CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-019582
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 PAS domain-containing serine/threonine-protein kinase 
Protein Synonyms/Alias
 PAS-kinase; PASKIN; hPASK 
Gene Name
 PASK 
Gene Synonyms/Alias
 KIAA0135 
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
132APVCNPNKAIFTVDAubiquitination[1]
316FPLSLKLKSQPSSEEubiquitination[1]
594WAGAAVAKPQAKGQLubiquitination[1]
930LFCCWLVKDLLHSQRubiquitination[1]
1129AVGYLRLKDIIHRDIubiquitination[1]
1277EEVFRVNKPESGVLSubiquitination[1]
Reference
 [1] Refined preparation and use of anti-diglycine remnant (K-ε-GG) antibody enables routine quantification of 10,000s of ubiquitination sites in single proteomics experiments.
 Udeshi ND, Svinkina T, Mertins P, Kuhn E, Mani DR, Qiao JW, Carr SA.
 Mol Cell Proteomics. 2013 Mar;12(3):825-31. [PMID: 23266961
Functional 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. 
Sequence Annotation
 DOMAIN 119 190 PAS 1.
 DOMAIN 335 402 PAS 2.
 DOMAIN 999 1251 Protein kinase.
 NP_BIND 1005 1013 ATP.
 NP_BIND 1082 1089 ATP.
 ACT_SITE 1128 1128 Proton acceptor.
 BINDING 1028 1028 ATP.
 BINDING 1146 1146 ATP.
 MOD_RES 1161 1161 Phosphothreonine; by autocatalysis.
 MOD_RES 1165 1165 Phosphothreonine; by autocatalysis.  
Keyword
 3D-structure; Alternative splicing; ATP-binding; Complete proteome; Cytoplasm; Kinase; Lipid-binding; Nucleotide-binding; Nucleus; Phosphoprotein; Polymorphism; Reference proteome; Repeat; Serine/threonine-protein kinase; Transferase. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 1323 AA 
Protein Sequence
MEDGGLTAFE EDQRCLSQSL PLPVSAEGPA AQTTAEPSRS FSSAHRHLSR RNGLSRLCQS 60
RTALSEDRWS SYCLSSLAAQ NICTSKLHCP AAPEHTDPSE PRGSVSCCSL LRGLSSGWSS 120
PLLPAPVCNP NKAIFTVDAK TTEILVANDK ACGLLGYSSQ DLIGQKLTQF FLRSDSDVVE 180
ALSEEHMEAD GHAAVVFGTV VDIISRSGEK IPVSVWMKRM RQERRLCCVV VLEPVERVST 240
WVAFQSDGTV TSCDSLFAHL HGYVSGEDVA GQHITDLIPS VQLPPSGQHI PKNLKIQRSV 300
GRARDGTTFP LSLKLKSQPS SEEATTGEAA PVSGYRASVW VFCTISGLIT LLPDGTIHGI 360
NHSFALTLFG YGKTELLGKN ITFLIPGFYS YMDLAYNSSL QLPDLASCLD VGNESGCGER 420
TLDPWQGQDP AEGGQDPRIN VVLAGGHVVP RDEIRKLMES QDIFTGTQTE LIAGGQLLSC 480
LSPQPAPGVD NVPEGSLPVH GEQALPKDQQ ITALGREEPV AIESPGQDLL GESRSEPVDV 540
KPFASCEDSE APVPAEDGGS DAGMCGLCQK AQLERMGVSG PSGSDLWAGA AVAKPQAKGQ 600
LAGGSLLMHC PCYGSEWGLW WRSQDLAPSP SGMAGLSFGT PTLDEPWLGV ENDREELQTC 660
LIKEQLSQLS LAGALDVPHA ELVPTECQAV TAPVSSCDLG GRDLCGGCTG SSSACYALAT 720
DLPGGLEAVE AQEVDVNSFS WNLKELFFSD QTDQTSSNCS CATSELRETP SSLAVGSDPD 780
VGSLQEQGSC VLDDRELLLL TGTCVDLGQG RRFRESCVGH DPTEPLEVCL VSSEHYAASD 840
RESPGHVPST LDAGPEDTCP SAEEPRLNVQ VTSTPVIVMR GAAGLQREIQ EGAYSGSCYH 900
RDGLRLSIQF EVRRVELQGP TPLFCCWLVK DLLHSQRDSA ARTRLFLASL PGSTHSTAAE 960
LTGPSLVEVL RARPWFEEPP KAVELEGLAA CEGEYSQKYS TMSPLGSGAF GFVWTAVDKE 1020
KNKEVVVKFI KKEKVLEDCW IEDPKLGKVT LEIAILSRVE HANIIKVLDI FENQGFFQLV 1080
MEKHGSGLDL FAFIDRHPRL DEPLASYIFR QVRAGQSRLV SAVGYLRLKD IIHRDIKDEN 1140
IVIAEDFTIK LIDFGSAAYL ERGKLFYTFC GTIEYCAPEV LMGNPYRGPE LEMWSLGVTL 1200
YTLVFEENPF CELEETVEAA IHPPYLVSKE LMSLVSGLLQ PVPERRTTLE KLVTDPWVTQ 1260
PVNLADYTWE EVFRVNKPES GVLSAASLEM GNRSLSDVAQ AQELCGGPVP GEAPNGQGCL 1320
HPGDPRLLTS 1330 
Gene Ontology
 GO:0005794; C:Golgi apparatus; IDA:HPA.
 GO:0005634; C:nucleus; IDA:UniProtKB.
 GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
 GO:0035091; F:phosphatidylinositol binding; IDA:UniProtKB.
 GO:0004674; F:protein serine/threonine kinase activity; IDA:UniProtKB.
 GO:0004871; F:signal transducer activity; IEA:InterPro.
 GO:0045719; P:negative regulation of glycogen biosynthetic process; IDA:UniProtKB.
 GO:0045727; P:positive regulation of translation; TAS:UniProtKB.
 GO:0046777; P:protein autophosphorylation; IDA:UniProtKB.
 GO:2000505; P:regulation of energy homeostasis; ISS:UniProtKB.
 GO:0070092; P:regulation of glucagon secretion; ISS:UniProtKB.
 GO:0043576; P:regulation of respiratory gaseous exchange; ISS:UniProtKB. 
Interpro
 IPR011009; Kinase-like_dom.
 IPR000014; PAS.
 IPR000719; Prot_kinase_cat_dom.
 IPR017441; Protein_kinase_ATP_BS.
 IPR002290; Ser/Thr_dual-sp_kinase_dom.
 IPR008271; Ser/Thr_kinase_AS. 
Pfam
 PF00069; Pkinase 
SMART
 SM00091; PAS
 SM00220; S_TKc 
PROSITE
 PS50112; PAS
 PS00107; PROTEIN_KINASE_ATP
 PS50011; PROTEIN_KINASE_DOM
 PS00108; PROTEIN_KINASE_ST 
PRINTS