASYIFRQLVSAVGYLRLKDIIHRDIKDENIVIAEDFTIKLIDFGSAAYLERGKLFYTFCGTIEYCAPEVLMGNPYRGPELEMWSLGVTLYTLVFEENPFCELEETVEAAIHPPYLVSKELMSLVSGLLQPVPERRTTLEKLVTDPWVTQPVNLADYTWEEVFRVNKPESGVLSAASLEMGNRSLSDVAQAQELCGGPVPGEAPNGQGCLHPGDPRLLTS
Overview of Protein Modification Sites with Functional and Structural Information
Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations Modification Substrate Peptides
&
Secondary Structure		 ASA (%) Reference Orthologous
Protein Cluster
1Acetylation-------MEDGGLTA
-------CCCCCCCC		45.1122814378
17PhosphorylationEEDQRCLSQSLPLPV
CCCHHHHHCCCCCCC		22.7327050516
19PhosphorylationDQRCLSQSLPLPVSA
CHHHHHCCCCCCCCC		28.6927050516
34PhosphorylationEGPAAQTTAEPSRSF
CCCCCCCCCCCCCCH		19.55-
40PhosphorylationTTAEPSRSFSSAHRH
CCCCCCCCHHHHHHH		33.5421712546
42PhosphorylationAEPSRSFSSAHRHLS
CCCCCCHHHHHHHHH		28.0623312004
55PhosphorylationLSRRNGLSRLCQSRT
HHHHCCHHHHHHHCC		25.30-
60PhosphorylationGLSRLCQSRTALSED
CHHHHHHHCCCCCCC		30.51-
62PhosphorylationSRLCQSRTALSEDRW
HHHHHHCCCCCCCHH		36.8828348404
65PhosphorylationCQSRTALSEDRWSSY
HHHCCCCCCCHHHHH		34.6828348404
70PhosphorylationALSEDRWSSYCLSSL
CCCCCHHHHHHHHHH		16.6028348404
71PhosphorylationLSEDRWSSYCLSSLA
CCCCHHHHHHHHHHH		16.9528348404
96PhosphorylationCPAAPEHTDPSEPRG
CCCCCCCCCCCCCCC		48.2028348404
99PhosphorylationAPEHTDPSEPRGSVS
CCCCCCCCCCCCCHH		64.1428348404
104PhosphorylationDPSEPRGSVSCCSLL
CCCCCCCCHHHHHHH		16.4928450419
106PhosphorylationSEPRGSVSCCSLLRG
CCCCCCHHHHHHHCC		15.8828450419
109PhosphorylationRGSVSCCSLLRGLSS
CCCHHHHHHHCCCCC		34.4628450419
115PhosphorylationCSLLRGLSSGWSSPL
HHHHCCCCCCCCCCC		29.6322617229
116PhosphorylationSLLRGLSSGWSSPLL
HHHCCCCCCCCCCCC		49.6921082442
119PhosphorylationRGLSSGWSSPLLPAP
CCCCCCCCCCCCCCC		26.1323898821
120PhosphorylationGLSSGWSSPLLPAPV
CCCCCCCCCCCCCCC		17.0428464451
132UbiquitinationAPVCNPNKAIFTVDA
CCCCCCCCEEEEEEC		44.08-
132 (in isoform 2)Ubiquitination-44.08-
218AcetylationIPVSVWMKRMRQERR
CCHHHHHHHHHHHHC		27.597481485
307PhosphorylationVGRARDGTTFPLSLK
ECCCCCCCEEEEEEE		29.56-
314UbiquitinationTTFPLSLKLKSQPSS
CEEEEEEEECCCCCC		50.96-
316UbiquitinationFPLSLKLKSQPSSEE
EEEEEEECCCCCCCC		45.5221906983
316 (in isoform 1)Ubiquitination-45.5221906983
316 (in isoform 2)Ubiquitination-45.5221906983
333PhosphorylationTGEAAPVSGYRASVW
CCCCCCCCCCCCEEE		29.1018669648
389PhosphorylationTFLIPGFYSYMDLAY
EEEECCHHHHHHHHC		12.57-
390PhosphorylationFLIPGFYSYMDLAYN
EEECCHHHHHHHHCC		16.24-
421PhosphorylationESGCGERTLDPWQGQ
CCCCCCCCCCCCCCC		31.0727732954
479PhosphorylationIAGGQLLSCLSPQPA
EECCEEEHHCCCCCC		22.9226074081
482PhosphorylationGQLLSCLSPQPAPGV
CEEEHHCCCCCCCCC		26.3026074081
512PhosphorylationLPKDQQITALGREEP
CCCCCCCEECCCCCC		16.1122210691
524PhosphorylationEEPVAIESPGQDLLG
CCCEEEECCCCCCCC		28.3730266825
533PhosphorylationGQDLLGESRSEPVDV
CCCCCCCCCCCCCCC		39.0330266825
570UbiquitinationGMCGLCQKAQLERMG
CCCHHHHHHHHHHHC		36.78-
579PhosphorylationQLERMGVSGPSGSDL
HHHHHCCCCCCHHHC		38.9828450419
582PhosphorylationRMGVSGPSGSDLWAG
HHCCCCCCHHHCCCC		55.2228464451
584PhosphorylationGVSGPSGSDLWAGAA
CCCCCCHHHCCCCCE		33.5928450419
594 (in isoform 2)Ubiquitination-30.9421906983
594 (in isoform 1)Ubiquitination-30.9421906983
594UbiquitinationWAGAAVAKPQAKGQL
CCCCEECCCCCCCCC		30.942190698
594AcetylationWAGAAVAKPQAKGQL
CCCCEECCCCCCCCC		30.9425953088
642PhosphorylationGLSFGTPTLDEPWLG
CCCCCCCCCCCCCCC		46.8317287469
667PhosphorylationCLIKEQLSQLSLAGA
HHHHHHHHHHHHCCC		28.8628348404
670PhosphorylationKEQLSQLSLAGALDV
HHHHHHHHHCCCCCC		14.4528348404
783PhosphorylationGSDPDVGSLQEQGSC
CCCCCCCCCCCCCCE		27.0826657352
832PhosphorylationPLEVCLVSSEHYAAS
CCEEEEEECCCCCCC		19.6328348404
833PhosphorylationLEVCLVSSEHYAASD
CEEEEEECCCCCCCC		22.4028348404
836PhosphorylationCLVSSEHYAASDRES
EEEECCCCCCCCCCC		10.3827642862
839PhosphorylationSSEHYAASDRESPGH
ECCCCCCCCCCCCCC		29.0928348404
843PhosphorylationYAASDRESPGHVPST
CCCCCCCCCCCCCCC		36.7625850435
849PhosphorylationESPGHVPSTLDAGPE
CCCCCCCCCCCCCCC		40.2827732954
850PhosphorylationSPGHVPSTLDAGPED
CCCCCCCCCCCCCCC		23.6927732954
872PhosphorylationPRLNVQVTSTPVIVM
CCCCEEEECCCEEEE		15.1423186163
873PhosphorylationRLNVQVTSTPVIVMR
CCCEEEECCCEEEEE		31.6829978859
874PhosphorylationLNVQVTSTPVIVMRG
CCEEEECCCEEEEEC		16.5329978859
895PhosphorylationEIQEGAYSGSCYHRD
HHHHCCCCCCCCCCC		24.5628985074
921PhosphorylationRVELQGPTPLFCCWL
EEECCCCCCEEHHHH		39.1724719451
930UbiquitinationLFCCWLVKDLLHSQR
EEHHHHHHHHHHHCC		40.25-
930 (in isoform 2)Ubiquitination-40.25-
935PhosphorylationLVKDLLHSQRDSAAR
HHHHHHHHCCHHHHH		27.2123401153
939PhosphorylationLLHSQRDSAARTRLF
HHHHCCHHHHHHHHH		26.4723401153
943PhosphorylationQRDSAARTRLFLASL
CCHHHHHHHHHHHCC		27.3122210691
949PhosphorylationRTRLFLASLPGSTHS
HHHHHHHCCCCCCCC		36.9320068231
953PhosphorylationFLASLPGSTHSTAAE
HHHCCCCCCCCCHHH		22.4720068231
954PhosphorylationLASLPGSTHSTAAEL
HHCCCCCCCCCHHHH		26.2620873877
956PhosphorylationSLPGSTHSTAAELTG
CCCCCCCCCHHHHHC		21.6020068231
957PhosphorylationLPGSTHSTAAELTGP
CCCCCCCCHHHHHCC		23.4528985074
962PhosphorylationHSTAAELTGPSLVEV
CCCHHHHHCCCHHHH		38.2520873877
965PhosphorylationAAELTGPSLVEVLRA
HHHHHCCCHHHHHHC		46.5220873877
981UbiquitinationPWFEEPPKAVELEGL
CCCCCCCCCEEEEHH		75.64-
999PhosphorylationEGEYSQKYSTMSPLG
CCCCCCCCCCCCCCC		11.18-
1000PhosphorylationGEYSQKYSTMSPLGS
CCCCCCCCCCCCCCC		25.35-
1001PhosphorylationEYSQKYSTMSPLGSG
CCCCCCCCCCCCCCC		20.69-
1003PhosphorylationSQKYSTMSPLGSGAF
CCCCCCCCCCCCCCC		19.63-
1034UbiquitinationVKFIKKEKVLEDCWI
EEEECHHHHEECCEE		62.08-
1045UbiquitinationDCWIEDPKLGKVTLE
CCEECCCCCCCEEEE		80.39-
1057PhosphorylationTLEIAILSRVEHANI
EEEEEHHHCCCCCCC		28.3220860994
1114PhosphorylationYIFRQLVSAVGYLRL
HHHHHHHHHHHHHHH		26.3228152594
1118PhosphorylationQLVSAVGYLRLKDII
HHHHHHHHHHHHHHH		5.0928152594
1122UbiquitinationAVGYLRLKDIIHRDI
HHHHHHHHHHHCCCC		40.21-
1129 (in isoform 2)Ubiquitination-6.46-
1161PhosphorylationERGKLFYTFCGTIEY
HCCCEEEEECCCHHH		12.7111459942
1165PhosphorylationLFYTFCGTIEYCAPE
EEEEECCCHHHHCHH		16.3020943661
1270UbiquitinationEEVFRVNKPESGVLS
HHHCCCCCCCCCCCC		47.51-
1273PhosphorylationFRVNKPESGVLSAAS
CCCCCCCCCCCCHHH		42.6118669648
1277 (in isoform 2)Ubiquitination-21.27-
1277PhosphorylationKPESGVLSAASLEMG
CCCCCCCCHHHHHCC		21.2725159151
1280PhosphorylationSGVLSAASLEMGNRS
CCCCCHHHHHCCCCC		25.2823401153
1287PhosphorylationSLEMGNRSLSDVAQA
HHHCCCCCHHHHHHH		35.9026074081
1289PhosphorylationEMGNRSLSDVAQAQE
HCCCCCHHHHHHHHH		31.1428450419
1322PhosphorylationPGDPRLLTS------
CCCCCCCCC------		36.66-
1323PhosphorylationGDPRLLTS-------
CCCCCCCC-------		37.89-
Upstream regulatory proteins (kinases for phosphorylation sites, E3 ubiquitin ligases of ubiquitination sites, ...)
Modified Location Modified Residue Modification Type of Upstream Proteins Gene Name of Upstream Proteins UniProt AC of Upstream Proteins Sources
1161TPhosphorylationKinasePASKQ96RG2
PSP
1165TPhosphorylationKinasePASKQ96RG2
PSP
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference
1161TPhosphorylation

11459942
1165TPhosphorylation

11459942
Disease-associated PTM Sites based on SAP

* Distance = the distance between SAP position and PTM sites.

Modified Location Modification Variant Position
(Distance <= 10) 		Residue Change SAP Related Disease Reference

Oops, there are no SNP-PTM records of PASK_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
STK16_HUMANSTK16physical
17353931
FBRL_HUMANFBLphysical
17353931
PSB1_HUMANPSMB1physical
17353931
WDR5_HUMANWDR5physical
17353931
AGO2_HUMANAGO2physical
24778252
AP1G1_HUMANAP1G1physical
24778252
PR14L_HUMANPRR14Lphysical
24778252
F120A_HUMANFAM120Aphysical
24778252
HJURP_HUMANHJURPphysical
24778252
IQGA3_HUMANIQGAP3physical
24778252
MAP7_HUMANMAP7physical
24778252
KI67_HUMANMKI67physical
24778252
NOL9_HUMANNOL9physical
24778252
NOM1_HUMANNOM1physical
24778252
P52K_HUMANPRKRIRphysical
24778252
PRP6_HUMANPRPF6physical
24778252
EMIL3_HUMANEMILIN3physical
24778252
ZBT21_HUMANZBTB21physical
24778252
AGO1_HUMANAGO1physical
24778252
OBSL1_HUMANOBSL1physical
24778252
ELP1_HUMANIKBKAPphysical
24778252
ZN628_HUMANZNF628physical
24778252
ZN574_HUMANZNF574physical
24778252
RAD50_HUMANRAD50physical
24778252
RECQ4_HUMANRECQL4physical
24778252
SENP5_HUMANSENP5physical
24778252
TAF6L_HUMANTAF6Lphysical
24778252
TF3C2_HUMANGTF3C2physical
24778252
TRM2A_HUMANTRMT2Aphysical
24778252
ZBT24_HUMANZBTB24physical
24778252
ZN638_HUMANZNF638physical
24778252
ZN768_HUMANZNF768physical
24778252
BAG6_HUMANBAG6physical
24778252
CEP78_HUMANCEP78physical
24778252
LAS1L_HUMANLAS1Lphysical
24778252
AAPK1_HUMANPRKAA1physical
22065581
PASK_HUMANPASKphysical
22065581
Drug and Disease Associations
Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
There are no disease associations of PTM sites.
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of PASK_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"A quantitative atlas of mitotic phosphorylation.";
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,Elledge S.J., Gygi S.P.;
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-524; SER-533; SER-1273;SER-1277 AND SER-1280, AND MASS SPECTROMETRY.
"Large-scale characterization of HeLa cell nuclear phosphoproteins.";
Beausoleil S.A., Jedrychowski M., Schwartz D., Elias J.E., Villen J.,Li J., Cohn M.A., Cantley L.C., Gygi S.P.;
Proc. Natl. Acad. Sci. U.S.A. 101:12130-12135(2004).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-116, AND MASSSPECTROMETRY.
"PAS kinase: an evolutionarily conserved PAS domain-regulatedserine/threonine kinase.";
Rutter J., Michnoff C.H., Harper S.M., Gardner K.H., McKnight S.L.;
Proc. Natl. Acad. Sci. U.S.A. 98:8991-8996(2001).
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), PHOSPHORYLATION AT THR-1161AND THR-1165, MUTAGENESIS OF LYS-1028; THR-1161 AND THR-1165, ANDVARIANT CYS-1266.

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