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Q96RG2

- PASK_HUMAN

UniProt

Q96RG2 - PASK_HUMAN

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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

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 serine/threonine kinase activity Source: UniProtKB
  4. 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
Complete GO annotation...

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
Complete GO annotation...

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

BgeeiQ96RG2.
CleanExiHS_PASK.
ExpressionAtlasiQ96RG2. baseline and differential.
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. 47 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, 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.
GeneTreeiENSGT00760000119045.
HOGENOMiHOG000115456.
HOVERGENiHBG047936.
InParanoidiQ96RG2.
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.
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) [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

        10         20         30         40         50
MEDGGLTAFE EDQRCLSQSL PLPVSAEGPA AQTTAEPSRS FSSAHRHLSR
60 70 80 90 100
RNGLSRLCQS RTALSEDRWS SYCLSSLAAQ NICTSKLHCP AAPEHTDPSE
110 120 130 140 150
PRGSVSCCSL LRGLSSGWSS PLLPAPVCNP NKAIFTVDAK TTEILVANDK
160 170 180 190 200
ACGLLGYSSQ DLIGQKLTQF FLRSDSDVVE ALSEEHMEAD GHAAVVFGTV
210 220 230 240 250
VDIISRSGEK IPVSVWMKRM RQERRLCCVV VLEPVERVST WVAFQSDGTV
260 270 280 290 300
TSCDSLFAHL HGYVSGEDVA GQHITDLIPS VQLPPSGQHI PKNLKIQRSV
310 320 330 340 350
GRARDGTTFP LSLKLKSQPS SEEATTGEAA PVSGYRASVW VFCTISGLIT
360 370 380 390 400
LLPDGTIHGI NHSFALTLFG YGKTELLGKN ITFLIPGFYS YMDLAYNSSL
410 420 430 440 450
QLPDLASCLD VGNESGCGER TLDPWQGQDP AEGGQDPRIN VVLAGGHVVP
460 470 480 490 500
RDEIRKLMES QDIFTGTQTE LIAGGQLLSC LSPQPAPGVD NVPEGSLPVH
510 520 530 540 550
GEQALPKDQQ ITALGREEPV AIESPGQDLL GESRSEPVDV KPFASCEDSE
560 570 580 590 600
APVPAEDGGS DAGMCGLCQK AQLERMGVSG PSGSDLWAGA AVAKPQAKGQ
610 620 630 640 650
LAGGSLLMHC PCYGSEWGLW WRSQDLAPSP SGMAGLSFGT PTLDEPWLGV
660 670 680 690 700
ENDREELQTC LIKEQLSQLS LAGALDVPHA ELVPTECQAV TAPVSSCDLG
710 720 730 740 750
GRDLCGGCTG SSSACYALAT DLPGGLEAVE AQEVDVNSFS WNLKELFFSD
760 770 780 790 800
QTDQTSSNCS CATSELRETP SSLAVGSDPD VGSLQEQGSC VLDDRELLLL
810 820 830 840 850
TGTCVDLGQG RRFRESCVGH DPTEPLEVCL VSSEHYAASD RESPGHVPST
860 870 880 890 900
LDAGPEDTCP SAEEPRLNVQ VTSTPVIVMR GAAGLQREIQ EGAYSGSCYH
910 920 930 940 950
RDGLRLSIQF EVRRVELQGP TPLFCCWLVK DLLHSQRDSA ARTRLFLASL
960 970 980 990 1000
PGSTHSTAAE LTGPSLVEVL RARPWFEEPP KAVELEGLAA CEGEYSQKYS
1010 1020 1030 1040 1050
TMSPLGSGAF GFVWTAVDKE KNKEVVVKFI KKEKVLEDCW IEDPKLGKVT
1060 1070 1080 1090 1100
LEIAILSRVE HANIIKVLDI FENQGFFQLV MEKHGSGLDL FAFIDRHPRL
1110 1120 1130 1140 1150
DEPLASYIFR QLVSAVGYLR LKDIIHRDIK DENIVIAEDF TIKLIDFGSA
1160 1170 1180 1190 1200
AYLERGKLFY TFCGTIEYCA PEVLMGNPYR GPELEMWSLG VTLYTLVFEE
1210 1220 1230 1240 1250
NPFCELEETV EAAIHPPYLV SKELMSLVSG LLQPVPERRT TLEKLVTDPW
1260 1270 1280 1290 1300
VTQPVNLADY TWEEVFRVNK PESGVLSAAS LEMGNRSLSD VAQAQELCGG
1310 1320
PVPGEAPNGQ GCLHPGDPRL LTS
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]
ENST00000544142; ENSP00000441374; 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, 929-1292.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 116790. 47 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 ]
ENST00000544142 ; ENSP00000441374 ; 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.
GeneTreei ENSGT00760000119045.
HOGENOMi HOG000115456.
HOVERGENi HBG047936.
InParanoidi Q96RG2.
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

Bgeei Q96RG2.
CleanExi HS_PASK.
ExpressionAtlasi Q96RG2. baseline and differential.
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.
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 ]
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  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 29, 2014
This is version 148 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

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