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STE20/SPS1-related proline-alanine-rich protein kinase (Ste-20-related kinase) (EC 2.7.11.1) (Serine/threonine-protein kinase 39)

 STK39_MOUSE             Reviewed;         556 AA.
Q9Z1W9; Q80W13;
01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
01-MAY-1999, sequence version 1.
22-NOV-2017, entry version 160.
RecName: Full=STE20/SPS1-related proline-alanine-rich protein kinase;
Short=Ste-20-related kinase;
EC=2.7.11.1;
AltName: Full=Serine/threonine-protein kinase 39;
Name=Stk39; Synonyms=Spak;
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Brain;
PubMed=10980603; DOI=10.1038/sj.onc.1203784;
Johnston A.M., Naselli G., Gonez L.J., Martin R.M., Harrison L.C.,
de Aizpurua H.J.;
"SPAK, a STE20/SPS1-related kinase that activates the p38 pathway.";
Oncogene 19:4290-4297(2000).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=C57BL/6J; TISSUE=Brain;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[3]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-397 AND SER-405, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Lung, Pancreas,
Spleen, and Testis;
PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
"A tissue-specific atlas of mouse protein phosphorylation and
expression.";
Cell 143:1174-1189(2010).
[4]
PHOSPHORYLATION AT THR-366 AND SER-383, AND INTERACTION WITH WNK2.
PubMed=21733846; DOI=10.1074/jbc.M111.222893;
Rinehart J., Vazquez N., Kahle K.T., Hodson C.A., Ring A.M.,
Gulcicek E.E., Louvi A., Bobadilla N.A., Gamba G., Lifton R.P.;
"WNK2 is a novel regulator of essential neuronal cation-chloride
cotransporters.";
J. Biol. Chem. 286:30171-30180(2011).
[5]
FUNCTION.
PubMed=21317537; DOI=10.1172/JCI43475;
Yang D., Li Q., So I., Huang C.L., Ando H., Mizutani A., Seki G.,
Mikoshiba K., Thomas P.J., Muallem S.;
"IRBIT governs epithelial secretion in mice by antagonizing the
WNK/SPAK kinase pathway.";
J. Clin. Invest. 121:956-965(2011).
[6]
FUNCTION.
PubMed=23542070; DOI=10.1053/j.gastro.2013.03.047;
Park S., Shcheynikov N., Hong J.H., Zheng C., Suh S.H., Kawaai K.,
Ando H., Mizutani A., Abe T., Kiyonari H., Seki G., Yule D.,
Mikoshiba K., Muallem S.;
"Irbit mediates synergy between ca(2+) and cAMP signaling pathways
during epithelial transport in mice.";
Gastroenterology 145:232-241(2013).
-!- FUNCTION: May act as a mediator of stress-activated signals.
Mediates the inhibiton of SLC4A4, SLC26A6 as well as CFTR
activities by the WNK scaffolds, probably through phosphorylation
(PubMed:21317537, PubMed:23542070). {ECO:0000269|PubMed:21317537,
ECO:0000269|PubMed:23542070}.
-!- CATALYTIC ACTIVITY: ATP + a protein = ADP + a phosphoprotein.
-!- SUBUNIT: The phosphorylated form forms a complex with WNK2.
-!- INTERACTION:
P47811:Mapk14; NbExp=2; IntAct=EBI-444764, EBI-298727;
P55012:Slc12a2; NbExp=3; IntAct=EBI-444764, EBI-621078;
Q924N4-1:Slc12a6; NbExp=4; IntAct=EBI-444764, EBI-620992;
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}. Nucleus
{ECO:0000305}. Note=Nucleus when caspase-cleaved. {ECO:0000305}.
-!- DOMAIN: PAPA box (proline-alanine repeats) may target the kinase
to a specific subcellular location by facilitating interaction
with intracellular proteins such as actin or actin-like proteins.
-!- PTM: Phosphorylated at Ser-321 by PRKCQ.
{ECO:0000269|PubMed:21733846}.
-!- SIMILARITY: Belongs to the protein kinase superfamily. STE Ser/Thr
protein kinase family. STE20 subfamily. {ECO:0000305}.
-----------------------------------------------------------------------
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EMBL; AF099988; AAC72237.1; -; mRNA.
EMBL; BC051964; AAH51964.2; -; mRNA.
EMBL; BC064443; AAH64443.1; -; mRNA.
CCDS; CCDS16084.1; -.
RefSeq; NP_058562.1; NM_016866.2.
UniGene; Mm.198414; -.
PDB; 5D9H; X-ray; 3.10 A; A/B=63-403.
PDB; 5DBX; X-ray; 2.50 A; A/B=63-390.
PDBsum; 5D9H; -.
PDBsum; 5DBX; -.
ProteinModelPortal; Q9Z1W9; -.
SMR; Q9Z1W9; -.
BioGrid; 207310; 2.
DIP; DIP-31911N; -.
ELM; Q9Z1W9; -.
IntAct; Q9Z1W9; 11.
STRING; 10090.ENSMUSP00000099776; -.
iPTMnet; Q9Z1W9; -.
PhosphoSitePlus; Q9Z1W9; -.
EPD; Q9Z1W9; -.
MaxQB; Q9Z1W9; -.
PaxDb; Q9Z1W9; -.
PRIDE; Q9Z1W9; -.
Ensembl; ENSMUST00000102715; ENSMUSP00000099776; ENSMUSG00000027030.
GeneID; 53416; -.
KEGG; mmu:53416; -.
UCSC; uc008jxo.1; mouse.
CTD; 27347; -.
MGI; MGI:1858416; Stk39.
eggNOG; KOG0582; Eukaryota.
eggNOG; ENOG410XSWS; LUCA.
GeneTree; ENSGT00900000140899; -.
HOGENOM; HOG000234204; -.
HOVERGEN; HBG108518; -.
InParanoid; Q9Z1W9; -.
KO; K08835; -.
OMA; LSVHDSQ; -.
OrthoDB; EOG091G0AKO; -.
PhylomeDB; Q9Z1W9; -.
TreeFam; TF105339; -.
BRENDA; 2.7.11.1; 3474.
ChiTaRS; Stk39; mouse.
PRO; PR:Q9Z1W9; -.
Proteomes; UP000000589; Chromosome 2.
Bgee; ENSMUSG00000027030; -.
ExpressionAtlas; Q9Z1W9; baseline and differential.
Genevisible; Q9Z1W9; MM.
GO; GO:0016324; C:apical plasma membrane; IDA:MGI.
GO; GO:0016323; C:basolateral plasma membrane; IDA:MGI.
GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
GO; GO:0005856; C:cytoskeleton; IEA:Ensembl.
GO; GO:0005829; C:cytosol; ISO:MGI.
GO; GO:0019898; C:extrinsic component of membrane; IEA:Ensembl.
GO; GO:0043231; C:intracellular membrane-bounded organelle; ISO:MGI.
GO; GO:0016020; C:membrane; IDA:MGI.
GO; GO:0005654; C:nucleoplasm; ISO:MGI.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0004672; F:protein kinase activity; IDA:MGI.
GO; GO:0019901; F:protein kinase binding; IEA:Ensembl.
GO; GO:0004674; F:protein serine/threonine kinase activity; IGI:ParkinsonsUK-UCL.
GO; GO:0032147; P:activation of protein kinase activity; IBA:GO_Central.
GO; GO:0071476; P:cellular hypotonic response; IGI:ParkinsonsUK-UCL.
GO; GO:0035556; P:intracellular signal transduction; IGI:ParkinsonsUK-UCL.
GO; GO:0036438; P:maintenance of lens transparency; IMP:ParkinsonsUK-UCL.
GO; GO:1905408; P:negative regulation of creatine transmembrane transporter activity; ISO:MGI.
GO; GO:0090188; P:negative regulation of pancreatic juice secretion; IMP:UniProtKB.
GO; GO:1901380; P:negative regulation of potassium ion transmembrane transport; IDA:MGI.
GO; GO:1901017; P:negative regulation of potassium ion transmembrane transporter activity; IGI:ParkinsonsUK-UCL.
GO; GO:0001933; P:negative regulation of protein phosphorylation; IDA:MGI.
GO; GO:2000687; P:negative regulation of rubidium ion transmembrane transporter activity; IGI:ParkinsonsUK-UCL.
GO; GO:2000681; P:negative regulation of rubidium ion transport; IGI:ParkinsonsUK-UCL.
GO; GO:2000650; P:negative regulation of sodium ion transmembrane transporter activity; ISO:MGI.
GO; GO:0018105; P:peptidyl-serine phosphorylation; ISO:MGI.
GO; GO:0018107; P:peptidyl-threonine phosphorylation; IGI:ParkinsonsUK-UCL.
GO; GO:0032414; P:positive regulation of ion transmembrane transporter activity; IEA:Ensembl.
GO; GO:0043268; P:positive regulation of potassium ion transport; IEA:Ensembl.
GO; GO:0046777; P:protein autophosphorylation; IEA:Ensembl.
GO; GO:0042981; P:regulation of apoptotic process; IBA:GO_Central.
GO; GO:0008217; P:regulation of blood pressure; IMP:MGI.
GO; GO:0050727; P:regulation of inflammatory response; IDA:MGI.
GO; GO:2000021; P:regulation of ion homeostasis; IMP:MGI.
GO; GO:0007346; P:regulation of mitotic cell cycle; IBA:GO_Central.
GO; GO:0023014; P:signal transduction by protein phosphorylation; ISO:MGI.
GO; GO:0023016; P:signal transduction by trans-phosphorylation; ISO:MGI.
GO; GO:0031098; P:stress-activated protein kinase signaling cascade; IBA:GO_Central.
InterPro; IPR011009; Kinase-like_dom_sf.
InterPro; IPR024678; Kinase_OSR1/WNK_CCT.
InterPro; IPR000719; Prot_kinase_dom.
InterPro; IPR017441; Protein_kinase_ATP_BS.
Pfam; PF12202; OSR1_C; 1.
Pfam; PF00069; Pkinase; 1.
SMART; SM00220; S_TKc; 1.
SUPFAM; SSF56112; SSF56112; 1.
PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
1: Evidence at protein level;
3D-structure; Acetylation; ATP-binding; Complete proteome; Cytoplasm;
Kinase; Nucleotide-binding; Nucleus; Phosphoprotein;
Reference proteome; Serine/threonine-protein kinase; Transferase.
CHAIN 1 556 STE20/SPS1-related proline-alanine-rich
protein kinase.
/FTId=PRO_0000086723.
DOMAIN 75 349 Protein kinase. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
NP_BIND 81 89 ATP. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
MOTIF 372 378 Nuclear localization signal.
{ECO:0000255}.
MOTIF 399 403 Caspase cleavage related site.
COMPBIAS 17 65 Ala/Pro-rich.
COMPBIAS 22 31 Poly-Ala.
ACT_SITE 204 204 Proton acceptor. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
BINDING 104 104 ATP. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
MOD_RES 321 321 Phosphoserine; by PKC/PRKCQ.
{ECO:0000250|UniProtKB:Q9UEW8}.
MOD_RES 361 361 N6-acetyllysine.
{ECO:0000250|UniProtKB:Q9UEW8}.
MOD_RES 366 366 Phosphothreonine.
{ECO:0000269|PubMed:21733846}.
MOD_RES 382 382 Phosphoserine.
{ECO:0000250|UniProtKB:Q9UEW8}.
MOD_RES 383 383 Phosphoserine.
{ECO:0000269|PubMed:21733846}.
MOD_RES 397 397 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 405 405 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
HELIX 72 74 {ECO:0000244|PDB:5DBX}.
STRAND 75 83 {ECO:0000244|PDB:5DBX}.
STRAND 88 94 {ECO:0000244|PDB:5DBX}.
TURN 95 98 {ECO:0000244|PDB:5DBX}.
STRAND 99 107 {ECO:0000244|PDB:5DBX}.
HELIX 108 110 {ECO:0000244|PDB:5DBX}.
HELIX 114 123 {ECO:0000244|PDB:5DBX}.
TURN 124 127 {ECO:0000244|PDB:5DBX}.
STRAND 137 142 {ECO:0000244|PDB:5DBX}.
STRAND 145 151 {ECO:0000244|PDB:5DBX}.
STRAND 155 157 {ECO:0000244|PDB:5DBX}.
HELIX 158 167 {ECO:0000244|PDB:5DBX}.
TURN 168 173 {ECO:0000244|PDB:5DBX}.
HELIX 178 197 {ECO:0000244|PDB:5DBX}.
HELIX 207 209 {ECO:0000244|PDB:5DBX}.
STRAND 210 212 {ECO:0000244|PDB:5DBX}.
STRAND 218 220 {ECO:0000244|PDB:5DBX}.
HELIX 224 228 {ECO:0000244|PDB:5DBX}.
TURN 230 232 {ECO:0000244|PDB:5D9H}.
HELIX 233 236 {ECO:0000244|PDB:5D9H}.
HELIX 248 250 {ECO:0000244|PDB:5DBX}.
HELIX 253 260 {ECO:0000244|PDB:5DBX}.
HELIX 265 280 {ECO:0000244|PDB:5DBX}.
TURN 284 287 {ECO:0000244|PDB:5DBX}.
HELIX 290 299 {ECO:0000244|PDB:5DBX}.
TURN 305 308 {ECO:0000244|PDB:5DBX}.
HELIX 312 315 {ECO:0000244|PDB:5DBX}.
HELIX 320 329 {ECO:0000244|PDB:5DBX}.
TURN 334 336 {ECO:0000244|PDB:5DBX}.
HELIX 340 343 {ECO:0000244|PDB:5DBX}.
HELIX 347 351 {ECO:0000244|PDB:5DBX}.
HELIX 355 361 {ECO:0000244|PDB:5DBX}.
TURN 362 364 {ECO:0000244|PDB:5DBX}.
SEQUENCE 556 AA; 60320 MW; 66085A90554311D8 CRC64;
MAEPSGSPVH VQLSQQAAPV TAAAATAPAA ATSAPAPAPA PAPAASAAPA PAPAAAPAPA
PAAQAVGWPI CRDAYELQEV IGSGATAVVQ AALCKPRQER VAIKRINLEK CQTSMDELLK
EIQAMSQCSH PNVVTYYTSF VVKDELWLVM KLLSGGSMLD IIKYIVNRGE HKNGVLEEAI
IATILKEVLE GLDYLHRNGQ IHRDLKAGNI LLGEDGSVQI ADFGVSAFLA TGGDVTRNKV
RKTFVGTPCW MAPEVMEQVR GYDFKADMWS FGITAIELAT GAAPYHKYPP MKVLMLTLQN
DPPTLETGVE DKEMMKKYGK SFRKLLSLCL QKDPSKRPTA AELLKCKFFQ KAKNREYLIE
KLLTRTPDIA QRAKKVRRVP GSSGHLHKTE DGDWEWSDDE MDEKSEEGKA AASQEKSRRV
KEENSEISVN AGGIPEQIQS LSVHDSQAQP NANEDYREGP CAVNLVLRLR NSRKELNDIR
FEFTPGRDTA DGVSQELFSA GLVDGHDVVI VAANLQKIVD DPKALKTLTF KLASGCDGSE
IPDEVKLIGF AQLSVS


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