Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Basket 0
(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Q96RG2

- PASK_HUMAN

UniProt

Q96RG2 - PASK_HUMAN

Protein

PAS domain-containing serine/threonine-protein kinase

Gene

PASK

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 147 (01 Oct 2014)
      Sequence version 3 (17 Oct 2006)
      Previous versions | rss
    • Help video
    • Feedback
    • Comment

    Functioni

    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.6 Publications

    Catalytic activityi

    ATP + a protein = ADP + a phosphoprotein.

    Enzyme regulationi

    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).3 Publications

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei1028 – 10281ATP
    Active sitei1128 – 11281Proton acceptor
    Binding sitei1146 – 11461ATP

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi1005 – 10139ATP
    Nucleotide bindingi1082 – 10898ATP

    GO - Molecular functioni

    1. ATP binding Source: UniProtKB-KW
    2. phosphatidylinositol binding Source: UniProtKB
    3. protein binding Source: UniProtKB
    4. protein serine/threonine kinase activity Source: UniProtKB
    5. signal transducer activity Source: InterPro

    GO - Biological processi

    1. negative regulation of glycogen biosynthetic process Source: UniProtKB
    2. positive regulation of translation Source: UniProtKB
    3. protein autophosphorylation Source: UniProtKB
    4. protein phosphorylation Source: UniProtKB
    5. regulation of energy homeostasis Source: UniProtKB
    6. regulation of glucagon secretion Source: UniProtKB
    7. regulation of respiratory gaseous exchange Source: UniProtKB

    Keywords - Molecular functioni

    Kinase, Serine/threonine-protein kinase, Transferase

    Keywords - Ligandi

    ATP-binding, Lipid-binding, Nucleotide-binding

    Enzyme and pathway databases

    SignaLinkiQ96RG2.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    PAS domain-containing serine/threonine-protein kinase (EC:2.7.11.1)
    Short name:
    PAS-kinase
    Short name:
    PASKIN
    Short name:
    hPASK
    Gene namesi
    Name:PASK
    Synonyms:KIAA0135
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 2

    Organism-specific databases

    HGNCiHGNC:17270. PASK.

    Subcellular locationi

    Cytoplasm 1 Publication. Nucleus 1 Publication
    Note: Localizes in the nucleus of testis germ cells and in the midpiece of sperm tails.

    GO - Cellular componenti

    1. cytoplasm Source: UniProtKB
    2. Golgi apparatus Source: HPA
    3. nucleus Source: UniProtKB

    Keywords - Cellular componenti

    Cytoplasm, Nucleus

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi1028 – 10281K → R: Loss of autophosphorylating activity. 2 Publications
    Mutagenesisi1058 – 10581R → A: Induces lower protein kinase activity. 1 Publication
    Mutagenesisi1058 – 10581R → K: Does not affect protein kinase activity. 1 Publication
    Mutagenesisi1151 – 11511A → K: Induces lower protein kinase activity and ability to autophosphorylate. 1 Publication
    Mutagenesisi1152 – 11521Y → F: Induces lower protein kinase activity. 1 Publication
    Mutagenesisi1161 – 11611T → 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. 3 Publications
    Mutagenesisi1165 – 11651T → A: Loss of catalytic activity. Does not affect protein translation. 2 Publications

    Organism-specific databases

    PharmGKBiPA32953.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 13231323PAS domain-containing serine/threonine-protein kinasePRO_0000086480Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei1 – 11N-acetylmethionine1 Publication
    Modified residuei1161 – 11611Phosphothreonine; by autocatalysis1 Publication
    Modified residuei1165 – 11651Phosphothreonine; by autocatalysis1 Publication

    Post-translational modificationi

    Autophosphorylated on Thr-1161 and Thr-1165. Autophosphorylation is activated by phospholipids.1 Publication

    Keywords - PTMi

    Acetylation, Phosphoprotein

    Proteomic databases

    MaxQBiQ96RG2.
    PaxDbiQ96RG2.
    PRIDEiQ96RG2.

    PTM databases

    PhosphoSiteiQ96RG2.

    Expressioni

    Tissue specificityi

    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).

    Gene expression databases

    ArrayExpressiQ96RG2.
    BgeeiQ96RG2.
    CleanExiHS_PASK.
    GenevestigatoriQ96RG2.

    Organism-specific databases

    HPAiHPA016450.
    HPA021079.

    Interactioni

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    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.

    Protein-protein interaction databases

    BioGridi116790. 38 interactions.
    IntActiQ96RG2. 52 interactions.
    STRINGi9606.ENSP00000234040.

    Structurei

    Secondary structure

    1
    1323
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi133 – 1386
    Turni139 – 1413
    Beta strandi143 – 1475
    Helixi151 – 1555
    Turni159 – 1613
    Helixi167 – 1704
    Turni174 – 1763
    Helixi177 – 1815
    Beta strandi188 – 1914
    Beta strandi198 – 2036
    Beta strandi211 – 2144
    Beta strandi221 – 23414
    Helixi987 – 9915
    Helixi994 – 9985
    Beta strandi999 – 10046
    Beta strandi1006 – 10105
    Beta strandi1012 – 10187
    Turni1019 – 10224
    Beta strandi1023 – 103210
    Beta strandi1039 – 10435
    Turni1044 – 10463
    Beta strandi1047 – 10504
    Helixi1051 – 10566
    Beta strandi1067 – 10726
    Beta strandi1074 – 10829
    Helixi1090 – 10956
    Helixi1102 – 112120
    Helixi1131 – 11333
    Beta strandi1134 – 11363
    Beta strandi1142 – 11443
    Helixi1166 – 11683
    Helixi1171 – 11744
    Helixi1182 – 119817
    Helixi1206 – 12094
    Turni1210 – 12123
    Helixi1222 – 123110
    Helixi1236 – 12383
    Helixi1242 – 12476
    Turni1249 – 12524
    Helixi1257 – 12593
    Helixi1262 – 12654

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1LL8NMR-A131-237[»]
    3DLSX-ray2.30A/B/C/D/E/F977-1300[»]
    ProteinModelPortaliQ96RG2.
    SMRiQ96RG2. Positions 131-237, 346-386, 929-1292.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ96RG2.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini119 – 19072PAS 1PROSITE-ProRule annotationAdd
    BLAST
    Domaini335 – 40268PAS 2PROSITE-ProRule annotationAdd
    BLAST
    Domaini999 – 1251253Protein kinasePROSITE-ProRule annotationAdd
    BLAST

    Domaini

    The protein kinase domain mediates binding to phosphatidylinositol.1 Publication

    Sequence similaritiesi

    Contains 2 PAS (PER-ARNT-SIM) domains.PROSITE-ProRule annotation
    Contains 1 protein kinase domain.PROSITE-ProRule annotation

    Keywords - Domaini

    Repeat

    Phylogenomic databases

    eggNOGiCOG0515.
    HOGENOMiHOG000115456.
    HOVERGENiHBG047936.
    KOiK08801.
    OMAiVANDKAC.
    OrthoDBiEOG76HQ0W.
    PhylomeDBiQ96RG2.
    TreeFamiTF323242.

    Family and domain databases

    InterProiIPR011009. 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]
    PfamiPF13426. PAS_9. 1 hit.
    PF00069. Pkinase. 1 hit.
    [Graphical view]
    SMARTiSM00091. PAS. 2 hits.
    SM00220. S_TKc. 1 hit.
    [Graphical view]
    SUPFAMiSSF55785. SSF55785. 1 hit.
    SSF56112. SSF56112. 1 hit.
    TIGRFAMsiTIGR00229. sensory_box. 1 hit.
    PROSITEiPS50112. PAS. 1 hit.
    PS00107. PROTEIN_KINASE_ATP. 1 hit.
    PS50011. PROTEIN_KINASE_DOM. 1 hit.
    PS00108. PROTEIN_KINASE_ST. 1 hit.
    [Graphical view]

    Sequences (3)i

    Sequence statusi: Complete.

    This entry describes 3 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: Q96RG2-1) [UniParc]FASTAAdd to Basket

    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.

    « Hide

    MEDGGLTAFE EDQRCLSQSL PLPVSAEGPA AQTTAEPSRS FSSAHRHLSR     50
    RNGLSRLCQS RTALSEDRWS SYCLSSLAAQ NICTSKLHCP AAPEHTDPSE 100
    PRGSVSCCSL LRGLSSGWSS PLLPAPVCNP NKAIFTVDAK TTEILVANDK 150
    ACGLLGYSSQ DLIGQKLTQF FLRSDSDVVE ALSEEHMEAD GHAAVVFGTV 200
    VDIISRSGEK IPVSVWMKRM RQERRLCCVV VLEPVERVST WVAFQSDGTV 250
    TSCDSLFAHL HGYVSGEDVA GQHITDLIPS VQLPPSGQHI PKNLKIQRSV 300
    GRARDGTTFP LSLKLKSQPS SEEATTGEAA PVSGYRASVW VFCTISGLIT 350
    LLPDGTIHGI NHSFALTLFG YGKTELLGKN ITFLIPGFYS YMDLAYNSSL 400
    QLPDLASCLD VGNESGCGER TLDPWQGQDP AEGGQDPRIN VVLAGGHVVP 450
    RDEIRKLMES QDIFTGTQTE LIAGGQLLSC LSPQPAPGVD NVPEGSLPVH 500
    GEQALPKDQQ ITALGREEPV AIESPGQDLL GESRSEPVDV KPFASCEDSE 550
    APVPAEDGGS DAGMCGLCQK AQLERMGVSG PSGSDLWAGA AVAKPQAKGQ 600
    LAGGSLLMHC PCYGSEWGLW WRSQDLAPSP SGMAGLSFGT PTLDEPWLGV 650
    ENDREELQTC LIKEQLSQLS LAGALDVPHA ELVPTECQAV TAPVSSCDLG 700
    GRDLCGGCTG SSSACYALAT DLPGGLEAVE AQEVDVNSFS WNLKELFFSD 750
    QTDQTSSNCS CATSELRETP SSLAVGSDPD VGSLQEQGSC VLDDRELLLL 800
    TGTCVDLGQG RRFRESCVGH DPTEPLEVCL VSSEHYAASD RESPGHVPST 850
    LDAGPEDTCP SAEEPRLNVQ VTSTPVIVMR GAAGLQREIQ EGAYSGSCYH 900
    RDGLRLSIQF EVRRVELQGP TPLFCCWLVK DLLHSQRDSA ARTRLFLASL 950
    PGSTHSTAAE LTGPSLVEVL RARPWFEEPP KAVELEGLAA CEGEYSQKYS 1000
    TMSPLGSGAF GFVWTAVDKE KNKEVVVKFI KKEKVLEDCW IEDPKLGKVT 1050
    LEIAILSRVE HANIIKVLDI FENQGFFQLV MEKHGSGLDL FAFIDRHPRL 1100
    DEPLASYIFR QLVSAVGYLR LKDIIHRDIK DENIVIAEDF TIKLIDFGSA 1150
    AYLERGKLFY TFCGTIEYCA PEVLMGNPYR GPELEMWSLG VTLYTLVFEE 1200
    NPFCELEETV EAAIHPPYLV SKELMSLVSG LLQPVPERRT TLEKLVTDPW 1250
    VTQPVNLADY TWEEVFRVNK PESGVLSAAS LEMGNRSLSD VAQAQELCGG 1300
    PVPGEAPNGQ GCLHPGDPRL LTS 1323
    Length:1,323
    Mass (Da):142,929
    Last modified:October 17, 2006 - v3
    Checksum:iF8A3633CC6F6C8CD
    GO
    Isoform 2 (identifier: Q96RG2-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1111-1111: Q → QVRAGQSR

    Note: No experimental confirmation available.

    Show »
    Length:1,330
    Mass (Da):143,684
    Checksum:i8177593F181C6914
    GO
    Isoform 3 (identifier: Q96RG2-4) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1112-1143: LVSAVGYLRLKDIIHRDIKDENIVIAEDFTIK → VRAGQSRVSVNAGLGAWVRWLQRSVIHTRFSL
         1144-1323: Missing.

    Note: No experimental confirmation available.

    Show »
    Length:1,143
    Mass (Da):123,048
    Checksum:i535BFCA305C18419
    GO

    Sequence cautioni

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

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti205 – 2051S → T in BAA09484. (PubMed:8590280)Curated
    Sequence conflicti407 – 4071S → C in CAH18087. (PubMed:17974005)Curated
    Sequence conflicti623 – 6231S → R in BAA09484. (PubMed:8590280)Curated
    Sequence conflicti741 – 7411W → R in CAH18087. (PubMed:17974005)Curated
    Sequence conflicti850 – 8501T → M in BAA09484. (PubMed:8590280)Curated
    Sequence conflicti899 – 8991Y → H in AAK69752. (PubMed:11459942)Curated
    Sequence conflicti1048 – 10481K → E in CAH18087. (PubMed:17974005)Curated
    Sequence conflicti1062 – 10621A → S in AAH50565. (PubMed:15489334)Curated
    Sequence conflicti1129 – 11291I → F in AAB50198. (PubMed:9110174)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti11 – 111E → K in a metastatic melanoma sample; somatic mutation. 1 Publication
    VAR_040986
    Natural varianti250 – 2501V → I.2 Publications
    Corresponds to variant rs1470414 [ dbSNP | Ensembl ].
    VAR_028293
    Natural varianti426 – 4261Q → R.1 Publication
    Corresponds to variant rs35187712 [ dbSNP | Ensembl ].
    VAR_040987
    Natural varianti512 – 5121T → A.1 Publication
    Corresponds to variant rs56033464 [ dbSNP | Ensembl ].
    VAR_040988
    Natural varianti514 – 5141L → S.1 Publication
    Corresponds to variant rs2240543 [ dbSNP | Ensembl ].
    VAR_028294
    Natural varianti684 – 6841P → R.1 Publication
    Corresponds to variant rs56372985 [ dbSNP | Ensembl ].
    VAR_040989
    Natural varianti694 – 6941V → M.1 Publication
    Corresponds to variant rs6727226 [ dbSNP | Ensembl ].
    VAR_028295
    Natural varianti725 – 7251G → D.1 Publication
    Corresponds to variant rs2005771 [ dbSNP | Ensembl ].
    VAR_028296
    Natural varianti796 – 7961E → K.1 Publication
    Corresponds to variant rs35129131 [ dbSNP | Ensembl ].
    VAR_040990
    Natural varianti844 – 8441P → Q.1 Publication
    Corresponds to variant rs36082918 [ dbSNP | Ensembl ].
    VAR_040991
    Natural varianti937 – 9371R → H.1 Publication
    Corresponds to variant rs56139954 [ dbSNP | Ensembl ].
    VAR_040992
    Natural varianti1210 – 12101V → M.1 Publication
    Corresponds to variant rs10167000 [ dbSNP | Ensembl ].
    VAR_028297
    Natural varianti1266 – 12661F → C.3 Publications
    Corresponds to variant rs1131293 [ dbSNP | Ensembl ].
    VAR_028298
    Natural varianti1301 – 13011P → S.1 Publication
    VAR_040993

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1111 – 11111Q → QVRAGQSR in isoform 2. 1 PublicationVSP_009302
    Alternative sequencei1112 – 114332LVSAV…DFTIK → VRAGQSRVSVNAGLGAWVRW LQRSVIHTRFSL in isoform 3. 1 PublicationVSP_045543Add
    BLAST
    Alternative sequencei1144 – 1323180Missing in isoform 3. 1 PublicationVSP_045544Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    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.
    CCDSiCCDS2545.1. [Q96RG2-1]
    CCDS58758.1. [Q96RG2-4]
    CCDS58759.1. [Q96RG2-2]
    PIRiT17211.
    RefSeqiNP_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]
    UniGeneiHs.397891.

    Genome annotation databases

    EnsembliENST00000234040; ENSP00000234040; ENSG00000115687. [Q96RG2-1]
    ENST00000358649; ENSP00000351475; ENSG00000115687. [Q96RG2-2]
    ENST00000403638; ENSP00000384438; ENSG00000115687. [Q96RG2-4]
    ENST00000405260; ENSP00000384016; ENSG00000115687. [Q96RG2-1]
    GeneIDi23178.
    KEGGihsa:23178.
    UCSCiuc002wao.2. human. [Q96RG2-1]
    uc002wap.3. human.
    uc010fzl.2. human. [Q96RG2-2]

    Polymorphism databases

    DMDMi116242701.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    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 .
    CCDSi CCDS2545.1. [Q96RG2-1 ]
    CCDS58758.1. [Q96RG2-4 ]
    CCDS58759.1. [Q96RG2-2 ]
    PIRi T17211.
    RefSeqi NP_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 ]
    UniGenei Hs.397891.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1LL8 NMR - A 131-237 [» ]
    3DLS X-ray 2.30 A/B/C/D/E/F 977-1300 [» ]
    ProteinModelPortali Q96RG2.
    SMRi Q96RG2. Positions 131-237, 346-386, 929-1292.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 116790. 38 interactions.
    IntActi Q96RG2. 52 interactions.
    STRINGi 9606.ENSP00000234040.

    Chemistry

    BindingDBi Q96RG2.
    ChEMBLi CHEMBL6054.
    GuidetoPHARMACOLOGYi 2139.

    PTM databases

    PhosphoSitei Q96RG2.

    Polymorphism databases

    DMDMi 116242701.

    Proteomic databases

    MaxQBi Q96RG2.
    PaxDbi Q96RG2.
    PRIDEi Q96RG2.

    Protocols and materials databases

    DNASUi 23178.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000234040 ; ENSP00000234040 ; ENSG00000115687 . [Q96RG2-1 ]
    ENST00000358649 ; ENSP00000351475 ; ENSG00000115687 . [Q96RG2-2 ]
    ENST00000403638 ; ENSP00000384438 ; ENSG00000115687 . [Q96RG2-4 ]
    ENST00000405260 ; ENSP00000384016 ; ENSG00000115687 . [Q96RG2-1 ]
    GeneIDi 23178.
    KEGGi hsa:23178.
    UCSCi uc002wao.2. human. [Q96RG2-1 ]
    uc002wap.3. human.
    uc010fzl.2. human. [Q96RG2-2 ]

    Organism-specific databases

    CTDi 23178.
    GeneCardsi GC02M242045.
    HGNCi HGNC:17270. PASK.
    HPAi HPA016450.
    HPA021079.
    MIMi 607505. gene.
    neXtProti NX_Q96RG2.
    PharmGKBi PA32953.
    HUGEi Search...
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG0515.
    HOGENOMi HOG000115456.
    HOVERGENi HBG047936.
    KOi K08801.
    OMAi VANDKAC.
    OrthoDBi EOG76HQ0W.
    PhylomeDBi Q96RG2.
    TreeFami TF323242.

    Enzyme and pathway databases

    SignaLinki Q96RG2.

    Miscellaneous databases

    EvolutionaryTracei Q96RG2.
    GeneWikii PASK.
    GenomeRNAii 23178.
    NextBioi 44625.
    PROi Q96RG2.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q96RG2.
    Bgeei Q96RG2.
    CleanExi HS_PASK.
    Genevestigatori Q96RG2.

    Family and domain databases

    InterProi IPR011009. 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 ]
    Pfami PF13426. PAS_9. 1 hit.
    PF00069. Pkinase. 1 hit.
    [Graphical view ]
    SMARTi SM00091. PAS. 2 hits.
    SM00220. S_TKc. 1 hit.
    [Graphical view ]
    SUPFAMi SSF55785. SSF55785. 1 hit.
    SSF56112. SSF56112. 1 hit.
    TIGRFAMsi TIGR00229. sensory_box. 1 hit.
    PROSITEi PS50112. PAS. 1 hit.
    PS00107. PROTEIN_KINASE_ATP. 1 hit.
    PS50011. PROTEIN_KINASE_DOM. 1 hit.
    PS00108. PROTEIN_KINASE_ST. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    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. 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.
      , 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. 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. 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. 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. 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.
      , 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.

    Entry informationi

    Entry nameiPASK_HUMAN
    AccessioniPrimary (citable) accession number: Q96RG2
    Secondary accession number(s): G5E9F1
    , Q05BE4, Q68DY3, Q6GSJ5, Q86XH6, Q99763, Q9UFR7
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: January 16, 2004
    Last sequence update: October 17, 2006
    Last modified: October 1, 2014
    This is version 147 of the entry and version 3 of the sequence. [Complete history]
    Entry statusiReviewed (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.

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. Human chromosome 2
      Human chromosome 2: entries, gene names and cross-references to MIM
    2. Human entries with polymorphisms or disease mutations
      List of human entries with polymorphisms or disease mutations
    3. Human polymorphisms and disease mutations
      Index of human polymorphisms and disease mutations
    4. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    5. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    6. Human and mouse protein kinases
      Human and mouse protein kinases: classification and index
    7. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3