Q96RG2 (PASK_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended 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

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	1323 AA.
Sequence status	Complete.
Protein existence	Evidence 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.18
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.18). 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.18
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 component	Cytoplasm Nucleus
Coding sequence diversity	Alternative splicing Polymorphism
Domain	Repeat
Ligand	ATP-binding Lipid-binding Nucleotide-binding
Molecular function	Kinase Serine/threonine-protein kinase Transferase
PTM	Phosphoprotein
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	negative 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.18Ref.15. 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_component	Golgi apparatus Inferred from direct assay. Source: HPA nucleus Inferred from direct assay Ref.11. Source: UniProtKB
Molecular_function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW phosphatidylinositol binding Inferred from direct assay Ref.15. Source: UniProtKB protein serine/threonine kinase activity Inferred from direct assay Ref.9Ref.11Ref.18Ref.15. Source: UniProtKB signal transducer activity Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

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 key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 1323

1323

PAS domain-containing serine/threonine-protein kinase

PRO_0000086480

Regions

Domain

119 – 190

72

PAS 1

Domain

335 – 402

68

PAS 2

Domain

999 – 1251

253

Protein kinase

Nucleotide binding

1005 – 1013

9

ATP

Nucleotide binding

1082 – 1089

8

ATP

Sites

Active site

1128

1

Proton acceptor

Binding site

1028

1

ATP

Binding site

1146

1

ATP

Amino acid modifications

Modified residue

1161

1

Phosphothreonine; by autocatalysis Ref.1

Modified residue

1165

1

Phosphothreonine; by autocatalysis Ref.1

Natural variations

Alternative sequence

1111

1

Q → QVRAGQSR in isoform 2.

VSP_009302

Alternative sequence

1112 – 1143

32

LVSAV…DFTIK → VRAGQSRVSVNAGLGAWVRW LQRSVIHTRFSL in isoform 3.

VSP_045543

Alternative sequence

1144 – 1323

180

Missing in isoform 3.

VSP_045544

Natural variant

11

1

E → K in a metastatic melanoma sample; somatic mutation. Ref.19

VAR_040986

Natural variant

250

1

V → I. Ref.7 Ref.19
Corresponds to variant rs1470414 [ dbSNP | Ensembl ].

VAR_028293

Natural variant

426

1

Q → R. Ref.19
Corresponds to variant rs35187712 [ dbSNP | Ensembl ].

VAR_040987

Natural variant

512

1

T → A. Ref.19
Corresponds to variant rs56033464 [ dbSNP | Ensembl ].

VAR_040988

Natural variant

514

1

L → S. Ref.19
Corresponds to variant rs2240543 [ dbSNP | Ensembl ].

VAR_028294

Natural variant

684

1

P → R. Ref.19
Corresponds to variant rs56372985 [ dbSNP | Ensembl ].

VAR_040989

Natural variant

694

1

V → M. Ref.2
Corresponds to variant rs6727226 [ dbSNP | Ensembl ].

VAR_028295

Natural variant

725

1

G → D. Ref.19
Corresponds to variant rs2005771 [ dbSNP | Ensembl ].

VAR_028296

Natural variant

796

1

E → K. Ref.19
Corresponds to variant rs35129131 [ dbSNP | Ensembl ].

VAR_040990

Natural variant

844

1

P → Q. Ref.19
Corresponds to variant rs36082918 [ dbSNP | Ensembl ].

VAR_040991

Natural variant

937

1

R → H. Ref.19
Corresponds to variant rs56139954 [ dbSNP | Ensembl ].

VAR_040992

Natural variant

1210

1

V → M. Ref.19
Corresponds to variant rs10167000 [ dbSNP | Ensembl ].

VAR_028297

Natural variant

1266

1

F → C. Ref.1 Ref.2 Ref.19
Corresponds to variant rs1131293 [ dbSNP | Ensembl ].

VAR_028298

Natural variant

1301

1

P → S. Ref.19

VAR_040993

Experimental info

Mutagenesis

1028

1

K → R: Loss of autophosphorylating activity. Ref.1 Ref.18

Mutagenesis

1058

1

R → A: Induces lower protein kinase activity. Ref.18

Mutagenesis

1058

1

R → K: Does not affect protein kinase activity. Ref.18

Mutagenesis

1151

1

A → K: Induces lower protein kinase activity and ability to autophosphorylate. Ref.18

Mutagenesis

1152

1

Y → F: Induces lower protein kinase activity. Ref.18

Mutagenesis

1161

1

T → 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.18

Mutagenesis

1165

1

T → A: Loss of catalytic activity. Does not affect protein translation. Ref.1 Ref.11

Sequence conflict

205

1

S → T in BAA09484. Ref.2

Sequence conflict

407

1

S → C in CAH18087. Ref.4

Sequence conflict

623

1

S → R in BAA09484. Ref.2

Sequence conflict

741

1

W → R in CAH18087. Ref.4

Sequence conflict

850

1

T → M in BAA09484. Ref.2

Sequence conflict

899

1

Y → H in AAK69752. Ref.1

Sequence conflict

1048

1

K → E in CAH18087. Ref.4

Sequence conflict

1062

1

A → S in AAH50565. Ref.7

Sequence conflict

1129

1

I → F in AAB50198. Ref.8

Secondary structure

1

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1323

Helix Strand Turn

Details...

Beta strand

133 – 138

6

Turn

139 – 141

3

Beta strand

143 – 147

5

Helix

151 – 155

5

Turn

159 – 161

3

Helix

167 – 170

4

Turn

174 – 176

3

Helix

177 – 181

5

Beta strand

188 – 191

4

Beta strand

198 – 203

6

Beta strand

211 – 214

4

Beta strand

221 – 234

14

Helix

987 – 991

5

Helix

994 – 998

5

Beta strand

999 – 1004

6

Beta strand

1006 – 1010

5

Beta strand

1012 – 1018

7

Turn

1019 – 1022

4

Beta strand

1023 – 1032

10

Beta strand

1039 – 1043

5

Turn

1044 – 1046

3

Beta strand

1047 – 1050

4

Helix

1051 – 1056

6

Beta strand

1067 – 1072

6

Beta strand

1074 – 1082

9

Helix

1090 – 1095

6

Helix

1102 – 1121

20

Helix

1131 – 1133

3

Beta strand

1134 – 1136

3

Beta strand

1142 – 1144

3

Helix

1166 – 1168

3

Helix

1171 – 1174

4

Helix

1182 – 1198

17

Helix

1206 – 1209

4

Turn

1210 – 1212

3

Helix

1222 – 1231

10

Helix

1236 – 1238

3

Helix

1242 – 1247

6

Turn

1249 – 1252

4

Helix

1257 – 1259

3

Helix

1262 – 1265

4

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified October 17, 2006. Version 3. Checksum: F8A3633CC6F6C8CD	FASTA	1,323	142,929
	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
	Isoform 2 [UniParc]. Checksum: 8177593F181C6914	FASTA	1,330	143,684
	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 QVRAGQSRLV SAVGYLRLKD IIHRDIKDEN 1150 1160 1170 1180 1190 1200 IVIAEDFTIK LIDFGSAAYL ERGKLFYTFC GTIEYCAPEV LMGNPYRGPE LEMWSLGVTL 1210 1220 1230 1240 1250 1260 YTLVFEENPF CELEETVEAA IHPPYLVSKE LMSLVSGLLQ PVPERRTTLE KLVTDPWVTQ 1270 1280 1290 1300 1310 1320 PVNLADYTWE EVFRVNKPES GVLSAASLEM GNRSLSDVAQ AQELCGGPVP GEAPNGQGCL 1330 HPGDPRLLTS
	Isoform 3 [UniParc]. Checksum: 535BFCA305C18419	FASTA	1,143	123,048
	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 QVRAGQSRVS VNAGLGAWVR WLQRSVIHTR FSL

References

	« Hide 'large scale' referencesShow '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. , 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. , 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]	"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.
[18]	"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.
[19]	"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.
+	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.

IPI

IPI00398824.
IPI00398825.
IPI00893189.

PIR

T17211.

RefSeq

NP_001239048.1. NM_001252119.1.
NP_001239049.1. NM_001252120.1.
NP_001239051.1. NM_001252122.1.
NP_001239053.1. NM_001252124.1.
NP_055963.2. NM_015148.3.

UniGene

Hs.397891.

3D structure databases

PDBe
RCSB PDB
PDBj

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	[»]

ProteinModelPortal

Q96RG2.

ModBase

Search...

Protein-protein interaction databases

IntAct

Q96RG2. 2 interactions.

STRING

9606.ENSP00000234040.

PTM databases

PhosphoSite

Q96RG2.

Polymorphism databases

DMDM

116242701.

Proteomic databases

PaxDb

Q96RG2.

PRIDE

Q96RG2.

Protocols and materials databases

DNASU

23178.

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000234040; ENSP00000234040; ENSG00000115687.
ENST00000358649; ENSP00000351475; ENSG00000115687.
ENST00000403638; ENSP00000384438; ENSG00000115687.
ENST00000405260; ENSP00000384016; ENSG00000115687.

GeneID

23178.

KEGG

hsa:23178.

UCSC

uc002wao.2. human.
uc002waq.3. human.

Organism-specific databases

CTD

23178.

GeneCards

GC02M242045.

HGNC

HGNC:17270. PASK.

HPA

HPA016450.
HPA021079.

MIM

607505. gene.

neXtProt

NX_Q96RG2.

PharmGKB

PA32953.

HUGE

Search...

GenAtlas

Search...

Phylogenomic databases

eggNOG

COG0515.

HOGENOM

HOG000115456.

HOVERGEN

HBG047936.

KO

K08801.

OMA

VANDKAC.

OrthoDB

EOG4933H1.

Gene expression databases

ArrayExpress

Q96RG2.

Bgee

Q96RG2.

CleanEx

HS_PASK.

Genevestigator

Q96RG2.

GermOnline

ENSG00000115687. Homo sapiens.

Family and domain databases

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.
[Graphical view]

Pfam

PF00069. Pkinase. 1 hit.
[Graphical view]

SMART

SM00091. PAS. 2 hits.
SM00220. S_TKc. 1 hit.
[Graphical view]

SUPFAM

SSF56112. Kinase_like. 1 hit.

TIGRFAMs

TIGR00229. sensory_box. 1 hit.

PROSITE

PS50112. PAS. 1 hit.
PS00107. PROTEIN_KINASE_ATP. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00108. PROTEIN_KINASE_ST. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

BindingDB

Q96RG2.

ChEMBL

CHEMBL6054.

EvolutionaryTrace

Q96RG2.

GenomeRNAi

23178.

NextBio

44625.

SOURCE

Search...

Entry information

Entry name

PASK_HUMAN

Accession

Primary (citable) accession number: Q96RG2
Secondary accession number(s): G5E9F1 , Q05BE4, Q68DY3, Q6GSJ5, Q86XH6, Q99763, Q9UFR7

Entry history

Integrated into UniProtKB/Swiss-Prot:	January 16, 2004
Last sequence update:	October 17, 2006
Last modified:	May 1, 2013
This is version 131 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.