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Q96RG2 (PASK_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 145. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (7) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
PAS domain-containing serine/threonine-protein kinase

Short name=PAS-kinase
Short name=PASKIN
Short name=hPASK
EC=2.7.11.1
Gene names
Name:PASK
Synonyms:KIAA0135
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length1323 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

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 evidences. May play a role in regulation of protein translation by phosphorylating EEF1A1, leading to increase translation efficiency. May also participate to respiratory regulation. Ref.9 Ref.10 Ref.11 Ref.14 Ref.15 Ref.19

Catalytic activity

ATP + a protein = ADP + a phosphoprotein.

Enzyme 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 (Ref.1). 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 (Ref.19). 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). Ref.15

Subcellular location

Cytoplasm. Nucleus. Note: Localizes in the nucleus of testis germ cells and in the midpiece of sperm tails. Ref.11

Tissue specificity

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 (at protein level).

Domain

The protein kinase domain mediates binding to phosphatidylinositol. Ref.15

Post-translational modification

Autophosphorylated on Thr-1161 and Thr-1165. Autophosphorylation is activated by phospholipids. Ref.1 Ref.11 Ref.15 Ref.19

Sequence similarities

Belongs to the protein kinase superfamily. CAMK Ser/Thr protein kinase family.

Contains 2 PAS (PER-ARNT-SIM) domains.

Contains 1 protein kinase domain.

Sequence caution

The sequence BAA09484.2 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.

Ontologies

Keywords
   Cellular componentCytoplasm
Nucleus
   Coding sequence diversityAlternative splicing
Polymorphism
   DomainRepeat
   LigandATP-binding
Lipid-binding
Nucleotide-binding
   Molecular functionKinase
Serine/threonine-protein kinase
Transferase
   PTMAcetylation
Phosphoprotein
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processnegative regulation of glycogen biosynthetic process

Inferred from direct assay Ref.9. Source: UniProtKB

positive regulation of translation

Traceable author statement Ref.11. Source: UniProtKB

protein autophosphorylation

Inferred from direct assay Ref.19Ref.15. Source: UniProtKB

protein phosphorylation

Inferred from direct assay Ref.9. Source: UniProtKB

regulation of energy homeostasis

Inferred from sequence or structural similarity. Source: UniProtKB

regulation of glucagon secretion

Inferred from sequence or structural similarity. Source: UniProtKB

regulation of respiratory gaseous exchange

Inferred from sequence or structural similarity. Source: UniProtKB

   Cellular_componentGolgi apparatus

Inferred from direct assay. Source: HPA

cytoplasm

Inferred from direct assay Ref.11. Source: UniProtKB

nucleus

Inferred from direct assay Ref.11. Source: UniProtKB

   Molecular_functionATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

phosphatidylinositol binding

Inferred from direct assay Ref.15. Source: UniProtKB

protein binding

Inferred from physical interaction Ref.9Ref.11Ref.15. Source: UniProtKB

protein serine/threonine kinase activity

Inferred from direct assay Ref.9Ref.11Ref.19Ref.15. Source: UniProtKB

signal transducer activity

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

CACNA1SP072932EBI-1042651,EBI-8613624From a different organism.
CREB1P162202EBI-1042651,EBI-711855
DESP025422EBI-1042651,EBI-8614455From a different organism.
GFAPQ281152EBI-1042651,EBI-907866From a different organism.
LMNAP025452EBI-1042651,EBI-351935
PHKBQ931002EBI-1042651,EBI-740559
RPS6P627533EBI-1042651,EBI-356625
TNNI3P026462EBI-1042651,EBI-8614386From a different organism.
VimP201522EBI-1042651,EBI-299269From a different organism.

Alternative products

This entry describes 3 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q96RG2-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
Isoform 2 (identifier: Q96RG2-2)

The sequence of this isoform differs from the canonical sequence as follows:
     1111-1111: Q → QVRAGQSR
Note: No experimental confirmation available.
Isoform 3 (identifier: Q96RG2-4)

The sequence of this isoform differs from the canonical sequence as follows:
     1112-1143: LVSAVGYLRLKDIIHRDIKDENIVIAEDFTIK → VRAGQSRVSVNAGLGAWVRWLQRSVIHTRFSL
     1144-1323: Missing.
Note: No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 13231323PAS domain-containing serine/threonine-protein kinase
PRO_0000086480

Regions

Domain119 – 19072PAS 1
Domain335 – 40268PAS 2
Domain999 – 1251253Protein kinase
Nucleotide binding1005 – 10139ATP
Nucleotide binding1082 – 10898ATP

Sites

Active site11281Proton acceptor
Binding site10281ATP
Binding site11461ATP

Amino acid modifications

Modified residue11N-acetylmethionine Ref.17
Modified residue11611Phosphothreonine; by autocatalysis Ref.1
Modified residue11651Phosphothreonine; by autocatalysis Ref.1

Natural variations

Alternative sequence11111Q → QVRAGQSR in isoform 2.
VSP_009302
Alternative sequence1112 – 114332LVSAV…DFTIK → VRAGQSRVSVNAGLGAWVRW LQRSVIHTRFSL in isoform 3.
VSP_045543
Alternative sequence1144 – 1323180Missing in isoform 3.
VSP_045544
Natural variant111E → K in a metastatic melanoma sample; somatic mutation. Ref.20
VAR_040986
Natural variant2501V → I. Ref.7 Ref.20
Corresponds to variant rs1470414 [ dbSNP | Ensembl ].
VAR_028293
Natural variant4261Q → R. Ref.20
Corresponds to variant rs35187712 [ dbSNP | Ensembl ].
VAR_040987
Natural variant5121T → A. Ref.20
Corresponds to variant rs56033464 [ dbSNP | Ensembl ].
VAR_040988
Natural variant5141L → S. Ref.20
Corresponds to variant rs2240543 [ dbSNP | Ensembl ].
VAR_028294
Natural variant6841P → R. Ref.20
Corresponds to variant rs56372985 [ dbSNP | Ensembl ].
VAR_040989
Natural variant6941V → M. Ref.2
Corresponds to variant rs6727226 [ dbSNP | Ensembl ].
VAR_028295
Natural variant7251G → D. Ref.20
Corresponds to variant rs2005771 [ dbSNP | Ensembl ].
VAR_028296
Natural variant7961E → K. Ref.20
Corresponds to variant rs35129131 [ dbSNP | Ensembl ].
VAR_040990
Natural variant8441P → Q. Ref.20
Corresponds to variant rs36082918 [ dbSNP | Ensembl ].
VAR_040991
Natural variant9371R → H. Ref.20
Corresponds to variant rs56139954 [ dbSNP | Ensembl ].
VAR_040992
Natural variant12101V → M. Ref.20
Corresponds to variant rs10167000 [ dbSNP | Ensembl ].
VAR_028297
Natural variant12661F → C. Ref.1 Ref.2 Ref.20
Corresponds to variant rs1131293 [ dbSNP | Ensembl ].
VAR_028298
Natural variant13011P → S. Ref.20
VAR_040993

Experimental info

Mutagenesis10281K → R: Loss of autophosphorylating activity. Ref.1 Ref.19
Mutagenesis10581R → A: Induces lower protein kinase activity. Ref.19
Mutagenesis10581R → K: Does not affect protein kinase activity. Ref.19
Mutagenesis11511A → K: Induces lower protein kinase activity and ability to autophosphorylate. Ref.19
Mutagenesis11521Y → F: Induces lower protein kinase activity. Ref.19
Mutagenesis11611T → 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. Ref.1 Ref.11 Ref.19
Mutagenesis11651T → A: Loss of catalytic activity. Does not affect protein translation. Ref.1 Ref.11
Sequence conflict2051S → T in BAA09484. Ref.2
Sequence conflict4071S → C in CAH18087. Ref.4
Sequence conflict6231S → R in BAA09484. Ref.2
Sequence conflict7411W → R in CAH18087. Ref.4
Sequence conflict8501T → M in BAA09484. Ref.2
Sequence conflict8991Y → H in AAK69752. Ref.1
Sequence conflict10481K → E in CAH18087. Ref.4
Sequence conflict10621A → S in AAH50565. Ref.7
Sequence conflict11291I → F in AAB50198. Ref.8

Secondary structure

......................................................................... 1323
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified October 17, 2006. Version 3.
Checksum: F8A3633CC6F6C8CD

FASTA1,323142,929
        10         20         30         40         50         60 
MEDGGLTAFE EDQRCLSQSL PLPVSAEGPA AQTTAEPSRS FSSAHRHLSR RNGLSRLCQS 

        70         80         90        100        110        120 
RTALSEDRWS SYCLSSLAAQ NICTSKLHCP AAPEHTDPSE PRGSVSCCSL LRGLSSGWSS 

       130        140        150        160        170        180 
PLLPAPVCNP NKAIFTVDAK TTEILVANDK ACGLLGYSSQ DLIGQKLTQF FLRSDSDVVE 

       190        200        210        220        230        240 
ALSEEHMEAD GHAAVVFGTV VDIISRSGEK IPVSVWMKRM RQERRLCCVV VLEPVERVST 

       250        260        270        280        290        300 
WVAFQSDGTV TSCDSLFAHL HGYVSGEDVA GQHITDLIPS VQLPPSGQHI PKNLKIQRSV 

       310        320        330        340        350        360 
GRARDGTTFP LSLKLKSQPS SEEATTGEAA PVSGYRASVW VFCTISGLIT LLPDGTIHGI 

       370        380        390        400        410        420 
NHSFALTLFG YGKTELLGKN ITFLIPGFYS YMDLAYNSSL QLPDLASCLD VGNESGCGER 

       430        440        450        460        470        480 
TLDPWQGQDP AEGGQDPRIN VVLAGGHVVP RDEIRKLMES QDIFTGTQTE LIAGGQLLSC 

       490        500        510        520        530        540 
LSPQPAPGVD NVPEGSLPVH GEQALPKDQQ ITALGREEPV AIESPGQDLL GESRSEPVDV 

       550        560        570        580        590        600 
KPFASCEDSE APVPAEDGGS DAGMCGLCQK AQLERMGVSG PSGSDLWAGA AVAKPQAKGQ 

       610        620        630        640        650        660 
LAGGSLLMHC PCYGSEWGLW WRSQDLAPSP SGMAGLSFGT PTLDEPWLGV ENDREELQTC 

       670        680        690        700        710        720 
LIKEQLSQLS LAGALDVPHA ELVPTECQAV TAPVSSCDLG GRDLCGGCTG SSSACYALAT 

       730        740        750        760        770        780 
DLPGGLEAVE AQEVDVNSFS WNLKELFFSD QTDQTSSNCS CATSELRETP SSLAVGSDPD 

       790        800        810        820        830        840 
VGSLQEQGSC VLDDRELLLL TGTCVDLGQG RRFRESCVGH DPTEPLEVCL VSSEHYAASD 

       850        860        870        880        890        900 
RESPGHVPST LDAGPEDTCP SAEEPRLNVQ VTSTPVIVMR GAAGLQREIQ EGAYSGSCYH 

       910        920        930        940        950        960 
RDGLRLSIQF EVRRVELQGP TPLFCCWLVK DLLHSQRDSA ARTRLFLASL PGSTHSTAAE 

       970        980        990       1000       1010       1020 
LTGPSLVEVL RARPWFEEPP KAVELEGLAA CEGEYSQKYS TMSPLGSGAF GFVWTAVDKE 

      1030       1040       1050       1060       1070       1080 
KNKEVVVKFI KKEKVLEDCW IEDPKLGKVT LEIAILSRVE HANIIKVLDI FENQGFFQLV 

      1090       1100       1110       1120       1130       1140 
MEKHGSGLDL FAFIDRHPRL DEPLASYIFR QLVSAVGYLR LKDIIHRDIK DENIVIAEDF 

      1150       1160       1170       1180       1190       1200 
TIKLIDFGSA AYLERGKLFY TFCGTIEYCA PEVLMGNPYR GPELEMWSLG VTLYTLVFEE 

      1210       1220       1230       1240       1250       1260 
NPFCELEETV EAAIHPPYLV SKELMSLVSG LLQPVPERRT TLEKLVTDPW VTQPVNLADY 

      1270       1280       1290       1300       1310       1320 
TWEEVFRVNK PESGVLSAAS LEMGNRSLSD VAQAQELCGG PVPGEAPNGQ GCLHPGDPRL 


LTS 

« Hide

Isoform 2 [UniParc].

Checksum: 8177593F181C6914
Show »

FASTA1,330143,684
Isoform 3 [UniParc].

Checksum: 535BFCA305C18419
Show »

FASTA1,143123,048

References

« Hide 'large scale' references
[1]"PAS kinase: an evolutionarily conserved PAS domain-regulated serine/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) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), PHOSPHORYLATION AT THR-1161 AND THR-1165, MUTAGENESIS OF LYS-1028; THR-1161 AND THR-1165, VARIANT CYS-1266.
Tissue: Cervix carcinoma.
[2]"Prediction of the coding sequences of unidentified human genes. IV. The coding sequences of 40 new genes (KIAA0121-KIAA0160) deduced by analysis of cDNA clones from human cell line KG-1."
Nagase T., Seki N., Tanaka A., Ishikawa K., Nomura N.
DNA Res. 2:167-174(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), VARIANTS MET-694 AND CYS-1266.
Tissue: Bone marrow.
[3]"Construction of expression-ready cDNA clones for KIAA genes: manual curation of 330 KIAA cDNA clones."
Nakajima D., Okazaki N., Yamakawa H., Kikuno R., Ohara O., Nagase T.
DNA Res. 9:99-106(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: SEQUENCE REVISION.
[4]"The full-ORF clone resource of the German cDNA consortium."
Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U., Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A., Wiemann S., Schupp I.
BMC Genomics 8:399-399(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
Tissue: Testis.
[5]"Generation and annotation of the DNA sequences of human chromosomes 2 and 4."
Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L., Du H. expand/collapse author list , Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K., McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C., Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S., Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H., Wilson R.K.
Nature 434:724-731(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[6]Mural R.J., Istrail S., Sutton G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[7]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 3), VARIANT ILE-250.
Tissue: Eye, Lymph and Testis.
[8]"Large-scale concatenation cDNA sequencing."
Yu W., Andersson B., Worley K.C., Muzny D.M., Ding Y., Liu W., Ricafrente J.Y., Wentland M.A., Lennon G., Gibbs R.A.
Genome Res. 7:353-358(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 866-1323 (ISOFORM 1).
Tissue: Brain.
[9]"Control of mammalian glycogen synthase by PAS kinase."
Wilson W.A., Skurat A.V., Probst B., de Paoli-Roach A., Roach P.J., Rutter J.
Proc. Natl. Acad. Sci. U.S.A. 102:16596-16601(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION IN PHOSPHORYLATION OF GYS1.
[10]"Regulation by Per-Arnt-Sim (PAS) kinase of pancreatic duodenal homeobox-1 nuclear import in pancreatic beta-cells."
An R., da Silva Xavier G., Hao H.X., Semplici F., Rutter J., Rutter G.A.
Biochem. Soc. Trans. 34:791-793(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION IN PHOSPHORYLATION OF PDX1.
[11]"Male germ cell expression of the PAS domain kinase PASKIN and its novel target eukaryotic translation elongation factor eEF1A1."
Eckhardt K., Troger J., Reissmann J., Katschinski D.M., Wagner K.F., Stengel P., Paasch U., Hunziker P., Borter E., Barth S., Schlafli P., Spielmann P., Stiehl D.P., Camenisch G., Wenger R.H.
Cell. Physiol. Biochem. 20:227-240(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION IN PHOSPHORYLATION OF EEF1A1, AUTOPHOSPHORYLATION, SUBCELLULAR LOCATION, MUTAGENESIS OF THR-1161 AND THR-1165.
[12]"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) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[13]"Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Leukemic T-cell.
[14]"Per-arnt-sim (PAS) domain-containing protein kinase is downregulated in human islets in type 2 diabetes and regulates glucagon secretion."
da Silva Xavier G., Farhan H., Kim H., Caxaria S., Johnson P., Hughes S., Bugliani M., Marselli L., Marchetti P., Birzele F., Sun G., Scharfmann R., Rutter J., Siniakowicz K., Weir G., Parker H., Reimann F., Gribble F.M., Rutter G.A.
Diabetologia 54:819-827(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[15]"Substrate preference and phosphatidylinositol monophosphate inhibition of the catalytic domain of the Per-Arnt-Sim domain kinase PASKIN."
Schlafli P., Troger J., Eckhardt K., Borter E., Spielmann P., Wenger R.H.
FEBS J. 278:1757-1768(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION IN PHOSPHORYLATION OF RPS6, ENZYME REGULATION, DOMAIN PROTEIN KINASE, AUTOPHOSPHORYLATION, LIPID-BINDING.
[16]"The PAS-domain kinase PASKIN: a new sensor in energy homeostasis."
Schlafli P., Borter E., Spielmann P., Wenger R.H.
Cell. Mol. Life Sci. 66:876-883(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: REVIEW ON FUNCTION.
[17]"N-terminal acetylome analyses and functional insights of the N-terminal acetyltransferase NatB."
Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A., Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[18]"Structure and interactions of PAS kinase N-terminal PAS domain: model for intramolecular kinase regulation."
Amezcua C.A., Harper S.M., Rutter J., Gardner K.H.
Structure 10:1349-1361(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: STRUCTURE BY NMR OF 131-237.
[19]"Structural bases of PAS domain-regulated kinase (PASK) activation in the absence of activation loop phosphorylation."
Kikani C.K., Antonysamy S.A., Bonanno J.B., Romero R., Zhang F.F., Russell M., Gheyi T., Iizuka M., Emtage S., Sauder J.M., Turk B.E., Burley S.K., Rutter J.
J. Biol. Chem. 285:41034-41043(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 977-1300 IN COMPLEX WITH ADP, AUTOPHOSPHORYLATION, FUNCTION, MUTAGENESIS OF LYS-1028; ARG-1058; ALA-1151; TYR-1152 AND THR-1161.
[20]"Patterns of somatic mutation in human cancer genomes."
Greenman C., Stephens P., Smith R., Dalgliesh G.L., Hunter C., Bignell G., Davies H., Teague J., Butler A., Stevens C., Edkins S., O'Meara S., Vastrik I., Schmidt E.E., Avis T., Barthorpe S., Bhamra G., Buck G. expand/collapse author list , Choudhury B., Clements J., Cole J., Dicks E., Forbes S., Gray K., Halliday K., Harrison R., Hills K., Hinton J., Jenkinson A., Jones D., Menzies A., Mironenko T., Perry J., Raine K., Richardson D., Shepherd R., Small A., Tofts C., Varian J., Webb T., West S., Widaa S., Yates A., Cahill D.P., Louis D.N., Goldstraw P., Nicholson A.G., Brasseur F., Looijenga L., Weber B.L., Chiew Y.-E., DeFazio A., Greaves M.F., Green A.R., Campbell P., Birney E., Easton D.F., Chenevix-Trench G., Tan M.-H., Khoo S.K., Teh B.T., Yuen S.T., Leung S.Y., Wooster R., Futreal P.A., Stratton M.R.
Nature 446:153-158(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS [LARGE SCALE ANALYSIS] LYS-11; ILE-250; ARG-426; ALA-512; SER-514; ARG-684; ASP-725; LYS-796; GLN-844; HIS-937; MET-1210; CYS-1266 AND SER-1301.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF387103 mRNA. Translation: AAK69752.1.
D50925 mRNA. Translation: BAA09484.2. Different initiation.
CR749231 mRNA. Translation: CAH18087.1.
AC005237 Genomic DNA. No translation available.
CH471063 Genomic DNA. Translation: EAW71238.1.
BC043495 mRNA. Translation: AAH43495.1.
BC050565 mRNA. Translation: AAH50565.1.
BC063585 mRNA. Translation: AAH63585.1.
U79240 mRNA. Translation: AAB50198.1.
CCDSCCDS2545.1. [Q96RG2-1]
CCDS58758.1. [Q96RG2-4]
CCDS58759.1. [Q96RG2-2]
PIRT17211.
RefSeqNP_001239048.1. NM_001252119.1. [Q96RG2-2]
NP_001239049.1. NM_001252120.1. [Q96RG2-1]
NP_001239051.1. NM_001252122.1.
NP_001239053.1. NM_001252124.1. [Q96RG2-4]
NP_055963.2. NM_015148.3. [Q96RG2-1]
UniGeneHs.397891.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1LL8NMR-A131-237[»]
3DLSX-ray2.30A/B/C/D/E/F977-1300[»]
ProteinModelPortalQ96RG2.
SMRQ96RG2. Positions 131-237, 346-386, 929-1292.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid116790. 7 interactions.
IntActQ96RG2. 52 interactions.
STRING9606.ENSP00000234040.

Chemistry

BindingDBQ96RG2.
ChEMBLCHEMBL6054.
GuidetoPHARMACOLOGY2139.

PTM databases

PhosphoSiteQ96RG2.

Polymorphism databases

DMDM116242701.

Proteomic databases

MaxQBQ96RG2.
PaxDbQ96RG2.
PRIDEQ96RG2.

Protocols and materials databases

DNASU23178.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000234040; ENSP00000234040; ENSG00000115687. [Q96RG2-1]
ENST00000358649; ENSP00000351475; ENSG00000115687. [Q96RG2-2]
ENST00000403638; ENSP00000384438; ENSG00000115687. [Q96RG2-4]
ENST00000405260; ENSP00000384016; ENSG00000115687. [Q96RG2-1]
GeneID23178.
KEGGhsa:23178.
UCSCuc002wao.2. human. [Q96RG2-1]
uc002wap.3. human.
uc010fzl.2. human. [Q96RG2-2]

Organism-specific databases

CTD23178.
GeneCardsGC02M242045.
HGNCHGNC:17270. PASK.
HPAHPA016450.
HPA021079.
MIM607505. gene.
neXtProtNX_Q96RG2.
PharmGKBPA32953.
HUGESearch...
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG0515.
HOGENOMHOG000115456.
HOVERGENHBG047936.
KOK08801.
OMAVANDKAC.
OrthoDBEOG76HQ0W.
PhylomeDBQ96RG2.
TreeFamTF323242.

Enzyme and pathway databases

SignaLinkQ96RG2.

Gene expression databases

ArrayExpressQ96RG2.
BgeeQ96RG2.
CleanExHS_PASK.
GenevestigatorQ96RG2.

Family and domain databases

InterProIPR011009. Kinase-like_dom.
IPR000014. PAS.
IPR000719. Prot_kinase_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR002290. Ser/Thr_dual-sp_kinase_dom.
IPR008271. Ser/Thr_kinase_AS.
[Graphical view]
PfamPF13426. PAS_9. 1 hit.
PF00069. Pkinase. 1 hit.
[Graphical view]
SMARTSM00091. PAS. 2 hits.
SM00220. S_TKc. 1 hit.
[Graphical view]
SUPFAMSSF55785. SSF55785. 1 hit.
SSF56112. SSF56112. 1 hit.
TIGRFAMsTIGR00229. sensory_box. 1 hit.
PROSITEPS50112. PAS. 1 hit.
PS00107. PROTEIN_KINASE_ATP. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00108. PROTEIN_KINASE_ST. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceQ96RG2.
GeneWikiPASK.
GenomeRNAi23178.
NextBio44625.
PROQ96RG2.
SOURCESearch...

Entry information

Entry namePASK_HUMAN
AccessionPrimary (citable) accession number: Q96RG2
Secondary accession number(s): G5E9F1 expand/collapse secondary AC list , Q05BE4, Q68DY3, Q6GSJ5, Q86XH6, Q99763, Q9UFR7
Entry history
Integrated into UniProtKB/Swiss-Prot: January 16, 2004
Last sequence update: October 17, 2006
Last modified: July 9, 2014
This is version 145 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Relevant documents

SIMILARITY comments

Index of protein domains and families

Human and mouse protein kinases

Human and mouse protein kinases: classification and index

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 2

Human chromosome 2: entries, gene names and cross-references to MIM